data_3KM9
# 
_entry.id   3KM9 
# 
_audit_conform.dict_name       mmcif_pdbx.dic 
_audit_conform.dict_version    5.287 
_audit_conform.dict_location   http://mmcif.pdb.org/dictionaries/ascii/mmcif_pdbx.dic 
# 
loop_
_database_2.database_id 
_database_2.database_code 
PDB   3KM9         
RCSB  RCSB056168   
WWPDB D_1000056168 
# 
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 SSL7-IgA Fc complex'                        unspecified 
PDB 3KLS 'Structure of complement C5 in complex with full length SSL7' unspecified 
# 
_pdbx_database_status.status_code                     REL 
_pdbx_database_status.entry_id                        3KM9 
_pdbx_database_status.recvd_initial_deposition_date   2009-11-10 
_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           3KM9 
_cell.length_a           144.790 
_cell.length_b           144.790 
_cell.length_c           245.280 
_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                         3KM9 
_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 'Staphylococcal enterotoxin-like toxin' 11770.348  2 ? ? 'C-terminal beta-grasp domain, residues 129-231' ? 
3 non-polymer syn 'CADMIUM ION'                           112.411    5 ? ? ?                                                ? 
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 
;SSETNTHLFVNKVYGGNLDASIDSFSINKEEVSLKELDFKIRQHLVKNYGLYKGTTKYGKITINLKDGEKQEIDLGDKLQ
FERMGDVLNSKDINKIEVTLKQI
;
;SSETNTHLFVNKVYGGNLDASIDSFSINKEEVSLKELDFKIRQHLVKNYGLYKGTTKYGKITINLKDGEKQEIDLGDKLQ
FERMGDVLNSKDINKIEVTLKQI
;
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    SER n 
2 2    SER n 
2 3    GLU n 
2 4    THR n 
2 5    ASN n 
2 6    THR n 
2 7    HIS n 
2 8    LEU n 
2 9    PHE n 
2 10   VAL n 
2 11   ASN n 
2 12   LYS n 
2 13   VAL n 
2 14   TYR n 
2 15   GLY n 
2 16   GLY n 
2 17   ASN n 
2 18   LEU n 
2 19   ASP n 
2 20   ALA n 
2 21   SER n 
2 22   ILE n 
2 23   ASP n 
2 24   SER n 
2 25   PHE n 
2 26   SER n 
2 27   ILE n 
2 28   ASN n 
2 29   LYS n 
2 30   GLU n 
2 31   GLU n 
2 32   VAL n 
2 33   SER n 
2 34   LEU n 
2 35   LYS n 
2 36   GLU n 
2 37   LEU n 
2 38   ASP n 
2 39   PHE n 
2 40   LYS n 
2 41   ILE n 
2 42   ARG n 
2 43   GLN n 
2 44   HIS n 
2 45   LEU n 
2 46   VAL n 
2 47   LYS n 
2 48   ASN n 
2 49   TYR n 
2 50   GLY n 
2 51   LEU n 
2 52   TYR n 
2 53   LYS n 
2 54   GLY n 
2 55   THR n 
2 56   THR n 
2 57   LYS n 
2 58   TYR n 
2 59   GLY n 
2 60   LYS n 
2 61   ILE n 
2 62   THR n 
2 63   ILE n 
2 64   ASN n 
2 65   LEU n 
2 66   LYS n 
2 67   ASP n 
2 68   GLY n 
2 69   GLU n 
2 70   LYS n 
2 71   GLN n 
2 72   GLU n 
2 73   ILE n 
2 74   ASP n 
2 75   LEU n 
2 76   GLY n 
2 77   ASP n 
2 78   LYS n 
2 79   LEU n 
2 80   GLN n 
2 81   PHE n 
2 82   GLU n 
2 83   ARG n 
2 84   MET n 
2 85   GLY n 
2 86   ASP n 
2 87   VAL n 
2 88   LEU n 
2 89   ASN n 
2 90   SER n 
2 91   LYS n 
2 92   ASP n 
2 93   ILE n 
2 94   ASN n 
2 95   LYS n 
2 96   ILE n 
2 97   GLU n 
2 98   VAL n 
2 99   THR n 
2 100  LEU n 
2 101  LYS n 
2 102  GLN n 
2 103  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                    Newman 
_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     426430 
_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          plasmid 
_entity_src_gen.pdbx_host_org_vector               ? 
_entity_src_gen.host_org_details                   ? 
_entity_src_gen.expression_system_id               ? 
_entity_src_gen.plasmid_name                       pET-32a-3c 
_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 A6QE84_STAAE A6QE84 2 
;SSETNTHLFVNKVYGGNLDASIDSFSINKEEVSLKELDFKIRQHLVKNYGLYKGTTKYGKITINLKDGEKQEIDLGDKLQ
FERMGDVLNSKDINKIEVTLKQI
;
129 ? 
# 
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 3KM9 A 1 ? 1676 ? P01031 1   ? 1676 ? 1   1676 
2 2 3KM9 X 1 ? 103  ? A6QE84 129 ? 231  ? 129 231  
3 1 3KM9 B 1 ? 1676 ? P01031 1   ? 1676 ? 1   1676 
4 2 3KM9 Y 1 ? 103  ? A6QE84 129 ? 231  ? 129 231  
# 
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          3KM9 
_exptl.method            'X-RAY DIFFRACTION' 
_exptl.crystals_number   1 
# 
_exptl_crystal.id                    1 
_exptl_crystal.density_meas          ? 
_exptl_crystal.density_Matthews      3.71 
_exptl_crystal.density_percent_sol   66.81 
_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, 50mM MES pH 6.2. Mixed 1:1 with concentrated 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               PIXEL 
_diffrn_detector.type                   'PSI PILATUS 6M' 
_diffrn_detector.pdbx_collection_date   2009-02-20 
_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                    Si111 
_diffrn_radiation.pdbx_diffrn_protocol             'SINGLE WAVELENGTH' 
_diffrn_radiation.pdbx_scattering_type             x-ray 
# 
_diffrn_radiation_wavelength.id           1 
_diffrn_radiation_wavelength.wavelength   0.900 
_diffrn_radiation_wavelength.wt           1.0 
# 
_diffrn_source.diffrn_id                   1 
_diffrn_source.source                      SYNCHROTRON 
_diffrn_source.type                        'SLS BEAMLINE X06DA' 
_diffrn_source.pdbx_synchrotron_site       SLS 
_diffrn_source.pdbx_synchrotron_beamline   X06DA 
_diffrn_source.pdbx_wavelength             ? 
_diffrn_source.pdbx_wavelength_list        0.900 
# 
_reflns.entry_id                     3KM9 
_reflns.observed_criterion_sigma_I   -3 
_reflns.observed_criterion_sigma_F   0 
_reflns.d_resolution_low             50 
_reflns.d_resolution_high            4.2 
_reflns.number_obs                   41914 
_reflns.number_all                   41983 
_reflns.percent_possible_obs         99.9 
_reflns.pdbx_Rmerge_I_obs            ? 
_reflns.pdbx_Rsym_value              0.141 
_reflns.pdbx_netI_over_sigmaI        14.4 
_reflns.B_iso_Wilson_estimate        115.360 
_reflns.pdbx_redundancy              5.3 
_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             4.2 
_reflns_shell.d_res_low              4.4 
_reflns_shell.percent_possible_all   100 
_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                                 3KM9 
_refine.ls_number_reflns_obs                     41792 
_refine.ls_number_reflns_all                     41960 
_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                             49.752 
_refine.ls_d_res_high                            4.200 
_refine.ls_percent_reflns_obs                    99.60 
_refine.ls_R_factor_obs                          0.2364 
_refine.ls_R_factor_all                          ? 
_refine.ls_R_factor_R_work                       0.2333 
_refine.ls_R_factor_R_free                       0.2971 
_refine.ls_R_factor_R_free_error                 ? 
_refine.ls_R_factor_R_free_error_details         ? 
_refine.ls_percent_reflns_R_free                 4.85 
_refine.ls_number_reflns_R_free                  2029 
_refine.ls_number_reflns_R_work                  39763 
_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                               205.604 
_refine.pdbx_isotropic_thermal_model             ? 
_refine.aniso_B[1][1]                            36.235 
_refine.aniso_B[2][2]                            36.235 
_refine.aniso_B[3][3]                            -45.221 
_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                 0.309 
_refine.solvent_model_param_bsol                 150.000 
_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 with the C345C domain removed' 
_refine.pdbx_method_to_determine_struct          'MOLECULAR REPLACEMENT' 
_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                            0.60 
_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                   0.751 
_refine.B_iso_max                                536.65 
_refine.B_iso_min                                77.33 
_refine.pdbx_overall_phase_error                 31.66 
_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        24720 
_refine_hist.pdbx_number_atoms_nucleic_acid   0 
_refine_hist.pdbx_number_atoms_ligand         89 
_refine_hist.number_atoms_solvent             0 
_refine_hist.number_atoms_total               24809 
_refine_hist.d_res_high                       4.200 
_refine_hist.d_res_low                        49.752 
# 
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           25344 0.011  ? ? ? 
'X-RAY DIFFRACTION' f_angle_d          34334 1.551  ? ? ? 
'X-RAY DIFFRACTION' f_chiral_restr     3922  0.097  ? ? ? 
'X-RAY DIFFRACTION' f_plane_restr      4356  0.007  ? ? ? 
'X-RAY DIFFRACTION' f_dihedral_angle_d 9212  20.621 ? ? ? 
# 
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' . 4.2004  4.3054  2865 0.3148 100.00 0.3608 . . 140 . . . . 
'X-RAY DIFFRACTION' . 4.3054  4.4217  2850 0.2729 100.00 0.2811 . . 132 . . . . 
'X-RAY DIFFRACTION' . 4.4217  4.5517  2835 0.2427 100.00 0.2706 . . 157 . . . . 
'X-RAY DIFFRACTION' . 4.5517  4.6986  2844 0.2258 100.00 0.3092 . . 144 . . . . 
'X-RAY DIFFRACTION' . 4.6986  4.8663  2806 0.2204 100.00 0.2827 . . 143 . . . . 
'X-RAY DIFFRACTION' . 4.8663  5.0610  2848 0.1910 99.00  0.2467 . . 172 . . . . 
'X-RAY DIFFRACTION' . 5.0610  5.2911  2854 0.1868 100.00 0.2144 . . 126 . . . . 
'X-RAY DIFFRACTION' . 5.2911  5.5697  2875 0.1884 100.00 0.2820 . . 152 . . . . 
'X-RAY DIFFRACTION' . 5.5697  5.9181  2771 0.2064 100.00 0.3000 . . 163 . . . . 
'X-RAY DIFFRACTION' . 5.9181  6.3742  2869 0.2215 100.00 0.2999 . . 138 . . . . 
'X-RAY DIFFRACTION' . 6.3742  7.0141  2840 0.2143 100.00 0.2965 . . 127 . . . . 
'X-RAY DIFFRACTION' . 7.0141  8.0254  2836 0.2053 100.00 0.2958 . . 176 . . . . 
'X-RAY DIFFRACTION' . 8.0254  10.0973 2854 0.1619 99.00  0.2361 . . 125 . . . . 
'X-RAY DIFFRACTION' . 10.0973 49.7554 2816 0.2308 98.00  0.2926 . . 134 . . . . 
# 
_struct.entry_id                  3KM9 
_struct.title                     'Structure of complement C5 in complex with the C-terminal beta-grasp domain of SSL7' 
_struct.pdbx_descriptor           'Complement C5, Staphylococcal enterotoxin-like toxin' 
_struct.pdbx_model_details        ? 
_struct.pdbx_CASP_flag            ? 
_struct.pdbx_model_type_details   ? 
# 
_struct_keywords.entry_id        3KM9 
_struct_keywords.pdbx_keywords   'IMMUNE SYSTEM' 
_struct_keywords.text            
;OB-fold, beta-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 3 ? 
G N N 3 ? 
H N N 4 ? 
I N N 4 ? 
J N N 4 ? 
K N N 3 ? 
L N N 3 ? 
M N N 4 ? 
N N N 4 ? 
O N N 4 ? 
# 
_struct_biol.id        1 
_struct_biol.details   ? 
# 
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  SER A 74   ? LYS A 78   ? SER A 74   LYS A 78   5 ? 5  
HELX_P HELX_P2  2  THR A 531  ? VAL A 535  ? THR A 531  VAL A 535  5 ? 5  
HELX_P HELX_P3  3  PRO A 619  ? GLU A 628  ? PRO A 619  GLU A 628  1 ? 10 
HELX_P HELX_P4  4  ASN A 641  ? ALA A 649  ? ASN A 641  ALA A 649  1 ? 9  
HELX_P HELX_P5  5  GLN A 680  ? GLU A 685  ? GLN A 680  GLU A 685  1 ? 6  
HELX_P HELX_P6  6  ILE A 686  ? TYR A 690  ? ILE A 686  TYR A 690  5 ? 5  
HELX_P HELX_P7  7  HIS A 692  ? CYS A 704  ? HIS A 692  CYS A 704  1 ? 13 
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  ? LEU A 992  ? GLY A 985  LEU A 992  1 ? 8  
HELX_P HELX_P10 10 ALA A 1008 ? MET A 1013 ? ALA A 1008 MET A 1013 1 ? 6  
HELX_P HELX_P11 11 SER A 1014 ? GLY A 1028 ? SER A 1014 GLY A 1028 1 ? 15 
HELX_P HELX_P12 12 HIS A 1030 ? PHE A 1034 ? HIS A 1030 PHE A 1034 5 ? 5  
HELX_P HELX_P13 13 ASP A 1037 ? SER A 1055 ? ASP A 1037 SER A 1055 1 ? 19 
HELX_P HELX_P14 14 ILE A 1056 ? ARG A 1060 ? ILE A 1056 ARG A 1060 5 ? 5  
HELX_P HELX_P15 15 SER A 1075 ? VAL A 1089 ? SER A 1075 VAL A 1089 1 ? 15 
HELX_P HELX_P16 16 ASN A 1090 ? TYR A 1092 ? ASN A 1090 TYR A 1092 5 ? 3  
HELX_P HELX_P17 17 ASN A 1096 ? GLN A 1112 ? ASN A 1096 GLN A 1112 1 ? 17 
HELX_P HELX_P18 18 THR A 1132 ? PHE A 1156 ? THR A 1132 PHE A 1156 1 ? 25 
HELX_P HELX_P19 19 ASP A 1157 ? CYS A 1159 ? ASP A 1157 CYS A 1159 5 ? 3  
HELX_P HELX_P20 20 LEU A 1161 ? LEU A 1180 ? LEU A 1161 LEU A 1180 1 ? 20 
HELX_P HELX_P21 21 SER A 1184 ? SER A 1196 ? SER A 1184 SER A 1196 1 ? 13 
HELX_P HELX_P22 22 HIS A 1202 ? ALA A 1216 ? HIS A 1202 ALA A 1216 1 ? 15 
HELX_P HELX_P23 23 THR A 1244 ? LYS A 1262 ? THR A 1244 LYS A 1262 1 ? 19 
HELX_P HELX_P24 24 ASP A 1263 ? ASN A 1268 ? ASP A 1263 ASN A 1268 1 ? 6  
HELX_P HELX_P25 25 PRO A 1269 ? SER A 1275 ? PRO A 1269 SER A 1275 1 ? 7  
HELX_P HELX_P26 26 THR A 1287 ? VAL A 1304 ? THR A 1287 VAL A 1304 1 ? 18 
HELX_P HELX_P27 27 ASN A 1435 ? GLU A 1444 ? ASN A 1435 GLU A 1444 1 ? 10 
HELX_P HELX_P28 28 LEU B 34   ? TYR B 49   ? LEU X 162  TYR X 177  1 ? 16 
HELX_P HELX_P29 29 GLU B 82   ? GLY B 85   ? GLU X 210  GLY X 213  5 ? 4  
HELX_P HELX_P30 30 SER C 74   ? LYS C 78   ? SER B 74   LYS B 78   5 ? 5  
HELX_P HELX_P31 31 THR C 531  ? VAL C 535  ? THR B 531  VAL B 535  5 ? 5  
HELX_P HELX_P32 32 LYS C 618  ? LEU C 627  ? LYS B 618  LEU B 627  1 ? 10 
HELX_P HELX_P33 33 ASN C 641  ? LEU C 648  ? ASN B 641  LEU B 648  1 ? 8  
HELX_P HELX_P34 34 GLN C 680  ? GLU C 685  ? GLN B 680  GLU B 685  1 ? 6  
HELX_P HELX_P35 35 ILE C 686  ? TYR C 690  ? ILE B 686  TYR B 690  5 ? 5  
HELX_P HELX_P36 36 HIS C 692  ? CYS C 704  ? HIS B 692  CYS B 704  1 ? 13 
HELX_P HELX_P37 37 GLY C 721  ? ALA C 740  ? GLY B 721  ALA B 740  1 ? 20 
HELX_P HELX_P38 38 GLY C 985  ? LEU C 992  ? GLY B 985  LEU B 992  1 ? 8  
HELX_P HELX_P39 39 ALA C 1008 ? MET C 1013 ? ALA B 1008 MET B 1013 1 ? 6  
HELX_P HELX_P40 40 VAL C 1015 ? GLY C 1028 ? VAL B 1015 GLY B 1028 1 ? 14 
HELX_P HELX_P41 41 HIS C 1030 ? PHE C 1034 ? HIS B 1030 PHE B 1034 5 ? 5  
HELX_P HELX_P42 42 ASP C 1037 ? SER C 1055 ? ASP B 1037 SER B 1055 1 ? 19 
HELX_P HELX_P43 43 ILE C 1056 ? ARG C 1060 ? ILE B 1056 ARG B 1060 5 ? 5  
HELX_P HELX_P44 44 SER C 1075 ? VAL C 1089 ? SER B 1075 VAL B 1089 1 ? 15 
HELX_P HELX_P45 45 ASN C 1090 ? TYR C 1092 ? ASN B 1090 TYR B 1092 5 ? 3  
HELX_P HELX_P46 46 ASN C 1096 ? GLN C 1112 ? ASN B 1096 GLN B 1112 1 ? 17 
HELX_P HELX_P47 47 THR C 1132 ? PHE C 1156 ? THR B 1132 PHE B 1156 1 ? 25 
HELX_P HELX_P48 48 ASP C 1157 ? CYS C 1159 ? ASP B 1157 CYS B 1159 5 ? 3  
HELX_P HELX_P49 49 LEU C 1161 ? LEU C 1180 ? LEU B 1161 LEU B 1180 1 ? 20 
HELX_P HELX_P50 50 SER C 1184 ? SER C 1196 ? SER B 1184 SER B 1196 1 ? 13 
HELX_P HELX_P51 51 HIS C 1202 ? ALA C 1216 ? HIS B 1202 ALA B 1216 1 ? 15 
HELX_P HELX_P52 52 THR C 1244 ? LEU C 1261 ? THR B 1244 LEU B 1261 1 ? 18 
HELX_P HELX_P53 53 ASP C 1263 ? ASN C 1268 ? ASP B 1263 ASN B 1268 1 ? 6  
HELX_P HELX_P54 54 VAL C 1270 ? GLN C 1278 ? VAL B 1270 GLN B 1278 1 ? 9  
HELX_P HELX_P55 55 THR C 1287 ? VAL C 1304 ? THR B 1287 VAL B 1304 1 ? 18 
HELX_P HELX_P56 56 ASN C 1435 ? GLU C 1444 ? ASN B 1435 GLU B 1444 1 ? 10 
HELX_P HELX_P57 57 LEU D 34   ? TYR D 49   ? LEU Y 162  TYR Y 177  1 ? 16 
HELX_P HELX_P58 58 GLU D 82   ? GLY D 85   ? GLU Y 210  GLY Y 213  5 ? 4  
# 
_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 ? ? ? ? ? ? ? 2.036 ? 
disulf2  disulf ? ? A CYS 634  SG  ? ? ? 1_555 A CYS 669  SG ? ? A CYS 634  A CYS 669  1_555 ? ? ? ? ? ? ? 2.039 ? 
disulf3  disulf ? ? A CYS 698  SG  ? ? ? 1_555 A CYS 724  SG ? ? A CYS 698  A CYS 724  1_555 ? ? ? ? ? ? ? 2.283 ? 
disulf4  disulf ? ? A CYS 699  SG  ? ? ? 1_555 A CYS 731  SG ? ? A CYS 699  A CYS 731  1_555 ? ? ? ? ? ? ? 2.026 ? 
disulf5  disulf ? ? A CYS 711  SG  ? ? ? 1_555 A CYS 732  SG ? ? A CYS 711  A CYS 732  1_555 ? ? ? ? ? ? ? 2.033 ? 
disulf6  disulf ? ? A CYS 856  SG  ? ? ? 1_555 A CYS 883  SG ? ? A CYS 856  A CYS 883  1_555 ? ? ? ? ? ? ? 2.032 ? 
disulf7  disulf ? ? A CYS 1101 SG  ? ? ? 1_555 A CYS 1159 SG ? ? A CYS 1101 A CYS 1159 1_555 ? ? ? ? ? ? ? 2.047 ? 
disulf8  disulf ? ? A CYS 1375 SG  ? ? ? 1_555 A CYS 1505 SG ? ? A CYS 1375 A CYS 1505 1_555 ? ? ? ? ? ? ? 2.030 ? 
disulf9  disulf ? ? A CYS 1405 SG  ? ? ? 1_555 A CYS 1474 SG ? ? A CYS 1405 A CYS 1474 1_555 ? ? ? ? ? ? ? 2.035 ? 
disulf10 disulf ? ? C CYS 567  SG  ? ? ? 1_555 C CYS 810  SG ? ? B CYS 567  B CYS 810  1_555 ? ? ? ? ? ? ? 2.034 ? 
disulf11 disulf ? ? C CYS 634  SG  ? ? ? 1_555 C CYS 669  SG ? ? B CYS 634  B CYS 669  1_555 ? ? ? ? ? ? ? 2.032 ? 
disulf12 disulf ? ? C CYS 698  SG  ? ? ? 1_555 C CYS 724  SG ? ? B CYS 698  B CYS 724  1_555 ? ? ? ? ? ? ? 2.039 ? 
disulf13 disulf ? ? C CYS 699  SG  ? ? ? 1_555 C CYS 731  SG ? ? B CYS 699  B CYS 731  1_555 ? ? ? ? ? ? ? 2.024 ? 
disulf14 disulf ? ? C CYS 711  SG  ? ? ? 1_555 C CYS 732  SG ? ? B CYS 711  B CYS 732  1_555 ? ? ? ? ? ? ? 2.036 ? 
disulf15 disulf ? ? C CYS 856  SG  ? ? ? 1_555 C CYS 883  SG ? ? B CYS 856  B CYS 883  1_555 ? ? ? ? ? ? ? 2.036 ? 
disulf16 disulf ? ? C CYS 1101 SG  ? ? ? 1_555 C CYS 1159 SG ? ? B CYS 1101 B CYS 1159 1_555 ? ? ? ? ? ? ? 2.045 ? 
disulf17 disulf ? ? C CYS 1375 SG  ? ? ? 1_555 C CYS 1505 SG ? ? B CYS 1375 B CYS 1505 1_555 ? ? ? ? ? ? ? 2.027 ? 
disulf18 disulf ? ? C CYS 1405 SG  ? ? ? 1_555 C CYS 1474 SG ? ? B CYS 1405 B CYS 1474 1_555 ? ? ? ? ? ? ? 2.039 ? 
covale1  covale ? ? M NAG .    O4  ? ? ? 1_555 N NAG .    C1 ? ? B NAG 2001 B NAG 2002 1_555 ? ? ? ? ? ? ? 1.372 ? 
covale2  covale ? ? H NAG .    O4  ? ? ? 1_555 I NAG .    C1 ? ? A NAG 2001 A NAG 2002 1_555 ? ? ? ? ? ? ? 1.373 ? 
covale3  covale ? ? A ASN 911  ND2 ? ? ? 1_555 H NAG .    C1 ? ? A ASN 911  A NAG 2001 1_555 ? ? ? ? ? ? ? 1.441 ? 
covale4  covale ? ? C ASN 911  ND2 ? ? ? 1_555 M NAG .    C1 ? ? B ASN 911  B NAG 2001 1_555 ? ? ? ? ? ? ? 1.442 ? 
covale5  covale ? ? A ASN 741  ND2 ? ? ? 1_555 J NAG .    C1 ? ? A ASN 741  A NAG 1680 1_555 ? ? ? ? ? ? ? 1.451 ? 
covale6  covale ? ? C ASN 741  ND2 ? ? ? 1_555 O NAG .    C1 ? ? B ASN 741  B NAG 1679 1_555 ? ? ? ? ? ? ? 1.452 ? 
metalc1  metalc ? ? A ASP 264  OD2 ? ? ? 1_555 G CD  .    CD ? ? A ASP 264  A CD  1679 1_555 ? ? ? ? ? ? ? 2.234 ? 
metalc2  metalc ? ? A ASP 471  OD1 ? ? ? 1_555 F CD  .    CD ? ? A ASP 471  A CD  1678 1_555 ? ? ? ? ? ? ? 2.293 ? 
metalc3  metalc ? ? A GLU 480  OE1 ? ? ? 1_555 F CD  .    CD ? ? A GLU 480  A CD  1678 1_555 ? ? ? ? ? ? ? 2.307 ? 
metalc4  metalc ? ? C ASP 471  OD1 ? ? ? 1_555 K CD  .    CD ? ? B ASP 471  B CD  1677 1_555 ? ? ? ? ? ? ? 2.311 ? 
metalc5  metalc ? ? C HIS 753  ND1 ? ? ? 1_555 L CD  .    CD ? ? B HIS 753  B CD  1678 1_555 ? ? ? ? ? ? ? 2.321 ? 
metalc6  metalc ? ? C GLU 247  OE1 ? ? ? 1_555 E CD  .    CD ? ? B GLU 247  A CD  1677 1_555 ? ? ? ? ? ? ? 2.354 ? 
metalc7  metalc ? ? C GLU 480  OE1 ? ? ? 1_555 K CD  .    CD ? ? B GLU 480  B CD  1677 1_555 ? ? ? ? ? ? ? 2.361 ? 
metalc8  metalc ? ? A GLU 247  OE1 ? ? ? 1_555 E CD  .    CD ? ? A GLU 247  A CD  1677 1_555 ? ? ? ? ? ? ? 2.365 ? 
metalc9  metalc ? ? C GLU 480  OE2 ? ? ? 1_555 K CD  .    CD ? ? B GLU 480  B CD  1677 1_555 ? ? ? ? ? ? ? 2.417 ? 
metalc10 metalc ? ? A HIS 753  ND1 ? ? ? 1_555 G CD  .    CD ? ? A HIS 753  A CD  1679 1_555 ? ? ? ? ? ? ? 2.423 ? 
metalc11 metalc ? ? A ASP 471  OD2 ? ? ? 1_555 F CD  .    CD ? ? A ASP 471  A CD  1678 1_555 ? ? ? ? ? ? ? 2.424 ? 
metalc12 metalc ? ? C ASP 471  OD2 ? ? ? 1_555 K CD  .    CD ? ? B ASP 471  B CD  1677 1_555 ? ? ? ? ? ? ? 2.433 ? 
metalc13 metalc ? ? A GLU 480  OE2 ? ? ? 1_555 F CD  .    CD ? ? A GLU 480  A CD  1678 1_555 ? ? ? ? ? ? ? 2.446 ? 
metalc14 metalc ? ? C ASP 264  OD2 ? ? ? 1_555 L CD  .    CD ? ? B ASP 264  B CD  1678 1_555 ? ? ? ? ? ? ? 2.455 ? 
# 
loop_
_struct_conn_type.id 
_struct_conn_type.criteria 
_struct_conn_type.reference 
disulf ? ? 
covale ? ? 
metalc ? ? 
# 
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 -8.92 
2 ASN 1221 C . ? ASN 1221 B PRO 1222 C ? PRO 1222 B 1 -7.71 
# 
loop_
_struct_sheet.id 
_struct_sheet.type 
_struct_sheet.number_strands 
_struct_sheet.details 
A  ? 4 ? 
B  ? 2 ? 
C  ? 4 ? 
D  ? 5 ? 
E  ? 5 ? 
F  ? 2 ? 
G  ? 2 ? 
H  ? 2 ? 
I  ? 2 ? 
J  ? 3 ? 
K  ? 2 ? 
L  ? 2 ? 
M  ? 3 ? 
N  ? 4 ? 
O  ? 3 ? 
P  ? 8 ? 
Q  ? 9 ? 
R  ? 3 ? 
S  ? 4 ? 
T  ? 2 ? 
U  ? 3 ? 
V  ? 2 ? 
W  ? 2 ? 
X  ? 3 ? 
Y  ? 4 ? 
Z  ? 2 ? 
AA ? 3 ? 
AB ? 5 ? 
AC ? 2 ? 
AD ? 4 ? 
AE ? 2 ? 
AF ? 4 ? 
AG ? 3 ? 
AH ? 5 ? 
AI ? 2 ? 
AJ ? 2 ? 
AK ? 3 ? 
AL ? 2 ? 
AM ? 3 ? 
AN ? 2 ? 
AO ? 4 ? 
AP ? 4 ? 
AQ ? 3 ? 
AR ? 8 ? 
AS ? 9 ? 
AT ? 3 ? 
AU ? 4 ? 
AV ? 3 ? 
AW ? 4 ? 
AX ? 2 ? 
AY ? 2 ? 
AZ ? 3 ? 
BA ? 4 ? 
BB ? 3 ? 
BC ? 2 ? 
BD ? 3 ? 
BE ? 5 ? 
BF ? 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 ? parallel      
D  2 3 ? anti-parallel 
D  3 4 ? anti-parallel 
D  4 5 ? anti-parallel 
E  1 2 ? parallel      
E  2 3 ? 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 
I  1 2 ? anti-parallel 
J  1 2 ? anti-parallel 
J  2 3 ? anti-parallel 
K  1 2 ? anti-parallel 
L  1 2 ? anti-parallel 
M  1 2 ? anti-parallel 
M  2 3 ? anti-parallel 
N  1 2 ? anti-parallel 
N  2 3 ? anti-parallel 
N  3 4 ? 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 
P  4 5 ? anti-parallel 
P  5 6 ? anti-parallel 
P  6 7 ? parallel      
P  7 8 ? anti-parallel 
Q  1 2 ? anti-parallel 
Q  2 3 ? anti-parallel 
Q  3 4 ? anti-parallel 
Q  4 5 ? anti-parallel 
Q  5 6 ? anti-parallel 
Q  6 7 ? parallel      
Q  7 8 ? anti-parallel 
Q  8 9 ? anti-parallel 
R  1 2 ? anti-parallel 
R  2 3 ? anti-parallel 
S  1 2 ? anti-parallel 
S  2 3 ? anti-parallel 
S  3 4 ? anti-parallel 
T  1 2 ? anti-parallel 
U  1 2 ? anti-parallel 
U  2 3 ? anti-parallel 
V  1 2 ? parallel      
W  1 2 ? anti-parallel 
X  1 2 ? anti-parallel 
X  2 3 ? anti-parallel 
Y  1 2 ? anti-parallel 
Y  2 3 ? anti-parallel 
Y  3 4 ? anti-parallel 
Z  1 2 ? 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 
AB 4 5 ? anti-parallel 
AC 1 2 ? anti-parallel 
AD 1 2 ? anti-parallel 
AD 2 3 ? anti-parallel 
AD 3 4 ? anti-parallel 
AE 1 2 ? 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 
AH 1 2 ? parallel      
AH 2 3 ? anti-parallel 
AH 3 4 ? anti-parallel 
AH 4 5 ? anti-parallel 
AI 1 2 ? anti-parallel 
AJ 1 2 ? parallel      
AK 1 2 ? anti-parallel 
AK 2 3 ? anti-parallel 
AL 1 2 ? anti-parallel 
AM 1 2 ? anti-parallel 
AM 2 3 ? 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 ? anti-parallel 
AP 2 3 ? anti-parallel 
AP 3 4 ? anti-parallel 
AQ 1 2 ? anti-parallel 
AQ 2 3 ? anti-parallel 
AR 1 2 ? anti-parallel 
AR 2 3 ? anti-parallel 
AR 3 4 ? anti-parallel 
AR 4 5 ? anti-parallel 
AR 5 6 ? anti-parallel 
AR 6 7 ? parallel      
AR 7 8 ? anti-parallel 
AS 1 2 ? anti-parallel 
AS 2 3 ? anti-parallel 
AS 3 4 ? anti-parallel 
AS 4 5 ? anti-parallel 
AS 5 6 ? anti-parallel 
AS 6 7 ? parallel      
AS 7 8 ? anti-parallel 
AS 8 9 ? anti-parallel 
AT 1 2 ? anti-parallel 
AT 2 3 ? anti-parallel 
AU 1 2 ? anti-parallel 
AU 2 3 ? anti-parallel 
AU 3 4 ? anti-parallel 
AV 1 2 ? anti-parallel 
AV 2 3 ? anti-parallel 
AW 1 2 ? anti-parallel 
AW 2 3 ? anti-parallel 
AW 3 4 ? anti-parallel 
AX 1 2 ? parallel      
AY 1 2 ? anti-parallel 
AZ 1 2 ? anti-parallel 
AZ 2 3 ? anti-parallel 
BA 1 2 ? anti-parallel 
BA 2 3 ? anti-parallel 
BA 3 4 ? anti-parallel 
BB 1 2 ? anti-parallel 
BB 2 3 ? anti-parallel 
BC 1 2 ? anti-parallel 
BD 1 2 ? anti-parallel 
BD 2 3 ? anti-parallel 
BE 1 2 ? anti-parallel 
BE 2 3 ? anti-parallel 
BE 3 4 ? anti-parallel 
BE 4 5 ? anti-parallel 
BF 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   ? ILE A 84   ? GLN A 80   ILE A 84   
A  2 ASN A 38   ? VAL A 43   ? ASN A 38   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   ? SER A 58   ? THR A 53   SER A 58   
C  3 VAL A 102  ? GLU A 105  ? VAL A 102  GLU A 105  
C  4 SER A 114  ? ARG A 116  ? SER A 114  ARG A 116  
D  1 VAL A 134  ? TYR A 135  ? VAL A 134  TYR A 135  
D  2 THR A 212  ? VAL A 219  ? THR A 212  VAL A 219  
D  3 GLY A 197  ? TYR A 205  ? GLY A 197  TYR A 205  
D  4 GLU A 158  ? LEU A 161  ? GLU A 158  LEU A 161  
D  5 VAL A 174  ? ILE A 177  ? VAL A 174  ILE A 177  
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 PHE A 125  ? PHE A 127  ? PHE A 125  PHE A 127  
E  4 VAL A 145  ? LEU A 148  ? VAL A 145  LEU A 148  
E  5 ILE A 182  ? ILE A 183  ? ILE A 182  ILE A 183  
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  ? VAL A 229  ? SER A 228  VAL A 229  
H  2 ALA A 252  ? ARG A 253  ? ALA A 252  ARG A 253  
I  1 GLU A 247  ? THR A 249  ? GLU A 247  THR A 249  
I  2 GLN A 298  ? THR A 300  ? GLN A 298  THR A 300  
J  1 ALA A 263  ? GLY A 270  ? ALA A 263  GLY A 270  
J  2 TYR A 324  ? GLU A 331  ? TYR A 324  GLU A 331  
J  3 GLU A 338  ? ILE A 342  ? GLU A 338  ILE A 342  
K  1 PRO A 368  ? TYR A 369  ? PRO A 368  TYR A 369  
K  2 LEU A 422  ? ASN A 423  ? LEU A 422  ASN A 423  
L  1 LYS A 372  ? GLN A 374  ? LYS A 372  GLN A 374  
L  2 VAL A 417  ? SER A 419  ? VAL A 417  SER A 419  
M  1 THR A 401  ? ASP A 403  ? THR A 401  ASP A 403  
M  2 PRO A 387  ? ILE A 395  ? PRO A 387  ILE A 395  
M  3 SER A 407  ? VAL A 410  ? SER A 407  VAL A 410  
N  1 THR A 401  ? ASP A 403  ? THR A 401  ASP A 403  
N  2 PRO A 387  ? ILE A 395  ? PRO A 387  ILE A 395  
N  3 VAL A 430  ? ASN A 434  ? VAL A 430  ASN A 434  
N  4 ALA A 454  ? ILE A 455  ? ALA A 454  ILE A 455  
O  1 TYR A 466  ? TRP A 469  ? TYR A 466  TRP A 469  
O  2 HIS A 481  ? THR A 487  ? HIS A 481  THR A 487  
O  3 SER A 525  ? PRO A 529  ? SER A 525  PRO A 529  
P  1 ALA A 552  ? TRP A 560  ? ALA A 552  TRP A 560  
P  2 ARG A 539  ? THR A 547  ? ARG A 539  THR A 547  
P  3 HIS A 498  ? SER A 505  ? HIS A 498  SER A 505  
P  4 LYS A 508  ? GLU A 516  ? LYS A 508  GLU A 516  
P  5 ASN B 17   ? SER B 24   ? ASN X 145  SER X 152  
P  6 HIS B 7    ? VAL B 13   ? HIS X 135  VAL X 141  
P  7 LEU B 100  ? LYS B 101  ? LEU X 228  LYS X 229  
P  8 TYR B 58   ? GLY B 59   ? TYR X 186  GLY X 187  
Q  1 ALA A 552  ? TRP A 560  ? ALA A 552  TRP A 560  
Q  2 ARG A 539  ? THR A 547  ? ARG A 539  THR A 547  
Q  3 HIS A 498  ? SER A 505  ? HIS A 498  SER A 505  
Q  4 LYS A 508  ? GLU A 516  ? LYS A 508  GLU A 516  
Q  5 ASN B 17   ? SER B 24   ? ASN X 145  SER X 152  
Q  6 HIS B 7    ? VAL B 13   ? HIS X 135  VAL X 141  
Q  7 ILE B 96   ? GLU B 97   ? ILE X 224  GLU X 225  
Q  8 THR B 62   ? ASN B 64   ? THR X 190  ASN X 192  
Q  9 LYS B 70   ? GLN B 71   ? LYS X 198  GLN X 199  
R  1 HIS A 574  ? LEU A 575  ? HIS A 574  LEU A 575  
R  2 LEU A 590  ? ALA A 593  ? LEU A 590  ALA A 593  
R  3 ARG A 783  ? GLN A 785  ? ARG A 783  GLN A 785  
S  1 VAL A 777  ? VAL A 780  ? VAL A 777  VAL A 780  
S  2 SER A 598  ? ALA A 601  ? SER A 598  ALA A 601  
S  3 ILE A 802  ? SER A 805  ? ILE A 802  SER A 805  
S  4 GLY A 808  ? VAL A 811  ? GLY A 808  VAL A 811  
T  1 ALA A 604  ? ASP A 606  ? ALA A 604  ASP A 606  
T  2 TRP A 797  ? ILE A 799  ? TRP A 797  ILE A 799  
U  1 VAL A 823  ? ASN A 828  ? VAL A 823  ASN A 828  
U  2 ILE A 839  ? ASN A 847  ? ILE A 839  ASN A 847  
U  3 SER A 893  ? VAL A 900  ? SER A 893  VAL A 900  
V  1 SER A 832  ? VAL A 834  ? SER A 832  VAL A 834  
V  2 ARG A 928  ? VAL A 930  ? ARG A 928  VAL A 930  
W  1 MET A 853  ? PHE A 855  ? MET A 853  PHE A 855  
W  2 GLN A 886  ? VAL A 888  ? GLN A 886  VAL A 888  
X  1 LYS A 858  ? MET A 859  ? LYS A 858  MET A 859  
X  2 ILE A 910  ? THR A 916  ? ILE A 910  THR A 916  
X  3 GLY A 919  ? LYS A 925  ? GLY A 919  LYS A 925  
Y  1 VAL A 934  ? GLU A 937  ? VAL A 934  GLU A 937  
Y  2 ALA A 1357 ? HIS A 1366 ? ALA A 1357 HIS A 1366 
Y  3 LYS A 974  ? GLY A 981  ? LYS A 974  GLY A 981  
Y  4 GLU A 1339 ? VAL A 1340 ? GLU A 1339 VAL A 1340 
Z  1 LEU A 1217 ? LYS A 1219 ? LEU A 1217 LYS A 1219 
Z  2 TYR A 1225 ? PHE A 1227 ? TYR A 1225 PHE A 1227 
AA 1 PHE A 1377 ? GLN A 1384 ? PHE A 1377 GLN A 1384 
AA 2 ARG A 1401 ? TYR A 1408 ? ARG A 1401 TYR A 1408 
AA 3 VAL A 1475 ? ARG A 1478 ? VAL A 1475 ARG A 1478 
AB 1 ILE A 1455 ? LYS A 1456 ? ILE A 1455 LYS A 1456 
AB 2 HIS A 1459 ? LEU A 1464 ? HIS A 1459 LEU A 1464 
AB 3 ALA A 1422 ? SER A 1427 ? ALA A 1422 SER A 1427 
AB 4 ALA A 1491 ? GLU A 1497 ? ALA A 1491 GLU A 1497 
AB 5 ARG A 1500 ? TYR A 1509 ? ARG A 1500 TYR A 1509 
AC 1 GLU B 31   ? SER B 33   ? GLU X 159  SER X 161  
AC 2 VAL B 87   ? ASN B 89   ? VAL X 215  ASN X 217  
AD 1 GLN C 80   ? ASN C 81   ? GLN B 80   ASN B 81   
AD 2 ILE C 41   ? VAL C 43   ? ILE B 41   VAL B 43   
AD 3 TYR C 23   ? PRO C 28   ? TYR B 23   PRO B 28   
AD 4 LEU C 651  ? LEU C 654  ? LEU B 651  LEU B 654  
AE 1 PHE C 31   ? ARG C 32   ? PHE B 31   ARG B 32   
AE 2 ILE C 119  ? THR C 120  ? ILE B 119  THR B 120  
AF 1 SER C 65   ? HIS C 70   ? SER B 65   HIS B 70   
AF 2 THR C 53   ? SER C 58   ? THR B 53   SER B 58   
AF 3 VAL C 102  ? VAL C 107  ? VAL B 102  VAL B 107  
AF 4 SER C 112  ? MET C 117  ? SER B 112  MET B 117  
AG 1 PHE C 125  ? PHE C 127  ? PHE B 125  PHE B 127  
AG 2 VAL C 145  ? LEU C 148  ? VAL B 145  LEU B 148  
AG 3 ILE C 182  ? ILE C 183  ? ILE B 182  ILE B 183  
AH 1 VAL C 134  ? TYR C 135  ? VAL B 134  TYR B 135  
AH 2 THR C 212  ? VAL C 219  ? THR B 212  VAL B 219  
AH 3 GLY C 197  ? TYR C 205  ? GLY B 197  TYR B 205  
AH 4 GLU C 158  ? LEU C 161  ? GLU B 158  LEU B 161  
AH 5 VAL C 174  ? ILE C 177  ? VAL B 174  ILE B 177  
AI 1 SER C 140  ? VAL C 141  ? SER B 140  VAL B 141  
AI 2 PHE C 188  ? LYS C 189  ? PHE B 188  LYS B 189  
AJ 1 GLU C 221  ? TYR C 222  ? GLU B 221  TYR B 222  
AJ 2 GLU C 764  ? ILE C 765  ? GLU B 764  ILE B 765  
AK 1 PHE C 227  ? VAL C 229  ? PHE B 227  VAL B 229  
AK 2 ALA C 252  ? TYR C 254  ? ALA B 252  TYR B 254  
AK 3 LYS C 258  ? VAL C 259  ? LYS B 258  VAL B 259  
AL 1 GLU C 247  ? THR C 249  ? GLU B 247  THR B 249  
AL 2 GLN C 298  ? THR C 300  ? GLN B 298  THR B 300  
AM 1 ALA C 263  ? GLY C 270  ? ALA B 263  GLY B 270  
AM 2 TYR C 324  ? GLU C 331  ? TYR B 324  GLU B 331  
AM 3 GLU C 339  ? ILE C 342  ? GLU B 339  ILE B 342  
AN 1 PRO C 368  ? GLN C 374  ? PRO B 368  GLN B 374  
AN 2 VAL C 417  ? ASN C 423  ? VAL B 417  ASN B 423  
AO 1 THR C 401  ? ASP C 403  ? THR B 401  ASP B 403  
AO 2 PRO C 387  ? ILE C 395  ? PRO B 387  ILE B 395  
AO 3 VAL C 430  ? LYS C 436  ? VAL B 430  LYS B 436  
AO 4 ARG C 449  ? GLY C 451  ? ARG B 449  GLY B 451  
AP 1 SER C 407  ? VAL C 410  ? SER B 407  VAL B 410  
AP 2 PRO C 387  ? ILE C 395  ? PRO B 387  ILE B 395  
AP 3 VAL C 430  ? LYS C 436  ? VAL B 430  LYS B 436  
AP 4 ALA C 454  ? ILE C 455  ? ALA B 454  ILE B 455  
AQ 1 ILE C 467  ? TRP C 469  ? ILE B 467  TRP B 469  
AQ 2 HIS C 481  ? VAL C 486  ? HIS B 481  VAL B 486  
AQ 3 SER C 525  ? PRO C 529  ? SER B 525  PRO B 529  
AR 1 ALA C 552  ? TRP C 560  ? ALA B 552  TRP B 560  
AR 2 ARG C 539  ? THR C 547  ? ARG B 539  THR B 547  
AR 3 HIS C 498  ? LEU C 504  ? HIS B 498  LEU B 504  
AR 4 ILE C 509  ? GLU C 516  ? ILE B 509  GLU B 516  
AR 5 ASN D 17   ? SER D 24   ? ASN Y 145  SER Y 152  
AR 6 HIS D 7    ? VAL D 13   ? HIS Y 135  VAL Y 141  
AR 7 LEU D 100  ? LYS D 101  ? LEU Y 228  LYS Y 229  
AR 8 TYR D 58   ? GLY D 59   ? TYR Y 186  GLY Y 187  
AS 1 ALA C 552  ? TRP C 560  ? ALA B 552  TRP B 560  
AS 2 ARG C 539  ? THR C 547  ? ARG B 539  THR B 547  
AS 3 HIS C 498  ? LEU C 504  ? HIS B 498  LEU B 504  
AS 4 ILE C 509  ? GLU C 516  ? ILE B 509  GLU B 516  
AS 5 ASN D 17   ? SER D 24   ? ASN Y 145  SER Y 152  
AS 6 HIS D 7    ? VAL D 13   ? HIS Y 135  VAL Y 141  
AS 7 ILE D 96   ? GLU D 97   ? ILE Y 224  GLU Y 225  
AS 8 THR D 62   ? ASN D 64   ? THR Y 190  ASN Y 192  
AS 9 LYS D 70   ? GLN D 71   ? LYS Y 198  GLN Y 199  
AT 1 GLN C 572  ? LEU C 575  ? GLN B 572  LEU B 575  
AT 2 LEU C 590  ? ALA C 593  ? LEU B 590  ALA B 593  
AT 3 ARG C 783  ? LEU C 786  ? ARG B 783  LEU B 786  
AU 1 VAL C 777  ? VAL C 780  ? VAL B 777  VAL B 780  
AU 2 SER C 598  ? ALA C 601  ? SER B 598  ALA B 601  
AU 3 ILE C 802  ? SER C 805  ? ILE B 802  SER B 805  
AU 4 GLY C 808  ? VAL C 811  ? GLY B 808  VAL B 811  
AV 1 ALA C 604  ? ASP C 606  ? ALA B 604  ASP B 606  
AV 2 THR C 795  ? ILE C 799  ? THR B 795  ILE B 799  
AV 3 LYS C 816  ? VAL C 819  ? LYS B 816  VAL B 819  
AW 1 PHE C 824  ? ASN C 828  ? PHE B 824  ASN B 828  
AW 2 ILE C 839  ? TYR C 846  ? ILE B 839  TYR B 846  
AW 3 SER C 893  ? PRO C 902  ? SER B 893  PRO B 902  
AW 4 ILE C 865  ? CYS C 866  ? ILE B 865  CYS B 866  
AX 1 SER C 832  ? VAL C 834  ? SER B 832  VAL B 834  
AX 2 ARG C 928  ? VAL C 930  ? ARG B 928  VAL B 930  
AY 1 MET C 853  ? GLN C 854  ? MET B 853  GLN B 854  
AY 2 LYS C 887  ? VAL C 888  ? LYS B 887  VAL B 888  
AZ 1 LYS C 858  ? MET C 859  ? LYS B 858  MET B 859  
AZ 2 ILE C 910  ? THR C 916  ? ILE B 910  THR B 916  
AZ 3 GLY C 919  ? LYS C 925  ? GLY B 919  LYS B 925  
BA 1 VAL C 934  ? ARG C 936  ? VAL B 934  ARG B 936  
BA 2 THR C 1363 ? HIS C 1366 ? THR B 1363 HIS B 1366 
BA 3 LYS C 974  ? ILE C 976  ? LYS B 974  ILE B 976  
BA 4 GLU C 1339 ? VAL C 1340 ? GLU B 1339 VAL B 1340 
BB 1 GLY C 941  ? LEU C 944  ? GLY B 941  LEU B 944  
BB 2 ALA C 1357 ? HIS C 1360 ? ALA B 1357 HIS B 1360 
BB 3 SER C 978  ? GLY C 981  ? SER B 978  GLY B 981  
BC 1 LEU C 1217 ? LYS C 1219 ? LEU B 1217 LYS B 1219 
BC 2 TYR C 1225 ? PHE C 1227 ? TYR B 1225 PHE B 1227 
BD 1 PHE C 1377 ? GLN C 1384 ? PHE B 1377 GLN B 1384 
BD 2 ARG C 1401 ? TYR C 1408 ? ARG B 1401 TYR B 1408 
BD 3 VAL C 1475 ? ARG C 1478 ? VAL B 1475 ARG B 1478 
BE 1 ILE C 1455 ? LYS C 1456 ? ILE B 1455 LYS B 1456 
BE 2 HIS C 1459 ? LEU C 1464 ? HIS B 1459 LEU B 1464 
BE 3 ALA C 1422 ? SER C 1427 ? ALA B 1422 SER B 1427 
BE 4 ALA C 1491 ? GLU C 1497 ? ALA B 1491 GLU B 1497 
BE 5 ARG C 1500 ? TYR C 1509 ? ARG B 1500 TYR B 1509 
BF 1 GLU D 31   ? SER D 33   ? GLU Y 159  SER Y 161  
BF 2 VAL D 87   ? ASN D 89   ? VAL Y 215  ASN Y 217  
# 
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 TYR A 66   ? O TYR A 66   N ILE A 56   ? N ILE A 56   
C  2 3 N SER A 55   ? N SER A 55   O GLU A 105  ? O GLU A 105  
C  3 4 N LEU A 104  ? N LEU A 104  O LYS A 115  ? O LYS A 115  
D  1 2 N TYR A 135  ? N TYR A 135  O GLU A 218  ? O GLU A 218  
D  2 3 O GLY A 213  ? O GLY A 213  N ALA A 203  ? N ALA A 203  
D  3 4 O LYS A 204  ? O LYS A 204  N VAL A 160  ? N VAL A 160  
D  4 5 N LEU A 161  ? N LEU A 161  O VAL A 174  ? O VAL A 174  
E  1 2 N TYR A 135  ? N TYR A 135  O GLU A 218  ? O GLU A 218  
E  2 3 O THR A 214  ? O THR A 214  N LEU A 126  ? N LEU A 126  
E  3 4 N PHE A 127  ? N PHE A 127  O TYR A 146  ? O TYR A 146  
E  4 5 N VAL A 145  ? N VAL A 145  O ILE A 183  ? O ILE A 183  
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 SER A 228  ? N SER A 228  O ARG A 253  ? O ARG A 253  
I  1 2 N ILE A 248  ? N ILE A 248  O VAL A 299  ? O VAL A 299  
J  1 2 N TYR A 266  ? N TYR A 266  O THR A 328  ? O THR A 328  
J  2 3 N ILE A 325  ? N ILE A 325  O ILE A 342  ? O ILE A 342  
K  1 2 N TYR A 369  ? N TYR A 369  O LEU A 422  ? O LEU A 422  
L  1 2 N VAL A 373  ? N VAL A 373  O ALA A 418  ? O ALA A 418  
M  1 2 O SER A 402  ? O SER A 402  N THR A 394  ? N THR A 394  
M  2 3 N LEU A 390  ? N LEU A 390  O SER A 407  ? O SER A 407  
N  1 2 O SER A 402  ? O SER A 402  N THR A 394  ? N THR A 394  
N  2 3 N ASN A 391  ? N ASN A 391  O ASN A 434  ? O ASN A 434  
N  3 4 N LEU A 431  ? N LEU A 431  O ALA A 454  ? O ALA A 454  
O  1 2 N ASP A 468  ? N ASP A 468  O ILE A 485  ? O ILE A 485  
O  2 3 N ILE A 484  ? N ILE A 484  O ILE A 526  ? O ILE A 526  
P  1 2 O GLU A 553  ? O GLU A 553  N VAL A 546  ? N VAL A 546  
P  2 3 O ARG A 539  ? O ARG A 539  N LEU A 504  ? N LEU A 504  
P  3 4 N ILE A 503  ? N ILE A 503  O HIS A 511  ? O HIS A 511  
P  4 5 N PHE A 512  ? N PHE A 512  O ALA B 20   ? O ALA X 148  
P  5 6 O SER B 21   ? O SER X 149  N VAL B 10   ? N VAL X 138  
P  6 7 N ASN B 11   ? N ASN X 139  O LEU B 100  ? O LEU X 228  
P  7 8 O LYS B 101  ? O LYS X 229  N TYR B 58   ? N TYR X 186  
Q  1 2 O GLU A 553  ? O GLU A 553  N VAL A 546  ? N VAL A 546  
Q  2 3 O ARG A 539  ? O ARG A 539  N LEU A 504  ? N LEU A 504  
Q  3 4 N ILE A 503  ? N ILE A 503  O HIS A 511  ? O HIS A 511  
Q  4 5 N PHE A 512  ? N PHE A 512  O ALA B 20   ? O ALA X 148  
Q  5 6 O SER B 21   ? O SER X 149  N VAL B 10   ? N VAL X 138  
Q  6 7 N PHE B 9    ? N PHE X 137  O ILE B 96   ? O ILE X 224  
Q  7 8 O GLU B 97   ? O GLU X 225  N THR B 62   ? N THR X 190  
Q  8 9 N ILE B 63   ? N ILE X 191  O GLN B 71   ? O GLN X 199  
R  1 2 N HIS A 574  ? N HIS A 574  O ASN A 591  ? O ASN A 591  
R  2 3 N MET A 592  ? N MET A 592  O LYS A 784  ? O LYS A 784  
S  1 2 O VAL A 780  ? O VAL A 780  N SER A 598  ? N SER A 598  
S  2 3 N TRP A 599  ? N TRP A 599  O ILE A 804  ? O ILE A 804  
S  3 4 N GLY A 803  ? N GLY A 803  O CYS A 810  ? O CYS A 810  
T  1 2 N VAL A 605  ? N VAL A 605  O GLU A 798  ? O GLU A 798  
U  1 2 N PHE A 824  ? N PHE A 824  O TYR A 846  ? O TYR A 846  
U  2 3 N ILE A 839  ? N ILE A 839  O VAL A 900  ? O VAL A 900  
V  1 2 N VAL A 833  ? N VAL A 833  O VAL A 930  ? O VAL A 930  
W  1 2 N MET A 853  ? N MET A 853  O VAL A 888  ? O VAL A 888  
X  1 2 N LYS A 858  ? N LYS A 858  O SER A 913  ? O SER A 913  
X  2 3 N THR A 916  ? N THR A 916  O GLY A 919  ? O GLY A 919  
Y  1 2 N LYS A 935  ? N LYS A 935  O VAL A 1365 ? O VAL A 1365 
Y  2 3 O VAL A 1364 ? O VAL A 1364 N LYS A 974  ? N LYS A 974  
Y  3 4 N ARG A 975  ? N ARG A 975  O VAL A 1340 ? O VAL A 1340 
Z  1 2 N LYS A 1219 ? N LYS A 1219 O TYR A 1225 ? O TYR A 1225 
AA 1 2 N LYS A 1380 ? N LYS A 1380 O CYS A 1405 ? O CYS A 1405 
AA 2 3 N ILE A 1402 ? N ILE A 1402 O PHE A 1477 ? O PHE A 1477 
AB 1 2 N LYS A 1456 ? N LYS A 1456 O HIS A 1459 ? O HIS A 1459 
AB 2 3 O VAL A 1460 ? O VAL A 1460 N ILE A 1426 ? N ILE A 1426 
AB 3 4 N ASP A 1425 ? N ASP A 1425 O THR A 1494 ? O THR A 1494 
AB 4 5 N PHE A 1493 ? N PHE A 1493 O MET A 1507 ? O MET A 1507 
AC 1 2 N VAL B 32   ? N VAL X 160  O LEU B 88   ? O LEU X 216  
AD 1 2 O ASN C 81   ? O ASN B 81   N ILE C 41   ? N ILE B 41   
AD 2 3 O GLN C 42   ? O GLN B 42   N VAL C 24   ? N VAL B 24   
AD 3 4 N ILE C 25   ? N ILE B 25   O LEU C 654  ? O LEU B 654  
AE 1 2 N PHE C 31   ? N PHE B 31   O THR C 120  ? O THR B 120  
AF 1 2 O TYR C 66   ? O TYR B 66   N ILE C 56   ? N ILE B 56   
AF 2 3 N LYS C 57   ? N LYS B 57   O TYR C 103  ? O TYR B 103  
AF 3 4 N LEU C 104  ? N LEU B 104  O LYS C 115  ? O LYS B 115  
AG 1 2 N PHE C 127  ? N PHE B 127  O TYR C 146  ? O TYR B 146  
AG 2 3 N VAL C 145  ? N VAL B 145  O ILE C 183  ? O ILE B 183  
AH 1 2 N TYR C 135  ? N TYR B 135  O GLU C 218  ? O GLU B 218  
AH 2 3 O GLY C 213  ? O GLY B 213  N ALA C 203  ? N ALA B 203  
AH 3 4 O LYS C 204  ? O LYS B 204  N VAL C 160  ? N VAL B 160  
AH 4 5 N LEU C 161  ? N LEU B 161  O VAL C 174  ? O VAL B 174  
AI 1 2 N VAL C 141  ? N VAL B 141  O PHE C 188  ? O PHE B 188  
AJ 1 2 N GLU C 221  ? N GLU B 221  O ILE C 765  ? O ILE B 765  
AK 1 2 N SER C 228  ? N SER B 228  O ARG C 253  ? O ARG B 253  
AK 2 3 N TYR C 254  ? N TYR B 254  O LYS C 258  ? O LYS B 258  
AL 1 2 N ILE C 248  ? N ILE B 248  O VAL C 299  ? O VAL B 299  
AM 1 2 N TYR C 266  ? N TYR B 266  O THR C 328  ? O THR B 328  
AM 2 3 N ILE C 325  ? N ILE B 325  O ILE C 342  ? O ILE B 342  
AN 1 2 N TYR C 369  ? N TYR B 369  O LEU C 422  ? O LEU B 422  
AO 1 2 O SER C 402  ? O SER B 402  N THR C 394  ? N THR B 394  
AO 2 3 N ASN C 391  ? N ASN B 391  O ASN C 434  ? O ASN B 434  
AO 3 4 N VAL C 435  ? N VAL B 435  O GLU C 450  ? O GLU B 450  
AP 1 2 O SER C 407  ? O SER B 407  N LEU C 390  ? N LEU B 390  
AP 2 3 N ASN C 391  ? N ASN B 391  O ASN C 434  ? O ASN B 434  
AP 3 4 N LEU C 431  ? N LEU B 431  O ALA C 454  ? O ALA B 454  
AQ 1 2 N ASP C 468  ? N ASP B 468  O ILE C 485  ? O ILE B 485  
AQ 2 3 N LEU C 482  ? N LEU B 482  O ILE C 528  ? O ILE B 528  
AR 1 2 O GLU C 553  ? O GLU B 553  N VAL C 546  ? N VAL B 546  
AR 2 3 O ARG C 539  ? O ARG B 539  N LEU C 504  ? N LEU B 504  
AR 3 4 N ILE C 503  ? N ILE B 503  O HIS C 511  ? O HIS B 511  
AR 4 5 N PHE C 512  ? N PHE B 512  O ALA D 20   ? O ALA Y 148  
AR 5 6 O SER D 21   ? O SER Y 149  N VAL D 10   ? N VAL Y 138  
AR 6 7 N ASN D 11   ? N ASN Y 139  O LEU D 100  ? O LEU Y 228  
AR 7 8 O LYS D 101  ? O LYS Y 229  N TYR D 58   ? N TYR Y 186  
AS 1 2 O GLU C 553  ? O GLU B 553  N VAL C 546  ? N VAL B 546  
AS 2 3 O ARG C 539  ? O ARG B 539  N LEU C 504  ? N LEU B 504  
AS 3 4 N ILE C 503  ? N ILE B 503  O HIS C 511  ? O HIS B 511  
AS 4 5 N PHE C 512  ? N PHE B 512  O ALA D 20   ? O ALA Y 148  
AS 5 6 O SER D 21   ? O SER Y 149  N VAL D 10   ? N VAL Y 138  
AS 6 7 N PHE D 9    ? N PHE Y 137  O ILE D 96   ? O ILE Y 224  
AS 7 8 O GLU D 97   ? O GLU Y 225  N THR D 62   ? N THR Y 190  
AS 8 9 N ILE D 63   ? N ILE Y 191  O GLN D 71   ? O GLN Y 199  
AT 1 2 N HIS C 574  ? N HIS B 574  O ASN C 591  ? O ASN B 591  
AT 2 3 N LEU C 590  ? N LEU B 590  O LEU C 786  ? O LEU B 786  
AU 1 2 O VAL C 780  ? O VAL B 780  N SER C 598  ? N SER B 598  
AU 2 3 N TRP C 599  ? N TRP B 599  O ILE C 804  ? O ILE B 804  
AU 3 4 N GLY C 803  ? N GLY B 803  O CYS C 810  ? O CYS B 810  
AV 1 2 N VAL C 605  ? N VAL B 605  O GLU C 798  ? O GLU B 798  
AV 2 3 N THR C 795  ? N THR B 795  O VAL C 819  ? O VAL B 819  
AW 1 2 N PHE C 824  ? N PHE B 824  O TYR C 846  ? O TYR B 846  
AW 2 3 N ILE C 839  ? N ILE B 839  O VAL C 900  ? O VAL B 900  
AW 3 4 O LEU C 901  ? O LEU B 901  N CYS C 866  ? N CYS B 866  
AX 1 2 N VAL C 833  ? N VAL B 833  O VAL C 930  ? O VAL B 930  
AY 1 2 N MET C 853  ? N MET B 853  O VAL C 888  ? O VAL B 888  
AZ 1 2 N LYS C 858  ? N LYS B 858  O SER C 913  ? O SER B 913  
AZ 2 3 N PHE C 912  ? N PHE B 912  O LEU C 923  ? O LEU B 923  
BA 1 2 N LYS C 935  ? N LYS B 935  O VAL C 1365 ? O VAL B 1365 
BA 2 3 O VAL C 1364 ? O VAL B 1364 N LYS C 974  ? N LYS B 974  
BA 3 4 N ARG C 975  ? N ARG B 975  O VAL C 1340 ? O VAL B 1340 
BB 1 2 N LEU C 944  ? N LEU B 944  O ALA C 1357 ? O ALA B 1357 
BB 2 3 O HIS C 1360 ? O HIS B 1360 N SER C 978  ? N SER B 978  
BC 1 2 N LYS C 1219 ? N LYS B 1219 O TYR C 1225 ? O TYR B 1225 
BD 1 2 N LYS C 1380 ? N LYS B 1380 O CYS C 1405 ? O CYS B 1405 
BD 2 3 N ILE C 1402 ? N ILE B 1402 O PHE C 1477 ? O PHE B 1477 
BE 1 2 N LYS C 1456 ? N LYS B 1456 O HIS C 1459 ? O HIS B 1459 
BE 2 3 O LEU C 1462 ? O LEU B 1462 N MET C 1424 ? N MET B 1424 
BE 3 4 N ASP C 1425 ? N ASP B 1425 O THR C 1494 ? O THR B 1494 
BE 4 5 N PHE C 1493 ? N PHE B 1493 O MET C 1507 ? O MET B 1507 
BF 1 2 N VAL D 32   ? N VAL Y 160  O LEU D 88   ? O LEU Y 216  
# 
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 ? ? ? ? 4 'BINDING SITE FOR RESIDUE CD A 1678'  
AC3 Software ? ? ? ? 2 'BINDING SITE FOR RESIDUE CD A 1679'  
AC4 Software ? ? ? ? 3 'BINDING SITE FOR RESIDUE NAG A 2001' 
AC5 Software ? ? ? ? 1 'BINDING SITE FOR RESIDUE NAG A 2002' 
AC6 Software ? ? ? ? 3 'BINDING SITE FOR RESIDUE CD B 1677'  
AC7 Software ? ? ? ? 2 'BINDING SITE FOR RESIDUE CD B 1678'  
AC8 Software ? ? ? ? 3 'BINDING SITE FOR RESIDUE NAG B 2001' 
AC9 Software ? ? ? ? 1 'BINDING SITE FOR RESIDUE NAG B 2002' 
BC1 Software ? ? ? ? 1 'BINDING SITE FOR RESIDUE NAG A 1680' 
BC2 Software ? ? ? ? 1 'BINDING SITE FOR RESIDUE NAG B 1679' 
# 
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 4 ASP A 471 ? ASP A 471  . ? 1_555 ? 
4  AC2 4 HIS A 473 ? HIS A 473  . ? 1_555 ? 
5  AC2 4 ALA A 475 ? ALA A 475  . ? 1_555 ? 
6  AC2 4 GLU A 480 ? GLU A 480  . ? 1_555 ? 
7  AC3 2 ASP A 264 ? ASP A 264  . ? 1_555 ? 
8  AC3 2 HIS A 753 ? HIS A 753  . ? 1_555 ? 
9  AC4 3 ASN A 911 ? ASN A 911  . ? 1_555 ? 
10 AC4 3 ILE A 922 ? ILE A 922  . ? 1_555 ? 
11 AC4 3 NAG I .   ? NAG A 2002 . ? 1_555 ? 
12 AC5 1 NAG H .   ? NAG A 2001 . ? 1_555 ? 
13 AC6 3 ASP C 471 ? ASP B 471  . ? 1_555 ? 
14 AC6 3 HIS C 473 ? HIS B 473  . ? 1_555 ? 
15 AC6 3 GLU C 480 ? GLU B 480  . ? 1_555 ? 
16 AC7 2 ASP C 264 ? ASP B 264  . ? 1_555 ? 
17 AC7 2 HIS C 753 ? HIS B 753  . ? 1_555 ? 
18 AC8 3 ASN C 911 ? ASN B 911  . ? 1_555 ? 
19 AC8 3 ILE C 922 ? ILE B 922  . ? 1_555 ? 
20 AC8 3 NAG N .   ? NAG B 2002 . ? 1_555 ? 
21 AC9 1 NAG M .   ? NAG B 2001 . ? 1_555 ? 
22 BC1 1 ASN A 741 ? ASN A 741  . ? 1_555 ? 
23 BC2 1 ASN C 741 ? ASN B 741  . ? 1_555 ? 
# 
_database_PDB_matrix.entry_id          3KM9 
_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                    3KM9 
_atom_sites.fract_transf_matrix[1][1]   0.006907 
_atom_sites.fract_transf_matrix[1][2]   0.003988 
_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]   0.007975 
_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]   0.004077 
_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   ? -24.318 35.767  14.782  1.00 227.01 ? 22   THR A N   1 
ATOM   2     C  CA  . THR A 1 22   ? -23.396 35.380  13.722  1.00 224.20 ? 22   THR A CA  1 
ATOM   3     C  C   . THR A 1 22   ? -22.955 33.922  13.874  1.00 222.27 ? 22   THR A C   1 
ATOM   4     O  O   . THR A 1 22   ? -23.208 33.275  14.903  1.00 222.80 ? 22   THR A O   1 
ATOM   5     C  CB  . THR A 1 22   ? -22.170 36.320  13.651  1.00 220.98 ? 22   THR A CB  1 
ATOM   6     O  OG1 . THR A 1 22   ? -21.895 36.840  14.955  1.00 218.65 ? 22   THR A OG1 1 
ATOM   7     C  CG2 . THR A 1 22   ? -22.436 37.489  12.707  1.00 219.70 ? 22   THR A CG2 1 
ATOM   8     N  N   . TYR A 1 23   ? -22.290 33.422  12.834  1.00 193.44 ? 23   TYR A N   1 
ATOM   9     C  CA  . TYR A 1 23   ? -22.007 31.994  12.690  1.00 198.84 ? 23   TYR A CA  1 
ATOM   10    C  C   . TYR A 1 23   ? -20.519 31.620  12.729  1.00 196.94 ? 23   TYR A C   1 
ATOM   11    O  O   . TYR A 1 23   ? -19.658 32.360  12.243  1.00 192.84 ? 23   TYR A O   1 
ATOM   12    C  CB  . TYR A 1 23   ? -22.656 31.450  11.405  1.00 206.02 ? 23   TYR A CB  1 
ATOM   13    C  CG  . TYR A 1 23   ? -22.349 32.248  10.146  1.00 211.20 ? 23   TYR A CG  1 
ATOM   14    C  CD1 . TYR A 1 23   ? -21.421 33.281  10.161  1.00 210.17 ? 23   TYR A CD1 1 
ATOM   15    C  CD2 . TYR A 1 23   ? -22.990 31.960  8.946   1.00 216.26 ? 23   TYR A CD2 1 
ATOM   16    C  CE1 . TYR A 1 23   ? -21.144 33.993  9.035   1.00 211.19 ? 23   TYR A CE1 1 
ATOM   17    C  CE2 . TYR A 1 23   ? -22.714 32.670  7.814   1.00 216.11 ? 23   TYR A CE2 1 
ATOM   18    C  CZ  . TYR A 1 23   ? -21.792 33.681  7.865   1.00 214.43 ? 23   TYR A CZ  1 
ATOM   19    O  OH  . TYR A 1 23   ? -21.525 34.381  6.727   1.00 213.97 ? 23   TYR A OH  1 
ATOM   20    N  N   . VAL A 1 24   ? -20.238 30.457  13.311  1.00 198.84 ? 24   VAL A N   1 
ATOM   21    C  CA  . VAL A 1 24   ? -18.882 29.934  13.399  1.00 195.36 ? 24   VAL A CA  1 
ATOM   22    C  C   . VAL A 1 24   ? -18.820 28.531  12.850  1.00 194.79 ? 24   VAL A C   1 
ATOM   23    O  O   . VAL A 1 24   ? -19.692 27.694  13.092  1.00 196.97 ? 24   VAL A O   1 
ATOM   24    C  CB  . VAL A 1 24   ? -18.354 29.889  14.836  1.00 197.80 ? 24   VAL A CB  1 
ATOM   25    C  CG1 . VAL A 1 24   ? -17.514 28.634  15.043  1.00 199.31 ? 24   VAL A CG1 1 
ATOM   26    C  CG2 . VAL A 1 24   ? -17.551 31.149  15.154  1.00 194.32 ? 24   VAL A CG2 1 
ATOM   27    N  N   . ILE A 1 25   ? -17.751 28.289  12.117  1.00 204.29 ? 25   ILE A N   1 
ATOM   28    C  CA  . ILE A 1 25   ? -17.539 27.038  11.436  1.00 210.13 ? 25   ILE A CA  1 
ATOM   29    C  C   . ILE A 1 25   ? -16.045 26.850  11.506  1.00 207.75 ? 25   ILE A C   1 
ATOM   30    O  O   . ILE A 1 25   ? -15.291 27.461  10.757  1.00 205.89 ? 25   ILE A O   1 
ATOM   31    C  CB  . ILE A 1 25   ? -17.994 27.131  9.955   1.00 215.13 ? 25   ILE A CB  1 
ATOM   32    C  CG1 . ILE A 1 25   ? -19.455 27.579  9.870   1.00 220.16 ? 25   ILE A CG1 1 
ATOM   33    C  CG2 . ILE A 1 25   ? -17.805 25.802  9.232   1.00 218.40 ? 25   ILE A CG2 1 
ATOM   34    C  CD1 . ILE A 1 25   ? -20.439 26.538  10.317  1.00 225.75 ? 25   ILE A CD1 1 
ATOM   35    N  N   . SER A 1 26   ? -15.597 26.039  12.440  1.00 176.81 ? 26   SER A N   1 
ATOM   36    C  CA  . SER A 1 26   ? -14.175 25.856  12.552  1.00 173.69 ? 26   SER A CA  1 
ATOM   37    C  C   . SER A 1 26   ? -13.709 24.720  11.650  1.00 176.45 ? 26   SER A C   1 
ATOM   38    O  O   . SER A 1 26   ? -14.497 23.852  11.251  1.00 178.19 ? 26   SER A O   1 
ATOM   39    C  CB  . SER A 1 26   ? -13.800 25.601  14.009  1.00 178.37 ? 26   SER A CB  1 
ATOM   40    O  OG  . SER A 1 26   ? -14.503 26.491  14.856  1.00 179.31 ? 26   SER A OG  1 
ATOM   41    N  N   . ALA A 1 27   ? -12.421 24.747  11.326  1.00 199.70 ? 27   ALA A N   1 
ATOM   42    C  CA  . ALA A 1 27   ? -11.776 23.664  10.600  1.00 198.01 ? 27   ALA A CA  1 
ATOM   43    C  C   . ALA A 1 27   ? -10.267 23.836  10.688  1.00 191.00 ? 27   ALA A C   1 
ATOM   44    O  O   . ALA A 1 27   ? -9.789  24.934  10.979  1.00 186.73 ? 27   ALA A O   1 
ATOM   45    C  CB  . ALA A 1 27   ? -12.217 23.665  9.178   1.00 197.59 ? 27   ALA A CB  1 
ATOM   46    N  N   . PRO A 1 28   ? -9.509  22.759  10.413  1.00 185.36 ? 28   PRO A N   1 
ATOM   47    C  CA  . PRO A 1 28   ? -8.065  22.787  10.660  1.00 185.18 ? 28   PRO A CA  1 
ATOM   48    C  C   . PRO A 1 28   ? -7.448  24.000  9.986   1.00 187.06 ? 28   PRO A C   1 
ATOM   49    O  O   . PRO A 1 28   ? -8.155  24.727  9.309   1.00 187.68 ? 28   PRO A O   1 
ATOM   50    C  CB  . PRO A 1 28   ? -7.563  21.510  9.984   1.00 182.34 ? 28   PRO A CB  1 
ATOM   51    C  CG  . PRO A 1 28   ? -8.746  20.628  9.840   1.00 183.96 ? 28   PRO A CG  1 
ATOM   52    C  CD  . PRO A 1 28   ? -9.941  21.519  9.739   1.00 185.64 ? 28   PRO A CD  1 
ATOM   53    N  N   . LYS A 1 29   ? -6.161  24.237  10.185  1.00 233.74 ? 29   LYS A N   1 
ATOM   54    C  CA  . LYS A 1 29   ? -5.477  25.246  9.389   1.00 231.79 ? 29   LYS A CA  1 
ATOM   55    C  C   . LYS A 1 29   ? -5.062  24.635  8.053   1.00 232.78 ? 29   LYS A C   1 
ATOM   56    O  O   . LYS A 1 29   ? -4.655  25.348  7.149   1.00 229.02 ? 29   LYS A O   1 
ATOM   57    C  CB  . LYS A 1 29   ? -4.274  25.841  10.130  1.00 231.94 ? 29   LYS A CB  1 
ATOM   58    C  CG  . LYS A 1 29   ? -3.190  26.464  9.243   1.00 232.62 ? 29   LYS A CG  1 
ATOM   59    C  CD  . LYS A 1 29   ? -3.682  27.650  8.422   1.00 272.90 ? 29   LYS A CD  1 
ATOM   60    C  CE  . LYS A 1 29   ? -2.720  27.921  7.263   1.00 263.65 ? 29   LYS A CE  1 
ATOM   61    N  NZ  . LYS A 1 29   ? -3.180  28.985  6.321   1.00 260.49 ? 29   LYS A NZ  1 
ATOM   62    N  N   . ILE A 1 30   ? -5.175  23.315  7.924   1.00 166.23 ? 30   ILE A N   1 
ATOM   63    C  CA  . ILE A 1 30   ? -4.867  22.633  6.666   1.00 165.77 ? 30   ILE A CA  1 
ATOM   64    C  C   . ILE A 1 30   ? -5.779  21.433  6.484   1.00 166.03 ? 30   ILE A C   1 
ATOM   65    O  O   . ILE A 1 30   ? -6.603  21.119  7.348   1.00 166.58 ? 30   ILE A O   1 
ATOM   66    C  CB  . ILE A 1 30   ? -3.431  22.096  6.636   1.00 165.80 ? 30   ILE A CB  1 
ATOM   67    C  CG1 . ILE A 1 30   ? -2.432  23.169  7.091   1.00 165.72 ? 30   ILE A CG1 1 
ATOM   68    C  CG2 . ILE A 1 30   ? -3.093  21.515  5.275   1.00 165.34 ? 30   ILE A CG2 1 
ATOM   69    C  CD1 . ILE A 1 30   ? -2.287  24.321  6.179   1.00 165.06 ? 30   ILE A CD1 1 
ATOM   70    N  N   . PHE A 1 31   ? -5.638  20.765  5.350   1.00 165.69 ? 31   PHE A N   1 
ATOM   71    C  CA  . PHE A 1 31   ? -6.375  19.547  5.118   1.00 165.97 ? 31   PHE A CA  1 
ATOM   72    C  C   . PHE A 1 31   ? -5.386  18.455  4.839   1.00 167.82 ? 31   PHE A C   1 
ATOM   73    O  O   . PHE A 1 31   ? -4.201  18.700  4.606   1.00 165.89 ? 31   PHE A O   1 
ATOM   74    C  CB  . PHE A 1 31   ? -7.340  19.671  3.921   1.00 165.56 ? 31   PHE A CB  1 
ATOM   75    C  CG  . PHE A 1 31   ? -8.498  20.635  4.137   1.00 165.60 ? 31   PHE A CG  1 
ATOM   76    C  CD1 . PHE A 1 31   ? -8.590  21.818  3.403   1.00 165.17 ? 31   PHE A CD1 1 
ATOM   77    C  CD2 . PHE A 1 31   ? -9.502  20.349  5.068   1.00 166.65 ? 31   PHE A CD2 1 
ATOM   78    C  CE1 . PHE A 1 31   ? -9.650  22.703  3.601   1.00 165.34 ? 31   PHE A CE1 1 
ATOM   79    C  CE2 . PHE A 1 31   ? -10.571 21.235  5.265   1.00 166.31 ? 31   PHE A CE2 1 
ATOM   80    C  CZ  . PHE A 1 31   ? -10.640 22.411  4.530   1.00 165.90 ? 31   PHE A CZ  1 
ATOM   81    N  N   . ARG A 1 32   ? -5.898  17.239  4.859   1.00 168.86 ? 32   ARG A N   1 
ATOM   82    C  CA  . ARG A 1 32   ? -5.128  16.101  4.430   1.00 166.74 ? 32   ARG A CA  1 
ATOM   83    C  C   . ARG A 1 32   ? -6.015  15.201  3.585   1.00 166.74 ? 32   ARG A C   1 
ATOM   84    O  O   . ARG A 1 32   ? -7.244  15.191  3.716   1.00 166.85 ? 32   ARG A O   1 
ATOM   85    C  CB  . ARG A 1 32   ? -4.572  15.314  5.640   1.00 171.31 ? 32   ARG A CB  1 
ATOM   86    C  CG  . ARG A 1 32   ? -3.146  15.716  6.190   1.00 171.20 ? 32   ARG A CG  1 
ATOM   87    C  CD  . ARG A 1 32   ? -2.778  15.024  7.578   1.00 173.56 ? 32   ARG A CD  1 
ATOM   88    N  NE  . ARG A 1 32   ? -1.508  15.458  8.204   1.00 170.08 ? 32   ARG A NE  1 
ATOM   89    C  CZ  . ARG A 1 32   ? -1.388  15.977  9.429   1.00 169.69 ? 32   ARG A CZ  1 
ATOM   90    N  NH1 . ARG A 1 32   ? -2.450  16.155  10.207  1.00 170.80 ? 32   ARG A NH1 1 
ATOM   91    N  NH2 . ARG A 1 32   ? -0.195  16.330  9.874   1.00 169.96 ? 32   ARG A NH2 1 
ATOM   92    N  N   . VAL A 1 33   ? -5.354  14.452  2.718   1.00 166.67 ? 33   VAL A N   1 
ATOM   93    C  CA  . VAL A 1 33   ? -5.948  13.341  2.000   1.00 168.53 ? 33   VAL A CA  1 
ATOM   94    C  C   . VAL A 1 33   ? -6.232  12.108  2.863   1.00 172.18 ? 33   VAL A C   1 
ATOM   95    O  O   . VAL A 1 33   ? -5.402  11.689  3.665   1.00 170.94 ? 33   VAL A O   1 
ATOM   96    C  CB  . VAL A 1 33   ? -4.988  12.918  0.924   1.00 167.74 ? 33   VAL A CB  1 
ATOM   97    C  CG1 . VAL A 1 33   ? -5.722  12.190  -0.203  1.00 171.46 ? 33   VAL A CG1 1 
ATOM   98    C  CG2 . VAL A 1 33   ? -4.271  14.158  0.424   1.00 165.93 ? 33   VAL A CG2 1 
ATOM   99    N  N   . GLY A 1 34   ? -7.405  11.515  2.672   1.00 207.07 ? 34   GLY A N   1 
ATOM   100   C  CA  . GLY A 1 34   ? -7.810  10.362  3.453   1.00 213.52 ? 34   GLY A CA  1 
ATOM   101   C  C   . GLY A 1 34   ? -7.911  10.744  4.910   1.00 218.02 ? 34   GLY A C   1 
ATOM   102   O  O   . GLY A 1 34   ? -7.680  9.923   5.801   1.00 220.39 ? 34   GLY A O   1 
ATOM   103   N  N   . ALA A 1 35   ? -8.255  12.007  5.142   1.00 175.89 ? 35   ALA A N   1 
ATOM   104   C  CA  . ALA A 1 35   ? -8.318  12.566  6.484   1.00 178.17 ? 35   ALA A CA  1 
ATOM   105   C  C   . ALA A 1 35   ? -9.745  12.767  6.936   1.00 184.11 ? 35   ALA A C   1 
ATOM   106   O  O   . ALA A 1 35   ? -10.485 13.524  6.327   1.00 182.79 ? 35   ALA A O   1 
ATOM   107   C  CB  . ALA A 1 35   ? -7.601  13.885  6.511   1.00 174.82 ? 35   ALA A CB  1 
ATOM   108   N  N   . SER A 1 36   ? -10.122 12.107  8.018   1.00 243.82 ? 36   SER A N   1 
ATOM   109   C  CA  . SER A 1 36   ? -11.439 12.298  8.585   1.00 247.48 ? 36   SER A CA  1 
ATOM   110   C  C   . SER A 1 36   ? -11.552 13.705  9.175   1.00 246.98 ? 36   SER A C   1 
ATOM   111   O  O   . SER A 1 36   ? -11.710 13.872  10.383  1.00 248.12 ? 36   SER A O   1 
ATOM   112   C  CB  . SER A 1 36   ? -11.677 11.239  9.653   1.00 248.61 ? 36   SER A CB  1 
ATOM   113   O  OG  . SER A 1 36   ? -11.076 10.011  9.265   1.00 247.36 ? 36   SER A OG  1 
ATOM   114   N  N   . GLU A 1 37   ? -11.472 14.715  8.314   1.00 216.69 ? 37   GLU A N   1 
ATOM   115   C  CA  . GLU A 1 37   ? -11.514 16.105  8.760   1.00 217.82 ? 37   GLU A CA  1 
ATOM   116   C  C   . GLU A 1 37   ? -12.785 16.430  9.545   1.00 218.71 ? 37   GLU A C   1 
ATOM   117   O  O   . GLU A 1 37   ? -13.905 16.336  9.039   1.00 220.06 ? 37   GLU A O   1 
ATOM   118   C  CB  . GLU A 1 37   ? -11.354 17.075  7.580   1.00 221.18 ? 37   GLU A CB  1 
ATOM   119   C  CG  . GLU A 1 37   ? -10.114 16.844  6.709   1.00 224.07 ? 37   GLU A CG  1 
ATOM   120   C  CD  . GLU A 1 37   ? -8.825  17.154  7.426   1.00 226.40 ? 37   GLU A CD  1 
ATOM   121   O  OE1 . GLU A 1 37   ? -8.811  17.079  8.672   1.00 228.60 ? 37   GLU A OE1 1 
ATOM   122   O  OE2 . GLU A 1 37   ? -7.829  17.466  6.739   1.00 225.72 ? 37   GLU A OE2 1 
ATOM   123   N  N   . ASN A 1 38   ? -12.590 16.814  10.797  1.00 216.22 ? 38   ASN A N   1 
ATOM   124   C  CA  . ASN A 1 38   ? -13.691 17.223  11.645  1.00 216.18 ? 38   ASN A CA  1 
ATOM   125   C  C   . ASN A 1 38   ? -14.033 18.702  11.407  1.00 214.07 ? 38   ASN A C   1 
ATOM   126   O  O   . ASN A 1 38   ? -13.139 19.550  11.376  1.00 211.27 ? 38   ASN A O   1 
ATOM   127   C  CB  . ASN A 1 38   ? -13.350 16.952  13.116  1.00 214.87 ? 38   ASN A CB  1 
ATOM   128   C  CG  . ASN A 1 38   ? -13.092 15.468  13.401  1.00 214.16 ? 38   ASN A CG  1 
ATOM   129   O  OD1 . ASN A 1 38   ? -13.217 14.617  12.512  1.00 213.50 ? 38   ASN A OD1 1 
ATOM   130   N  ND2 . ASN A 1 38   ? -12.729 15.158  14.646  1.00 214.50 ? 38   ASN A ND2 1 
ATOM   131   N  N   . ILE A 1 39   ? -15.322 18.996  11.218  1.00 170.69 ? 39   ILE A N   1 
ATOM   132   C  CA  . ILE A 1 39   ? -15.804 20.353  10.946  1.00 170.40 ? 39   ILE A CA  1 
ATOM   133   C  C   . ILE A 1 39   ? -17.097 20.684  11.684  1.00 171.16 ? 39   ILE A C   1 
ATOM   134   O  O   . ILE A 1 39   ? -18.189 20.250  11.304  1.00 171.41 ? 39   ILE A O   1 
ATOM   135   C  CB  . ILE A 1 39   ? -16.052 20.543  9.472   1.00 169.71 ? 39   ILE A CB  1 
ATOM   136   C  CG1 . ILE A 1 39   ? -14.832 20.059  8.688   1.00 169.04 ? 39   ILE A CG1 1 
ATOM   137   C  CG2 . ILE A 1 39   ? -16.369 21.997  9.179   1.00 169.49 ? 39   ILE A CG2 1 
ATOM   138   C  CD1 . ILE A 1 39   ? -13.537 20.720  9.109   1.00 172.92 ? 39   ILE A CD1 1 
ATOM   139   N  N   . VAL A 1 40   ? -16.949 21.462  12.747  1.00 192.99 ? 40   VAL A N   1 
ATOM   140   C  CA  . VAL A 1 40   ? -18.060 21.821  13.601  1.00 197.47 ? 40   VAL A CA  1 
ATOM   141   C  C   . VAL A 1 40   ? -18.739 23.035  13.050  1.00 198.33 ? 40   VAL A C   1 
ATOM   142   O  O   . VAL A 1 40   ? -18.104 23.900  12.450  1.00 193.31 ? 40   VAL A O   1 
ATOM   143   C  CB  . VAL A 1 40   ? -17.604 22.221  15.016  1.00 202.91 ? 40   VAL A CB  1 
ATOM   144   C  CG1 . VAL A 1 40   ? -16.682 21.167  15.625  1.00 205.30 ? 40   VAL A CG1 1 
ATOM   145   C  CG2 . VAL A 1 40   ? -16.935 23.595  14.985  1.00 198.21 ? 40   VAL A CG2 1 
ATOM   146   N  N   . ILE A 1 41   ? -20.037 23.105  13.288  1.00 212.98 ? 41   ILE A N   1 
ATOM   147   C  CA  . ILE A 1 41   ? -20.798 24.303  13.025  1.00 213.17 ? 41   ILE A CA  1 
ATOM   148   C  C   . ILE A 1 41   ? -21.572 24.604  14.284  1.00 213.35 ? 41   ILE A C   1 
ATOM   149   O  O   . ILE A 1 41   ? -22.156 23.708  14.877  1.00 214.82 ? 41   ILE A O   1 
ATOM   150   C  CB  . ILE A 1 41   ? -21.792 24.093  11.889  1.00 219.59 ? 41   ILE A CB  1 
ATOM   151   C  CG1 . ILE A 1 41   ? -22.903 25.139  11.970  1.00 220.24 ? 41   ILE A CG1 1 
ATOM   152   C  CG2 . ILE A 1 41   ? -22.384 22.703  11.962  1.00 224.24 ? 41   ILE A CG2 1 
ATOM   153   C  CD1 . ILE A 1 41   ? -24.047 24.890  11.012  1.00 223.18 ? 41   ILE A CD1 1 
ATOM   154   N  N   . GLN A 1 42   ? -21.576 25.867  14.686  1.00 253.81 ? 42   GLN A N   1 
ATOM   155   C  CA  . GLN A 1 42   ? -22.294 26.316  15.876  1.00 260.52 ? 42   GLN A CA  1 
ATOM   156   C  C   . GLN A 1 42   ? -22.678 27.764  15.609  1.00 262.11 ? 42   GLN A C   1 
ATOM   157   O  O   . GLN A 1 42   ? -21.979 28.447  14.864  1.00 257.99 ? 42   GLN A O   1 
ATOM   158   C  CB  . GLN A 1 42   ? -21.396 26.209  17.106  1.00 262.74 ? 42   GLN A CB  1 
ATOM   159   C  CG  . GLN A 1 42   ? -21.450 27.399  18.033  1.00 262.55 ? 42   GLN A CG  1 
ATOM   160   C  CD  . GLN A 1 42   ? -20.081 27.755  18.551  1.00 261.96 ? 42   GLN A CD  1 
ATOM   161   O  OE1 . GLN A 1 42   ? -19.874 28.842  19.082  1.00 261.89 ? 42   GLN A OE1 1 
ATOM   162   N  NE2 . GLN A 1 42   ? -19.129 26.844  18.384  1.00 261.92 ? 42   GLN A NE2 1 
ATOM   163   N  N   . VAL A 1 43   ? -23.779 28.250  16.174  1.00 204.59 ? 43   VAL A N   1 
ATOM   164   C  CA  . VAL A 1 43   ? -24.265 29.538  15.700  1.00 200.10 ? 43   VAL A CA  1 
ATOM   165   C  C   . VAL A 1 43   ? -25.211 30.259  16.628  1.00 205.02 ? 43   VAL A C   1 
ATOM   166   O  O   . VAL A 1 43   ? -25.960 29.647  17.380  1.00 208.97 ? 43   VAL A O   1 
ATOM   167   C  CB  . VAL A 1 43   ? -24.911 29.414  14.285  1.00 193.79 ? 43   VAL A CB  1 
ATOM   168   C  CG1 . VAL A 1 43   ? -26.182 28.568  14.315  1.00 195.02 ? 43   VAL A CG1 1 
ATOM   169   C  CG2 . VAL A 1 43   ? -25.200 30.780  13.717  1.00 187.41 ? 43   VAL A CG2 1 
ATOM   170   N  N   . TYR A 1 44   ? -25.163 31.580  16.549  1.00 274.82 ? 44   TYR A N   1 
ATOM   171   C  CA  . TYR A 1 44   ? -26.025 32.436  17.335  1.00 280.85 ? 44   TYR A CA  1 
ATOM   172   C  C   . TYR A 1 44   ? -27.374 32.689  16.653  1.00 299.65 ? 44   TYR A C   1 
ATOM   173   O  O   . TYR A 1 44   ? -28.015 33.716  16.882  1.00 295.47 ? 44   TYR A O   1 
ATOM   174   C  CB  . TYR A 1 44   ? -25.307 33.755  17.588  1.00 286.84 ? 44   TYR A CB  1 
ATOM   175   C  CG  . TYR A 1 44   ? -25.819 34.484  18.795  1.00 299.39 ? 44   TYR A CG  1 
ATOM   176   C  CD1 . TYR A 1 44   ? -25.510 34.044  20.069  1.00 305.62 ? 44   TYR A CD1 1 
ATOM   177   C  CD2 . TYR A 1 44   ? -26.610 35.614  18.664  1.00 303.83 ? 44   TYR A CD2 1 
ATOM   178   C  CE1 . TYR A 1 44   ? -25.978 34.702  21.174  1.00 308.37 ? 44   TYR A CE1 1 
ATOM   179   C  CE2 . TYR A 1 44   ? -27.080 36.284  19.771  1.00 306.58 ? 44   TYR A CE2 1 
ATOM   180   C  CZ  . TYR A 1 44   ? -26.758 35.825  21.024  1.00 308.18 ? 44   TYR A CZ  1 
ATOM   181   O  OH  . TYR A 1 44   ? -27.223 36.492  22.131  1.00 308.34 ? 44   TYR A OH  1 
ATOM   182   N  N   . GLY A 1 45   ? -27.806 31.758  15.809  1.00 217.46 ? 45   GLY A N   1 
ATOM   183   C  CA  . GLY A 1 45   ? -29.051 31.932  15.083  1.00 220.01 ? 45   GLY A CA  1 
ATOM   184   C  C   . GLY A 1 45   ? -30.221 31.977  16.037  1.00 222.11 ? 45   GLY A C   1 
ATOM   185   O  O   . GLY A 1 45   ? -30.142 31.418  17.129  1.00 221.72 ? 45   GLY A O   1 
ATOM   186   N  N   . TYR A 1 46   ? -31.299 32.641  15.630  1.00 272.00 ? 46   TYR A N   1 
ATOM   187   C  CA  . TYR A 1 46   ? -32.510 32.742  16.449  1.00 277.43 ? 46   TYR A CA  1 
ATOM   188   C  C   . TYR A 1 46   ? -33.378 31.477  16.402  1.00 280.83 ? 46   TYR A C   1 
ATOM   189   O  O   . TYR A 1 46   ? -33.041 30.508  15.719  1.00 286.13 ? 46   TYR A O   1 
ATOM   190   C  CB  . TYR A 1 46   ? -33.336 33.952  16.025  1.00 280.56 ? 46   TYR A CB  1 
ATOM   191   C  CG  . TYR A 1 46   ? -33.460 34.050  14.535  1.00 283.66 ? 46   TYR A CG  1 
ATOM   192   C  CD1 . TYR A 1 46   ? -34.321 33.216  13.837  1.00 288.27 ? 46   TYR A CD1 1 
ATOM   193   C  CD2 . TYR A 1 46   ? -32.694 34.952  13.818  1.00 281.92 ? 46   TYR A CD2 1 
ATOM   194   C  CE1 . TYR A 1 46   ? -34.428 33.292  12.468  1.00 289.32 ? 46   TYR A CE1 1 
ATOM   195   C  CE2 . TYR A 1 46   ? -32.796 35.038  12.449  1.00 282.90 ? 46   TYR A CE2 1 
ATOM   196   C  CZ  . TYR A 1 46   ? -33.664 34.204  11.780  1.00 286.92 ? 46   TYR A CZ  1 
ATOM   197   O  OH  . TYR A 1 46   ? -33.770 34.281  10.416  1.00 288.02 ? 46   TYR A OH  1 
ATOM   198   N  N   . THR A 1 47   ? -34.506 31.514  17.115  1.00 413.33 ? 47   THR A N   1 
ATOM   199   C  CA  . THR A 1 47   ? -35.336 30.329  17.377  1.00 412.57 ? 47   THR A CA  1 
ATOM   200   C  C   . THR A 1 47   ? -35.523 29.405  16.175  1.00 411.94 ? 47   THR A C   1 
ATOM   201   O  O   . THR A 1 47   ? -35.581 28.183  16.325  1.00 413.45 ? 47   THR A O   1 
ATOM   202   C  CB  . THR A 1 47   ? -36.737 30.711  17.925  1.00 457.03 ? 47   THR A CB  1 
ATOM   203   O  OG1 . THR A 1 47   ? -36.598 31.550  19.077  1.00 455.81 ? 47   THR A OG1 1 
ATOM   204   C  CG2 . THR A 1 47   ? -37.519 29.463  18.312  1.00 459.72 ? 47   THR A CG2 1 
ATOM   205   N  N   . GLU A 1 48   ? -35.618 29.988  14.987  1.00 341.57 ? 48   GLU A N   1 
ATOM   206   C  CA  . GLU A 1 48   ? -35.845 29.210  13.780  1.00 341.78 ? 48   GLU A CA  1 
ATOM   207   C  C   . GLU A 1 48   ? -34.745 28.180  13.552  1.00 337.57 ? 48   GLU A C   1 
ATOM   208   O  O   . GLU A 1 48   ? -33.628 28.529  13.163  1.00 334.36 ? 48   GLU A O   1 
ATOM   209   C  CB  . GLU A 1 48   ? -35.941 30.133  12.566  1.00 341.09 ? 48   GLU A CB  1 
ATOM   210   C  CG  . GLU A 1 48   ? -36.503 29.459  11.333  1.00 343.24 ? 48   GLU A CG  1 
ATOM   211   C  CD  . GLU A 1 48   ? -37.924 28.983  11.545  1.00 346.36 ? 48   GLU A CD  1 
ATOM   212   O  OE1 . GLU A 1 48   ? -38.605 29.521  12.444  1.00 345.98 ? 48   GLU A OE1 1 
ATOM   213   O  OE2 . GLU A 1 48   ? -38.362 28.073  10.814  1.00 348.66 ? 48   GLU A OE2 1 
ATOM   214   N  N   . ALA A 1 49   ? -35.064 26.912  13.797  1.00 332.32 ? 49   ALA A N   1 
ATOM   215   C  CA  . ALA A 1 49   ? -34.161 25.824  13.451  1.00 329.09 ? 49   ALA A CA  1 
ATOM   216   C  C   . ALA A 1 49   ? -33.892 25.903  11.950  1.00 325.75 ? 49   ALA A C   1 
ATOM   217   O  O   . ALA A 1 49   ? -34.726 26.402  11.193  1.00 326.78 ? 49   ALA A O   1 
ATOM   218   C  CB  . ALA A 1 49   ? -34.780 24.485  13.819  1.00 332.96 ? 49   ALA A CB  1 
ATOM   219   N  N   . PHE A 1 50   ? -32.731 25.430  11.509  1.00 311.79 ? 50   PHE A N   1 
ATOM   220   C  CA  . PHE A 1 50   ? -32.401 25.541  10.091  1.00 310.98 ? 50   PHE A CA  1 
ATOM   221   C  C   . PHE A 1 50   ? -31.338 24.567  9.602   1.00 305.86 ? 50   PHE A C   1 
ATOM   222   O  O   . PHE A 1 50   ? -30.415 24.200  10.331  1.00 303.07 ? 50   PHE A O   1 
ATOM   223   C  CB  . PHE A 1 50   ? -32.037 26.985  9.726   1.00 315.17 ? 50   PHE A CB  1 
ATOM   224   C  CG  . PHE A 1 50   ? -30.759 27.480  10.346  1.00 320.64 ? 50   PHE A CG  1 
ATOM   225   C  CD1 . PHE A 1 50   ? -29.652 27.745  9.557   1.00 322.06 ? 50   PHE A CD1 1 
ATOM   226   C  CD2 . PHE A 1 50   ? -30.669 27.700  11.711  1.00 325.06 ? 50   PHE A CD2 1 
ATOM   227   C  CE1 . PHE A 1 50   ? -28.480 28.209  10.118  1.00 321.62 ? 50   PHE A CE1 1 
ATOM   228   C  CE2 . PHE A 1 50   ? -29.495 28.164  12.277  1.00 324.08 ? 50   PHE A CE2 1 
ATOM   229   C  CZ  . PHE A 1 50   ? -28.401 28.418  11.480  1.00 322.40 ? 50   PHE A CZ  1 
ATOM   230   N  N   . ASP A 1 51   ? -31.487 24.157  8.349   1.00 217.55 ? 51   ASP A N   1 
ATOM   231   C  CA  . ASP A 1 51   ? -30.639 23.125  7.766   1.00 216.23 ? 51   ASP A CA  1 
ATOM   232   C  C   . ASP A 1 51   ? -29.220 23.594  7.461   1.00 212.36 ? 51   ASP A C   1 
ATOM   233   O  O   . ASP A 1 51   ? -28.981 24.791  7.278   1.00 210.30 ? 51   ASP A O   1 
ATOM   234   C  CB  . ASP A 1 51   ? -31.278 22.565  6.500   1.00 216.22 ? 51   ASP A CB  1 
ATOM   235   C  CG  . ASP A 1 51   ? -31.712 21.128  6.657   1.00 217.87 ? 51   ASP A CG  1 
ATOM   236   O  OD1 . ASP A 1 51   ? -32.145 20.744  7.762   1.00 217.56 ? 51   ASP A OD1 1 
ATOM   237   O  OD2 . ASP A 1 51   ? -31.625 20.384  5.666   1.00 219.18 ? 51   ASP A OD2 1 
ATOM   238   N  N   . ALA A 1 52   ? -28.294 22.631  7.401   1.00 313.20 ? 52   ALA A N   1 
ATOM   239   C  CA  . ALA A 1 52   ? -26.867 22.892  7.159   1.00 306.51 ? 52   ALA A CA  1 
ATOM   240   C  C   . ALA A 1 52   ? -26.109 21.714  6.520   1.00 306.03 ? 52   ALA A C   1 
ATOM   241   O  O   . ALA A 1 52   ? -25.831 20.709  7.179   1.00 308.32 ? 52   ALA A O   1 
ATOM   242   C  CB  . ALA A 1 52   ? -26.178 23.300  8.452   1.00 302.62 ? 52   ALA A CB  1 
ATOM   243   N  N   . THR A 1 53   ? -25.762 21.861  5.241   1.00 279.56 ? 53   THR A N   1 
ATOM   244   C  CA  . THR A 1 53   ? -24.935 20.885  4.521   1.00 277.79 ? 53   THR A CA  1 
ATOM   245   C  C   . THR A 1 53   ? -23.586 21.474  4.113   1.00 271.98 ? 53   THR A C   1 
ATOM   246   O  O   . THR A 1 53   ? -23.520 22.524  3.474   1.00 268.82 ? 53   THR A O   1 
ATOM   247   C  CB  . THR A 1 53   ? -25.626 20.360  3.238   1.00 284.94 ? 53   THR A CB  1 
ATOM   248   O  OG1 . THR A 1 53   ? -26.470 19.250  3.558   1.00 289.15 ? 53   THR A OG1 1 
ATOM   249   C  CG2 . THR A 1 53   ? -24.594 19.895  2.233   1.00 283.37 ? 53   THR A CG2 1 
ATOM   250   N  N   . ILE A 1 54   ? -22.511 20.785  4.475   1.00 217.46 ? 54   ILE A N   1 
ATOM   251   C  CA  . ILE A 1 54   ? -21.164 21.209  4.117   1.00 212.83 ? 54   ILE A CA  1 
ATOM   252   C  C   . ILE A 1 54   ? -20.651 20.301  3.017   1.00 210.75 ? 54   ILE A C   1 
ATOM   253   O  O   . ILE A 1 54   ? -21.247 19.261  2.745   1.00 210.18 ? 54   ILE A O   1 
ATOM   254   C  CB  . ILE A 1 54   ? -20.192 21.079  5.315   1.00 215.04 ? 54   ILE A CB  1 
ATOM   255   C  CG1 . ILE A 1 54   ? -20.821 21.616  6.606   1.00 215.62 ? 54   ILE A CG1 1 
ATOM   256   C  CG2 . ILE A 1 54   ? -18.865 21.779  5.033   1.00 211.05 ? 54   ILE A CG2 1 
ATOM   257   C  CD1 . ILE A 1 54   ? -19.927 21.456  7.840   1.00 214.89 ? 54   ILE A CD1 1 
ATOM   258   N  N   . SER A 1 55   ? -19.545 20.691  2.393   1.00 168.56 ? 55   SER A N   1 
ATOM   259   C  CA  . SER A 1 55   ? -18.831 19.805  1.487   1.00 169.00 ? 55   SER A CA  1 
ATOM   260   C  C   . SER A 1 55   ? -17.553 20.442  0.960   1.00 168.41 ? 55   SER A C   1 
ATOM   261   O  O   . SER A 1 55   ? -17.240 21.600  1.250   1.00 167.28 ? 55   SER A O   1 
ATOM   262   C  CB  . SER A 1 55   ? -19.728 19.340  0.340   1.00 172.53 ? 55   SER A CB  1 
ATOM   263   O  OG  . SER A 1 55   ? -20.162 20.425  -0.453  1.00 168.33 ? 55   SER A OG  1 
ATOM   264   N  N   . ILE A 1 56   ? -16.831 19.662  0.169   1.00 208.04 ? 56   ILE A N   1 
ATOM   265   C  CA  . ILE A 1 56   ? -15.459 19.961  -0.185  1.00 212.84 ? 56   ILE A CA  1 
ATOM   266   C  C   . ILE A 1 56   ? -15.304 20.037  -1.692  1.00 216.78 ? 56   ILE A C   1 
ATOM   267   O  O   . ILE A 1 56   ? -15.464 19.037  -2.388  1.00 217.31 ? 56   ILE A O   1 
ATOM   268   C  CB  . ILE A 1 56   ? -14.576 18.842  0.342   1.00 218.32 ? 56   ILE A CB  1 
ATOM   269   C  CG1 . ILE A 1 56   ? -15.212 17.486  0.016   1.00 224.85 ? 56   ILE A CG1 1 
ATOM   270   C  CG2 . ILE A 1 56   ? -14.427 18.962  1.854   1.00 226.27 ? 56   ILE A CG2 1 
ATOM   271   C  CD1 . ILE A 1 56   ? -14.651 16.328  0.845   1.00 229.16 ? 56   ILE A CD1 1 
ATOM   272   N  N   . LYS A 1 57   ? -14.995 21.227  -2.195  1.00 240.91 ? 57   LYS A N   1 
ATOM   273   C  CA  . LYS A 1 57   ? -14.975 21.453  -3.637  1.00 244.21 ? 57   LYS A CA  1 
ATOM   274   C  C   . LYS A 1 57   ? -13.659 22.047  -4.111  1.00 242.95 ? 57   LYS A C   1 
ATOM   275   O  O   . LYS A 1 57   ? -12.943 22.690  -3.346  1.00 242.30 ? 57   LYS A O   1 
ATOM   276   C  CB  . LYS A 1 57   ? -16.165 22.312  -4.088  1.00 243.84 ? 57   LYS A CB  1 
ATOM   277   C  CG  . LYS A 1 57   ? -17.493 21.576  -3.988  1.00 246.20 ? 57   LYS A CG  1 
ATOM   278   C  CD  . LYS A 1 57   ? -18.684 22.476  -4.246  1.00 245.75 ? 57   LYS A CD  1 
ATOM   279   C  CE  . LYS A 1 57   ? -19.975 21.735  -3.949  1.00 248.91 ? 57   LYS A CE  1 
ATOM   280   N  NZ  . LYS A 1 57   ? -21.159 22.622  -4.049  1.00 250.01 ? 57   LYS A NZ  1 
ATOM   281   N  N   . SER A 1 58   ? -13.363 21.818  -5.388  1.00 295.80 ? 58   SER A N   1 
ATOM   282   C  CA  . SER A 1 58   ? -12.035 22.032  -5.956  1.00 294.64 ? 58   SER A CA  1 
ATOM   283   C  C   . SER A 1 58   ? -11.804 23.446  -6.476  1.00 290.32 ? 58   SER A C   1 
ATOM   284   O  O   . SER A 1 58   ? -12.665 24.015  -7.137  1.00 291.57 ? 58   SER A O   1 
ATOM   285   C  CB  . SER A 1 58   ? -11.792 21.024  -7.081  1.00 297.69 ? 58   SER A CB  1 
ATOM   286   O  OG  . SER A 1 58   ? -12.906 20.970  -7.961  1.00 301.07 ? 58   SER A OG  1 
ATOM   287   N  N   . TYR A 1 59   ? -10.614 23.974  -6.201  1.00 265.10 ? 59   TYR A N   1 
ATOM   288   C  CA  . TYR A 1 59   ? -10.241 25.368  -6.469  1.00 261.71 ? 59   TYR A CA  1 
ATOM   289   C  C   . TYR A 1 59   ? -11.310 26.322  -7.095  1.00 291.25 ? 59   TYR A C   1 
ATOM   290   O  O   . TYR A 1 59   ? -12.330 26.569  -6.441  1.00 294.29 ? 59   TYR A O   1 
ATOM   291   C  CB  . TYR A 1 59   ? -8.857  25.452  -7.120  1.00 257.77 ? 59   TYR A CB  1 
ATOM   292   C  CG  . TYR A 1 59   ? -8.205  26.781  -6.864  1.00 252.95 ? 59   TYR A CG  1 
ATOM   293   C  CD1 . TYR A 1 59   ? -8.385  27.424  -5.650  1.00 251.76 ? 59   TYR A CD1 1 
ATOM   294   C  CD2 . TYR A 1 59   ? -7.423  27.401  -7.828  1.00 249.32 ? 59   TYR A CD2 1 
ATOM   295   C  CE1 . TYR A 1 59   ? -7.811  28.644  -5.400  1.00 248.05 ? 59   TYR A CE1 1 
ATOM   296   C  CE2 . TYR A 1 59   ? -6.844  28.627  -7.590  1.00 245.72 ? 59   TYR A CE2 1 
ATOM   297   C  CZ  . TYR A 1 59   ? -7.040  29.242  -6.370  1.00 245.10 ? 59   TYR A CZ  1 
ATOM   298   O  OH  . TYR A 1 59   ? -6.465  30.462  -6.110  1.00 241.77 ? 59   TYR A OH  1 
ATOM   299   N  N   . PRO A 1 60   ? -11.090 26.875  -8.325  1.00 212.58 ? 60   PRO A N   1 
ATOM   300   C  CA  . PRO A 1 60   ? -12.026 27.942  -8.750  1.00 209.76 ? 60   PRO A CA  1 
ATOM   301   C  C   . PRO A 1 60   ? -13.438 27.520  -9.258  1.00 208.31 ? 60   PRO A C   1 
ATOM   302   O  O   . PRO A 1 60   ? -14.410 28.260  -9.038  1.00 208.07 ? 60   PRO A O   1 
ATOM   303   C  CB  . PRO A 1 60   ? -11.226 28.694  -9.834  1.00 208.95 ? 60   PRO A CB  1 
ATOM   304   C  CG  . PRO A 1 60   ? -9.796  28.239  -9.654  1.00 207.12 ? 60   PRO A CG  1 
ATOM   305   C  CD  . PRO A 1 60   ? -9.958  26.805  -9.263  1.00 209.66 ? 60   PRO A CD  1 
ATOM   306   N  N   . ASP A 1 61   ? -13.543 26.363  -9.912  1.00 233.97 ? 61   ASP A N   1 
ATOM   307   C  CA  . ASP A 1 61   ? -14.830 25.820  -10.355 1.00 234.68 ? 61   ASP A CA  1 
ATOM   308   C  C   . ASP A 1 61   ? -15.473 24.969  -9.272  1.00 234.85 ? 61   ASP A C   1 
ATOM   309   O  O   . ASP A 1 61   ? -15.066 23.829  -9.060  1.00 234.79 ? 61   ASP A O   1 
ATOM   310   C  CB  . ASP A 1 61   ? -14.633 24.939  -11.590 1.00 236.55 ? 61   ASP A CB  1 
ATOM   311   C  CG  . ASP A 1 61   ? -13.805 23.691  -11.294 1.00 238.09 ? 61   ASP A CG  1 
ATOM   312   O  OD1 . ASP A 1 61   ? -14.391 22.593  -11.148 1.00 241.65 ? 61   ASP A OD1 1 
ATOM   313   O  OD2 . ASP A 1 61   ? -12.567 23.811  -11.194 1.00 234.82 ? 61   ASP A OD2 1 
ATOM   314   N  N   . LYS A 1 62   ? -16.480 25.494  -8.589  1.00 269.10 ? 62   LYS A N   1 
ATOM   315   C  CA  . LYS A 1 62   ? -17.128 24.693  -7.556  1.00 270.51 ? 62   LYS A CA  1 
ATOM   316   C  C   . LYS A 1 62   ? -17.866 23.497  -8.168  1.00 274.10 ? 62   LYS A C   1 
ATOM   317   O  O   . LYS A 1 62   ? -19.017 23.227  -7.831  1.00 278.84 ? 62   LYS A O   1 
ATOM   318   C  CB  . LYS A 1 62   ? -18.049 25.550  -6.679  1.00 267.65 ? 62   LYS A CB  1 
ATOM   319   C  CG  . LYS A 1 62   ? -17.335 26.242  -5.509  1.00 260.34 ? 62   LYS A CG  1 
ATOM   320   C  CD  . LYS A 1 62   ? -18.156 27.405  -4.979  1.00 254.93 ? 62   LYS A CD  1 
ATOM   321   C  CE  . LYS A 1 62   ? -17.377 28.246  -3.992  1.00 247.52 ? 62   LYS A CE  1 
ATOM   322   N  NZ  . LYS A 1 62   ? -18.140 29.474  -3.647  1.00 244.45 ? 62   LYS A NZ  1 
ATOM   323   N  N   . LYS A 1 63   ? -17.184 22.784  -9.065  1.00 289.27 ? 63   LYS A N   1 
ATOM   324   C  CA  . LYS A 1 63   ? -17.755 21.628  -9.753  1.00 291.33 ? 63   LYS A CA  1 
ATOM   325   C  C   . LYS A 1 63   ? -17.612 20.315  -8.980  1.00 290.75 ? 63   LYS A C   1 
ATOM   326   O  O   . LYS A 1 63   ? -18.607 19.772  -8.503  1.00 293.76 ? 63   LYS A O   1 
ATOM   327   C  CB  . LYS A 1 63   ? -17.182 21.492  -11.168 1.00 291.73 ? 63   LYS A CB  1 
ATOM   328   C  CG  . LYS A 1 63   ? -17.604 22.613  -12.109 1.00 293.96 ? 63   LYS A CG  1 
ATOM   329   C  CD  . LYS A 1 63   ? -19.111 22.860  -12.051 1.00 299.75 ? 63   LYS A CD  1 
ATOM   330   C  CE  . LYS A 1 63   ? -19.902 21.627  -12.462 1.00 304.36 ? 63   LYS A CE  1 
ATOM   331   N  NZ  . LYS A 1 63   ? -21.371 21.832  -12.330 1.00 308.21 ? 63   LYS A NZ  1 
ATOM   332   N  N   . PHE A 1 64   ? -16.390 19.800  -8.858  1.00 253.79 ? 64   PHE A N   1 
ATOM   333   C  CA  . PHE A 1 64   ? -16.183 18.567  -8.099  1.00 251.99 ? 64   PHE A CA  1 
ATOM   334   C  C   . PHE A 1 64   ? -16.550 18.759  -6.625  1.00 252.62 ? 64   PHE A C   1 
ATOM   335   O  O   . PHE A 1 64   ? -16.226 19.780  -6.015  1.00 250.44 ? 64   PHE A O   1 
ATOM   336   C  CB  . PHE A 1 64   ? -14.740 18.058  -8.230  1.00 247.40 ? 64   PHE A CB  1 
ATOM   337   C  CG  . PHE A 1 64   ? -14.615 16.719  -8.929  1.00 246.27 ? 64   PHE A CG  1 
ATOM   338   C  CD1 . PHE A 1 64   ? -14.036 16.638  -10.192 1.00 243.24 ? 64   PHE A CD1 1 
ATOM   339   C  CD2 . PHE A 1 64   ? -15.061 15.546  -8.325  1.00 247.50 ? 64   PHE A CD2 1 
ATOM   340   C  CE1 . PHE A 1 64   ? -13.904 15.419  -10.843 1.00 243.41 ? 64   PHE A CE1 1 
ATOM   341   C  CE2 . PHE A 1 64   ? -14.934 14.321  -8.971  1.00 247.77 ? 64   PHE A CE2 1 
ATOM   342   C  CZ  . PHE A 1 64   ? -14.353 14.259  -10.234 1.00 245.80 ? 64   PHE A CZ  1 
ATOM   343   N  N   . SER A 1 65   ? -17.239 17.766  -6.073  1.00 250.29 ? 65   SER A N   1 
ATOM   344   C  CA  . SER A 1 65   ? -17.588 17.738  -4.660  1.00 252.35 ? 65   SER A CA  1 
ATOM   345   C  C   . SER A 1 65   ? -17.370 16.312  -4.166  1.00 254.46 ? 65   SER A C   1 
ATOM   346   O  O   . SER A 1 65   ? -18.105 15.390  -4.531  1.00 258.54 ? 65   SER A O   1 
ATOM   347   C  CB  . SER A 1 65   ? -19.035 18.190  -4.436  1.00 256.54 ? 65   SER A CB  1 
ATOM   348   O  OG  . SER A 1 65   ? -19.965 17.189  -4.820  1.00 261.21 ? 65   SER A OG  1 
ATOM   349   N  N   . TYR A 1 66   ? -16.334 16.147  -3.350  1.00 239.81 ? 66   TYR A N   1 
ATOM   350   C  CA  . TYR A 1 66   ? -15.875 14.838  -2.910  1.00 236.73 ? 66   TYR A CA  1 
ATOM   351   C  C   . TYR A 1 66   ? -16.832 14.212  -1.893  1.00 240.55 ? 66   TYR A C   1 
ATOM   352   O  O   . TYR A 1 66   ? -17.189 13.035  -2.005  1.00 242.86 ? 66   TYR A O   1 
ATOM   353   C  CB  . TYR A 1 66   ? -14.460 14.979  -2.357  1.00 227.20 ? 66   TYR A CB  1 
ATOM   354   C  CG  . TYR A 1 66   ? -13.598 15.895  -3.207  1.00 216.41 ? 66   TYR A CG  1 
ATOM   355   C  CD1 . TYR A 1 66   ? -12.894 15.397  -4.292  1.00 212.58 ? 66   TYR A CD1 1 
ATOM   356   C  CD2 . TYR A 1 66   ? -13.502 17.258  -2.935  1.00 210.65 ? 66   TYR A CD2 1 
ATOM   357   C  CE1 . TYR A 1 66   ? -12.112 16.216  -5.082  1.00 205.99 ? 66   TYR A CE1 1 
ATOM   358   C  CE2 . TYR A 1 66   ? -12.715 18.092  -3.722  1.00 204.48 ? 66   TYR A CE2 1 
ATOM   359   C  CZ  . TYR A 1 66   ? -12.020 17.557  -4.799  1.00 201.23 ? 66   TYR A CZ  1 
ATOM   360   O  OH  . TYR A 1 66   ? -11.229 18.348  -5.608  1.00 193.78 ? 66   TYR A OH  1 
ATOM   361   N  N   . SER A 1 67   ? -17.258 15.008  -0.913  1.00 192.49 ? 67   SER A N   1 
ATOM   362   C  CA  . SER A 1 67   ? -18.303 14.586  0.026   1.00 193.84 ? 67   SER A CA  1 
ATOM   363   C  C   . SER A 1 67   ? -18.970 15.767  0.732   1.00 190.11 ? 67   SER A C   1 
ATOM   364   O  O   . SER A 1 67   ? -18.593 16.923  0.543   1.00 185.68 ? 67   SER A O   1 
ATOM   365   C  CB  . SER A 1 67   ? -17.784 13.555  1.042   1.00 195.27 ? 67   SER A CB  1 
ATOM   366   O  OG  . SER A 1 67   ? -16.879 14.127  1.975   1.00 192.19 ? 67   SER A OG  1 
ATOM   367   N  N   . SER A 1 68   ? -19.963 15.454  1.550   1.00 243.64 ? 68   SER A N   1 
ATOM   368   C  CA  . SER A 1 68   ? -20.817 16.463  2.141   1.00 245.37 ? 68   SER A CA  1 
ATOM   369   C  C   . SER A 1 68   ? -21.504 15.835  3.328   1.00 250.10 ? 68   SER A C   1 
ATOM   370   O  O   . SER A 1 68   ? -21.240 14.683  3.655   1.00 249.61 ? 68   SER A O   1 
ATOM   371   C  CB  . SER A 1 68   ? -21.891 16.849  1.151   1.00 247.69 ? 68   SER A CB  1 
ATOM   372   O  OG  . SER A 1 68   ? -22.790 15.766  1.009   1.00 252.76 ? 68   SER A OG  1 
ATOM   373   N  N   . GLY A 1 69   ? -22.411 16.579  3.950   1.00 223.72 ? 69   GLY A N   1 
ATOM   374   C  CA  . GLY A 1 69   ? -23.090 16.089  5.130   1.00 230.81 ? 69   GLY A CA  1 
ATOM   375   C  C   . GLY A 1 69   ? -24.249 16.975  5.504   1.00 233.45 ? 69   GLY A C   1 
ATOM   376   O  O   . GLY A 1 69   ? -24.110 18.190  5.626   1.00 230.53 ? 69   GLY A O   1 
ATOM   377   N  N   . HIS A 1 70   ? -25.404 16.353  5.687   1.00 328.60 ? 70   HIS A N   1 
ATOM   378   C  CA  . HIS A 1 70   ? -26.629 17.085  5.936   1.00 331.81 ? 70   HIS A CA  1 
ATOM   379   C  C   . HIS A 1 70   ? -26.853 17.195  7.435   1.00 329.38 ? 70   HIS A C   1 
ATOM   380   O  O   . HIS A 1 70   ? -27.629 16.442  8.018   1.00 330.72 ? 70   HIS A O   1 
ATOM   381   C  CB  . HIS A 1 70   ? -27.794 16.364  5.264   1.00 341.50 ? 70   HIS A CB  1 
ATOM   382   C  CG  . HIS A 1 70   ? -28.955 17.252  4.939   1.00 348.82 ? 70   HIS A CG  1 
ATOM   383   N  ND1 . HIS A 1 70   ? -29.063 17.925  3.743   1.00 350.17 ? 70   HIS A ND1 1 
ATOM   384   C  CD2 . HIS A 1 70   ? -30.063 17.562  5.652   1.00 354.66 ? 70   HIS A CD2 1 
ATOM   385   C  CE1 . HIS A 1 70   ? -30.189 18.619  3.733   1.00 352.96 ? 70   HIS A CE1 1 
ATOM   386   N  NE2 . HIS A 1 70   ? -30.815 18.413  4.875   1.00 355.72 ? 70   HIS A NE2 1 
ATOM   387   N  N   . VAL A 1 71   ? -26.162 18.135  8.062   1.00 266.68 ? 71   VAL A N   1 
ATOM   388   C  CA  . VAL A 1 71   ? -26.192 18.230  9.511   1.00 266.52 ? 71   VAL A CA  1 
ATOM   389   C  C   . VAL A 1 71   ? -27.075 19.380  10.008  1.00 266.13 ? 71   VAL A C   1 
ATOM   390   O  O   . VAL A 1 71   ? -26.661 20.542  10.043  1.00 261.98 ? 71   VAL A O   1 
ATOM   391   C  CB  . VAL A 1 71   ? -24.766 18.316  10.063  1.00 261.71 ? 71   VAL A CB  1 
ATOM   392   C  CG1 . VAL A 1 71   ? -24.061 16.975  9.864   1.00 262.47 ? 71   VAL A CG1 1 
ATOM   393   C  CG2 . VAL A 1 71   ? -24.002 19.426  9.366   1.00 256.55 ? 71   VAL A CG2 1 
ATOM   394   N  N   . HIS A 1 72   ? -28.299 19.032  10.394  1.00 216.40 ? 72   HIS A N   1 
ATOM   395   C  CA  . HIS A 1 72   ? -29.315 20.021  10.722  1.00 220.02 ? 72   HIS A CA  1 
ATOM   396   C  C   . HIS A 1 72   ? -29.277 20.470  12.157  1.00 219.68 ? 72   HIS A C   1 
ATOM   397   O  O   . HIS A 1 72   ? -29.455 19.665  13.060  1.00 222.12 ? 72   HIS A O   1 
ATOM   398   C  CB  . HIS A 1 72   ? -30.709 19.471  10.445  1.00 229.63 ? 72   HIS A CB  1 
ATOM   399   C  CG  . HIS A 1 72   ? -31.800 20.310  11.026  1.00 235.87 ? 72   HIS A CG  1 
ATOM   400   N  ND1 . HIS A 1 72   ? -32.357 21.384  10.356  1.00 236.83 ? 72   HIS A ND1 1 
ATOM   401   C  CD2 . HIS A 1 72   ? -32.428 20.252  12.223  1.00 240.44 ? 72   HIS A CD2 1 
ATOM   402   C  CE1 . HIS A 1 72   ? -33.284 21.939  11.111  1.00 239.19 ? 72   HIS A CE1 1 
ATOM   403   N  NE2 . HIS A 1 72   ? -33.347 21.273  12.252  1.00 241.31 ? 72   HIS A NE2 1 
ATOM   404   N  N   . LEU A 1 73   ? -29.098 21.767  12.359  1.00 246.75 ? 73   LEU A N   1 
ATOM   405   C  CA  . LEU A 1 73   ? -29.057 22.338  13.700  1.00 248.51 ? 73   LEU A CA  1 
ATOM   406   C  C   . LEU A 1 73   ? -30.417 22.857  14.174  1.00 254.42 ? 73   LEU A C   1 
ATOM   407   O  O   . LEU A 1 73   ? -31.329 23.041  13.377  1.00 254.80 ? 73   LEU A O   1 
ATOM   408   C  CB  . LEU A 1 73   ? -28.026 23.466  13.745  1.00 240.76 ? 73   LEU A CB  1 
ATOM   409   C  CG  . LEU A 1 73   ? -27.883 24.264  12.444  1.00 235.79 ? 73   LEU A CG  1 
ATOM   410   C  CD1 . LEU A 1 73   ? -27.272 25.620  12.722  1.00 230.60 ? 73   LEU A CD1 1 
ATOM   411   C  CD2 . LEU A 1 73   ? -27.063 23.491  11.429  1.00 234.42 ? 73   LEU A CD2 1 
ATOM   412   N  N   . SER A 1 74   ? -30.544 23.090  15.476  1.00 285.86 ? 74   SER A N   1 
ATOM   413   C  CA  . SER A 1 74   ? -31.781 23.615  16.041  1.00 291.28 ? 74   SER A CA  1 
ATOM   414   C  C   . SER A 1 74   ? -31.539 24.026  17.484  1.00 294.64 ? 74   SER A C   1 
ATOM   415   O  O   . SER A 1 74   ? -30.465 23.775  18.031  1.00 296.45 ? 74   SER A O   1 
ATOM   416   C  CB  . SER A 1 74   ? -32.901 22.574  15.983  1.00 294.46 ? 74   SER A CB  1 
ATOM   417   O  OG  . SER A 1 74   ? -32.733 21.581  16.981  1.00 295.43 ? 74   SER A OG  1 
ATOM   418   N  N   . SER A 1 75   ? -32.533 24.656  18.101  1.00 281.36 ? 75   SER A N   1 
ATOM   419   C  CA  . SER A 1 75   ? -32.417 25.046  19.501  1.00 284.81 ? 75   SER A CA  1 
ATOM   420   C  C   . SER A 1 75   ? -32.204 23.819  20.383  1.00 288.66 ? 75   SER A C   1 
ATOM   421   O  O   . SER A 1 75   ? -31.702 23.931  21.502  1.00 287.34 ? 75   SER A O   1 
ATOM   422   C  CB  . SER A 1 75   ? -33.647 25.835  19.955  1.00 289.91 ? 75   SER A CB  1 
ATOM   423   O  OG  . SER A 1 75   ? -33.603 27.170  19.480  1.00 288.72 ? 75   SER A OG  1 
ATOM   424   N  N   . GLU A 1 76   ? -32.588 22.650  19.872  1.00 303.47 ? 76   GLU A N   1 
ATOM   425   C  CA  . GLU A 1 76   ? -32.373 21.387  20.574  1.00 304.46 ? 76   GLU A CA  1 
ATOM   426   C  C   . GLU A 1 76   ? -30.908 20.994  20.533  1.00 296.97 ? 76   GLU A C   1 
ATOM   427   O  O   . GLU A 1 76   ? -30.394 20.338  21.442  1.00 299.49 ? 76   GLU A O   1 
ATOM   428   C  CB  . GLU A 1 76   ? -33.194 20.275  19.941  1.00 310.27 ? 76   GLU A CB  1 
ATOM   429   C  CG  . GLU A 1 76   ? -32.845 18.908  20.479  1.00 313.98 ? 76   GLU A CG  1 
ATOM   430   C  CD  . GLU A 1 76   ? -33.469 17.811  19.671  1.00 317.01 ? 76   GLU A CD  1 
ATOM   431   O  OE1 . GLU A 1 76   ? -34.178 18.137  18.696  1.00 316.04 ? 76   GLU A OE1 1 
ATOM   432   O  OE2 . GLU A 1 76   ? -33.251 16.630  20.007  1.00 320.06 ? 76   GLU A OE2 1 
ATOM   433   N  N   . ASN A 1 77   ? -30.253 21.380  19.446  1.00 260.41 ? 77   ASN A N   1 
ATOM   434   C  CA  . ASN A 1 77   ? -28.823 21.188  19.288  1.00 250.59 ? 77   ASN A CA  1 
ATOM   435   C  C   . ASN A 1 77   ? -28.092 22.502  19.531  1.00 233.42 ? 77   ASN A C   1 
ATOM   436   O  O   . ASN A 1 77   ? -26.950 22.670  19.111  1.00 226.27 ? 77   ASN A O   1 
ATOM   437   C  CB  . ASN A 1 77   ? -28.513 20.670  17.887  1.00 254.83 ? 77   ASN A CB  1 
ATOM   438   C  CG  . ASN A 1 77   ? -27.359 19.699  17.873  1.00 262.59 ? 77   ASN A CG  1 
ATOM   439   O  OD1 . ASN A 1 77   ? -26.730 19.447  18.899  1.00 266.01 ? 77   ASN A OD1 1 
ATOM   440   N  ND2 . ASN A 1 77   ? -27.078 19.142  16.710  1.00 264.63 ? 77   ASN A ND2 1 
ATOM   441   N  N   . LYS A 1 78   ? -28.775 23.434  20.192  1.00 235.48 ? 78   LYS A N   1 
ATOM   442   C  CA  . LYS A 1 78   ? -28.228 24.756  20.478  1.00 223.26 ? 78   LYS A CA  1 
ATOM   443   C  C   . LYS A 1 78   ? -27.517 25.328  19.267  1.00 213.31 ? 78   LYS A C   1 
ATOM   444   O  O   . LYS A 1 78   ? -26.577 26.105  19.401  1.00 208.76 ? 78   LYS A O   1 
ATOM   445   C  CB  . LYS A 1 78   ? -27.251 24.697  21.645  1.00 215.11 ? 78   LYS A CB  1 
ATOM   446   C  CG  . LYS A 1 78   ? -27.806 24.055  22.909  1.00 210.17 ? 78   LYS A CG  1 
ATOM   447   C  CD  . LYS A 1 78   ? -29.003 24.812  23.467  1.00 199.72 ? 78   LYS A CD  1 
ATOM   448   C  CE  . LYS A 1 78   ? -29.407 24.272  24.835  1.00 197.46 ? 78   LYS A CE  1 
ATOM   449   N  NZ  . LYS A 1 78   ? -30.597 24.985  25.374  1.00 196.59 ? 78   LYS A NZ  1 
ATOM   450   N  N   . PHE A 1 79   ? -27.962 24.919  18.084  1.00 234.60 ? 79   PHE A N   1 
ATOM   451   C  CA  . PHE A 1 79   ? -27.350 25.338  16.827  1.00 230.58 ? 79   PHE A CA  1 
ATOM   452   C  C   . PHE A 1 79   ? -25.882 24.996  16.740  1.00 230.85 ? 79   PHE A C   1 
ATOM   453   O  O   . PHE A 1 79   ? -25.020 25.870  16.788  1.00 228.86 ? 79   PHE A O   1 
ATOM   454   C  CB  . PHE A 1 79   ? -27.561 26.828  16.576  1.00 226.10 ? 79   PHE A CB  1 
ATOM   455   C  CG  . PHE A 1 79   ? -28.965 27.169  16.233  1.00 229.78 ? 79   PHE A CG  1 
ATOM   456   C  CD1 . PHE A 1 79   ? -29.734 27.912  17.102  1.00 229.20 ? 79   PHE A CD1 1 
ATOM   457   C  CD2 . PHE A 1 79   ? -29.532 26.702  15.059  1.00 231.49 ? 79   PHE A CD2 1 
ATOM   458   C  CE1 . PHE A 1 79   ? -31.036 28.209  16.795  1.00 230.18 ? 79   PHE A CE1 1 
ATOM   459   C  CE2 . PHE A 1 79   ? -30.834 26.991  14.748  1.00 232.78 ? 79   PHE A CE2 1 
ATOM   460   C  CZ  . PHE A 1 79   ? -31.588 27.748  15.612  1.00 231.94 ? 79   PHE A CZ  1 
ATOM   461   N  N   . GLN A 1 80   ? -25.611 23.709  16.602  1.00 247.55 ? 80   GLN A N   1 
ATOM   462   C  CA  . GLN A 1 80   ? -24.256 23.229  16.450  1.00 248.70 ? 80   GLN A CA  1 
ATOM   463   C  C   . GLN A 1 80   ? -24.327 21.868  15.771  1.00 250.32 ? 80   GLN A C   1 
ATOM   464   O  O   . GLN A 1 80   ? -25.358 21.193  15.841  1.00 253.59 ? 80   GLN A O   1 
ATOM   465   C  CB  . GLN A 1 80   ? -23.544 23.117  17.811  1.00 251.64 ? 80   GLN A CB  1 
ATOM   466   C  CG  . GLN A 1 80   ? -23.484 24.404  18.661  1.00 250.92 ? 80   GLN A CG  1 
ATOM   467   C  CD  . GLN A 1 80   ? -22.448 24.343  19.788  1.00 251.13 ? 80   GLN A CD  1 
ATOM   468   O  OE1 . GLN A 1 80   ? -22.038 23.264  20.223  1.00 253.81 ? 80   GLN A OE1 1 
ATOM   469   N  NE2 . GLN A 1 80   ? -22.026 25.510  20.265  1.00 248.00 ? 80   GLN A NE2 1 
ATOM   470   N  N   . ASN A 1 81   ? -23.242 21.477  15.104  1.00 203.50 ? 81   ASN A N   1 
ATOM   471   C  CA  . ASN A 1 81   ? -23.135 20.135  14.531  1.00 207.35 ? 81   ASN A CA  1 
ATOM   472   C  C   . ASN A 1 81   ? -21.823 19.805  13.787  1.00 202.19 ? 81   ASN A C   1 
ATOM   473   O  O   . ASN A 1 81   ? -21.111 20.698  13.317  1.00 196.28 ? 81   ASN A O   1 
ATOM   474   C  CB  . ASN A 1 81   ? -24.337 19.833  13.646  1.00 213.00 ? 81   ASN A CB  1 
ATOM   475   C  CG  . ASN A 1 81   ? -25.026 18.556  14.041  1.00 220.96 ? 81   ASN A CG  1 
ATOM   476   O  OD1 . ASN A 1 81   ? -24.438 17.478  13.966  1.00 222.55 ? 81   ASN A OD1 1 
ATOM   477   N  ND2 . ASN A 1 81   ? -26.277 18.663  14.469  1.00 225.12 ? 81   ASN A ND2 1 
ATOM   478   N  N   . SER A 1 82   ? -21.528 18.507  13.679  1.00 195.99 ? 82   SER A N   1 
ATOM   479   C  CA  . SER A 1 82   ? -20.262 18.007  13.119  1.00 195.74 ? 82   SER A CA  1 
ATOM   480   C  C   . SER A 1 82   ? -20.418 17.233  11.813  1.00 199.09 ? 82   SER A C   1 
ATOM   481   O  O   . SER A 1 82   ? -21.447 16.607  11.559  1.00 203.29 ? 82   SER A O   1 
ATOM   482   C  CB  . SER A 1 82   ? -19.555 17.077  14.123  1.00 196.76 ? 82   SER A CB  1 
ATOM   483   O  OG  . SER A 1 82   ? -19.029 17.765  15.250  1.00 195.50 ? 82   SER A OG  1 
ATOM   484   N  N   . ALA A 1 83   ? -19.351 17.227  11.024  1.00 182.93 ? 83   ALA A N   1 
ATOM   485   C  CA  . ALA A 1 83   ? -19.373 16.594  9.718   1.00 182.78 ? 83   ALA A CA  1 
ATOM   486   C  C   . ALA A 1 83   ? -18.016 16.016  9.306   1.00 182.50 ? 83   ALA A C   1 
ATOM   487   O  O   . ALA A 1 83   ? -17.028 16.748  9.213   1.00 181.61 ? 83   ALA A O   1 
ATOM   488   C  CB  . ALA A 1 83   ? -19.837 17.600  8.687   1.00 179.85 ? 83   ALA A CB  1 
ATOM   489   N  N   . ILE A 1 84   ? -17.976 14.702  9.064   1.00 201.21 ? 84   ILE A N   1 
ATOM   490   C  CA  . ILE A 1 84   ? -16.800 14.060  8.469   1.00 196.77 ? 84   ILE A CA  1 
ATOM   491   C  C   . ILE A 1 84   ? -16.811 14.146  6.930   1.00 195.41 ? 84   ILE A C   1 
ATOM   492   O  O   . ILE A 1 84   ? -17.295 13.250  6.224   1.00 196.06 ? 84   ILE A O   1 
ATOM   493   C  CB  . ILE A 1 84   ? -16.576 12.596  8.954   1.00 256.43 ? 84   ILE A CB  1 
ATOM   494   C  CG1 . ILE A 1 84   ? -17.805 11.725  8.684   1.00 259.89 ? 84   ILE A CG1 1 
ATOM   495   C  CG2 . ILE A 1 84   ? -16.201 12.576  10.428  1.00 255.34 ? 84   ILE A CG2 1 
ATOM   496   C  CD1 . ILE A 1 84   ? -17.547 10.238  8.839   1.00 259.73 ? 84   ILE A CD1 1 
ATOM   497   N  N   . LEU A 1 85   ? -16.286 15.260  6.433   1.00 236.84 ? 85   LEU A N   1 
ATOM   498   C  CA  . LEU A 1 85   ? -16.009 15.436  5.021   1.00 233.08 ? 85   LEU A CA  1 
ATOM   499   C  C   . LEU A 1 85   ? -14.904 14.462  4.689   1.00 225.48 ? 85   LEU A C   1 
ATOM   500   O  O   . LEU A 1 85   ? -14.704 13.502  5.428   1.00 225.35 ? 85   LEU A O   1 
ATOM   501   C  CB  . LEU A 1 85   ? -15.542 16.865  4.760   1.00 229.22 ? 85   LEU A CB  1 
ATOM   502   C  CG  . LEU A 1 85   ? -16.554 17.920  5.220   1.00 229.12 ? 85   LEU A CG  1 
ATOM   503   C  CD1 . LEU A 1 85   ? -17.950 17.551  4.736   1.00 232.58 ? 85   LEU A CD1 1 
ATOM   504   C  CD2 . LEU A 1 85   ? -16.557 18.082  6.725   1.00 229.18 ? 85   LEU A CD2 1 
ATOM   505   N  N   . THR A 1 86   ? -14.190 14.698  3.591   1.00 248.39 ? 86   THR A N   1 
ATOM   506   C  CA  . THR A 1 86   ? -13.017 13.890  3.267   1.00 242.69 ? 86   THR A CA  1 
ATOM   507   C  C   . THR A 1 86   ? -12.572 13.956  1.796   1.00 241.19 ? 86   THR A C   1 
ATOM   508   O  O   . THR A 1 86   ? -13.234 13.389  0.931   1.00 241.27 ? 86   THR A O   1 
ATOM   509   C  CB  . THR A 1 86   ? -13.223 12.397  3.690   1.00 229.67 ? 86   THR A CB  1 
ATOM   510   O  OG1 . THR A 1 86   ? -12.015 11.659  3.479   1.00 227.56 ? 86   THR A OG1 1 
ATOM   511   C  CG2 . THR A 1 86   ? -14.374 11.739  2.924   1.00 232.26 ? 86   THR A CG2 1 
ATOM   512   N  N   . ILE A 1 87   ? -11.452 14.635  1.515   1.00 176.58 ? 87   ILE A N   1 
ATOM   513   C  CA  . ILE A 1 87   ? -10.823 14.597  0.173   1.00 176.45 ? 87   ILE A CA  1 
ATOM   514   C  C   . ILE A 1 87   ? -10.106 13.273  -0.095  1.00 191.74 ? 87   ILE A C   1 
ATOM   515   O  O   . ILE A 1 87   ? -8.989  13.075  0.379   1.00 193.89 ? 87   ILE A O   1 
ATOM   516   C  CB  . ILE A 1 87   ? -9.696  15.661  -0.024  1.00 165.65 ? 87   ILE A CB  1 
ATOM   517   C  CG1 . ILE A 1 87   ? -10.195 17.088  0.038   1.00 165.38 ? 87   ILE A CG1 1 
ATOM   518   C  CG2 . ILE A 1 87   ? -9.039  15.486  -1.367  1.00 165.25 ? 87   ILE A CG2 1 
ATOM   519   C  CD1 . ILE A 1 87   ? -9.098  18.065  -0.325  1.00 164.88 ? 87   ILE A CD1 1 
ATOM   520   N  N   . GLN A 1 88   ? -10.710 12.376  -0.865  1.00 236.74 ? 88   GLN A N   1 
ATOM   521   C  CA  . GLN A 1 88   ? -10.006 11.157  -1.253  1.00 243.71 ? 88   GLN A CA  1 
ATOM   522   C  C   . GLN A 1 88   ? -9.046  11.499  -2.402  1.00 251.66 ? 88   GLN A C   1 
ATOM   523   O  O   . GLN A 1 88   ? -8.915  12.668  -2.751  1.00 250.87 ? 88   GLN A O   1 
ATOM   524   C  CB  . GLN A 1 88   ? -11.005 10.052  -1.610  1.00 248.07 ? 88   GLN A CB  1 
ATOM   525   C  CG  . GLN A 1 88   ? -12.046 9.818   -0.524  1.00 251.24 ? 88   GLN A CG  1 
ATOM   526   C  CD  . GLN A 1 88   ? -12.216 8.355   -0.154  1.00 253.83 ? 88   GLN A CD  1 
ATOM   527   O  OE1 . GLN A 1 88   ? -13.220 7.972   0.448   1.00 257.34 ? 88   GLN A OE1 1 
ATOM   528   N  NE2 . GLN A 1 88   ? -11.235 7.531   -0.509  1.00 251.15 ? 88   GLN A NE2 1 
ATOM   529   N  N   . PRO A 1 89   ? -8.329  10.499  -2.942  1.00 179.17 ? 89   PRO A N   1 
ATOM   530   C  CA  . PRO A 1 89   ? -7.408  10.593  -4.099  1.00 181.15 ? 89   PRO A CA  1 
ATOM   531   C  C   . PRO A 1 89   ? -7.982  10.833  -5.535  1.00 178.48 ? 89   PRO A C   1 
ATOM   532   O  O   . PRO A 1 89   ? -8.013  9.890   -6.343  1.00 174.58 ? 89   PRO A O   1 
ATOM   533   C  CB  . PRO A 1 89   ? -6.678  9.252   -4.052  1.00 181.74 ? 89   PRO A CB  1 
ATOM   534   C  CG  . PRO A 1 89   ? -6.742  8.850   -2.594  1.00 181.32 ? 89   PRO A CG  1 
ATOM   535   C  CD  . PRO A 1 89   ? -8.075  9.293   -2.132  1.00 181.92 ? 89   PRO A CD  1 
ATOM   536   N  N   . LYS A 1 90   ? -8.396  12.071  -5.838  1.00 167.51 ? 90   LYS A N   1 
ATOM   537   C  CA  . LYS A 1 90   ? -8.756  12.488  -7.194  1.00 172.82 ? 90   LYS A CA  1 
ATOM   538   C  C   . LYS A 1 90   ? -7.484  12.640  -7.988  1.00 182.21 ? 90   LYS A C   1 
ATOM   539   O  O   . LYS A 1 90   ? -6.846  11.652  -8.351  1.00 181.84 ? 90   LYS A O   1 
ATOM   540   C  CB  . LYS A 1 90   ? -9.450  13.853  -7.217  1.00 164.82 ? 90   LYS A CB  1 
ATOM   541   C  CG  . LYS A 1 90   ? -10.635 13.970  -6.334  1.00 170.52 ? 90   LYS A CG  1 
ATOM   542   C  CD  . LYS A 1 90   ? -11.649 12.893  -6.605  1.00 165.97 ? 90   LYS A CD  1 
ATOM   543   C  CE  . LYS A 1 90   ? -12.486 12.656  -5.358  1.00 165.91 ? 90   LYS A CE  1 
ATOM   544   N  NZ  . LYS A 1 90   ? -13.858 12.143  -5.622  1.00 168.65 ? 90   LYS A NZ  1 
ATOM   545   N  N   . GLN A 1 91   ? -7.113  13.899  -8.221  1.00 351.85 ? 91   GLN A N   1 
ATOM   546   C  CA  . GLN A 1 91   ? -5.972  14.274  -9.056  1.00 366.00 ? 91   GLN A CA  1 
ATOM   547   C  C   . GLN A 1 91   ? -4.710  13.455  -8.797  1.00 379.70 ? 91   GLN A C   1 
ATOM   548   O  O   . GLN A 1 91   ? -4.051  13.620  -7.770  1.00 379.25 ? 91   GLN A O   1 
ATOM   549   C  CB  . GLN A 1 91   ? -5.661  15.767  -8.884  1.00 365.42 ? 91   GLN A CB  1 
ATOM   550   C  CG  . GLN A 1 91   ? -6.763  16.685  -9.376  1.00 368.96 ? 91   GLN A CG  1 
ATOM   551   C  CD  . GLN A 1 91   ? -7.161  16.379  -10.800 1.00 372.92 ? 91   GLN A CD  1 
ATOM   552   O  OE1 . GLN A 1 91   ? -8.290  15.967  -11.067 1.00 376.56 ? 91   GLN A OE1 1 
ATOM   553   N  NE2 . GLN A 1 91   ? -6.227  16.562  -11.726 1.00 371.93 ? 91   GLN A NE2 1 
ATOM   554   N  N   . LEU A 1 92   ? -4.374  12.585  -9.747  1.00 259.98 ? 92   LEU A N   1 
ATOM   555   C  CA  . LEU A 1 92   ? -3.177  11.749  -9.651  1.00 272.81 ? 92   LEU A CA  1 
ATOM   556   C  C   . LEU A 1 92   ? -2.067  12.075  -10.688 1.00 280.92 ? 92   LEU A C   1 
ATOM   557   O  O   . LEU A 1 92   ? -1.047  11.380  -10.728 1.00 279.37 ? 92   LEU A O   1 
ATOM   558   C  CB  . LEU A 1 92   ? -3.554  10.247  -9.700  1.00 279.19 ? 92   LEU A CB  1 
ATOM   559   C  CG  . LEU A 1 92   ? -4.509  9.627   -8.655  1.00 284.87 ? 92   LEU A CG  1 
ATOM   560   C  CD1 . LEU A 1 92   ? -5.022  8.252   -9.081  1.00 288.30 ? 92   LEU A CD1 1 
ATOM   561   C  CD2 . LEU A 1 92   ? -3.869  9.535   -7.284  1.00 283.99 ? 92   LEU A CD2 1 
ATOM   562   N  N   . PRO A 1 93   ? -2.242  13.137  -11.512 1.00 306.40 ? 93   PRO A N   1 
ATOM   563   C  CA  . PRO A 1 93   ? -1.216  13.402  -12.531 1.00 309.85 ? 93   PRO A CA  1 
ATOM   564   C  C   . PRO A 1 93   ? 0.107   13.874  -11.932 1.00 311.77 ? 93   PRO A C   1 
ATOM   565   O  O   . PRO A 1 93   ? 0.243   15.062  -11.639 1.00 312.06 ? 93   PRO A O   1 
ATOM   566   C  CB  . PRO A 1 93   ? -1.823  14.547  -13.357 1.00 309.48 ? 93   PRO A CB  1 
ATOM   567   C  CG  . PRO A 1 93   ? -3.254  14.629  -12.953 1.00 311.68 ? 93   PRO A CG  1 
ATOM   568   C  CD  . PRO A 1 93   ? -3.295  14.165  -11.541 1.00 311.22 ? 93   PRO A CD  1 
ATOM   569   N  N   . GLY A 1 94   ? 1.067   12.968  -11.765 1.00 327.82 ? 94   GLY A N   1 
ATOM   570   C  CA  . GLY A 1 94   ? 2.384   13.348  -11.287 1.00 327.41 ? 94   GLY A CA  1 
ATOM   571   C  C   . GLY A 1 94   ? 2.951   14.454  -12.155 1.00 327.63 ? 94   GLY A C   1 
ATOM   572   O  O   . GLY A 1 94   ? 2.686   14.498  -13.354 1.00 329.02 ? 94   GLY A O   1 
ATOM   573   N  N   . GLY A 1 95   ? 3.728   15.349  -11.560 1.00 297.21 ? 95   GLY A N   1 
ATOM   574   C  CA  . GLY A 1 95   ? 4.252   16.485  -12.293 1.00 295.55 ? 95   GLY A CA  1 
ATOM   575   C  C   . GLY A 1 95   ? 3.355   17.703  -12.179 1.00 297.34 ? 95   GLY A C   1 
ATOM   576   O  O   . GLY A 1 95   ? 3.780   18.736  -11.664 1.00 295.78 ? 95   GLY A O   1 
ATOM   577   N  N   . GLN A 1 96   ? 2.118   17.593  -12.659 1.00 318.34 ? 96   GLN A N   1 
ATOM   578   C  CA  . GLN A 1 96   ? 1.138   18.647  -12.437 1.00 317.82 ? 96   GLN A CA  1 
ATOM   579   C  C   . GLN A 1 96   ? 1.204   18.953  -10.953 1.00 320.01 ? 96   GLN A C   1 
ATOM   580   O  O   . GLN A 1 96   ? 1.406   18.043  -10.157 1.00 322.35 ? 96   GLN A O   1 
ATOM   581   C  CB  . GLN A 1 96   ? -0.267  18.169  -12.821 1.00 316.59 ? 96   GLN A CB  1 
ATOM   582   C  CG  . GLN A 1 96   ? -1.388  19.125  -12.432 1.00 314.29 ? 96   GLN A CG  1 
ATOM   583   C  CD  . GLN A 1 96   ? -2.762  18.608  -12.813 1.00 316.23 ? 96   GLN A CD  1 
ATOM   584   O  OE1 . GLN A 1 96   ? -2.887  17.598  -13.502 1.00 317.59 ? 96   GLN A OE1 1 
ATOM   585   N  NE2 . GLN A 1 96   ? -3.803  19.304  -12.365 1.00 316.89 ? 96   GLN A NE2 1 
ATOM   586   N  N   . ASN A 1 97   ? 1.091   20.224  -10.578 1.00 369.27 ? 97   ASN A N   1 
ATOM   587   C  CA  . ASN A 1 97   ? 1.045   20.591  -9.165  1.00 367.51 ? 97   ASN A CA  1 
ATOM   588   C  C   . ASN A 1 97   ? -0.379  20.466  -8.644  1.00 363.73 ? 97   ASN A C   1 
ATOM   589   O  O   . ASN A 1 97   ? -1.027  21.474  -8.362  1.00 363.76 ? 97   ASN A O   1 
ATOM   590   C  CB  . ASN A 1 97   ? 1.542   22.024  -8.958  1.00 368.80 ? 97   ASN A CB  1 
ATOM   591   C  CG  . ASN A 1 97   ? 2.936   22.246  -9.507  1.00 369.91 ? 97   ASN A CG  1 
ATOM   592   O  OD1 . ASN A 1 97   ? 3.689   21.298  -9.724  1.00 369.79 ? 97   ASN A OD1 1 
ATOM   593   N  ND2 . ASN A 1 97   ? 3.289   23.506  -9.732  1.00 369.07 ? 97   ASN A ND2 1 
ATOM   594   N  N   . PRO A 1 98   ? -0.873  19.227  -8.498  1.00 394.53 ? 98   PRO A N   1 
ATOM   595   C  CA  . PRO A 1 98   ? -2.306  19.057  -8.290  1.00 388.53 ? 98   PRO A CA  1 
ATOM   596   C  C   . PRO A 1 98   ? -2.622  19.322  -6.839  1.00 374.92 ? 98   PRO A C   1 
ATOM   597   O  O   . PRO A 1 98   ? -1.703  19.459  -6.034  1.00 374.61 ? 98   PRO A O   1 
ATOM   598   C  CB  . PRO A 1 98   ? -2.519  17.562  -8.575  1.00 395.54 ? 98   PRO A CB  1 
ATOM   599   C  CG  . PRO A 1 98   ? -1.113  16.949  -8.685  1.00 394.80 ? 98   PRO A CG  1 
ATOM   600   C  CD  . PRO A 1 98   ? -0.159  17.986  -8.178  1.00 393.35 ? 98   PRO A CD  1 
ATOM   601   N  N   . VAL A 1 99   ? -3.902  19.404  -6.509  1.00 370.95 ? 99   VAL A N   1 
ATOM   602   C  CA  . VAL A 1 99   ? -4.308  19.329  -5.118  1.00 356.87 ? 99   VAL A CA  1 
ATOM   603   C  C   . VAL A 1 99   ? -3.893  20.541  -4.274  1.00 336.02 ? 99   VAL A C   1 
ATOM   604   O  O   . VAL A 1 99   ? -4.480  20.791  -3.225  1.00 336.98 ? 99   VAL A O   1 
ATOM   605   C  CB  . VAL A 1 99   ? -3.742  18.045  -4.483  1.00 361.27 ? 99   VAL A CB  1 
ATOM   606   C  CG1 . VAL A 1 99   ? -4.174  17.919  -3.036  1.00 364.13 ? 99   VAL A CG1 1 
ATOM   607   C  CG2 . VAL A 1 99   ? -4.164  16.824  -5.293  1.00 364.03 ? 99   VAL A CG2 1 
ATOM   608   N  N   . SER A 1 100  ? -2.896  21.299  -4.721  1.00 200.31 ? 100  SER A N   1 
ATOM   609   C  CA  . SER A 1 100  ? -2.429  22.451  -3.945  1.00 179.74 ? 100  SER A CA  1 
ATOM   610   C  C   . SER A 1 100  ? -3.499  23.539  -3.818  1.00 164.56 ? 100  SER A C   1 
ATOM   611   O  O   . SER A 1 100  ? -3.612  24.355  -4.715  1.00 165.65 ? 100  SER A O   1 
ATOM   612   C  CB  . SER A 1 100  ? -1.168  23.055  -4.575  1.00 172.26 ? 100  SER A CB  1 
ATOM   613   O  OG  . SER A 1 100  ? -0.526  22.138  -5.441  1.00 170.55 ? 100  SER A OG  1 
ATOM   614   N  N   . TYR A 1 101  ? -4.247  23.561  -2.705  1.00 229.41 ? 101  TYR A N   1 
ATOM   615   C  CA  . TYR A 1 101  ? -5.351  24.523  -2.423  1.00 215.50 ? 101  TYR A CA  1 
ATOM   616   C  C   . TYR A 1 101  ? -6.746  23.919  -2.600  1.00 210.51 ? 101  TYR A C   1 
ATOM   617   O  O   . TYR A 1 101  ? -6.998  23.203  -3.565  1.00 211.04 ? 101  TYR A O   1 
ATOM   618   C  CB  . TYR A 1 101  ? -5.282  25.796  -3.276  1.00 208.12 ? 101  TYR A CB  1 
ATOM   619   C  CG  . TYR A 1 101  ? -4.179  26.769  -2.936  1.00 202.70 ? 101  TYR A CG  1 
ATOM   620   C  CD1 . TYR A 1 101  ? -4.472  28.016  -2.417  1.00 202.52 ? 101  TYR A CD1 1 
ATOM   621   C  CD2 . TYR A 1 101  ? -2.844  26.454  -3.168  1.00 199.85 ? 101  TYR A CD2 1 
ATOM   622   C  CE1 . TYR A 1 101  ? -3.472  28.910  -2.123  1.00 200.20 ? 101  TYR A CE1 1 
ATOM   623   C  CE2 . TYR A 1 101  ? -1.838  27.342  -2.877  1.00 197.75 ? 101  TYR A CE2 1 
ATOM   624   C  CZ  . TYR A 1 101  ? -2.159  28.569  -2.354  1.00 198.37 ? 101  TYR A CZ  1 
ATOM   625   O  OH  . TYR A 1 101  ? -1.158  29.461  -2.061  1.00 196.23 ? 101  TYR A OH  1 
ATOM   626   N  N   . VAL A 1 102  ? -7.666  24.229  -1.694  1.00 223.69 ? 102  VAL A N   1 
ATOM   627   C  CA  . VAL A 1 102  ? -9.044  23.810  -1.908  1.00 222.59 ? 102  VAL A CA  1 
ATOM   628   C  C   . VAL A 1 102  ? -10.074 24.760  -1.354  1.00 224.34 ? 102  VAL A C   1 
ATOM   629   O  O   . VAL A 1 102  ? -9.768  25.700  -0.612  1.00 222.05 ? 102  VAL A O   1 
ATOM   630   C  CB  . VAL A 1 102  ? -9.372  22.414  -1.335  1.00 221.83 ? 102  VAL A CB  1 
ATOM   631   C  CG1 . VAL A 1 102  ? -8.298  21.404  -1.698  1.00 219.28 ? 102  VAL A CG1 1 
ATOM   632   C  CG2 . VAL A 1 102  ? -9.567  22.494  0.168   1.00 221.90 ? 102  VAL A CG2 1 
ATOM   633   N  N   . TYR A 1 103  ? -11.310 24.476  -1.755  1.00 260.78 ? 103  TYR A N   1 
ATOM   634   C  CA  . TYR A 1 103  ? -12.481 25.211  -1.327  1.00 262.57 ? 103  TYR A CA  1 
ATOM   635   C  C   . TYR A 1 103  ? -13.324 24.323  -0.427  1.00 263.96 ? 103  TYR A C   1 
ATOM   636   O  O   . TYR A 1 103  ? -13.709 23.202  -0.775  1.00 261.04 ? 103  TYR A O   1 
ATOM   637   C  CB  . TYR A 1 103  ? -13.282 25.732  -2.537  1.00 273.81 ? 103  TYR A CB  1 
ATOM   638   C  CG  . TYR A 1 103  ? -12.754 27.041  -3.124  1.00 278.00 ? 103  TYR A CG  1 
ATOM   639   C  CD1 . TYR A 1 103  ? -11.479 27.118  -3.673  1.00 281.31 ? 103  TYR A CD1 1 
ATOM   640   C  CD2 . TYR A 1 103  ? -13.535 28.193  -3.136  1.00 282.25 ? 103  TYR A CD2 1 
ATOM   641   C  CE1 . TYR A 1 103  ? -10.992 28.308  -4.207  1.00 281.85 ? 103  TYR A CE1 1 
ATOM   642   C  CE2 . TYR A 1 103  ? -13.053 29.389  -3.672  1.00 282.75 ? 103  TYR A CE2 1 
ATOM   643   C  CZ  . TYR A 1 103  ? -11.782 29.438  -4.204  1.00 282.97 ? 103  TYR A CZ  1 
ATOM   644   O  OH  . TYR A 1 103  ? -11.300 30.615  -4.731  1.00 282.15 ? 103  TYR A OH  1 
ATOM   645   N  N   . LEU A 1 104  ? -13.563 24.839  0.761   1.00 167.70 ? 104  LEU A N   1 
ATOM   646   C  CA  . LEU A 1 104  ? -14.390 24.189  1.734   1.00 171.58 ? 104  LEU A CA  1 
ATOM   647   C  C   . LEU A 1 104  ? -15.690 24.929  1.637   1.00 172.89 ? 104  LEU A C   1 
ATOM   648   O  O   . LEU A 1 104  ? -15.685 26.154  1.597   1.00 167.87 ? 104  LEU A O   1 
ATOM   649   C  CB  . LEU A 1 104  ? -13.773 24.440  3.108   1.00 170.34 ? 104  LEU A CB  1 
ATOM   650   C  CG  . LEU A 1 104  ? -14.198 23.689  4.373   1.00 170.56 ? 104  LEU A CG  1 
ATOM   651   C  CD1 . LEU A 1 104  ? -14.005 22.184  4.207   1.00 172.58 ? 104  LEU A CD1 1 
ATOM   652   C  CD2 . LEU A 1 104  ? -13.393 24.206  5.550   1.00 167.84 ? 104  LEU A CD2 1 
ATOM   653   N  N   . GLU A 1 105  ? -16.802 24.209  1.617   1.00 219.76 ? 105  GLU A N   1 
ATOM   654   C  CA  . GLU A 1 105  ? -18.079 24.861  1.383   1.00 224.66 ? 105  GLU A CA  1 
ATOM   655   C  C   . GLU A 1 105  ? -19.171 24.440  2.348   1.00 228.20 ? 105  GLU A C   1 
ATOM   656   O  O   . GLU A 1 105  ? -19.324 23.264  2.660   1.00 230.36 ? 105  GLU A O   1 
ATOM   657   C  CB  . GLU A 1 105  ? -18.533 24.612  -0.059  1.00 228.19 ? 105  GLU A CB  1 
ATOM   658   C  CG  . GLU A 1 105  ? -19.585 25.597  -0.596  1.00 230.61 ? 105  GLU A CG  1 
ATOM   659   C  CD  . GLU A 1 105  ? -19.638 25.638  -2.130  1.00 232.72 ? 105  GLU A CD  1 
ATOM   660   O  OE1 . GLU A 1 105  ? -19.947 24.602  -2.756  1.00 235.84 ? 105  GLU A OE1 1 
ATOM   661   O  OE2 . GLU A 1 105  ? -19.377 26.712  -2.709  1.00 231.16 ? 105  GLU A OE2 1 
ATOM   662   N  N   . VAL A 1 106  ? -19.940 25.419  2.802   1.00 229.12 ? 106  VAL A N   1 
ATOM   663   C  CA  . VAL A 1 106  ? -21.093 25.142  3.635   1.00 232.33 ? 106  VAL A CA  1 
ATOM   664   C  C   . VAL A 1 106  ? -22.351 25.698  2.980   1.00 234.10 ? 106  VAL A C   1 
ATOM   665   O  O   . VAL A 1 106  ? -22.272 26.438  2.001   1.00 232.66 ? 106  VAL A O   1 
ATOM   666   C  CB  . VAL A 1 106  ? -20.911 25.741  5.024   1.00 231.25 ? 106  VAL A CB  1 
ATOM   667   C  CG1 . VAL A 1 106  ? -22.077 25.357  5.928   1.00 234.92 ? 106  VAL A CG1 1 
ATOM   668   C  CG2 . VAL A 1 106  ? -19.604 25.253  5.609   1.00 230.70 ? 106  VAL A CG2 1 
ATOM   669   N  N   . VAL A 1 107  ? -23.512 25.327  3.509   1.00 221.72 ? 107  VAL A N   1 
ATOM   670   C  CA  . VAL A 1 107  ? -24.784 25.758  2.946   1.00 223.31 ? 107  VAL A CA  1 
ATOM   671   C  C   . VAL A 1 107  ? -25.817 25.905  4.060   1.00 224.01 ? 107  VAL A C   1 
ATOM   672   O  O   . VAL A 1 107  ? -25.685 25.303  5.133   1.00 224.81 ? 107  VAL A O   1 
ATOM   673   C  CB  . VAL A 1 107  ? -25.299 24.757  1.877   1.00 232.03 ? 107  VAL A CB  1 
ATOM   674   C  CG1 . VAL A 1 107  ? -26.563 25.274  1.223   1.00 233.70 ? 107  VAL A CG1 1 
ATOM   675   C  CG2 . VAL A 1 107  ? -24.236 24.500  0.825   1.00 229.86 ? 107  VAL A CG2 1 
ATOM   676   N  N   . SER A 1 108  ? -26.833 26.721  3.802   1.00 196.60 ? 108  SER A N   1 
ATOM   677   C  CA  . SER A 1 108  ? -27.930 26.901  4.741   1.00 201.18 ? 108  SER A CA  1 
ATOM   678   C  C   . SER A 1 108  ? -29.012 27.798  4.145   1.00 208.35 ? 108  SER A C   1 
ATOM   679   O  O   . SER A 1 108  ? -28.876 28.282  3.024   1.00 208.87 ? 108  SER A O   1 
ATOM   680   C  CB  . SER A 1 108  ? -27.421 27.460  6.078   1.00 199.37 ? 108  SER A CB  1 
ATOM   681   O  OG  . SER A 1 108  ? -26.347 28.369  5.891   1.00 195.75 ? 108  SER A OG  1 
ATOM   682   N  N   . LYS A 1 109  ? -30.086 28.005  4.901   1.00 289.29 ? 109  LYS A N   1 
ATOM   683   C  CA  . LYS A 1 109  ? -31.196 28.847  4.462   1.00 295.30 ? 109  LYS A CA  1 
ATOM   684   C  C   . LYS A 1 109  ? -30.854 30.330  4.500   1.00 296.75 ? 109  LYS A C   1 
ATOM   685   O  O   . LYS A 1 109  ? -31.352 31.104  3.694   1.00 297.20 ? 109  LYS A O   1 
ATOM   686   C  CB  . LYS A 1 109  ? -32.456 28.578  5.302   1.00 298.67 ? 109  LYS A CB  1 
ATOM   687   C  CG  . LYS A 1 109  ? -32.267 28.645  6.834   1.00 300.61 ? 109  LYS A CG  1 
ATOM   688   C  CD  . LYS A 1 109  ? -32.180 30.077  7.369   1.00 295.85 ? 109  LYS A CD  1 
ATOM   689   C  CE  . LYS A 1 109  ? -31.971 30.136  8.888   1.00 294.13 ? 109  LYS A CE  1 
ATOM   690   N  NZ  . LYS A 1 109  ? -33.249 30.176  9.664   1.00 296.06 ? 109  LYS A NZ  1 
ATOM   691   N  N   . HIS A 1 110  ? -30.000 30.720  5.437   1.00 303.12 ? 110  HIS A N   1 
ATOM   692   C  CA  . HIS A 1 110  ? -29.771 32.132  5.733   1.00 303.41 ? 110  HIS A CA  1 
ATOM   693   C  C   . HIS A 1 110  ? -28.593 32.728  4.954   1.00 296.63 ? 110  HIS A C   1 
ATOM   694   O  O   . HIS A 1 110  ? -28.428 33.950  4.901   1.00 295.03 ? 110  HIS A O   1 
ATOM   695   C  CB  . HIS A 1 110  ? -29.587 32.304  7.248   1.00 309.17 ? 110  HIS A CB  1 
ATOM   696   C  CG  . HIS A 1 110  ? -29.243 33.696  7.672   1.00 314.26 ? 110  HIS A CG  1 
ATOM   697   N  ND1 . HIS A 1 110  ? -28.474 33.960  8.785   1.00 315.88 ? 110  HIS A ND1 1 
ATOM   698   C  CD2 . HIS A 1 110  ? -29.562 34.899  7.140   1.00 316.39 ? 110  HIS A CD2 1 
ATOM   699   C  CE1 . HIS A 1 110  ? -28.331 35.266  8.919   1.00 315.44 ? 110  HIS A CE1 1 
ATOM   700   N  NE2 . HIS A 1 110  ? -28.980 35.859  7.931   1.00 315.68 ? 110  HIS A NE2 1 
ATOM   701   N  N   . PHE A 1 111  ? -27.794 31.857  4.339   1.00 269.67 ? 111  PHE A N   1 
ATOM   702   C  CA  . PHE A 1 111  ? -26.551 32.266  3.685   1.00 261.54 ? 111  PHE A CA  1 
ATOM   703   C  C   . PHE A 1 111  ? -25.780 31.043  3.174   1.00 252.84 ? 111  PHE A C   1 
ATOM   704   O  O   . PHE A 1 111  ? -26.259 29.909  3.251   1.00 251.62 ? 111  PHE A O   1 
ATOM   705   C  CB  . PHE A 1 111  ? -25.674 33.049  4.675   1.00 261.12 ? 111  PHE A CB  1 
ATOM   706   C  CG  . PHE A 1 111  ? -24.784 34.083  4.030   1.00 259.90 ? 111  PHE A CG  1 
ATOM   707   C  CD1 . PHE A 1 111  ? -25.232 35.385  3.855   1.00 260.29 ? 111  PHE A CD1 1 
ATOM   708   C  CD2 . PHE A 1 111  ? -23.497 33.759  3.617   1.00 258.36 ? 111  PHE A CD2 1 
ATOM   709   C  CE1 . PHE A 1 111  ? -24.419 36.340  3.270   1.00 258.11 ? 111  PHE A CE1 1 
ATOM   710   C  CE2 . PHE A 1 111  ? -22.676 34.708  3.029   1.00 255.70 ? 111  PHE A CE2 1 
ATOM   711   C  CZ  . PHE A 1 111  ? -23.137 36.000  2.857   1.00 255.61 ? 111  PHE A CZ  1 
ATOM   712   N  N   . SER A 1 112  ? -24.583 31.290  2.653   1.00 205.55 ? 112  SER A N   1 
ATOM   713   C  CA  . SER A 1 112  ? -23.663 30.229  2.263   1.00 200.54 ? 112  SER A CA  1 
ATOM   714   C  C   . SER A 1 112  ? -22.254 30.826  2.101   1.00 196.56 ? 112  SER A C   1 
ATOM   715   O  O   . SER A 1 112  ? -22.102 31.945  1.593   1.00 195.09 ? 112  SER A O   1 
ATOM   716   C  CB  . SER A 1 112  ? -24.132 29.546  0.974   1.00 198.35 ? 112  SER A CB  1 
ATOM   717   O  OG  . SER A 1 112  ? -23.859 28.151  0.991   1.00 197.34 ? 112  SER A OG  1 
ATOM   718   N  N   . LYS A 1 113  ? -21.232 30.093  2.556   1.00 194.07 ? 113  LYS A N   1 
ATOM   719   C  CA  . LYS A 1 113  ? -19.850 30.581  2.502   1.00 187.38 ? 113  LYS A CA  1 
ATOM   720   C  C   . LYS A 1 113  ? -18.791 29.480  2.568   1.00 182.90 ? 113  LYS A C   1 
ATOM   721   O  O   . LYS A 1 113  ? -19.061 28.340  2.954   1.00 183.59 ? 113  LYS A O   1 
ATOM   722   C  CB  . LYS A 1 113  ? -19.601 31.644  3.577   1.00 186.90 ? 113  LYS A CB  1 
ATOM   723   C  CG  . LYS A 1 113  ? -18.227 32.300  3.534   1.00 186.51 ? 113  LYS A CG  1 
ATOM   724   C  CD  . LYS A 1 113  ? -18.073 33.290  2.392   1.00 187.19 ? 113  LYS A CD  1 
ATOM   725   C  CE  . LYS A 1 113  ? -16.732 34.016  2.490   1.00 184.97 ? 113  LYS A CE  1 
ATOM   726   N  NZ  . LYS A 1 113  ? -16.841 35.264  3.310   1.00 182.99 ? 113  LYS A NZ  1 
ATOM   727   N  N   . SER A 1 114  ? -17.576 29.860  2.198   1.00 201.36 ? 114  SER A N   1 
ATOM   728   C  CA  . SER A 1 114  ? -16.553 28.908  1.822   1.00 205.60 ? 114  SER A CA  1 
ATOM   729   C  C   . SER A 1 114  ? -15.204 29.609  1.697   1.00 203.81 ? 114  SER A C   1 
ATOM   730   O  O   . SER A 1 114  ? -15.122 30.831  1.867   1.00 200.55 ? 114  SER A O   1 
ATOM   731   C  CB  . SER A 1 114  ? -16.947 28.291  0.493   1.00 209.48 ? 114  SER A CB  1 
ATOM   732   O  OG  . SER A 1 114  ? -17.803 29.170  -0.225  1.00 210.76 ? 114  SER A OG  1 
ATOM   733   N  N   . LYS A 1 115  ? -14.150 28.859  1.374   1.00 211.16 ? 115  LYS A N   1 
ATOM   734   C  CA  . LYS A 1 115  ? -12.802 29.379  1.591   1.00 208.34 ? 115  LYS A CA  1 
ATOM   735   C  C   . LYS A 1 115  ? -11.661 28.663  0.852   1.00 207.65 ? 115  LYS A C   1 
ATOM   736   O  O   . LYS A 1 115  ? -11.822 27.532  0.410   1.00 207.90 ? 115  LYS A O   1 
ATOM   737   C  CB  . LYS A 1 115  ? -12.537 29.354  3.094   1.00 208.53 ? 115  LYS A CB  1 
ATOM   738   C  CG  . LYS A 1 115  ? -11.117 29.602  3.471   1.00 203.90 ? 115  LYS A CG  1 
ATOM   739   C  CD  . LYS A 1 115  ? -10.978 30.808  4.360   1.00 199.15 ? 115  LYS A CD  1 
ATOM   740   C  CE  . LYS A 1 115  ? -9.612  30.789  5.019   1.00 195.10 ? 115  LYS A CE  1 
ATOM   741   N  NZ  . LYS A 1 115  ? -9.344  31.996  5.845   1.00 191.67 ? 115  LYS A NZ  1 
ATOM   742   N  N   . ARG A 1 116  ? -10.517 29.339  0.720   1.00 244.97 ? 116  ARG A N   1 
ATOM   743   C  CA  . ARG A 1 116  ? -9.297  28.755  0.147   1.00 248.24 ? 116  ARG A CA  1 
ATOM   744   C  C   . ARG A 1 116  ? -8.180  28.677  1.183   1.00 248.40 ? 116  ARG A C   1 
ATOM   745   O  O   . ARG A 1 116  ? -7.860  29.681  1.817   1.00 248.59 ? 116  ARG A O   1 
ATOM   746   C  CB  . ARG A 1 116  ? -8.804  29.593  -1.026  1.00 249.33 ? 116  ARG A CB  1 
ATOM   747   C  CG  . ARG A 1 116  ? -7.332  29.387  -1.370  1.00 251.90 ? 116  ARG A CG  1 
ATOM   748   C  CD  . ARG A 1 116  ? -6.402  30.275  -0.533  1.00 254.46 ? 116  ARG A CD  1 
ATOM   749   N  NE  . ARG A 1 116  ? -5.367  30.897  -1.356  1.00 256.30 ? 116  ARG A NE  1 
ATOM   750   C  CZ  . ARG A 1 116  ? -4.315  31.561  -0.884  1.00 257.02 ? 116  ARG A CZ  1 
ATOM   751   N  NH1 . ARG A 1 116  ? -4.133  31.693  0.424   1.00 257.75 ? 116  ARG A NH1 1 
ATOM   752   N  NH2 . ARG A 1 116  ? -3.434  32.089  -1.728  1.00 255.75 ? 116  ARG A NH2 1 
ATOM   753   N  N   . MET A 1 117  ? -7.552  27.506  1.308   1.00 240.25 ? 117  MET A N   1 
ATOM   754   C  CA  . MET A 1 117  ? -6.649  27.194  2.432   1.00 238.62 ? 117  MET A CA  1 
ATOM   755   C  C   . MET A 1 117  ? -5.808  25.944  2.129   1.00 236.40 ? 117  MET A C   1 
ATOM   756   O  O   . MET A 1 117  ? -6.368  24.871  1.898   1.00 236.57 ? 117  MET A O   1 
ATOM   757   C  CB  . MET A 1 117  ? -7.491  26.933  3.678   1.00 241.82 ? 117  MET A CB  1 
ATOM   758   C  CG  . MET A 1 117  ? -8.667  26.014  3.377   1.00 245.20 ? 117  MET A CG  1 
ATOM   759   S  SD  . MET A 1 117  ? -9.930  25.868  4.649   1.00 249.25 ? 117  MET A SD  1 
ATOM   760   C  CE  . MET A 1 117  ? -9.907  27.510  5.338   1.00 208.55 ? 117  MET A CE  1 
ATOM   761   N  N   . PRO A 1 118  ? -4.464  26.066  2.160   1.00 190.93 ? 118  PRO A N   1 
ATOM   762   C  CA  . PRO A 1 118  ? -3.572  25.018  1.625   1.00 189.47 ? 118  PRO A CA  1 
ATOM   763   C  C   . PRO A 1 118  ? -3.928  23.609  2.102   1.00 191.20 ? 118  PRO A C   1 
ATOM   764   O  O   . PRO A 1 118  ? -4.646  23.494  3.090   1.00 191.24 ? 118  PRO A O   1 
ATOM   765   C  CB  . PRO A 1 118  ? -2.190  25.431  2.136   1.00 187.01 ? 118  PRO A CB  1 
ATOM   766   C  CG  . PRO A 1 118  ? -2.282  26.907  2.343   1.00 185.43 ? 118  PRO A CG  1 
ATOM   767   C  CD  . PRO A 1 118  ? -3.719  27.230  2.670   1.00 188.30 ? 118  PRO A CD  1 
ATOM   768   N  N   . ILE A 1 119  ? -3.473  22.568  1.404   1.00 207.51 ? 119  ILE A N   1 
ATOM   769   C  CA  . ILE A 1 119  ? -3.668  21.193  1.877   1.00 207.47 ? 119  ILE A CA  1 
ATOM   770   C  C   . ILE A 1 119  ? -2.492  20.316  1.488   1.00 204.37 ? 119  ILE A C   1 
ATOM   771   O  O   . ILE A 1 119  ? -1.702  20.710  0.636   1.00 200.08 ? 119  ILE A O   1 
ATOM   772   C  CB  . ILE A 1 119  ? -4.963  20.554  1.338   1.00 208.48 ? 119  ILE A CB  1 
ATOM   773   C  CG1 . ILE A 1 119  ? -4.641  19.488  0.286   1.00 205.45 ? 119  ILE A CG1 1 
ATOM   774   C  CG2 . ILE A 1 119  ? -5.921  21.621  0.832   1.00 207.85 ? 119  ILE A CG2 1 
ATOM   775   C  CD1 . ILE A 1 119  ? -5.771  18.501  0.049   1.00 208.40 ? 119  ILE A CD1 1 
ATOM   776   N  N   . THR A 1 120  ? -2.370  19.140  2.111   1.00 164.76 ? 120  THR A N   1 
ATOM   777   C  CA  . THR A 1 120  ? -1.254  18.243  1.803   1.00 164.96 ? 120  THR A CA  1 
ATOM   778   C  C   . THR A 1 120  ? -1.641  16.766  1.784   1.00 165.47 ? 120  THR A C   1 
ATOM   779   O  O   . THR A 1 120  ? -2.817  16.381  1.957   1.00 165.63 ? 120  THR A O   1 
ATOM   780   C  CB  . THR A 1 120  ? 0.051   18.490  2.700   1.00 165.30 ? 120  THR A CB  1 
ATOM   781   O  OG1 . THR A 1 120  ? 0.435   19.867  2.647   1.00 164.83 ? 120  THR A OG1 1 
ATOM   782   C  CG2 . THR A 1 120  ? 1.272   17.645  2.241   1.00 165.56 ? 120  THR A CG2 1 
ATOM   783   N  N   . TYR A 1 121  ? -0.588  15.984  1.545   1.00 219.07 ? 121  TYR A N   1 
ATOM   784   C  CA  . TYR A 1 121  ? -0.589  14.559  1.292   1.00 219.89 ? 121  TYR A CA  1 
ATOM   785   C  C   . TYR A 1 121  ? 0.124   13.863  2.440   1.00 212.74 ? 121  TYR A C   1 
ATOM   786   O  O   . TYR A 1 121  ? 0.809   12.870  2.226   1.00 213.57 ? 121  TYR A O   1 
ATOM   787   C  CB  . TYR A 1 121  ? 0.229   14.269  0.029   1.00 223.02 ? 121  TYR A CB  1 
ATOM   788   C  CG  . TYR A 1 121  ? -0.121  15.072  -1.223  1.00 226.58 ? 121  TYR A CG  1 
ATOM   789   C  CD1 . TYR A 1 121  ? -1.134  14.655  -2.075  1.00 231.44 ? 121  TYR A CD1 1 
ATOM   790   C  CD2 . TYR A 1 121  ? 0.592   16.219  -1.573  1.00 224.55 ? 121  TYR A CD2 1 
ATOM   791   C  CE1 . TYR A 1 121  ? -1.448  15.364  -3.217  1.00 233.25 ? 121  TYR A CE1 1 
ATOM   792   C  CE2 . TYR A 1 121  ? 0.283   16.933  -2.721  1.00 225.74 ? 121  TYR A CE2 1 
ATOM   793   C  CZ  . TYR A 1 121  ? -0.739  16.496  -3.533  1.00 231.53 ? 121  TYR A CZ  1 
ATOM   794   O  OH  . TYR A 1 121  ? -1.063  17.190  -4.673  1.00 235.54 ? 121  TYR A OH  1 
ATOM   795   N  N   . ASP A 1 122  ? -0.024  14.397  3.649   1.00 223.13 ? 122  ASP A N   1 
ATOM   796   C  CA  . ASP A 1 122  ? 0.657   13.871  4.831   1.00 216.82 ? 122  ASP A CA  1 
ATOM   797   C  C   . ASP A 1 122  ? -0.234  13.057  5.781   1.00 215.12 ? 122  ASP A C   1 
ATOM   798   O  O   . ASP A 1 122  ? -0.441  13.451  6.924   1.00 218.33 ? 122  ASP A O   1 
ATOM   799   C  CB  . ASP A 1 122  ? 1.281   15.027  5.604   1.00 215.90 ? 122  ASP A CB  1 
ATOM   800   C  CG  . ASP A 1 122  ? 2.657   14.703  6.107   1.00 215.00 ? 122  ASP A CG  1 
ATOM   801   O  OD1 . ASP A 1 122  ? 3.386   15.651  6.473   1.00 213.30 ? 122  ASP A OD1 1 
ATOM   802   O  OD2 . ASP A 1 122  ? 3.009   13.503  6.127   1.00 215.72 ? 122  ASP A OD2 1 
ATOM   803   N  N   . ASN A 1 123  ? -0.731  11.914  5.320   1.00 244.00 ? 123  ASN A N   1 
ATOM   804   C  CA  . ASN A 1 123  ? -1.672  11.112  6.102   1.00 245.04 ? 123  ASN A CA  1 
ATOM   805   C  C   . ASN A 1 123  ? -1.014  9.973   6.885   1.00 245.89 ? 123  ASN A C   1 
ATOM   806   O  O   . ASN A 1 123  ? -0.568  8.987   6.299   1.00 246.47 ? 123  ASN A O   1 
ATOM   807   C  CB  . ASN A 1 123  ? -2.774  10.564  5.183   1.00 248.20 ? 123  ASN A CB  1 
ATOM   808   C  CG  . ASN A 1 123  ? -3.902  9.885   5.943   1.00 250.77 ? 123  ASN A CG  1 
ATOM   809   O  OD1 . ASN A 1 123  ? -5.043  9.854   5.477   1.00 254.06 ? 123  ASN A OD1 1 
ATOM   810   N  ND2 . ASN A 1 123  ? -3.590  9.335   7.110   1.00 251.13 ? 123  ASN A ND2 1 
ATOM   811   N  N   . GLY A 1 124  ? -0.969  10.108  8.208   1.00 170.56 ? 124  GLY A N   1 
ATOM   812   C  CA  . GLY A 1 124  ? -0.474  9.045   9.072   1.00 173.35 ? 124  GLY A CA  1 
ATOM   813   C  C   . GLY A 1 124  ? 1.003   9.112   9.431   1.00 179.36 ? 124  GLY A C   1 
ATOM   814   O  O   . GLY A 1 124  ? 1.588   10.189  9.455   1.00 176.72 ? 124  GLY A O   1 
ATOM   815   N  N   . PHE A 1 125  ? 1.617   7.967   9.722   1.00 185.12 ? 125  PHE A N   1 
ATOM   816   C  CA  . PHE A 1 125  ? 3.039   7.959   10.045  1.00 181.31 ? 125  PHE A CA  1 
ATOM   817   C  C   . PHE A 1 125  ? 3.642   6.607   9.869   1.00 180.75 ? 125  PHE A C   1 
ATOM   818   O  O   . PHE A 1 125  ? 2.940   5.590   9.872   1.00 182.49 ? 125  PHE A O   1 
ATOM   819   C  CB  . PHE A 1 125  ? 3.243   8.390   11.468  1.00 180.79 ? 125  PHE A CB  1 
ATOM   820   C  CG  . PHE A 1 125  ? 2.260   9.388   11.896  1.00 182.30 ? 125  PHE A CG  1 
ATOM   821   C  CD1 . PHE A 1 125  ? 1.031   8.989   12.395  1.00 186.08 ? 125  PHE A CD1 1 
ATOM   822   C  CD2 . PHE A 1 125  ? 2.523   10.734  11.739  1.00 180.02 ? 125  PHE A CD2 1 
ATOM   823   C  CE1 . PHE A 1 125  ? 0.085   9.919   12.771  1.00 188.09 ? 125  PHE A CE1 1 
ATOM   824   C  CE2 . PHE A 1 125  ? 1.585   11.677  12.108  1.00 182.74 ? 125  PHE A CE2 1 
ATOM   825   C  CZ  . PHE A 1 125  ? 0.360   11.271  12.627  1.00 186.91 ? 125  PHE A CZ  1 
ATOM   826   N  N   . LEU A 1 126  ? 4.958   6.608   9.712   1.00 152.86 ? 126  LEU A N   1 
ATOM   827   C  CA  . LEU A 1 126  ? 5.686   5.372   9.525   1.00 151.86 ? 126  LEU A CA  1 
ATOM   828   C  C   . LEU A 1 126  ? 6.744   5.146   10.633  1.00 151.76 ? 126  LEU A C   1 
ATOM   829   O  O   . LEU A 1 126  ? 7.640   5.971   10.856  1.00 150.76 ? 126  LEU A O   1 
ATOM   830   C  CB  . LEU A 1 126  ? 6.274   5.295   8.095   1.00 149.54 ? 126  LEU A CB  1 
ATOM   831   C  CG  . LEU A 1 126  ? 5.442   4.894   6.854   1.00 149.41 ? 126  LEU A CG  1 
ATOM   832   C  CD1 . LEU A 1 126  ? 4.257   3.969   7.156   1.00 151.52 ? 126  LEU A CD1 1 
ATOM   833   C  CD2 . LEU A 1 126  ? 4.971   6.105   6.076   1.00 148.98 ? 126  LEU A CD2 1 
ATOM   834   N  N   . PHE A 1 127  ? 6.598   4.017   11.325  1.00 152.94 ? 127  PHE A N   1 
ATOM   835   C  CA  . PHE A 1 127  ? 7.471   3.621   12.408  1.00 153.13 ? 127  PHE A CA  1 
ATOM   836   C  C   . PHE A 1 127  ? 8.268   2.422   11.991  1.00 151.83 ? 127  PHE A C   1 
ATOM   837   O  O   . PHE A 1 127  ? 7.714   1.369   11.699  1.00 152.44 ? 127  PHE A O   1 
ATOM   838   C  CB  . PHE A 1 127  ? 6.640   3.239   13.625  1.00 155.78 ? 127  PHE A CB  1 
ATOM   839   C  CG  . PHE A 1 127  ? 5.963   4.407   14.289  1.00 157.37 ? 127  PHE A CG  1 
ATOM   840   C  CD1 . PHE A 1 127  ? 6.507   5.678   14.222  1.00 156.41 ? 127  PHE A CD1 1 
ATOM   841   C  CD2 . PHE A 1 127  ? 4.790   4.237   14.988  1.00 159.94 ? 127  PHE A CD2 1 
ATOM   842   C  CE1 . PHE A 1 127  ? 5.882   6.759   14.838  1.00 157.99 ? 127  PHE A CE1 1 
ATOM   843   C  CE2 . PHE A 1 127  ? 4.166   5.317   15.600  1.00 161.54 ? 127  PHE A CE2 1 
ATOM   844   C  CZ  . PHE A 1 127  ? 4.714   6.575   15.522  1.00 160.56 ? 127  PHE A CZ  1 
ATOM   845   N  N   . ILE A 1 128  ? 9.578   2.571   11.980  1.00 150.15 ? 128  ILE A N   1 
ATOM   846   C  CA  . ILE A 1 128  ? 10.417  1.499   11.495  1.00 148.79 ? 128  ILE A CA  1 
ATOM   847   C  C   . ILE A 1 128  ? 11.191  0.775   12.562  1.00 149.20 ? 128  ILE A C   1 
ATOM   848   O  O   . ILE A 1 128  ? 12.384  1.007   12.740  1.00 147.97 ? 128  ILE A O   1 
ATOM   849   C  CB  . ILE A 1 128  ? 11.446  2.016   10.553  1.00 146.46 ? 128  ILE A CB  1 
ATOM   850   C  CG1 . ILE A 1 128  ? 11.125  3.446   10.154  1.00 146.14 ? 128  ILE A CG1 1 
ATOM   851   C  CG2 . ILE A 1 128  ? 11.495  1.123   9.358   1.00 145.38 ? 128  ILE A CG2 1 
ATOM   852   C  CD1 . ILE A 1 128  ? 11.753  3.824   8.831   1.00 143.99 ? 128  ILE A CD1 1 
ATOM   853   N  N   . HIS A 1 129  ? 10.516  -0.137  13.237  1.00 184.92 ? 129  HIS A N   1 
ATOM   854   C  CA  . HIS A 1 129  ? 11.100  -0.869  14.344  1.00 187.63 ? 129  HIS A CA  1 
ATOM   855   C  C   . HIS A 1 129  ? 12.265  -1.737  13.891  1.00 189.96 ? 129  HIS A C   1 
ATOM   856   O  O   . HIS A 1 129  ? 12.100  -2.939  13.696  1.00 194.24 ? 129  HIS A O   1 
ATOM   857   C  CB  . HIS A 1 129  ? 9.997   -1.702  15.019  1.00 187.84 ? 129  HIS A CB  1 
ATOM   858   C  CG  . HIS A 1 129  ? 10.487  -2.727  16.000  1.00 186.23 ? 129  HIS A CG  1 
ATOM   859   N  ND1 . HIS A 1 129  ? 9.620   -3.469  16.773  1.00 187.94 ? 129  HIS A ND1 1 
ATOM   860   C  CD2 . HIS A 1 129  ? 11.732  -3.151  16.324  1.00 184.47 ? 129  HIS A CD2 1 
ATOM   861   C  CE1 . HIS A 1 129  ? 10.306  -4.299  17.536  1.00 189.57 ? 129  HIS A CE1 1 
ATOM   862   N  NE2 . HIS A 1 129  ? 11.591  -4.127  17.282  1.00 187.98 ? 129  HIS A NE2 1 
ATOM   863   N  N   . THR A 1 130  ? 13.441  -1.139  13.707  1.00 148.30 ? 130  THR A N   1 
ATOM   864   C  CA  . THR A 1 130  ? 14.630  -1.962  13.504  1.00 146.96 ? 130  THR A CA  1 
ATOM   865   C  C   . THR A 1 130  ? 14.727  -2.783  14.776  1.00 148.45 ? 130  THR A C   1 
ATOM   866   O  O   . THR A 1 130  ? 14.319  -2.306  15.817  1.00 149.98 ? 130  THR A O   1 
ATOM   867   C  CB  . THR A 1 130  ? 15.911  -1.132  13.233  1.00 145.11 ? 130  THR A CB  1 
ATOM   868   O  OG1 . THR A 1 130  ? 17.060  -1.871  13.653  1.00 144.55 ? 130  THR A OG1 1 
ATOM   869   C  CG2 . THR A 1 130  ? 15.874  0.208   13.942  1.00 145.66 ? 130  THR A CG2 1 
ATOM   870   N  N   . ASP A 1 131  ? 15.200  -4.021  14.714  1.00 183.98 ? 131  ASP A N   1 
ATOM   871   C  CA  . ASP A 1 131  ? 15.207  -4.836  15.926  1.00 185.73 ? 131  ASP A CA  1 
ATOM   872   C  C   . ASP A 1 131  ? 16.203  -4.275  16.935  1.00 187.66 ? 131  ASP A C   1 
ATOM   873   O  O   . ASP A 1 131  ? 15.837  -3.943  18.063  1.00 189.86 ? 131  ASP A O   1 
ATOM   874   C  CB  . ASP A 1 131  ? 15.577  -6.278  15.629  1.00 186.30 ? 131  ASP A CB  1 
ATOM   875   C  CG  . ASP A 1 131  ? 17.035  -6.542  15.873  1.00 185.97 ? 131  ASP A CG  1 
ATOM   876   O  OD1 . ASP A 1 131  ? 17.840  -6.000  15.102  1.00 183.75 ? 131  ASP A OD1 1 
ATOM   877   O  OD2 . ASP A 1 131  ? 17.384  -7.241  16.845  1.00 188.39 ? 131  ASP A OD2 1 
ATOM   878   N  N   . LYS A 1 132  ? 17.467  -4.190  16.522  1.00 147.85 ? 132  LYS A N   1 
ATOM   879   C  CA  . LYS A 1 132  ? 18.532  -3.560  17.306  1.00 147.53 ? 132  LYS A CA  1 
ATOM   880   C  C   . LYS A 1 132  ? 19.205  -2.519  16.424  1.00 145.64 ? 132  LYS A C   1 
ATOM   881   O  O   . LYS A 1 132  ? 18.982  -2.523  15.221  1.00 144.51 ? 132  LYS A O   1 
ATOM   882   C  CB  . LYS A 1 132  ? 19.526  -4.589  17.854  1.00 158.09 ? 132  LYS A CB  1 
ATOM   883   C  CG  . LYS A 1 132  ? 20.354  -5.335  16.840  1.00 151.48 ? 132  LYS A CG  1 
ATOM   884   C  CD  . LYS A 1 132  ? 20.615  -6.756  17.324  1.00 148.53 ? 132  LYS A CD  1 
ATOM   885   C  CE  . LYS A 1 132  ? 21.751  -7.443  16.570  1.00 145.76 ? 132  LYS A CE  1 
ATOM   886   N  NZ  . LYS A 1 132  ? 21.712  -8.925  16.781  1.00 151.79 ? 132  LYS A NZ  1 
ATOM   887   N  N   . PRO A 1 133  ? 19.983  -1.596  17.011  1.00 145.44 ? 133  PRO A N   1 
ATOM   888   C  CA  . PRO A 1 133  ? 20.410  -0.393  16.321  1.00 144.09 ? 133  PRO A CA  1 
ATOM   889   C  C   . PRO A 1 133  ? 21.893  -0.425  16.256  1.00 142.74 ? 133  PRO A C   1 
ATOM   890   O  O   . PRO A 1 133  ? 22.529  0.618   16.372  1.00 142.25 ? 133  PRO A O   1 
ATOM   891   C  CB  . PRO A 1 133  ? 20.043  0.692   17.305  1.00 145.46 ? 133  PRO A CB  1 
ATOM   892   C  CG  . PRO A 1 133  ? 20.264  -0.004  18.658  1.00 146.98 ? 133  PRO A CG  1 
ATOM   893   C  CD  . PRO A 1 133  ? 20.428  -1.508  18.393  1.00 146.66 ? 133  PRO A CD  1 
ATOM   894   N  N   . VAL A 1 134  ? 22.424  -1.633  16.138  1.00 157.38 ? 134  VAL A N   1 
ATOM   895   C  CA  . VAL A 1 134  ? 23.780  -1.822  15.652  1.00 152.88 ? 134  VAL A CA  1 
ATOM   896   C  C   . VAL A 1 134  ? 24.130  -3.267  15.253  1.00 158.47 ? 134  VAL A C   1 
ATOM   897   O  O   . VAL A 1 134  ? 23.789  -4.242  15.944  1.00 165.08 ? 134  VAL A O   1 
ATOM   898   C  CB  . VAL A 1 134  ? 24.826  -1.191  16.585  1.00 154.35 ? 134  VAL A CB  1 
ATOM   899   C  CG1 . VAL A 1 134  ? 26.137  -1.934  16.488  1.00 154.22 ? 134  VAL A CG1 1 
ATOM   900   C  CG2 . VAL A 1 134  ? 25.025  0.267   16.219  1.00 151.29 ? 134  VAL A CG2 1 
ATOM   901   N  N   . TYR A 1 135  ? 24.809  -3.377  14.110  1.00 147.98 ? 135  TYR A N   1 
ATOM   902   C  CA  . TYR A 1 135  ? 25.123  -4.661  13.526  1.00 147.68 ? 135  TYR A CA  1 
ATOM   903   C  C   . TYR A 1 135  ? 26.572  -4.773  13.100  1.00 145.34 ? 135  TYR A C   1 
ATOM   904   O  O   . TYR A 1 135  ? 27.249  -3.792  12.797  1.00 145.07 ? 135  TYR A O   1 
ATOM   905   C  CB  . TYR A 1 135  ? 24.227  -4.916  12.325  1.00 147.76 ? 135  TYR A CB  1 
ATOM   906   C  CG  . TYR A 1 135  ? 22.758  -4.842  12.623  1.00 149.35 ? 135  TYR A CG  1 
ATOM   907   C  CD1 . TYR A 1 135  ? 21.998  -5.995  12.794  1.00 152.68 ? 135  TYR A CD1 1 
ATOM   908   C  CD2 . TYR A 1 135  ? 22.129  -3.621  12.727  1.00 147.70 ? 135  TYR A CD2 1 
ATOM   909   C  CE1 . TYR A 1 135  ? 20.642  -5.928  13.063  1.00 154.31 ? 135  TYR A CE1 1 
ATOM   910   C  CE2 . TYR A 1 135  ? 20.783  -3.537  13.000  1.00 149.33 ? 135  TYR A CE2 1 
ATOM   911   C  CZ  . TYR A 1 135  ? 20.033  -4.688  13.170  1.00 152.62 ? 135  TYR A CZ  1 
ATOM   912   O  OH  . TYR A 1 135  ? 18.676  -4.570  13.447  1.00 154.37 ? 135  TYR A OH  1 
ATOM   913   N  N   . THR A 1 136  ? 27.019  -6.011  13.081  1.00 157.93 ? 136  THR A N   1 
ATOM   914   C  CA  . THR A 1 136  ? 28.356  -6.352  12.685  1.00 158.10 ? 136  THR A CA  1 
ATOM   915   C  C   . THR A 1 136  ? 28.236  -7.232  11.445  1.00 150.27 ? 136  THR A C   1 
ATOM   916   O  O   . THR A 1 136  ? 27.170  -7.804  11.195  1.00 161.38 ? 136  THR A O   1 
ATOM   917   C  CB  . THR A 1 136  ? 29.001  -7.132  13.803  1.00 151.12 ? 136  THR A CB  1 
ATOM   918   O  OG1 . THR A 1 136  ? 28.093  -8.154  14.230  1.00 154.82 ? 136  THR A OG1 1 
ATOM   919   C  CG2 . THR A 1 136  ? 29.269  -6.208  14.989  1.00 160.45 ? 136  THR A CG2 1 
ATOM   920   N  N   . PRO A 1 137  ? 29.323  -7.361  10.661  1.00 161.32 ? 137  PRO A N   1 
ATOM   921   C  CA  . PRO A 1 137  ? 29.226  -8.078  9.389   1.00 159.61 ? 137  PRO A CA  1 
ATOM   922   C  C   . PRO A 1 137  ? 28.384  -9.348  9.468   1.00 163.56 ? 137  PRO A C   1 
ATOM   923   O  O   . PRO A 1 137  ? 28.596  -10.191 10.340  1.00 165.26 ? 137  PRO A O   1 
ATOM   924   C  CB  . PRO A 1 137  ? 30.677  -8.460  9.107   1.00 161.67 ? 137  PRO A CB  1 
ATOM   925   C  CG  . PRO A 1 137  ? 31.464  -7.390  9.731   1.00 156.45 ? 137  PRO A CG  1 
ATOM   926   C  CD  . PRO A 1 137  ? 30.711  -6.973  10.959  1.00 158.20 ? 137  PRO A CD  1 
ATOM   927   N  N   . ASP A 1 138  ? 27.432  -9.469  8.556   1.00 179.51 ? 138  ASP A N   1 
ATOM   928   C  CA  . ASP A 1 138  ? 26.778  -10.743 8.299   1.00 183.65 ? 138  ASP A CA  1 
ATOM   929   C  C   . ASP A 1 138  ? 25.587  -11.040 9.190   1.00 189.36 ? 138  ASP A C   1 
ATOM   930   O  O   . ASP A 1 138  ? 24.997  -12.113 9.110   1.00 192.31 ? 138  ASP A O   1 
ATOM   931   C  CB  . ASP A 1 138  ? 27.785  -11.899 8.352   1.00 196.41 ? 138  ASP A CB  1 
ATOM   932   C  CG  . ASP A 1 138  ? 28.590  -12.037 7.064   1.00 200.57 ? 138  ASP A CG  1 
ATOM   933   O  OD1 . ASP A 1 138  ? 27.966  -12.152 5.986   1.00 202.64 ? 138  ASP A OD1 1 
ATOM   934   O  OD2 . ASP A 1 138  ? 29.841  -12.038 7.132   1.00 199.75 ? 138  ASP A OD2 1 
ATOM   935   N  N   . GLN A 1 139  ? 25.210  -10.107 10.039  1.00 153.12 ? 139  GLN A N   1 
ATOM   936   C  CA  . GLN A 1 139  ? 23.988  -10.340 10.774  1.00 155.64 ? 139  GLN A CA  1 
ATOM   937   C  C   . GLN A 1 139  ? 22.815  -10.112 9.825   1.00 158.50 ? 139  GLN A C   1 
ATOM   938   O  O   . GLN A 1 139  ? 22.981  -9.501  8.772   1.00 156.96 ? 139  GLN A O   1 
ATOM   939   C  CB  . GLN A 1 139  ? 23.906  -9.438  12.016  1.00 155.92 ? 139  GLN A CB  1 
ATOM   940   C  CG  . GLN A 1 139  ? 24.970  -9.691  13.117  1.00 155.83 ? 139  GLN A CG  1 
ATOM   941   C  CD  . GLN A 1 139  ? 24.642  -8.979  14.431  1.00 155.88 ? 139  GLN A CD  1 
ATOM   942   O  OE1 . GLN A 1 139  ? 25.143  -7.884  14.713  1.00 151.00 ? 139  GLN A OE1 1 
ATOM   943   N  NE2 . GLN A 1 139  ? 23.781  -9.599  15.231  1.00 160.05 ? 139  GLN A NE2 1 
ATOM   944   N  N   . SER A 1 140  ? 21.645  -10.636 10.176  1.00 169.15 ? 140  SER A N   1 
ATOM   945   C  CA  . SER A 1 140  ? 20.419  -10.287 9.465   1.00 170.61 ? 140  SER A CA  1 
ATOM   946   C  C   . SER A 1 140  ? 19.598  -9.257  10.261  1.00 166.98 ? 140  SER A C   1 
ATOM   947   O  O   . SER A 1 140  ? 19.046  -9.560  11.322  1.00 168.01 ? 140  SER A O   1 
ATOM   948   C  CB  . SER A 1 140  ? 19.587  -11.540 9.150   1.00 175.32 ? 140  SER A CB  1 
ATOM   949   O  OG  . SER A 1 140  ? 18.916  -11.425 7.902   1.00 175.71 ? 140  SER A OG  1 
ATOM   950   N  N   . VAL A 1 141  ? 19.539  -8.036  9.738   1.00 146.01 ? 141  VAL A N   1 
ATOM   951   C  CA  . VAL A 1 141  ? 18.705  -6.967  10.279  1.00 141.34 ? 141  VAL A CA  1 
ATOM   952   C  C   . VAL A 1 141  ? 17.210  -7.319  10.291  1.00 145.44 ? 141  VAL A C   1 
ATOM   953   O  O   . VAL A 1 141  ? 16.508  -7.068  9.316   1.00 145.10 ? 141  VAL A O   1 
ATOM   954   C  CB  . VAL A 1 141  ? 18.888  -5.670  9.436   1.00 143.33 ? 141  VAL A CB  1 
ATOM   955   C  CG1 . VAL A 1 141  ? 17.908  -4.581  9.854   1.00 141.35 ? 141  VAL A CG1 1 
ATOM   956   C  CG2 . VAL A 1 141  ? 20.302  -5.172  9.534   1.00 139.52 ? 141  VAL A CG2 1 
ATOM   957   N  N   . LYS A 1 142  ? 16.712  -7.904  11.376  1.00 166.45 ? 142  LYS A N   1 
ATOM   958   C  CA  . LYS A 1 142  ? 15.264  -8.007  11.525  1.00 171.57 ? 142  LYS A CA  1 
ATOM   959   C  C   . LYS A 1 142  ? 14.681  -6.598  11.491  1.00 172.58 ? 142  LYS A C   1 
ATOM   960   O  O   . LYS A 1 142  ? 15.298  -5.649  11.970  1.00 172.79 ? 142  LYS A O   1 
ATOM   961   C  CB  . LYS A 1 142  ? 14.871  -8.715  12.822  1.00 172.44 ? 142  LYS A CB  1 
ATOM   962   C  CG  . LYS A 1 142  ? 14.840  -10.230 12.718  1.00 176.45 ? 142  LYS A CG  1 
ATOM   963   C  CD  . LYS A 1 142  ? 13.841  -10.852 13.690  1.00 179.73 ? 142  LYS A CD  1 
ATOM   964   C  CE  . LYS A 1 142  ? 13.822  -12.358 13.537  1.00 183.67 ? 142  LYS A CE  1 
ATOM   965   N  NZ  . LYS A 1 142  ? 15.217  -12.855 13.377  1.00 183.22 ? 142  LYS A NZ  1 
ATOM   966   N  N   . VAL A 1 143  ? 13.504  -6.450  10.906  1.00 154.06 ? 143  VAL A N   1 
ATOM   967   C  CA  . VAL A 1 143  ? 12.858  -5.153  10.914  1.00 151.22 ? 143  VAL A CA  1 
ATOM   968   C  C   . VAL A 1 143  ? 11.424  -5.275  10.480  1.00 150.54 ? 143  VAL A C   1 
ATOM   969   O  O   . VAL A 1 143  ? 11.080  -6.151  9.699   1.00 153.29 ? 143  VAL A O   1 
ATOM   970   C  CB  . VAL A 1 143  ? 13.583  -4.155  10.010  1.00 150.37 ? 143  VAL A CB  1 
ATOM   971   C  CG1 . VAL A 1 143  ? 14.020  -4.845  8.766   1.00 146.06 ? 143  VAL A CG1 1 
ATOM   972   C  CG2 . VAL A 1 143  ? 12.679  -2.980  9.690   1.00 146.18 ? 143  VAL A CG2 1 
ATOM   973   N  N   . ARG A 1 144  ? 10.585  -4.405  11.018  1.00 149.86 ? 144  ARG A N   1 
ATOM   974   C  CA  . ARG A 1 144  ? 9.228   -4.299  10.543  1.00 151.05 ? 144  ARG A CA  1 
ATOM   975   C  C   . ARG A 1 144  ? 8.781   -2.844  10.519  1.00 151.05 ? 144  ARG A C   1 
ATOM   976   O  O   . ARG A 1 144  ? 9.600   -1.932  10.625  1.00 149.80 ? 144  ARG A O   1 
ATOM   977   C  CB  . ARG A 1 144  ? 8.282   -5.158  11.374  1.00 155.07 ? 144  ARG A CB  1 
ATOM   978   C  CG  . ARG A 1 144  ? 8.707   -5.407  12.794  1.00 156.81 ? 144  ARG A CG  1 
ATOM   979   C  CD  . ARG A 1 144  ? 7.538   -6.026  13.566  1.00 161.25 ? 144  ARG A CD  1 
ATOM   980   N  NE  . ARG A 1 144  ? 7.724   -6.057  15.016  1.00 162.66 ? 144  ARG A NE  1 
ATOM   981   C  CZ  . ARG A 1 144  ? 7.834   -7.173  15.730  1.00 166.53 ? 144  ARG A CZ  1 
ATOM   982   N  NH1 . ARG A 1 144  ? 7.773   -8.352  15.134  1.00 168.52 ? 144  ARG A NH1 1 
ATOM   983   N  NH2 . ARG A 1 144  ? 7.999   -7.113  17.040  1.00 167.70 ? 144  ARG A NH2 1 
ATOM   984   N  N   . VAL A 1 145  ? 7.478   -2.636  10.368  1.00 152.52 ? 145  VAL A N   1 
ATOM   985   C  CA  . VAL A 1 145  ? 6.923   -1.296  10.337  1.00 152.76 ? 145  VAL A CA  1 
ATOM   986   C  C   . VAL A 1 145  ? 5.493   -1.221  10.842  1.00 155.23 ? 145  VAL A C   1 
ATOM   987   O  O   . VAL A 1 145  ? 4.617   -2.008  10.457  1.00 156.34 ? 145  VAL A O   1 
ATOM   988   C  CB  . VAL A 1 145  ? 7.015   -0.664  8.960   1.00 151.01 ? 145  VAL A CB  1 
ATOM   989   C  CG1 . VAL A 1 145  ? 5.959   0.403   8.800   1.00 151.92 ? 145  VAL A CG1 1 
ATOM   990   C  CG2 . VAL A 1 145  ? 8.377   -0.065  8.783   1.00 148.88 ? 145  VAL A CG2 1 
ATOM   991   N  N   . TYR A 1 146  ? 5.291   -0.268  11.746  1.00 171.40 ? 146  TYR A N   1 
ATOM   992   C  CA  . TYR A 1 146  ? 3.972   0.065   12.245  1.00 173.85 ? 146  TYR A CA  1 
ATOM   993   C  C   . TYR A 1 146  ? 3.537   1.307   11.504  1.00 176.31 ? 146  TYR A C   1 
ATOM   994   O  O   . TYR A 1 146  ? 4.340   2.217   11.290  1.00 175.10 ? 146  TYR A O   1 
ATOM   995   C  CB  . TYR A 1 146  ? 4.036   0.316   13.746  1.00 177.60 ? 146  TYR A CB  1 
ATOM   996   C  CG  . TYR A 1 146  ? 4.848   -0.740  14.427  1.00 176.26 ? 146  TYR A CG  1 
ATOM   997   C  CD1 . TYR A 1 146  ? 4.485   -2.075  14.341  1.00 180.88 ? 146  TYR A CD1 1 
ATOM   998   C  CD2 . TYR A 1 146  ? 5.994   -0.419  15.118  1.00 176.23 ? 146  TYR A CD2 1 
ATOM   999   C  CE1 . TYR A 1 146  ? 5.234   -3.063  14.942  1.00 181.13 ? 146  TYR A CE1 1 
ATOM   1000  C  CE2 . TYR A 1 146  ? 6.748   -1.400  15.730  1.00 175.56 ? 146  TYR A CE2 1 
ATOM   1001  C  CZ  . TYR A 1 146  ? 6.365   -2.722  15.639  1.00 177.52 ? 146  TYR A CZ  1 
ATOM   1002  O  OH  . TYR A 1 146  ? 7.116   -3.704  16.248  1.00 175.96 ? 146  TYR A OH  1 
ATOM   1003  N  N   . SER A 1 147  ? 2.272   1.342   11.101  1.00 191.65 ? 147  SER A N   1 
ATOM   1004  C  CA  . SER A 1 147  ? 1.785   2.433   10.267  1.00 194.07 ? 147  SER A CA  1 
ATOM   1005  C  C   . SER A 1 147  ? 0.370   2.841   10.633  1.00 198.29 ? 147  SER A C   1 
ATOM   1006  O  O   . SER A 1 147  ? -0.532  2.006   10.731  1.00 201.70 ? 147  SER A O   1 
ATOM   1007  C  CB  . SER A 1 147  ? 1.841   2.044   8.795   1.00 196.16 ? 147  SER A CB  1 
ATOM   1008  O  OG  . SER A 1 147  ? 0.869   1.061   8.494   1.00 200.89 ? 147  SER A OG  1 
ATOM   1009  N  N   . LEU A 1 148  ? 0.192   4.139   10.830  1.00 235.38 ? 148  LEU A N   1 
ATOM   1010  C  CA  . LEU A 1 148  ? -1.085  4.681   11.237  1.00 238.01 ? 148  LEU A CA  1 
ATOM   1011  C  C   . LEU A 1 148  ? -1.509  5.773   10.297  1.00 243.94 ? 148  LEU A C   1 
ATOM   1012  O  O   . LEU A 1 148  ? -0.681  6.393   9.640   1.00 245.29 ? 148  LEU A O   1 
ATOM   1013  C  CB  . LEU A 1 148  ? -0.997  5.253   12.643  1.00 236.02 ? 148  LEU A CB  1 
ATOM   1014  C  CG  . LEU A 1 148  ? -1.612  4.342   13.692  1.00 237.04 ? 148  LEU A CG  1 
ATOM   1015  C  CD1 . LEU A 1 148  ? -1.149  2.923   13.447  1.00 236.23 ? 148  LEU A CD1 1 
ATOM   1016  C  CD2 . LEU A 1 148  ? -1.240  4.802   15.086  1.00 236.90 ? 148  LEU A CD2 1 
ATOM   1017  N  N   . ASN A 1 149  ? -2.814  5.992   10.234  1.00 233.08 ? 149  ASN A N   1 
ATOM   1018  C  CA  . ASN A 1 149  ? -3.375  7.114   9.507   1.00 232.61 ? 149  ASN A CA  1 
ATOM   1019  C  C   . ASN A 1 149  ? -3.641  8.255   10.473  1.00 231.19 ? 149  ASN A C   1 
ATOM   1020  O  O   . ASN A 1 149  ? -3.691  8.049   11.677  1.00 229.73 ? 149  ASN A O   1 
ATOM   1021  C  CB  . ASN A 1 149  ? -4.667  6.697   8.811   1.00 239.61 ? 149  ASN A CB  1 
ATOM   1022  C  CG  . ASN A 1 149  ? -5.676  6.111   9.770   1.00 246.43 ? 149  ASN A CG  1 
ATOM   1023  O  OD1 . ASN A 1 149  ? -5.323  5.593   10.830  1.00 246.33 ? 149  ASN A OD1 1 
ATOM   1024  N  ND2 . ASN A 1 149  ? -6.941  6.180   9.400   1.00 252.00 ? 149  ASN A ND2 1 
ATOM   1025  N  N   . ASP A 1 150  ? -3.782  9.456   9.937   1.00 194.44 ? 150  ASP A N   1 
ATOM   1026  C  CA  . ASP A 1 150  ? -4.232  10.600  10.696  1.00 197.78 ? 150  ASP A CA  1 
ATOM   1027  C  C   . ASP A 1 150  ? -5.093  10.210  11.881  1.00 197.98 ? 150  ASP A C   1 
ATOM   1028  O  O   . ASP A 1 150  ? -4.952  10.798  12.936  1.00 198.02 ? 150  ASP A O   1 
ATOM   1029  C  CB  . ASP A 1 150  ? -5.096  11.446  9.801   1.00 200.48 ? 150  ASP A CB  1 
ATOM   1030  C  CG  . ASP A 1 150  ? -6.199  10.625  9.144   1.00 218.67 ? 150  ASP A CG  1 
ATOM   1031  O  OD1 . ASP A 1 150  ? -7.357  11.106  9.065   1.00 220.28 ? 150  ASP A OD1 1 
ATOM   1032  O  OD2 . ASP A 1 150  ? -5.906  9.475   8.732   1.00 220.32 ? 150  ASP A OD2 1 
ATOM   1033  N  N   . ASP A 1 151  ? -6.007  9.253   11.715  1.00 242.49 ? 151  ASP A N   1 
ATOM   1034  C  CA  . ASP A 1 151  ? -6.937  8.881   12.800  1.00 249.36 ? 151  ASP A CA  1 
ATOM   1035  C  C   . ASP A 1 151  ? -6.341  7.856   13.779  1.00 247.66 ? 151  ASP A C   1 
ATOM   1036  O  O   . ASP A 1 151  ? -7.045  7.299   14.623  1.00 251.88 ? 151  ASP A O   1 
ATOM   1037  C  CB  . ASP A 1 151  ? -8.270  8.354   12.236  1.00 257.05 ? 151  ASP A CB  1 
ATOM   1038  C  CG  . ASP A 1 151  ? -9.460  9.288   12.510  1.00 262.97 ? 151  ASP A CG  1 
ATOM   1039  O  OD1 . ASP A 1 151  ? -9.353  10.204  13.358  1.00 267.10 ? 151  ASP A OD1 1 
ATOM   1040  O  OD2 . ASP A 1 151  ? -10.518 9.091   11.870  1.00 262.91 ? 151  ASP A OD2 1 
ATOM   1041  N  N   . LEU A 1 152  ? -5.043  7.606   13.648  1.00 190.20 ? 152  LEU A N   1 
ATOM   1042  C  CA  . LEU A 1 152  ? -4.329  6.684   14.526  1.00 191.78 ? 152  LEU A CA  1 
ATOM   1043  C  C   . LEU A 1 152  ? -5.076  5.343   14.669  1.00 197.09 ? 152  LEU A C   1 
ATOM   1044  O  O   . LEU A 1 152  ? -5.311  4.843   15.776  1.00 197.78 ? 152  LEU A O   1 
ATOM   1045  C  CB  . LEU A 1 152  ? -4.002  7.350   15.875  1.00 192.03 ? 152  LEU A CB  1 
ATOM   1046  C  CG  . LEU A 1 152  ? -3.072  8.585   15.909  1.00 190.51 ? 152  LEU A CG  1 
ATOM   1047  C  CD1 . LEU A 1 152  ? -1.897  8.457   14.952  1.00 186.56 ? 152  LEU A CD1 1 
ATOM   1048  C  CD2 . LEU A 1 152  ? -3.810  9.893   15.664  1.00 193.95 ? 152  LEU A CD2 1 
ATOM   1049  N  N   . LYS A 1 153  ? -5.458  4.789   13.518  1.00 224.07 ? 153  LYS A N   1 
ATOM   1050  C  CA  . LYS A 1 153  ? -6.009  3.437   13.425  1.00 226.63 ? 153  LYS A CA  1 
ATOM   1051  C  C   . LYS A 1 153  ? -5.218  2.623   12.399  1.00 225.88 ? 153  LYS A C   1 
ATOM   1052  O  O   . LYS A 1 153  ? -4.488  3.201   11.594  1.00 220.54 ? 153  LYS A O   1 
ATOM   1053  C  CB  . LYS A 1 153  ? -7.497  3.470   13.083  1.00 233.40 ? 153  LYS A CB  1 
ATOM   1054  C  CG  . LYS A 1 153  ? -8.389  3.441   14.308  1.00 237.08 ? 153  LYS A CG  1 
ATOM   1055  C  CD  . LYS A 1 153  ? -9.857  3.552   13.930  1.00 243.62 ? 153  LYS A CD  1 
ATOM   1056  C  CE  . LYS A 1 153  ? -10.768 3.434   15.153  1.00 248.48 ? 153  LYS A CE  1 
ATOM   1057  N  NZ  . LYS A 1 153  ? -10.493 4.456   16.212  1.00 247.69 ? 153  LYS A NZ  1 
ATOM   1058  N  N   . PRO A 1 154  ? -5.360  1.282   12.426  1.00 203.55 ? 154  PRO A N   1 
ATOM   1059  C  CA  . PRO A 1 154  ? -4.450  0.348   11.750  1.00 206.37 ? 154  PRO A CA  1 
ATOM   1060  C  C   . PRO A 1 154  ? -3.815  0.925   10.496  1.00 206.31 ? 154  PRO A C   1 
ATOM   1061  O  O   . PRO A 1 154  ? -2.607  0.775   10.299  1.00 205.37 ? 154  PRO A O   1 
ATOM   1062  C  CB  . PRO A 1 154  ? -5.364  -0.827  11.412  1.00 209.12 ? 154  PRO A CB  1 
ATOM   1063  C  CG  . PRO A 1 154  ? -6.310  -0.866  12.570  1.00 212.01 ? 154  PRO A CG  1 
ATOM   1064  C  CD  . PRO A 1 154  ? -6.509  0.572   13.017  1.00 209.55 ? 154  PRO A CD  1 
ATOM   1065  N  N   . ALA A 1 155  ? -4.633  1.582   9.678   1.00 311.71 ? 155  ALA A N   1 
ATOM   1066  C  CA  . ALA A 1 155  ? -4.182  2.305   8.491   1.00 311.71 ? 155  ALA A CA  1 
ATOM   1067  C  C   . ALA A 1 155  ? -3.727  1.366   7.376   1.00 315.60 ? 155  ALA A C   1 
ATOM   1068  O  O   . ALA A 1 155  ? -2.819  1.694   6.607   1.00 313.34 ? 155  ALA A O   1 
ATOM   1069  C  CB  . ALA A 1 155  ? -3.077  3.289   8.850   1.00 306.66 ? 155  ALA A CB  1 
ATOM   1070  N  N   . LYS A 1 156  ? -4.378  0.208   7.290   1.00 188.53 ? 156  LYS A N   1 
ATOM   1071  C  CA  . LYS A 1 156  ? -4.016  -0.816  6.326   1.00 188.76 ? 156  LYS A CA  1 
ATOM   1072  C  C   . LYS A 1 156  ? -3.623  -0.112  5.035   1.00 184.53 ? 156  LYS A C   1 
ATOM   1073  O  O   . LYS A 1 156  ? -4.248  0.874   4.654   1.00 185.27 ? 156  LYS A O   1 
ATOM   1074  C  CB  . LYS A 1 156  ? -5.185  -1.795  6.130   1.00 195.79 ? 156  LYS A CB  1 
ATOM   1075  C  CG  . LYS A 1 156  ? -5.580  -2.564  7.407   1.00 198.92 ? 156  LYS A CG  1 
ATOM   1076  C  CD  . LYS A 1 156  ? -7.054  -3.010  7.451   1.00 206.01 ? 156  LYS A CD  1 
ATOM   1077  C  CE  . LYS A 1 156  ? -7.409  -3.618  8.817   1.00 209.41 ? 156  LYS A CE  1 
ATOM   1078  N  NZ  . LYS A 1 156  ? -8.853  -3.952  8.999   1.00 216.14 ? 156  LYS A NZ  1 
ATOM   1079  N  N   . ARG A 1 157  ? -2.558  -0.586  4.397   1.00 223.23 ? 157  ARG A N   1 
ATOM   1080  C  CA  . ARG A 1 157  ? -2.094  -0.015  3.141   1.00 219.64 ? 157  ARG A CA  1 
ATOM   1081  C  C   . ARG A 1 157  ? -0.927  -0.811  2.590   1.00 220.07 ? 157  ARG A C   1 
ATOM   1082  O  O   . ARG A 1 157  ? -0.454  -1.749  3.222   1.00 220.62 ? 157  ARG A O   1 
ATOM   1083  C  CB  . ARG A 1 157  ? -1.653  1.436   3.336   1.00 211.01 ? 157  ARG A CB  1 
ATOM   1084  C  CG  . ARG A 1 157  ? -2.780  2.427   3.543   1.00 207.40 ? 157  ARG A CG  1 
ATOM   1085  C  CD  . ARG A 1 157  ? -2.254  3.822   3.669   1.00 199.93 ? 157  ARG A CD  1 
ATOM   1086  N  NE  . ARG A 1 157  ? -3.121  4.654   4.484   1.00 200.34 ? 157  ARG A NE  1 
ATOM   1087  C  CZ  . ARG A 1 157  ? -2.818  5.893   4.851   1.00 198.12 ? 157  ARG A CZ  1 
ATOM   1088  N  NH1 . ARG A 1 157  ? -1.666  6.437   4.470   1.00 193.52 ? 157  ARG A NH1 1 
ATOM   1089  N  NH2 . ARG A 1 157  ? -3.664  6.586   5.601   1.00 200.34 ? 157  ARG A NH2 1 
ATOM   1090  N  N   . GLU A 1 158  ? -0.470  -0.431  1.402   1.00 254.96 ? 158  GLU A N   1 
ATOM   1091  C  CA  . GLU A 1 158  ? 0.767   -0.977  0.856   1.00 254.64 ? 158  GLU A CA  1 
ATOM   1092  C  C   . GLU A 1 158  ? 1.904   0.033   0.964   1.00 248.56 ? 158  GLU A C   1 
ATOM   1093  O  O   . GLU A 1 158  ? 1.773   1.180   0.527   1.00 249.25 ? 158  GLU A O   1 
ATOM   1094  C  CB  . GLU A 1 158  ? 0.592   -1.414  -0.599  1.00 261.82 ? 158  GLU A CB  1 
ATOM   1095  C  CG  . GLU A 1 158  ? -0.116  -2.749  -0.761  1.00 270.26 ? 158  GLU A CG  1 
ATOM   1096  C  CD  . GLU A 1 158  ? 0.302   -3.478  -2.026  1.00 276.23 ? 158  GLU A CD  1 
ATOM   1097  O  OE1 . GLU A 1 158  ? 1.518   -3.700  -2.206  1.00 275.46 ? 158  GLU A OE1 1 
ATOM   1098  O  OE2 . GLU A 1 158  ? -0.581  -3.831  -2.838  1.00 281.56 ? 158  GLU A OE2 1 
ATOM   1099  N  N   . THR A 1 159  ? 3.022   -0.404  1.539   1.00 178.67 ? 159  THR A N   1 
ATOM   1100  C  CA  . THR A 1 159  ? 4.168   0.464   1.755   1.00 168.75 ? 159  THR A CA  1 
ATOM   1101  C  C   . THR A 1 159  ? 5.433   -0.182  1.258   1.00 158.46 ? 159  THR A C   1 
ATOM   1102  O  O   . THR A 1 159  ? 5.504   -1.403  1.078   1.00 158.52 ? 159  THR A O   1 
ATOM   1103  C  CB  . THR A 1 159  ? 4.420   0.732   3.251   1.00 170.67 ? 159  THR A CB  1 
ATOM   1104  O  OG1 . THR A 1 159  ? 3.200   1.087   3.924   1.00 173.59 ? 159  THR A OG1 1 
ATOM   1105  C  CG2 . THR A 1 159  ? 5.434   1.842   3.411   1.00 168.00 ? 159  THR A CG2 1 
ATOM   1106  N  N   . VAL A 1 160  ? 6.437   0.666   1.066   1.00 145.78 ? 160  VAL A N   1 
ATOM   1107  C  CA  . VAL A 1 160  ? 7.783   0.247   0.688   1.00 143.62 ? 160  VAL A CA  1 
ATOM   1108  C  C   . VAL A 1 160  ? 8.812   1.060   1.439   1.00 142.61 ? 160  VAL A C   1 
ATOM   1109  O  O   . VAL A 1 160  ? 8.685   2.288   1.577   1.00 146.42 ? 160  VAL A O   1 
ATOM   1110  C  CB  . VAL A 1 160  ? 8.128   0.543   -0.791  1.00 142.08 ? 160  VAL A CB  1 
ATOM   1111  C  CG1 . VAL A 1 160  ? 9.485   1.249   -0.893  1.00 140.17 ? 160  VAL A CG1 1 
ATOM   1112  C  CG2 . VAL A 1 160  ? 8.168   -0.714  -1.611  1.00 142.83 ? 160  VAL A CG2 1 
ATOM   1113  N  N   . LEU A 1 161  ? 9.852   0.360   1.880   1.00 177.14 ? 161  LEU A N   1 
ATOM   1114  C  CA  . LEU A 1 161  ? 11.092  0.980   2.302   1.00 174.28 ? 161  LEU A CA  1 
ATOM   1115  C  C   . LEU A 1 161  ? 12.203  0.826   1.257   1.00 174.14 ? 161  LEU A C   1 
ATOM   1116  O  O   . LEU A 1 161  ? 12.042  0.170   0.220   1.00 176.20 ? 161  LEU A O   1 
ATOM   1117  C  CB  . LEU A 1 161  ? 11.535  0.395   3.632   1.00 173.06 ? 161  LEU A CB  1 
ATOM   1118  C  CG  . LEU A 1 161  ? 10.964  -0.986  3.896   1.00 174.23 ? 161  LEU A CG  1 
ATOM   1119  C  CD1 . LEU A 1 161  ? 11.887  -2.106  3.392   1.00 174.91 ? 161  LEU A CD1 1 
ATOM   1120  C  CD2 . LEU A 1 161  ? 10.728  -1.094  5.369   1.00 172.80 ? 161  LEU A CD2 1 
ATOM   1121  N  N   . THR A 1 162  ? 13.346  1.414   1.579   1.00 195.19 ? 162  THR A N   1 
ATOM   1122  C  CA  . THR A 1 162  ? 14.407  1.608   0.620   1.00 191.78 ? 162  THR A CA  1 
ATOM   1123  C  C   . THR A 1 162  ? 15.754  1.851   1.323   1.00 188.33 ? 162  THR A C   1 
ATOM   1124  O  O   . THR A 1 162  ? 16.206  2.992   1.425   1.00 185.74 ? 162  THR A O   1 
ATOM   1125  C  CB  . THR A 1 162  ? 14.028  2.772   -0.326  1.00 213.35 ? 162  THR A CB  1 
ATOM   1126  O  OG1 . THR A 1 162  ? 15.079  3.740   -0.395  1.00 209.98 ? 162  THR A OG1 1 
ATOM   1127  C  CG2 . THR A 1 162  ? 12.768  3.472   0.170   1.00 212.20 ? 162  THR A CG2 1 
ATOM   1128  N  N   . PHE A 1 163  ? 16.390  0.769   1.795   1.00 189.55 ? 163  PHE A N   1 
ATOM   1129  C  CA  . PHE A 1 163  ? 17.653  0.843   2.558   1.00 186.30 ? 163  PHE A CA  1 
ATOM   1130  C  C   . PHE A 1 163  ? 18.658  1.676   1.798   1.00 184.00 ? 163  PHE A C   1 
ATOM   1131  O  O   . PHE A 1 163  ? 18.594  1.740   0.583   1.00 185.50 ? 163  PHE A O   1 
ATOM   1132  C  CB  . PHE A 1 163  ? 18.249  -0.540  2.802   1.00 187.79 ? 163  PHE A CB  1 
ATOM   1133  C  CG  . PHE A 1 163  ? 17.297  -1.506  3.426   1.00 190.25 ? 163  PHE A CG  1 
ATOM   1134  C  CD1 . PHE A 1 163  ? 16.042  -1.710  2.884   1.00 193.62 ? 163  PHE A CD1 1 
ATOM   1135  C  CD2 . PHE A 1 163  ? 17.659  -2.235  4.533   1.00 188.91 ? 163  PHE A CD2 1 
ATOM   1136  C  CE1 . PHE A 1 163  ? 15.160  -2.607  3.449   1.00 197.98 ? 163  PHE A CE1 1 
ATOM   1137  C  CE2 . PHE A 1 163  ? 16.778  -3.132  5.098   1.00 192.41 ? 163  PHE A CE2 1 
ATOM   1138  C  CZ  . PHE A 1 163  ? 15.528  -3.318  4.552   1.00 197.42 ? 163  PHE A CZ  1 
ATOM   1139  N  N   . ILE A 1 164  ? 19.596  2.299   2.497   1.00 156.13 ? 164  ILE A N   1 
ATOM   1140  C  CA  . ILE A 1 164  ? 20.499  3.249   1.857   1.00 156.80 ? 164  ILE A CA  1 
ATOM   1141  C  C   . ILE A 1 164  ? 21.889  3.248   2.475   1.00 157.36 ? 164  ILE A C   1 
ATOM   1142  O  O   . ILE A 1 164  ? 22.131  3.899   3.479   1.00 155.44 ? 164  ILE A O   1 
ATOM   1143  C  CB  . ILE A 1 164  ? 19.928  4.680   1.910   1.00 159.05 ? 164  ILE A CB  1 
ATOM   1144  C  CG1 . ILE A 1 164  ? 18.626  4.776   1.102   1.00 162.85 ? 164  ILE A CG1 1 
ATOM   1145  C  CG2 . ILE A 1 164  ? 20.952  5.689   1.408   1.00 157.70 ? 164  ILE A CG2 1 
ATOM   1146  C  CD1 . ILE A 1 164  ? 18.037  6.181   1.032   1.00 161.93 ? 164  ILE A CD1 1 
ATOM   1147  N  N   . ASP A 1 165  ? 22.811  2.534   1.843   1.00 198.17 ? 165  ASP A N   1 
ATOM   1148  C  CA  . ASP A 1 165  ? 24.161  2.376   2.369   1.00 200.73 ? 165  ASP A CA  1 
ATOM   1149  C  C   . ASP A 1 165  ? 24.740  3.666   2.914   1.00 192.60 ? 165  ASP A C   1 
ATOM   1150  O  O   . ASP A 1 165  ? 24.315  4.757   2.542   1.00 188.28 ? 165  ASP A O   1 
ATOM   1151  C  CB  . ASP A 1 165  ? 25.101  1.750   1.326   1.00 210.21 ? 165  ASP A CB  1 
ATOM   1152  C  CG  . ASP A 1 165  ? 25.695  2.768   0.368   1.00 217.66 ? 165  ASP A CG  1 
ATOM   1153  O  OD1 . ASP A 1 165  ? 25.484  3.991   0.541   1.00 219.37 ? 165  ASP A OD1 1 
ATOM   1154  O  OD2 . ASP A 1 165  ? 26.382  2.323   -0.574  1.00 220.60 ? 165  ASP A OD2 1 
ATOM   1155  N  N   . PRO A 1 166  ? 25.712  3.527   3.812   1.00 175.14 ? 166  PRO A N   1 
ATOM   1156  C  CA  . PRO A 1 166  ? 26.378  4.591   4.572   1.00 172.47 ? 166  PRO A CA  1 
ATOM   1157  C  C   . PRO A 1 166  ? 27.033  5.722   3.741   1.00 168.70 ? 166  PRO A C   1 
ATOM   1158  O  O   . PRO A 1 166  ? 27.772  6.540   4.283   1.00 165.76 ? 166  PRO A O   1 
ATOM   1159  C  CB  . PRO A 1 166  ? 27.408  3.817   5.406   1.00 175.00 ? 166  PRO A CB  1 
ATOM   1160  C  CG  . PRO A 1 166  ? 26.779  2.447   5.589   1.00 179.00 ? 166  PRO A CG  1 
ATOM   1161  C  CD  . PRO A 1 166  ? 26.043  2.182   4.318   1.00 179.08 ? 166  PRO A CD  1 
ATOM   1162  N  N   . GLU A 1 167  ? 26.751  5.788   2.449   1.00 183.85 ? 167  GLU A N   1 
ATOM   1163  C  CA  . GLU A 1 167  ? 27.274  6.881   1.639   1.00 183.88 ? 167  GLU A CA  1 
ATOM   1164  C  C   . GLU A 1 167  ? 26.128  7.574   0.931   1.00 184.46 ? 167  GLU A C   1 
ATOM   1165  O  O   . GLU A 1 167  ? 26.273  8.695   0.447   1.00 185.21 ? 167  GLU A O   1 
ATOM   1166  C  CB  . GLU A 1 167  ? 28.319  6.382   0.631   1.00 187.39 ? 167  GLU A CB  1 
ATOM   1167  C  CG  . GLU A 1 167  ? 29.671  5.961   1.255   1.00 189.95 ? 167  GLU A CG  1 
ATOM   1168  C  CD  . GLU A 1 167  ? 30.718  5.426   0.242   1.00 194.78 ? 167  GLU A CD  1 
ATOM   1169  O  OE1 . GLU A 1 167  ? 31.216  6.206   -0.603  1.00 194.77 ? 167  GLU A OE1 1 
ATOM   1170  O  OE2 . GLU A 1 167  ? 31.065  4.223   0.317   1.00 197.75 ? 167  GLU A OE2 1 
ATOM   1171  N  N   . GLY A 1 168  ? 24.987  6.898   0.877   1.00 204.00 ? 168  GLY A N   1 
ATOM   1172  C  CA  . GLY A 1 168  ? 23.770  7.533   0.424   1.00 205.41 ? 168  GLY A CA  1 
ATOM   1173  C  C   . GLY A 1 168  ? 23.355  7.120   -0.965  1.00 210.44 ? 168  GLY A C   1 
ATOM   1174  O  O   . GLY A 1 168  ? 22.859  7.934   -1.738  1.00 210.86 ? 168  GLY A O   1 
ATOM   1175  N  N   . SER A 1 169  ? 23.562  5.850   -1.284  1.00 155.97 ? 169  SER A N   1 
ATOM   1176  C  CA  . SER A 1 169  ? 23.115  5.289   -2.557  1.00 162.23 ? 169  SER A CA  1 
ATOM   1177  C  C   . SER A 1 169  ? 22.191  4.089   -2.341  1.00 162.59 ? 169  SER A C   1 
ATOM   1178  O  O   . SER A 1 169  ? 22.601  3.112   -1.729  1.00 161.43 ? 169  SER A O   1 
ATOM   1179  C  CB  . SER A 1 169  ? 24.330  4.848   -3.365  1.00 166.65 ? 169  SER A CB  1 
ATOM   1180  O  OG  . SER A 1 169  ? 24.030  3.685   -4.116  1.00 172.09 ? 169  SER A OG  1 
ATOM   1181  N  N   . GLU A 1 170  ? 20.962  4.145   -2.847  1.00 150.05 ? 170  GLU A N   1 
ATOM   1182  C  CA  . GLU A 1 170  ? 20.006  3.064   -2.602  1.00 153.09 ? 170  GLU A CA  1 
ATOM   1183  C  C   . GLU A 1 170  ? 20.724  1.724   -2.593  1.00 149.89 ? 170  GLU A C   1 
ATOM   1184  O  O   . GLU A 1 170  ? 21.828  1.632   -3.091  1.00 154.44 ? 170  GLU A O   1 
ATOM   1185  C  CB  . GLU A 1 170  ? 18.921  3.038   -3.679  1.00 162.15 ? 170  GLU A CB  1 
ATOM   1186  C  CG  . GLU A 1 170  ? 17.968  4.240   -3.719  1.00 166.78 ? 170  GLU A CG  1 
ATOM   1187  C  CD  . GLU A 1 170  ? 16.720  3.974   -4.565  1.00 176.31 ? 170  GLU A CD  1 
ATOM   1188  O  OE1 . GLU A 1 170  ? 16.742  3.015   -5.372  1.00 181.67 ? 170  GLU A OE1 1 
ATOM   1189  O  OE2 . GLU A 1 170  ? 15.722  4.721   -4.419  1.00 178.18 ? 170  GLU A OE2 1 
ATOM   1190  N  N   . VAL A 1 171  ? 20.106  0.680   -2.055  1.00 143.05 ? 171  VAL A N   1 
ATOM   1191  C  CA  . VAL A 1 171  ? 20.741  -0.627  -2.098  1.00 145.16 ? 171  VAL A CA  1 
ATOM   1192  C  C   . VAL A 1 171  ? 19.738  -1.780  -2.212  1.00 145.66 ? 171  VAL A C   1 
ATOM   1193  O  O   . VAL A 1 171  ? 20.098  -2.909  -2.514  1.00 147.97 ? 171  VAL A O   1 
ATOM   1194  C  CB  . VAL A 1 171  ? 21.783  -0.817  -0.933  1.00 147.86 ? 171  VAL A CB  1 
ATOM   1195  C  CG1 . VAL A 1 171  ? 22.301  -2.251  -0.855  1.00 151.26 ? 171  VAL A CG1 1 
ATOM   1196  C  CG2 . VAL A 1 171  ? 22.959  0.124   -1.095  1.00 144.74 ? 171  VAL A CG2 1 
ATOM   1197  N  N   . ASP A 1 172  ? 18.466  -1.490  -2.034  1.00 168.95 ? 172  ASP A N   1 
ATOM   1198  C  CA  . ASP A 1 172  ? 17.478  -2.549  -2.115  1.00 174.23 ? 172  ASP A CA  1 
ATOM   1199  C  C   . ASP A 1 172  ? 16.138  -1.872  -2.224  1.00 175.40 ? 172  ASP A C   1 
ATOM   1200  O  O   . ASP A 1 172  ? 16.059  -0.757  -2.732  1.00 172.44 ? 172  ASP A O   1 
ATOM   1201  C  CB  . ASP A 1 172  ? 17.544  -3.410  -0.857  1.00 176.71 ? 172  ASP A CB  1 
ATOM   1202  C  CG  . ASP A 1 172  ? 16.831  -4.756  -0.998  1.00 184.27 ? 172  ASP A CG  1 
ATOM   1203  O  OD1 . ASP A 1 172  ? 17.444  -5.770  -0.600  1.00 185.36 ? 172  ASP A OD1 1 
ATOM   1204  O  OD2 . ASP A 1 172  ? 15.678  -4.817  -1.471  1.00 187.15 ? 172  ASP A OD2 1 
ATOM   1205  N  N   . MET A 1 173  ? 15.094  -2.528  -1.729  1.00 167.50 ? 173  MET A N   1 
ATOM   1206  C  CA  . MET A 1 173  ? 13.749  -1.992  -1.787  1.00 167.36 ? 173  MET A CA  1 
ATOM   1207  C  C   . MET A 1 173  ? 12.839  -3.151  -1.517  1.00 167.68 ? 173  MET A C   1 
ATOM   1208  O  O   . MET A 1 173  ? 13.281  -4.295  -1.504  1.00 170.61 ? 173  MET A O   1 
ATOM   1209  C  CB  . MET A 1 173  ? 13.471  -1.484  -3.194  1.00 170.33 ? 173  MET A CB  1 
ATOM   1210  C  CG  . MET A 1 173  ? 12.782  -0.155  -3.267  1.00 171.17 ? 173  MET A CG  1 
ATOM   1211  S  SD  . MET A 1 173  ? 12.996  0.577   -4.899  1.00 186.59 ? 173  MET A SD  1 
ATOM   1212  C  CE  . MET A 1 173  ? 14.745  0.954   -4.883  1.00 176.15 ? 173  MET A CE  1 
ATOM   1213  N  N   . VAL A 1 174  ? 11.568  -2.859  -1.306  1.00 171.99 ? 174  VAL A N   1 
ATOM   1214  C  CA  . VAL A 1 174  ? 10.560  -3.901  -1.275  1.00 176.37 ? 174  VAL A CA  1 
ATOM   1215  C  C   . VAL A 1 174  ? 9.302   -3.332  -0.644  1.00 176.49 ? 174  VAL A C   1 
ATOM   1216  O  O   . VAL A 1 174  ? 9.373   -2.386  0.139   1.00 176.12 ? 174  VAL A O   1 
ATOM   1217  C  CB  . VAL A 1 174  ? 11.059  -5.144  -0.521  1.00 179.93 ? 174  VAL A CB  1 
ATOM   1218  C  CG1 . VAL A 1 174  ? 11.668  -4.732  0.799   1.00 178.05 ? 174  VAL A CG1 1 
ATOM   1219  C  CG2 . VAL A 1 174  ? 9.945   -6.162  -0.333  1.00 183.23 ? 174  VAL A CG2 1 
ATOM   1220  N  N   . GLU A 1 175  ? 8.155   -3.887  -1.012  1.00 176.21 ? 175  GLU A N   1 
ATOM   1221  C  CA  . GLU A 1 175  ? 6.876   -3.403  -0.525  1.00 177.34 ? 175  GLU A CA  1 
ATOM   1222  C  C   . GLU A 1 175  ? 6.281   -4.519  0.308   1.00 178.14 ? 175  GLU A C   1 
ATOM   1223  O  O   . GLU A 1 175  ? 6.954   -5.519  0.536   1.00 177.23 ? 175  GLU A O   1 
ATOM   1224  C  CB  . GLU A 1 175  ? 5.984   -3.069  -1.729  1.00 183.63 ? 175  GLU A CB  1 
ATOM   1225  C  CG  . GLU A 1 175  ? 6.607   -3.476  -3.100  1.00 187.85 ? 175  GLU A CG  1 
ATOM   1226  C  CD  . GLU A 1 175  ? 6.145   -2.606  -4.278  1.00 189.38 ? 175  GLU A CD  1 
ATOM   1227  O  OE1 . GLU A 1 175  ? 4.930   -2.577  -4.580  1.00 190.79 ? 175  GLU A OE1 1 
ATOM   1228  O  OE2 . GLU A 1 175  ? 7.005   -1.959  -4.915  1.00 187.89 ? 175  GLU A OE2 1 
ATOM   1229  N  N   . GLU A 1 176  ? 5.044   -4.364  0.776   1.00 166.43 ? 176  GLU A N   1 
ATOM   1230  C  CA  . GLU A 1 176  ? 4.276   -5.529  1.240   1.00 158.31 ? 176  GLU A CA  1 
ATOM   1231  C  C   . GLU A 1 176  ? 2.825   -5.174  1.538   1.00 165.24 ? 176  GLU A C   1 
ATOM   1232  O  O   . GLU A 1 176  ? 2.409   -4.039  1.325   1.00 163.82 ? 176  GLU A O   1 
ATOM   1233  C  CB  . GLU A 1 176  ? 4.948   -6.250  2.422   1.00 168.11 ? 176  GLU A CB  1 
ATOM   1234  C  CG  . GLU A 1 176  ? 4.788   -7.793  2.428   1.00 174.79 ? 176  GLU A CG  1 
ATOM   1235  C  CD  . GLU A 1 176  ? 6.116   -8.561  2.224   1.00 188.03 ? 176  GLU A CD  1 
ATOM   1236  O  OE1 . GLU A 1 176  ? 7.005   -8.068  1.495   1.00 187.80 ? 176  GLU A OE1 1 
ATOM   1237  O  OE2 . GLU A 1 176  ? 6.276   -9.672  2.782   1.00 187.60 ? 176  GLU A OE2 1 
ATOM   1238  N  N   . ILE A 1 177  ? 2.060   -6.160  1.997   1.00 209.43 ? 177  ILE A N   1 
ATOM   1239  C  CA  . ILE A 1 177  ? 0.628   -5.993  2.246   1.00 215.93 ? 177  ILE A CA  1 
ATOM   1240  C  C   . ILE A 1 177  ? 0.307   -5.674  3.707   1.00 218.38 ? 177  ILE A C   1 
ATOM   1241  O  O   . ILE A 1 177  ? 0.832   -6.305  4.626   1.00 215.88 ? 177  ILE A O   1 
ATOM   1242  C  CB  . ILE A 1 177  ? -0.164  -7.256  1.800   1.00 221.71 ? 177  ILE A CB  1 
ATOM   1243  C  CG1 . ILE A 1 177  ? -0.480  -8.189  2.986   1.00 223.28 ? 177  ILE A CG1 1 
ATOM   1244  C  CG2 . ILE A 1 177  ? 0.610   -8.000  0.715   1.00 222.88 ? 177  ILE A CG2 1 
ATOM   1245  C  CD1 . ILE A 1 177  ? -1.805  -7.907  3.722   1.00 223.60 ? 177  ILE A CD1 1 
ATOM   1246  N  N   . ASP A 1 178  ? -0.565  -4.698  3.930   1.00 228.05 ? 178  ASP A N   1 
ATOM   1247  C  CA  . ASP A 1 178  ? -0.975  -4.405  5.292   1.00 231.51 ? 178  ASP A CA  1 
ATOM   1248  C  C   . ASP A 1 178  ? -2.263  -5.123  5.661   1.00 238.77 ? 178  ASP A C   1 
ATOM   1249  O  O   . ASP A 1 178  ? -3.356  -4.675  5.328   1.00 242.13 ? 178  ASP A O   1 
ATOM   1250  C  CB  . ASP A 1 178  ? -1.121  -2.910  5.515   1.00 227.40 ? 178  ASP A CB  1 
ATOM   1251  C  CG  . ASP A 1 178  ? -1.060  -2.548  6.970   1.00 221.40 ? 178  ASP A CG  1 
ATOM   1252  O  OD1 . ASP A 1 178  ? -1.017  -1.344  7.288   1.00 218.46 ? 178  ASP A OD1 1 
ATOM   1253  O  OD2 . ASP A 1 178  ? -1.045  -3.483  7.795   1.00 220.37 ? 178  ASP A OD2 1 
ATOM   1254  N  N   . HIS A 1 179  ? -2.118  -6.239  6.362   1.00 274.69 ? 179  HIS A N   1 
ATOM   1255  C  CA  . HIS A 1 179  ? -3.262  -6.985  6.857   1.00 280.49 ? 179  HIS A CA  1 
ATOM   1256  C  C   . HIS A 1 179  ? -3.787  -6.397  8.179   1.00 278.10 ? 179  HIS A C   1 
ATOM   1257  O  O   . HIS A 1 179  ? -5.004  -6.314  8.375   1.00 280.33 ? 179  HIS A O   1 
ATOM   1258  C  CB  . HIS A 1 179  ? -2.887  -8.460  7.030   1.00 287.91 ? 179  HIS A CB  1 
ATOM   1259  C  CG  . HIS A 1 179  ? -4.035  -9.411  6.863   1.00 299.58 ? 179  HIS A CG  1 
ATOM   1260  N  ND1 . HIS A 1 179  ? -4.179  -10.210 5.752   1.00 304.45 ? 179  HIS A ND1 1 
ATOM   1261  C  CD2 . HIS A 1 179  ? -5.078  -9.703  7.676   1.00 305.35 ? 179  HIS A CD2 1 
ATOM   1262  C  CE1 . HIS A 1 179  ? -5.266  -10.951 5.882   1.00 310.88 ? 179  HIS A CE1 1 
ATOM   1263  N  NE2 . HIS A 1 179  ? -5.830  -10.663 7.041   1.00 311.45 ? 179  HIS A NE2 1 
ATOM   1264  N  N   . ILE A 1 180  ? -2.881  -5.988  9.077   1.00 245.02 ? 180  ILE A N   1 
ATOM   1265  C  CA  . ILE A 1 180  ? -3.273  -5.431  10.391  1.00 242.70 ? 180  ILE A CA  1 
ATOM   1266  C  C   . ILE A 1 180  ? -2.727  -4.027  10.687  1.00 234.18 ? 180  ILE A C   1 
ATOM   1267  O  O   . ILE A 1 180  ? -3.445  -3.165  11.189  1.00 230.34 ? 180  ILE A O   1 
ATOM   1268  C  CB  . ILE A 1 180  ? -2.923  -6.385  11.570  1.00 227.06 ? 180  ILE A CB  1 
ATOM   1269  C  CG1 . ILE A 1 180  ? -1.514  -6.946  11.426  1.00 222.35 ? 180  ILE A CG1 1 
ATOM   1270  C  CG2 . ILE A 1 180  ? -3.893  -7.535  11.628  1.00 232.47 ? 180  ILE A CG2 1 
ATOM   1271  C  CD1 . ILE A 1 180  ? -1.338  -8.276  12.116  1.00 221.78 ? 180  ILE A CD1 1 
ATOM   1272  N  N   . GLY A 1 181  ? -1.455  -3.807  10.382  1.00 166.46 ? 181  GLY A N   1 
ATOM   1273  C  CA  . GLY A 1 181  ? -0.841  -2.505  10.552  1.00 165.05 ? 181  GLY A CA  1 
ATOM   1274  C  C   . GLY A 1 181  ? 0.613   -2.736  10.876  1.00 163.15 ? 181  GLY A C   1 
ATOM   1275  O  O   . GLY A 1 181  ? 1.458   -1.857  10.733  1.00 161.31 ? 181  GLY A O   1 
ATOM   1276  N  N   . ILE A 1 182  ? 0.892   -3.943  11.345  1.00 227.80 ? 182  ILE A N   1 
ATOM   1277  C  CA  . ILE A 1 182  ? 2.257   -4.371  11.577  1.00 224.22 ? 182  ILE A CA  1 
ATOM   1278  C  C   . ILE A 1 182  ? 2.773   -4.959  10.273  1.00 221.94 ? 182  ILE A C   1 
ATOM   1279  O  O   . ILE A 1 182  ? 2.651   -6.158  10.027  1.00 223.71 ? 182  ILE A O   1 
ATOM   1280  C  CB  . ILE A 1 182  ? 2.314   -5.450  12.666  1.00 224.47 ? 182  ILE A CB  1 
ATOM   1281  C  CG1 . ILE A 1 182  ? 1.279   -5.162  13.759  1.00 226.76 ? 182  ILE A CG1 1 
ATOM   1282  C  CG2 . ILE A 1 182  ? 3.728   -5.582  13.233  1.00 221.42 ? 182  ILE A CG2 1 
ATOM   1283  C  CD1 . ILE A 1 182  ? 1.150   -6.267  14.790  1.00 229.51 ? 182  ILE A CD1 1 
ATOM   1284  N  N   . ILE A 1 183  ? 3.337   -4.112  9.424   1.00 199.38 ? 183  ILE A N   1 
ATOM   1285  C  CA  . ILE A 1 183  ? 3.816   -4.573  8.125   1.00 196.91 ? 183  ILE A CA  1 
ATOM   1286  C  C   . ILE A 1 183  ? 5.069   -5.423  8.295   1.00 194.78 ? 183  ILE A C   1 
ATOM   1287  O  O   . ILE A 1 183  ? 6.092   -4.919  8.738   1.00 193.68 ? 183  ILE A O   1 
ATOM   1288  C  CB  . ILE A 1 183  ? 4.134   -3.399  7.184   1.00 193.88 ? 183  ILE A CB  1 
ATOM   1289  C  CG1 . ILE A 1 183  ? 2.873   -2.568  6.906   1.00 194.58 ? 183  ILE A CG1 1 
ATOM   1290  C  CG2 . ILE A 1 183  ? 4.691   -3.927  5.893   1.00 194.36 ? 183  ILE A CG2 1 
ATOM   1291  C  CD1 . ILE A 1 183  ? 3.131   -1.230  6.209   1.00 193.29 ? 183  ILE A CD1 1 
ATOM   1292  N  N   . SER A 1 184  ? 4.996   -6.696  7.914   1.00 181.70 ? 184  SER A N   1 
ATOM   1293  C  CA  . SER A 1 184  ? 6.043   -7.671  8.240   1.00 179.45 ? 184  SER A CA  1 
ATOM   1294  C  C   . SER A 1 184  ? 7.113   -7.867  7.163   1.00 185.76 ? 184  SER A C   1 
ATOM   1295  O  O   . SER A 1 184  ? 7.129   -8.894  6.494   1.00 188.45 ? 184  SER A O   1 
ATOM   1296  C  CB  . SER A 1 184  ? 5.408   -9.034  8.545   1.00 182.82 ? 184  SER A CB  1 
ATOM   1297  O  OG  . SER A 1 184  ? 4.055   -8.891  8.953   1.00 183.10 ? 184  SER A OG  1 
ATOM   1298  N  N   . PHE A 1 185  ? 8.024   -6.917  7.014   1.00 190.08 ? 185  PHE A N   1 
ATOM   1299  C  CA  . PHE A 1 185  ? 9.046   -7.030  5.978   1.00 189.28 ? 185  PHE A CA  1 
ATOM   1300  C  C   . PHE A 1 185  ? 9.921   -8.287  6.131   1.00 187.96 ? 185  PHE A C   1 
ATOM   1301  O  O   . PHE A 1 185  ? 9.670   -9.100  7.025   1.00 186.60 ? 185  PHE A O   1 
ATOM   1302  C  CB  . PHE A 1 185  ? 9.890   -5.766  5.941   1.00 186.05 ? 185  PHE A CB  1 
ATOM   1303  C  CG  . PHE A 1 185  ? 9.146   -4.566  5.466   1.00 185.22 ? 185  PHE A CG  1 
ATOM   1304  C  CD1 . PHE A 1 185  ? 9.429   -4.004  4.232   1.00 185.65 ? 185  PHE A CD1 1 
ATOM   1305  C  CD2 . PHE A 1 185  ? 8.155   -4.002  6.245   1.00 185.49 ? 185  PHE A CD2 1 
ATOM   1306  C  CE1 . PHE A 1 185  ? 8.738   -2.898  3.784   1.00 186.22 ? 185  PHE A CE1 1 
ATOM   1307  C  CE2 . PHE A 1 185  ? 7.476   -2.888  5.810   1.00 186.05 ? 185  PHE A CE2 1 
ATOM   1308  C  CZ  . PHE A 1 185  ? 7.768   -2.333  4.573   1.00 187.09 ? 185  PHE A CZ  1 
ATOM   1309  N  N   . PRO A 1 186  ? 10.925  -8.461  5.237   1.00 150.58 ? 186  PRO A N   1 
ATOM   1310  C  CA  . PRO A 1 186  ? 11.803  -9.633  5.187   1.00 154.81 ? 186  PRO A CA  1 
ATOM   1311  C  C   . PRO A 1 186  ? 13.260  -9.313  5.511   1.00 152.67 ? 186  PRO A C   1 
ATOM   1312  O  O   . PRO A 1 186  ? 13.805  -8.311  5.029   1.00 151.89 ? 186  PRO A O   1 
ATOM   1313  C  CB  . PRO A 1 186  ? 11.687  -10.062 3.728   1.00 157.38 ? 186  PRO A CB  1 
ATOM   1314  C  CG  . PRO A 1 186  ? 11.038  -8.852  2.990   1.00 156.66 ? 186  PRO A CG  1 
ATOM   1315  C  CD  . PRO A 1 186  ? 11.007  -7.728  3.970   1.00 151.83 ? 186  PRO A CD  1 
ATOM   1316  N  N   . ASP A 1 187  ? 13.877  -10.198 6.295   1.00 197.18 ? 187  ASP A N   1 
ATOM   1317  C  CA  . ASP A 1 187  ? 15.203  -9.968  6.859   1.00 194.52 ? 187  ASP A CA  1 
ATOM   1318  C  C   . ASP A 1 187  ? 16.110  -9.347  5.815   1.00 191.12 ? 187  ASP A C   1 
ATOM   1319  O  O   . ASP A 1 187  ? 16.054  -9.719  4.656   1.00 189.94 ? 187  ASP A O   1 
ATOM   1320  C  CB  . ASP A 1 187  ? 15.820  -11.284 7.370   1.00 198.85 ? 187  ASP A CB  1 
ATOM   1321  C  CG  . ASP A 1 187  ? 15.264  -11.723 8.729   1.00 202.91 ? 187  ASP A CG  1 
ATOM   1322  O  OD1 . ASP A 1 187  ? 14.224  -11.179 9.162   1.00 203.48 ? 187  ASP A OD1 1 
ATOM   1323  O  OD2 . ASP A 1 187  ? 15.869  -12.622 9.361   1.00 204.94 ? 187  ASP A OD2 1 
ATOM   1324  N  N   . PHE A 1 188  ? 16.925  -8.384  6.225   1.00 166.63 ? 188  PHE A N   1 
ATOM   1325  C  CA  . PHE A 1 188  ? 17.960  -7.833  5.369   1.00 161.66 ? 188  PHE A CA  1 
ATOM   1326  C  C   . PHE A 1 188  ? 19.276  -8.296  5.962   1.00 161.23 ? 188  PHE A C   1 
ATOM   1327  O  O   . PHE A 1 188  ? 19.578  -7.974  7.105   1.00 159.50 ? 188  PHE A O   1 
ATOM   1328  C  CB  . PHE A 1 188  ? 17.876  -6.310  5.372   1.00 156.11 ? 188  PHE A CB  1 
ATOM   1329  C  CG  . PHE A 1 188  ? 19.003  -5.616  4.641   1.00 150.36 ? 188  PHE A CG  1 
ATOM   1330  C  CD1 . PHE A 1 188  ? 20.289  -5.592  5.160   1.00 148.53 ? 188  PHE A CD1 1 
ATOM   1331  C  CD2 . PHE A 1 188  ? 18.761  -4.936  3.466   1.00 151.61 ? 188  PHE A CD2 1 
ATOM   1332  C  CE1 . PHE A 1 188  ? 21.313  -4.932  4.499   1.00 145.53 ? 188  PHE A CE1 1 
ATOM   1333  C  CE2 . PHE A 1 188  ? 19.781  -4.271  2.809   1.00 149.23 ? 188  PHE A CE2 1 
ATOM   1334  C  CZ  . PHE A 1 188  ? 21.055  -4.270  3.326   1.00 146.21 ? 188  PHE A CZ  1 
ATOM   1335  N  N   . LYS A 1 189  ? 20.042  -9.072  5.197   1.00 220.67 ? 189  LYS A N   1 
ATOM   1336  C  CA  . LYS A 1 189  ? 21.334  -9.580  5.650   1.00 217.76 ? 189  LYS A CA  1 
ATOM   1337  C  C   . LYS A 1 189  ? 22.466  -8.622  5.327   1.00 214.16 ? 189  LYS A C   1 
ATOM   1338  O  O   . LYS A 1 189  ? 22.527  -8.038  4.246   1.00 212.62 ? 189  LYS A O   1 
ATOM   1339  C  CB  . LYS A 1 189  ? 21.635  -10.947 5.033   1.00 224.28 ? 189  LYS A CB  1 
ATOM   1340  C  CG  . LYS A 1 189  ? 23.102  -11.162 4.645   1.00 225.93 ? 189  LYS A CG  1 
ATOM   1341  C  CD  . LYS A 1 189  ? 23.816  -12.127 5.591   1.00 229.60 ? 189  LYS A CD  1 
ATOM   1342  C  CE  . LYS A 1 189  ? 24.789  -13.056 4.852   1.00 232.56 ? 189  LYS A CE  1 
ATOM   1343  N  NZ  . LYS A 1 189  ? 25.781  -12.331 4.001   1.00 230.42 ? 189  LYS A NZ  1 
ATOM   1344  N  N   . ILE A 1 190  ? 23.366  -8.476  6.284   1.00 205.02 ? 190  ILE A N   1 
ATOM   1345  C  CA  . ILE A 1 190  ? 24.520  -7.619  6.129   1.00 202.68 ? 190  ILE A CA  1 
ATOM   1346  C  C   . ILE A 1 190  ? 25.588  -8.345  5.319   1.00 207.37 ? 190  ILE A C   1 
ATOM   1347  O  O   . ILE A 1 190  ? 25.827  -9.530  5.531   1.00 216.38 ? 190  ILE A O   1 
ATOM   1348  C  CB  . ILE A 1 190  ? 25.061  -7.226  7.506   1.00 197.77 ? 190  ILE A CB  1 
ATOM   1349  C  CG1 . ILE A 1 190  ? 23.913  -6.697  8.342   1.00 190.08 ? 190  ILE A CG1 1 
ATOM   1350  C  CG2 . ILE A 1 190  ? 26.117  -6.155  7.390   1.00 187.50 ? 190  ILE A CG2 1 
ATOM   1351  C  CD1 . ILE A 1 190  ? 23.163  -5.587  7.649   1.00 187.27 ? 190  ILE A CD1 1 
ATOM   1352  N  N   . PRO A 1 191  ? 26.221  -7.638  4.371   1.00 182.49 ? 191  PRO A N   1 
ATOM   1353  C  CA  . PRO A 1 191  ? 27.320  -8.146  3.543   1.00 182.07 ? 191  PRO A CA  1 
ATOM   1354  C  C   . PRO A 1 191  ? 28.421  -8.868  4.313   1.00 187.25 ? 191  PRO A C   1 
ATOM   1355  O  O   . PRO A 1 191  ? 28.802  -8.449  5.404   1.00 183.60 ? 191  PRO A O   1 
ATOM   1356  C  CB  . PRO A 1 191  ? 27.902  -6.872  2.935   1.00 177.85 ? 191  PRO A CB  1 
ATOM   1357  C  CG  . PRO A 1 191  ? 26.737  -5.969  2.801   1.00 176.08 ? 191  PRO A CG  1 
ATOM   1358  C  CD  . PRO A 1 191  ? 25.770  -6.312  3.916   1.00 177.14 ? 191  PRO A CD  1 
ATOM   1359  N  N   . SER A 1 192  ? 28.936  -9.939  3.718   1.00 182.85 ? 192  SER A N   1 
ATOM   1360  C  CA  . SER A 1 192  ? 30.065  -10.673 4.271   1.00 182.51 ? 192  SER A CA  1 
ATOM   1361  C  C   . SER A 1 192  ? 31.181  -9.680  4.547   1.00 172.53 ? 192  SER A C   1 
ATOM   1362  O  O   . SER A 1 192  ? 32.114  -9.955  5.298   1.00 168.65 ? 192  SER A O   1 
ATOM   1363  C  CB  . SER A 1 192  ? 30.555  -11.725 3.266   1.00 187.68 ? 192  SER A CB  1 
ATOM   1364  O  OG  . SER A 1 192  ? 29.507  -12.211 2.432   1.00 191.87 ? 192  SER A OG  1 
ATOM   1365  N  N   . ASN A 1 193  ? 31.059  -8.518  3.917   1.00 163.56 ? 193  ASN A N   1 
ATOM   1366  C  CA  . ASN A 1 193  ? 32.005  -7.433  4.069   1.00 162.32 ? 193  ASN A CA  1 
ATOM   1367  C  C   . ASN A 1 193  ? 31.383  -6.163  3.505   1.00 160.71 ? 193  ASN A C   1 
ATOM   1368  O  O   . ASN A 1 193  ? 31.586  -5.837  2.349   1.00 161.92 ? 193  ASN A O   1 
ATOM   1369  C  CB  . ASN A 1 193  ? 33.318  -7.773  3.365   1.00 164.01 ? 193  ASN A CB  1 
ATOM   1370  C  CG  . ASN A 1 193  ? 34.289  -6.614  3.351   1.00 162.36 ? 193  ASN A CG  1 
ATOM   1371  O  OD1 . ASN A 1 193  ? 34.002  -5.550  3.888   1.00 159.51 ? 193  ASN A OD1 1 
ATOM   1372  N  ND2 . ASN A 1 193  ? 35.446  -6.813  2.727   1.00 163.67 ? 193  ASN A ND2 1 
ATOM   1373  N  N   . PRO A 1 194  ? 30.592  -5.458  4.331   1.00 199.71 ? 194  PRO A N   1 
ATOM   1374  C  CA  . PRO A 1 194  ? 29.849  -4.225  4.009   1.00 195.93 ? 194  PRO A CA  1 
ATOM   1375  C  C   . PRO A 1 194  ? 30.645  -2.918  4.166   1.00 190.46 ? 194  PRO A C   1 
ATOM   1376  O  O   . PRO A 1 194  ? 31.729  -2.934  4.738   1.00 188.25 ? 194  PRO A O   1 
ATOM   1377  C  CB  . PRO A 1 194  ? 28.718  -4.212  5.050   1.00 197.74 ? 194  PRO A CB  1 
ATOM   1378  C  CG  . PRO A 1 194  ? 28.890  -5.453  5.897   1.00 202.07 ? 194  PRO A CG  1 
ATOM   1379  C  CD  . PRO A 1 194  ? 30.282  -5.941  5.686   1.00 201.45 ? 194  PRO A CD  1 
ATOM   1380  N  N   . ARG A 1 195  ? 30.093  -1.805  3.680   1.00 178.13 ? 195  ARG A N   1 
ATOM   1381  C  CA  . ARG A 1 195  ? 30.656  -0.477  3.937   1.00 177.67 ? 195  ARG A CA  1 
ATOM   1382  C  C   . ARG A 1 195  ? 30.388  -0.026  5.368   1.00 177.19 ? 195  ARG A C   1 
ATOM   1383  O  O   . ARG A 1 195  ? 29.240  -0.018  5.821   1.00 178.25 ? 195  ARG A O   1 
ATOM   1384  C  CB  . ARG A 1 195  ? 30.080  0.563   2.976   1.00 180.00 ? 195  ARG A CB  1 
ATOM   1385  C  CG  . ARG A 1 195  ? 30.688  0.567   1.579   1.00 181.91 ? 195  ARG A CG  1 
ATOM   1386  C  CD  . ARG A 1 195  ? 29.687  0.096   0.522   1.00 188.60 ? 195  ARG A CD  1 
ATOM   1387  N  NE  . ARG A 1 195  ? 29.319  1.136   -0.436  1.00 191.58 ? 195  ARG A NE  1 
ATOM   1388  C  CZ  . ARG A 1 195  ? 30.185  1.954   -1.030  1.00 192.03 ? 195  ARG A CZ  1 
ATOM   1389  N  NH1 . ARG A 1 195  ? 31.482  1.868   -0.773  1.00 190.47 ? 195  ARG A NH1 1 
ATOM   1390  N  NH2 . ARG A 1 195  ? 29.754  2.868   -1.887  1.00 193.27 ? 195  ARG A NH2 1 
ATOM   1391  N  N   . TYR A 1 196  ? 31.443  0.380   6.068   1.00 176.85 ? 196  TYR A N   1 
ATOM   1392  C  CA  . TYR A 1 196  ? 31.336  0.673   7.498   1.00 172.98 ? 196  TYR A CA  1 
ATOM   1393  C  C   . TYR A 1 196  ? 30.862  2.091   7.861   1.00 167.84 ? 196  TYR A C   1 
ATOM   1394  O  O   . TYR A 1 196  ? 31.495  3.089   7.527   1.00 164.84 ? 196  TYR A O   1 
ATOM   1395  C  CB  . TYR A 1 196  ? 32.635  0.270   8.224   1.00 175.86 ? 196  TYR A CB  1 
ATOM   1396  C  CG  . TYR A 1 196  ? 32.829  -1.244  8.275   1.00 179.20 ? 196  TYR A CG  1 
ATOM   1397  C  CD1 . TYR A 1 196  ? 31.864  -2.058  8.866   1.00 180.21 ? 196  TYR A CD1 1 
ATOM   1398  C  CD2 . TYR A 1 196  ? 33.957  -1.858  7.735   1.00 179.60 ? 196  TYR A CD2 1 
ATOM   1399  C  CE1 . TYR A 1 196  ? 32.005  -3.436  8.915   1.00 183.09 ? 196  TYR A CE1 1 
ATOM   1400  C  CE2 . TYR A 1 196  ? 34.108  -3.248  7.784   1.00 181.60 ? 196  TYR A CE2 1 
ATOM   1401  C  CZ  . TYR A 1 196  ? 33.120  -4.026  8.378   1.00 182.99 ? 196  TYR A CZ  1 
ATOM   1402  O  OH  . TYR A 1 196  ? 33.213  -5.399  8.458   1.00 184.73 ? 196  TYR A OH  1 
ATOM   1403  N  N   . GLY A 1 197  ? 29.733  2.159   8.552   1.00 184.75 ? 197  GLY A N   1 
ATOM   1404  C  CA  . GLY A 1 197  ? 29.198  3.433   8.968   1.00 184.70 ? 197  GLY A CA  1 
ATOM   1405  C  C   . GLY A 1 197  ? 27.744  3.393   9.389   1.00 185.42 ? 197  GLY A C   1 
ATOM   1406  O  O   . GLY A 1 197  ? 27.300  2.462   10.072  1.00 189.07 ? 197  GLY A O   1 
ATOM   1407  N  N   . MET A 1 198  ? 27.002  4.415   8.964   1.00 166.25 ? 198  MET A N   1 
ATOM   1408  C  CA  . MET A 1 198  ? 25.622  4.638   9.394   1.00 167.60 ? 198  MET A CA  1 
ATOM   1409  C  C   . MET A 1 198  ? 24.572  4.399   8.289   1.00 164.45 ? 198  MET A C   1 
ATOM   1410  O  O   . MET A 1 198  ? 24.404  5.207   7.376   1.00 159.18 ? 198  MET A O   1 
ATOM   1411  C  CB  . MET A 1 198  ? 25.500  6.060   9.948   1.00 170.66 ? 198  MET A CB  1 
ATOM   1412  C  CG  . MET A 1 198  ? 24.108  6.416   10.417  1.00 196.27 ? 198  MET A CG  1 
ATOM   1413  S  SD  . MET A 1 198  ? 23.402  5.147   11.481  1.00 211.92 ? 198  MET A SD  1 
ATOM   1414  C  CE  . MET A 1 198  ? 24.564  5.176   12.839  1.00 158.06 ? 198  MET A CE  1 
ATOM   1415  N  N   . TRP A 1 199  ? 23.852  3.291   8.393   1.00 175.78 ? 199  TRP A N   1 
ATOM   1416  C  CA  . TRP A 1 199  ? 22.808  2.963   7.440   1.00 178.06 ? 199  TRP A CA  1 
ATOM   1417  C  C   . TRP A 1 199  ? 21.558  3.797   7.672   1.00 179.54 ? 199  TRP A C   1 
ATOM   1418  O  O   . TRP A 1 199  ? 21.361  4.295   8.765   1.00 181.84 ? 199  TRP A O   1 
ATOM   1419  C  CB  . TRP A 1 199  ? 22.487  1.494   7.577   1.00 183.02 ? 199  TRP A CB  1 
ATOM   1420  C  CG  . TRP A 1 199  ? 23.513  0.659   6.920   1.00 186.85 ? 199  TRP A CG  1 
ATOM   1421  C  CD1 . TRP A 1 199  ? 24.815  0.491   7.296   1.00 187.51 ? 199  TRP A CD1 1 
ATOM   1422  C  CD2 . TRP A 1 199  ? 23.333  -0.117  5.740   1.00 189.62 ? 199  TRP A CD2 1 
ATOM   1423  N  NE1 . TRP A 1 199  ? 25.454  -0.356  6.419   1.00 190.53 ? 199  TRP A NE1 1 
ATOM   1424  C  CE2 . TRP A 1 199  ? 24.558  -0.743  5.458   1.00 190.79 ? 199  TRP A CE2 1 
ATOM   1425  C  CE3 . TRP A 1 199  ? 22.242  -0.350  4.891   1.00 191.49 ? 199  TRP A CE3 1 
ATOM   1426  C  CZ2 . TRP A 1 199  ? 24.718  -1.585  4.366   1.00 190.58 ? 199  TRP A CZ2 1 
ATOM   1427  C  CZ3 . TRP A 1 199  ? 22.404  -1.189  3.806   1.00 192.28 ? 199  TRP A CZ3 1 
ATOM   1428  C  CH2 . TRP A 1 199  ? 23.629  -1.793  3.552   1.00 192.58 ? 199  TRP A CH2 1 
ATOM   1429  N  N   . THR A 1 200  ? 20.718  3.947   6.652   1.00 135.57 ? 200  THR A N   1 
ATOM   1430  C  CA  . THR A 1 200  ? 19.475  4.697   6.787   1.00 142.15 ? 200  THR A CA  1 
ATOM   1431  C  C   . THR A 1 200  ? 18.272  3.932   6.226   1.00 137.15 ? 200  THR A C   1 
ATOM   1432  O  O   . THR A 1 200  ? 18.231  3.675   5.053   1.00 136.25 ? 200  THR A O   1 
ATOM   1433  C  CB  . THR A 1 200  ? 19.571  6.018   6.009   1.00 135.66 ? 200  THR A CB  1 
ATOM   1434  O  OG1 . THR A 1 200  ? 20.870  6.597   6.179   1.00 137.27 ? 200  THR A OG1 1 
ATOM   1435  C  CG2 . THR A 1 200  ? 18.532  6.971   6.496   1.00 136.83 ? 200  THR A CG2 1 
ATOM   1436  N  N   . ILE A 1 201  ? 17.280  3.571   7.023   1.00 140.02 ? 201  ILE A N   1 
ATOM   1437  C  CA  . ILE A 1 201  ? 16.092  2.975   6.421   1.00 139.49 ? 201  ILE A CA  1 
ATOM   1438  C  C   . ILE A 1 201  ? 14.960  4.003   6.324   1.00 140.28 ? 201  ILE A C   1 
ATOM   1439  O  O   . ILE A 1 201  ? 14.559  4.582   7.338   1.00 144.91 ? 201  ILE A O   1 
ATOM   1440  C  CB  . ILE A 1 201  ? 15.607  1.707   7.168   1.00 140.88 ? 201  ILE A CB  1 
ATOM   1441  C  CG1 . ILE A 1 201  ? 16.646  0.614   7.097   1.00 140.09 ? 201  ILE A CG1 1 
ATOM   1442  C  CG2 . ILE A 1 201  ? 14.356  1.131   6.536   1.00 144.78 ? 201  ILE A CG2 1 
ATOM   1443  C  CD1 . ILE A 1 201  ? 16.044  -0.727  7.384   1.00 142.24 ? 201  ILE A CD1 1 
ATOM   1444  N  N   . LYS A 1 202  ? 14.479  4.246   5.100   1.00 175.51 ? 202  LYS A N   1 
ATOM   1445  C  CA  . LYS A 1 202  ? 13.311  5.093   4.833   1.00 175.27 ? 202  LYS A CA  1 
ATOM   1446  C  C   . LYS A 1 202  ? 12.090  4.260   4.475   1.00 178.04 ? 202  LYS A C   1 
ATOM   1447  O  O   . LYS A 1 202  ? 12.205  3.094   4.142   1.00 179.32 ? 202  LYS A O   1 
ATOM   1448  C  CB  . LYS A 1 202  ? 13.606  6.090   3.719   1.00 179.30 ? 202  LYS A CB  1 
ATOM   1449  C  CG  . LYS A 1 202  ? 14.584  7.150   4.125   1.00 180.24 ? 202  LYS A CG  1 
ATOM   1450  C  CD  . LYS A 1 202  ? 14.643  8.234   3.108   1.00 183.54 ? 202  LYS A CD  1 
ATOM   1451  C  CE  . LYS A 1 202  ? 15.752  9.192   3.430   1.00 183.47 ? 202  LYS A CE  1 
ATOM   1452  N  NZ  . LYS A 1 202  ? 16.305  9.747   2.177   1.00 184.15 ? 202  LYS A NZ  1 
ATOM   1453  N  N   . ALA A 1 203  ? 10.917  4.863   4.537   1.00 165.15 ? 203  ALA A N   1 
ATOM   1454  C  CA  . ALA A 1 203  ? 9.706   4.126   4.247   1.00 170.19 ? 203  ALA A CA  1 
ATOM   1455  C  C   . ALA A 1 203  ? 8.649   5.075   3.701   1.00 173.50 ? 203  ALA A C   1 
ATOM   1456  O  O   . ALA A 1 203  ? 8.457   6.169   4.255   1.00 171.20 ? 203  ALA A O   1 
ATOM   1457  C  CB  . ALA A 1 203  ? 9.204   3.419   5.494   1.00 168.25 ? 203  ALA A CB  1 
ATOM   1458  N  N   . LYS A 1 204  ? 7.967   4.632   2.629   1.00 167.16 ? 204  LYS A N   1 
ATOM   1459  C  CA  . LYS A 1 204  ? 6.892   5.384   1.947   1.00 171.78 ? 204  LYS A CA  1 
ATOM   1460  C  C   . LYS A 1 204  ? 5.706   4.523   1.508   1.00 173.40 ? 204  LYS A C   1 
ATOM   1461  O  O   . LYS A 1 204  ? 5.867   3.366   1.137   1.00 172.05 ? 204  LYS A O   1 
ATOM   1462  C  CB  . LYS A 1 204  ? 7.447   6.066   0.714   1.00 174.16 ? 204  LYS A CB  1 
ATOM   1463  C  CG  . LYS A 1 204  ? 8.350   5.144   -0.076  1.00 180.70 ? 204  LYS A CG  1 
ATOM   1464  C  CD  . LYS A 1 204  ? 9.047   5.886   -1.198  1.00 183.15 ? 204  LYS A CD  1 
ATOM   1465  C  CE  . LYS A 1 204  ? 10.129  5.035   -1.847  1.00 185.49 ? 204  LYS A CE  1 
ATOM   1466  N  NZ  . LYS A 1 204  ? 10.535  5.599   -3.163  1.00 186.88 ? 204  LYS A NZ  1 
ATOM   1467  N  N   . TYR A 1 205  ? 4.513   5.104   1.539   1.00 197.97 ? 205  TYR A N   1 
ATOM   1468  C  CA  . TYR A 1 205  ? 3.335   4.393   1.079   1.00 207.26 ? 205  TYR A CA  1 
ATOM   1469  C  C   . TYR A 1 205  ? 3.442   4.184   -0.411  1.00 215.90 ? 205  TYR A C   1 
ATOM   1470  O  O   . TYR A 1 205  ? 3.832   5.104   -1.128  1.00 218.75 ? 205  TYR A O   1 
ATOM   1471  C  CB  . TYR A 1 205  ? 2.065   5.173   1.412   1.00 208.72 ? 205  TYR A CB  1 
ATOM   1472  C  CG  . TYR A 1 205  ? 1.607   4.902   2.806   1.00 209.63 ? 205  TYR A CG  1 
ATOM   1473  C  CD1 . TYR A 1 205  ? 1.642   5.885   3.781   1.00 208.26 ? 205  TYR A CD1 1 
ATOM   1474  C  CD2 . TYR A 1 205  ? 1.189   3.633   3.162   1.00 212.35 ? 205  TYR A CD2 1 
ATOM   1475  C  CE1 . TYR A 1 205  ? 1.246   5.609   5.069   1.00 208.58 ? 205  TYR A CE1 1 
ATOM   1476  C  CE2 . TYR A 1 205  ? 0.797   3.347   4.441   1.00 212.41 ? 205  TYR A CE2 1 
ATOM   1477  C  CZ  . TYR A 1 205  ? 0.824   4.332   5.392   1.00 210.58 ? 205  TYR A CZ  1 
ATOM   1478  O  OH  . TYR A 1 205  ? 0.423   4.017   6.669   1.00 210.23 ? 205  TYR A OH  1 
ATOM   1479  N  N   . LYS A 1 206  ? 3.101   2.985   -0.886  1.00 207.78 ? 206  LYS A N   1 
ATOM   1480  C  CA  . LYS A 1 206  ? 3.170   2.714   -2.323  1.00 210.59 ? 206  LYS A CA  1 
ATOM   1481  C  C   . LYS A 1 206  ? 2.320   3.751   -3.031  1.00 213.76 ? 206  LYS A C   1 
ATOM   1482  O  O   . LYS A 1 206  ? 2.835   4.618   -3.745  1.00 212.31 ? 206  LYS A O   1 
ATOM   1483  C  CB  . LYS A 1 206  ? 2.686   1.296   -2.674  1.00 214.69 ? 206  LYS A CB  1 
ATOM   1484  C  CG  . LYS A 1 206  ? 2.972   0.877   -4.123  1.00 217.43 ? 206  LYS A CG  1 
ATOM   1485  C  CD  . LYS A 1 206  ? 2.758   -0.614  -4.341  1.00 221.39 ? 206  LYS A CD  1 
ATOM   1486  C  CE  . LYS A 1 206  ? 1.308   -1.015  -4.136  1.00 226.72 ? 206  LYS A CE  1 
ATOM   1487  N  NZ  . LYS A 1 206  ? 1.045   -2.374  -4.691  1.00 230.61 ? 206  LYS A NZ  1 
ATOM   1488  N  N   . GLU A 1 207  ? 1.016   3.673   -2.778  1.00 206.42 ? 207  GLU A N   1 
ATOM   1489  C  CA  . GLU A 1 207  ? 0.035   4.559   -3.393  1.00 209.60 ? 207  GLU A CA  1 
ATOM   1490  C  C   . GLU A 1 207  ? 0.266   6.034   -3.062  1.00 205.04 ? 207  GLU A C   1 
ATOM   1491  O  O   . GLU A 1 207  ? 1.383   6.456   -2.761  1.00 200.24 ? 207  GLU A O   1 
ATOM   1492  C  CB  . GLU A 1 207  ? -1.391  4.138   -3.006  1.00 216.83 ? 207  GLU A CB  1 
ATOM   1493  C  CG  . GLU A 1 207  ? -1.851  2.790   -3.586  1.00 222.00 ? 207  GLU A CG  1 
ATOM   1494  C  CD  . GLU A 1 207  ? -2.032  2.807   -5.103  1.00 225.70 ? 207  GLU A CD  1 
ATOM   1495  O  OE1 . GLU A 1 207  ? -1.873  3.884   -5.717  1.00 224.90 ? 207  GLU A OE1 1 
ATOM   1496  O  OE2 . GLU A 1 207  ? -2.339  1.737   -5.678  1.00 229.66 ? 207  GLU A OE2 1 
ATOM   1497  N  N   . ASP A 1 208  ? -0.799  6.817   -3.156  1.00 225.43 ? 208  ASP A N   1 
ATOM   1498  C  CA  . ASP A 1 208  ? -0.742  8.236   -2.857  1.00 217.88 ? 208  ASP A CA  1 
ATOM   1499  C  C   . ASP A 1 208  ? -0.514  8.414   -1.381  1.00 212.54 ? 208  ASP A C   1 
ATOM   1500  O  O   . ASP A 1 208  ? -0.754  7.491   -0.607  1.00 214.98 ? 208  ASP A O   1 
ATOM   1501  C  CB  . ASP A 1 208  ? -2.065  8.869   -3.211  1.00 217.65 ? 208  ASP A CB  1 
ATOM   1502  C  CG  . ASP A 1 208  ? -3.224  8.047   -2.726  1.00 219.25 ? 208  ASP A CG  1 
ATOM   1503  O  OD1 . ASP A 1 208  ? -3.251  7.722   -1.518  1.00 216.12 ? 208  ASP A OD1 1 
ATOM   1504  O  OD2 . ASP A 1 208  ? -4.090  7.706   -3.557  1.00 223.73 ? 208  ASP A OD2 1 
ATOM   1505  N  N   . PHE A 1 209  ? -0.100  9.623   -1.012  1.00 221.14 ? 209  PHE A N   1 
ATOM   1506  C  CA  . PHE A 1 209  ? 0.358   9.967   0.333   1.00 215.77 ? 209  PHE A CA  1 
ATOM   1507  C  C   . PHE A 1 209  ? 1.876   10.215  0.353   1.00 211.29 ? 209  PHE A C   1 
ATOM   1508  O  O   . PHE A 1 209  ? 2.674   9.328   0.029   1.00 211.68 ? 209  PHE A O   1 
ATOM   1509  C  CB  . PHE A 1 209  ? -0.012  8.896   1.363   1.00 214.07 ? 209  PHE A CB  1 
ATOM   1510  C  CG  . PHE A 1 209  ? -1.487  8.769   1.616   1.00 215.02 ? 209  PHE A CG  1 
ATOM   1511  C  CD1 . PHE A 1 209  ? -2.044  7.531   1.898   1.00 217.03 ? 209  PHE A CD1 1 
ATOM   1512  C  CD2 . PHE A 1 209  ? -2.312  9.878   1.577   1.00 212.34 ? 209  PHE A CD2 1 
ATOM   1513  C  CE1 . PHE A 1 209  ? -3.394  7.402   2.140   1.00 217.97 ? 209  PHE A CE1 1 
ATOM   1514  C  CE2 . PHE A 1 209  ? -3.668  9.758   1.820   1.00 216.02 ? 209  PHE A CE2 1 
ATOM   1515  C  CZ  . PHE A 1 209  ? -4.210  8.518   2.102   1.00 218.37 ? 209  PHE A CZ  1 
ATOM   1516  N  N   . SER A 1 210  ? 2.261   11.428  0.741   1.00 224.28 ? 210  SER A N   1 
ATOM   1517  C  CA  . SER A 1 210  ? 3.664   11.830  0.830   1.00 219.79 ? 210  SER A CA  1 
ATOM   1518  C  C   . SER A 1 210  ? 4.375   11.270  2.076   1.00 217.05 ? 210  SER A C   1 
ATOM   1519  O  O   . SER A 1 210  ? 5.596   11.389  2.201   1.00 211.96 ? 210  SER A O   1 
ATOM   1520  C  CB  . SER A 1 210  ? 3.756   13.361  0.841   1.00 218.10 ? 210  SER A CB  1 
ATOM   1521  O  OG  . SER A 1 210  ? 5.100   13.798  0.856   1.00 214.71 ? 210  SER A OG  1 
ATOM   1522  N  N   . THR A 1 211  ? 3.609   10.648  2.980   1.00 195.24 ? 211  THR A N   1 
ATOM   1523  C  CA  . THR A 1 211  ? 4.053   10.342  4.354   1.00 194.33 ? 211  THR A CA  1 
ATOM   1524  C  C   . THR A 1 211  ? 5.426   9.669   4.497   1.00 191.42 ? 211  THR A C   1 
ATOM   1525  O  O   . THR A 1 211  ? 5.671   8.611   3.938   1.00 191.59 ? 211  THR A O   1 
ATOM   1526  C  CB  . THR A 1 211  ? 2.960   9.581   5.184   1.00 198.69 ? 211  THR A CB  1 
ATOM   1527  O  OG1 . THR A 1 211  ? 2.365   8.534   4.405   1.00 202.95 ? 211  THR A OG1 1 
ATOM   1528  C  CG2 . THR A 1 211  ? 1.870   10.547  5.642   1.00 198.84 ? 211  THR A CG2 1 
ATOM   1529  N  N   . THR A 1 212  ? 6.302   10.302  5.271   1.00 175.70 ? 212  THR A N   1 
ATOM   1530  C  CA  . THR A 1 212  ? 7.693   9.870   5.442   1.00 173.96 ? 212  THR A CA  1 
ATOM   1531  C  C   . THR A 1 212  ? 7.985   8.983   6.673   1.00 176.19 ? 212  THR A C   1 
ATOM   1532  O  O   . THR A 1 212  ? 7.833   9.398   7.833   1.00 179.29 ? 212  THR A O   1 
ATOM   1533  C  CB  . THR A 1 212  ? 8.626   11.107  5.534   1.00 170.28 ? 212  THR A CB  1 
ATOM   1534  O  OG1 . THR A 1 212  ? 8.241   12.073  4.550   1.00 170.82 ? 212  THR A OG1 1 
ATOM   1535  C  CG2 . THR A 1 212  ? 10.087  10.714  5.351   1.00 167.81 ? 212  THR A CG2 1 
ATOM   1536  N  N   . GLY A 1 213  ? 8.429   7.763   6.418   1.00 236.05 ? 213  GLY A N   1 
ATOM   1537  C  CA  . GLY A 1 213  ? 9.043   6.981   7.468   1.00 235.42 ? 213  GLY A CA  1 
ATOM   1538  C  C   . GLY A 1 213  ? 10.550  7.112   7.375   1.00 231.64 ? 213  GLY A C   1 
ATOM   1539  O  O   . GLY A 1 213  ? 11.097  7.081   6.275   1.00 231.53 ? 213  GLY A O   1 
ATOM   1540  N  N   . THR A 1 214  ? 11.222  7.284   8.511   1.00 169.98 ? 214  THR A N   1 
ATOM   1541  C  CA  . THR A 1 214  ? 12.673  7.125   8.555   1.00 165.57 ? 214  THR A CA  1 
ATOM   1542  C  C   . THR A 1 214  ? 13.016  6.277   9.759   1.00 161.39 ? 214  THR A C   1 
ATOM   1543  O  O   . THR A 1 214  ? 12.160  6.021   10.592  1.00 162.36 ? 214  THR A O   1 
ATOM   1544  C  CB  . THR A 1 214  ? 13.413  8.463   8.661   1.00 165.34 ? 214  THR A CB  1 
ATOM   1545  O  OG1 . THR A 1 214  ? 12.892  9.371   7.687   1.00 166.01 ? 214  THR A OG1 1 
ATOM   1546  C  CG2 . THR A 1 214  ? 14.904  8.269   8.423   1.00 160.77 ? 214  THR A CG2 1 
ATOM   1547  N  N   . ALA A 1 215  ? 14.253  5.807   9.823   1.00 197.78 ? 215  ALA A N   1 
ATOM   1548  C  CA  . ALA A 1 215  ? 14.793  5.127   10.993  1.00 195.48 ? 215  ALA A CA  1 
ATOM   1549  C  C   . ALA A 1 215  ? 16.255  4.998   10.692  1.00 192.78 ? 215  ALA A C   1 
ATOM   1550  O  O   . ALA A 1 215  ? 16.696  5.427   9.627   1.00 189.91 ? 215  ALA A O   1 
ATOM   1551  C  CB  . ALA A 1 215  ? 14.178  3.762   11.174  1.00 196.72 ? 215  ALA A CB  1 
ATOM   1552  N  N   . TYR A 1 216  ? 17.022  4.418   11.604  1.00 169.41 ? 216  TYR A N   1 
ATOM   1553  C  CA  . TYR A 1 216  ? 18.424  4.201   11.300  1.00 174.58 ? 216  TYR A CA  1 
ATOM   1554  C  C   . TYR A 1 216  ? 18.958  2.935   11.890  1.00 173.82 ? 216  TYR A C   1 
ATOM   1555  O  O   . TYR A 1 216  ? 18.260  2.189   12.587  1.00 172.18 ? 216  TYR A O   1 
ATOM   1556  C  CB  . TYR A 1 216  ? 19.301  5.351   11.776  1.00 176.31 ? 216  TYR A CB  1 
ATOM   1557  C  CG  . TYR A 1 216  ? 18.964  6.676   11.168  1.00 179.84 ? 216  TYR A CG  1 
ATOM   1558  C  CD1 . TYR A 1 216  ? 19.878  7.352   10.382  1.00 180.95 ? 216  TYR A CD1 1 
ATOM   1559  C  CD2 . TYR A 1 216  ? 17.728  7.263   11.399  1.00 186.23 ? 216  TYR A CD2 1 
ATOM   1560  C  CE1 . TYR A 1 216  ? 19.564  8.574   9.826   1.00 182.62 ? 216  TYR A CE1 1 
ATOM   1561  C  CE2 . TYR A 1 216  ? 17.397  8.478   10.848  1.00 188.14 ? 216  TYR A CE2 1 
ATOM   1562  C  CZ  . TYR A 1 216  ? 18.318  9.133   10.060  1.00 186.48 ? 216  TYR A CZ  1 
ATOM   1563  O  OH  . TYR A 1 216  ? 17.980  10.352  9.517   1.00 187.65 ? 216  TYR A OH  1 
ATOM   1564  N  N   . PHE A 1 217  ? 20.225  2.721   11.570  1.00 155.32 ? 217  PHE A N   1 
ATOM   1565  C  CA  . PHE A 1 217  ? 21.000  1.615   12.081  1.00 153.92 ? 217  PHE A CA  1 
ATOM   1566  C  C   . PHE A 1 217  ? 22.448  1.648   11.575  1.00 154.06 ? 217  PHE A C   1 
ATOM   1567  O  O   . PHE A 1 217  ? 22.711  1.931   10.405  1.00 154.02 ? 217  PHE A O   1 
ATOM   1568  C  CB  . PHE A 1 217  ? 20.295  0.279   11.823  1.00 155.17 ? 217  PHE A CB  1 
ATOM   1569  C  CG  . PHE A 1 217  ? 20.610  -0.352  10.499  1.00 155.82 ? 217  PHE A CG  1 
ATOM   1570  C  CD1 . PHE A 1 217  ? 21.616  -1.295  10.398  1.00 154.48 ? 217  PHE A CD1 1 
ATOM   1571  C  CD2 . PHE A 1 217  ? 19.866  -0.054  9.379   1.00 157.10 ? 217  PHE A CD2 1 
ATOM   1572  C  CE1 . PHE A 1 217  ? 21.892  -1.898  9.208   1.00 153.34 ? 217  PHE A CE1 1 
ATOM   1573  C  CE2 . PHE A 1 217  ? 20.140  -0.653  8.198   1.00 153.44 ? 217  PHE A CE2 1 
ATOM   1574  C  CZ  . PHE A 1 217  ? 21.159  -1.579  8.111   1.00 153.53 ? 217  PHE A CZ  1 
ATOM   1575  N  N   . GLU A 1 218  ? 23.371  1.370   12.491  1.00 189.94 ? 218  GLU A N   1 
ATOM   1576  C  CA  . GLU A 1 218  ? 24.795  1.489   12.256  1.00 192.22 ? 218  GLU A CA  1 
ATOM   1577  C  C   . GLU A 1 218  ? 25.381  0.103   12.084  1.00 191.97 ? 218  GLU A C   1 
ATOM   1578  O  O   . GLU A 1 218  ? 24.970  -0.852  12.747  1.00 193.02 ? 218  GLU A O   1 
ATOM   1579  C  CB  . GLU A 1 218  ? 25.435  2.169   13.465  1.00 199.08 ? 218  GLU A CB  1 
ATOM   1580  C  CG  . GLU A 1 218  ? 26.824  2.748   13.244  1.00 204.40 ? 218  GLU A CG  1 
ATOM   1581  C  CD  . GLU A 1 218  ? 27.286  3.595   14.426  1.00 209.85 ? 218  GLU A CD  1 
ATOM   1582  O  OE1 . GLU A 1 218  ? 28.489  3.931   14.504  1.00 211.01 ? 218  GLU A OE1 1 
ATOM   1583  O  OE2 . GLU A 1 218  ? 26.438  3.921   15.285  1.00 213.05 ? 218  GLU A OE2 1 
ATOM   1584  N  N   . VAL A 1 219  ? 26.333  -0.009  11.176  1.00 143.02 ? 219  VAL A N   1 
ATOM   1585  C  CA  . VAL A 1 219  ? 27.056  -1.241  11.026  1.00 143.25 ? 219  VAL A CA  1 
ATOM   1586  C  C   . VAL A 1 219  ? 28.452  -0.964  11.421  1.00 141.73 ? 219  VAL A C   1 
ATOM   1587  O  O   . VAL A 1 219  ? 29.058  0.001   10.954  1.00 139.37 ? 219  VAL A O   1 
ATOM   1588  C  CB  . VAL A 1 219  ? 27.181  -1.656  9.580   1.00 141.09 ? 219  VAL A CB  1 
ATOM   1589  C  CG1 . VAL A 1 219  ? 28.250  -2.736  9.458   1.00 143.74 ? 219  VAL A CG1 1 
ATOM   1590  C  CG2 . VAL A 1 219  ? 25.845  -2.131  9.037   1.00 142.39 ? 219  VAL A CG2 1 
ATOM   1591  N  N   . LYS A 1 220  ? 28.975  -1.834  12.262  1.00 177.84 ? 220  LYS A N   1 
ATOM   1592  C  CA  . LYS A 1 220  ? 30.315  -1.664  12.762  1.00 176.12 ? 220  LYS A CA  1 
ATOM   1593  C  C   . LYS A 1 220  ? 31.053  -2.944  12.499  1.00 175.35 ? 220  LYS A C   1 
ATOM   1594  O  O   . LYS A 1 220  ? 30.449  -4.016  12.407  1.00 170.86 ? 220  LYS A O   1 
ATOM   1595  C  CB  . LYS A 1 220  ? 30.299  -1.358  14.267  1.00 175.63 ? 220  LYS A CB  1 
ATOM   1596  C  CG  . LYS A 1 220  ? 29.833  0.063   14.657  1.00 175.30 ? 220  LYS A CG  1 
ATOM   1597  C  CD  . LYS A 1 220  ? 29.513  0.170   16.160  1.00 182.08 ? 220  LYS A CD  1 
ATOM   1598  C  CE  . LYS A 1 220  ? 29.014  1.551   16.563  1.00 180.53 ? 220  LYS A CE  1 
ATOM   1599  N  NZ  . LYS A 1 220  ? 30.105  2.556   16.611  1.00 178.34 ? 220  LYS A NZ  1 
ATOM   1600  N  N   . GLU A 1 221  ? 32.364  -2.817  12.374  1.00 180.24 ? 221  GLU A N   1 
ATOM   1601  C  CA  . GLU A 1 221  ? 33.212  -3.952  12.114  1.00 191.06 ? 221  GLU A CA  1 
ATOM   1602  C  C   . GLU A 1 221  ? 33.666  -4.644  13.389  1.00 190.61 ? 221  GLU A C   1 
ATOM   1603  O  O   . GLU A 1 221  ? 34.523  -4.133  14.107  1.00 188.05 ? 221  GLU A O   1 
ATOM   1604  C  CB  . GLU A 1 221  ? 34.447  -3.509  11.355  1.00 199.86 ? 221  GLU A CB  1 
ATOM   1605  C  CG  . GLU A 1 221  ? 35.493  -4.591  11.356  1.00 211.49 ? 221  GLU A CG  1 
ATOM   1606  C  CD  . GLU A 1 221  ? 36.771  -4.186  10.680  1.00 217.09 ? 221  GLU A CD  1 
ATOM   1607  O  OE1 . GLU A 1 221  ? 36.771  -3.130  10.005  1.00 216.10 ? 221  GLU A OE1 1 
ATOM   1608  O  OE2 . GLU A 1 221  ? 37.766  -4.938  10.825  1.00 221.22 ? 221  GLU A OE2 1 
ATOM   1609  N  N   . TYR A 1 222  ? 33.119  -5.825  13.654  1.00 208.06 ? 222  TYR A N   1 
ATOM   1610  C  CA  . TYR A 1 222  ? 33.546  -6.606  14.810  1.00 209.01 ? 222  TYR A CA  1 
ATOM   1611  C  C   . TYR A 1 222  ? 35.044  -6.877  14.780  1.00 209.79 ? 222  TYR A C   1 
ATOM   1612  O  O   . TYR A 1 222  ? 35.620  -7.166  13.735  1.00 210.23 ? 222  TYR A O   1 
ATOM   1613  C  CB  . TYR A 1 222  ? 32.791  -7.935  14.896  1.00 209.93 ? 222  TYR A CB  1 
ATOM   1614  C  CG  . TYR A 1 222  ? 33.249  -8.795  16.047  1.00 210.78 ? 222  TYR A CG  1 
ATOM   1615  C  CD1 . TYR A 1 222  ? 32.786  -8.562  17.337  1.00 210.61 ? 222  TYR A CD1 1 
ATOM   1616  C  CD2 . TYR A 1 222  ? 34.155  -9.829  15.849  1.00 213.34 ? 222  TYR A CD2 1 
ATOM   1617  C  CE1 . TYR A 1 222  ? 33.207  -9.337  18.396  1.00 213.53 ? 222  TYR A CE1 1 
ATOM   1618  C  CE2 . TYR A 1 222  ? 34.582  -10.610 16.901  1.00 215.99 ? 222  TYR A CE2 1 
ATOM   1619  C  CZ  . TYR A 1 222  ? 34.106  -10.359 18.170  1.00 215.98 ? 222  TYR A CZ  1 
ATOM   1620  O  OH  . TYR A 1 222  ? 34.530  -11.140 19.218  1.00 217.91 ? 222  TYR A OH  1 
ATOM   1621  N  N   . VAL A 1 223  ? 35.673  -6.766  15.937  1.00 160.92 ? 223  VAL A N   1 
ATOM   1622  C  CA  . VAL A 1 223  ? 37.048  -7.198  16.085  1.00 158.65 ? 223  VAL A CA  1 
ATOM   1623  C  C   . VAL A 1 223  ? 37.093  -8.120  17.293  1.00 162.16 ? 223  VAL A C   1 
ATOM   1624  O  O   . VAL A 1 223  ? 36.135  -8.168  18.062  1.00 161.78 ? 223  VAL A O   1 
ATOM   1625  C  CB  . VAL A 1 223  ? 38.011  -5.993  16.250  1.00 154.21 ? 223  VAL A CB  1 
ATOM   1626  C  CG1 . VAL A 1 223  ? 39.465  -6.460  16.352  1.00 153.25 ? 223  VAL A CG1 1 
ATOM   1627  C  CG2 . VAL A 1 223  ? 37.834  -5.008  15.094  1.00 151.32 ? 223  VAL A CG2 1 
ATOM   1628  N  N   . LEU A 1 224  ? 38.170  -8.883  17.445  1.00 206.32 ? 224  LEU A N   1 
ATOM   1629  C  CA  . LEU A 1 224  ? 38.284  -9.749  18.608  1.00 211.36 ? 224  LEU A CA  1 
ATOM   1630  C  C   . LEU A 1 224  ? 39.072  -9.051  19.699  1.00 212.20 ? 224  LEU A C   1 
ATOM   1631  O  O   . LEU A 1 224  ? 40.187  -8.567  19.455  1.00 211.47 ? 224  LEU A O   1 
ATOM   1632  C  CB  . LEU A 1 224  ? 38.920  -11.097 18.262  1.00 211.74 ? 224  LEU A CB  1 
ATOM   1633  C  CG  . LEU A 1 224  ? 38.435  -12.307 19.079  1.00 216.03 ? 224  LEU A CG  1 
ATOM   1634  C  CD1 . LEU A 1 224  ? 38.934  -12.238 20.513  1.00 218.06 ? 224  LEU A CD1 1 
ATOM   1635  C  CD2 . LEU A 1 224  ? 36.914  -12.451 19.039  1.00 215.75 ? 224  LEU A CD2 1 
ATOM   1636  N  N   . PRO A 1 225  ? 38.474  -8.974  20.904  1.00 257.96 ? 225  PRO A N   1 
ATOM   1637  C  CA  . PRO A 1 225  ? 39.103  -8.410  22.097  1.00 249.65 ? 225  PRO A CA  1 
ATOM   1638  C  C   . PRO A 1 225  ? 40.127  -9.373  22.671  1.00 253.29 ? 225  PRO A C   1 
ATOM   1639  O  O   . PRO A 1 225  ? 39.783  -10.502 23.034  1.00 254.49 ? 225  PRO A O   1 
ATOM   1640  C  CB  . PRO A 1 225  ? 37.937  -8.282  23.091  1.00 247.17 ? 225  PRO A CB  1 
ATOM   1641  C  CG  . PRO A 1 225  ? 36.697  -8.546  22.321  1.00 250.60 ? 225  PRO A CG  1 
ATOM   1642  C  CD  . PRO A 1 225  ? 37.102  -9.426  21.188  1.00 257.96 ? 225  PRO A CD  1 
ATOM   1643  N  N   . HIS A 1 226  ? 41.372  -8.919  22.748  1.00 210.97 ? 226  HIS A N   1 
ATOM   1644  C  CA  . HIS A 1 226  ? 42.412  -9.631  23.469  1.00 217.79 ? 226  HIS A CA  1 
ATOM   1645  C  C   . HIS A 1 226  ? 42.287  -9.380  24.989  1.00 210.56 ? 226  HIS A C   1 
ATOM   1646  O  O   . HIS A 1 226  ? 42.359  -10.316 25.792  1.00 210.28 ? 226  HIS A O   1 
ATOM   1647  C  CB  . HIS A 1 226  ? 43.796  -9.209  22.959  1.00 224.58 ? 226  HIS A CB  1 
ATOM   1648  C  CG  . HIS A 1 226  ? 44.005  -9.434  21.494  1.00 236.25 ? 226  HIS A CG  1 
ATOM   1649  N  ND1 . HIS A 1 226  ? 44.131  -8.399  20.589  1.00 238.47 ? 226  HIS A ND1 1 
ATOM   1650  C  CD2 . HIS A 1 226  ? 44.121  -10.574 20.774  1.00 244.41 ? 226  HIS A CD2 1 
ATOM   1651  C  CE1 . HIS A 1 226  ? 44.312  -8.892  19.382  1.00 245.59 ? 226  HIS A CE1 1 
ATOM   1652  N  NE2 . HIS A 1 226  ? 44.311  -10.212 19.465  1.00 249.29 ? 226  HIS A NE2 1 
ATOM   1653  N  N   . PHE A 1 227  ? 42.092  -8.119  25.377  1.00 207.47 ? 227  PHE A N   1 
ATOM   1654  C  CA  . PHE A 1 227  ? 41.927  -7.750  26.786  1.00 201.45 ? 227  PHE A CA  1 
ATOM   1655  C  C   . PHE A 1 227  ? 41.006  -6.546  26.960  1.00 196.64 ? 227  PHE A C   1 
ATOM   1656  O  O   . PHE A 1 227  ? 41.050  -5.587  26.194  1.00 198.19 ? 227  PHE A O   1 
ATOM   1657  C  CB  . PHE A 1 227  ? 43.280  -7.463  27.437  1.00 196.23 ? 227  PHE A CB  1 
ATOM   1658  C  CG  . PHE A 1 227  ? 44.060  -6.379  26.755  1.00 188.77 ? 227  PHE A CG  1 
ATOM   1659  C  CD1 . PHE A 1 227  ? 43.634  -5.069  26.797  1.00 180.99 ? 227  PHE A CD1 1 
ATOM   1660  C  CD2 . PHE A 1 227  ? 45.225  -6.671  26.079  1.00 191.55 ? 227  PHE A CD2 1 
ATOM   1661  C  CE1 . PHE A 1 227  ? 44.351  -4.080  26.171  1.00 179.71 ? 227  PHE A CE1 1 
ATOM   1662  C  CE2 . PHE A 1 227  ? 45.940  -5.681  25.453  1.00 189.42 ? 227  PHE A CE2 1 
ATOM   1663  C  CZ  . PHE A 1 227  ? 45.503  -4.390  25.497  1.00 184.09 ? 227  PHE A CZ  1 
ATOM   1664  N  N   . SER A 1 228  ? 40.177  -6.600  27.987  1.00 236.92 ? 228  SER A N   1 
ATOM   1665  C  CA  . SER A 1 228  ? 39.168  -5.584  28.201  1.00 234.09 ? 228  SER A CA  1 
ATOM   1666  C  C   . SER A 1 228  ? 39.766  -4.262  28.686  1.00 225.25 ? 228  SER A C   1 
ATOM   1667  O  O   . SER A 1 228  ? 40.242  -4.182  29.817  1.00 222.59 ? 228  SER A O   1 
ATOM   1668  C  CB  . SER A 1 228  ? 38.165  -6.113  29.219  1.00 237.53 ? 228  SER A CB  1 
ATOM   1669  O  OG  . SER A 1 228  ? 37.301  -5.089  29.660  1.00 234.84 ? 228  SER A OG  1 
ATOM   1670  N  N   . VAL A 1 229  ? 39.757  -3.232  27.838  1.00 181.12 ? 229  VAL A N   1 
ATOM   1671  C  CA  . VAL A 1 229  ? 40.110  -1.882  28.296  1.00 165.14 ? 229  VAL A CA  1 
ATOM   1672  C  C   . VAL A 1 229  ? 38.858  -1.048  28.512  1.00 165.49 ? 229  VAL A C   1 
ATOM   1673  O  O   . VAL A 1 229  ? 38.082  -0.848  27.583  1.00 163.56 ? 229  VAL A O   1 
ATOM   1674  C  CB  . VAL A 1 229  ? 41.025  -1.120  27.310  1.00 170.07 ? 229  VAL A CB  1 
ATOM   1675  C  CG1 . VAL A 1 229  ? 40.849  0.380   27.465  1.00 162.12 ? 229  VAL A CG1 1 
ATOM   1676  C  CG2 . VAL A 1 229  ? 42.466  -1.488  27.536  1.00 170.05 ? 229  VAL A CG2 1 
ATOM   1677  N  N   . SER A 1 230  ? 38.648  -0.584  29.740  1.00 198.63 ? 230  SER A N   1 
ATOM   1678  C  CA  . SER A 1 230  ? 37.555  0.338   30.031  1.00 192.70 ? 230  SER A CA  1 
ATOM   1679  C  C   . SER A 1 230  ? 38.116  1.739   30.043  1.00 188.62 ? 230  SER A C   1 
ATOM   1680  O  O   . SER A 1 230  ? 39.287  1.951   29.728  1.00 189.99 ? 230  SER A O   1 
ATOM   1681  C  CB  . SER A 1 230  ? 36.895  0.035   31.385  1.00 189.83 ? 230  SER A CB  1 
ATOM   1682  O  OG  . SER A 1 230  ? 37.761  0.332   32.473  1.00 187.84 ? 230  SER A OG  1 
ATOM   1683  N  N   . ILE A 1 231  ? 37.275  2.696   30.407  1.00 137.27 ? 231  ILE A N   1 
ATOM   1684  C  CA  . ILE A 1 231  ? 37.720  4.069   30.567  1.00 134.82 ? 231  ILE A CA  1 
ATOM   1685  C  C   . ILE A 1 231  ? 36.590  4.874   31.213  1.00 136.55 ? 231  ILE A C   1 
ATOM   1686  O  O   . ILE A 1 231  ? 35.528  5.069   30.620  1.00 138.03 ? 231  ILE A O   1 
ATOM   1687  C  CB  . ILE A 1 231  ? 38.185  4.653   29.220  1.00 139.72 ? 231  ILE A CB  1 
ATOM   1688  C  CG1 . ILE A 1 231  ? 38.272  6.171   29.256  1.00 136.19 ? 231  ILE A CG1 1 
ATOM   1689  C  CG2 . ILE A 1 231  ? 37.242  4.245   28.131  1.00 141.53 ? 231  ILE A CG2 1 
ATOM   1690  C  CD1 . ILE A 1 231  ? 38.267  6.782   27.861  1.00 138.17 ? 231  ILE A CD1 1 
ATOM   1691  N  N   . GLU A 1 232  ? 36.815  5.285   32.460  1.00 188.43 ? 232  GLU A N   1 
ATOM   1692  C  CA  . GLU A 1 232  ? 35.845  6.057   33.221  1.00 189.38 ? 232  GLU A CA  1 
ATOM   1693  C  C   . GLU A 1 232  ? 36.393  7.449   33.444  1.00 186.00 ? 232  GLU A C   1 
ATOM   1694  O  O   . GLU A 1 232  ? 37.563  7.652   33.770  1.00 185.01 ? 232  GLU A O   1 
ATOM   1695  C  CB  . GLU A 1 232  ? 35.537  5.403   34.570  1.00 195.45 ? 232  GLU A CB  1 
ATOM   1696  C  CG  . GLU A 1 232  ? 35.583  3.883   34.563  1.00 207.06 ? 232  GLU A CG  1 
ATOM   1697  C  CD  . GLU A 1 232  ? 36.401  3.298   35.719  1.00 214.30 ? 232  GLU A CD  1 
ATOM   1698  O  OE1 . GLU A 1 232  ? 36.649  4.009   36.722  1.00 214.29 ? 232  GLU A OE1 1 
ATOM   1699  O  OE2 . GLU A 1 232  ? 36.794  2.115   35.615  1.00 219.39 ? 232  GLU A OE2 1 
ATOM   1700  N  N   . PRO A 1 233  ? 35.525  8.419   33.278  1.00 165.35 ? 233  PRO A N   1 
ATOM   1701  C  CA  . PRO A 1 233  ? 35.801  9.843   33.309  1.00 165.41 ? 233  PRO A CA  1 
ATOM   1702  C  C   . PRO A 1 233  ? 35.587  10.341  34.727  1.00 162.12 ? 233  PRO A C   1 
ATOM   1703  O  O   . PRO A 1 233  ? 34.814  9.713   35.460  1.00 163.22 ? 233  PRO A O   1 
ATOM   1704  C  CB  . PRO A 1 233  ? 34.702  10.401  32.398  1.00 165.29 ? 233  PRO A CB  1 
ATOM   1705  C  CG  . PRO A 1 233  ? 33.758  9.196   32.091  1.00 163.81 ? 233  PRO A CG  1 
ATOM   1706  C  CD  . PRO A 1 233  ? 34.099  8.157   33.081  1.00 164.39 ? 233  PRO A CD  1 
ATOM   1707  N  N   . GLU A 1 234  ? 36.231  11.442  35.107  1.00 183.87 ? 234  GLU A N   1 
ATOM   1708  C  CA  . GLU A 1 234  ? 36.014  11.993  36.434  1.00 178.32 ? 234  GLU A CA  1 
ATOM   1709  C  C   . GLU A 1 234  ? 34.510  12.058  36.754  1.00 172.80 ? 234  GLU A C   1 
ATOM   1710  O  O   . GLU A 1 234  ? 34.031  11.346  37.633  1.00 173.78 ? 234  GLU A O   1 
ATOM   1711  C  CB  . GLU A 1 234  ? 36.707  13.356  36.591  1.00 178.90 ? 234  GLU A CB  1 
ATOM   1712  C  CG  . GLU A 1 234  ? 37.374  13.545  37.972  1.00 193.79 ? 234  GLU A CG  1 
ATOM   1713  C  CD  . GLU A 1 234  ? 37.948  14.953  38.198  1.00 194.95 ? 234  GLU A CD  1 
ATOM   1714  O  OE1 . GLU A 1 234  ? 38.019  15.731  37.215  1.00 196.98 ? 234  GLU A OE1 1 
ATOM   1715  O  OE2 . GLU A 1 234  ? 38.325  15.286  39.356  1.00 193.72 ? 234  GLU A OE2 1 
ATOM   1716  N  N   . TYR A 1 235  ? 33.767  12.883  36.025  1.00 151.26 ? 235  TYR A N   1 
ATOM   1717  C  CA  . TYR A 1 235  ? 32.320  12.973  36.200  1.00 145.81 ? 235  TYR A CA  1 
ATOM   1718  C  C   . TYR A 1 235  ? 31.705  12.702  34.835  1.00 144.01 ? 235  TYR A C   1 
ATOM   1719  O  O   . TYR A 1 235  ? 32.380  12.161  33.976  1.00 145.90 ? 235  TYR A O   1 
ATOM   1720  C  CB  . TYR A 1 235  ? 31.903  14.358  36.703  1.00 144.80 ? 235  TYR A CB  1 
ATOM   1721  C  CG  . TYR A 1 235  ? 32.651  14.869  37.927  1.00 147.18 ? 235  TYR A CG  1 
ATOM   1722  C  CD1 . TYR A 1 235  ? 31.973  15.454  38.998  1.00 148.67 ? 235  TYR A CD1 1 
ATOM   1723  C  CD2 . TYR A 1 235  ? 34.040  14.783  38.012  1.00 150.39 ? 235  TYR A CD2 1 
ATOM   1724  C  CE1 . TYR A 1 235  ? 32.669  15.931  40.130  1.00 151.65 ? 235  TYR A CE1 1 
ATOM   1725  C  CE2 . TYR A 1 235  ? 34.734  15.254  39.134  1.00 153.15 ? 235  TYR A CE2 1 
ATOM   1726  C  CZ  . TYR A 1 235  ? 34.050  15.828  40.185  1.00 154.27 ? 235  TYR A CZ  1 
ATOM   1727  O  OH  . TYR A 1 235  ? 34.756  16.291  41.276  1.00 156.18 ? 235  TYR A OH  1 
ATOM   1728  N  N   . ASN A 1 236  ? 30.452  13.092  34.609  1.00 192.39 ? 236  ASN A N   1 
ATOM   1729  C  CA  . ASN A 1 236  ? 29.814  12.815  33.316  1.00 192.87 ? 236  ASN A CA  1 
ATOM   1730  C  C   . ASN A 1 236  ? 29.591  13.993  32.381  1.00 189.12 ? 236  ASN A C   1 
ATOM   1731  O  O   . ASN A 1 236  ? 29.154  13.805  31.246  1.00 195.27 ? 236  ASN A O   1 
ATOM   1732  C  CB  . ASN A 1 236  ? 28.495  12.072  33.488  1.00 196.84 ? 236  ASN A CB  1 
ATOM   1733  C  CG  . ASN A 1 236  ? 28.666  10.574  33.410  1.00 205.58 ? 236  ASN A CG  1 
ATOM   1734  O  OD1 . ASN A 1 236  ? 29.718  10.042  33.769  1.00 207.41 ? 236  ASN A OD1 1 
ATOM   1735  N  ND2 . ASN A 1 236  ? 27.636  9.879   32.939  1.00 210.51 ? 236  ASN A ND2 1 
ATOM   1736  N  N   . PHE A 1 237  ? 29.858  15.200  32.863  1.00 131.69 ? 237  PHE A N   1 
ATOM   1737  C  CA  . PHE A 1 237  ? 29.750  16.400  32.051  1.00 136.12 ? 237  PHE A CA  1 
ATOM   1738  C  C   . PHE A 1 237  ? 30.986  17.146  32.357  1.00 133.82 ? 237  PHE A C   1 
ATOM   1739  O  O   . PHE A 1 237  ? 31.944  16.557  32.800  1.00 136.05 ? 237  PHE A O   1 
ATOM   1740  C  CB  . PHE A 1 237  ? 28.567  17.231  32.473  1.00 129.48 ? 237  PHE A CB  1 
ATOM   1741  C  CG  . PHE A 1 237  ? 27.257  16.544  32.263  1.00 129.62 ? 237  PHE A CG  1 
ATOM   1742  C  CD1 . PHE A 1 237  ? 26.335  17.040  31.346  1.00 130.46 ? 237  PHE A CD1 1 
ATOM   1743  C  CD2 . PHE A 1 237  ? 26.943  15.392  32.970  1.00 129.37 ? 237  PHE A CD2 1 
ATOM   1744  C  CE1 . PHE A 1 237  ? 25.107  16.409  31.137  1.00 131.45 ? 237  PHE A CE1 1 
ATOM   1745  C  CE2 . PHE A 1 237  ? 25.726  14.753  32.772  1.00 129.42 ? 237  PHE A CE2 1 
ATOM   1746  C  CZ  . PHE A 1 237  ? 24.802  15.262  31.851  1.00 130.86 ? 237  PHE A CZ  1 
ATOM   1747  N  N   . ILE A 1 238  ? 30.991  18.443  32.171  1.00 108.58 ? 238  ILE A N   1 
ATOM   1748  C  CA  . ILE A 1 238  ? 32.138  19.160  32.645  1.00 107.12 ? 238  ILE A CA  1 
ATOM   1749  C  C   . ILE A 1 238  ? 31.684  20.530  32.967  1.00 109.35 ? 238  ILE A C   1 
ATOM   1750  O  O   . ILE A 1 238  ? 31.681  21.388  32.087  1.00 111.05 ? 238  ILE A O   1 
ATOM   1751  C  CB  . ILE A 1 238  ? 33.263  19.209  31.628  1.00 107.53 ? 238  ILE A CB  1 
ATOM   1752  C  CG1 . ILE A 1 238  ? 33.949  17.856  31.566  1.00 107.72 ? 238  ILE A CG1 1 
ATOM   1753  C  CG2 . ILE A 1 238  ? 34.304  20.192  32.054  1.00 107.79 ? 238  ILE A CG2 1 
ATOM   1754  C  CD1 . ILE A 1 238  ? 35.360  17.921  31.051  1.00 107.50 ? 238  ILE A CD1 1 
ATOM   1755  N  N   . GLY A 1 239  ? 31.269  20.693  34.231  1.00 146.49 ? 239  GLY A N   1 
ATOM   1756  C  CA  . GLY A 1 239  ? 30.790  21.936  34.823  1.00 147.15 ? 239  GLY A CA  1 
ATOM   1757  C  C   . GLY A 1 239  ? 31.934  22.795  35.307  1.00 151.27 ? 239  GLY A C   1 
ATOM   1758  O  O   . GLY A 1 239  ? 32.986  22.295  35.707  1.00 152.22 ? 239  GLY A O   1 
ATOM   1759  N  N   . TYR A 1 240  ? 31.719  24.096  35.290  1.00 164.82 ? 240  TYR A N   1 
ATOM   1760  C  CA  . TYR A 1 240  ? 32.824  25.025  35.337  1.00 170.38 ? 240  TYR A CA  1 
ATOM   1761  C  C   . TYR A 1 240  ? 33.855  24.736  36.407  1.00 171.06 ? 240  TYR A C   1 
ATOM   1762  O  O   . TYR A 1 240  ? 34.929  25.316  36.371  1.00 168.59 ? 240  TYR A O   1 
ATOM   1763  C  CB  . TYR A 1 240  ? 32.301  26.409  35.598  1.00 168.10 ? 240  TYR A CB  1 
ATOM   1764  C  CG  . TYR A 1 240  ? 31.914  26.537  37.015  1.00 160.46 ? 240  TYR A CG  1 
ATOM   1765  C  CD1 . TYR A 1 240  ? 32.750  27.159  37.928  1.00 153.02 ? 240  TYR A CD1 1 
ATOM   1766  C  CD2 . TYR A 1 240  ? 30.723  25.986  37.458  1.00 160.45 ? 240  TYR A CD2 1 
ATOM   1767  C  CE1 . TYR A 1 240  ? 32.391  27.254  39.254  1.00 148.45 ? 240  TYR A CE1 1 
ATOM   1768  C  CE2 . TYR A 1 240  ? 30.342  26.077  38.774  1.00 156.49 ? 240  TYR A CE2 1 
ATOM   1769  C  CZ  . TYR A 1 240  ? 31.169  26.706  39.681  1.00 151.67 ? 240  TYR A CZ  1 
ATOM   1770  O  OH  . TYR A 1 240  ? 30.736  26.778  41.004  1.00 151.89 ? 240  TYR A OH  1 
ATOM   1771  N  N   . LYS A 1 241  ? 33.535  23.882  37.371  1.00 234.25 ? 241  LYS A N   1 
ATOM   1772  C  CA  . LYS A 1 241  ? 34.480  23.579  38.441  1.00 236.76 ? 241  LYS A CA  1 
ATOM   1773  C  C   . LYS A 1 241  ? 35.838  23.123  37.913  1.00 242.51 ? 241  LYS A C   1 
ATOM   1774  O  O   . LYS A 1 241  ? 36.868  23.696  38.272  1.00 241.95 ? 241  LYS A O   1 
ATOM   1775  C  CB  . LYS A 1 241  ? 33.898  22.547  39.404  1.00 220.24 ? 241  LYS A CB  1 
ATOM   1776  C  CG  . LYS A 1 241  ? 32.789  23.110  40.266  1.00 199.80 ? 241  LYS A CG  1 
ATOM   1777  C  CD  . LYS A 1 241  ? 32.037  22.023  41.009  1.00 214.62 ? 241  LYS A CD  1 
ATOM   1778  C  CE  . LYS A 1 241  ? 30.974  22.625  41.930  1.00 243.54 ? 241  LYS A CE  1 
ATOM   1779  N  NZ  . LYS A 1 241  ? 29.929  23.428  41.220  1.00 242.20 ? 241  LYS A NZ  1 
ATOM   1780  N  N   . ASN A 1 242  ? 35.841  22.096  37.066  1.00 164.55 ? 242  ASN A N   1 
ATOM   1781  C  CA  . ASN A 1 242  ? 37.068  21.663  36.397  1.00 167.26 ? 242  ASN A CA  1 
ATOM   1782  C  C   . ASN A 1 242  ? 37.022  22.157  34.989  1.00 172.89 ? 242  ASN A C   1 
ATOM   1783  O  O   . ASN A 1 242  ? 36.111  21.804  34.256  1.00 170.60 ? 242  ASN A O   1 
ATOM   1784  C  CB  . ASN A 1 242  ? 37.156  20.148  36.332  1.00 163.21 ? 242  ASN A CB  1 
ATOM   1785  C  CG  . ASN A 1 242  ? 36.255  19.458  37.338  1.00 155.00 ? 242  ASN A CG  1 
ATOM   1786  O  OD1 . ASN A 1 242  ? 36.724  18.633  38.124  1.00 153.24 ? 242  ASN A OD1 1 
ATOM   1787  N  ND2 . ASN A 1 242  ? 34.955  19.779  37.313  1.00 149.34 ? 242  ASN A ND2 1 
ATOM   1788  N  N   . PHE A 1 243  ? 37.983  22.967  34.589  1.00 183.04 ? 243  PHE A N   1 
ATOM   1789  C  CA  . PHE A 1 243  ? 37.964  23.463  33.220  1.00 193.19 ? 243  PHE A CA  1 
ATOM   1790  C  C   . PHE A 1 243  ? 39.411  23.526  32.797  1.00 199.37 ? 243  PHE A C   1 
ATOM   1791  O  O   . PHE A 1 243  ? 39.749  23.599  31.606  1.00 202.79 ? 243  PHE A O   1 
ATOM   1792  C  CB  . PHE A 1 243  ? 37.272  24.833  33.138  1.00 192.59 ? 243  PHE A CB  1 
ATOM   1793  C  CG  . PHE A 1 243  ? 37.011  25.316  31.727  1.00 198.55 ? 243  PHE A CG  1 
ATOM   1794  C  CD1 . PHE A 1 243  ? 36.339  24.520  30.816  1.00 200.15 ? 243  PHE A CD1 1 
ATOM   1795  C  CD2 . PHE A 1 243  ? 37.414  26.582  31.331  1.00 199.54 ? 243  PHE A CD2 1 
ATOM   1796  C  CE1 . PHE A 1 243  ? 36.102  24.966  29.540  1.00 202.52 ? 243  PHE A CE1 1 
ATOM   1797  C  CE2 . PHE A 1 243  ? 37.177  27.029  30.054  1.00 203.70 ? 243  PHE A CE2 1 
ATOM   1798  C  CZ  . PHE A 1 243  ? 36.524  26.220  29.161  1.00 205.67 ? 243  PHE A CZ  1 
ATOM   1799  N  N   . LYS A 1 244  ? 40.259  23.484  33.817  1.00 307.11 ? 244  LYS A N   1 
ATOM   1800  C  CA  . LYS A 1 244  ? 41.677  23.280  33.646  1.00 315.88 ? 244  LYS A CA  1 
ATOM   1801  C  C   . LYS A 1 244  ? 42.018  21.877  34.107  1.00 318.31 ? 244  LYS A C   1 
ATOM   1802  O  O   . LYS A 1 244  ? 43.197  21.521  34.180  1.00 325.03 ? 244  LYS A O   1 
ATOM   1803  C  CB  . LYS A 1 244  ? 42.471  24.310  34.438  1.00 316.87 ? 244  LYS A CB  1 
ATOM   1804  C  CG  . LYS A 1 244  ? 42.232  25.723  33.975  1.00 319.53 ? 244  LYS A CG  1 
ATOM   1805  C  CD  . LYS A 1 244  ? 43.391  26.614  34.344  1.00 322.50 ? 244  LYS A CD  1 
ATOM   1806  C  CE  . LYS A 1 244  ? 43.123  28.044  33.935  1.00 323.95 ? 244  LYS A CE  1 
ATOM   1807  N  NZ  . LYS A 1 244  ? 42.002  28.630  34.708  1.00 318.95 ? 244  LYS A NZ  1 
ATOM   1808  N  N   . ASN A 1 245  ? 40.990  21.077  34.409  1.00 188.74 ? 245  ASN A N   1 
ATOM   1809  C  CA  . ASN A 1 245  ? 41.245  19.678  34.773  1.00 188.56 ? 245  ASN A CA  1 
ATOM   1810  C  C   . ASN A 1 245  ? 40.076  18.686  34.848  1.00 183.01 ? 245  ASN A C   1 
ATOM   1811  O  O   . ASN A 1 245  ? 38.972  19.026  35.248  1.00 180.87 ? 245  ASN A O   1 
ATOM   1812  C  CB  . ASN A 1 245  ? 41.932  19.649  36.117  1.00 187.16 ? 245  ASN A CB  1 
ATOM   1813  C  CG  . ASN A 1 245  ? 40.991  19.953  37.206  1.00 186.42 ? 245  ASN A CG  1 
ATOM   1814  O  OD1 . ASN A 1 245  ? 39.974  20.615  36.980  1.00 186.27 ? 245  ASN A OD1 1 
ATOM   1815  N  ND2 . ASN A 1 245  ? 41.293  19.467  38.399  1.00 188.10 ? 245  ASN A ND2 1 
ATOM   1816  N  N   . PHE A 1 246  ? 40.389  17.432  34.519  1.00 115.98 ? 246  PHE A N   1 
ATOM   1817  C  CA  . PHE A 1 246  ? 39.452  16.309  34.540  1.00 138.20 ? 246  PHE A CA  1 
ATOM   1818  C  C   . PHE A 1 246  ? 40.223  15.012  34.833  1.00 133.44 ? 246  PHE A C   1 
ATOM   1819  O  O   . PHE A 1 246  ? 41.190  14.706  34.152  1.00 134.12 ? 246  PHE A O   1 
ATOM   1820  C  CB  . PHE A 1 246  ? 38.847  16.178  33.156  1.00 128.29 ? 246  PHE A CB  1 
ATOM   1821  C  CG  . PHE A 1 246  ? 37.480  15.570  33.124  1.00 115.29 ? 246  PHE A CG  1 
ATOM   1822  C  CD1 . PHE A 1 246  ? 36.396  16.257  33.602  1.00 114.84 ? 246  PHE A CD1 1 
ATOM   1823  C  CD2 . PHE A 1 246  ? 37.271  14.345  32.530  1.00 122.01 ? 246  PHE A CD2 1 
ATOM   1824  C  CE1 . PHE A 1 246  ? 35.140  15.714  33.534  1.00 109.81 ? 246  PHE A CE1 1 
ATOM   1825  C  CE2 . PHE A 1 246  ? 36.012  13.808  32.459  1.00 116.99 ? 246  PHE A CE2 1 
ATOM   1826  C  CZ  . PHE A 1 246  ? 34.949  14.494  32.965  1.00 111.48 ? 246  PHE A CZ  1 
ATOM   1827  N  N   . GLU A 1 247  ? 39.806  14.227  35.818  1.00 205.41 ? 247  GLU A N   1 
ATOM   1828  C  CA  . GLU A 1 247  ? 40.517  12.982  36.103  1.00 207.62 ? 247  GLU A CA  1 
ATOM   1829  C  C   . GLU A 1 247  ? 39.884  11.768  35.418  1.00 212.70 ? 247  GLU A C   1 
ATOM   1830  O  O   . GLU A 1 247  ? 38.859  11.229  35.860  1.00 212.19 ? 247  GLU A O   1 
ATOM   1831  C  CB  . GLU A 1 247  ? 40.620  12.738  37.616  1.00 251.23 ? 247  GLU A CB  1 
ATOM   1832  C  CG  . GLU A 1 247  ? 41.975  12.135  38.071  1.00 234.43 ? 247  GLU A CG  1 
ATOM   1833  C  CD  . GLU A 1 247  ? 41.862  11.545  39.446  1.00 182.82 ? 247  GLU A CD  1 
ATOM   1834  O  OE1 . GLU A 1 247  ? 41.046  12.074  40.195  1.00 177.02 ? 247  GLU A OE1 1 
ATOM   1835  O  OE2 . GLU A 1 247  ? 42.556  10.560  39.788  1.00 178.13 ? 247  GLU A OE2 1 
ATOM   1836  N  N   . ILE A 1 248  ? 40.534  11.326  34.352  1.00 162.46 ? 248  ILE A N   1 
ATOM   1837  C  CA  . ILE A 1 248  ? 40.146  10.108  33.669  1.00 158.25 ? 248  ILE A CA  1 
ATOM   1838  C  C   . ILE A 1 248  ? 41.024  8.949   34.109  1.00 158.00 ? 248  ILE A C   1 
ATOM   1839  O  O   . ILE A 1 248  ? 42.250  9.069   34.164  1.00 161.17 ? 248  ILE A O   1 
ATOM   1840  C  CB  . ILE A 1 248  ? 40.294  10.234  32.150  1.00 158.78 ? 248  ILE A CB  1 
ATOM   1841  C  CG1 . ILE A 1 248  ? 39.730  11.567  31.661  1.00 155.83 ? 248  ILE A CG1 1 
ATOM   1842  C  CG2 . ILE A 1 248  ? 39.579  9.079   31.461  1.00 160.15 ? 248  ILE A CG2 1 
ATOM   1843  C  CD1 . ILE A 1 248  ? 40.151  11.931  30.235  1.00 157.86 ? 248  ILE A CD1 1 
ATOM   1844  N  N   . THR A 1 249  ? 40.385  7.817   34.376  1.00 166.01 ? 249  THR A N   1 
ATOM   1845  C  CA  . THR A 1 249  ? 41.065  6.601   34.790  1.00 169.18 ? 249  THR A CA  1 
ATOM   1846  C  C   . THR A 1 249  ? 40.801  5.492   33.781  1.00 174.26 ? 249  THR A C   1 
ATOM   1847  O  O   . THR A 1 249  ? 39.648  5.137   33.559  1.00 172.74 ? 249  THR A O   1 
ATOM   1848  C  CB  . THR A 1 249  ? 40.479  6.121   36.101  1.00 174.50 ? 249  THR A CB  1 
ATOM   1849  O  OG1 . THR A 1 249  ? 39.542  7.096   36.581  1.00 171.05 ? 249  THR A OG1 1 
ATOM   1850  C  CG2 . THR A 1 249  ? 41.577  5.896   37.108  1.00 175.42 ? 249  THR A CG2 1 
ATOM   1851  N  N   . ILE A 1 250  ? 41.849  4.940   33.172  1.00 141.92 ? 250  ILE A N   1 
ATOM   1852  C  CA  . ILE A 1 250  ? 41.691  3.878   32.170  1.00 146.74 ? 250  ILE A CA  1 
ATOM   1853  C  C   . ILE A 1 250  ? 42.221  2.564   32.712  1.00 153.32 ? 250  ILE A C   1 
ATOM   1854  O  O   . ILE A 1 250  ? 43.376  2.484   33.116  1.00 154.29 ? 250  ILE A O   1 
ATOM   1855  C  CB  . ILE A 1 250  ? 42.491  4.196   30.911  1.00 147.90 ? 250  ILE A CB  1 
ATOM   1856  C  CG1 . ILE A 1 250  ? 43.942  4.499   31.312  1.00 151.83 ? 250  ILE A CG1 1 
ATOM   1857  C  CG2 . ILE A 1 250  ? 41.814  5.335   30.126  1.00 143.46 ? 250  ILE A CG2 1 
ATOM   1858  C  CD1 . ILE A 1 250  ? 44.908  4.725   30.177  1.00 155.89 ? 250  ILE A CD1 1 
ATOM   1859  N  N   . LYS A 1 251  ? 41.387  1.529   32.687  1.00 199.38 ? 251  LYS A N   1 
ATOM   1860  C  CA  . LYS A 1 251  ? 41.691  0.288   33.395  1.00 209.20 ? 251  LYS A CA  1 
ATOM   1861  C  C   . LYS A 1 251  ? 41.691  -0.957  32.510  1.00 220.69 ? 251  LYS A C   1 
ATOM   1862  O  O   . LYS A 1 251  ? 40.632  -1.494  32.183  1.00 221.59 ? 251  LYS A O   1 
ATOM   1863  C  CB  . LYS A 1 251  ? 40.698  0.089   34.540  1.00 208.45 ? 251  LYS A CB  1 
ATOM   1864  C  CG  . LYS A 1 251  ? 40.539  1.290   35.445  1.00 205.44 ? 251  LYS A CG  1 
ATOM   1865  C  CD  . LYS A 1 251  ? 39.890  0.903   36.760  1.00 205.59 ? 251  LYS A CD  1 
ATOM   1866  C  CE  . LYS A 1 251  ? 38.512  0.294   36.571  1.00 205.66 ? 251  LYS A CE  1 
ATOM   1867  N  NZ  . LYS A 1 251  ? 37.729  0.333   37.839  1.00 202.89 ? 251  LYS A NZ  1 
ATOM   1868  N  N   . ALA A 1 252  ? 42.883  -1.434  32.164  1.00 202.86 ? 252  ALA A N   1 
ATOM   1869  C  CA  . ALA A 1 252  ? 43.025  -2.617  31.321  1.00 209.89 ? 252  ALA A CA  1 
ATOM   1870  C  C   . ALA A 1 252  ? 43.224  -3.892  32.141  1.00 213.45 ? 252  ALA A C   1 
ATOM   1871  O  O   . ALA A 1 252  ? 43.775  -3.852  33.230  1.00 213.83 ? 252  ALA A O   1 
ATOM   1872  C  CB  . ALA A 1 252  ? 44.180  -2.429  30.348  1.00 212.95 ? 252  ALA A CB  1 
ATOM   1873  N  N   . ARG A 1 253  ? 42.796  -5.027  31.601  1.00 254.15 ? 253  ARG A N   1 
ATOM   1874  C  CA  . ARG A 1 253  ? 42.912  -6.292  32.315  1.00 259.18 ? 253  ARG A CA  1 
ATOM   1875  C  C   . ARG A 1 253  ? 42.557  -7.471  31.420  1.00 258.54 ? 253  ARG A C   1 
ATOM   1876  O  O   . ARG A 1 253  ? 41.573  -7.429  30.679  1.00 258.97 ? 253  ARG A O   1 
ATOM   1877  C  CB  . ARG A 1 253  ? 41.984  -6.293  33.522  1.00 262.99 ? 253  ARG A CB  1 
ATOM   1878  C  CG  . ARG A 1 253  ? 40.511  -6.196  33.154  1.00 268.91 ? 253  ARG A CG  1 
ATOM   1879  C  CD  . ARG A 1 253  ? 39.627  -6.719  34.274  1.00 276.77 ? 253  ARG A CD  1 
ATOM   1880  N  NE  . ARG A 1 253  ? 40.074  -8.022  34.773  1.00 288.56 ? 253  ARG A NE  1 
ATOM   1881  C  CZ  . ARG A 1 253  ? 40.909  -8.190  35.797  1.00 293.54 ? 253  ARG A CZ  1 
ATOM   1882  N  NH1 . ARG A 1 253  ? 41.399  -7.141  36.436  1.00 290.74 ? 253  ARG A NH1 1 
ATOM   1883  N  NH2 . ARG A 1 253  ? 41.259  -9.404  36.187  1.00 299.82 ? 253  ARG A NH2 1 
ATOM   1884  N  N   . TYR A 1 254  ? 43.357  -8.529  31.496  1.00 211.24 ? 254  TYR A N   1 
ATOM   1885  C  CA  . TYR A 1 254  ? 43.109  -9.716  30.688  1.00 209.35 ? 254  TYR A CA  1 
ATOM   1886  C  C   . TYR A 1 254  ? 41.855  -10.444 31.187  1.00 205.14 ? 254  TYR A C   1 
ATOM   1887  O  O   . TYR A 1 254  ? 41.332  -10.145 32.261  1.00 200.01 ? 254  TYR A O   1 
ATOM   1888  C  CB  . TYR A 1 254  ? 44.341  -10.641 30.656  1.00 214.27 ? 254  TYR A CB  1 
ATOM   1889  C  CG  . TYR A 1 254  ? 45.633  -9.946  30.235  1.00 214.04 ? 254  TYR A CG  1 
ATOM   1890  C  CD1 . TYR A 1 254  ? 46.819  -10.138 30.945  1.00 216.73 ? 254  TYR A CD1 1 
ATOM   1891  C  CD2 . TYR A 1 254  ? 45.659  -9.090  29.135  1.00 212.80 ? 254  TYR A CD2 1 
ATOM   1892  C  CE1 . TYR A 1 254  ? 47.994  -9.500  30.566  1.00 216.04 ? 254  TYR A CE1 1 
ATOM   1893  C  CE2 . TYR A 1 254  ? 46.827  -8.446  28.749  1.00 212.98 ? 254  TYR A CE2 1 
ATOM   1894  C  CZ  . TYR A 1 254  ? 47.990  -8.654  29.466  1.00 214.77 ? 254  TYR A CZ  1 
ATOM   1895  O  OH  . TYR A 1 254  ? 49.147  -8.011  29.080  1.00 213.97 ? 254  TYR A OH  1 
ATOM   1896  N  N   . PHE A 1 255  ? 41.362  -11.380 30.385  1.00 215.73 ? 255  PHE A N   1 
ATOM   1897  C  CA  . PHE A 1 255  ? 40.168  -12.142 30.734  1.00 219.31 ? 255  PHE A CA  1 
ATOM   1898  C  C   . PHE A 1 255  ? 40.432  -13.131 31.868  1.00 229.38 ? 255  PHE A C   1 
ATOM   1899  O  O   . PHE A 1 255  ? 39.515  -13.468 32.616  1.00 228.01 ? 255  PHE A O   1 
ATOM   1900  C  CB  . PHE A 1 255  ? 39.580  -12.841 29.494  1.00 222.63 ? 255  PHE A CB  1 
ATOM   1901  C  CG  . PHE A 1 255  ? 38.774  -11.922 28.611  1.00 217.67 ? 255  PHE A CG  1 
ATOM   1902  C  CD1 . PHE A 1 255  ? 37.442  -12.194 28.329  1.00 217.19 ? 255  PHE A CD1 1 
ATOM   1903  C  CD2 . PHE A 1 255  ? 39.341  -10.765 28.097  1.00 213.70 ? 255  PHE A CD2 1 
ATOM   1904  C  CE1 . PHE A 1 255  ? 36.699  -11.341 27.533  1.00 214.29 ? 255  PHE A CE1 1 
ATOM   1905  C  CE2 . PHE A 1 255  ? 38.603  -9.907  27.305  1.00 210.32 ? 255  PHE A CE2 1 
ATOM   1906  C  CZ  . PHE A 1 255  ? 37.279  -10.197 27.020  1.00 211.05 ? 255  PHE A CZ  1 
ATOM   1907  N  N   . TYR A 1 256  ? 41.683  -13.575 32.003  1.00 271.30 ? 256  TYR A N   1 
ATOM   1908  C  CA  . TYR A 1 256  ? 42.063  -14.513 33.070  1.00 284.47 ? 256  TYR A CA  1 
ATOM   1909  C  C   . TYR A 1 256  ? 42.356  -13.858 34.438  1.00 294.78 ? 256  TYR A C   1 
ATOM   1910  O  O   . TYR A 1 256  ? 43.323  -14.213 35.126  1.00 302.14 ? 256  TYR A O   1 
ATOM   1911  C  CB  . TYR A 1 256  ? 43.204  -15.448 32.630  1.00 286.73 ? 256  TYR A CB  1 
ATOM   1912  C  CG  . TYR A 1 256  ? 44.363  -14.775 31.927  1.00 280.94 ? 256  TYR A CG  1 
ATOM   1913  C  CD1 . TYR A 1 256  ? 45.420  -14.237 32.647  1.00 278.33 ? 256  TYR A CD1 1 
ATOM   1914  C  CD2 . TYR A 1 256  ? 44.408  -14.699 30.542  1.00 280.00 ? 256  TYR A CD2 1 
ATOM   1915  C  CE1 . TYR A 1 256  ? 46.479  -13.626 32.010  1.00 274.49 ? 256  TYR A CE1 1 
ATOM   1916  C  CE2 . TYR A 1 256  ? 45.466  -14.093 29.896  1.00 277.44 ? 256  TYR A CE2 1 
ATOM   1917  C  CZ  . TYR A 1 256  ? 46.498  -13.558 30.637  1.00 274.45 ? 256  TYR A CZ  1 
ATOM   1918  O  OH  . TYR A 1 256  ? 47.554  -12.952 30.003  1.00 271.14 ? 256  TYR A OH  1 
ATOM   1919  N  N   . ASN A 1 257  ? 41.489  -12.916 34.813  1.00 374.48 ? 257  ASN A N   1 
ATOM   1920  C  CA  . ASN A 1 257  ? 41.536  -12.197 36.095  1.00 376.61 ? 257  ASN A CA  1 
ATOM   1921  C  C   . ASN A 1 257  ? 42.918  -11.743 36.570  1.00 372.18 ? 257  ASN A C   1 
ATOM   1922  O  O   . ASN A 1 257  ? 43.285  -11.945 37.725  1.00 371.23 ? 257  ASN A O   1 
ATOM   1923  C  CB  . ASN A 1 257  ? 40.795  -12.955 37.203  1.00 389.75 ? 257  ASN A CB  1 
ATOM   1924  C  CG  . ASN A 1 257  ? 41.319  -14.354 37.402  1.00 407.54 ? 257  ASN A CG  1 
ATOM   1925  O  OD1 . ASN A 1 257  ? 41.314  -15.165 36.479  1.00 415.47 ? 257  ASN A OD1 1 
ATOM   1926  N  ND2 . ASN A 1 257  ? 41.771  -14.651 38.613  1.00 411.69 ? 257  ASN A ND2 1 
ATOM   1927  N  N   . LYS A 1 258  ? 43.665  -11.114 35.669  1.00 261.69 ? 258  LYS A N   1 
ATOM   1928  C  CA  . LYS A 1 258  ? 44.966  -10.538 35.986  1.00 261.13 ? 258  LYS A CA  1 
ATOM   1929  C  C   . LYS A 1 258  ? 45.146  -9.270  35.163  1.00 249.78 ? 258  LYS A C   1 
ATOM   1930  O  O   . LYS A 1 258  ? 45.225  -9.314  33.939  1.00 251.98 ? 258  LYS A O   1 
ATOM   1931  C  CB  . LYS A 1 258  ? 46.103  -11.533 35.697  1.00 270.35 ? 258  LYS A CB  1 
ATOM   1932  C  CG  . LYS A 1 258  ? 46.653  -12.285 36.922  1.00 275.81 ? 258  LYS A CG  1 
ATOM   1933  C  CD  . LYS A 1 258  ? 47.618  -11.428 37.752  1.00 274.44 ? 258  LYS A CD  1 
ATOM   1934  C  CE  . LYS A 1 258  ? 48.224  -12.217 38.914  1.00 278.75 ? 258  LYS A CE  1 
ATOM   1935  N  NZ  . LYS A 1 258  ? 49.074  -11.378 39.811  1.00 276.41 ? 258  LYS A NZ  1 
ATOM   1936  N  N   . VAL A 1 259  ? 45.201  -8.136  35.845  1.00 246.77 ? 259  VAL A N   1 
ATOM   1937  C  CA  . VAL A 1 259  ? 45.391  -6.859  35.183  1.00 236.86 ? 259  VAL A CA  1 
ATOM   1938  C  C   . VAL A 1 259  ? 46.666  -6.865  34.364  1.00 236.25 ? 259  VAL A C   1 
ATOM   1939  O  O   . VAL A 1 259  ? 47.574  -7.645  34.624  1.00 238.38 ? 259  VAL A O   1 
ATOM   1940  C  CB  . VAL A 1 259  ? 45.530  -5.718  36.207  1.00 226.66 ? 259  VAL A CB  1 
ATOM   1941  C  CG1 . VAL A 1 259  ? 44.478  -5.839  37.303  1.00 224.50 ? 259  VAL A CG1 1 
ATOM   1942  C  CG2 . VAL A 1 259  ? 46.934  -5.705  36.810  1.00 229.16 ? 259  VAL A CG2 1 
ATOM   1943  N  N   . VAL A 1 260  ? 46.734  -5.980  33.379  1.00 227.17 ? 260  VAL A N   1 
ATOM   1944  C  CA  . VAL A 1 260  ? 47.971  -5.751  32.647  1.00 229.93 ? 260  VAL A CA  1 
ATOM   1945  C  C   . VAL A 1 260  ? 48.975  -5.066  33.560  1.00 230.77 ? 260  VAL A C   1 
ATOM   1946  O  O   . VAL A 1 260  ? 48.594  -4.455  34.553  1.00 227.55 ? 260  VAL A O   1 
ATOM   1947  C  CB  . VAL A 1 260  ? 47.742  -4.832  31.428  1.00 225.27 ? 260  VAL A CB  1 
ATOM   1948  C  CG1 . VAL A 1 260  ? 49.060  -4.524  30.726  1.00 227.35 ? 260  VAL A CG1 1 
ATOM   1949  C  CG2 . VAL A 1 260  ? 46.749  -5.458  30.457  1.00 225.35 ? 260  VAL A CG2 1 
ATOM   1950  N  N   . THR A 1 261  ? 50.257  -5.179  33.236  1.00 174.62 ? 261  THR A N   1 
ATOM   1951  C  CA  . THR A 1 261  ? 51.249  -4.297  33.834  1.00 176.36 ? 261  THR A CA  1 
ATOM   1952  C  C   . THR A 1 261  ? 51.730  -3.348  32.740  1.00 177.12 ? 261  THR A C   1 
ATOM   1953  O  O   . THR A 1 261  ? 50.953  -2.520  32.280  1.00 176.42 ? 261  THR A O   1 
ATOM   1954  C  CB  . THR A 1 261  ? 52.394  -5.061  34.523  1.00 180.73 ? 261  THR A CB  1 
ATOM   1955  O  OG1 . THR A 1 261  ? 51.838  -6.135  35.288  1.00 183.62 ? 261  THR A OG1 1 
ATOM   1956  C  CG2 . THR A 1 261  ? 53.190  -4.134  35.459  1.00 180.11 ? 261  THR A CG2 1 
ATOM   1957  N  N   . GLU A 1 262  ? 52.974  -3.451  32.293  1.00 319.05 ? 262  GLU A N   1 
ATOM   1958  C  CA  . GLU A 1 262  ? 53.407  -2.493  31.284  1.00 322.76 ? 262  GLU A CA  1 
ATOM   1959  C  C   . GLU A 1 262  ? 52.505  -2.544  30.066  1.00 322.54 ? 262  GLU A C   1 
ATOM   1960  O  O   . GLU A 1 262  ? 52.142  -3.620  29.579  1.00 323.57 ? 262  GLU A O   1 
ATOM   1961  C  CB  . GLU A 1 262  ? 54.868  -2.675  30.872  1.00 332.83 ? 262  GLU A CB  1 
ATOM   1962  C  CG  . GLU A 1 262  ? 55.339  -1.588  29.895  1.00 340.02 ? 262  GLU A CG  1 
ATOM   1963  C  CD  . GLU A 1 262  ? 56.725  -1.840  29.330  1.00 350.51 ? 262  GLU A CD  1 
ATOM   1964  O  OE1 . GLU A 1 262  ? 56.933  -1.617  28.117  1.00 354.78 ? 262  GLU A OE1 1 
ATOM   1965  O  OE2 . GLU A 1 262  ? 57.607  -2.260  30.101  1.00 354.24 ? 262  GLU A OE2 1 
ATOM   1966  N  N   . ALA A 1 263  ? 52.131  -1.360  29.595  1.00 255.74 ? 263  ALA A N   1 
ATOM   1967  C  CA  . ALA A 1 263  ? 51.381  -1.197  28.346  1.00 257.53 ? 263  ALA A CA  1 
ATOM   1968  C  C   . ALA A 1 263  ? 51.534  0.250   27.873  1.00 253.47 ? 263  ALA A C   1 
ATOM   1969  O  O   . ALA A 1 263  ? 51.608  1.163   28.691  1.00 252.10 ? 263  ALA A O   1 
ATOM   1970  C  CB  . ALA A 1 263  ? 49.911  -1.526  28.556  1.00 258.75 ? 263  ALA A CB  1 
ATOM   1971  N  N   . ASP A 1 264  ? 51.588  0.449   26.563  1.00 328.44 ? 264  ASP A N   1 
ATOM   1972  C  CA  . ASP A 1 264  ? 51.661  1.809   26.096  1.00 327.03 ? 264  ASP A CA  1 
ATOM   1973  C  C   . ASP A 1 264  ? 50.238  2.380   26.025  1.00 323.09 ? 264  ASP A C   1 
ATOM   1974  O  O   . ASP A 1 264  ? 49.285  1.704   25.603  1.00 320.28 ? 264  ASP A O   1 
ATOM   1975  C  CB  . ASP A 1 264  ? 52.369  1.918   24.735  1.00 335.76 ? 264  ASP A CB  1 
ATOM   1976  C  CG  . ASP A 1 264  ? 53.528  2.995   24.694  1.00 342.53 ? 264  ASP A CG  1 
ATOM   1977  O  OD1 . ASP A 1 264  ? 53.283  3.948   25.504  1.00 340.97 ? 264  ASP A OD1 1 
ATOM   1978  O  OD2 . ASP A 1 264  ? 54.521  2.848   23.880  1.00 349.49 ? 264  ASP A OD2 1 
ATOM   1979  N  N   . VAL A 1 265  ? 50.113  3.646   26.409  1.00 200.43 ? 265  VAL A N   1 
ATOM   1980  C  CA  . VAL A 1 265  ? 48.824  4.306   26.487  1.00 192.86 ? 265  VAL A CA  1 
ATOM   1981  C  C   . VAL A 1 265  ? 48.742  5.382   25.405  1.00 194.61 ? 265  VAL A C   1 
ATOM   1982  O  O   . VAL A 1 265  ? 49.616  6.235   25.307  1.00 197.98 ? 265  VAL A O   1 
ATOM   1983  C  CB  . VAL A 1 265  ? 48.653  4.912   27.897  1.00 179.79 ? 265  VAL A CB  1 
ATOM   1984  C  CG1 . VAL A 1 265  ? 47.388  5.726   27.980  1.00 172.36 ? 265  VAL A CG1 1 
ATOM   1985  C  CG2 . VAL A 1 265  ? 48.605  3.804   28.907  1.00 177.96 ? 265  VAL A CG2 1 
ATOM   1986  N  N   . TYR A 1 266  ? 47.713  5.338   24.571  1.00 294.56 ? 266  TYR A N   1 
ATOM   1987  C  CA  . TYR A 1 266  ? 47.519  6.406   23.590  1.00 296.99 ? 266  TYR A CA  1 
ATOM   1988  C  C   . TYR A 1 266  ? 46.106  6.946   23.693  1.00 288.32 ? 266  TYR A C   1 
ATOM   1989  O  O   . TYR A 1 266  ? 45.146  6.222   23.442  1.00 287.56 ? 266  TYR A O   1 
ATOM   1990  C  CB  . TYR A 1 266  ? 47.797  5.922   22.160  1.00 309.65 ? 266  TYR A CB  1 
ATOM   1991  C  CG  . TYR A 1 266  ? 49.268  5.868   21.799  1.00 323.85 ? 266  TYR A CG  1 
ATOM   1992  C  CD1 . TYR A 1 266  ? 50.102  4.924   22.377  1.00 331.08 ? 266  TYR A CD1 1 
ATOM   1993  C  CD2 . TYR A 1 266  ? 49.821  6.754   20.878  1.00 332.59 ? 266  TYR A CD2 1 
ATOM   1994  C  CE1 . TYR A 1 266  ? 51.449  4.861   22.057  1.00 339.35 ? 266  TYR A CE1 1 
ATOM   1995  C  CE2 . TYR A 1 266  ? 51.174  6.700   20.550  1.00 341.15 ? 266  TYR A CE2 1 
ATOM   1996  C  CZ  . TYR A 1 266  ? 51.983  5.751   21.144  1.00 344.56 ? 266  TYR A CZ  1 
ATOM   1997  O  OH  . TYR A 1 266  ? 53.321  5.690   20.824  1.00 348.62 ? 266  TYR A OH  1 
ATOM   1998  N  N   . ILE A 1 267  ? 45.966  8.212   24.067  1.00 161.99 ? 267  ILE A N   1 
ATOM   1999  C  CA  . ILE A 1 267  ? 44.625  8.758   24.194  1.00 152.38 ? 267  ILE A CA  1 
ATOM   2000  C  C   . ILE A 1 267  ? 44.325  10.005  23.377  1.00 151.97 ? 267  ILE A C   1 
ATOM   2001  O  O   . ILE A 1 267  ? 44.872  11.083  23.618  1.00 154.73 ? 267  ILE A O   1 
ATOM   2002  C  CB  . ILE A 1 267  ? 44.281  9.075   25.628  1.00 149.09 ? 267  ILE A CB  1 
ATOM   2003  C  CG1 . ILE A 1 267  ? 44.790  7.977   26.552  1.00 146.46 ? 267  ILE A CG1 1 
ATOM   2004  C  CG2 . ILE A 1 267  ? 42.787  9.221   25.732  1.00 145.91 ? 267  ILE A CG2 1 
ATOM   2005  C  CD1 . ILE A 1 267  ? 44.575  8.291   27.987  1.00 140.60 ? 267  ILE A CD1 1 
ATOM   2006  N  N   . THR A 1 268  ? 43.426  9.869   22.420  1.00 219.19 ? 268  THR A N   1 
ATOM   2007  C  CA  . THR A 1 268  ? 42.992  11.055  21.712  1.00 218.40 ? 268  THR A CA  1 
ATOM   2008  C  C   . THR A 1 268  ? 41.800  11.708  22.417  1.00 214.62 ? 268  THR A C   1 
ATOM   2009  O  O   . THR A 1 268  ? 41.264  11.166  23.384  1.00 212.61 ? 268  THR A O   1 
ATOM   2010  C  CB  . THR A 1 268  ? 42.731  10.781  20.201  1.00 225.44 ? 268  THR A CB  1 
ATOM   2011  O  OG1 . THR A 1 268  ? 41.760  9.739   20.038  1.00 225.82 ? 268  THR A OG1 1 
ATOM   2012  C  CG2 . THR A 1 268  ? 44.024  10.368  19.516  1.00 230.84 ? 268  THR A CG2 1 
ATOM   2013  N  N   . PHE A 1 269  ? 41.420  12.892  21.951  1.00 242.57 ? 269  PHE A N   1 
ATOM   2014  C  CA  . PHE A 1 269  ? 40.198  13.539  22.402  1.00 234.70 ? 269  PHE A CA  1 
ATOM   2015  C  C   . PHE A 1 269  ? 39.597  14.248  21.237  1.00 229.19 ? 269  PHE A C   1 
ATOM   2016  O  O   . PHE A 1 269  ? 40.209  14.337  20.179  1.00 234.37 ? 269  PHE A O   1 
ATOM   2017  C  CB  . PHE A 1 269  ? 40.491  14.571  23.452  1.00 233.22 ? 269  PHE A CB  1 
ATOM   2018  C  CG  . PHE A 1 269  ? 41.345  14.076  24.530  1.00 232.43 ? 269  PHE A CG  1 
ATOM   2019  C  CD1 . PHE A 1 269  ? 42.699  14.303  24.494  1.00 234.97 ? 269  PHE A CD1 1 
ATOM   2020  C  CD2 . PHE A 1 269  ? 40.799  13.367  25.582  1.00 228.69 ? 269  PHE A CD2 1 
ATOM   2021  C  CE1 . PHE A 1 269  ? 43.497  13.842  25.494  1.00 234.77 ? 269  PHE A CE1 1 
ATOM   2022  C  CE2 . PHE A 1 269  ? 41.589  12.903  26.591  1.00 228.24 ? 269  PHE A CE2 1 
ATOM   2023  C  CZ  . PHE A 1 269  ? 42.943  13.139  26.553  1.00 231.50 ? 269  PHE A CZ  1 
ATOM   2024  N  N   . GLY A 1 270  ? 38.403  14.783  21.431  1.00 265.59 ? 270  GLY A N   1 
ATOM   2025  C  CA  . GLY A 1 270  ? 37.763  15.498  20.352  1.00 265.19 ? 270  GLY A CA  1 
ATOM   2026  C  C   . GLY A 1 270  ? 36.594  16.356  20.765  1.00 257.23 ? 270  GLY A C   1 
ATOM   2027  O  O   . GLY A 1 270  ? 36.112  16.260  21.893  1.00 256.04 ? 270  GLY A O   1 
ATOM   2028  N  N   . ILE A 1 271  ? 36.171  17.221  19.849  1.00 177.11 ? 271  ILE A N   1 
ATOM   2029  C  CA  . ILE A 1 271  ? 34.889  17.874  19.955  1.00 166.79 ? 271  ILE A CA  1 
ATOM   2030  C  C   . ILE A 1 271  ? 33.924  17.084  19.059  1.00 170.01 ? 271  ILE A C   1 
ATOM   2031  O  O   . ILE A 1 271  ? 34.217  15.950  18.690  1.00 173.44 ? 271  ILE A O   1 
ATOM   2032  C  CB  . ILE A 1 271  ? 34.981  19.364  19.611  1.00 161.85 ? 271  ILE A CB  1 
ATOM   2033  C  CG1 . ILE A 1 271  ? 36.320  19.926  20.084  1.00 160.03 ? 271  ILE A CG1 1 
ATOM   2034  C  CG2 . ILE A 1 271  ? 33.904  20.103  20.341  1.00 158.07 ? 271  ILE A CG2 1 
ATOM   2035  C  CD1 . ILE A 1 271  ? 36.422  20.029  21.568  1.00 152.74 ? 271  ILE A CD1 1 
ATOM   2036  N  N   . ARG A 1 272  ? 32.775  17.655  18.729  1.00 213.44 ? 272  ARG A N   1 
ATOM   2037  C  CA  . ARG A 1 272  ? 31.706  16.881  18.118  1.00 222.00 ? 272  ARG A CA  1 
ATOM   2038  C  C   . ARG A 1 272  ? 30.491  17.745  18.208  1.00 228.14 ? 272  ARG A C   1 
ATOM   2039  O  O   . ARG A 1 272  ? 30.544  18.810  18.803  1.00 225.11 ? 272  ARG A O   1 
ATOM   2040  C  CB  . ARG A 1 272  ? 31.469  15.619  18.925  1.00 217.92 ? 272  ARG A CB  1 
ATOM   2041  C  CG  . ARG A 1 272  ? 30.382  14.709  18.415  1.00 218.59 ? 272  ARG A CG  1 
ATOM   2042  C  CD  . ARG A 1 272  ? 30.528  13.418  19.178  1.00 216.56 ? 272  ARG A CD  1 
ATOM   2043  N  NE  . ARG A 1 272  ? 29.781  12.303  18.615  1.00 218.95 ? 272  ARG A NE  1 
ATOM   2044  C  CZ  . ARG A 1 272  ? 30.179  11.035  18.698  1.00 221.82 ? 272  ARG A CZ  1 
ATOM   2045  N  NH1 . ARG A 1 272  ? 31.325  10.738  19.305  1.00 222.08 ? 272  ARG A NH1 1 
ATOM   2046  N  NH2 . ARG A 1 272  ? 29.441  10.062  18.168  1.00 224.11 ? 272  ARG A NH2 1 
ATOM   2047  N  N   . GLU A 1 273  ? 29.387  17.314  17.631  1.00 195.94 ? 273  GLU A N   1 
ATOM   2048  C  CA  . GLU A 1 273  ? 28.194  18.106  17.808  1.00 201.22 ? 273  GLU A CA  1 
ATOM   2049  C  C   . GLU A 1 273  ? 27.207  17.363  18.666  1.00 198.82 ? 273  GLU A C   1 
ATOM   2050  O  O   . GLU A 1 273  ? 26.747  17.877  19.688  1.00 195.26 ? 273  GLU A O   1 
ATOM   2051  C  CB  . GLU A 1 273  ? 27.582  18.542  16.475  1.00 213.60 ? 273  GLU A CB  1 
ATOM   2052  C  CG  . GLU A 1 273  ? 28.094  19.904  16.011  1.00 220.55 ? 273  GLU A CG  1 
ATOM   2053  C  CD  . GLU A 1 273  ? 28.607  20.754  17.171  1.00 219.17 ? 273  GLU A CD  1 
ATOM   2054  O  OE1 . GLU A 1 273  ? 27.766  21.333  17.895  1.00 216.06 ? 273  GLU A OE1 1 
ATOM   2055  O  OE2 . GLU A 1 273  ? 29.847  20.826  17.358  1.00 220.78 ? 273  GLU A OE2 1 
ATOM   2056  N  N   . ASP A 1 274  ? 26.906  16.138  18.259  1.00 303.51 ? 274  ASP A N   1 
ATOM   2057  C  CA  . ASP A 1 274  ? 25.908  15.336  18.944  1.00 301.38 ? 274  ASP A CA  1 
ATOM   2058  C  C   . ASP A 1 274  ? 26.319  13.875  18.956  1.00 304.53 ? 274  ASP A C   1 
ATOM   2059  O  O   . ASP A 1 274  ? 27.466  13.550  18.650  1.00 304.35 ? 274  ASP A O   1 
ATOM   2060  C  CB  . ASP A 1 274  ? 24.515  15.514  18.309  1.00 305.13 ? 274  ASP A CB  1 
ATOM   2061  C  CG  . ASP A 1 274  ? 24.504  15.288  16.794  1.00 342.71 ? 274  ASP A CG  1 
ATOM   2062  O  OD1 . ASP A 1 274  ? 23.490  14.761  16.289  1.00 345.83 ? 274  ASP A OD1 1 
ATOM   2063  O  OD2 . ASP A 1 274  ? 25.486  15.646  16.109  1.00 345.27 ? 274  ASP A OD2 1 
ATOM   2064  N  N   . LEU A 1 275  ? 25.384  13.007  19.342  1.00 206.89 ? 275  LEU A N   1 
ATOM   2065  C  CA  . LEU A 1 275  ? 25.606  11.559  19.325  1.00 212.46 ? 275  LEU A CA  1 
ATOM   2066  C  C   . LEU A 1 275  ? 25.061  10.871  18.039  1.00 226.14 ? 275  LEU A C   1 
ATOM   2067  O  O   . LEU A 1 275  ? 25.133  9.645   17.902  1.00 228.84 ? 275  LEU A O   1 
ATOM   2068  C  CB  . LEU A 1 275  ? 25.069  10.883  20.617  1.00 204.25 ? 275  LEU A CB  1 
ATOM   2069  C  CG  . LEU A 1 275  ? 25.687  11.132  22.014  1.00 195.43 ? 275  LEU A CG  1 
ATOM   2070  C  CD1 . LEU A 1 275  ? 25.430  9.955   22.958  1.00 192.32 ? 275  LEU A CD1 1 
ATOM   2071  C  CD2 . LEU A 1 275  ? 27.179  11.424  21.958  1.00 194.60 ? 275  LEU A CD2 1 
ATOM   2072  N  N   . LYS A 1 276  ? 24.522  11.665  17.108  1.00 201.65 ? 276  LYS A N   1 
ATOM   2073  C  CA  . LYS A 1 276  ? 24.039  11.158  15.814  1.00 213.15 ? 276  LYS A CA  1 
ATOM   2074  C  C   . LYS A 1 276  ? 25.004  11.572  14.685  1.00 226.04 ? 276  LYS A C   1 
ATOM   2075  O  O   . LYS A 1 276  ? 24.719  11.380  13.499  1.00 235.28 ? 276  LYS A O   1 
ATOM   2076  C  CB  . LYS A 1 276  ? 22.605  11.653  15.529  1.00 208.84 ? 276  LYS A CB  1 
ATOM   2077  C  CG  . LYS A 1 276  ? 21.810  10.812  14.513  1.00 210.10 ? 276  LYS A CG  1 
ATOM   2078  C  CD  . LYS A 1 276  ? 20.426  11.411  14.179  1.00 205.73 ? 276  LYS A CD  1 
ATOM   2079  C  CE  . LYS A 1 276  ? 20.491  12.546  13.133  1.00 201.29 ? 276  LYS A CE  1 
ATOM   2080  N  NZ  . LYS A 1 276  ? 20.938  12.135  11.753  1.00 205.96 ? 276  LYS A NZ  1 
ATOM   2081  N  N   . ASP A 1 277  ? 26.141  12.147  15.079  1.00 225.02 ? 277  ASP A N   1 
ATOM   2082  C  CA  . ASP A 1 277  ? 27.189  12.601  14.161  1.00 236.82 ? 277  ASP A CA  1 
ATOM   2083  C  C   . ASP A 1 277  ? 28.351  11.596  14.153  1.00 241.10 ? 277  ASP A C   1 
ATOM   2084  O  O   . ASP A 1 277  ? 29.069  11.466  15.146  1.00 238.30 ? 277  ASP A O   1 
ATOM   2085  C  CB  . ASP A 1 277  ? 27.680  13.996  14.595  1.00 239.61 ? 277  ASP A CB  1 
ATOM   2086  C  CG  . ASP A 1 277  ? 28.627  14.640  13.588  1.00 250.92 ? 277  ASP A CG  1 
ATOM   2087  O  OD1 . ASP A 1 277  ? 28.763  14.109  12.474  1.00 259.84 ? 277  ASP A OD1 1 
ATOM   2088  O  OD2 . ASP A 1 277  ? 29.233  15.688  13.906  1.00 250.37 ? 277  ASP A OD2 1 
ATOM   2089  N  N   . ASP A 1 278  ? 28.530  10.889  13.034  1.00 310.31 ? 278  ASP A N   1 
ATOM   2090  C  CA  . ASP A 1 278  ? 29.592  9.881   12.892  1.00 311.38 ? 278  ASP A CA  1 
ATOM   2091  C  C   . ASP A 1 278  ? 31.002  10.482  12.786  1.00 307.37 ? 278  ASP A C   1 
ATOM   2092  O  O   . ASP A 1 278  ? 31.995  9.752   12.692  1.00 308.26 ? 278  ASP A O   1 
ATOM   2093  C  CB  . ASP A 1 278  ? 29.305  8.923   11.713  1.00 350.60 ? 278  ASP A CB  1 
ATOM   2094  C  CG  . ASP A 1 278  ? 28.791  9.641   10.461  1.00 353.46 ? 278  ASP A CG  1 
ATOM   2095  O  OD1 . ASP A 1 278  ? 28.902  10.881  10.380  1.00 350.18 ? 278  ASP A OD1 1 
ATOM   2096  O  OD2 . ASP A 1 278  ? 28.276  8.956   9.548   1.00 358.69 ? 278  ASP A OD2 1 
ATOM   2097  N  N   . GLN A 1 279  ? 31.069  11.815  12.826  1.00 197.72 ? 279  GLN A N   1 
ATOM   2098  C  CA  . GLN A 1 279  ? 32.315  12.563  12.649  1.00 193.20 ? 279  GLN A CA  1 
ATOM   2099  C  C   . GLN A 1 279  ? 32.472  13.745  13.603  1.00 178.60 ? 279  GLN A C   1 
ATOM   2100  O  O   . GLN A 1 279  ? 31.606  14.615  13.737  1.00 172.32 ? 279  GLN A O   1 
ATOM   2101  C  CB  . GLN A 1 279  ? 32.468  13.057  11.209  1.00 204.45 ? 279  GLN A CB  1 
ATOM   2102  C  CG  . GLN A 1 279  ? 33.676  13.973  10.980  1.00 208.98 ? 279  GLN A CG  1 
ATOM   2103  C  CD  . GLN A 1 279  ? 35.009  13.247  11.103  1.00 212.82 ? 279  GLN A CD  1 
ATOM   2104  O  OE1 . GLN A 1 279  ? 35.984  13.805  11.610  1.00 210.36 ? 279  GLN A OE1 1 
ATOM   2105  N  NE2 . GLN A 1 279  ? 35.055  11.998  10.642  1.00 218.92 ? 279  GLN A NE2 1 
ATOM   2106  N  N   . LYS A 1 280  ? 33.637  13.770  14.225  1.00 212.17 ? 280  LYS A N   1 
ATOM   2107  C  CA  . LYS A 1 280  ? 33.931  14.691  15.293  1.00 201.92 ? 280  LYS A CA  1 
ATOM   2108  C  C   . LYS A 1 280  ? 35.344  15.211  15.101  1.00 203.34 ? 280  LYS A C   1 
ATOM   2109  O  O   . LYS A 1 280  ? 36.301  14.446  15.008  1.00 207.68 ? 280  LYS A O   1 
ATOM   2110  C  CB  . LYS A 1 280  ? 33.808  13.976  16.641  1.00 192.14 ? 280  LYS A CB  1 
ATOM   2111  C  CG  . LYS A 1 280  ? 34.587  12.649  16.747  1.00 188.69 ? 280  LYS A CG  1 
ATOM   2112  C  CD  . LYS A 1 280  ? 33.790  11.461  16.186  1.00 188.19 ? 280  LYS A CD  1 
ATOM   2113  C  CE  . LYS A 1 280  ? 34.515  10.126  16.356  1.00 188.04 ? 280  LYS A CE  1 
ATOM   2114  N  NZ  . LYS A 1 280  ? 33.681  8.996   15.847  1.00 189.52 ? 280  LYS A NZ  1 
ATOM   2115  N  N   . GLU A 1 281  ? 35.465  16.524  15.050  1.00 172.73 ? 281  GLU A N   1 
ATOM   2116  C  CA  . GLU A 1 281  ? 36.720  17.151  14.691  1.00 176.24 ? 281  GLU A CA  1 
ATOM   2117  C  C   . GLU A 1 281  ? 37.735  17.155  15.832  1.00 166.73 ? 281  GLU A C   1 
ATOM   2118  O  O   . GLU A 1 281  ? 37.793  18.074  16.639  1.00 160.14 ? 281  GLU A O   1 
ATOM   2119  C  CB  . GLU A 1 281  ? 36.440  18.557  14.174  1.00 185.48 ? 281  GLU A CB  1 
ATOM   2120  C  CG  . GLU A 1 281  ? 35.085  18.663  13.455  1.00 198.65 ? 281  GLU A CG  1 
ATOM   2121  C  CD  . GLU A 1 281  ? 34.995  17.804  12.208  1.00 215.64 ? 281  GLU A CD  1 
ATOM   2122  O  OE1 . GLU A 1 281  ? 36.036  17.306  11.732  1.00 222.33 ? 281  GLU A OE1 1 
ATOM   2123  O  OE2 . GLU A 1 281  ? 33.871  17.632  11.701  1.00 221.42 ? 281  GLU A OE2 1 
ATOM   2124  N  N   . MET A 1 282  ? 38.548  16.113  15.861  1.00 170.74 ? 282  MET A N   1 
ATOM   2125  C  CA  . MET A 1 282  ? 39.604  15.984  16.837  1.00 168.84 ? 282  MET A CA  1 
ATOM   2126  C  C   . MET A 1 282  ? 40.342  17.267  17.165  1.00 170.40 ? 282  MET A C   1 
ATOM   2127  O  O   . MET A 1 282  ? 40.066  18.356  16.656  1.00 172.23 ? 282  MET A O   1 
ATOM   2128  C  CB  . MET A 1 282  ? 40.655  14.976  16.371  1.00 172.90 ? 282  MET A CB  1 
ATOM   2129  C  CG  . MET A 1 282  ? 40.223  13.523  16.327  1.00 173.17 ? 282  MET A CG  1 
ATOM   2130  S  SD  . MET A 1 282  ? 39.923  12.717  17.897  1.00 173.36 ? 282  MET A SD  1 
ATOM   2131  C  CE  . MET A 1 282  ? 38.142  12.577  17.770  1.00 146.96 ? 282  MET A CE  1 
ATOM   2132  N  N   . MET A 1 283  ? 41.326  17.060  18.029  1.00 204.89 ? 283  MET A N   1 
ATOM   2133  C  CA  . MET A 1 283  ? 42.120  18.087  18.663  1.00 211.24 ? 283  MET A CA  1 
ATOM   2134  C  C   . MET A 1 283  ? 43.525  17.542  18.586  1.00 225.03 ? 283  MET A C   1 
ATOM   2135  O  O   . MET A 1 283  ? 43.725  16.328  18.605  1.00 225.25 ? 283  MET A O   1 
ATOM   2136  C  CB  . MET A 1 283  ? 41.708  18.258  20.149  1.00 204.30 ? 283  MET A CB  1 
ATOM   2137  C  CG  . MET A 1 283  ? 40.243  18.775  20.376  1.00 214.18 ? 283  MET A CG  1 
ATOM   2138  S  SD  . MET A 1 283  ? 39.510  18.856  22.053  1.00 146.20 ? 283  MET A SD  1 
ATOM   2139  C  CE  . MET A 1 283  ? 39.556  17.133  22.501  1.00 140.34 ? 283  MET A CE  1 
ATOM   2140  N  N   . GLN A 1 284  ? 44.489  18.440  18.467  1.00 269.77 ? 284  GLN A N   1 
ATOM   2141  C  CA  . GLN A 1 284  ? 45.886  18.079  18.539  1.00 280.45 ? 284  GLN A CA  1 
ATOM   2142  C  C   . GLN A 1 284  ? 46.359  18.262  19.981  1.00 281.53 ? 284  GLN A C   1 
ATOM   2143  O  O   . GLN A 1 284  ? 45.609  18.738  20.829  1.00 277.87 ? 284  GLN A O   1 
ATOM   2144  C  CB  . GLN A 1 284  ? 46.698  18.937  17.570  1.00 287.16 ? 284  GLN A CB  1 
ATOM   2145  C  CG  . GLN A 1 284  ? 46.467  20.441  17.713  1.00 285.52 ? 284  GLN A CG  1 
ATOM   2146  C  CD  . GLN A 1 284  ? 45.188  20.943  17.036  1.00 283.38 ? 284  GLN A CD  1 
ATOM   2147  O  OE1 . GLN A 1 284  ? 44.179  20.239  16.960  1.00 279.26 ? 284  GLN A OE1 1 
ATOM   2148  N  NE2 . GLN A 1 284  ? 45.234  22.176  16.545  1.00 286.81 ? 284  GLN A NE2 1 
ATOM   2149  N  N   . THR A 1 285  ? 47.594  17.861  20.258  1.00 264.13 ? 285  THR A N   1 
ATOM   2150  C  CA  . THR A 1 285  ? 48.156  17.950  21.604  1.00 263.69 ? 285  THR A CA  1 
ATOM   2151  C  C   . THR A 1 285  ? 47.365  17.143  22.640  1.00 256.60 ? 285  THR A C   1 
ATOM   2152  O  O   . THR A 1 285  ? 47.275  17.529  23.808  1.00 251.75 ? 285  THR A O   1 
ATOM   2153  C  CB  . THR A 1 285  ? 48.270  19.403  22.072  1.00 266.73 ? 285  THR A CB  1 
ATOM   2154  O  OG1 . THR A 1 285  ? 48.586  20.237  20.953  1.00 273.06 ? 285  THR A OG1 1 
ATOM   2155  C  CG2 . THR A 1 285  ? 49.355  19.530  23.129  1.00 269.00 ? 285  THR A CG2 1 
ATOM   2156  N  N   . ALA A 1 286  ? 46.791  16.028  22.190  1.00 326.85 ? 286  ALA A N   1 
ATOM   2157  C  CA  . ALA A 1 286  ? 46.127  15.064  23.064  1.00 319.91 ? 286  ALA A CA  1 
ATOM   2158  C  C   . ALA A 1 286  ? 47.127  14.005  23.532  1.00 318.74 ? 286  ALA A C   1 
ATOM   2159  O  O   . ALA A 1 286  ? 47.620  13.210  22.734  1.00 319.57 ? 286  ALA A O   1 
ATOM   2160  C  CB  . ALA A 1 286  ? 44.958  14.418  22.344  1.00 319.19 ? 286  ALA A CB  1 
ATOM   2161  N  N   . MET A 1 287  ? 47.390  13.987  24.837  1.00 228.93 ? 287  MET A N   1 
ATOM   2162  C  CA  . MET A 1 287  ? 48.522  13.262  25.424  1.00 228.54 ? 287  MET A CA  1 
ATOM   2163  C  C   . MET A 1 287  ? 48.677  11.780  25.105  1.00 231.48 ? 287  MET A C   1 
ATOM   2164  O  O   . MET A 1 287  ? 47.850  10.939  25.478  1.00 228.71 ? 287  MET A O   1 
ATOM   2165  C  CB  . MET A 1 287  ? 48.561  13.449  26.938  1.00 221.77 ? 287  MET A CB  1 
ATOM   2166  C  CG  . MET A 1 287  ? 48.928  14.843  27.375  1.00 219.36 ? 287  MET A CG  1 
ATOM   2167  S  SD  . MET A 1 287  ? 48.492  15.123  29.112  1.00 254.72 ? 287  MET A SD  1 
ATOM   2168  C  CE  . MET A 1 287  ? 46.705  14.936  29.090  1.00 212.50 ? 287  MET A CE  1 
ATOM   2169  N  N   . GLN A 1 288  ? 49.786  11.494  24.432  1.00 438.38 ? 288  GLN A N   1 
ATOM   2170  C  CA  . GLN A 1 288  ? 50.292  10.145  24.248  1.00 446.01 ? 288  GLN A CA  1 
ATOM   2171  C  C   . GLN A 1 288  ? 51.024  9.685   25.508  1.00 446.67 ? 288  GLN A C   1 
ATOM   2172  O  O   . GLN A 1 288  ? 51.508  10.500  26.296  1.00 444.64 ? 288  GLN A O   1 
ATOM   2173  C  CB  . GLN A 1 288  ? 51.244  10.097  23.039  1.00 454.79 ? 288  GLN A CB  1 
ATOM   2174  C  CG  . GLN A 1 288  ? 52.350  11.166  23.051  1.00 459.70 ? 288  GLN A CG  1 
ATOM   2175  C  CD  . GLN A 1 288  ? 53.322  11.057  21.877  1.00 466.02 ? 288  GLN A CD  1 
ATOM   2176  O  OE1 . GLN A 1 288  ? 53.440  10.007  21.243  1.00 468.86 ? 288  GLN A OE1 1 
ATOM   2177  N  NE2 . GLN A 1 288  ? 54.031  12.147  21.593  1.00 468.47 ? 288  GLN A NE2 1 
ATOM   2178  N  N   . ASN A 1 289  ? 51.062  8.372   25.701  1.00 287.01 ? 289  ASN A N   1 
ATOM   2179  C  CA  . ASN A 1 289  ? 51.942  7.710   26.666  1.00 289.07 ? 289  ASN A CA  1 
ATOM   2180  C  C   . ASN A 1 289  ? 52.015  8.266   28.097  1.00 280.15 ? 289  ASN A C   1 
ATOM   2181  O  O   . ASN A 1 289  ? 52.532  9.358   28.343  1.00 276.13 ? 289  ASN A O   1 
ATOM   2182  C  CB  . ASN A 1 289  ? 53.361  7.557   26.078  1.00 299.50 ? 289  ASN A CB  1 
ATOM   2183  C  CG  . ASN A 1 289  ? 53.356  7.042   24.633  1.00 309.13 ? 289  ASN A CG  1 
ATOM   2184  O  OD1 . ASN A 1 289  ? 52.313  6.671   24.095  1.00 312.40 ? 289  ASN A OD1 1 
ATOM   2185  N  ND2 . ASN A 1 289  ? 54.528  7.028   24.004  1.00 313.27 ? 289  ASN A ND2 1 
ATOM   2186  N  N   . THR A 1 290  ? 51.491  7.479   29.028  1.00 209.66 ? 290  THR A N   1 
ATOM   2187  C  CA  . THR A 1 290  ? 51.860  7.568   30.445  1.00 205.12 ? 290  THR A CA  1 
ATOM   2188  C  C   . THR A 1 290  ? 51.983  6.135   30.966  1.00 202.21 ? 290  THR A C   1 
ATOM   2189  O  O   . THR A 1 290  ? 51.993  5.867   32.177  1.00 201.98 ? 290  THR A O   1 
ATOM   2190  C  CB  . THR A 1 290  ? 50.900  8.458   31.288  1.00 170.87 ? 290  THR A CB  1 
ATOM   2191  O  OG1 . THR A 1 290  ? 51.379  9.804   31.244  1.00 170.14 ? 290  THR A OG1 1 
ATOM   2192  C  CG2 . THR A 1 290  ? 50.822  8.014   32.763  1.00 168.13 ? 290  THR A CG2 1 
ATOM   2193  N  N   . MET A 1 291  ? 52.089  5.223   30.001  1.00 310.80 ? 291  MET A N   1 
ATOM   2194  C  CA  . MET A 1 291  ? 52.290  3.806   30.257  1.00 308.57 ? 291  MET A CA  1 
ATOM   2195  C  C   . MET A 1 291  ? 51.301  3.291   31.285  1.00 300.95 ? 291  MET A C   1 
ATOM   2196  O  O   . MET A 1 291  ? 51.387  3.613   32.470  1.00 298.80 ? 291  MET A O   1 
ATOM   2197  C  CB  . MET A 1 291  ? 53.731  3.522   30.695  1.00 312.38 ? 291  MET A CB  1 
ATOM   2198  C  CG  . MET A 1 291  ? 54.771  3.752   29.606  1.00 316.73 ? 291  MET A CG  1 
ATOM   2199  S  SD  . MET A 1 291  ? 56.409  3.169   30.082  1.00 343.11 ? 291  MET A SD  1 
ATOM   2200  C  CE  . MET A 1 291  ? 56.489  3.779   31.758  1.00 336.71 ? 291  MET A CE  1 
ATOM   2201  N  N   . LEU A 1 292  ? 50.344  2.503   30.815  1.00 265.70 ? 292  LEU A N   1 
ATOM   2202  C  CA  . LEU A 1 292  ? 49.438  1.837   31.719  1.00 258.88 ? 292  LEU A CA  1 
ATOM   2203  C  C   . LEU A 1 292  ? 50.360  1.212   32.716  1.00 254.25 ? 292  LEU A C   1 
ATOM   2204  O  O   . LEU A 1 292  ? 51.366  0.613   32.344  1.00 256.82 ? 292  LEU A O   1 
ATOM   2205  C  CB  . LEU A 1 292  ? 48.661  0.741   30.998  1.00 259.76 ? 292  LEU A CB  1 
ATOM   2206  C  CG  . LEU A 1 292  ? 47.541  0.074   31.802  1.00 256.58 ? 292  LEU A CG  1 
ATOM   2207  C  CD1 . LEU A 1 292  ? 48.072  -0.662  33.021  1.00 257.75 ? 292  LEU A CD1 1 
ATOM   2208  C  CD2 . LEU A 1 292  ? 46.513  1.107   32.213  1.00 250.01 ? 292  LEU A CD2 1 
ATOM   2209  N  N   . ILE A 1 293  ? 50.038  1.354   33.987  1.00 224.90 ? 293  ILE A N   1 
ATOM   2210  C  CA  . ILE A 1 293  ? 50.924  0.826   35.003  1.00 220.24 ? 293  ILE A CA  1 
ATOM   2211  C  C   . ILE A 1 293  ? 50.200  0.076   36.129  1.00 217.05 ? 293  ILE A C   1 
ATOM   2212  O  O   . ILE A 1 293  ? 49.580  0.660   37.015  1.00 214.24 ? 293  ILE A O   1 
ATOM   2213  C  CB  . ILE A 1 293  ? 51.908  1.910   35.496  1.00 217.05 ? 293  ILE A CB  1 
ATOM   2214  C  CG1 . ILE A 1 293  ? 52.904  2.234   34.366  1.00 216.43 ? 293  ILE A CG1 1 
ATOM   2215  C  CG2 . ILE A 1 293  ? 52.621  1.434   36.753  1.00 217.86 ? 293  ILE A CG2 1 
ATOM   2216  C  CD1 . ILE A 1 293  ? 53.599  3.589   34.445  1.00 214.24 ? 293  ILE A CD1 1 
ATOM   2217  N  N   . ASN A 1 294  ? 50.319  -1.243  36.066  1.00 183.14 ? 294  ASN A N   1 
ATOM   2218  C  CA  . ASN A 1 294  ? 49.577  -2.166  36.908  1.00 183.71 ? 294  ASN A CA  1 
ATOM   2219  C  C   . ASN A 1 294  ? 48.070  -2.006  36.859  1.00 176.15 ? 294  ASN A C   1 
ATOM   2220  O  O   . ASN A 1 294  ? 47.427  -1.707  37.862  1.00 172.48 ? 294  ASN A O   1 
ATOM   2221  C  CB  . ASN A 1 294  ? 50.020  -2.120  38.351  1.00 189.30 ? 294  ASN A CB  1 
ATOM   2222  C  CG  . ASN A 1 294  ? 49.316  -3.167  39.174  1.00 196.62 ? 294  ASN A CG  1 
ATOM   2223  O  OD1 . ASN A 1 294  ? 48.330  -2.888  39.850  1.00 196.70 ? 294  ASN A OD1 1 
ATOM   2224  N  ND2 . ASN A 1 294  ? 49.790  -4.399  39.079  1.00 202.00 ? 294  ASN A ND2 1 
ATOM   2225  N  N   . GLY A 1 295  ? 47.506  -2.229  35.686  1.00 247.98 ? 295  GLY A N   1 
ATOM   2226  C  CA  . GLY A 1 295  ? 46.068  -2.231  35.559  1.00 242.18 ? 295  GLY A CA  1 
ATOM   2227  C  C   . GLY A 1 295  ? 45.482  -0.847  35.663  1.00 234.88 ? 295  GLY A C   1 
ATOM   2228  O  O   . GLY A 1 295  ? 44.262  -0.702  35.726  1.00 230.28 ? 295  GLY A O   1 
ATOM   2229  N  N   . ILE A 1 296  ? 46.349  0.165   35.695  1.00 181.32 ? 296  ILE A N   1 
ATOM   2230  C  CA  . ILE A 1 296  ? 45.907  1.558   35.560  1.00 173.35 ? 296  ILE A CA  1 
ATOM   2231  C  C   . ILE A 1 296  ? 46.988  2.562   35.056  1.00 177.37 ? 296  ILE A C   1 
ATOM   2232  O  O   . ILE A 1 296  ? 48.077  2.180   34.607  1.00 182.11 ? 296  ILE A O   1 
ATOM   2233  C  CB  . ILE A 1 296  ? 45.273  2.105   36.880  1.00 160.66 ? 296  ILE A CB  1 
ATOM   2234  C  CG1 . ILE A 1 296  ? 44.773  0.963   37.791  1.00 158.75 ? 296  ILE A CG1 1 
ATOM   2235  C  CG2 . ILE A 1 296  ? 44.203  3.157   36.565  1.00 150.89 ? 296  ILE A CG2 1 
ATOM   2236  C  CD1 . ILE A 1 296  ? 43.288  0.613   37.679  1.00 154.75 ? 296  ILE A CD1 1 
ATOM   2237  N  N   . ALA A 1 297  ? 46.597  3.839   35.073  1.00 184.33 ? 297  ALA A N   1 
ATOM   2238  C  CA  . ALA A 1 297  ? 47.439  5.035   34.946  1.00 183.32 ? 297  ALA A CA  1 
ATOM   2239  C  C   . ALA A 1 297  ? 46.403  6.164   34.993  1.00 180.95 ? 297  ALA A C   1 
ATOM   2240  O  O   . ALA A 1 297  ? 45.236  5.906   35.314  1.00 179.55 ? 297  ALA A O   1 
ATOM   2241  C  CB  . ALA A 1 297  ? 48.242  5.062   33.656  1.00 184.39 ? 297  ALA A CB  1 
ATOM   2242  N  N   . GLN A 1 298  ? 46.789  7.398   34.681  1.00 188.00 ? 298  GLN A N   1 
ATOM   2243  C  CA  . GLN A 1 298  ? 45.817  8.494   34.710  1.00 184.39 ? 298  GLN A CA  1 
ATOM   2244  C  C   . GLN A 1 298  ? 46.319  9.790   34.139  1.00 182.19 ? 298  GLN A C   1 
ATOM   2245  O  O   . GLN A 1 298  ? 47.506  9.934   33.830  1.00 185.74 ? 298  GLN A O   1 
ATOM   2246  C  CB  . GLN A 1 298  ? 45.420  8.806   36.136  1.00 185.49 ? 298  GLN A CB  1 
ATOM   2247  C  CG  . GLN A 1 298  ? 44.278  8.027   36.687  1.00 188.96 ? 298  GLN A CG  1 
ATOM   2248  C  CD  . GLN A 1 298  ? 44.014  8.425   38.127  1.00 192.42 ? 298  GLN A CD  1 
ATOM   2249  O  OE1 . GLN A 1 298  ? 44.519  9.446   38.603  1.00 194.51 ? 298  GLN A OE1 1 
ATOM   2250  N  NE2 . GLN A 1 298  ? 43.232  7.621   38.834  1.00 192.82 ? 298  GLN A NE2 1 
ATOM   2251  N  N   . VAL A 1 299  ? 45.390  10.739  34.046  1.00 132.31 ? 299  VAL A N   1 
ATOM   2252  C  CA  . VAL A 1 299  ? 45.703  12.121  33.690  1.00 127.61 ? 299  VAL A CA  1 
ATOM   2253  C  C   . VAL A 1 299  ? 44.566  13.098  34.051  1.00 126.49 ? 299  VAL A C   1 
ATOM   2254  O  O   . VAL A 1 299  ? 43.565  12.704  34.671  1.00 122.50 ? 299  VAL A O   1 
ATOM   2255  C  CB  . VAL A 1 299  ? 46.150  12.295  32.208  1.00 129.22 ? 299  VAL A CB  1 
ATOM   2256  C  CG1 . VAL A 1 299  ? 47.681  12.161  32.067  1.00 133.46 ? 299  VAL A CG1 1 
ATOM   2257  C  CG2 . VAL A 1 299  ? 45.418  11.320  31.301  1.00 129.14 ? 299  VAL A CG2 1 
ATOM   2258  N  N   . THR A 1 300  ? 44.752  14.366  33.671  1.00 179.51 ? 300  THR A N   1 
ATOM   2259  C  CA  . THR A 1 300  ? 43.865  15.470  34.040  1.00 175.33 ? 300  THR A CA  1 
ATOM   2260  C  C   . THR A 1 300  ? 43.975  16.591  33.005  1.00 180.69 ? 300  THR A C   1 
ATOM   2261  O  O   . THR A 1 300  ? 45.060  17.108  32.739  1.00 180.67 ? 300  THR A O   1 
ATOM   2262  C  CB  . THR A 1 300  ? 44.242  16.009  35.416  1.00 211.33 ? 300  THR A CB  1 
ATOM   2263  O  OG1 . THR A 1 300  ? 45.666  16.153  35.478  1.00 212.70 ? 300  THR A OG1 1 
ATOM   2264  C  CG2 . THR A 1 300  ? 43.789  15.048  36.512  1.00 209.86 ? 300  THR A CG2 1 
ATOM   2265  N  N   . PHE A 1 301  ? 42.848  16.989  32.439  1.00 149.67 ? 301  PHE A N   1 
ATOM   2266  C  CA  . PHE A 1 301  ? 42.885  17.531  31.089  1.00 159.41 ? 301  PHE A CA  1 
ATOM   2267  C  C   . PHE A 1 301  ? 42.353  18.960  30.992  1.00 166.92 ? 301  PHE A C   1 
ATOM   2268  O  O   . PHE A 1 301  ? 41.182  19.188  30.704  1.00 168.17 ? 301  PHE A O   1 
ATOM   2269  C  CB  . PHE A 1 301  ? 42.196  16.485  30.188  1.00 155.78 ? 301  PHE A CB  1 
ATOM   2270  C  CG  . PHE A 1 301  ? 41.623  16.989  28.911  1.00 152.32 ? 301  PHE A CG  1 
ATOM   2271  C  CD1 . PHE A 1 301  ? 42.389  17.046  27.781  1.00 154.41 ? 301  PHE A CD1 1 
ATOM   2272  C  CD2 . PHE A 1 301  ? 40.260  17.285  28.822  1.00 148.03 ? 301  PHE A CD2 1 
ATOM   2273  C  CE1 . PHE A 1 301  ? 41.818  17.461  26.608  1.00 154.96 ? 301  PHE A CE1 1 
ATOM   2274  C  CE2 . PHE A 1 301  ? 39.678  17.700  27.648  1.00 147.45 ? 301  PHE A CE2 1 
ATOM   2275  C  CZ  . PHE A 1 301  ? 40.451  17.789  26.544  1.00 151.84 ? 301  PHE A CZ  1 
ATOM   2276  N  N   . ASP A 1 302  ? 43.248  19.915  31.254  1.00 198.46 ? 302  ASP A N   1 
ATOM   2277  C  CA  . ASP A 1 302  ? 42.929  21.344  31.186  1.00 197.78 ? 302  ASP A CA  1 
ATOM   2278  C  C   . ASP A 1 302  ? 42.243  21.647  29.876  1.00 198.72 ? 302  ASP A C   1 
ATOM   2279  O  O   . ASP A 1 302  ? 42.895  21.852  28.859  1.00 200.28 ? 302  ASP A O   1 
ATOM   2280  C  CB  . ASP A 1 302  ? 44.186  22.228  31.342  1.00 202.75 ? 302  ASP A CB  1 
ATOM   2281  C  CG  . ASP A 1 302  ? 43.939  23.696  30.946  1.00 208.23 ? 302  ASP A CG  1 
ATOM   2282  O  OD1 . ASP A 1 302  ? 44.912  24.467  30.788  1.00 211.69 ? 302  ASP A OD1 1 
ATOM   2283  O  OD2 . ASP A 1 302  ? 42.766  24.080  30.792  1.00 209.35 ? 302  ASP A OD2 1 
ATOM   2284  N  N   . SER A 1 303  ? 40.919  21.687  29.921  1.00 204.16 ? 303  SER A N   1 
ATOM   2285  C  CA  . SER A 1 303  ? 40.103  21.850  28.731  1.00 203.35 ? 303  SER A CA  1 
ATOM   2286  C  C   . SER A 1 303  ? 40.429  23.140  27.953  1.00 206.98 ? 303  SER A C   1 
ATOM   2287  O  O   . SER A 1 303  ? 40.332  23.204  26.709  1.00 210.24 ? 303  SER A O   1 
ATOM   2288  C  CB  . SER A 1 303  ? 38.633  21.815  29.137  1.00 196.52 ? 303  SER A CB  1 
ATOM   2289  O  OG  . SER A 1 303  ? 38.337  20.599  29.800  1.00 191.02 ? 303  SER A OG  1 
ATOM   2290  N  N   . GLU A 1 304  ? 40.822  24.157  28.713  1.00 261.63 ? 304  GLU A N   1 
ATOM   2291  C  CA  . GLU A 1 304  ? 41.192  25.475  28.205  1.00 258.08 ? 304  GLU A CA  1 
ATOM   2292  C  C   . GLU A 1 304  ? 42.088  25.397  26.986  1.00 259.40 ? 304  GLU A C   1 
ATOM   2293  O  O   . GLU A 1 304  ? 41.657  25.598  25.834  1.00 259.85 ? 304  GLU A O   1 
ATOM   2294  C  CB  . GLU A 1 304  ? 41.974  26.193  29.300  1.00 255.45 ? 304  GLU A CB  1 
ATOM   2295  C  CG  . GLU A 1 304  ? 41.543  27.603  29.592  1.00 256.00 ? 304  GLU A CG  1 
ATOM   2296  C  CD  . GLU A 1 304  ? 42.263  28.163  30.787  1.00 256.29 ? 304  GLU A CD  1 
ATOM   2297  O  OE1 . GLU A 1 304  ? 43.304  27.580  31.169  1.00 258.18 ? 304  GLU A OE1 1 
ATOM   2298  O  OE2 . GLU A 1 304  ? 41.784  29.177  31.337  1.00 255.85 ? 304  GLU A OE2 1 
ATOM   2299  N  N   . THR A 1 305  ? 43.358  25.156  27.293  1.00 172.07 ? 305  THR A N   1 
ATOM   2300  C  CA  . THR A 1 305  ? 44.344  24.810  26.311  1.00 179.59 ? 305  THR A CA  1 
ATOM   2301  C  C   . THR A 1 305  ? 43.588  24.096  25.222  1.00 185.07 ? 305  THR A C   1 
ATOM   2302  O  O   . THR A 1 305  ? 43.047  24.730  24.329  1.00 185.70 ? 305  THR A O   1 
ATOM   2303  C  CB  . THR A 1 305  ? 45.390  23.840  26.915  1.00 177.56 ? 305  THR A CB  1 
ATOM   2304  O  OG1 . THR A 1 305  ? 45.655  24.197  28.281  1.00 173.84 ? 305  THR A OG1 1 
ATOM   2305  C  CG2 . THR A 1 305  ? 46.683  23.859  26.114  1.00 182.64 ? 305  THR A CG2 1 
ATOM   2306  N  N   . ALA A 1 306  ? 43.482  22.780  25.358  1.00 170.34 ? 306  ALA A N   1 
ATOM   2307  C  CA  . ALA A 1 306  ? 43.146  21.899  24.240  1.00 180.35 ? 306  ALA A CA  1 
ATOM   2308  C  C   . ALA A 1 306  ? 41.780  22.077  23.566  1.00 186.72 ? 306  ALA A C   1 
ATOM   2309  O  O   . ALA A 1 306  ? 40.968  21.153  23.547  1.00 186.54 ? 306  ALA A O   1 
ATOM   2310  C  CB  . ALA A 1 306  ? 43.377  20.448  24.620  1.00 176.25 ? 306  ALA A CB  1 
ATOM   2311  N  N   . VAL A 1 307  ? 41.565  23.266  22.999  1.00 431.97 ? 307  VAL A N   1 
ATOM   2312  C  CA  . VAL A 1 307  ? 40.498  23.540  22.032  1.00 445.86 ? 307  VAL A CA  1 
ATOM   2313  C  C   . VAL A 1 307  ? 40.702  24.903  21.360  1.00 463.75 ? 307  VAL A C   1 
ATOM   2314  O  O   . VAL A 1 307  ? 40.463  25.051  20.161  1.00 463.98 ? 307  VAL A O   1 
ATOM   2315  C  CB  . VAL A 1 307  ? 39.080  23.524  22.650  1.00 380.42 ? 307  VAL A CB  1 
ATOM   2316  C  CG1 . VAL A 1 307  ? 38.091  24.086  21.656  1.00 381.50 ? 307  VAL A CG1 1 
ATOM   2317  C  CG2 . VAL A 1 307  ? 38.655  22.123  23.033  1.00 377.24 ? 307  VAL A CG2 1 
ATOM   2318  N  N   . LYS A 1 308  ? 41.148  25.890  22.135  1.00 244.34 ? 308  LYS A N   1 
ATOM   2319  C  CA  . LYS A 1 308  ? 41.272  27.262  21.648  1.00 266.89 ? 308  LYS A CA  1 
ATOM   2320  C  C   . LYS A 1 308  ? 41.887  27.300  20.260  1.00 290.73 ? 308  LYS A C   1 
ATOM   2321  O  O   . LYS A 1 308  ? 41.171  27.370  19.269  1.00 293.90 ? 308  LYS A O   1 
ATOM   2322  C  CB  . LYS A 1 308  ? 42.071  28.126  22.630  1.00 266.47 ? 308  LYS A CB  1 
ATOM   2323  C  CG  . LYS A 1 308  ? 41.398  28.339  23.992  1.00 256.79 ? 308  LYS A CG  1 
ATOM   2324  C  CD  . LYS A 1 308  ? 42.270  29.195  24.893  1.00 254.78 ? 308  LYS A CD  1 
ATOM   2325  C  CE  . LYS A 1 308  ? 43.632  28.546  25.089  1.00 255.00 ? 308  LYS A CE  1 
ATOM   2326  N  NZ  . LYS A 1 308  ? 44.657  29.511  25.566  1.00 257.85 ? 308  LYS A NZ  1 
ATOM   2327  N  N   . GLU A 1 309  ? 43.208  27.243  20.181  1.00 328.45 ? 309  GLU A N   1 
ATOM   2328  C  CA  . GLU A 1 309  ? 43.847  27.202  18.876  1.00 345.72 ? 309  GLU A CA  1 
ATOM   2329  C  C   . GLU A 1 309  ? 43.514  25.889  18.167  1.00 335.47 ? 309  GLU A C   1 
ATOM   2330  O  O   . GLU A 1 309  ? 43.742  25.756  16.966  1.00 352.51 ? 309  GLU A O   1 
ATOM   2331  C  CB  . GLU A 1 309  ? 45.364  27.407  18.986  1.00 372.36 ? 309  GLU A CB  1 
ATOM   2332  C  CG  . GLU A 1 309  ? 46.147  27.267  17.668  1.00 403.00 ? 309  GLU A CG  1 
ATOM   2333  C  CD  . GLU A 1 309  ? 46.004  28.460  16.731  1.00 424.12 ? 309  GLU A CD  1 
ATOM   2334  O  OE1 . GLU A 1 309  ? 45.559  29.534  17.183  1.00 429.87 ? 309  GLU A OE1 1 
ATOM   2335  O  OE2 . GLU A 1 309  ? 46.349  28.323  15.537  1.00 435.55 ? 309  GLU A OE2 1 
ATOM   2336  N  N   . LEU A 1 310  ? 42.953  24.928  18.899  1.00 330.62 ? 310  LEU A N   1 
ATOM   2337  C  CA  . LEU A 1 310  ? 42.743  23.589  18.334  1.00 319.14 ? 310  LEU A CA  1 
ATOM   2338  C  C   . LEU A 1 310  ? 41.385  23.381  17.627  1.00 301.24 ? 310  LEU A C   1 
ATOM   2339  O  O   . LEU A 1 310  ? 41.094  22.293  17.122  1.00 298.46 ? 310  LEU A O   1 
ATOM   2340  C  CB  . LEU A 1 310  ? 43.027  22.497  19.380  1.00 318.61 ? 310  LEU A CB  1 
ATOM   2341  C  CG  . LEU A 1 310  ? 44.309  22.627  20.226  1.00 319.61 ? 310  LEU A CG  1 
ATOM   2342  C  CD1 . LEU A 1 310  ? 44.761  21.278  20.762  1.00 317.13 ? 310  LEU A CD1 1 
ATOM   2343  C  CD2 . LEU A 1 310  ? 45.444  23.275  19.456  1.00 326.62 ? 310  LEU A CD2 1 
ATOM   2344  N  N   . SER A 1 311  ? 40.577  24.439  17.597  1.00 302.32 ? 311  SER A N   1 
ATOM   2345  C  CA  . SER A 1 311  ? 39.344  24.506  16.807  1.00 289.22 ? 311  SER A CA  1 
ATOM   2346  C  C   . SER A 1 311  ? 38.680  25.873  17.029  1.00 282.86 ? 311  SER A C   1 
ATOM   2347  O  O   . SER A 1 311  ? 39.244  26.724  17.719  1.00 281.12 ? 311  SER A O   1 
ATOM   2348  C  CB  . SER A 1 311  ? 38.374  23.366  17.149  1.00 278.42 ? 311  SER A CB  1 
ATOM   2349  O  OG  . SER A 1 311  ? 38.713  22.166  16.475  1.00 276.13 ? 311  SER A OG  1 
ATOM   2350  N  N   . TYR A 1 312  ? 37.494  26.074  16.445  1.00 265.66 ? 312  TYR A N   1 
ATOM   2351  C  CA  . TYR A 1 312  ? 36.714  27.328  16.574  1.00 264.69 ? 312  TYR A CA  1 
ATOM   2352  C  C   . TYR A 1 312  ? 36.266  27.740  18.025  1.00 216.30 ? 312  TYR A C   1 
ATOM   2353  O  O   . TYR A 1 312  ? 35.609  28.785  18.195  1.00 214.37 ? 312  TYR A O   1 
ATOM   2354  C  CB  . TYR A 1 312  ? 35.484  27.303  15.625  1.00 267.25 ? 312  TYR A CB  1 
ATOM   2355  C  CG  . TYR A 1 312  ? 35.635  27.991  14.263  1.00 276.23 ? 312  TYR A CG  1 
ATOM   2356  C  CD1 . TYR A 1 312  ? 34.978  27.501  13.136  1.00 280.44 ? 312  TYR A CD1 1 
ATOM   2357  C  CD2 . TYR A 1 312  ? 36.405  29.138  14.112  1.00 281.00 ? 312  TYR A CD2 1 
ATOM   2358  C  CE1 . TYR A 1 312  ? 35.098  28.125  11.902  1.00 287.89 ? 312  TYR A CE1 1 
ATOM   2359  C  CE2 . TYR A 1 312  ? 36.529  29.766  12.879  1.00 288.25 ? 312  TYR A CE2 1 
ATOM   2360  C  CZ  . TYR A 1 312  ? 35.875  29.256  11.781  1.00 291.20 ? 312  TYR A CZ  1 
ATOM   2361  O  OH  . TYR A 1 312  ? 36.005  29.888  10.564  1.00 298.41 ? 312  TYR A OH  1 
ATOM   2362  N  N   . TYR A 1 313  ? 36.601  26.930  19.047  1.00 269.23 ? 313  TYR A N   1 
ATOM   2363  C  CA  . TYR A 1 313  ? 36.274  27.235  20.461  1.00 259.62 ? 313  TYR A CA  1 
ATOM   2364  C  C   . TYR A 1 313  ? 37.484  27.737  21.285  1.00 263.33 ? 313  TYR A C   1 
ATOM   2365  O  O   . TYR A 1 313  ? 38.410  26.977  21.553  1.00 264.53 ? 313  TYR A O   1 
ATOM   2366  C  CB  . TYR A 1 313  ? 35.636  26.023  21.185  1.00 245.98 ? 313  TYR A CB  1 
ATOM   2367  C  CG  . TYR A 1 313  ? 34.867  25.065  20.303  1.00 238.92 ? 313  TYR A CG  1 
ATOM   2368  C  CD1 . TYR A 1 313  ? 35.445  23.870  19.870  1.00 238.53 ? 313  TYR A CD1 1 
ATOM   2369  C  CD2 . TYR A 1 313  ? 33.566  25.353  19.896  1.00 235.85 ? 313  TYR A CD2 1 
ATOM   2370  C  CE1 . TYR A 1 313  ? 34.749  22.982  19.040  1.00 239.32 ? 313  TYR A CE1 1 
ATOM   2371  C  CE2 . TYR A 1 313  ? 32.859  24.477  19.065  1.00 236.33 ? 313  TYR A CE2 1 
ATOM   2372  C  CZ  . TYR A 1 313  ? 33.454  23.286  18.636  1.00 237.59 ? 313  TYR A CZ  1 
ATOM   2373  O  OH  . TYR A 1 313  ? 32.764  22.403  17.808  1.00 238.36 ? 313  TYR A OH  1 
ATOM   2374  N  N   . SER A 1 314  ? 37.472  29.009  21.683  1.00 261.83 ? 314  SER A N   1 
ATOM   2375  C  CA  . SER A 1 314  ? 38.495  29.557  22.583  1.00 261.44 ? 314  SER A CA  1 
ATOM   2376  C  C   . SER A 1 314  ? 37.860  29.926  23.927  1.00 249.12 ? 314  SER A C   1 
ATOM   2377  O  O   . SER A 1 314  ? 38.556  30.174  24.920  1.00 243.12 ? 314  SER A O   1 
ATOM   2378  C  CB  . SER A 1 314  ? 39.178  30.781  21.954  1.00 273.41 ? 314  SER A CB  1 
ATOM   2379  O  OG  . SER A 1 314  ? 38.223  31.684  21.415  1.00 277.16 ? 314  SER A OG  1 
ATOM   2380  N  N   . LEU A 1 315  ? 36.525  29.938  23.927  1.00 197.48 ? 315  LEU A N   1 
ATOM   2381  C  CA  . LEU A 1 315  ? 35.693  30.357  25.061  1.00 190.83 ? 315  LEU A CA  1 
ATOM   2382  C  C   . LEU A 1 315  ? 35.012  29.199  25.795  1.00 178.05 ? 315  LEU A C   1 
ATOM   2383  O  O   . LEU A 1 315  ? 34.369  28.351  25.157  1.00 176.28 ? 315  LEU A O   1 
ATOM   2384  C  CB  . LEU A 1 315  ? 34.604  31.313  24.570  1.00 197.95 ? 315  LEU A CB  1 
ATOM   2385  C  CG  . LEU A 1 315  ? 34.815  32.803  24.810  1.00 205.44 ? 315  LEU A CG  1 
ATOM   2386  C  CD1 . LEU A 1 315  ? 33.839  33.612  23.970  1.00 209.37 ? 315  LEU A CD1 1 
ATOM   2387  C  CD2 . LEU A 1 315  ? 34.692  33.132  26.303  1.00 198.27 ? 315  LEU A CD2 1 
ATOM   2388  N  N   . GLU A 1 316  ? 35.144  29.186  27.129  1.00 148.98 ? 316  GLU A N   1 
ATOM   2389  C  CA  . GLU A 1 316  ? 34.366  28.279  27.965  1.00 139.52 ? 316  GLU A CA  1 
ATOM   2390  C  C   . GLU A 1 316  ? 32.969  28.383  27.369  1.00 133.19 ? 316  GLU A C   1 
ATOM   2391  O  O   . GLU A 1 316  ? 32.646  27.753  26.334  1.00 130.77 ? 316  GLU A O   1 
ATOM   2392  C  CB  . GLU A 1 316  ? 34.372  28.733  29.442  1.00 138.80 ? 316  GLU A CB  1 
ATOM   2393  C  CG  . GLU A 1 316  ? 34.315  27.592  30.487  1.00 140.53 ? 316  GLU A CG  1 
ATOM   2394  C  CD  . GLU A 1 316  ? 32.915  27.145  30.864  1.00 143.38 ? 316  GLU A CD  1 
ATOM   2395  O  OE1 . GLU A 1 316  ? 32.002  27.991  30.935  1.00 145.29 ? 316  GLU A OE1 1 
ATOM   2396  O  OE2 . GLU A 1 316  ? 32.739  25.937  31.121  1.00 142.91 ? 316  GLU A OE2 1 
ATOM   2397  N  N   . ASP A 1 317  ? 32.153  29.192  28.029  1.00 170.78 ? 317  ASP A N   1 
ATOM   2398  C  CA  . ASP A 1 317  ? 30.966  29.731  27.415  1.00 172.61 ? 317  ASP A CA  1 
ATOM   2399  C  C   . ASP A 1 317  ? 30.741  29.059  26.060  1.00 177.10 ? 317  ASP A C   1 
ATOM   2400  O  O   . ASP A 1 317  ? 29.917  28.140  25.951  1.00 173.45 ? 317  ASP A O   1 
ATOM   2401  C  CB  . ASP A 1 317  ? 31.185  31.230  27.239  1.00 177.04 ? 317  ASP A CB  1 
ATOM   2402  C  CG  . ASP A 1 317  ? 29.904  32.031  27.336  1.00 190.70 ? 317  ASP A CG  1 
ATOM   2403  O  OD1 . ASP A 1 317  ? 28.823  31.483  27.026  1.00 191.09 ? 317  ASP A OD1 1 
ATOM   2404  O  OD2 . ASP A 1 317  ? 29.986  33.220  27.717  1.00 191.47 ? 317  ASP A OD2 1 
ATOM   2405  N  N   . LEU A 1 318  ? 31.508  29.506  25.052  1.00 278.51 ? 318  LEU A N   1 
ATOM   2406  C  CA  . LEU A 1 318  ? 31.398  29.040  23.656  1.00 283.92 ? 318  LEU A CA  1 
ATOM   2407  C  C   . LEU A 1 318  ? 31.464  27.517  23.568  1.00 280.38 ? 318  LEU A C   1 
ATOM   2408  O  O   . LEU A 1 318  ? 31.818  26.951  22.527  1.00 281.29 ? 318  LEU A O   1 
ATOM   2409  C  CB  . LEU A 1 318  ? 32.466  29.678  22.735  1.00 291.78 ? 318  LEU A CB  1 
ATOM   2410  C  CG  . LEU A 1 318  ? 32.085  30.760  21.702  1.00 301.02 ? 318  LEU A CG  1 
ATOM   2411  C  CD1 . LEU A 1 318  ? 33.315  31.507  21.195  1.00 307.60 ? 318  LEU A CD1 1 
ATOM   2412  C  CD2 . LEU A 1 318  ? 31.289  30.204  20.523  1.00 306.37 ? 318  LEU A CD2 1 
ATOM   2413  N  N   . ASN A 1 319  ? 31.125  26.852  24.665  1.00 126.89 ? 319  ASN A N   1 
ATOM   2414  C  CA  . ASN A 1 319  ? 30.939  25.435  24.592  1.00 118.54 ? 319  ASN A CA  1 
ATOM   2415  C  C   . ASN A 1 319  ? 29.748  24.885  25.333  1.00 116.93 ? 319  ASN A C   1 
ATOM   2416  O  O   . ASN A 1 319  ? 29.667  24.999  26.540  1.00 119.24 ? 319  ASN A O   1 
ATOM   2417  C  CB  . ASN A 1 319  ? 32.182  24.730  25.038  1.00 117.77 ? 319  ASN A CB  1 
ATOM   2418  C  CG  . ASN A 1 319  ? 32.269  23.378  24.426  1.00 123.91 ? 319  ASN A CG  1 
ATOM   2419  O  OD1 . ASN A 1 319  ? 31.605  23.098  23.411  1.00 127.37 ? 319  ASN A OD1 1 
ATOM   2420  N  ND2 . ASN A 1 319  ? 33.064  22.506  25.035  1.00 125.83 ? 319  ASN A ND2 1 
ATOM   2421  N  N   . ASN A 1 320  ? 28.827  24.281  24.594  1.00 162.31 ? 320  ASN A N   1 
ATOM   2422  C  CA  . ASN A 1 320  ? 27.685  23.607  25.191  1.00 158.74 ? 320  ASN A CA  1 
ATOM   2423  C  C   . ASN A 1 320  ? 27.395  22.369  24.407  1.00 161.85 ? 320  ASN A C   1 
ATOM   2424  O  O   . ASN A 1 320  ? 26.305  21.785  24.485  1.00 161.25 ? 320  ASN A O   1 
ATOM   2425  C  CB  . ASN A 1 320  ? 26.470  24.503  25.233  1.00 158.63 ? 320  ASN A CB  1 
ATOM   2426  C  CG  . ASN A 1 320  ? 26.563  25.510  26.332  1.00 159.40 ? 320  ASN A CG  1 
ATOM   2427  O  OD1 . ASN A 1 320  ? 25.705  25.558  27.207  1.00 156.61 ? 320  ASN A OD1 1 
ATOM   2428  N  ND2 . ASN A 1 320  ? 27.632  26.301  26.328  1.00 162.60 ? 320  ASN A ND2 1 
ATOM   2429  N  N   . LYS A 1 321  ? 28.411  22.007  23.634  1.00 219.37 ? 321  LYS A N   1 
ATOM   2430  C  CA  . LYS A 1 321  ? 28.475  20.766  22.894  1.00 223.15 ? 321  LYS A CA  1 
ATOM   2431  C  C   . LYS A 1 321  ? 29.398  19.799  23.626  1.00 218.46 ? 321  LYS A C   1 
ATOM   2432  O  O   . LYS A 1 321  ? 29.713  19.999  24.791  1.00 214.42 ? 321  LYS A O   1 
ATOM   2433  C  CB  . LYS A 1 321  ? 28.999  21.036  21.492  1.00 234.68 ? 321  LYS A CB  1 
ATOM   2434  C  CG  . LYS A 1 321  ? 30.244  21.908  21.459  1.00 241.09 ? 321  LYS A CG  1 
ATOM   2435  C  CD  . LYS A 1 321  ? 30.700  22.211  20.018  1.00 252.49 ? 321  LYS A CD  1 
ATOM   2436  C  CE  . LYS A 1 321  ? 29.807  23.239  19.305  1.00 256.49 ? 321  LYS A CE  1 
ATOM   2437  N  NZ  . LYS A 1 321  ? 30.239  23.555  17.902  1.00 263.52 ? 321  LYS A NZ  1 
ATOM   2438  N  N   . TYR A 1 322  ? 29.845  18.759  22.940  1.00 179.78 ? 322  TYR A N   1 
ATOM   2439  C  CA  . TYR A 1 322  ? 30.429  17.606  23.617  1.00 177.48 ? 322  TYR A CA  1 
ATOM   2440  C  C   . TYR A 1 322  ? 31.950  17.572  23.781  1.00 180.94 ? 322  TYR A C   1 
ATOM   2441  O  O   . TYR A 1 322  ? 32.658  18.492  23.344  1.00 185.29 ? 322  TYR A O   1 
ATOM   2442  C  CB  . TYR A 1 322  ? 29.930  16.321  22.949  1.00 177.95 ? 322  TYR A CB  1 
ATOM   2443  C  CG  . TYR A 1 322  ? 28.474  16.091  23.201  1.00 176.08 ? 322  TYR A CG  1 
ATOM   2444  C  CD1 . TYR A 1 322  ? 27.985  14.826  23.487  1.00 174.07 ? 322  TYR A CD1 1 
ATOM   2445  C  CD2 . TYR A 1 322  ? 27.591  17.157  23.196  1.00 179.46 ? 322  TYR A CD2 1 
ATOM   2446  C  CE1 . TYR A 1 322  ? 26.636  14.632  23.748  1.00 176.76 ? 322  TYR A CE1 1 
ATOM   2447  C  CE2 . TYR A 1 322  ? 26.256  16.983  23.451  1.00 181.01 ? 322  TYR A CE2 1 
ATOM   2448  C  CZ  . TYR A 1 322  ? 25.774  15.722  23.733  1.00 181.07 ? 322  TYR A CZ  1 
ATOM   2449  O  OH  . TYR A 1 322  ? 24.428  15.569  23.999  1.00 182.77 ? 322  TYR A OH  1 
ATOM   2450  N  N   . LEU A 1 323  ? 32.409  16.488  24.430  1.00 132.95 ? 323  LEU A N   1 
ATOM   2451  C  CA  . LEU A 1 323  ? 33.835  16.112  24.597  1.00 137.03 ? 323  LEU A CA  1 
ATOM   2452  C  C   . LEU A 1 323  ? 34.054  14.581  24.407  1.00 142.49 ? 323  LEU A C   1 
ATOM   2453  O  O   . LEU A 1 323  ? 33.750  13.815  25.312  1.00 141.39 ? 323  LEU A O   1 
ATOM   2454  C  CB  . LEU A 1 323  ? 34.343  16.557  25.972  1.00 133.47 ? 323  LEU A CB  1 
ATOM   2455  C  CG  . LEU A 1 323  ? 35.833  16.674  26.291  1.00 135.16 ? 323  LEU A CG  1 
ATOM   2456  C  CD1 . LEU A 1 323  ? 36.374  15.387  26.827  1.00 135.03 ? 323  LEU A CD1 1 
ATOM   2457  C  CD2 . LEU A 1 323  ? 36.602  17.090  25.088  1.00 140.00 ? 323  LEU A CD2 1 
ATOM   2458  N  N   . TYR A 1 324  ? 34.589  14.161  23.243  1.00 161.30 ? 324  TYR A N   1 
ATOM   2459  C  CA  . TYR A 1 324  ? 34.770  12.740  22.857  1.00 168.18 ? 324  TYR A CA  1 
ATOM   2460  C  C   . TYR A 1 324  ? 36.138  12.202  23.214  1.00 169.76 ? 324  TYR A C   1 
ATOM   2461  O  O   . TYR A 1 324  ? 37.167  12.838  22.922  1.00 170.49 ? 324  TYR A O   1 
ATOM   2462  C  CB  . TYR A 1 324  ? 34.553  12.520  21.347  1.00 177.74 ? 324  TYR A CB  1 
ATOM   2463  C  CG  . TYR A 1 324  ? 35.213  11.252  20.771  1.00 186.41 ? 324  TYR A CG  1 
ATOM   2464  C  CD1 . TYR A 1 324  ? 34.446  10.215  20.237  1.00 191.58 ? 324  TYR A CD1 1 
ATOM   2465  C  CD2 . TYR A 1 324  ? 36.608  11.103  20.738  1.00 190.25 ? 324  TYR A CD2 1 
ATOM   2466  C  CE1 . TYR A 1 324  ? 35.054  9.055   19.690  1.00 196.66 ? 324  TYR A CE1 1 
ATOM   2467  C  CE2 . TYR A 1 324  ? 37.225  9.950   20.201  1.00 195.21 ? 324  TYR A CE2 1 
ATOM   2468  C  CZ  . TYR A 1 324  ? 36.449  8.932   19.678  1.00 197.60 ? 324  TYR A CZ  1 
ATOM   2469  O  OH  . TYR A 1 324  ? 37.065  7.805   19.150  1.00 200.88 ? 324  TYR A OH  1 
ATOM   2470  N  N   . ILE A 1 325  ? 36.132  11.010  23.816  1.00 150.93 ? 325  ILE A N   1 
ATOM   2471  C  CA  . ILE A 1 325  ? 37.357  10.333  24.251  1.00 149.43 ? 325  ILE A CA  1 
ATOM   2472  C  C   . ILE A 1 325  ? 37.563  8.946   23.602  1.00 151.46 ? 325  ILE A C   1 
ATOM   2473  O  O   . ILE A 1 325  ? 36.621  8.179   23.390  1.00 151.59 ? 325  ILE A O   1 
ATOM   2474  C  CB  . ILE A 1 325  ? 37.437  10.175  25.805  1.00 143.08 ? 325  ILE A CB  1 
ATOM   2475  C  CG1 . ILE A 1 325  ? 37.189  11.488  26.515  1.00 140.28 ? 325  ILE A CG1 1 
ATOM   2476  C  CG2 . ILE A 1 325  ? 38.811  9.789   26.230  1.00 143.54 ? 325  ILE A CG2 1 
ATOM   2477  C  CD1 . ILE A 1 325  ? 37.629  11.444  27.917  1.00 136.37 ? 325  ILE A CD1 1 
ATOM   2478  N  N   . ALA A 1 326  ? 38.824  8.635   23.321  1.00 161.89 ? 326  ALA A N   1 
ATOM   2479  C  CA  . ALA A 1 326  ? 39.218  7.353   22.768  1.00 165.44 ? 326  ALA A CA  1 
ATOM   2480  C  C   . ALA A 1 326  ? 40.667  7.085   23.133  1.00 166.96 ? 326  ALA A C   1 
ATOM   2481  O  O   . ALA A 1 326  ? 41.564  7.900   22.882  1.00 166.61 ? 326  ALA A O   1 
ATOM   2482  C  CB  . ALA A 1 326  ? 39.049  7.355   21.276  1.00 168.28 ? 326  ALA A CB  1 
ATOM   2483  N  N   . VAL A 1 327  ? 40.873  5.941   23.766  1.00 147.66 ? 327  VAL A N   1 
ATOM   2484  C  CA  . VAL A 1 327  ? 42.202  5.478   24.123  1.00 151.18 ? 327  VAL A CA  1 
ATOM   2485  C  C   . VAL A 1 327  ? 42.546  4.315   23.182  1.00 157.84 ? 327  VAL A C   1 
ATOM   2486  O  O   . VAL A 1 327  ? 41.670  3.761   22.495  1.00 161.35 ? 327  VAL A O   1 
ATOM   2487  C  CB  . VAL A 1 327  ? 42.291  4.985   25.629  1.00 144.40 ? 327  VAL A CB  1 
ATOM   2488  C  CG1 . VAL A 1 327  ? 43.722  4.695   26.023  1.00 146.71 ? 327  VAL A CG1 1 
ATOM   2489  C  CG2 . VAL A 1 327  ? 41.693  5.985   26.604  1.00 137.39 ? 327  VAL A CG2 1 
ATOM   2490  N  N   . THR A 1 328  ? 43.833  3.981   23.133  1.00 191.22 ? 328  THR A N   1 
ATOM   2491  C  CA  . THR A 1 328  ? 44.308  2.691   22.644  1.00 197.63 ? 328  THR A CA  1 
ATOM   2492  C  C   . THR A 1 328  ? 45.390  2.247   23.651  1.00 199.01 ? 328  THR A C   1 
ATOM   2493  O  O   . THR A 1 328  ? 46.278  3.027   24.027  1.00 195.25 ? 328  THR A O   1 
ATOM   2494  C  CB  . THR A 1 328  ? 44.811  2.748   21.155  1.00 204.81 ? 328  THR A CB  1 
ATOM   2495  O  OG1 . THR A 1 328  ? 43.733  3.132   20.290  1.00 206.71 ? 328  THR A OG1 1 
ATOM   2496  C  CG2 . THR A 1 328  ? 45.334  1.398   20.682  1.00 209.26 ? 328  THR A CG2 1 
ATOM   2497  N  N   . VAL A 1 329  ? 45.251  1.015   24.135  1.00 190.61 ? 329  VAL A N   1 
ATOM   2498  C  CA  . VAL A 1 329  ? 46.209  0.403   25.048  1.00 194.80 ? 329  VAL A CA  1 
ATOM   2499  C  C   . VAL A 1 329  ? 46.730  -0.897  24.433  1.00 208.85 ? 329  VAL A C   1 
ATOM   2500  O  O   . VAL A 1 329  ? 46.061  -1.934  24.483  1.00 215.08 ? 329  VAL A O   1 
ATOM   2501  C  CB  . VAL A 1 329  ? 45.561  0.078   26.400  1.00 186.04 ? 329  VAL A CB  1 
ATOM   2502  C  CG1 . VAL A 1 329  ? 46.629  -0.178  27.449  1.00 184.19 ? 329  VAL A CG1 1 
ATOM   2503  C  CG2 . VAL A 1 329  ? 44.647  1.209   26.827  1.00 179.42 ? 329  VAL A CG2 1 
ATOM   2504  N  N   . ILE A 1 330  ? 47.909  -0.827  23.817  1.00 242.37 ? 330  ILE A N   1 
ATOM   2505  C  CA  . ILE A 1 330  ? 48.578  -2.015  23.296  1.00 253.49 ? 330  ILE A CA  1 
ATOM   2506  C  C   . ILE A 1 330  ? 49.498  -2.550  24.404  1.00 262.04 ? 330  ILE A C   1 
ATOM   2507  O  O   . ILE A 1 330  ? 50.316  -1.810  24.960  1.00 258.73 ? 330  ILE A O   1 
ATOM   2508  C  CB  . ILE A 1 330  ? 49.333  -1.741  21.943  1.00 268.70 ? 330  ILE A CB  1 
ATOM   2509  C  CG1 . ILE A 1 330  ? 50.446  -0.712  22.099  1.00 268.10 ? 330  ILE A CG1 1 
ATOM   2510  C  CG2 . ILE A 1 330  ? 48.406  -1.183  20.898  1.00 267.39 ? 330  ILE A CG2 1 
ATOM   2511  C  CD1 . ILE A 1 330  ? 50.901  -0.132  20.756  1.00 271.55 ? 330  ILE A CD1 1 
ATOM   2512  N  N   . GLU A 1 331  ? 49.328  -3.825  24.747  1.00 303.86 ? 331  GLU A N   1 
ATOM   2513  C  CA  . GLU A 1 331  ? 50.040  -4.439  25.869  1.00 314.73 ? 331  GLU A CA  1 
ATOM   2514  C  C   . GLU A 1 331  ? 51.535  -4.599  25.602  1.00 324.92 ? 331  GLU A C   1 
ATOM   2515  O  O   . GLU A 1 331  ? 51.937  -4.945  24.494  1.00 329.96 ? 331  GLU A O   1 
ATOM   2516  C  CB  . GLU A 1 331  ? 49.426  -5.798  26.194  1.00 317.72 ? 331  GLU A CB  1 
ATOM   2517  C  CG  . GLU A 1 331  ? 50.407  -6.781  26.793  1.00 320.25 ? 331  GLU A CG  1 
ATOM   2518  C  CD  . GLU A 1 331  ? 50.072  -8.219  26.448  1.00 325.95 ? 331  GLU A CD  1 
ATOM   2519  O  OE1 . GLU A 1 331  ? 49.048  -8.450  25.772  1.00 327.68 ? 331  GLU A OE1 1 
ATOM   2520  O  OE2 . GLU A 1 331  ? 50.836  -9.119  26.852  1.00 328.45 ? 331  GLU A OE2 1 
ATOM   2521  N  N   . SER A 1 332  ? 52.356  -4.370  26.623  1.00 277.42 ? 332  SER A N   1 
ATOM   2522  C  CA  . SER A 1 332  ? 53.812  -4.373  26.452  1.00 286.77 ? 332  SER A CA  1 
ATOM   2523  C  C   . SER A 1 332  ? 54.432  -5.748  26.282  1.00 297.65 ? 332  SER A C   1 
ATOM   2524  O  O   . SER A 1 332  ? 55.417  -5.908  25.559  1.00 300.66 ? 332  SER A O   1 
ATOM   2525  C  CB  . SER A 1 332  ? 54.503  -3.690  27.626  1.00 285.18 ? 332  SER A CB  1 
ATOM   2526  O  OG  . SER A 1 332  ? 55.895  -3.964  27.603  1.00 288.98 ? 332  SER A OG  1 
ATOM   2527  N  N   . THR A 1 333  ? 53.883  -6.733  26.978  1.00 266.30 ? 333  THR A N   1 
ATOM   2528  C  CA  . THR A 1 333  ? 54.446  -8.071  26.925  1.00 275.26 ? 333  THR A CA  1 
ATOM   2529  C  C   . THR A 1 333  ? 54.174  -8.759  25.584  1.00 281.55 ? 333  THR A C   1 
ATOM   2530  O  O   . THR A 1 333  ? 55.108  -9.155  24.894  1.00 285.99 ? 333  THR A O   1 
ATOM   2531  C  CB  . THR A 1 333  ? 53.959  -8.935  28.102  1.00 276.53 ? 333  THR A CB  1 
ATOM   2532  O  OG1 . THR A 1 333  ? 53.381  -10.145 27.604  1.00 281.28 ? 333  THR A OG1 1 
ATOM   2533  C  CG2 . THR A 1 333  ? 52.926  -8.178  28.921  1.00 271.64 ? 333  THR A CG2 1 
ATOM   2534  N  N   . GLY A 1 334  ? 52.903  -8.873  25.205  1.00 303.71 ? 334  GLY A N   1 
ATOM   2535  C  CA  . GLY A 1 334  ? 52.515  -9.624  24.018  1.00 307.56 ? 334  GLY A CA  1 
ATOM   2536  C  C   . GLY A 1 334  ? 52.687  -8.945  22.667  1.00 306.10 ? 334  GLY A C   1 
ATOM   2537  O  O   . GLY A 1 334  ? 52.975  -9.606  21.671  1.00 314.17 ? 334  GLY A O   1 
ATOM   2538  N  N   . GLY A 1 335  ? 52.510  -7.629  22.622  1.00 288.46 ? 335  GLY A N   1 
ATOM   2539  C  CA  . GLY A 1 335  ? 52.576  -6.902  21.367  1.00 281.10 ? 335  GLY A CA  1 
ATOM   2540  C  C   . GLY A 1 335  ? 51.198  -6.722  20.759  1.00 273.07 ? 335  GLY A C   1 
ATOM   2541  O  O   . GLY A 1 335  ? 51.052  -6.246  19.632  1.00 273.82 ? 335  GLY A O   1 
ATOM   2542  N  N   . PHE A 1 336  ? 50.183  -7.119  21.518  1.00 246.13 ? 336  PHE A N   1 
ATOM   2543  C  CA  . PHE A 1 336  ? 48.795  -6.951  21.114  1.00 233.73 ? 336  PHE A CA  1 
ATOM   2544  C  C   . PHE A 1 336  ? 48.426  -5.479  20.992  1.00 221.33 ? 336  PHE A C   1 
ATOM   2545  O  O   . PHE A 1 336  ? 49.265  -4.590  21.136  1.00 219.68 ? 336  PHE A O   1 
ATOM   2546  C  CB  . PHE A 1 336  ? 47.862  -7.563  22.157  1.00 226.35 ? 336  PHE A CB  1 
ATOM   2547  C  CG  . PHE A 1 336  ? 47.721  -9.051  22.073  1.00 225.35 ? 336  PHE A CG  1 
ATOM   2548  C  CD1 . PHE A 1 336  ? 48.088  -9.849  23.147  1.00 222.46 ? 336  PHE A CD1 1 
ATOM   2549  C  CD2 . PHE A 1 336  ? 47.187  -9.647  20.944  1.00 227.69 ? 336  PHE A CD2 1 
ATOM   2550  C  CE1 . PHE A 1 336  ? 47.942  -11.208 23.094  1.00 226.38 ? 336  PHE A CE1 1 
ATOM   2551  C  CE2 . PHE A 1 336  ? 47.042  -11.010 20.879  1.00 232.28 ? 336  PHE A CE2 1 
ATOM   2552  C  CZ  . PHE A 1 336  ? 47.417  -11.793 21.956  1.00 232.09 ? 336  PHE A CZ  1 
ATOM   2553  N  N   . SER A 1 337  ? 47.144  -5.238  20.748  1.00 247.53 ? 337  SER A N   1 
ATOM   2554  C  CA  . SER A 1 337  ? 46.590  -3.896  20.786  1.00 235.84 ? 337  SER A CA  1 
ATOM   2555  C  C   . SER A 1 337  ? 45.115  -3.970  21.124  1.00 232.26 ? 337  SER A C   1 
ATOM   2556  O  O   . SER A 1 337  ? 44.406  -4.866  20.659  1.00 235.28 ? 337  SER A O   1 
ATOM   2557  C  CB  . SER A 1 337  ? 46.766  -3.193  19.444  1.00 234.00 ? 337  SER A CB  1 
ATOM   2558  O  OG  . SER A 1 337  ? 46.239  -1.878  19.496  1.00 224.58 ? 337  SER A OG  1 
ATOM   2559  N  N   . GLU A 1 338  ? 44.658  -3.028  21.942  1.00 224.92 ? 338  GLU A N   1 
ATOM   2560  C  CA  . GLU A 1 338  ? 43.243  -2.927  22.273  1.00 221.68 ? 338  GLU A CA  1 
ATOM   2561  C  C   . GLU A 1 338  ? 42.803  -1.470  22.268  1.00 213.77 ? 338  GLU A C   1 
ATOM   2562  O  O   . GLU A 1 338  ? 43.539  -0.595  22.702  1.00 209.59 ? 338  GLU A O   1 
ATOM   2563  C  CB  . GLU A 1 338  ? 42.960  -3.550  23.633  1.00 223.22 ? 338  GLU A CB  1 
ATOM   2564  C  CG  . GLU A 1 338  ? 41.557  -4.086  23.760  1.00 227.11 ? 338  GLU A CG  1 
ATOM   2565  C  CD  . GLU A 1 338  ? 41.263  -5.140  22.711  1.00 237.20 ? 338  GLU A CD  1 
ATOM   2566  O  OE1 . GLU A 1 338  ? 42.193  -5.891  22.346  1.00 242.71 ? 338  GLU A OE1 1 
ATOM   2567  O  OE2 . GLU A 1 338  ? 40.107  -5.218  22.246  1.00 239.66 ? 338  GLU A OE2 1 
ATOM   2568  N  N   . GLU A 1 339  ? 41.603  -1.205  21.772  1.00 253.46 ? 339  GLU A N   1 
ATOM   2569  C  CA  . GLU A 1 339  ? 41.125  0.163   21.680  1.00 249.79 ? 339  GLU A CA  1 
ATOM   2570  C  C   . GLU A 1 339  ? 39.840  0.329   22.469  1.00 238.57 ? 339  GLU A C   1 
ATOM   2571  O  O   . GLU A 1 339  ? 39.100  -0.632  22.665  1.00 235.94 ? 339  GLU A O   1 
ATOM   2572  C  CB  . GLU A 1 339  ? 40.915  0.546   20.221  1.00 261.03 ? 339  GLU A CB  1 
ATOM   2573  C  CG  . GLU A 1 339  ? 42.207  0.610   19.435  1.00 273.70 ? 339  GLU A CG  1 
ATOM   2574  C  CD  . GLU A 1 339  ? 41.985  0.531   17.944  1.00 288.33 ? 339  GLU A CD  1 
ATOM   2575  O  OE1 . GLU A 1 339  ? 40.820  0.654   17.508  1.00 291.98 ? 339  GLU A OE1 1 
ATOM   2576  O  OE2 . GLU A 1 339  ? 42.977  0.340   17.208  1.00 295.35 ? 339  GLU A OE2 1 
ATOM   2577  N  N   . ALA A 1 340  ? 39.577  1.549   22.924  1.00 175.88 ? 340  ALA A N   1 
ATOM   2578  C  CA  . ALA A 1 340  ? 38.377  1.837   23.709  1.00 171.02 ? 340  ALA A CA  1 
ATOM   2579  C  C   . ALA A 1 340  ? 38.028  3.330   23.683  1.00 165.04 ? 340  ALA A C   1 
ATOM   2580  O  O   . ALA A 1 340  ? 38.899  4.191   23.804  1.00 163.44 ? 340  ALA A O   1 
ATOM   2581  C  CB  . ALA A 1 340  ? 38.548  1.338   25.139  1.00 170.90 ? 340  ALA A CB  1 
ATOM   2582  N  N   . GLU A 1 341  ? 36.749  3.639   23.518  1.00 199.92 ? 341  GLU A N   1 
ATOM   2583  C  CA  . GLU A 1 341  ? 36.358  5.020   23.285  1.00 198.75 ? 341  GLU A CA  1 
ATOM   2584  C  C   . GLU A 1 341  ? 35.215  5.453   24.176  1.00 169.14 ? 341  GLU A C   1 
ATOM   2585  O  O   . GLU A 1 341  ? 34.475  4.616   24.694  1.00 168.23 ? 341  GLU A O   1 
ATOM   2586  C  CB  . GLU A 1 341  ? 35.915  5.197   21.836  1.00 204.21 ? 341  GLU A CB  1 
ATOM   2587  C  CG  . GLU A 1 341  ? 34.606  4.472   21.485  1.00 208.41 ? 341  GLU A CG  1 
ATOM   2588  C  CD  . GLU A 1 341  ? 34.131  4.776   20.067  1.00 212.78 ? 341  GLU A CD  1 
ATOM   2589  O  OE1 . GLU A 1 341  ? 34.842  5.507   19.345  1.00 213.46 ? 341  GLU A OE1 1 
ATOM   2590  O  OE2 . GLU A 1 341  ? 33.051  4.290   19.672  1.00 215.87 ? 341  GLU A OE2 1 
ATOM   2591  N  N   . ILE A 1 342  ? 35.072  6.768   24.341  1.00 151.77 ? 342  ILE A N   1 
ATOM   2592  C  CA  . ILE A 1 342  ? 33.880  7.351   24.951  1.00 145.86 ? 342  ILE A CA  1 
ATOM   2593  C  C   . ILE A 1 342  ? 33.209  8.345   24.027  1.00 147.91 ? 342  ILE A C   1 
ATOM   2594  O  O   . ILE A 1 342  ? 33.816  9.341   23.632  1.00 148.87 ? 342  ILE A O   1 
ATOM   2595  C  CB  . ILE A 1 342  ? 34.175  8.066   26.263  1.00 136.38 ? 342  ILE A CB  1 
ATOM   2596  C  CG1 . ILE A 1 342  ? 34.937  7.136   27.211  1.00 137.10 ? 342  ILE A CG1 1 
ATOM   2597  C  CG2 . ILE A 1 342  ? 32.864  8.560   26.894  1.00 137.71 ? 342  ILE A CG2 1 
ATOM   2598  C  CD1 . ILE A 1 342  ? 35.025  7.649   28.637  1.00 133.83 ? 342  ILE A CD1 1 
ATOM   2599  N  N   . PRO A 1 343  ? 31.927  8.093   23.725  1.00 177.54 ? 343  PRO A N   1 
ATOM   2600  C  CA  . PRO A 1 343  ? 31.205  8.844   22.699  1.00 178.84 ? 343  PRO A CA  1 
ATOM   2601  C  C   . PRO A 1 343  ? 31.528  10.297  22.862  1.00 173.86 ? 343  PRO A C   1 
ATOM   2602  O  O   . PRO A 1 343  ? 32.206  10.935  22.049  1.00 178.95 ? 343  PRO A O   1 
ATOM   2603  C  CB  . PRO A 1 343  ? 29.736  8.657   23.097  1.00 177.43 ? 343  PRO A CB  1 
ATOM   2604  C  CG  . PRO A 1 343  ? 29.698  7.399   23.866  1.00 177.68 ? 343  PRO A CG  1 
ATOM   2605  C  CD  . PRO A 1 343  ? 31.029  7.258   24.542  1.00 176.01 ? 343  PRO A CD  1 
ATOM   2606  N  N   . GLY A 1 344  ? 31.023  10.804  23.975  1.00 196.18 ? 344  GLY A N   1 
ATOM   2607  C  CA  . GLY A 1 344  ? 31.197  12.182  24.348  1.00 191.48 ? 344  GLY A CA  1 
ATOM   2608  C  C   . GLY A 1 344  ? 30.937  12.431  25.820  1.00 183.36 ? 344  GLY A C   1 
ATOM   2609  O  O   . GLY A 1 344  ? 30.498  11.560  26.582  1.00 183.65 ? 344  GLY A O   1 
ATOM   2610  N  N   . ILE A 1 345  ? 31.211  13.667  26.200  1.00 119.97 ? 345  ILE A N   1 
ATOM   2611  C  CA  . ILE A 1 345  ? 31.108  14.134  27.562  1.00 116.31 ? 345  ILE A CA  1 
ATOM   2612  C  C   . ILE A 1 345  ? 30.614  15.564  27.408  1.00 115.77 ? 345  ILE A C   1 
ATOM   2613  O  O   . ILE A 1 345  ? 31.396  16.458  27.099  1.00 117.20 ? 345  ILE A O   1 
ATOM   2614  C  CB  . ILE A 1 345  ? 32.502  14.107  28.217  1.00 137.29 ? 345  ILE A CB  1 
ATOM   2615  C  CG1 . ILE A 1 345  ? 32.853  12.698  28.661  1.00 126.93 ? 345  ILE A CG1 1 
ATOM   2616  C  CG2 . ILE A 1 345  ? 32.578  15.012  29.407  1.00 134.22 ? 345  ILE A CG2 1 
ATOM   2617  C  CD1 . ILE A 1 345  ? 34.005  12.671  29.593  1.00 126.16 ? 345  ILE A CD1 1 
ATOM   2618  N  N   . LYS A 1 346  ? 29.310  15.773  27.571  1.00 168.72 ? 346  LYS A N   1 
ATOM   2619  C  CA  . LYS A 1 346  ? 28.709  17.083  27.323  1.00 157.44 ? 346  LYS A CA  1 
ATOM   2620  C  C   . LYS A 1 346  ? 29.291  18.128  28.275  1.00 154.70 ? 346  LYS A C   1 
ATOM   2621  O  O   . LYS A 1 346  ? 29.129  17.992  29.482  1.00 157.68 ? 346  LYS A O   1 
ATOM   2622  C  CB  . LYS A 1 346  ? 27.189  17.001  27.528  1.00 156.08 ? 346  LYS A CB  1 
ATOM   2623  C  CG  . LYS A 1 346  ? 26.389  18.110  26.846  1.00 159.92 ? 346  LYS A CG  1 
ATOM   2624  C  CD  . LYS A 1 346  ? 24.977  18.309  27.438  1.00 160.56 ? 346  LYS A CD  1 
ATOM   2625  C  CE  . LYS A 1 346  ? 23.913  17.346  26.887  1.00 164.39 ? 346  LYS A CE  1 
ATOM   2626  N  NZ  . LYS A 1 346  ? 22.509  17.748  27.266  1.00 164.13 ? 346  LYS A NZ  1 
ATOM   2627  N  N   . TYR A 1 347  ? 29.984  19.148  27.761  1.00 130.12 ? 347  TYR A N   1 
ATOM   2628  C  CA  . TYR A 1 347  ? 30.373  20.294  28.594  1.00 128.74 ? 347  TYR A CA  1 
ATOM   2629  C  C   . TYR A 1 347  ? 29.139  20.994  29.058  1.00 129.11 ? 347  TYR A C   1 
ATOM   2630  O  O   . TYR A 1 347  ? 28.131  20.890  28.383  1.00 126.26 ? 347  TYR A O   1 
ATOM   2631  C  CB  . TYR A 1 347  ? 31.096  21.336  27.784  1.00 132.74 ? 347  TYR A CB  1 
ATOM   2632  C  CG  . TYR A 1 347  ? 32.552  21.127  27.751  1.00 132.21 ? 347  TYR A CG  1 
ATOM   2633  C  CD1 . TYR A 1 347  ? 33.425  22.153  28.050  1.00 132.95 ? 347  TYR A CD1 1 
ATOM   2634  C  CD2 . TYR A 1 347  ? 33.063  19.890  27.428  1.00 136.08 ? 347  TYR A CD2 1 
ATOM   2635  C  CE1 . TYR A 1 347  ? 34.776  21.951  28.010  1.00 136.77 ? 347  TYR A CE1 1 
ATOM   2636  C  CE2 . TYR A 1 347  ? 34.400  19.673  27.388  1.00 139.56 ? 347  TYR A CE2 1 
ATOM   2637  C  CZ  . TYR A 1 347  ? 35.258  20.701  27.684  1.00 140.87 ? 347  TYR A CZ  1 
ATOM   2638  O  OH  . TYR A 1 347  ? 36.606  20.451  27.649  1.00 144.61 ? 347  TYR A OH  1 
ATOM   2639  N  N   . VAL A 1 348  ? 29.196  21.742  30.161  1.00 111.16 ? 348  VAL A N   1 
ATOM   2640  C  CA  . VAL A 1 348  ? 28.082  22.648  30.485  1.00 111.44 ? 348  VAL A CA  1 
ATOM   2641  C  C   . VAL A 1 348  ? 28.580  23.987  30.964  1.00 110.35 ? 348  VAL A C   1 
ATOM   2642  O  O   . VAL A 1 348  ? 29.693  24.157  31.459  1.00 108.97 ? 348  VAL A O   1 
ATOM   2643  C  CB  . VAL A 1 348  ? 27.040  22.105  31.504  1.00 111.11 ? 348  VAL A CB  1 
ATOM   2644  C  CG1 . VAL A 1 348  ? 25.983  23.131  31.787  1.00 111.45 ? 348  VAL A CG1 1 
ATOM   2645  C  CG2 . VAL A 1 348  ? 26.361  20.855  30.994  1.00 112.53 ? 348  VAL A CG2 1 
ATOM   2646  N  N   . LEU A 1 349  ? 27.733  24.962  30.785  1.00 120.63 ? 349  LEU A N   1 
ATOM   2647  C  CA  . LEU A 1 349  ? 28.031  26.257  31.281  1.00 121.12 ? 349  LEU A CA  1 
ATOM   2648  C  C   . LEU A 1 349  ? 27.655  26.267  32.752  1.00 114.54 ? 349  LEU A C   1 
ATOM   2649  O  O   . LEU A 1 349  ? 28.527  26.319  33.620  1.00 111.75 ? 349  LEU A O   1 
ATOM   2650  C  CB  . LEU A 1 349  ? 27.173  27.222  30.501  1.00 127.36 ? 349  LEU A CB  1 
ATOM   2651  C  CG  . LEU A 1 349  ? 27.486  28.689  30.658  1.00 130.26 ? 349  LEU A CG  1 
ATOM   2652  C  CD1 . LEU A 1 349  ? 26.208  29.428  31.058  1.00 129.16 ? 349  LEU A CD1 1 
ATOM   2653  C  CD2 . LEU A 1 349  ? 28.632  28.842  31.667  1.00 130.36 ? 349  LEU A CD2 1 
ATOM   2654  N  N   . SER A 1 350  ? 26.338  26.181  32.990  1.00 140.12 ? 350  SER A N   1 
ATOM   2655  C  CA  . SER A 1 350  ? 25.648  26.256  34.295  1.00 136.77 ? 350  SER A CA  1 
ATOM   2656  C  C   . SER A 1 350  ? 24.692  25.063  34.459  1.00 136.75 ? 350  SER A C   1 
ATOM   2657  O  O   . SER A 1 350  ? 23.827  24.828  33.621  1.00 141.32 ? 350  SER A O   1 
ATOM   2658  C  CB  . SER A 1 350  ? 24.820  27.528  34.345  1.00 139.17 ? 350  SER A CB  1 
ATOM   2659  O  OG  . SER A 1 350  ? 24.004  27.564  35.492  1.00 138.54 ? 350  SER A OG  1 
ATOM   2660  N  N   . PRO A 1 351  ? 24.818  24.328  35.562  1.00 115.36 ? 351  PRO A N   1 
ATOM   2661  C  CA  . PRO A 1 351  ? 24.248  22.985  35.745  1.00 115.80 ? 351  PRO A CA  1 
ATOM   2662  C  C   . PRO A 1 351  ? 22.727  22.957  35.835  1.00 120.30 ? 351  PRO A C   1 
ATOM   2663  O  O   . PRO A 1 351  ? 22.131  21.897  36.042  1.00 123.39 ? 351  PRO A O   1 
ATOM   2664  C  CB  . PRO A 1 351  ? 24.877  22.515  37.056  1.00 110.80 ? 351  PRO A CB  1 
ATOM   2665  C  CG  . PRO A 1 351  ? 26.060  23.444  37.260  1.00 107.98 ? 351  PRO A CG  1 
ATOM   2666  C  CD  . PRO A 1 351  ? 25.607  24.747  36.718  1.00 110.54 ? 351  PRO A CD  1 
ATOM   2667  N  N   . TYR A 1 352  ? 22.116  24.121  35.656  1.00 135.76 ? 352  TYR A N   1 
ATOM   2668  C  CA  . TYR A 1 352  ? 20.665  24.255  35.651  1.00 139.63 ? 352  TYR A CA  1 
ATOM   2669  C  C   . TYR A 1 352  ? 20.195  24.826  34.307  1.00 142.56 ? 352  TYR A C   1 
ATOM   2670  O  O   . TYR A 1 352  ? 20.942  25.519  33.629  1.00 140.27 ? 352  TYR A O   1 
ATOM   2671  C  CB  . TYR A 1 352  ? 20.198  25.222  36.750  1.00 141.56 ? 352  TYR A CB  1 
ATOM   2672  C  CG  . TYR A 1 352  ? 20.544  24.914  38.207  1.00 140.30 ? 352  TYR A CG  1 
ATOM   2673  C  CD1 . TYR A 1 352  ? 19.581  24.379  39.066  1.00 142.29 ? 352  TYR A CD1 1 
ATOM   2674  C  CD2 . TYR A 1 352  ? 21.797  25.232  38.737  1.00 138.66 ? 352  TYR A CD2 1 
ATOM   2675  C  CE1 . TYR A 1 352  ? 19.858  24.115  40.379  1.00 140.50 ? 352  TYR A CE1 1 
ATOM   2676  C  CE2 . TYR A 1 352  ? 22.084  24.976  40.057  1.00 138.13 ? 352  TYR A CE2 1 
ATOM   2677  C  CZ  . TYR A 1 352  ? 21.107  24.411  40.873  1.00 138.86 ? 352  TYR A CZ  1 
ATOM   2678  O  OH  . TYR A 1 352  ? 21.372  24.136  42.190  1.00 137.31 ? 352  TYR A OH  1 
ATOM   2679  N  N   . LYS A 1 353  ? 18.939  24.593  33.952  1.00 119.29 ? 353  LYS A N   1 
ATOM   2680  C  CA  . LYS A 1 353  ? 18.439  25.067  32.678  1.00 124.91 ? 353  LYS A CA  1 
ATOM   2681  C  C   . LYS A 1 353  ? 16.988  25.474  32.774  1.00 122.53 ? 353  LYS A C   1 
ATOM   2682  O  O   . LYS A 1 353  ? 16.116  24.632  32.876  1.00 119.43 ? 353  LYS A O   1 
ATOM   2683  C  CB  . LYS A 1 353  ? 18.584  23.968  31.625  1.00 132.58 ? 353  LYS A CB  1 
ATOM   2684  C  CG  . LYS A 1 353  ? 18.112  22.606  32.078  1.00 138.96 ? 353  LYS A CG  1 
ATOM   2685  C  CD  . LYS A 1 353  ? 19.000  21.499  31.499  1.00 143.92 ? 353  LYS A CD  1 
ATOM   2686  C  CE  . LYS A 1 353  ? 18.609  21.059  30.079  1.00 150.86 ? 353  LYS A CE  1 
ATOM   2687  N  NZ  . LYS A 1 353  ? 19.582  20.051  29.495  1.00 151.34 ? 353  LYS A NZ  1 
ATOM   2688  N  N   . LEU A 1 354  ? 16.722  26.766  32.713  1.00 130.77 ? 354  LEU A N   1 
ATOM   2689  C  CA  . LEU A 1 354  ? 15.365  27.247  32.889  1.00 134.43 ? 354  LEU A CA  1 
ATOM   2690  C  C   . LEU A 1 354  ? 14.537  26.926  31.673  1.00 137.36 ? 354  LEU A C   1 
ATOM   2691  O  O   . LEU A 1 354  ? 15.056  26.870  30.581  1.00 138.96 ? 354  LEU A O   1 
ATOM   2692  C  CB  . LEU A 1 354  ? 15.344  28.759  33.043  1.00 136.90 ? 354  LEU A CB  1 
ATOM   2693  C  CG  . LEU A 1 354  ? 16.387  29.530  33.853  1.00 132.37 ? 354  LEU A CG  1 
ATOM   2694  C  CD1 . LEU A 1 354  ? 15.922  29.826  35.301  1.00 132.74 ? 354  LEU A CD1 1 
ATOM   2695  C  CD2 . LEU A 1 354  ? 17.767  28.852  33.780  1.00 127.87 ? 354  LEU A CD2 1 
ATOM   2696  N  N   . ASN A 1 355  ? 13.239  26.754  31.853  1.00 129.28 ? 355  ASN A N   1 
ATOM   2697  C  CA  . ASN A 1 355  ? 12.336  26.719  30.722  1.00 125.83 ? 355  ASN A CA  1 
ATOM   2698  C  C   . ASN A 1 355  ? 10.930  27.038  31.132  1.00 128.29 ? 355  ASN A C   1 
ATOM   2699  O  O   . ASN A 1 355  ? 10.315  26.286  31.869  1.00 134.45 ? 355  ASN A O   1 
ATOM   2700  C  CB  . ASN A 1 355  ? 12.404  25.390  29.967  1.00 130.58 ? 355  ASN A CB  1 
ATOM   2701  C  CG  . ASN A 1 355  ? 12.010  24.206  30.806  1.00 135.27 ? 355  ASN A CG  1 
ATOM   2702  O  OD1 . ASN A 1 355  ? 12.814  23.682  31.576  1.00 133.66 ? 355  ASN A OD1 1 
ATOM   2703  N  ND2 . ASN A 1 355  ? 10.776  23.748  30.632  1.00 141.50 ? 355  ASN A ND2 1 
ATOM   2704  N  N   . LEU A 1 356  ? 10.428  28.168  30.655  1.00 102.54 ? 356  LEU A N   1 
ATOM   2705  C  CA  . LEU A 1 356  ? 9.076   28.576  30.968  1.00 103.79 ? 356  LEU A CA  1 
ATOM   2706  C  C   . LEU A 1 356  ? 8.153   27.370  30.965  1.00 105.88 ? 356  LEU A C   1 
ATOM   2707  O  O   . LEU A 1 356  ? 8.447   26.384  30.299  1.00 108.99 ? 356  LEU A O   1 
ATOM   2708  C  CB  . LEU A 1 356  ? 8.591   29.550  29.914  1.00 108.24 ? 356  LEU A CB  1 
ATOM   2709  C  CG  . LEU A 1 356  ? 9.180   30.943  29.878  1.00 105.77 ? 356  LEU A CG  1 
ATOM   2710  C  CD1 . LEU A 1 356  ? 8.495   31.723  28.790  1.00 110.46 ? 356  LEU A CD1 1 
ATOM   2711  C  CD2 . LEU A 1 356  ? 8.927   31.564  31.208  1.00 105.28 ? 356  LEU A CD2 1 
ATOM   2712  N  N   . VAL A 1 357  ? 7.033   27.426  31.684  1.00 110.25 ? 357  VAL A N   1 
ATOM   2713  C  CA  . VAL A 1 357  ? 6.119   26.285  31.658  1.00 115.30 ? 357  VAL A CA  1 
ATOM   2714  C  C   . VAL A 1 357  ? 4.635   26.599  31.602  1.00 110.37 ? 357  VAL A C   1 
ATOM   2715  O  O   . VAL A 1 357  ? 4.141   27.362  32.412  1.00 121.83 ? 357  VAL A O   1 
ATOM   2716  C  CB  . VAL A 1 357  ? 6.319   25.401  32.851  1.00 107.93 ? 357  VAL A CB  1 
ATOM   2717  C  CG1 . VAL A 1 357  ? 5.516   24.130  32.644  1.00 112.33 ? 357  VAL A CG1 1 
ATOM   2718  C  CG2 . VAL A 1 357  ? 7.773   25.100  33.012  1.00 104.07 ? 357  VAL A CG2 1 
ATOM   2719  N  N   . ALA A 1 358  ? 3.921   25.982  30.666  1.00 151.63 ? 358  ALA A N   1 
ATOM   2720  C  CA  . ALA A 1 358  ? 2.523   26.317  30.436  1.00 160.66 ? 358  ALA A CA  1 
ATOM   2721  C  C   . ALA A 1 358  ? 2.221   27.800  30.729  1.00 161.08 ? 358  ALA A C   1 
ATOM   2722  O  O   . ALA A 1 358  ? 1.296   28.114  31.480  1.00 157.58 ? 358  ALA A O   1 
ATOM   2723  C  CB  . ALA A 1 358  ? 1.625   25.398  31.236  1.00 166.50 ? 358  ALA A CB  1 
ATOM   2724  N  N   . THR A 1 359  ? 3.011   28.697  30.123  1.00 142.94 ? 359  THR A N   1 
ATOM   2725  C  CA  . THR A 1 359  ? 2.889   30.157  30.298  1.00 142.95 ? 359  THR A CA  1 
ATOM   2726  C  C   . THR A 1 359  ? 2.908   30.993  28.989  1.00 142.40 ? 359  THR A C   1 
ATOM   2727  O  O   . THR A 1 359  ? 3.967   31.463  28.574  1.00 136.64 ? 359  THR A O   1 
ATOM   2728  C  CB  . THR A 1 359  ? 3.986   30.711  31.262  1.00 123.31 ? 359  THR A CB  1 
ATOM   2729  O  OG1 . THR A 1 359  ? 5.263   30.143  30.946  1.00 122.21 ? 359  THR A OG1 1 
ATOM   2730  C  CG2 . THR A 1 359  ? 3.653   30.360  32.696  1.00 120.76 ? 359  THR A CG2 1 
ATOM   2731  N  N   . PRO A 1 360  ? 1.729   31.196  28.353  1.00 154.76 ? 360  PRO A N   1 
ATOM   2732  C  CA  . PRO A 1 360  ? 1.534   31.955  27.106  1.00 157.11 ? 360  PRO A CA  1 
ATOM   2733  C  C   . PRO A 1 360  ? 2.260   33.300  27.116  1.00 154.01 ? 360  PRO A C   1 
ATOM   2734  O  O   . PRO A 1 360  ? 2.333   33.885  28.207  1.00 143.03 ? 360  PRO A O   1 
ATOM   2735  C  CB  . PRO A 1 360  ? 0.021   32.205  27.102  1.00 161.26 ? 360  PRO A CB  1 
ATOM   2736  C  CG  . PRO A 1 360  ? -0.551  31.021  27.779  1.00 162.63 ? 360  PRO A CG  1 
ATOM   2737  C  CD  . PRO A 1 360  ? 0.465   30.591  28.811  1.00 157.16 ? 360  PRO A CD  1 
ATOM   2738  N  N   . LEU A 1 361  ? 2.758   33.777  25.961  1.00 120.17 ? 361  LEU A N   1 
ATOM   2739  C  CA  . LEU A 1 361  ? 3.513   35.048  25.887  1.00 118.89 ? 361  LEU A CA  1 
ATOM   2740  C  C   . LEU A 1 361  ? 2.786   36.264  25.275  1.00 121.04 ? 361  LEU A C   1 
ATOM   2741  O  O   . LEU A 1 361  ? 3.392   37.124  24.654  1.00 120.99 ? 361  LEU A O   1 
ATOM   2742  C  CB  . LEU A 1 361  ? 4.878   34.839  25.237  1.00 117.68 ? 361  LEU A CB  1 
ATOM   2743  C  CG  . LEU A 1 361  ? 5.858   33.882  25.928  1.00 115.13 ? 361  LEU A CG  1 
ATOM   2744  C  CD1 . LEU A 1 361  ? 5.332   32.440  26.054  1.00 115.95 ? 361  LEU A CD1 1 
ATOM   2745  C  CD2 . LEU A 1 361  ? 7.184   33.922  25.190  1.00 114.28 ? 361  LEU A CD2 1 
ATOM   2746  N  N   . PHE A 1 362  ? 1.479   36.321  25.498  1.00 184.34 ? 362  PHE A N   1 
ATOM   2747  C  CA  . PHE A 1 362  ? 0.685   37.523  25.265  1.00 192.49 ? 362  PHE A CA  1 
ATOM   2748  C  C   . PHE A 1 362  ? -0.127  37.917  26.497  1.00 182.11 ? 362  PHE A C   1 
ATOM   2749  O  O   . PHE A 1 362  ? -1.122  37.274  26.866  1.00 179.91 ? 362  PHE A O   1 
ATOM   2750  C  CB  . PHE A 1 362  ? -0.243  37.309  24.099  1.00 212.02 ? 362  PHE A CB  1 
ATOM   2751  C  CG  . PHE A 1 362  ? 0.360   36.504  23.053  1.00 226.30 ? 362  PHE A CG  1 
ATOM   2752  C  CD1 . PHE A 1 362  ? 0.088   35.164  22.965  1.00 232.30 ? 362  PHE A CD1 1 
ATOM   2753  C  CD2 . PHE A 1 362  ? 1.255   37.070  22.189  1.00 231.38 ? 362  PHE A CD2 1 
ATOM   2754  C  CE1 . PHE A 1 362  ? 0.669   34.408  22.004  1.00 239.58 ? 362  PHE A CE1 1 
ATOM   2755  C  CE2 . PHE A 1 362  ? 1.842   36.325  21.221  1.00 237.94 ? 362  PHE A CE2 1 
ATOM   2756  C  CZ  . PHE A 1 362  ? 1.553   34.986  21.122  1.00 240.51 ? 362  PHE A CZ  1 
ATOM   2757  N  N   . LEU A 1 363  ? 0.296   38.995  27.130  1.00 140.40 ? 363  LEU A N   1 
ATOM   2758  C  CA  . LEU A 1 363  ? -0.392  39.464  28.292  1.00 134.51 ? 363  LEU A CA  1 
ATOM   2759  C  C   . LEU A 1 363  ? -1.598  40.246  27.864  1.00 134.98 ? 363  LEU A C   1 
ATOM   2760  O  O   . LEU A 1 363  ? -1.461  41.305  27.298  1.00 135.18 ? 363  LEU A O   1 
ATOM   2761  C  CB  . LEU A 1 363  ? 0.564   40.348  29.077  1.00 126.47 ? 363  LEU A CB  1 
ATOM   2762  C  CG  . LEU A 1 363  ? 1.538   41.085  28.164  1.00 126.84 ? 363  LEU A CG  1 
ATOM   2763  C  CD1 . LEU A 1 363  ? 0.948   42.444  27.965  1.00 130.66 ? 363  LEU A CD1 1 
ATOM   2764  C  CD2 . LEU A 1 363  ? 2.928   41.169  28.777  1.00 120.59 ? 363  LEU A CD2 1 
ATOM   2765  N  N   . LYS A 1 364  ? -2.782  39.704  28.092  1.00 152.02 ? 364  LYS A N   1 
ATOM   2766  C  CA  . LYS A 1 364  ? -3.989  40.514  28.020  1.00 148.32 ? 364  LYS A CA  1 
ATOM   2767  C  C   . LYS A 1 364  ? -3.784  41.693  29.000  1.00 148.13 ? 364  LYS A C   1 
ATOM   2768  O  O   . LYS A 1 364  ? -2.936  41.600  29.889  1.00 141.14 ? 364  LYS A O   1 
ATOM   2769  C  CB  . LYS A 1 364  ? -5.219  39.677  28.372  1.00 153.27 ? 364  LYS A CB  1 
ATOM   2770  C  CG  . LYS A 1 364  ? -5.354  38.386  27.577  1.00 160.86 ? 364  LYS A CG  1 
ATOM   2771  C  CD  . LYS A 1 364  ? -4.129  37.502  27.685  1.00 158.64 ? 364  LYS A CD  1 
ATOM   2772  C  CE  . LYS A 1 364  ? -4.473  36.116  27.248  1.00 164.34 ? 364  LYS A CE  1 
ATOM   2773  N  NZ  . LYS A 1 364  ? -5.584  36.182  26.277  1.00 173.13 ? 364  LYS A NZ  1 
ATOM   2774  N  N   . PRO A 1 365  ? -4.498  42.830  28.805  1.00 201.37 ? 365  PRO A N   1 
ATOM   2775  C  CA  . PRO A 1 365  ? -4.264  44.024  29.639  1.00 199.87 ? 365  PRO A CA  1 
ATOM   2776  C  C   . PRO A 1 365  ? -5.116  44.089  30.888  1.00 202.75 ? 365  PRO A C   1 
ATOM   2777  O  O   . PRO A 1 365  ? -6.230  43.574  30.904  1.00 208.71 ? 365  PRO A O   1 
ATOM   2778  C  CB  . PRO A 1 365  ? -4.646  45.188  28.713  1.00 203.19 ? 365  PRO A CB  1 
ATOM   2779  C  CG  . PRO A 1 365  ? -4.795  44.605  27.352  1.00 206.91 ? 365  PRO A CG  1 
ATOM   2780  C  CD  . PRO A 1 365  ? -5.248  43.184  27.591  1.00 207.54 ? 365  PRO A CD  1 
ATOM   2781  N  N   . GLY A 1 366  ? -4.603  44.745  31.920  1.00 215.50 ? 366  GLY A N   1 
ATOM   2782  C  CA  . GLY A 1 366  ? -5.315  44.808  33.180  1.00 222.71 ? 366  GLY A CA  1 
ATOM   2783  C  C   . GLY A 1 366  ? -5.221  43.530  33.991  1.00 214.03 ? 366  GLY A C   1 
ATOM   2784  O  O   . GLY A 1 366  ? -5.116  43.584  35.217  1.00 211.38 ? 366  GLY A O   1 
ATOM   2785  N  N   . ILE A 1 367  ? -5.274  42.380  33.325  1.00 182.30 ? 367  ILE A N   1 
ATOM   2786  C  CA  . ILE A 1 367  ? -5.022  41.114  34.016  1.00 176.17 ? 367  ILE A CA  1 
ATOM   2787  C  C   . ILE A 1 367  ? -3.549  41.105  34.472  1.00 168.40 ? 367  ILE A C   1 
ATOM   2788  O  O   . ILE A 1 367  ? -2.729  41.855  33.930  1.00 167.59 ? 367  ILE A O   1 
ATOM   2789  C  CB  . ILE A 1 367  ? -5.405  39.892  33.124  1.00 180.70 ? 367  ILE A CB  1 
ATOM   2790  C  CG1 . ILE A 1 367  ? -6.921  39.750  33.064  1.00 185.24 ? 367  ILE A CG1 1 
ATOM   2791  C  CG2 . ILE A 1 367  ? -4.807  38.601  33.636  1.00 177.07 ? 367  ILE A CG2 1 
ATOM   2792  C  CD1 . ILE A 1 367  ? -7.379  38.440  32.512  1.00 189.47 ? 367  ILE A CD1 1 
ATOM   2793  N  N   . PRO A 1 368  ? -3.226  40.324  35.515  1.00 149.65 ? 368  PRO A N   1 
ATOM   2794  C  CA  . PRO A 1 368  ? -1.826  40.169  35.898  1.00 143.06 ? 368  PRO A CA  1 
ATOM   2795  C  C   . PRO A 1 368  ? -1.221  39.025  35.108  1.00 139.61 ? 368  PRO A C   1 
ATOM   2796  O  O   . PRO A 1 368  ? -1.880  38.013  34.852  1.00 144.33 ? 368  PRO A O   1 
ATOM   2797  C  CB  . PRO A 1 368  ? -1.901  39.789  37.384  1.00 136.62 ? 368  PRO A CB  1 
ATOM   2798  C  CG  . PRO A 1 368  ? -3.333  39.593  37.709  1.00 141.27 ? 368  PRO A CG  1 
ATOM   2799  C  CD  . PRO A 1 368  ? -4.125  39.625  36.444  1.00 148.84 ? 368  PRO A CD  1 
ATOM   2800  N  N   . TYR A 1 369  ? 0.032   39.177  34.727  1.00 125.06 ? 369  TYR A N   1 
ATOM   2801  C  CA  . TYR A 1 369  ? 0.658   38.152  33.930  1.00 123.76 ? 369  TYR A CA  1 
ATOM   2802  C  C   . TYR A 1 369  ? 1.318   37.037  34.782  1.00 124.86 ? 369  TYR A C   1 
ATOM   2803  O  O   . TYR A 1 369  ? 2.057   37.325  35.727  1.00 120.08 ? 369  TYR A O   1 
ATOM   2804  C  CB  . TYR A 1 369  ? 1.618   38.840  32.975  1.00 128.79 ? 369  TYR A CB  1 
ATOM   2805  C  CG  . TYR A 1 369  ? 2.186   37.957  31.905  1.00 127.51 ? 369  TYR A CG  1 
ATOM   2806  C  CD1 . TYR A 1 369  ? 1.388   37.012  31.249  1.00 136.53 ? 369  TYR A CD1 1 
ATOM   2807  C  CD2 . TYR A 1 369  ? 3.522   38.085  31.532  1.00 128.23 ? 369  TYR A CD2 1 
ATOM   2808  C  CE1 . TYR A 1 369  ? 1.916   36.209  30.285  1.00 138.64 ? 369  TYR A CE1 1 
ATOM   2809  C  CE2 . TYR A 1 369  ? 4.052   37.287  30.587  1.00 131.94 ? 369  TYR A CE2 1 
ATOM   2810  C  CZ  . TYR A 1 369  ? 3.250   36.354  29.969  1.00 138.51 ? 369  TYR A CZ  1 
ATOM   2811  O  OH  . TYR A 1 369  ? 3.791   35.548  29.022  1.00 143.68 ? 369  TYR A OH  1 
ATOM   2812  N  N   . PRO A 1 370  ? 1.004   35.759  34.470  1.00 124.63 ? 370  PRO A N   1 
ATOM   2813  C  CA  . PRO A 1 370  ? 1.492   34.540  35.154  1.00 121.81 ? 370  PRO A CA  1 
ATOM   2814  C  C   . PRO A 1 370  ? 2.827   33.967  34.653  1.00 129.53 ? 370  PRO A C   1 
ATOM   2815  O  O   . PRO A 1 370  ? 2.802   33.136  33.756  1.00 133.12 ? 370  PRO A O   1 
ATOM   2816  C  CB  . PRO A 1 370  ? 0.384   33.505  34.874  1.00 126.82 ? 370  PRO A CB  1 
ATOM   2817  C  CG  . PRO A 1 370  ? -0.777  34.288  34.280  1.00 134.68 ? 370  PRO A CG  1 
ATOM   2818  C  CD  . PRO A 1 370  ? -0.166  35.479  33.617  1.00 131.16 ? 370  PRO A CD  1 
ATOM   2819  N  N   . ILE A 1 371  ? 3.960   34.335  35.241  1.00 160.76 ? 371  ILE A N   1 
ATOM   2820  C  CA  . ILE A 1 371  ? 5.243   33.801  34.768  1.00 159.42 ? 371  ILE A CA  1 
ATOM   2821  C  C   . ILE A 1 371  ? 5.778   32.565  35.542  1.00 160.00 ? 371  ILE A C   1 
ATOM   2822  O  O   . ILE A 1 371  ? 6.332   32.701  36.640  1.00 154.70 ? 371  ILE A O   1 
ATOM   2823  C  CB  . ILE A 1 371  ? 6.324   34.894  34.765  1.00 157.80 ? 371  ILE A CB  1 
ATOM   2824  C  CG1 . ILE A 1 371  ? 5.735   36.226  34.328  1.00 158.11 ? 371  ILE A CG1 1 
ATOM   2825  C  CG2 . ILE A 1 371  ? 7.437   34.507  33.838  1.00 155.77 ? 371  ILE A CG2 1 
ATOM   2826  C  CD1 . ILE A 1 371  ? 6.781   37.262  34.073  1.00 155.51 ? 371  ILE A CD1 1 
ATOM   2827  N  N   . LYS A 1 372  ? 5.644   31.369  34.962  1.00 126.88 ? 372  LYS A N   1 
ATOM   2828  C  CA  . LYS A 1 372  ? 6.080   30.131  35.632  1.00 123.76 ? 372  LYS A CA  1 
ATOM   2829  C  C   . LYS A 1 372  ? 7.345   29.527  35.037  1.00 122.77 ? 372  LYS A C   1 
ATOM   2830  O  O   . LYS A 1 372  ? 7.262   28.667  34.159  1.00 130.14 ? 372  LYS A O   1 
ATOM   2831  C  CB  . LYS A 1 372  ? 4.982   29.060  35.610  1.00 128.07 ? 372  LYS A CB  1 
ATOM   2832  C  CG  . LYS A 1 372  ? 3.657   29.449  36.228  1.00 135.85 ? 372  LYS A CG  1 
ATOM   2833  C  CD  . LYS A 1 372  ? 2.581   28.451  35.873  1.00 143.75 ? 372  LYS A CD  1 
ATOM   2834  C  CE  . LYS A 1 372  ? 1.397   29.151  35.213  1.00 155.46 ? 372  LYS A CE  1 
ATOM   2835  N  NZ  . LYS A 1 372  ? 0.160   29.010  36.034  1.00 156.26 ? 372  LYS A NZ  1 
ATOM   2836  N  N   . VAL A 1 373  ? 8.506   29.973  35.515  1.00 119.91 ? 373  VAL A N   1 
ATOM   2837  C  CA  . VAL A 1 373  ? 9.781   29.373  35.119  1.00 121.05 ? 373  VAL A CA  1 
ATOM   2838  C  C   . VAL A 1 373  ? 9.968   28.038  35.834  1.00 114.43 ? 373  VAL A C   1 
ATOM   2839  O  O   . VAL A 1 373  ? 9.190   27.730  36.724  1.00 115.77 ? 373  VAL A O   1 
ATOM   2840  C  CB  . VAL A 1 373  ? 10.963  30.336  35.357  1.00 112.05 ? 373  VAL A CB  1 
ATOM   2841  C  CG1 . VAL A 1 373  ? 10.479  31.582  36.060  1.00 113.27 ? 373  VAL A CG1 1 
ATOM   2842  C  CG2 . VAL A 1 373  ? 12.106  29.664  36.106  1.00 108.34 ? 373  VAL A CG2 1 
ATOM   2843  N  N   . GLN A 1 374  ? 10.968  27.244  35.448  1.00 123.50 ? 374  GLN A N   1 
ATOM   2844  C  CA  . GLN A 1 374  ? 11.086  25.870  35.942  1.00 119.72 ? 374  GLN A CA  1 
ATOM   2845  C  C   . GLN A 1 374  ? 12.501  25.341  35.763  1.00 122.78 ? 374  GLN A C   1 
ATOM   2846  O  O   . GLN A 1 374  ? 12.914  25.016  34.659  1.00 129.12 ? 374  GLN A O   1 
ATOM   2847  C  CB  . GLN A 1 374  ? 10.052  24.966  35.244  1.00 126.50 ? 374  GLN A CB  1 
ATOM   2848  C  CG  . GLN A 1 374  ? 10.418  23.497  35.120  1.00 125.74 ? 374  GLN A CG  1 
ATOM   2849  C  CD  . GLN A 1 374  ? 9.330   22.678  34.433  1.00 136.69 ? 374  GLN A CD  1 
ATOM   2850  O  OE1 . GLN A 1 374  ? 9.414   22.381  33.246  1.00 139.82 ? 374  GLN A OE1 1 
ATOM   2851  N  NE2 . GLN A 1 374  ? 8.304   22.318  35.180  1.00 140.94 ? 374  GLN A NE2 1 
ATOM   2852  N  N   . VAL A 1 375  ? 13.245  25.278  36.859  1.00 121.28 ? 375  VAL A N   1 
ATOM   2853  C  CA  . VAL A 1 375  ? 14.644  24.903  36.805  1.00 114.86 ? 375  VAL A CA  1 
ATOM   2854  C  C   . VAL A 1 375  ? 14.839  23.414  36.680  1.00 117.50 ? 375  VAL A C   1 
ATOM   2855  O  O   . VAL A 1 375  ? 14.030  22.633  37.171  1.00 119.41 ? 375  VAL A O   1 
ATOM   2856  C  CB  . VAL A 1 375  ? 15.407  25.395  38.043  1.00 110.58 ? 375  VAL A CB  1 
ATOM   2857  C  CG1 . VAL A 1 375  ? 16.714  24.665  38.197  1.00 108.13 ? 375  VAL A CG1 1 
ATOM   2858  C  CG2 . VAL A 1 375  ? 15.656  26.874  37.940  1.00 111.47 ? 375  VAL A CG2 1 
ATOM   2859  N  N   . LYS A 1 376  ? 15.914  23.040  35.996  1.00 114.88 ? 376  LYS A N   1 
ATOM   2860  C  CA  . LYS A 1 376  ? 16.321  21.658  35.867  1.00 112.28 ? 376  LYS A CA  1 
ATOM   2861  C  C   . LYS A 1 376  ? 17.826  21.608  35.870  1.00 103.76 ? 376  LYS A C   1 
ATOM   2862  O  O   . LYS A 1 376  ? 18.506  22.618  35.782  1.00 99.85  ? 376  LYS A O   1 
ATOM   2863  C  CB  . LYS A 1 376  ? 15.840  21.047  34.553  1.00 117.63 ? 376  LYS A CB  1 
ATOM   2864  C  CG  . LYS A 1 376  ? 14.320  20.987  34.315  1.00 125.28 ? 376  LYS A CG  1 
ATOM   2865  C  CD  . LYS A 1 376  ? 14.002  20.686  32.816  1.00 130.51 ? 376  LYS A CD  1 
ATOM   2866  C  CE  . LYS A 1 376  ? 12.546  20.273  32.561  1.00 136.08 ? 376  LYS A CE  1 
ATOM   2867  N  NZ  . LYS A 1 376  ? 11.876  21.194  31.587  1.00 141.97 ? 376  LYS A NZ  1 
ATOM   2868  N  N   . ASP A 1 377  ? 18.332  20.397  35.932  1.00 125.18 ? 377  ASP A N   1 
ATOM   2869  C  CA  . ASP A 1 377  ? 19.745  20.162  36.030  1.00 125.45 ? 377  ASP A CA  1 
ATOM   2870  C  C   . ASP A 1 377  ? 20.244  19.604  34.727  1.00 131.87 ? 377  ASP A C   1 
ATOM   2871  O  O   . ASP A 1 377  ? 19.464  19.285  33.833  1.00 137.14 ? 377  ASP A O   1 
ATOM   2872  C  CB  . ASP A 1 377  ? 19.947  19.068  37.030  1.00 123.79 ? 377  ASP A CB  1 
ATOM   2873  C  CG  . ASP A 1 377  ? 19.224  17.824  36.629  1.00 129.64 ? 377  ASP A CG  1 
ATOM   2874  O  OD1 . ASP A 1 377  ? 18.018  17.937  36.289  1.00 134.68 ? 377  ASP A OD1 1 
ATOM   2875  O  OD2 . ASP A 1 377  ? 19.877  16.756  36.620  1.00 131.13 ? 377  ASP A OD2 1 
ATOM   2876  N  N   . SER A 1 378  ? 21.551  19.409  34.656  1.00 150.95 ? 378  SER A N   1 
ATOM   2877  C  CA  . SER A 1 378  ? 22.206  18.869  33.476  1.00 153.85 ? 378  SER A CA  1 
ATOM   2878  C  C   . SER A 1 378  ? 21.649  17.525  33.030  1.00 132.65 ? 378  SER A C   1 
ATOM   2879  O  O   . SER A 1 378  ? 21.976  17.050  31.953  1.00 134.50 ? 378  SER A O   1 
ATOM   2880  C  CB  . SER A 1 378  ? 23.682  18.715  33.798  1.00 152.87 ? 378  SER A CB  1 
ATOM   2881  O  OG  . SER A 1 378  ? 23.887  18.972  35.191  1.00 149.36 ? 378  SER A OG  1 
ATOM   2882  N  N   . LEU A 1 379  ? 20.805  16.920  33.855  1.00 135.11 ? 379  LEU A N   1 
ATOM   2883  C  CA  . LEU A 1 379  ? 20.271  15.593  33.570  1.00 141.76 ? 379  LEU A CA  1 
ATOM   2884  C  C   . LEU A 1 379  ? 18.759  15.553  33.367  1.00 153.59 ? 379  LEU A C   1 
ATOM   2885  O  O   . LEU A 1 379  ? 18.148  14.483  33.236  1.00 159.31 ? 379  LEU A O   1 
ATOM   2886  C  CB  . LEU A 1 379  ? 20.668  14.650  34.686  1.00 138.26 ? 379  LEU A CB  1 
ATOM   2887  C  CG  . LEU A 1 379  ? 21.848  13.798  34.241  1.00 137.33 ? 379  LEU A CG  1 
ATOM   2888  C  CD1 . LEU A 1 379  ? 22.719  13.243  35.406  1.00 134.09 ? 379  LEU A CD1 1 
ATOM   2889  C  CD2 . LEU A 1 379  ? 21.322  12.688  33.302  1.00 142.52 ? 379  LEU A CD2 1 
ATOM   2890  N  N   . ASP A 1 380  ? 18.166  16.739  33.369  1.00 169.89 ? 380  ASP A N   1 
ATOM   2891  C  CA  . ASP A 1 380  ? 16.754  16.929  33.057  1.00 179.07 ? 380  ASP A CA  1 
ATOM   2892  C  C   . ASP A 1 380  ? 15.783  16.271  34.017  1.00 182.96 ? 380  ASP A C   1 
ATOM   2893  O  O   . ASP A 1 380  ? 14.839  15.606  33.592  1.00 187.65 ? 380  ASP A O   1 
ATOM   2894  C  CB  . ASP A 1 380  ? 16.445  16.516  31.625  1.00 189.10 ? 380  ASP A CB  1 
ATOM   2895  C  CG  . ASP A 1 380  ? 16.933  17.532  30.615  1.00 195.93 ? 380  ASP A CG  1 
ATOM   2896  O  OD1 . ASP A 1 380  ? 16.362  18.646  30.573  1.00 197.52 ? 380  ASP A OD1 1 
ATOM   2897  O  OD2 . ASP A 1 380  ? 17.887  17.216  29.867  1.00 200.34 ? 380  ASP A OD2 1 
ATOM   2898  N  N   . GLN A 1 381  ? 16.044  16.452  35.307  1.00 185.32 ? 381  GLN A N   1 
ATOM   2899  C  CA  . GLN A 1 381  ? 15.026  16.297  36.331  1.00 188.30 ? 381  GLN A CA  1 
ATOM   2900  C  C   . GLN A 1 381  ? 14.743  17.676  36.865  1.00 184.42 ? 381  GLN A C   1 
ATOM   2901  O  O   . GLN A 1 381  ? 15.549  18.591  36.697  1.00 180.13 ? 381  GLN A O   1 
ATOM   2902  C  CB  . GLN A 1 381  ? 15.502  15.442  37.496  1.00 190.09 ? 381  GLN A CB  1 
ATOM   2903  C  CG  . GLN A 1 381  ? 15.885  14.036  37.135  1.00 196.05 ? 381  GLN A CG  1 
ATOM   2904  C  CD  . GLN A 1 381  ? 17.307  13.727  37.551  1.00 197.03 ? 381  GLN A CD  1 
ATOM   2905  O  OE1 . GLN A 1 381  ? 17.548  12.951  38.482  1.00 198.22 ? 381  GLN A OE1 1 
ATOM   2906  N  NE2 . GLN A 1 381  ? 18.264  14.353  36.873  1.00 195.91 ? 381  GLN A NE2 1 
ATOM   2907  N  N   . LEU A 1 382  ? 13.596  17.814  37.515  1.00 153.11 ? 382  LEU A N   1 
ATOM   2908  C  CA  . LEU A 1 382  ? 13.241  19.054  38.175  1.00 149.00 ? 382  LEU A CA  1 
ATOM   2909  C  C   . LEU A 1 382  ? 14.133  19.209  39.378  1.00 145.72 ? 382  LEU A C   1 
ATOM   2910  O  O   . LEU A 1 382  ? 14.519  18.216  39.967  1.00 148.35 ? 382  LEU A O   1 
ATOM   2911  C  CB  . LEU A 1 382  ? 11.803  18.973  38.638  1.00 152.25 ? 382  LEU A CB  1 
ATOM   2912  C  CG  . LEU A 1 382  ? 10.845  19.308  37.511  1.00 157.08 ? 382  LEU A CG  1 
ATOM   2913  C  CD1 . LEU A 1 382  ? 9.413   19.169  37.972  1.00 163.00 ? 382  LEU A CD1 1 
ATOM   2914  C  CD2 . LEU A 1 382  ? 11.140  20.722  37.057  1.00 154.09 ? 382  LEU A CD2 1 
ATOM   2915  N  N   . VAL A 1 383  ? 14.465  20.436  39.756  1.00 131.36 ? 383  VAL A N   1 
ATOM   2916  C  CA  . VAL A 1 383  ? 15.270  20.645  40.956  1.00 124.50 ? 383  VAL A CA  1 
ATOM   2917  C  C   . VAL A 1 383  ? 14.718  21.825  41.711  1.00 125.92 ? 383  VAL A C   1 
ATOM   2918  O  O   . VAL A 1 383  ? 14.723  22.952  41.215  1.00 126.91 ? 383  VAL A O   1 
ATOM   2919  C  CB  . VAL A 1 383  ? 16.768  20.854  40.637  1.00 115.81 ? 383  VAL A CB  1 
ATOM   2920  C  CG1 . VAL A 1 383  ? 16.922  21.298  39.221  1.00 118.59 ? 383  VAL A CG1 1 
ATOM   2921  C  CG2 . VAL A 1 383  ? 17.408  21.869  41.573  1.00 107.28 ? 383  VAL A CG2 1 
ATOM   2922  N  N   . GLY A 1 384  ? 14.218  21.548  42.909  1.00 108.56 ? 384  GLY A N   1 
ATOM   2923  C  CA  . GLY A 1 384  ? 13.498  22.547  43.662  1.00 110.49 ? 384  GLY A CA  1 
ATOM   2924  C  C   . GLY A 1 384  ? 14.400  23.259  44.627  1.00 109.04 ? 384  GLY A C   1 
ATOM   2925  O  O   . GLY A 1 384  ? 15.504  22.787  44.909  1.00 107.49 ? 384  GLY A O   1 
ATOM   2926  N  N   . GLY A 1 385  ? 13.923  24.394  45.126  1.00 146.46 ? 385  GLY A N   1 
ATOM   2927  C  CA  . GLY A 1 385  ? 14.605  25.122  46.177  1.00 143.30 ? 385  GLY A CA  1 
ATOM   2928  C  C   . GLY A 1 385  ? 15.720  25.991  45.645  1.00 139.93 ? 385  GLY A C   1 
ATOM   2929  O  O   . GLY A 1 385  ? 16.824  26.036  46.199  1.00 137.37 ? 385  GLY A O   1 
ATOM   2930  N  N   . VAL A 1 386  ? 15.427  26.702  44.568  1.00 109.89 ? 386  VAL A N   1 
ATOM   2931  C  CA  . VAL A 1 386  ? 16.455  27.456  43.903  1.00 106.27 ? 386  VAL A CA  1 
ATOM   2932  C  C   . VAL A 1 386  ? 15.908  28.810  43.559  1.00 103.17 ? 386  VAL A C   1 
ATOM   2933  O  O   . VAL A 1 386  ? 14.779  28.905  43.109  1.00 106.40 ? 386  VAL A O   1 
ATOM   2934  C  CB  . VAL A 1 386  ? 16.931  26.714  42.629  1.00 96.29  ? 386  VAL A CB  1 
ATOM   2935  C  CG1 . VAL A 1 386  ? 18.453  26.824  42.465  1.00 91.80  ? 386  VAL A CG1 1 
ATOM   2936  C  CG2 . VAL A 1 386  ? 16.534  25.233  42.667  1.00 96.84  ? 386  VAL A CG2 1 
ATOM   2937  N  N   . PRO A 1 387  ? 16.726  29.852  43.762  1.00 102.76 ? 387  PRO A N   1 
ATOM   2938  C  CA  . PRO A 1 387  ? 16.486  31.284  43.549  1.00 107.18 ? 387  PRO A CA  1 
ATOM   2939  C  C   . PRO A 1 387  ? 16.299  31.642  42.047  1.00 113.52 ? 387  PRO A C   1 
ATOM   2940  O  O   . PRO A 1 387  ? 16.884  30.973  41.216  1.00 114.48 ? 387  PRO A O   1 
ATOM   2941  C  CB  . PRO A 1 387  ? 17.752  31.944  44.118  1.00 103.83 ? 387  PRO A CB  1 
ATOM   2942  C  CG  . PRO A 1 387  ? 18.738  30.848  44.351  1.00 93.08  ? 387  PRO A CG  1 
ATOM   2943  C  CD  . PRO A 1 387  ? 18.150  29.556  43.963  1.00 94.87  ? 387  PRO A CD  1 
ATOM   2944  N  N   . VAL A 1 388  ? 15.544  32.691  41.711  1.00 110.98 ? 388  VAL A N   1 
ATOM   2945  C  CA  . VAL A 1 388  ? 15.044  32.881  40.358  1.00 113.55 ? 388  VAL A CA  1 
ATOM   2946  C  C   . VAL A 1 388  ? 14.745  34.345  40.013  1.00 115.66 ? 388  VAL A C   1 
ATOM   2947  O  O   . VAL A 1 388  ? 13.617  34.679  39.724  1.00 118.08 ? 388  VAL A O   1 
ATOM   2948  C  CB  . VAL A 1 388  ? 13.733  32.081  40.213  1.00 116.94 ? 388  VAL A CB  1 
ATOM   2949  C  CG1 . VAL A 1 388  ? 13.075  32.333  38.902  1.00 121.52 ? 388  VAL A CG1 1 
ATOM   2950  C  CG2 . VAL A 1 388  ? 13.994  30.606  40.376  1.00 114.49 ? 388  VAL A CG2 1 
ATOM   2951  N  N   . THR A 1 389  ? 15.746  35.219  40.017  1.00 143.29 ? 389  THR A N   1 
ATOM   2952  C  CA  . THR A 1 389  ? 15.507  36.662  39.824  1.00 145.17 ? 389  THR A CA  1 
ATOM   2953  C  C   . THR A 1 389  ? 14.886  37.029  38.466  1.00 149.55 ? 389  THR A C   1 
ATOM   2954  O  O   . THR A 1 389  ? 15.460  36.722  37.423  1.00 155.27 ? 389  THR A O   1 
ATOM   2955  C  CB  . THR A 1 389  ? 16.794  37.486  40.000  1.00 157.30 ? 389  THR A CB  1 
ATOM   2956  O  OG1 . THR A 1 389  ? 17.881  36.620  40.314  1.00 156.42 ? 389  THR A OG1 1 
ATOM   2957  C  CG2 . THR A 1 389  ? 16.652  38.492  41.114  1.00 155.54 ? 389  THR A CG2 1 
ATOM   2958  N  N   . LEU A 1 390  ? 13.741  37.724  38.486  1.00 107.51 ? 390  LEU A N   1 
ATOM   2959  C  CA  . LEU A 1 390  ? 12.995  38.087  37.261  1.00 108.71 ? 390  LEU A CA  1 
ATOM   2960  C  C   . LEU A 1 390  ? 12.997  39.575  36.895  1.00 114.54 ? 390  LEU A C   1 
ATOM   2961  O  O   . LEU A 1 390  ? 12.002  40.240  37.118  1.00 120.24 ? 390  LEU A O   1 
ATOM   2962  C  CB  . LEU A 1 390  ? 11.528  37.623  37.345  1.00 113.77 ? 390  LEU A CB  1 
ATOM   2963  C  CG  . LEU A 1 390  ? 10.693  38.010  36.123  1.00 114.95 ? 390  LEU A CG  1 
ATOM   2964  C  CD1 . LEU A 1 390  ? 11.418  37.455  34.952  1.00 120.18 ? 390  LEU A CD1 1 
ATOM   2965  C  CD2 . LEU A 1 390  ? 9.269   37.496  36.149  1.00 118.97 ? 390  LEU A CD2 1 
ATOM   2966  N  N   . ASN A 1 391  ? 14.078  40.097  36.319  1.00 134.97 ? 391  ASN A N   1 
ATOM   2967  C  CA  . ASN A 1 391  ? 14.077  41.477  35.829  1.00 140.69 ? 391  ASN A CA  1 
ATOM   2968  C  C   . ASN A 1 391  ? 13.264  41.613  34.553  1.00 147.42 ? 391  ASN A C   1 
ATOM   2969  O  O   . ASN A 1 391  ? 13.389  40.809  33.640  1.00 151.34 ? 391  ASN A O   1 
ATOM   2970  C  CB  . ASN A 1 391  ? 15.489  41.921  35.564  1.00 144.38 ? 391  ASN A CB  1 
ATOM   2971  C  CG  . ASN A 1 391  ? 16.301  41.917  36.791  1.00 144.55 ? 391  ASN A CG  1 
ATOM   2972  O  OD1 . ASN A 1 391  ? 16.467  40.890  37.437  1.00 141.71 ? 391  ASN A OD1 1 
ATOM   2973  N  ND2 . ASN A 1 391  ? 16.806  43.072  37.146  1.00 146.86 ? 391  ASN A ND2 1 
ATOM   2974  N  N   . ALA A 1 392  ? 12.445  42.645  34.462  1.00 142.32 ? 392  ALA A N   1 
ATOM   2975  C  CA  . ALA A 1 392  ? 11.581  42.786  33.303  1.00 145.41 ? 392  ALA A CA  1 
ATOM   2976  C  C   . ALA A 1 392  ? 11.752  44.187  32.741  1.00 146.42 ? 392  ALA A C   1 
ATOM   2977  O  O   . ALA A 1 392  ? 12.499  44.991  33.304  1.00 145.90 ? 392  ALA A O   1 
ATOM   2978  C  CB  . ALA A 1 392  ? 10.135  42.524  33.692  1.00 146.40 ? 392  ALA A CB  1 
ATOM   2979  N  N   . GLN A 1 393  ? 11.081  44.461  31.620  1.00 148.74 ? 393  GLN A N   1 
ATOM   2980  C  CA  . GLN A 1 393  ? 11.090  45.771  30.956  1.00 157.13 ? 393  GLN A CA  1 
ATOM   2981  C  C   . GLN A 1 393  ? 9.864   45.836  30.047  1.00 161.75 ? 393  GLN A C   1 
ATOM   2982  O  O   . GLN A 1 393  ? 9.403   44.822  29.509  1.00 160.84 ? 393  GLN A O   1 
ATOM   2983  C  CB  . GLN A 1 393  ? 12.377  45.970  30.155  1.00 159.85 ? 393  GLN A CB  1 
ATOM   2984  C  CG  . GLN A 1 393  ? 12.627  47.386  29.622  1.00 163.63 ? 393  GLN A CG  1 
ATOM   2985  C  CD  . GLN A 1 393  ? 12.370  47.528  28.113  1.00 168.68 ? 393  GLN A CD  1 
ATOM   2986  O  OE1 . GLN A 1 393  ? 11.980  48.599  27.629  1.00 172.66 ? 393  GLN A OE1 1 
ATOM   2987  N  NE2 . GLN A 1 393  ? 12.581  46.444  27.368  1.00 168.52 ? 393  GLN A NE2 1 
ATOM   2988  N  N   . THR A 1 394  ? 9.319   47.029  29.899  1.00 203.79 ? 394  THR A N   1 
ATOM   2989  C  CA  . THR A 1 394  ? 8.088   47.186  29.158  1.00 210.43 ? 394  THR A CA  1 
ATOM   2990  C  C   . THR A 1 394  ? 8.015   48.595  28.608  1.00 224.11 ? 394  THR A C   1 
ATOM   2991  O  O   . THR A 1 394  ? 8.839   49.442  28.960  1.00 227.71 ? 394  THR A O   1 
ATOM   2992  C  CB  . THR A 1 394  ? 6.859   46.878  30.038  1.00 203.00 ? 394  THR A CB  1 
ATOM   2993  O  OG1 . THR A 1 394  ? 6.153   45.761  29.487  1.00 203.33 ? 394  THR A OG1 1 
ATOM   2994  C  CG2 . THR A 1 394  ? 5.918   48.076  30.135  1.00 206.22 ? 394  THR A CG2 1 
ATOM   2995  N  N   . ILE A 1 395  ? 7.049   48.834  27.724  1.00 171.23 ? 395  ILE A N   1 
ATOM   2996  C  CA  . ILE A 1 395  ? 6.865   50.144  27.136  1.00 179.00 ? 395  ILE A CA  1 
ATOM   2997  C  C   . ILE A 1 395  ? 5.376   50.427  27.003  1.00 186.76 ? 395  ILE A C   1 
ATOM   2998  O  O   . ILE A 1 395  ? 4.571   49.520  26.816  1.00 188.61 ? 395  ILE A O   1 
ATOM   2999  C  CB  . ILE A 1 395  ? 7.574   50.217  25.802  1.00 182.04 ? 395  ILE A CB  1 
ATOM   3000  C  CG1 . ILE A 1 395  ? 6.790   49.436  24.755  1.00 183.77 ? 395  ILE A CG1 1 
ATOM   3001  C  CG2 . ILE A 1 395  ? 9.000   49.685  25.940  1.00 179.52 ? 395  ILE A CG2 1 
ATOM   3002  C  CD1 . ILE A 1 395  ? 6.111   50.338  23.740  1.00 190.71 ? 395  ILE A CD1 1 
ATOM   3003  N  N   . ASP A 1 396  ? 5.016   51.690  27.164  1.00 189.67 ? 396  ASP A N   1 
ATOM   3004  C  CA  . ASP A 1 396  ? 3.629   52.097  27.150  1.00 194.11 ? 396  ASP A CA  1 
ATOM   3005  C  C   . ASP A 1 396  ? 3.194   51.940  25.725  1.00 198.85 ? 396  ASP A C   1 
ATOM   3006  O  O   . ASP A 1 396  ? 4.035   51.796  24.853  1.00 200.92 ? 396  ASP A O   1 
ATOM   3007  C  CB  . ASP A 1 396  ? 3.533   53.570  27.528  1.00 200.44 ? 396  ASP A CB  1 
ATOM   3008  C  CG  . ASP A 1 396  ? 2.320   53.881  28.389  1.00 206.75 ? 396  ASP A CG  1 
ATOM   3009  O  OD1 . ASP A 1 396  ? 2.189   55.046  28.821  1.00 212.35 ? 396  ASP A OD1 1 
ATOM   3010  O  OD2 . ASP A 1 396  ? 1.505   52.968  28.646  1.00 205.74 ? 396  ASP A OD2 1 
ATOM   3011  N  N   . VAL A 1 397  ? 1.888   51.966  25.481  1.00 222.60 ? 397  VAL A N   1 
ATOM   3012  C  CA  . VAL A 1 397  ? 1.384   52.206  24.136  1.00 231.70 ? 397  VAL A CA  1 
ATOM   3013  C  C   . VAL A 1 397  ? 1.820   53.627  23.798  1.00 235.66 ? 397  VAL A C   1 
ATOM   3014  O  O   . VAL A 1 397  ? 2.022   53.982  22.638  1.00 240.04 ? 397  VAL A O   1 
ATOM   3015  C  CB  . VAL A 1 397  ? -0.155  52.076  24.047  1.00 236.83 ? 397  VAL A CB  1 
ATOM   3016  C  CG1 . VAL A 1 397  ? -0.845  53.366  24.499  1.00 238.34 ? 397  VAL A CG1 1 
ATOM   3017  C  CG2 . VAL A 1 397  ? -0.575  51.708  22.629  1.00 244.15 ? 397  VAL A CG2 1 
ATOM   3018  N  N   . ASN A 1 398  ? 1.983   54.424  24.849  1.00 258.45 ? 398  ASN A N   1 
ATOM   3019  C  CA  . ASN A 1 398  ? 2.459   55.795  24.752  1.00 263.27 ? 398  ASN A CA  1 
ATOM   3020  C  C   . ASN A 1 398  ? 3.912   55.864  24.297  1.00 261.48 ? 398  ASN A C   1 
ATOM   3021  O  O   . ASN A 1 398  ? 4.547   56.912  24.397  1.00 261.22 ? 398  ASN A O   1 
ATOM   3022  C  CB  . ASN A 1 398  ? 2.329   56.470  26.118  1.00 263.89 ? 398  ASN A CB  1 
ATOM   3023  C  CG  . ASN A 1 398  ? 1.802   57.885  26.026  1.00 272.59 ? 398  ASN A CG  1 
ATOM   3024  O  OD1 . ASN A 1 398  ? 1.284   58.296  24.993  1.00 280.21 ? 398  ASN A OD1 1 
ATOM   3025  N  ND2 . ASN A 1 398  ? 1.923   58.637  27.115  1.00 271.27 ? 398  ASN A ND2 1 
ATOM   3026  N  N   . GLN A 1 399  ? 4.431   54.743  23.800  1.00 233.18 ? 399  GLN A N   1 
ATOM   3027  C  CA  . GLN A 1 399  ? 5.861   54.598  23.512  1.00 233.81 ? 399  GLN A CA  1 
ATOM   3028  C  C   . GLN A 1 399  ? 6.715   55.188  24.638  1.00 231.01 ? 399  GLN A C   1 
ATOM   3029  O  O   . GLN A 1 399  ? 7.669   55.938  24.379  1.00 231.86 ? 399  GLN A O   1 
ATOM   3030  C  CB  . GLN A 1 399  ? 6.247   55.188  22.149  1.00 241.39 ? 399  GLN A CB  1 
ATOM   3031  C  CG  . GLN A 1 399  ? 5.730   54.397  20.943  1.00 245.64 ? 399  GLN A CG  1 
ATOM   3032  C  CD  . GLN A 1 399  ? 6.374   53.026  20.796  1.00 242.04 ? 399  GLN A CD  1 
ATOM   3033  O  OE1 . GLN A 1 399  ? 7.585   52.916  20.629  1.00 241.58 ? 399  GLN A OE1 1 
ATOM   3034  N  NE2 . GLN A 1 399  ? 5.561   51.976  20.845  1.00 239.81 ? 399  GLN A NE2 1 
ATOM   3035  N  N   . GLU A 1 400  ? 6.338   54.847  25.879  1.00 230.07 ? 400  GLU A N   1 
ATOM   3036  C  CA  . GLU A 1 400  ? 7.092   55.193  27.092  1.00 226.20 ? 400  GLU A CA  1 
ATOM   3037  C  C   . GLU A 1 400  ? 7.643   53.920  27.753  1.00 215.40 ? 400  GLU A C   1 
ATOM   3038  O  O   . GLU A 1 400  ? 6.929   52.932  27.872  1.00 212.12 ? 400  GLU A O   1 
ATOM   3039  C  CB  . GLU A 1 400  ? 6.207   55.970  28.075  1.00 229.04 ? 400  GLU A CB  1 
ATOM   3040  C  CG  . GLU A 1 400  ? 6.981   56.885  29.017  1.00 232.93 ? 400  GLU A CG  1 
ATOM   3041  C  CD  . GLU A 1 400  ? 6.098   57.924  29.693  1.00 240.41 ? 400  GLU A CD  1 
ATOM   3042  O  OE1 . GLU A 1 400  ? 6.275   59.129  29.423  1.00 245.77 ? 400  GLU A OE1 1 
ATOM   3043  O  OE2 . GLU A 1 400  ? 5.224   57.540  30.494  1.00 240.63 ? 400  GLU A OE2 1 
ATOM   3044  N  N   . THR A 1 401  ? 8.910   53.940  28.165  1.00 253.06 ? 401  THR A N   1 
ATOM   3045  C  CA  . THR A 1 401  ? 9.543   52.744  28.724  1.00 242.79 ? 401  THR A CA  1 
ATOM   3046  C  C   . THR A 1 401  ? 9.345   52.603  30.209  1.00 234.45 ? 401  THR A C   1 
ATOM   3047  O  O   . THR A 1 401  ? 8.878   53.522  30.881  1.00 237.69 ? 401  THR A O   1 
ATOM   3048  C  CB  . THR A 1 401  ? 11.061  52.732  28.544  1.00 241.38 ? 401  THR A CB  1 
ATOM   3049  O  OG1 . THR A 1 401  ? 11.645  53.745  29.375  1.00 240.73 ? 401  THR A OG1 1 
ATOM   3050  C  CG2 . THR A 1 401  ? 11.427  52.952  27.105  1.00 247.25 ? 401  THR A CG2 1 
ATOM   3051  N  N   . SER A 1 402  ? 9.752   51.446  30.717  1.00 212.26 ? 402  SER A N   1 
ATOM   3052  C  CA  . SER A 1 402  ? 9.622   51.140  32.125  1.00 202.55 ? 402  SER A CA  1 
ATOM   3053  C  C   . SER A 1 402  ? 10.608  50.060  32.513  1.00 192.58 ? 402  SER A C   1 
ATOM   3054  O  O   . SER A 1 402  ? 10.564  48.947  31.982  1.00 187.86 ? 402  SER A O   1 
ATOM   3055  C  CB  . SER A 1 402  ? 8.198   50.681  32.443  1.00 203.07 ? 402  SER A CB  1 
ATOM   3056  O  OG  . SER A 1 402  ? 7.825   49.575  31.640  1.00 203.26 ? 402  SER A OG  1 
ATOM   3057  N  N   . ASP A 1 403  ? 11.512  50.406  33.424  1.00 203.44 ? 403  ASP A N   1 
ATOM   3058  C  CA  . ASP A 1 403  ? 12.354  49.411  34.068  1.00 198.15 ? 403  ASP A CA  1 
ATOM   3059  C  C   . ASP A 1 403  ? 11.768  48.942  35.386  1.00 191.86 ? 403  ASP A C   1 
ATOM   3060  O  O   . ASP A 1 403  ? 11.747  49.665  36.375  1.00 192.14 ? 403  ASP A O   1 
ATOM   3061  C  CB  . ASP A 1 403  ? 13.773  49.916  34.270  1.00 201.69 ? 403  ASP A CB  1 
ATOM   3062  C  CG  . ASP A 1 403  ? 14.726  49.343  33.260  1.00 206.49 ? 403  ASP A CG  1 
ATOM   3063  O  OD1 . ASP A 1 403  ? 14.658  48.122  32.989  1.00 203.41 ? 403  ASP A OD1 1 
ATOM   3064  O  OD2 . ASP A 1 403  ? 15.537  50.123  32.734  1.00 212.29 ? 403  ASP A OD2 1 
ATOM   3065  N  N   . LEU A 1 404  ? 11.293  47.712  35.384  1.00 131.06 ? 404  LEU A N   1 
ATOM   3066  C  CA  . LEU A 1 404  ? 10.726  47.140  36.567  1.00 124.75 ? 404  LEU A CA  1 
ATOM   3067  C  C   . LEU A 1 404  ? 11.741  46.883  37.667  1.00 122.15 ? 404  LEU A C   1 
ATOM   3068  O  O   . LEU A 1 404  ? 12.935  47.244  37.594  1.00 123.52 ? 404  LEU A O   1 
ATOM   3069  C  CB  . LEU A 1 404  ? 10.015  45.827  36.250  1.00 117.89 ? 404  LEU A CB  1 
ATOM   3070  C  CG  . LEU A 1 404  ? 8.611   45.898  35.672  1.00 117.50 ? 404  LEU A CG  1 
ATOM   3071  C  CD1 . LEU A 1 404  ? 8.054   44.513  35.657  1.00 122.40 ? 404  LEU A CD1 1 
ATOM   3072  C  CD2 . LEU A 1 404  ? 7.765   46.792  36.514  1.00 116.28 ? 404  LEU A CD2 1 
ATOM   3073  N  N   . ASP A 1 405  ? 11.197  46.227  38.687  1.00 157.21 ? 405  ASP A N   1 
ATOM   3074  C  CA  . ASP A 1 405  ? 11.872  45.955  39.927  1.00 151.88 ? 405  ASP A CA  1 
ATOM   3075  C  C   . ASP A 1 405  ? 11.914  44.480  40.151  1.00 144.50 ? 405  ASP A C   1 
ATOM   3076  O  O   . ASP A 1 405  ? 10.916  43.772  39.996  1.00 143.55 ? 405  ASP A O   1 
ATOM   3077  C  CB  . ASP A 1 405  ? 11.175  46.650  41.078  1.00 156.20 ? 405  ASP A CB  1 
ATOM   3078  C  CG  . ASP A 1 405  ? 11.576  48.088  41.182  1.00 174.15 ? 405  ASP A CG  1 
ATOM   3079  O  OD1 . ASP A 1 405  ? 12.799  48.334  41.002  1.00 175.85 ? 405  ASP A OD1 1 
ATOM   3080  O  OD2 . ASP A 1 405  ? 10.686  48.949  41.419  1.00 174.28 ? 405  ASP A OD2 1 
ATOM   3081  N  N   . PRO A 1 406  ? 13.089  44.032  40.560  1.00 125.76 ? 406  PRO A N   1 
ATOM   3082  C  CA  . PRO A 1 406  ? 13.570  42.661  40.510  1.00 122.53 ? 406  PRO A CA  1 
ATOM   3083  C  C   . PRO A 1 406  ? 12.733  41.833  41.416  1.00 125.20 ? 406  PRO A C   1 
ATOM   3084  O  O   . PRO A 1 406  ? 12.779  42.072  42.607  1.00 128.22 ? 406  PRO A O   1 
ATOM   3085  C  CB  . PRO A 1 406  ? 14.976  42.762  41.101  1.00 120.35 ? 406  PRO A CB  1 
ATOM   3086  C  CG  . PRO A 1 406  ? 15.324  44.223  41.072  1.00 123.30 ? 406  PRO A CG  1 
ATOM   3087  C  CD  . PRO A 1 406  ? 14.039  44.935  41.222  1.00 124.49 ? 406  PRO A CD  1 
ATOM   3088  N  N   . SER A 1 407  ? 11.971  40.899  40.886  1.00 136.86 ? 407  SER A N   1 
ATOM   3089  C  CA  . SER A 1 407  ? 11.323  39.962  41.761  1.00 139.04 ? 407  SER A CA  1 
ATOM   3090  C  C   . SER A 1 407  ? 12.221  38.766  41.860  1.00 137.94 ? 407  SER A C   1 
ATOM   3091  O  O   . SER A 1 407  ? 13.031  38.553  40.963  1.00 139.60 ? 407  SER A O   1 
ATOM   3092  C  CB  . SER A 1 407  ? 9.969   39.582  41.217  1.00 143.37 ? 407  SER A CB  1 
ATOM   3093  O  OG  . SER A 1 407  ? 9.175   40.745  41.117  1.00 148.28 ? 407  SER A OG  1 
ATOM   3094  N  N   . LYS A 1 408  ? 12.096  38.012  42.954  1.00 145.53 ? 408  LYS A N   1 
ATOM   3095  C  CA  . LYS A 1 408  ? 12.854  36.783  43.163  1.00 139.88 ? 408  LYS A CA  1 
ATOM   3096  C  C   . LYS A 1 408  ? 11.988  35.829  43.899  1.00 134.72 ? 408  LYS A C   1 
ATOM   3097  O  O   . LYS A 1 408  ? 11.532  36.149  44.970  1.00 135.01 ? 408  LYS A O   1 
ATOM   3098  C  CB  . LYS A 1 408  ? 14.083  37.019  44.031  1.00 138.35 ? 408  LYS A CB  1 
ATOM   3099  C  CG  . LYS A 1 408  ? 14.619  35.744  44.650  1.00 140.23 ? 408  LYS A CG  1 
ATOM   3100  C  CD  . LYS A 1 408  ? 15.808  36.044  45.533  1.00 143.23 ? 408  LYS A CD  1 
ATOM   3101  C  CE  . LYS A 1 408  ? 16.682  37.143  44.951  1.00 145.45 ? 408  LYS A CE  1 
ATOM   3102  N  NZ  . LYS A 1 408  ? 18.036  37.200  45.577  1.00 143.41 ? 408  LYS A NZ  1 
ATOM   3103  N  N   . SER A 1 409  ? 11.743  34.667  43.325  1.00 107.49 ? 409  SER A N   1 
ATOM   3104  C  CA  . SER A 1 409  ? 11.081  33.618  44.059  1.00 110.98 ? 409  SER A CA  1 
ATOM   3105  C  C   . SER A 1 409  ? 12.131  32.600  44.217  1.00 116.61 ? 409  SER A C   1 
ATOM   3106  O  O   . SER A 1 409  ? 13.304  32.875  43.969  1.00 110.84 ? 409  SER A O   1 
ATOM   3107  C  CB  . SER A 1 409  ? 9.913   32.987  43.299  1.00 119.58 ? 409  SER A CB  1 
ATOM   3108  O  OG  . SER A 1 409  ? 9.336   31.913  44.045  1.00 120.43 ? 409  SER A OG  1 
ATOM   3109  N  N   . VAL A 1 410  ? 11.687  31.420  44.624  1.00 125.10 ? 410  VAL A N   1 
ATOM   3110  C  CA  . VAL A 1 410  ? 12.514  30.248  44.624  1.00 128.80 ? 410  VAL A CA  1 
ATOM   3111  C  C   . VAL A 1 410  ? 11.632  29.088  44.194  1.00 137.71 ? 410  VAL A C   1 
ATOM   3112  O  O   . VAL A 1 410  ? 10.425  29.070  44.448  1.00 141.22 ? 410  VAL A O   1 
ATOM   3113  C  CB  . VAL A 1 410  ? 13.129  30.029  45.997  1.00 126.13 ? 410  VAL A CB  1 
ATOM   3114  C  CG1 . VAL A 1 410  ? 13.939  28.740  46.012  1.00 127.90 ? 410  VAL A CG1 1 
ATOM   3115  C  CG2 . VAL A 1 410  ? 14.000  31.238  46.359  1.00 120.93 ? 410  VAL A CG2 1 
ATOM   3116  N  N   . THR A 1 411  ? 12.255  28.155  43.492  1.00 103.32 ? 411  THR A N   1 
ATOM   3117  C  CA  . THR A 1 411  ? 11.570  27.060  42.852  1.00 104.21 ? 411  THR A CA  1 
ATOM   3118  C  C   . THR A 1 411  ? 10.987  26.115  43.878  1.00 103.47 ? 411  THR A C   1 
ATOM   3119  O  O   . THR A 1 411  ? 11.685  25.700  44.793  1.00 96.50  ? 411  THR A O   1 
ATOM   3120  C  CB  . THR A 1 411  ? 12.580  26.298  42.018  1.00 103.28 ? 411  THR A CB  1 
ATOM   3121  O  OG1 . THR A 1 411  ? 12.177  24.932  41.890  1.00 108.22 ? 411  THR A OG1 1 
ATOM   3122  C  CG2 . THR A 1 411  ? 13.842  26.323  42.725  1.00 96.10  ? 411  THR A CG2 1 
ATOM   3123  N  N   . ARG A 1 412  ? 9.720   25.749  43.688  1.00 126.56 ? 412  ARG A N   1 
ATOM   3124  C  CA  . ARG A 1 412  ? 9.030   24.781  44.541  1.00 137.65 ? 412  ARG A CA  1 
ATOM   3125  C  C   . ARG A 1 412  ? 9.763   23.433  44.682  1.00 136.25 ? 412  ARG A C   1 
ATOM   3126  O  O   . ARG A 1 412  ? 10.653  23.122  43.899  1.00 135.03 ? 412  ARG A O   1 
ATOM   3127  C  CB  . ARG A 1 412  ? 7.599   24.551  44.034  1.00 153.27 ? 412  ARG A CB  1 
ATOM   3128  C  CG  . ARG A 1 412  ? 6.686   23.839  45.039  1.00 166.05 ? 412  ARG A CG  1 
ATOM   3129  C  CD  . ARG A 1 412  ? 5.285   23.557  44.494  1.00 181.35 ? 412  ARG A CD  1 
ATOM   3130  N  NE  . ARG A 1 412  ? 4.255   24.384  45.112  1.00 188.11 ? 412  ARG A NE  1 
ATOM   3131  C  CZ  . ARG A 1 412  ? 2.964   24.312  44.810  1.00 197.44 ? 412  ARG A CZ  1 
ATOM   3132  N  NH1 . ARG A 1 412  ? 2.545   23.449  43.898  1.00 203.61 ? 412  ARG A NH1 1 
ATOM   3133  N  NH2 . ARG A 1 412  ? 2.093   25.103  45.420  1.00 199.06 ? 412  ARG A NH2 1 
ATOM   3134  N  N   . VAL A 1 413  ? 9.361   22.639  45.677  1.00 125.61 ? 413  VAL A N   1 
ATOM   3135  C  CA  . VAL A 1 413  ? 10.029  21.384  46.034  1.00 124.40 ? 413  VAL A CA  1 
ATOM   3136  C  C   . VAL A 1 413  ? 9.441   20.176  45.328  1.00 128.54 ? 413  VAL A C   1 
ATOM   3137  O  O   . VAL A 1 413  ? 10.142  19.224  44.980  1.00 126.40 ? 413  VAL A O   1 
ATOM   3138  C  CB  . VAL A 1 413  ? 9.864   21.104  47.531  1.00 126.59 ? 413  VAL A CB  1 
ATOM   3139  C  CG1 . VAL A 1 413  ? 10.901  20.091  47.985  1.00 123.24 ? 413  VAL A CG1 1 
ATOM   3140  C  CG2 . VAL A 1 413  ? 9.965   22.392  48.348  1.00 124.96 ? 413  VAL A CG2 1 
ATOM   3141  N  N   . ASP A 1 414  ? 8.127   20.220  45.169  1.00 178.91 ? 414  ASP A N   1 
ATOM   3142  C  CA  . ASP A 1 414  ? 7.375   19.183  44.491  1.00 184.33 ? 414  ASP A CA  1 
ATOM   3143  C  C   . ASP A 1 414  ? 7.169   19.554  43.027  1.00 182.86 ? 414  ASP A C   1 
ATOM   3144  O  O   . ASP A 1 414  ? 6.833   18.704  42.201  1.00 185.77 ? 414  ASP A O   1 
ATOM   3145  C  CB  . ASP A 1 414  ? 6.004   19.055  45.150  1.00 194.05 ? 414  ASP A CB  1 
ATOM   3146  C  CG  . ASP A 1 414  ? 5.276   20.392  45.245  1.00 199.92 ? 414  ASP A CG  1 
ATOM   3147  O  OD1 . ASP A 1 414  ? 5.674   21.225  46.094  1.00 198.27 ? 414  ASP A OD1 1 
ATOM   3148  O  OD2 . ASP A 1 414  ? 4.306   20.605  44.479  1.00 205.40 ? 414  ASP A OD2 1 
ATOM   3149  N  N   . ASP A 1 415  ? 7.374   20.835  42.724  1.00 162.01 ? 415  ASP A N   1 
ATOM   3150  C  CA  . ASP A 1 415  ? 6.939   21.434  41.466  1.00 163.69 ? 415  ASP A CA  1 
ATOM   3151  C  C   . ASP A 1 415  ? 8.080   21.727  40.514  1.00 152.05 ? 415  ASP A C   1 
ATOM   3152  O  O   . ASP A 1 415  ? 7.964   21.534  39.306  1.00 151.09 ? 415  ASP A O   1 
ATOM   3153  C  CB  . ASP A 1 415  ? 6.233   22.751  41.753  1.00 172.97 ? 415  ASP A CB  1 
ATOM   3154  C  CG  . ASP A 1 415  ? 5.485   23.272  40.566  1.00 183.84 ? 415  ASP A CG  1 
ATOM   3155  O  OD1 . ASP A 1 415  ? 5.668   22.709  39.469  1.00 188.30 ? 415  ASP A OD1 1 
ATOM   3156  O  OD2 . ASP A 1 415  ? 4.713   24.243  40.731  1.00 187.23 ? 415  ASP A OD2 1 
ATOM   3157  N  N   . GLY A 1 416  ? 9.176   22.215  41.073  1.00 129.95 ? 416  GLY A N   1 
ATOM   3158  C  CA  . GLY A 1 416  ? 10.311  22.622  40.281  1.00 125.76 ? 416  GLY A CA  1 
ATOM   3159  C  C   . GLY A 1 416  ? 9.982   23.959  39.668  1.00 130.40 ? 416  GLY A C   1 
ATOM   3160  O  O   . GLY A 1 416  ? 10.770  24.530  38.914  1.00 131.32 ? 416  GLY A O   1 
ATOM   3161  N  N   . VAL A 1 417  ? 8.796   24.452  40.001  1.00 131.39 ? 417  VAL A N   1 
ATOM   3162  C  CA  . VAL A 1 417  ? 8.316   25.712  39.475  1.00 133.38 ? 417  VAL A CA  1 
ATOM   3163  C  C   . VAL A 1 417  ? 8.539   26.872  40.411  1.00 129.97 ? 417  VAL A C   1 
ATOM   3164  O  O   . VAL A 1 417  ? 8.178   26.819  41.578  1.00 129.59 ? 417  VAL A O   1 
ATOM   3165  C  CB  . VAL A 1 417  ? 6.822   25.647  39.201  1.00 143.21 ? 417  VAL A CB  1 
ATOM   3166  C  CG1 . VAL A 1 417  ? 6.254   27.044  39.009  1.00 145.87 ? 417  VAL A CG1 1 
ATOM   3167  C  CG2 . VAL A 1 417  ? 6.558   24.771  37.999  1.00 147.72 ? 417  VAL A CG2 1 
ATOM   3168  N  N   . ALA A 1 418  ? 9.128   27.928  39.876  1.00 137.72 ? 418  ALA A N   1 
ATOM   3169  C  CA  . ALA A 1 418  ? 9.233   29.193  40.575  1.00 137.82 ? 418  ALA A CA  1 
ATOM   3170  C  C   . ALA A 1 418  ? 8.171   30.177  40.056  1.00 140.16 ? 418  ALA A C   1 
ATOM   3171  O  O   . ALA A 1 418  ? 8.452   31.010  39.193  1.00 140.65 ? 418  ALA A O   1 
ATOM   3172  C  CB  . ALA A 1 418  ? 10.632  29.771  40.406  1.00 134.95 ? 418  ALA A CB  1 
ATOM   3173  N  N   . SER A 1 419  ? 6.962   30.108  40.607  1.00 129.43 ? 419  SER A N   1 
ATOM   3174  C  CA  . SER A 1 419  ? 5.860   30.960  40.154  1.00 133.76 ? 419  SER A CA  1 
ATOM   3175  C  C   . SER A 1 419  ? 6.117   32.443  40.380  1.00 127.63 ? 419  SER A C   1 
ATOM   3176  O  O   . SER A 1 419  ? 6.607   32.830  41.429  1.00 124.73 ? 419  SER A O   1 
ATOM   3177  C  CB  . SER A 1 419  ? 4.588   30.560  40.886  1.00 139.96 ? 419  SER A CB  1 
ATOM   3178  O  OG  . SER A 1 419  ? 4.656   29.200  41.260  1.00 142.42 ? 419  SER A OG  1 
ATOM   3179  N  N   . PHE A 1 420  ? 5.769   33.269  39.403  1.00 130.58 ? 420  PHE A N   1 
ATOM   3180  C  CA  . PHE A 1 420  ? 5.829   34.716  39.558  1.00 134.51 ? 420  PHE A CA  1 
ATOM   3181  C  C   . PHE A 1 420  ? 4.517   35.349  39.141  1.00 124.05 ? 420  PHE A C   1 
ATOM   3182  O  O   . PHE A 1 420  ? 3.649   34.664  38.625  1.00 134.34 ? 420  PHE A O   1 
ATOM   3183  C  CB  . PHE A 1 420  ? 6.827   35.280  38.603  1.00 132.84 ? 420  PHE A CB  1 
ATOM   3184  C  CG  . PHE A 1 420  ? 8.210   35.082  38.993  1.00 115.66 ? 420  PHE A CG  1 
ATOM   3185  C  CD1 . PHE A 1 420  ? 8.933   36.140  39.488  1.00 113.31 ? 420  PHE A CD1 1 
ATOM   3186  C  CD2 . PHE A 1 420  ? 8.819   33.867  38.812  1.00 117.44 ? 420  PHE A CD2 1 
ATOM   3187  C  CE1 . PHE A 1 420  ? 10.235  35.993  39.812  1.00 111.30 ? 420  PHE A CE1 1 
ATOM   3188  C  CE2 . PHE A 1 420  ? 10.135  33.700  39.142  1.00 118.01 ? 420  PHE A CE2 1 
ATOM   3189  C  CZ  . PHE A 1 420  ? 10.848  34.764  39.642  1.00 113.43 ? 420  PHE A CZ  1 
ATOM   3190  N  N   . VAL A 1 421  ? 4.388   36.660  39.330  1.00 152.98 ? 421  VAL A N   1 
ATOM   3191  C  CA  . VAL A 1 421  ? 3.293   37.429  38.748  1.00 151.63 ? 421  VAL A CA  1 
ATOM   3192  C  C   . VAL A 1 421  ? 3.681   38.893  38.812  1.00 149.74 ? 421  VAL A C   1 
ATOM   3193  O  O   . VAL A 1 421  ? 4.056   39.378  39.878  1.00 147.58 ? 421  VAL A O   1 
ATOM   3194  C  CB  . VAL A 1 421  ? 1.941   37.228  39.506  1.00 150.00 ? 421  VAL A CB  1 
ATOM   3195  C  CG1 . VAL A 1 421  ? 1.168   38.537  39.615  1.00 150.22 ? 421  VAL A CG1 1 
ATOM   3196  C  CG2 . VAL A 1 421  ? 1.081   36.167  38.832  1.00 152.53 ? 421  VAL A CG2 1 
ATOM   3197  N  N   . LEU A 1 422  ? 3.658   39.565  37.659  1.00 119.44 ? 422  LEU A N   1 
ATOM   3198  C  CA  . LEU A 1 422  ? 3.711   41.025  37.583  1.00 119.41 ? 422  LEU A CA  1 
ATOM   3199  C  C   . LEU A 1 422  ? 2.351   41.504  37.082  1.00 128.69 ? 422  LEU A C   1 
ATOM   3200  O  O   . LEU A 1 422  ? 1.776   40.931  36.149  1.00 132.63 ? 422  LEU A O   1 
ATOM   3201  C  CB  . LEU A 1 422  ? 4.864   41.544  36.695  1.00 117.65 ? 422  LEU A CB  1 
ATOM   3202  C  CG  . LEU A 1 422  ? 5.839   40.592  35.984  1.00 109.91 ? 422  LEU A CG  1 
ATOM   3203  C  CD1 . LEU A 1 422  ? 5.160   40.036  34.768  1.00 115.52 ? 422  LEU A CD1 1 
ATOM   3204  C  CD2 . LEU A 1 422  ? 7.187   41.241  35.611  1.00 107.62 ? 422  LEU A CD2 1 
ATOM   3205  N  N   . ASN A 1 423  ? 1.816   42.519  37.748  1.00 193.69 ? 423  ASN A N   1 
ATOM   3206  C  CA  . ASN A 1 423  ? 0.519   43.061  37.400  1.00 198.66 ? 423  ASN A CA  1 
ATOM   3207  C  C   . ASN A 1 423  ? 0.825   44.184  36.443  1.00 199.37 ? 423  ASN A C   1 
ATOM   3208  O  O   . ASN A 1 423  ? 1.686   45.009  36.742  1.00 194.45 ? 423  ASN A O   1 
ATOM   3209  C  CB  . ASN A 1 423  ? -0.159  43.582  38.660  1.00 197.08 ? 423  ASN A CB  1 
ATOM   3210  C  CG  . ASN A 1 423  ? 0.310   42.853  39.902  1.00 192.44 ? 423  ASN A CG  1 
ATOM   3211  O  OD1 . ASN A 1 423  ? -0.367  41.962  40.410  1.00 195.28 ? 423  ASN A OD1 1 
ATOM   3212  N  ND2 . ASN A 1 423  ? 1.493   43.211  40.381  1.00 186.03 ? 423  ASN A ND2 1 
ATOM   3213  N  N   . LEU A 1 424  ? 0.170   44.211  35.283  1.00 137.68 ? 424  LEU A N   1 
ATOM   3214  C  CA  . LEU A 1 424  ? 0.608   45.132  34.227  1.00 140.84 ? 424  LEU A CA  1 
ATOM   3215  C  C   . LEU A 1 424  ? -0.309  46.276  33.841  1.00 146.85 ? 424  LEU A C   1 
ATOM   3216  O  O   . LEU A 1 424  ? -1.477  46.060  33.514  1.00 150.88 ? 424  LEU A O   1 
ATOM   3217  C  CB  . LEU A 1 424  ? 1.032   44.369  32.971  1.00 142.01 ? 424  LEU A CB  1 
ATOM   3218  C  CG  . LEU A 1 424  ? 2.427   43.752  33.159  1.00 137.21 ? 424  LEU A CG  1 
ATOM   3219  C  CD1 . LEU A 1 424  ? 3.062   43.226  31.851  1.00 140.76 ? 424  LEU A CD1 1 
ATOM   3220  C  CD2 . LEU A 1 424  ? 3.350   44.758  33.849  1.00 132.83 ? 424  LEU A CD2 1 
ATOM   3221  N  N   . PRO A 1 425  ? 0.256   47.497  33.836  1.00 167.41 ? 425  PRO A N   1 
ATOM   3222  C  CA  . PRO A 1 425  ? -0.431  48.752  33.524  1.00 174.77 ? 425  PRO A CA  1 
ATOM   3223  C  C   . PRO A 1 425  ? -1.102  48.696  32.158  1.00 186.18 ? 425  PRO A C   1 
ATOM   3224  O  O   . PRO A 1 425  ? -0.503  49.195  31.210  1.00 192.22 ? 425  PRO A O   1 
ATOM   3225  C  CB  . PRO A 1 425  ? 0.713   49.775  33.474  1.00 171.40 ? 425  PRO A CB  1 
ATOM   3226  C  CG  . PRO A 1 425  ? 1.804   49.191  34.275  1.00 164.02 ? 425  PRO A CG  1 
ATOM   3227  C  CD  . PRO A 1 425  ? 1.683   47.710  34.134  1.00 160.75 ? 425  PRO A CD  1 
ATOM   3228  N  N   . SER A 1 426  ? -2.310  48.136  32.073  1.00 204.36 ? 426  SER A N   1 
ATOM   3229  C  CA  . SER A 1 426  ? -3.038  47.897  30.811  1.00 213.88 ? 426  SER A CA  1 
ATOM   3230  C  C   . SER A 1 426  ? -2.427  48.442  29.501  1.00 224.12 ? 426  SER A C   1 
ATOM   3231  O  O   . SER A 1 426  ? -2.441  47.757  28.470  1.00 224.93 ? 426  SER A O   1 
ATOM   3232  C  CB  . SER A 1 426  ? -4.500  48.345  30.944  1.00 221.83 ? 426  SER A CB  1 
ATOM   3233  O  OG  . SER A 1 426  ? -4.603  49.663  31.451  1.00 221.85 ? 426  SER A OG  1 
ATOM   3234  N  N   . GLY A 1 427  ? -1.912  49.671  29.544  1.00 167.35 ? 427  GLY A N   1 
ATOM   3235  C  CA  . GLY A 1 427  ? -1.219  50.276  28.415  1.00 170.63 ? 427  GLY A CA  1 
ATOM   3236  C  C   . GLY A 1 427  ? 0.112   49.630  28.072  1.00 165.21 ? 427  GLY A C   1 
ATOM   3237  O  O   . GLY A 1 427  ? 0.877   50.121  27.235  1.00 166.06 ? 427  GLY A O   1 
ATOM   3238  N  N   . VAL A 1 428  ? 0.406   48.520  28.728  1.00 164.03 ? 428  VAL A N   1 
ATOM   3239  C  CA  . VAL A 1 428  ? 1.591   47.772  28.367  1.00 157.75 ? 428  VAL A CA  1 
ATOM   3240  C  C   . VAL A 1 428  ? 1.347   47.226  26.971  1.00 160.27 ? 428  VAL A C   1 
ATOM   3241  O  O   . VAL A 1 428  ? 0.277   47.450  26.413  1.00 165.33 ? 428  VAL A O   1 
ATOM   3242  C  CB  . VAL A 1 428  ? 1.879   46.634  29.348  1.00 152.03 ? 428  VAL A CB  1 
ATOM   3243  C  CG1 . VAL A 1 428  ? 0.885   45.497  29.142  1.00 155.20 ? 428  VAL A CG1 1 
ATOM   3244  C  CG2 . VAL A 1 428  ? 3.332   46.169  29.204  1.00 147.85 ? 428  VAL A CG2 1 
ATOM   3245  N  N   . THR A 1 429  ? 2.315   46.481  26.432  1.00 122.07 ? 429  THR A N   1 
ATOM   3246  C  CA  . THR A 1 429  ? 2.484   46.323  24.991  1.00 123.93 ? 429  THR A CA  1 
ATOM   3247  C  C   . THR A 1 429  ? 3.173   45.020  24.651  1.00 124.74 ? 429  THR A C   1 
ATOM   3248  O  O   . THR A 1 429  ? 2.578   43.981  24.317  1.00 130.69 ? 429  THR A O   1 
ATOM   3249  C  CB  . THR A 1 429  ? 3.417   47.479  24.496  1.00 130.17 ? 429  THR A CB  1 
ATOM   3250  O  OG1 . THR A 1 429  ? 4.753   47.306  25.007  1.00 126.54 ? 429  THR A OG1 1 
ATOM   3251  C  CG2 . THR A 1 429  ? 2.875   48.816  24.979  1.00 133.17 ? 429  THR A CG2 1 
ATOM   3252  N  N   . VAL A 1 430  ? 4.477   45.145  24.725  1.00 169.73 ? 430  VAL A N   1 
ATOM   3253  C  CA  . VAL A 1 430  ? 5.376   44.052  24.679  1.00 163.66 ? 430  VAL A CA  1 
ATOM   3254  C  C   . VAL A 1 430  ? 6.081   44.084  25.988  1.00 159.35 ? 430  VAL A C   1 
ATOM   3255  O  O   . VAL A 1 430  ? 6.339   45.151  26.539  1.00 157.23 ? 430  VAL A O   1 
ATOM   3256  C  CB  . VAL A 1 430  ? 6.409   44.335  23.679  1.00 160.32 ? 430  VAL A CB  1 
ATOM   3257  C  CG1 . VAL A 1 430  ? 7.358   43.155  23.537  1.00 156.19 ? 430  VAL A CG1 1 
ATOM   3258  C  CG2 . VAL A 1 430  ? 5.725   44.613  22.426  1.00 166.95 ? 430  VAL A CG2 1 
ATOM   3259  N  N   . LEU A 1 431  ? 6.431   42.906  26.469  1.00 157.58 ? 431  LEU A N   1 
ATOM   3260  C  CA  . LEU A 1 431  ? 7.028   42.784  27.760  1.00 146.80 ? 431  LEU A CA  1 
ATOM   3261  C  C   . LEU A 1 431  ? 8.209   41.917  27.506  1.00 145.22 ? 431  LEU A C   1 
ATOM   3262  O  O   . LEU A 1 431  ? 8.061   40.756  27.156  1.00 136.55 ? 431  LEU A O   1 
ATOM   3263  C  CB  . LEU A 1 431  ? 6.064   42.072  28.677  1.00 140.02 ? 431  LEU A CB  1 
ATOM   3264  C  CG  . LEU A 1 431  ? 6.417   42.224  30.135  1.00 132.06 ? 431  LEU A CG  1 
ATOM   3265  C  CD1 . LEU A 1 431  ? 5.825   41.106  31.021  1.00 127.83 ? 431  LEU A CD1 1 
ATOM   3266  C  CD2 . LEU A 1 431  ? 7.933   42.278  30.250  1.00 128.05 ? 431  LEU A CD2 1 
ATOM   3267  N  N   . GLU A 1 432  ? 9.387   42.492  27.647  1.00 196.84 ? 432  GLU A N   1 
ATOM   3268  C  CA  . GLU A 1 432  ? 10.581  41.682  27.641  1.00 195.30 ? 432  GLU A CA  1 
ATOM   3269  C  C   . GLU A 1 432  ? 10.992  41.439  29.110  1.00 190.73 ? 432  GLU A C   1 
ATOM   3270  O  O   . GLU A 1 432  ? 10.852  42.333  29.951  1.00 191.13 ? 432  GLU A O   1 
ATOM   3271  C  CB  . GLU A 1 432  ? 11.684  42.377  26.849  1.00 196.80 ? 432  GLU A CB  1 
ATOM   3272  C  CG  . GLU A 1 432  ? 11.211  43.010  25.558  1.00 207.50 ? 432  GLU A CG  1 
ATOM   3273  C  CD  . GLU A 1 432  ? 11.611  42.216  24.332  1.00 214.28 ? 432  GLU A CD  1 
ATOM   3274  O  OE1 . GLU A 1 432  ? 12.037  41.053  24.485  1.00 209.01 ? 432  GLU A OE1 1 
ATOM   3275  O  OE2 . GLU A 1 432  ? 11.498  42.764  23.216  1.00 222.61 ? 432  GLU A OE2 1 
ATOM   3276  N  N   . PHE A 1 433  ? 11.480  40.237  29.429  1.00 122.57 ? 433  PHE A N   1 
ATOM   3277  C  CA  . PHE A 1 433  ? 11.916  39.938  30.788  1.00 115.21 ? 433  PHE A CA  1 
ATOM   3278  C  C   . PHE A 1 433  ? 13.040  38.888  30.834  1.00 105.26 ? 433  PHE A C   1 
ATOM   3279  O  O   . PHE A 1 433  ? 13.099  38.004  29.986  1.00 110.16 ? 433  PHE A O   1 
ATOM   3280  C  CB  . PHE A 1 433  ? 10.714  39.589  31.686  1.00 111.02 ? 433  PHE A CB  1 
ATOM   3281  C  CG  . PHE A 1 433  ? 9.845   38.419  31.213  1.00 114.18 ? 433  PHE A CG  1 
ATOM   3282  C  CD1 . PHE A 1 433  ? 8.456   38.531  31.227  1.00 116.42 ? 433  PHE A CD1 1 
ATOM   3283  C  CD2 . PHE A 1 433  ? 10.391  37.202  30.852  1.00 123.33 ? 433  PHE A CD2 1 
ATOM   3284  C  CE1 . PHE A 1 433  ? 7.640   37.479  30.858  1.00 118.80 ? 433  PHE A CE1 1 
ATOM   3285  C  CE2 . PHE A 1 433  ? 9.572   36.149  30.479  1.00 113.32 ? 433  PHE A CE2 1 
ATOM   3286  C  CZ  . PHE A 1 433  ? 8.198   36.294  30.487  1.00 116.72 ? 433  PHE A CZ  1 
ATOM   3287  N  N   . ASN A 1 434  ? 13.950  39.011  31.798  1.00 145.70 ? 434  ASN A N   1 
ATOM   3288  C  CA  . ASN A 1 434  ? 15.006  38.013  32.003  1.00 141.89 ? 434  ASN A CA  1 
ATOM   3289  C  C   . ASN A 1 434  ? 14.874  37.197  33.306  1.00 142.16 ? 434  ASN A C   1 
ATOM   3290  O  O   . ASN A 1 434  ? 14.900  37.740  34.412  1.00 141.27 ? 434  ASN A O   1 
ATOM   3291  C  CB  . ASN A 1 434  ? 16.386  38.663  31.935  1.00 137.87 ? 434  ASN A CB  1 
ATOM   3292  C  CG  . ASN A 1 434  ? 16.538  39.557  30.736  1.00 138.62 ? 434  ASN A CG  1 
ATOM   3293  O  OD1 . ASN A 1 434  ? 17.045  39.135  29.709  1.00 138.58 ? 434  ASN A OD1 1 
ATOM   3294  N  ND2 . ASN A 1 434  ? 16.050  40.784  30.839  1.00 140.55 ? 434  ASN A ND2 1 
ATOM   3295  N  N   . VAL A 1 435  ? 14.750  35.887  33.169  1.00 105.41 ? 435  VAL A N   1 
ATOM   3296  C  CA  . VAL A 1 435  ? 14.824  34.991  34.308  1.00 103.03 ? 435  VAL A CA  1 
ATOM   3297  C  C   . VAL A 1 435  ? 16.259  34.557  34.510  1.00 99.19  ? 435  VAL A C   1 
ATOM   3298  O  O   . VAL A 1 435  ? 17.062  34.711  33.615  1.00 98.51  ? 435  VAL A O   1 
ATOM   3299  C  CB  . VAL A 1 435  ? 13.997  33.762  34.042  1.00 111.38 ? 435  VAL A CB  1 
ATOM   3300  C  CG1 . VAL A 1 435  ? 14.380  32.629  34.939  1.00 107.61 ? 435  VAL A CG1 1 
ATOM   3301  C  CG2 . VAL A 1 435  ? 12.551  34.129  34.202  1.00 113.64 ? 435  VAL A CG2 1 
ATOM   3302  N  N   . LYS A 1 436  ? 16.590  34.031  35.678  1.00 154.75 ? 436  LYS A N   1 
ATOM   3303  C  CA  . LYS A 1 436  ? 17.925  33.516  35.954  1.00 148.34 ? 436  LYS A CA  1 
ATOM   3304  C  C   . LYS A 1 436  ? 17.988  32.955  37.367  1.00 149.01 ? 436  LYS A C   1 
ATOM   3305  O  O   . LYS A 1 436  ? 17.375  33.495  38.284  1.00 149.32 ? 436  LYS A O   1 
ATOM   3306  C  CB  . LYS A 1 436  ? 19.009  34.580  35.745  1.00 143.65 ? 436  LYS A CB  1 
ATOM   3307  C  CG  . LYS A 1 436  ? 19.062  35.729  36.725  1.00 139.62 ? 436  LYS A CG  1 
ATOM   3308  C  CD  . LYS A 1 436  ? 20.382  35.701  37.490  1.00 154.81 ? 436  LYS A CD  1 
ATOM   3309  C  CE  . LYS A 1 436  ? 20.908  37.102  37.759  1.00 160.61 ? 436  LYS A CE  1 
ATOM   3310  N  NZ  . LYS A 1 436  ? 21.361  37.746  36.501  1.00 161.51 ? 436  LYS A NZ  1 
ATOM   3311  N  N   . THR A 1 437  ? 18.712  31.862  37.549  1.00 126.61 ? 437  THR A N   1 
ATOM   3312  C  CA  . THR A 1 437  ? 18.937  31.349  38.881  1.00 130.23 ? 437  THR A CA  1 
ATOM   3313  C  C   . THR A 1 437  ? 19.931  32.270  39.561  1.00 123.86 ? 437  THR A C   1 
ATOM   3314  O  O   . THR A 1 437  ? 20.788  32.861  38.888  1.00 117.95 ? 437  THR A O   1 
ATOM   3315  C  CB  . THR A 1 437  ? 19.524  29.963  38.819  1.00 118.08 ? 437  THR A CB  1 
ATOM   3316  O  OG1 . THR A 1 437  ? 20.618  29.984  37.900  1.00 117.47 ? 437  THR A OG1 1 
ATOM   3317  C  CG2 . THR A 1 437  ? 18.464  28.980  38.344  1.00 120.11 ? 437  THR A CG2 1 
ATOM   3318  N  N   . ASP A 1 438  ? 19.804  32.403  40.882  1.00 133.69 ? 438  ASP A N   1 
ATOM   3319  C  CA  . ASP A 1 438  ? 20.808  33.094  41.675  1.00 139.57 ? 438  ASP A CA  1 
ATOM   3320  C  C   . ASP A 1 438  ? 21.298  32.172  42.751  1.00 135.06 ? 438  ASP A C   1 
ATOM   3321  O  O   . ASP A 1 438  ? 21.538  32.571  43.888  1.00 130.48 ? 438  ASP A O   1 
ATOM   3322  C  CB  . ASP A 1 438  ? 20.289  34.399  42.261  1.00 147.02 ? 438  ASP A CB  1 
ATOM   3323  C  CG  . ASP A 1 438  ? 21.278  35.540  42.081  1.00 153.62 ? 438  ASP A CG  1 
ATOM   3324  O  OD1 . ASP A 1 438  ? 22.487  35.249  41.934  1.00 153.72 ? 438  ASP A OD1 1 
ATOM   3325  O  OD2 . ASP A 1 438  ? 20.846  36.717  42.076  1.00 157.70 ? 438  ASP A OD2 1 
ATOM   3326  N  N   . ALA A 1 439  ? 21.439  30.914  42.362  1.00 173.55 ? 439  ALA A N   1 
ATOM   3327  C  CA  . ALA A 1 439  ? 22.127  29.966  43.193  1.00 173.62 ? 439  ALA A CA  1 
ATOM   3328  C  C   . ALA A 1 439  ? 23.179  30.785  43.880  1.00 173.81 ? 439  ALA A C   1 
ATOM   3329  O  O   . ALA A 1 439  ? 23.770  31.693  43.302  1.00 176.88 ? 439  ALA A O   1 
ATOM   3330  C  CB  . ALA A 1 439  ? 22.760  28.883  42.365  1.00 174.16 ? 439  ALA A CB  1 
ATOM   3331  N  N   . PRO A 1 440  ? 23.394  30.496  45.139  1.00 139.85 ? 440  PRO A N   1 
ATOM   3332  C  CA  . PRO A 1 440  ? 24.221  31.400  45.913  1.00 133.74 ? 440  PRO A CA  1 
ATOM   3333  C  C   . PRO A 1 440  ? 25.648  30.977  45.748  1.00 128.78 ? 440  PRO A C   1 
ATOM   3334  O  O   . PRO A 1 440  ? 26.536  31.813  45.901  1.00 127.94 ? 440  PRO A O   1 
ATOM   3335  C  CB  . PRO A 1 440  ? 23.781  31.124  47.341  1.00 131.30 ? 440  PRO A CB  1 
ATOM   3336  C  CG  . PRO A 1 440  ? 22.799  29.919  47.266  1.00 139.24 ? 440  PRO A CG  1 
ATOM   3337  C  CD  . PRO A 1 440  ? 22.946  29.336  45.909  1.00 140.56 ? 440  PRO A CD  1 
ATOM   3338  N  N   . ASP A 1 441  ? 25.838  29.691  45.445  1.00 143.88 ? 441  ASP A N   1 
ATOM   3339  C  CA  . ASP A 1 441  ? 27.152  29.068  45.296  1.00 144.74 ? 441  ASP A CA  1 
ATOM   3340  C  C   . ASP A 1 441  ? 27.823  29.151  43.877  1.00 143.33 ? 441  ASP A C   1 
ATOM   3341  O  O   . ASP A 1 441  ? 29.029  28.886  43.722  1.00 141.71 ? 441  ASP A O   1 
ATOM   3342  C  CB  . ASP A 1 441  ? 27.109  27.616  45.801  1.00 152.87 ? 441  ASP A CB  1 
ATOM   3343  C  CG  . ASP A 1 441  ? 25.793  26.915  45.490  1.00 161.68 ? 441  ASP A CG  1 
ATOM   3344  O  OD1 . ASP A 1 441  ? 25.799  25.675  45.350  1.00 166.02 ? 441  ASP A OD1 1 
ATOM   3345  O  OD2 . ASP A 1 441  ? 24.753  27.589  45.385  1.00 162.48 ? 441  ASP A OD2 1 
ATOM   3346  N  N   . LEU A 1 442  ? 27.077  29.521  42.835  1.00 92.08  ? 442  LEU A N   1 
ATOM   3347  C  CA  . LEU A 1 442  ? 27.624  29.431  41.488  1.00 89.43  ? 442  LEU A CA  1 
ATOM   3348  C  C   . LEU A 1 442  ? 28.325  30.696  41.058  1.00 93.21  ? 442  LEU A C   1 
ATOM   3349  O  O   . LEU A 1 442  ? 28.002  31.775  41.485  1.00 95.04  ? 442  LEU A O   1 
ATOM   3350  C  CB  . LEU A 1 442  ? 26.509  29.041  40.542  1.00 100.30 ? 442  LEU A CB  1 
ATOM   3351  C  CG  . LEU A 1 442  ? 25.980  27.658  40.963  1.00 93.85  ? 442  LEU A CG  1 
ATOM   3352  C  CD1 . LEU A 1 442  ? 24.726  27.189  40.208  1.00 94.62  ? 442  LEU A CD1 1 
ATOM   3353  C  CD2 . LEU A 1 442  ? 27.082  26.581  40.920  1.00 98.46  ? 442  LEU A CD2 1 
ATOM   3354  N  N   . PRO A 1 443  ? 29.340  30.568  40.234  1.00 276.86 ? 443  PRO A N   1 
ATOM   3355  C  CA  . PRO A 1 443  ? 29.784  31.855  39.721  1.00 281.63 ? 443  PRO A CA  1 
ATOM   3356  C  C   . PRO A 1 443  ? 28.561  32.532  39.145  1.00 291.95 ? 443  PRO A C   1 
ATOM   3357  O  O   . PRO A 1 443  ? 27.677  31.837  38.636  1.00 294.07 ? 443  PRO A O   1 
ATOM   3358  C  CB  . PRO A 1 443  ? 30.737  31.458  38.602  1.00 277.44 ? 443  PRO A CB  1 
ATOM   3359  C  CG  . PRO A 1 443  ? 31.296  30.145  39.049  1.00 273.64 ? 443  PRO A CG  1 
ATOM   3360  C  CD  . PRO A 1 443  ? 30.235  29.464  39.882  1.00 272.32 ? 443  PRO A CD  1 
ATOM   3361  N  N   . GLU A 1 444  ? 28.475  33.848  39.269  1.00 169.25 ? 444  GLU A N   1 
ATOM   3362  C  CA  . GLU A 1 444  ? 27.480  34.559  38.518  1.00 175.23 ? 444  GLU A CA  1 
ATOM   3363  C  C   . GLU A 1 444  ? 27.593  33.968  37.124  1.00 167.85 ? 444  GLU A C   1 
ATOM   3364  O  O   . GLU A 1 444  ? 26.652  33.349  36.626  1.00 162.90 ? 444  GLU A O   1 
ATOM   3365  C  CB  . GLU A 1 444  ? 27.811  36.039  38.505  1.00 191.18 ? 444  GLU A CB  1 
ATOM   3366  C  CG  . GLU A 1 444  ? 26.592  36.922  38.378  1.00 205.88 ? 444  GLU A CG  1 
ATOM   3367  C  CD  . GLU A 1 444  ? 25.968  36.850  36.997  1.00 218.89 ? 444  GLU A CD  1 
ATOM   3368  O  OE1 . GLU A 1 444  ? 26.632  36.333  36.068  1.00 221.80 ? 444  GLU A OE1 1 
ATOM   3369  O  OE2 . GLU A 1 444  ? 24.817  37.322  36.837  1.00 223.52 ? 444  GLU A OE2 1 
ATOM   3370  N  N   . GLU A 1 445  ? 28.772  34.111  36.523  1.00 159.93 ? 445  GLU A N   1 
ATOM   3371  C  CA  . GLU A 1 445  ? 29.025  33.556  35.201  1.00 161.25 ? 445  GLU A CA  1 
ATOM   3372  C  C   . GLU A 1 445  ? 28.116  32.391  34.932  1.00 154.11 ? 445  GLU A C   1 
ATOM   3373  O  O   . GLU A 1 445  ? 27.344  32.392  33.994  1.00 155.95 ? 445  GLU A O   1 
ATOM   3374  C  CB  . GLU A 1 445  ? 30.446  33.024  35.103  1.00 166.14 ? 445  GLU A CB  1 
ATOM   3375  C  CG  . GLU A 1 445  ? 31.478  34.013  34.687  1.00 176.61 ? 445  GLU A CG  1 
ATOM   3376  C  CD  . GLU A 1 445  ? 32.791  33.322  34.419  1.00 183.88 ? 445  GLU A CD  1 
ATOM   3377  O  OE1 . GLU A 1 445  ? 32.936  32.148  34.823  1.00 182.90 ? 445  GLU A OE1 1 
ATOM   3378  O  OE2 . GLU A 1 445  ? 33.678  33.943  33.806  1.00 189.67 ? 445  GLU A OE2 1 
ATOM   3379  N  N   . ASN A 1 446  ? 28.198  31.401  35.796  1.00 101.76 ? 446  ASN A N   1 
ATOM   3380  C  CA  . ASN A 1 446  ? 27.704  30.094  35.474  1.00 100.46 ? 446  ASN A CA  1 
ATOM   3381  C  C   . ASN A 1 446  ? 26.296  29.855  35.924  1.00 110.40 ? 446  ASN A C   1 
ATOM   3382  O  O   . ASN A 1 446  ? 25.911  28.737  36.168  1.00 107.96 ? 446  ASN A O   1 
ATOM   3383  C  CB  . ASN A 1 446  ? 28.676  29.085  36.049  1.00 94.82  ? 446  ASN A CB  1 
ATOM   3384  C  CG  . ASN A 1 446  ? 30.098  29.322  35.538  1.00 98.85  ? 446  ASN A CG  1 
ATOM   3385  O  OD1 . ASN A 1 446  ? 31.048  29.507  36.309  1.00 98.46  ? 446  ASN A OD1 1 
ATOM   3386  N  ND2 . ASN A 1 446  ? 30.235  29.357  34.217  1.00 103.78 ? 446  ASN A ND2 1 
ATOM   3387  N  N   . GLN A 1 447  ? 25.528  30.925  35.999  1.00 132.00 ? 447  GLN A N   1 
ATOM   3388  C  CA  . GLN A 1 447  ? 24.150  30.843  36.405  1.00 136.91 ? 447  GLN A CA  1 
ATOM   3389  C  C   . GLN A 1 447  ? 23.271  30.704  35.185  1.00 138.51 ? 447  GLN A C   1 
ATOM   3390  O  O   . GLN A 1 447  ? 23.256  31.584  34.321  1.00 138.51 ? 447  GLN A O   1 
ATOM   3391  C  CB  . GLN A 1 447  ? 23.761  32.118  37.137  1.00 140.40 ? 447  GLN A CB  1 
ATOM   3392  C  CG  . GLN A 1 447  ? 24.384  32.275  38.501  1.00 141.58 ? 447  GLN A CG  1 
ATOM   3393  C  CD  . GLN A 1 447  ? 23.538  31.632  39.566  1.00 142.22 ? 447  GLN A CD  1 
ATOM   3394  O  OE1 . GLN A 1 447  ? 22.676  30.805  39.263  1.00 142.47 ? 447  GLN A OE1 1 
ATOM   3395  N  NE2 . GLN A 1 447  ? 23.760  32.017  40.820  1.00 142.40 ? 447  GLN A NE2 1 
ATOM   3396  N  N   . ALA A 1 448  ? 22.510  29.617  35.124  1.00 117.32 ? 448  ALA A N   1 
ATOM   3397  C  CA  . ALA A 1 448  ? 21.587  29.395  34.005  1.00 120.69 ? 448  ALA A CA  1 
ATOM   3398  C  C   . ALA A 1 448  ? 20.571  30.519  33.857  1.00 134.08 ? 448  ALA A C   1 
ATOM   3399  O  O   . ALA A 1 448  ? 20.006  30.958  34.853  1.00 131.61 ? 448  ALA A O   1 
ATOM   3400  C  CB  . ALA A 1 448  ? 20.872  28.070  34.156  1.00 120.51 ? 448  ALA A CB  1 
ATOM   3401  N  N   . ARG A 1 449  ? 20.314  30.949  32.616  1.00 114.30 ? 449  ARG A N   1 
ATOM   3402  C  CA  . ARG A 1 449  ? 19.304  31.982  32.340  1.00 118.78 ? 449  ARG A CA  1 
ATOM   3403  C  C   . ARG A 1 449  ? 18.573  31.937  30.988  1.00 123.83 ? 449  ARG A C   1 
ATOM   3404  O  O   . ARG A 1 449  ? 18.891  31.148  30.104  1.00 123.75 ? 449  ARG A O   1 
ATOM   3405  C  CB  . ARG A 1 449  ? 19.896  33.361  32.529  1.00 119.66 ? 449  ARG A CB  1 
ATOM   3406  C  CG  . ARG A 1 449  ? 20.911  33.724  31.552  1.00 117.05 ? 449  ARG A CG  1 
ATOM   3407  C  CD  . ARG A 1 449  ? 21.663  34.831  32.145  1.00 121.65 ? 449  ARG A CD  1 
ATOM   3408  N  NE  . ARG A 1 449  ? 22.922  34.367  32.668  1.00 121.44 ? 449  ARG A NE  1 
ATOM   3409  C  CZ  . ARG A 1 449  ? 23.742  35.139  33.352  1.00 123.98 ? 449  ARG A CZ  1 
ATOM   3410  N  NH1 . ARG A 1 449  ? 23.406  36.400  33.609  1.00 127.12 ? 449  ARG A NH1 1 
ATOM   3411  N  NH2 . ARG A 1 449  ? 24.885  34.641  33.782  1.00 121.10 ? 449  ARG A NH2 1 
ATOM   3412  N  N   . GLU A 1 450  ? 17.579  32.806  30.851  1.00 132.19 ? 450  GLU A N   1 
ATOM   3413  C  CA  . GLU A 1 450  ? 16.760  32.887  29.657  1.00 137.43 ? 450  GLU A CA  1 
ATOM   3414  C  C   . GLU A 1 450  ? 16.254  34.289  29.537  1.00 139.44 ? 450  GLU A C   1 
ATOM   3415  O  O   . GLU A 1 450  ? 16.581  35.158  30.342  1.00 138.85 ? 450  GLU A O   1 
ATOM   3416  C  CB  . GLU A 1 450  ? 15.547  31.981  29.762  1.00 126.68 ? 450  GLU A CB  1 
ATOM   3417  C  CG  . GLU A 1 450  ? 15.865  30.530  29.701  1.00 131.52 ? 450  GLU A CG  1 
ATOM   3418  C  CD  . GLU A 1 450  ? 16.154  30.106  28.307  1.00 139.89 ? 450  GLU A CD  1 
ATOM   3419  O  OE1 . GLU A 1 450  ? 15.529  30.717  27.418  1.00 147.04 ? 450  GLU A OE1 1 
ATOM   3420  O  OE2 . GLU A 1 450  ? 16.993  29.193  28.102  1.00 138.76 ? 450  GLU A OE2 1 
ATOM   3421  N  N   . GLY A 1 451  ? 15.434  34.496  28.527  1.00 112.53 ? 451  GLY A N   1 
ATOM   3422  C  CA  . GLY A 1 451  ? 14.847  35.788  28.286  1.00 114.00 ? 451  GLY A CA  1 
ATOM   3423  C  C   . GLY A 1 451  ? 13.702  35.415  27.400  1.00 136.70 ? 451  GLY A C   1 
ATOM   3424  O  O   . GLY A 1 451  ? 13.765  34.344  26.803  1.00 116.96 ? 451  GLY A O   1 
ATOM   3425  N  N   . TYR A 1 452  ? 12.653  36.238  27.357  1.00 109.41 ? 452  TYR A N   1 
ATOM   3426  C  CA  . TYR A 1 452  ? 11.490  35.990  26.492  1.00 114.02 ? 452  TYR A CA  1 
ATOM   3427  C  C   . TYR A 1 452  ? 10.794  37.283  26.006  1.00 119.81 ? 452  TYR A C   1 
ATOM   3428  O  O   . TYR A 1 452  ? 11.451  38.305  25.846  1.00 118.67 ? 452  TYR A O   1 
ATOM   3429  C  CB  . TYR A 1 452  ? 10.502  35.042  27.166  1.00 113.14 ? 452  TYR A CB  1 
ATOM   3430  C  CG  . TYR A 1 452  ? 11.086  33.710  27.548  1.00 110.08 ? 452  TYR A CG  1 
ATOM   3431  C  CD1 . TYR A 1 452  ? 10.710  32.556  26.893  1.00 112.94 ? 452  TYR A CD1 1 
ATOM   3432  C  CD2 . TYR A 1 452  ? 12.021  33.610  28.561  1.00 105.62 ? 452  TYR A CD2 1 
ATOM   3433  C  CE1 . TYR A 1 452  ? 11.250  31.340  27.241  1.00 111.57 ? 452  TYR A CE1 1 
ATOM   3434  C  CE2 . TYR A 1 452  ? 12.574  32.407  28.909  1.00 103.61 ? 452  TYR A CE2 1 
ATOM   3435  C  CZ  . TYR A 1 452  ? 12.184  31.277  28.254  1.00 104.46 ? 452  TYR A CZ  1 
ATOM   3436  O  OH  . TYR A 1 452  ? 12.751  30.085  28.624  1.00 102.10 ? 452  TYR A OH  1 
ATOM   3437  N  N   . ARG A 1 453  ? 9.483   37.223  25.753  1.00 139.12 ? 453  ARG A N   1 
ATOM   3438  C  CA  . ARG A 1 453  ? 8.702   38.387  25.305  1.00 139.90 ? 453  ARG A CA  1 
ATOM   3439  C  C   . ARG A 1 453  ? 7.173   38.144  25.333  1.00 143.57 ? 453  ARG A C   1 
ATOM   3440  O  O   . ARG A 1 453  ? 6.708   37.115  24.857  1.00 147.33 ? 453  ARG A O   1 
ATOM   3441  C  CB  . ARG A 1 453  ? 9.132   38.753  23.882  1.00 144.77 ? 453  ARG A CB  1 
ATOM   3442  C  CG  . ARG A 1 453  ? 8.622   40.088  23.353  1.00 148.92 ? 453  ARG A CG  1 
ATOM   3443  C  CD  . ARG A 1 453  ? 8.862   40.219  21.846  1.00 156.90 ? 453  ARG A CD  1 
ATOM   3444  N  NE  . ARG A 1 453  ? 9.922   41.174  21.558  1.00 159.33 ? 453  ARG A NE  1 
ATOM   3445  C  CZ  . ARG A 1 453  ? 11.193  40.842  21.354  1.00 161.18 ? 453  ARG A CZ  1 
ATOM   3446  N  NH1 . ARG A 1 453  ? 11.572  39.571  21.385  1.00 159.38 ? 453  ARG A NH1 1 
ATOM   3447  N  NH2 . ARG A 1 453  ? 12.091  41.782  21.108  1.00 162.44 ? 453  ARG A NH2 1 
ATOM   3448  N  N   . ALA A 1 454  ? 6.386   39.073  25.877  1.00 144.16 ? 454  ALA A N   1 
ATOM   3449  C  CA  . ALA A 1 454  ? 4.925   38.914  25.849  1.00 145.38 ? 454  ALA A CA  1 
ATOM   3450  C  C   . ALA A 1 454  ? 4.273   40.082  25.151  1.00 153.00 ? 454  ALA A C   1 
ATOM   3451  O  O   . ALA A 1 454  ? 4.824   41.174  25.125  1.00 153.74 ? 454  ALA A O   1 
ATOM   3452  C  CB  . ALA A 1 454  ? 4.370   38.793  27.220  1.00 146.31 ? 454  ALA A CB  1 
ATOM   3453  N  N   . ILE A 1 455  ? 3.083   39.882  24.605  1.00 190.11 ? 455  ILE A N   1 
ATOM   3454  C  CA  . ILE A 1 455  ? 2.510   40.933  23.787  1.00 196.50 ? 455  ILE A CA  1 
ATOM   3455  C  C   . ILE A 1 455  ? 1.009   41.013  23.874  1.00 198.06 ? 455  ILE A C   1 
ATOM   3456  O  O   . ILE A 1 455  ? 0.333   39.994  23.960  1.00 199.04 ? 455  ILE A O   1 
ATOM   3457  C  CB  . ILE A 1 455  ? 2.874   40.712  22.344  1.00 191.57 ? 455  ILE A CB  1 
ATOM   3458  C  CG1 . ILE A 1 455  ? 4.338   41.060  22.125  1.00 188.86 ? 455  ILE A CG1 1 
ATOM   3459  C  CG2 . ILE A 1 455  ? 2.007   41.558  21.458  1.00 198.24 ? 455  ILE A CG2 1 
ATOM   3460  C  CD1 . ILE A 1 455  ? 4.849   40.638  20.745  1.00 195.85 ? 455  ILE A CD1 1 
ATOM   3461  N  N   . ALA A 1 456  ? 0.496   42.238  23.813  1.00 139.57 ? 456  ALA A N   1 
ATOM   3462  C  CA  . ALA A 1 456  ? -0.931  42.479  24.010  1.00 141.28 ? 456  ALA A CA  1 
ATOM   3463  C  C   . ALA A 1 456  ? -1.846  42.089  22.837  1.00 150.63 ? 456  ALA A C   1 
ATOM   3464  O  O   . ALA A 1 456  ? -1.769  42.687  21.762  1.00 154.45 ? 456  ALA A O   1 
ATOM   3465  C  CB  . ALA A 1 456  ? -1.157  43.920  24.385  1.00 140.82 ? 456  ALA A CB  1 
ATOM   3466  N  N   . TYR A 1 457  ? -2.704  41.090  23.072  1.00 143.33 ? 457  TYR A N   1 
ATOM   3467  C  CA  . TYR A 1 457  ? -3.791  40.713  22.171  1.00 152.97 ? 457  TYR A CA  1 
ATOM   3468  C  C   . TYR A 1 457  ? -4.535  41.982  21.847  1.00 158.59 ? 457  TYR A C   1 
ATOM   3469  O  O   . TYR A 1 457  ? -5.538  42.306  22.469  1.00 157.43 ? 457  TYR A O   1 
ATOM   3470  C  CB  . TYR A 1 457  ? -4.725  39.687  22.844  1.00 157.68 ? 457  TYR A CB  1 
ATOM   3471  C  CG  . TYR A 1 457  ? -6.057  39.386  22.157  1.00 151.48 ? 457  TYR A CG  1 
ATOM   3472  C  CD1 . TYR A 1 457  ? -6.817  38.255  22.513  1.00 155.76 ? 457  TYR A CD1 1 
ATOM   3473  C  CD2 . TYR A 1 457  ? -6.555  40.219  21.161  1.00 159.60 ? 457  TYR A CD2 1 
ATOM   3474  C  CE1 . TYR A 1 457  ? -8.036  37.979  21.886  1.00 163.54 ? 457  TYR A CE1 1 
ATOM   3475  C  CE2 . TYR A 1 457  ? -7.766  39.952  20.525  1.00 167.71 ? 457  TYR A CE2 1 
ATOM   3476  C  CZ  . TYR A 1 457  ? -8.506  38.839  20.886  1.00 168.67 ? 457  TYR A CZ  1 
ATOM   3477  O  OH  . TYR A 1 457  ? -9.704  38.616  20.219  1.00 175.27 ? 457  TYR A OH  1 
ATOM   3478  N  N   . SER A 1 458  ? -4.018  42.712  20.872  1.00 195.52 ? 458  SER A N   1 
ATOM   3479  C  CA  . SER A 1 458  ? -4.621  43.959  20.467  1.00 204.26 ? 458  SER A CA  1 
ATOM   3480  C  C   . SER A 1 458  ? -6.001  43.632  19.906  1.00 211.76 ? 458  SER A C   1 
ATOM   3481  O  O   . SER A 1 458  ? -6.200  42.593  19.267  1.00 212.06 ? 458  SER A O   1 
ATOM   3482  C  CB  . SER A 1 458  ? -3.724  44.658  19.443  1.00 208.42 ? 458  SER A CB  1 
ATOM   3483  O  OG  . SER A 1 458  ? -2.356  44.557  19.831  1.00 202.68 ? 458  SER A OG  1 
ATOM   3484  N  N   . SER A 1 459  ? -6.956  44.507  20.194  1.00 202.08 ? 459  SER A N   1 
ATOM   3485  C  CA  . SER A 1 459  ? -8.344  44.337  19.784  1.00 210.79 ? 459  SER A CA  1 
ATOM   3486  C  C   . SER A 1 459  ? -9.036  45.667  20.007  1.00 215.92 ? 459  SER A C   1 
ATOM   3487  O  O   . SER A 1 459  ? -9.066  46.176  21.123  1.00 210.57 ? 459  SER A O   1 
ATOM   3488  C  CB  . SER A 1 459  ? -9.029  43.236  20.601  1.00 208.03 ? 459  SER A CB  1 
ATOM   3489  O  OG  . SER A 1 459  ? -10.315 42.916  20.081  1.00 214.48 ? 459  SER A OG  1 
ATOM   3490  N  N   . LEU A 1 460  ? -9.585  46.236  18.944  1.00 237.46 ? 460  LEU A N   1 
ATOM   3491  C  CA  . LEU A 1 460  ? -10.097 47.592  19.023  1.00 248.78 ? 460  LEU A CA  1 
ATOM   3492  C  C   . LEU A 1 460  ? -11.315 47.739  19.944  1.00 255.51 ? 460  LEU A C   1 
ATOM   3493  O  O   . LEU A 1 460  ? -11.490 48.786  20.569  1.00 256.67 ? 460  LEU A O   1 
ATOM   3494  C  CB  . LEU A 1 460  ? -10.386 48.160  17.634  1.00 262.23 ? 460  LEU A CB  1 
ATOM   3495  C  CG  . LEU A 1 460  ? -10.144 49.671  17.595  1.00 268.75 ? 460  LEU A CG  1 
ATOM   3496  C  CD1 . LEU A 1 460  ? -8.648  49.961  17.498  1.00 264.71 ? 460  LEU A CD1 1 
ATOM   3497  C  CD2 . LEU A 1 460  ? -10.911 50.347  16.465  1.00 281.21 ? 460  LEU A CD2 1 
ATOM   3498  N  N   . SER A 1 461  ? -12.150 46.703  20.042  1.00 249.18 ? 461  SER A N   1 
ATOM   3499  C  CA  . SER A 1 461  ? -13.307 46.734  20.951  1.00 252.71 ? 461  SER A CA  1 
ATOM   3500  C  C   . SER A 1 461  ? -12.870 46.873  22.406  1.00 247.66 ? 461  SER A C   1 
ATOM   3501  O  O   . SER A 1 461  ? -13.691 46.800  23.318  1.00 247.35 ? 461  SER A O   1 
ATOM   3502  C  CB  . SER A 1 461  ? -14.185 45.483  20.791  1.00 253.44 ? 461  SER A CB  1 
ATOM   3503  O  OG  . SER A 1 461  ? -15.252 45.692  19.874  1.00 260.62 ? 461  SER A OG  1 
ATOM   3504  N  N   . GLN A 1 462  ? -11.570 47.064  22.611  1.00 181.91 ? 462  GLN A N   1 
ATOM   3505  C  CA  . GLN A 1 462  ? -10.983 47.109  23.943  1.00 174.58 ? 462  GLN A CA  1 
ATOM   3506  C  C   . GLN A 1 462  ? -11.203 45.784  24.649  1.00 163.98 ? 462  GLN A C   1 
ATOM   3507  O  O   . GLN A 1 462  ? -10.774 45.596  25.778  1.00 160.58 ? 462  GLN A O   1 
ATOM   3508  C  CB  . GLN A 1 462  ? -11.577 48.252  24.765  1.00 177.95 ? 462  GLN A CB  1 
ATOM   3509  C  CG  . GLN A 1 462  ? -10.890 49.590  24.553  1.00 180.20 ? 462  GLN A CG  1 
ATOM   3510  C  CD  . GLN A 1 462  ? -9.450  49.610  25.056  1.00 174.88 ? 462  GLN A CD  1 
ATOM   3511  O  OE1 . GLN A 1 462  ? -8.916  48.597  25.501  1.00 167.25 ? 462  GLN A OE1 1 
ATOM   3512  N  NE2 . GLN A 1 462  ? -8.818  50.775  24.982  1.00 179.55 ? 462  GLN A NE2 1 
ATOM   3513  N  N   . SER A 1 463  ? -11.871 44.869  23.957  1.00 239.85 ? 463  SER A N   1 
ATOM   3514  C  CA  . SER A 1 463  ? -12.292 43.592  24.516  1.00 232.46 ? 463  SER A CA  1 
ATOM   3515  C  C   . SER A 1 463  ? -11.201 42.518  24.470  1.00 222.16 ? 463  SER A C   1 
ATOM   3516  O  O   . SER A 1 463  ? -10.587 42.308  23.425  1.00 224.22 ? 463  SER A O   1 
ATOM   3517  C  CB  . SER A 1 463  ? -13.524 43.115  23.751  1.00 236.45 ? 463  SER A CB  1 
ATOM   3518  O  OG  . SER A 1 463  ? -13.736 41.726  23.898  1.00 233.89 ? 463  SER A OG  1 
ATOM   3519  N  N   . TYR A 1 464  ? -10.963 41.838  25.595  1.00 169.60 ? 464  TYR A N   1 
ATOM   3520  C  CA  . TYR A 1 464  ? -9.999  40.733  25.639  1.00 160.77 ? 464  TYR A CA  1 
ATOM   3521  C  C   . TYR A 1 464  ? -10.591 39.502  26.281  1.00 156.27 ? 464  TYR A C   1 
ATOM   3522  O  O   . TYR A 1 464  ? -11.784 39.438  26.549  1.00 157.10 ? 464  TYR A O   1 
ATOM   3523  C  CB  . TYR A 1 464  ? -8.740  41.128  26.401  1.00 157.64 ? 464  TYR A CB  1 
ATOM   3524  C  CG  . TYR A 1 464  ? -8.385  42.547  26.141  1.00 163.06 ? 464  TYR A CG  1 
ATOM   3525  C  CD1 . TYR A 1 464  ? -8.258  43.019  24.834  1.00 167.70 ? 464  TYR A CD1 1 
ATOM   3526  C  CD2 . TYR A 1 464  ? -8.213  43.434  27.181  1.00 164.12 ? 464  TYR A CD2 1 
ATOM   3527  C  CE1 . TYR A 1 464  ? -7.956  44.343  24.571  1.00 173.18 ? 464  TYR A CE1 1 
ATOM   3528  C  CE2 . TYR A 1 464  ? -7.904  44.761  26.933  1.00 170.08 ? 464  TYR A CE2 1 
ATOM   3529  C  CZ  . TYR A 1 464  ? -7.774  45.211  25.624  1.00 174.75 ? 464  TYR A CZ  1 
ATOM   3530  O  OH  . TYR A 1 464  ? -7.466  46.532  25.359  1.00 179.31 ? 464  TYR A OH  1 
ATOM   3531  N  N   . LEU A 1 465  ? -9.744  38.516  26.518  1.00 137.10 ? 465  LEU A N   1 
ATOM   3532  C  CA  . LEU A 1 465  ? -10.167 37.308  27.199  1.00 136.08 ? 465  LEU A CA  1 
ATOM   3533  C  C   . LEU A 1 465  ? -8.920  36.701  27.830  1.00 132.57 ? 465  LEU A C   1 
ATOM   3534  O  O   . LEU A 1 465  ? -7.798  36.935  27.344  1.00 132.70 ? 465  LEU A O   1 
ATOM   3535  C  CB  . LEU A 1 465  ? -10.822 36.317  26.228  1.00 137.92 ? 465  LEU A CB  1 
ATOM   3536  C  CG  . LEU A 1 465  ? -11.719 35.224  26.817  1.00 138.18 ? 465  LEU A CG  1 
ATOM   3537  C  CD1 . LEU A 1 465  ? -13.081 35.794  27.035  1.00 143.39 ? 465  LEU A CD1 1 
ATOM   3538  C  CD2 . LEU A 1 465  ? -11.816 34.032  25.908  1.00 138.72 ? 465  LEU A CD2 1 
ATOM   3539  N  N   . TYR A 1 466  ? -9.124  35.963  28.929  1.00 149.70 ? 466  TYR A N   1 
ATOM   3540  C  CA  . TYR A 1 466  ? -8.084  35.185  29.612  1.00 157.88 ? 466  TYR A CA  1 
ATOM   3541  C  C   . TYR A 1 466  ? -8.770  34.010  30.222  1.00 156.27 ? 466  TYR A C   1 
ATOM   3542  O  O   . TYR A 1 466  ? -9.710  34.168  30.977  1.00 160.30 ? 466  TYR A O   1 
ATOM   3543  C  CB  . TYR A 1 466  ? -7.428  35.968  30.747  1.00 154.70 ? 466  TYR A CB  1 
ATOM   3544  C  CG  . TYR A 1 466  ? -6.382  35.186  31.544  1.00 146.94 ? 466  TYR A CG  1 
ATOM   3545  C  CD1 . TYR A 1 466  ? -6.003  33.901  31.173  1.00 144.57 ? 466  TYR A CD1 1 
ATOM   3546  C  CD2 . TYR A 1 466  ? -5.754  35.749  32.654  1.00 143.44 ? 466  TYR A CD2 1 
ATOM   3547  C  CE1 . TYR A 1 466  ? -5.028  33.187  31.893  1.00 140.22 ? 466  TYR A CE1 1 
ATOM   3548  C  CE2 . TYR A 1 466  ? -4.779  35.047  33.386  1.00 143.50 ? 466  TYR A CE2 1 
ATOM   3549  C  CZ  . TYR A 1 466  ? -4.420  33.762  33.001  1.00 140.76 ? 466  TYR A CZ  1 
ATOM   3550  O  OH  . TYR A 1 466  ? -3.461  33.051  33.710  1.00 143.50 ? 466  TYR A OH  1 
ATOM   3551  N  N   . ILE A 1 467  ? -8.295  32.826  29.900  1.00 147.72 ? 467  ILE A N   1 
ATOM   3552  C  CA  . ILE A 1 467  ? -8.793  31.667  30.581  1.00 144.93 ? 467  ILE A CA  1 
ATOM   3553  C  C   . ILE A 1 467  ? -7.636  30.947  31.258  1.00 141.69 ? 467  ILE A C   1 
ATOM   3554  O  O   . ILE A 1 467  ? -6.525  30.914  30.713  1.00 139.61 ? 467  ILE A O   1 
ATOM   3555  C  CB  . ILE A 1 467  ? -9.556  30.731  29.643  1.00 143.71 ? 467  ILE A CB  1 
ATOM   3556  C  CG1 . ILE A 1 467  ? -8.610  29.821  28.877  1.00 138.72 ? 467  ILE A CG1 1 
ATOM   3557  C  CG2 . ILE A 1 467  ? -10.406 31.540  28.691  1.00 149.10 ? 467  ILE A CG2 1 
ATOM   3558  C  CD1 . ILE A 1 467  ? -9.334  28.691  28.175  1.00 138.25 ? 467  ILE A CD1 1 
ATOM   3559  N  N   . ASP A 1 468  ? -7.914  30.400  32.453  1.00 126.93 ? 468  ASP A N   1 
ATOM   3560  C  CA  . ASP A 1 468  ? -6.950  29.662  33.288  1.00 123.28 ? 468  ASP A CA  1 
ATOM   3561  C  C   . ASP A 1 468  ? -7.631  28.438  33.921  1.00 122.75 ? 468  ASP A C   1 
ATOM   3562  O  O   . ASP A 1 468  ? -8.721  28.038  33.506  1.00 123.27 ? 468  ASP A O   1 
ATOM   3563  C  CB  . ASP A 1 468  ? -6.350  30.575  34.373  1.00 130.16 ? 468  ASP A CB  1 
ATOM   3564  C  CG  . ASP A 1 468  ? -4.922  30.186  34.766  1.00 132.49 ? 468  ASP A CG  1 
ATOM   3565  O  OD1 . ASP A 1 468  ? -4.160  29.640  33.934  1.00 132.61 ? 468  ASP A OD1 1 
ATOM   3566  O  OD2 . ASP A 1 468  ? -4.551  30.449  35.929  1.00 133.53 ? 468  ASP A OD2 1 
ATOM   3567  N  N   . TRP A 1 469  ? -6.965  27.845  34.904  1.00 192.08 ? 469  TRP A N   1 
ATOM   3568  C  CA  . TRP A 1 469  ? -7.458  26.676  35.622  1.00 200.02 ? 469  TRP A CA  1 
ATOM   3569  C  C   . TRP A 1 469  ? -6.371  26.337  36.622  1.00 210.37 ? 469  TRP A C   1 
ATOM   3570  O  O   . TRP A 1 469  ? -5.246  26.850  36.510  1.00 208.82 ? 469  TRP A O   1 
ATOM   3571  C  CB  . TRP A 1 469  ? -7.744  25.499  34.675  1.00 197.29 ? 469  TRP A CB  1 
ATOM   3572  C  CG  . TRP A 1 469  ? -6.541  24.712  34.074  1.00 192.37 ? 469  TRP A CG  1 
ATOM   3573  C  CD1 . TRP A 1 469  ? -6.395  23.345  34.048  1.00 190.37 ? 469  TRP A CD1 1 
ATOM   3574  C  CD2 . TRP A 1 469  ? -5.380  25.238  33.390  1.00 191.03 ? 469  TRP A CD2 1 
ATOM   3575  N  NE1 . TRP A 1 469  ? -5.223  22.994  33.412  1.00 186.62 ? 469  TRP A NE1 1 
ATOM   3576  C  CE2 . TRP A 1 469  ? -4.582  24.134  33.004  1.00 187.63 ? 469  TRP A CE2 1 
ATOM   3577  C  CE3 . TRP A 1 469  ? -4.934  26.528  33.077  1.00 192.96 ? 469  TRP A CE3 1 
ATOM   3578  C  CZ2 . TRP A 1 469  ? -3.374  24.288  32.323  1.00 186.54 ? 469  TRP A CZ2 1 
ATOM   3579  C  CZ3 . TRP A 1 469  ? -3.728  26.673  32.396  1.00 190.63 ? 469  TRP A CZ3 1 
ATOM   3580  C  CH2 . TRP A 1 469  ? -2.969  25.563  32.029  1.00 187.36 ? 469  TRP A CH2 1 
ATOM   3581  N  N   . THR A 1 470  ? -6.669  25.514  37.619  1.00 212.03 ? 470  THR A N   1 
ATOM   3582  C  CA  . THR A 1 470  ? -5.548  25.026  38.407  1.00 220.64 ? 470  THR A CA  1 
ATOM   3583  C  C   . THR A 1 470  ? -5.579  23.558  38.771  1.00 234.74 ? 470  THR A C   1 
ATOM   3584  O  O   . THR A 1 470  ? -6.614  23.010  39.144  1.00 238.60 ? 470  THR A O   1 
ATOM   3585  C  CB  . THR A 1 470  ? -5.272  25.875  39.636  1.00 217.56 ? 470  THR A CB  1 
ATOM   3586  O  OG1 . THR A 1 470  ? -5.367  27.256  39.274  1.00 218.17 ? 470  THR A OG1 1 
ATOM   3587  C  CG2 . THR A 1 470  ? -3.847  25.593  40.127  1.00 211.22 ? 470  THR A CG2 1 
ATOM   3588  N  N   . ASP A 1 471  ? -4.398  22.966  38.625  1.00 193.00 ? 471  ASP A N   1 
ATOM   3589  C  CA  . ASP A 1 471  ? -4.065  21.633  39.065  1.00 208.46 ? 471  ASP A CA  1 
ATOM   3590  C  C   . ASP A 1 471  ? -2.601  21.641  39.565  1.00 218.75 ? 471  ASP A C   1 
ATOM   3591  O  O   . ASP A 1 471  ? -1.720  22.193  38.886  1.00 217.53 ? 471  ASP A O   1 
ATOM   3592  C  CB  . ASP A 1 471  ? -4.183  20.664  37.895  1.00 214.59 ? 471  ASP A CB  1 
ATOM   3593  C  CG  . ASP A 1 471  ? -4.113  19.140  38.308  1.00 222.04 ? 471  ASP A CG  1 
ATOM   3594  O  OD1 . ASP A 1 471  ? -4.996  18.581  39.036  1.00 226.91 ? 471  ASP A OD1 1 
ATOM   3595  O  OD2 . ASP A 1 471  ? -3.240  18.420  37.736  1.00 223.50 ? 471  ASP A OD2 1 
ATOM   3596  N  N   . ASN A 1 472  ? -2.354  21.005  40.721  1.00 346.02 ? 472  ASN A N   1 
ATOM   3597  C  CA  . ASN A 1 472  ? -1.019  20.901  41.338  1.00 346.54 ? 472  ASN A CA  1 
ATOM   3598  C  C   . ASN A 1 472  ? -0.058  19.862  40.727  1.00 349.57 ? 472  ASN A C   1 
ATOM   3599  O  O   . ASN A 1 472  ? 1.139   19.908  40.987  1.00 342.23 ? 472  ASN A O   1 
ATOM   3600  C  CB  . ASN A 1 472  ? -1.111  20.746  42.878  1.00 341.84 ? 472  ASN A CB  1 
ATOM   3601  C  CG  . ASN A 1 472  ? -2.121  19.687  43.324  1.00 342.82 ? 472  ASN A CG  1 
ATOM   3602  O  OD1 . ASN A 1 472  ? -2.664  18.945  42.510  1.00 346.92 ? 472  ASN A OD1 1 
ATOM   3603  N  ND2 . ASN A 1 472  ? -2.369  19.618  44.634  1.00 338.97 ? 472  ASN A ND2 1 
ATOM   3604  N  N   . HIS A 1 473  ? -0.588  18.948  39.912  1.00 298.49 ? 473  HIS A N   1 
ATOM   3605  C  CA  . HIS A 1 473  ? 0.213   17.932  39.220  1.00 303.89 ? 473  HIS A CA  1 
ATOM   3606  C  C   . HIS A 1 473  ? 0.492   18.275  37.755  1.00 293.58 ? 473  HIS A C   1 
ATOM   3607  O  O   . HIS A 1 473  ? -0.372  18.805  37.049  1.00 296.15 ? 473  HIS A O   1 
ATOM   3608  C  CB  . HIS A 1 473  ? -0.421  16.533  39.333  1.00 327.33 ? 473  HIS A CB  1 
ATOM   3609  C  CG  . HIS A 1 473  ? -1.482  16.412  40.385  1.00 353.50 ? 473  HIS A CG  1 
ATOM   3610  N  ND1 . HIS A 1 473  ? -2.758  16.929  40.221  1.00 365.23 ? 473  HIS A ND1 1 
ATOM   3611  C  CD2 . HIS A 1 473  ? -1.488  15.806  41.598  1.00 361.56 ? 473  HIS A CD2 1 
ATOM   3612  C  CE1 . HIS A 1 473  ? -3.483  16.657  41.292  1.00 381.89 ? 473  HIS A CE1 1 
ATOM   3613  N  NE2 . HIS A 1 473  ? -2.740  15.983  42.141  1.00 373.37 ? 473  HIS A NE2 1 
ATOM   3614  N  N   . LYS A 1 474  ? 1.698   17.920  37.314  1.00 302.98 ? 474  LYS A N   1 
ATOM   3615  C  CA  . LYS A 1 474  ? 2.251   18.364  36.041  1.00 293.84 ? 474  LYS A CA  1 
ATOM   3616  C  C   . LYS A 1 474  ? 1.474   17.805  34.853  1.00 283.74 ? 474  LYS A C   1 
ATOM   3617  O  O   . LYS A 1 474  ? 1.728   18.180  33.705  1.00 285.21 ? 474  LYS A O   1 
ATOM   3618  C  CB  . LYS A 1 474  ? 3.713   17.936  35.941  1.00 289.73 ? 474  LYS A CB  1 
ATOM   3619  C  CG  . LYS A 1 474  ? 3.946   16.487  36.351  1.00 288.01 ? 474  LYS A CG  1 
ATOM   3620  C  CD  . LYS A 1 474  ? 5.363   16.044  36.087  1.00 283.68 ? 474  LYS A CD  1 
ATOM   3621  C  CE  . LYS A 1 474  ? 5.611   15.903  34.602  1.00 288.77 ? 474  LYS A CE  1 
ATOM   3622  N  NZ  . LYS A 1 474  ? 6.988   15.423  34.312  1.00 283.89 ? 474  LYS A NZ  1 
ATOM   3623  N  N   . ALA A 1 475  ? 0.524   16.923  35.150  1.00 262.76 ? 475  ALA A N   1 
ATOM   3624  C  CA  . ALA A 1 475  ? -0.342  16.353  34.142  1.00 246.60 ? 475  ALA A CA  1 
ATOM   3625  C  C   . ALA A 1 475  ? -1.738  16.120  34.706  1.00 233.56 ? 475  ALA A C   1 
ATOM   3626  O  O   . ALA A 1 475  ? -1.901  16.128  35.924  1.00 231.59 ? 475  ALA A O   1 
ATOM   3627  C  CB  . ALA A 1 475  ? 0.266   15.050  33.591  1.00 245.22 ? 475  ALA A CB  1 
ATOM   3628  N  N   . LEU A 1 476  ? -2.712  15.932  33.816  1.00 186.94 ? 476  LEU A N   1 
ATOM   3629  C  CA  . LEU A 1 476  ? -4.078  15.888  34.215  1.00 176.93 ? 476  LEU A CA  1 
ATOM   3630  C  C   . LEU A 1 476  ? -4.665  14.598  33.718  1.00 172.47 ? 476  LEU A C   1 
ATOM   3631  O  O   . LEU A 1 476  ? -5.236  14.538  32.647  1.00 174.66 ? 476  LEU A O   1 
ATOM   3632  C  CB  . LEU A 1 476  ? -4.810  17.103  33.659  1.00 170.45 ? 476  LEU A CB  1 
ATOM   3633  C  CG  . LEU A 1 476  ? -3.943  18.388  33.336  1.00 162.89 ? 476  LEU A CG  1 
ATOM   3634  C  CD1 . LEU A 1 476  ? -4.785  19.520  32.848  1.00 163.21 ? 476  LEU A CD1 1 
ATOM   3635  C  CD2 . LEU A 1 476  ? -3.084  18.920  34.425  1.00 161.36 ? 476  LEU A CD2 1 
ATOM   3636  N  N   . LEU A 1 477  ? -4.453  13.579  34.534  1.00 202.83 ? 477  LEU A N   1 
ATOM   3637  C  CA  . LEU A 1 477  ? -4.925  12.239  34.346  1.00 198.13 ? 477  LEU A CA  1 
ATOM   3638  C  C   . LEU A 1 477  ? -6.268  12.246  33.652  1.00 192.89 ? 477  LEU A C   1 
ATOM   3639  O  O   . LEU A 1 477  ? -6.996  13.233  33.679  1.00 193.84 ? 477  LEU A O   1 
ATOM   3640  C  CB  . LEU A 1 477  ? -5.057  11.555  35.717  1.00 202.83 ? 477  LEU A CB  1 
ATOM   3641  C  CG  . LEU A 1 477  ? -3.966  12.013  36.708  1.00 206.72 ? 477  LEU A CG  1 
ATOM   3642  C  CD1 . LEU A 1 477  ? -4.220  11.501  38.124  1.00 211.32 ? 477  LEU A CD1 1 
ATOM   3643  C  CD2 . LEU A 1 477  ? -2.557  11.652  36.236  1.00 205.33 ? 477  LEU A CD2 1 
ATOM   3644  N  N   . VAL A 1 478  ? -6.566  11.151  32.974  1.00 141.67 ? 478  VAL A N   1 
ATOM   3645  C  CA  . VAL A 1 478  ? -7.837  10.991  32.312  1.00 145.07 ? 478  VAL A CA  1 
ATOM   3646  C  C   . VAL A 1 478  ? -8.867  10.591  33.328  1.00 147.77 ? 478  VAL A C   1 
ATOM   3647  O  O   . VAL A 1 478  ? -8.606  9.752   34.177  1.00 145.76 ? 478  VAL A O   1 
ATOM   3648  C  CB  . VAL A 1 478  ? -7.797  9.843   31.295  1.00 145.48 ? 478  VAL A CB  1 
ATOM   3649  C  CG1 . VAL A 1 478  ? -7.853  8.498   32.003  1.00 147.04 ? 478  VAL A CG1 1 
ATOM   3650  C  CG2 . VAL A 1 478  ? -8.956  9.965   30.335  1.00 147.65 ? 478  VAL A CG2 1 
ATOM   3651  N  N   . GLY A 1 479  ? -10.062 11.154  33.227  1.00 137.21 ? 479  GLY A N   1 
ATOM   3652  C  CA  . GLY A 1 479  ? -11.137 10.823  34.155  1.00 143.26 ? 479  GLY A CA  1 
ATOM   3653  C  C   . GLY A 1 479  ? -11.415 11.986  35.087  1.00 145.18 ? 479  GLY A C   1 
ATOM   3654  O  O   . GLY A 1 479  ? -12.569 12.226  35.447  1.00 151.27 ? 479  GLY A O   1 
ATOM   3655  N  N   . GLU A 1 480  ? -10.340 12.688  35.464  1.00 179.74 ? 480  GLU A N   1 
ATOM   3656  C  CA  . GLU A 1 480  ? -10.409 13.924  36.226  1.00 179.60 ? 480  GLU A CA  1 
ATOM   3657  C  C   . GLU A 1 480  ? -11.406 14.867  35.649  1.00 181.08 ? 480  GLU A C   1 
ATOM   3658  O  O   . GLU A 1 480  ? -12.152 14.519  34.745  1.00 181.47 ? 480  GLU A O   1 
ATOM   3659  C  CB  . GLU A 1 480  ? -9.067  14.585  36.284  1.00 179.83 ? 480  GLU A CB  1 
ATOM   3660  C  CG  . GLU A 1 480  ? -8.346  14.230  37.596  1.00 186.84 ? 480  GLU A CG  1 
ATOM   3661  C  CD  . GLU A 1 480  ? -7.015  14.987  37.749  1.00 193.10 ? 480  GLU A CD  1 
ATOM   3662  O  OE1 . GLU A 1 480  ? -6.529  15.344  38.853  1.00 194.60 ? 480  GLU A OE1 1 
ATOM   3663  O  OE2 . GLU A 1 480  ? -6.372  15.239  36.694  1.00 195.51 ? 480  GLU A OE2 1 
ATOM   3664  N  N   . HIS A 1 481  ? -11.367 16.099  36.108  1.00 185.91 ? 481  HIS A N   1 
ATOM   3665  C  CA  . HIS A 1 481  ? -12.242 17.075  35.516  1.00 190.76 ? 481  HIS A CA  1 
ATOM   3666  C  C   . HIS A 1 481  ? -11.584 18.421  35.484  1.00 186.21 ? 481  HIS A C   1 
ATOM   3667  O  O   . HIS A 1 481  ? -10.879 18.792  36.413  1.00 183.74 ? 481  HIS A O   1 
ATOM   3668  C  CB  . HIS A 1 481  ? -13.566 17.131  36.263  1.00 201.46 ? 481  HIS A CB  1 
ATOM   3669  C  CG  . HIS A 1 481  ? -14.531 16.062  35.849  1.00 209.14 ? 481  HIS A CG  1 
ATOM   3670  N  ND1 . HIS A 1 481  ? -15.480 16.255  34.864  1.00 214.46 ? 481  HIS A ND1 1 
ATOM   3671  C  CD2 . HIS A 1 481  ? -14.683 14.784  36.268  1.00 211.36 ? 481  HIS A CD2 1 
ATOM   3672  C  CE1 . HIS A 1 481  ? -16.183 15.149  34.709  1.00 217.27 ? 481  HIS A CE1 1 
ATOM   3673  N  NE2 . HIS A 1 481  ? -15.720 14.238  35.548  1.00 215.57 ? 481  HIS A NE2 1 
ATOM   3674  N  N   . LEU A 1 482  ? -11.780 19.136  34.388  1.00 179.09 ? 482  LEU A N   1 
ATOM   3675  C  CA  . LEU A 1 482  ? -11.123 20.419  34.251  1.00 178.25 ? 482  LEU A CA  1 
ATOM   3676  C  C   . LEU A 1 482  ? -11.989 21.620  34.629  1.00 182.12 ? 482  LEU A C   1 
ATOM   3677  O  O   . LEU A 1 482  ? -12.925 21.983  33.910  1.00 186.36 ? 482  LEU A O   1 
ATOM   3678  C  CB  . LEU A 1 482  ? -10.535 20.593  32.846  1.00 175.67 ? 482  LEU A CB  1 
ATOM   3679  C  CG  . LEU A 1 482  ? -9.235  21.422  32.839  1.00 171.34 ? 482  LEU A CG  1 
ATOM   3680  C  CD1 . LEU A 1 482  ? -8.311  21.085  31.659  1.00 166.96 ? 482  LEU A CD1 1 
ATOM   3681  C  CD2 . LEU A 1 482  ? -9.508  22.928  32.942  1.00 173.77 ? 482  LEU A CD2 1 
ATOM   3682  N  N   . ASN A 1 483  ? -11.659 22.235  35.762  1.00 202.02 ? 483  ASN A N   1 
ATOM   3683  C  CA  . ASN A 1 483  ? -12.227 23.530  36.101  1.00 203.58 ? 483  ASN A CA  1 
ATOM   3684  C  C   . ASN A 1 483  ? -11.392 24.676  35.567  1.00 200.78 ? 483  ASN A C   1 
ATOM   3685  O  O   . ASN A 1 483  ? -10.275 24.927  36.047  1.00 199.12 ? 483  ASN A O   1 
ATOM   3686  C  CB  . ASN A 1 483  ? -12.410 23.706  37.603  1.00 207.23 ? 483  ASN A CB  1 
ATOM   3687  C  CG  . ASN A 1 483  ? -13.410 24.800  37.934  1.00 213.25 ? 483  ASN A CG  1 
ATOM   3688  O  OD1 . ASN A 1 483  ? -14.485 24.874  37.333  1.00 216.34 ? 483  ASN A OD1 1 
ATOM   3689  N  ND2 . ASN A 1 483  ? -13.061 25.656  38.887  1.00 214.34 ? 483  ASN A ND2 1 
ATOM   3690  N  N   . ILE A 1 484  ? -11.969 25.371  34.587  1.00 135.86 ? 484  ILE A N   1 
ATOM   3691  C  CA  . ILE A 1 484  ? -11.356 26.536  33.959  1.00 131.06 ? 484  ILE A CA  1 
ATOM   3692  C  C   . ILE A 1 484  ? -12.180 27.819  34.151  1.00 130.47 ? 484  ILE A C   1 
ATOM   3693  O  O   . ILE A 1 484  ? -13.391 27.841  33.942  1.00 133.30 ? 484  ILE A O   1 
ATOM   3694  C  CB  . ILE A 1 484  ? -11.108 26.287  32.471  1.00 129.52 ? 484  ILE A CB  1 
ATOM   3695  C  CG1 . ILE A 1 484  ? -11.054 27.620  31.723  1.00 129.66 ? 484  ILE A CG1 1 
ATOM   3696  C  CG2 . ILE A 1 484  ? -12.154 25.316  31.905  1.00 131.25 ? 484  ILE A CG2 1 
ATOM   3697  C  CD1 . ILE A 1 484  ? -11.477 27.542  30.274  1.00 128.01 ? 484  ILE A CD1 1 
ATOM   3698  N  N   . ILE A 1 485  ? -11.493 28.872  34.577  1.00 126.01 ? 485  ILE A N   1 
ATOM   3699  C  CA  . ILE A 1 485  ? -12.100 30.145  34.907  1.00 128.47 ? 485  ILE A CA  1 
ATOM   3700  C  C   . ILE A 1 485  ? -11.996 30.969  33.672  1.00 128.28 ? 485  ILE A C   1 
ATOM   3701  O  O   . ILE A 1 485  ? -10.937 31.022  33.070  1.00 127.97 ? 485  ILE A O   1 
ATOM   3702  C  CB  . ILE A 1 485  ? -11.289 30.862  35.984  1.00 126.04 ? 485  ILE A CB  1 
ATOM   3703  C  CG1 . ILE A 1 485  ? -11.684 30.360  37.378  1.00 132.27 ? 485  ILE A CG1 1 
ATOM   3704  C  CG2 . ILE A 1 485  ? -11.466 32.353  35.888  1.00 129.81 ? 485  ILE A CG2 1 
ATOM   3705  C  CD1 . ILE A 1 485  ? -10.996 29.043  37.825  1.00 123.65 ? 485  ILE A CD1 1 
ATOM   3706  N  N   . VAL A 1 486  ? -13.089 31.621  33.306  1.00 130.99 ? 486  VAL A N   1 
ATOM   3707  C  CA  . VAL A 1 486  ? -13.193 32.312  32.040  1.00 131.74 ? 486  VAL A CA  1 
ATOM   3708  C  C   . VAL A 1 486  ? -13.400 33.793  32.306  1.00 126.27 ? 486  VAL A C   1 
ATOM   3709  O  O   . VAL A 1 486  ? -14.515 34.272  32.244  1.00 128.07 ? 486  VAL A O   1 
ATOM   3710  C  CB  . VAL A 1 486  ? -14.398 31.768  31.248  1.00 126.84 ? 486  VAL A CB  1 
ATOM   3711  C  CG1 . VAL A 1 486  ? -14.697 32.644  30.064  1.00 129.64 ? 486  VAL A CG1 1 
ATOM   3712  C  CG2 . VAL A 1 486  ? -14.160 30.322  30.823  1.00 129.68 ? 486  VAL A CG2 1 
ATOM   3713  N  N   . THR A 1 487  ? -12.329 34.516  32.610  1.00 167.73 ? 487  THR A N   1 
ATOM   3714  C  CA  . THR A 1 487  ? -12.437 35.928  32.983  1.00 170.34 ? 487  THR A CA  1 
ATOM   3715  C  C   . THR A 1 487  ? -12.357 36.866  31.782  1.00 173.73 ? 487  THR A C   1 
ATOM   3716  O  O   . THR A 1 487  ? -11.259 37.168  31.324  1.00 170.90 ? 487  THR A O   1 
ATOM   3717  C  CB  . THR A 1 487  ? -11.308 36.341  33.944  1.00 170.48 ? 487  THR A CB  1 
ATOM   3718  O  OG1 . THR A 1 487  ? -10.042 36.120  33.314  1.00 168.07 ? 487  THR A OG1 1 
ATOM   3719  C  CG2 . THR A 1 487  ? -11.373 35.538  35.223  1.00 167.21 ? 487  THR A CG2 1 
ATOM   3720  N  N   . PRO A 1 488  ? -13.507 37.355  31.281  1.00 133.93 ? 488  PRO A N   1 
ATOM   3721  C  CA  . PRO A 1 488  ? -13.484 38.232  30.100  1.00 139.44 ? 488  PRO A CA  1 
ATOM   3722  C  C   . PRO A 1 488  ? -12.953 39.640  30.371  1.00 136.57 ? 488  PRO A C   1 
ATOM   3723  O  O   . PRO A 1 488  ? -12.914 40.438  29.438  1.00 144.86 ? 488  PRO A O   1 
ATOM   3724  C  CB  . PRO A 1 488  ? -14.959 38.300  29.675  1.00 141.73 ? 488  PRO A CB  1 
ATOM   3725  C  CG  . PRO A 1 488  ? -15.615 37.149  30.346  1.00 139.53 ? 488  PRO A CG  1 
ATOM   3726  C  CD  . PRO A 1 488  ? -14.880 36.979  31.641  1.00 136.16 ? 488  PRO A CD  1 
ATOM   3727  N  N   . LYS A 1 489  ? -12.548 39.912  31.612  1.00 162.50 ? 489  LYS A N   1 
ATOM   3728  C  CA  . LYS A 1 489  ? -12.061 41.224  32.072  1.00 177.13 ? 489  LYS A CA  1 
ATOM   3729  C  C   . LYS A 1 489  ? -11.764 42.254  30.979  1.00 188.88 ? 489  LYS A C   1 
ATOM   3730  O  O   . LYS A 1 489  ? -11.089 41.959  29.997  1.00 189.00 ? 489  LYS A O   1 
ATOM   3731  C  CB  . LYS A 1 489  ? -10.831 41.039  32.987  1.00 175.53 ? 489  LYS A CB  1 
ATOM   3732  C  CG  . LYS A 1 489  ? -10.273 42.314  33.667  1.00 178.90 ? 489  LYS A CG  1 
ATOM   3733  C  CD  . LYS A 1 489  ? -9.361  41.957  34.863  1.00 178.47 ? 489  LYS A CD  1 
ATOM   3734  C  CE  . LYS A 1 489  ? -8.879  43.179  35.658  1.00 181.87 ? 489  LYS A CE  1 
ATOM   3735  N  NZ  . LYS A 1 489  ? -9.959  43.827  36.448  1.00 187.58 ? 489  LYS A NZ  1 
ATOM   3736  N  N   . SER A 1 490  ? -12.295 43.459  31.167  1.00 245.66 ? 490  SER A N   1 
ATOM   3737  C  CA  . SER A 1 490  ? -11.991 44.619  30.323  1.00 254.10 ? 490  SER A CA  1 
ATOM   3738  C  C   . SER A 1 490  ? -13.077 45.048  29.306  1.00 261.69 ? 490  SER A C   1 
ATOM   3739  O  O   . SER A 1 490  ? -13.640 46.142  29.452  1.00 267.85 ? 490  SER A O   1 
ATOM   3740  C  CB  . SER A 1 490  ? -10.599 44.495  29.692  1.00 254.28 ? 490  SER A CB  1 
ATOM   3741  O  OG  . SER A 1 490  ? -9.617  44.324  30.703  1.00 252.16 ? 490  SER A OG  1 
ATOM   3742  N  N   . PRO A 1 491  ? -13.388 44.203  28.295  1.00 224.40 ? 491  PRO A N   1 
ATOM   3743  C  CA  . PRO A 1 491  ? -14.381 44.639  27.306  1.00 225.22 ? 491  PRO A CA  1 
ATOM   3744  C  C   . PRO A 1 491  ? -15.297 45.748  27.819  1.00 219.13 ? 491  PRO A C   1 
ATOM   3745  O  O   . PRO A 1 491  ? -15.995 45.561  28.819  1.00 215.33 ? 491  PRO A O   1 
ATOM   3746  C  CB  . PRO A 1 491  ? -15.166 43.354  27.046  1.00 228.88 ? 491  PRO A CB  1 
ATOM   3747  C  CG  . PRO A 1 491  ? -14.093 42.264  27.143  1.00 225.55 ? 491  PRO A CG  1 
ATOM   3748  C  CD  . PRO A 1 491  ? -12.983 42.804  28.050  1.00 222.25 ? 491  PRO A CD  1 
ATOM   3749  N  N   . TYR A 1 492  ? -15.278 46.891  27.142  1.00 207.34 ? 492  TYR A N   1 
ATOM   3750  C  CA  . TYR A 1 492  ? -16.000 48.037  27.633  1.00 208.63 ? 492  TYR A CA  1 
ATOM   3751  C  C   . TYR A 1 492  ? -17.311 47.556  28.175  1.00 210.23 ? 492  TYR A C   1 
ATOM   3752  O  O   . TYR A 1 492  ? -17.863 48.188  29.061  1.00 214.41 ? 492  TYR A O   1 
ATOM   3753  C  CB  . TYR A 1 492  ? -16.231 49.098  26.558  1.00 213.23 ? 492  TYR A CB  1 
ATOM   3754  C  CG  . TYR A 1 492  ? -17.181 48.728  25.429  1.00 214.47 ? 492  TYR A CG  1 
ATOM   3755  C  CD1 . TYR A 1 492  ? -17.522 49.675  24.458  1.00 219.01 ? 492  TYR A CD1 1 
ATOM   3756  C  CD2 . TYR A 1 492  ? -17.719 47.448  25.310  1.00 209.95 ? 492  TYR A CD2 1 
ATOM   3757  C  CE1 . TYR A 1 492  ? -18.375 49.362  23.398  1.00 221.36 ? 492  TYR A CE1 1 
ATOM   3758  C  CE2 . TYR A 1 492  ? -18.583 47.121  24.255  1.00 212.36 ? 492  TYR A CE2 1 
ATOM   3759  C  CZ  . TYR A 1 492  ? -18.905 48.085  23.294  1.00 218.80 ? 492  TYR A CZ  1 
ATOM   3760  O  OH  . TYR A 1 492  ? -19.751 47.784  22.235  1.00 223.78 ? 492  TYR A OH  1 
ATOM   3761  N  N   . ILE A 1 493  ? -17.806 46.428  27.665  1.00 213.85 ? 493  ILE A N   1 
ATOM   3762  C  CA  . ILE A 1 493  ? -19.069 45.889  28.173  1.00 219.54 ? 493  ILE A CA  1 
ATOM   3763  C  C   . ILE A 1 493  ? -19.194 44.357  28.304  1.00 219.61 ? 493  ILE A C   1 
ATOM   3764  O  O   . ILE A 1 493  ? -18.387 43.592  27.778  1.00 217.32 ? 493  ILE A O   1 
ATOM   3765  C  CB  . ILE A 1 493  ? -20.327 46.549  27.491  1.00 294.59 ? 493  ILE A CB  1 
ATOM   3766  C  CG1 . ILE A 1 493  ? -20.951 47.600  28.429  1.00 297.77 ? 493  ILE A CG1 1 
ATOM   3767  C  CG2 . ILE A 1 493  ? -21.365 45.508  27.110  1.00 296.01 ? 493  ILE A CG2 1 
ATOM   3768  C  CD1 . ILE A 1 493  ? -22.253 48.232  27.937  1.00 305.03 ? 493  ILE A CD1 1 
ATOM   3769  N  N   . ASP A 1 494  ? -20.226 43.961  29.047  1.00 251.20 ? 494  ASP A N   1 
ATOM   3770  C  CA  . ASP A 1 494  ? -20.475 42.598  29.488  1.00 247.98 ? 494  ASP A CA  1 
ATOM   3771  C  C   . ASP A 1 494  ? -21.675 41.948  28.801  1.00 251.87 ? 494  ASP A C   1 
ATOM   3772  O  O   . ASP A 1 494  ? -22.187 40.939  29.286  1.00 250.83 ? 494  ASP A O   1 
ATOM   3773  C  CB  . ASP A 1 494  ? -20.751 42.605  30.997  1.00 248.18 ? 494  ASP A CB  1 
ATOM   3774  C  CG  . ASP A 1 494  ? -21.984 43.443  31.373  1.00 247.79 ? 494  ASP A CG  1 
ATOM   3775  O  OD1 . ASP A 1 494  ? -22.194 44.516  30.764  1.00 250.41 ? 494  ASP A OD1 1 
ATOM   3776  O  OD2 . ASP A 1 494  ? -22.742 43.036  32.285  1.00 248.61 ? 494  ASP A OD2 1 
ATOM   3777  N  N   . LYS A 1 495  ? -22.136 42.523  27.692  1.00 211.18 ? 495  LYS A N   1 
ATOM   3778  C  CA  . LYS A 1 495  ? -23.392 42.084  27.065  1.00 213.54 ? 495  LYS A CA  1 
ATOM   3779  C  C   . LYS A 1 495  ? -23.307 40.692  26.457  1.00 205.57 ? 495  LYS A C   1 
ATOM   3780  O  O   . LYS A 1 495  ? -23.985 40.366  25.474  1.00 206.50 ? 495  LYS A O   1 
ATOM   3781  C  CB  . LYS A 1 495  ? -23.901 43.108  26.042  1.00 222.32 ? 495  LYS A CB  1 
ATOM   3782  C  CG  . LYS A 1 495  ? -24.661 44.284  26.673  1.00 228.74 ? 495  LYS A CG  1 
ATOM   3783  C  CD  . LYS A 1 495  ? -25.498 43.846  27.879  1.00 227.96 ? 495  LYS A CD  1 
ATOM   3784  C  CE  . LYS A 1 495  ? -24.717 43.998  29.189  1.00 221.80 ? 495  LYS A CE  1 
ATOM   3785  N  NZ  . LYS A 1 495  ? -25.126 43.031  30.262  1.00 216.81 ? 495  LYS A NZ  1 
ATOM   3786  N  N   . ILE A 1 496  ? -22.486 39.867  27.091  1.00 200.97 ? 496  ILE A N   1 
ATOM   3787  C  CA  . ILE A 1 496  ? -22.139 38.565  26.562  1.00 195.23 ? 496  ILE A CA  1 
ATOM   3788  C  C   . ILE A 1 496  ? -23.267 37.563  26.618  1.00 199.00 ? 496  ILE A C   1 
ATOM   3789  O  O   . ILE A 1 496  ? -23.788 37.246  27.679  1.00 199.04 ? 496  ILE A O   1 
ATOM   3790  C  CB  . ILE A 1 496  ? -20.948 37.961  27.294  1.00 184.87 ? 496  ILE A CB  1 
ATOM   3791  C  CG1 . ILE A 1 496  ? -19.898 39.044  27.592  1.00 178.21 ? 496  ILE A CG1 1 
ATOM   3792  C  CG2 . ILE A 1 496  ? -20.383 36.795  26.471  1.00 184.43 ? 496  ILE A CG2 1 
ATOM   3793  C  CD1 . ILE A 1 496  ? -19.834 39.482  29.046  1.00 174.62 ? 496  ILE A CD1 1 
ATOM   3794  N  N   . THR A 1 497  ? -23.620 37.055  25.452  1.00 162.48 ? 497  THR A N   1 
ATOM   3795  C  CA  . THR A 1 497  ? -24.549 35.957  25.353  1.00 168.10 ? 497  THR A CA  1 
ATOM   3796  C  C   . THR A 1 497  ? -23.936 34.689  25.927  1.00 163.65 ? 497  THR A C   1 
ATOM   3797  O  O   . THR A 1 497  ? -24.184 34.330  27.075  1.00 163.82 ? 497  THR A O   1 
ATOM   3798  C  CB  . THR A 1 497  ? -24.933 35.691  23.895  1.00 176.42 ? 497  THR A CB  1 
ATOM   3799  O  OG1 . THR A 1 497  ? -25.417 34.349  23.784  1.00 177.39 ? 497  THR A OG1 1 
ATOM   3800  C  CG2 . THR A 1 497  ? -23.723 35.877  22.951  1.00 175.17 ? 497  THR A CG2 1 
ATOM   3801  N  N   . HIS A 1 498  ? -23.107 34.027  25.130  1.00 216.51 ? 498  HIS A N   1 
ATOM   3802  C  CA  . HIS A 1 498  ? -22.652 32.692  25.471  1.00 209.70 ? 498  HIS A CA  1 
ATOM   3803  C  C   . HIS A 1 498  ? -21.133 32.567  25.412  1.00 200.32 ? 498  HIS A C   1 
ATOM   3804  O  O   . HIS A 1 498  ? -20.478 33.258  24.630  1.00 201.00 ? 498  HIS A O   1 
ATOM   3805  C  CB  . HIS A 1 498  ? -23.292 31.675  24.522  1.00 214.38 ? 498  HIS A CB  1 
ATOM   3806  C  CG  . HIS A 1 498  ? -24.782 31.553  24.667  1.00 223.07 ? 498  HIS A CG  1 
ATOM   3807  N  ND1 . HIS A 1 498  ? -25.654 31.841  23.648  1.00 229.92 ? 498  HIS A ND1 1 
ATOM   3808  C  CD2 . HIS A 1 498  ? -25.539 31.162  25.721  1.00 224.15 ? 498  HIS A CD2 1 
ATOM   3809  C  CE1 . HIS A 1 498  ? -26.898 31.636  24.064  1.00 234.45 ? 498  HIS A CE1 1 
ATOM   3810  N  NE2 . HIS A 1 498  ? -26.852 31.227  25.313  1.00 231.03 ? 498  HIS A NE2 1 
ATOM   3811  N  N   . TYR A 1 499  ? -20.580 31.703  26.261  1.00 175.02 ? 499  TYR A N   1 
ATOM   3812  C  CA  . TYR A 1 499  ? -19.210 31.265  26.088  1.00 162.62 ? 499  TYR A CA  1 
ATOM   3813  C  C   . TYR A 1 499  ? -19.232 30.044  25.210  1.00 155.83 ? 499  TYR A C   1 
ATOM   3814  O  O   . TYR A 1 499  ? -20.151 29.219  25.313  1.00 154.76 ? 499  TYR A O   1 
ATOM   3815  C  CB  . TYR A 1 499  ? -18.544 30.948  27.410  1.00 156.74 ? 499  TYR A CB  1 
ATOM   3816  C  CG  . TYR A 1 499  ? -18.338 32.176  28.219  1.00 157.12 ? 499  TYR A CG  1 
ATOM   3817  C  CD1 . TYR A 1 499  ? -17.382 33.120  27.857  1.00 156.05 ? 499  TYR A CD1 1 
ATOM   3818  C  CD2 . TYR A 1 499  ? -19.120 32.413  29.335  1.00 160.61 ? 499  TYR A CD2 1 
ATOM   3819  C  CE1 . TYR A 1 499  ? -17.198 34.267  28.609  1.00 157.40 ? 499  TYR A CE1 1 
ATOM   3820  C  CE2 . TYR A 1 499  ? -18.951 33.543  30.096  1.00 161.91 ? 499  TYR A CE2 1 
ATOM   3821  C  CZ  . TYR A 1 499  ? -17.989 34.473  29.738  1.00 160.32 ? 499  TYR A CZ  1 
ATOM   3822  O  OH  . TYR A 1 499  ? -17.847 35.605  30.523  1.00 160.72 ? 499  TYR A OH  1 
ATOM   3823  N  N   . ASN A 1 500  ? -18.221 29.961  24.338  1.00 179.76 ? 500  ASN A N   1 
ATOM   3824  C  CA  . ASN A 1 500  ? -18.083 28.904  23.334  1.00 176.51 ? 500  ASN A CA  1 
ATOM   3825  C  C   . ASN A 1 500  ? -16.648 28.351  23.289  1.00 166.71 ? 500  ASN A C   1 
ATOM   3826  O  O   . ASN A 1 500  ? -15.671 29.096  23.168  1.00 166.03 ? 500  ASN A O   1 
ATOM   3827  C  CB  . ASN A 1 500  ? -18.483 29.422  21.944  1.00 181.47 ? 500  ASN A CB  1 
ATOM   3828  C  CG  . ASN A 1 500  ? -19.692 30.364  21.978  1.00 188.18 ? 500  ASN A CG  1 
ATOM   3829  O  OD1 . ASN A 1 500  ? -20.508 30.338  22.911  1.00 190.69 ? 500  ASN A OD1 1 
ATOM   3830  N  ND2 . ASN A 1 500  ? -19.814 31.193  20.945  1.00 190.94 ? 500  ASN A ND2 1 
ATOM   3831  N  N   . TYR A 1 501  ? -16.519 27.038  23.384  1.00 187.20 ? 501  TYR A N   1 
ATOM   3832  C  CA  . TYR A 1 501  ? -15.197 26.460  23.429  1.00 180.57 ? 501  TYR A CA  1 
ATOM   3833  C  C   . TYR A 1 501  ? -14.902 25.514  22.301  1.00 179.52 ? 501  TYR A C   1 
ATOM   3834  O  O   . TYR A 1 501  ? -15.771 25.161  21.506  1.00 181.81 ? 501  TYR A O   1 
ATOM   3835  C  CB  . TYR A 1 501  ? -14.961 25.745  24.741  1.00 179.87 ? 501  TYR A CB  1 
ATOM   3836  C  CG  . TYR A 1 501  ? -15.837 24.532  25.011  1.00 183.64 ? 501  TYR A CG  1 
ATOM   3837  C  CD1 . TYR A 1 501  ? -15.405 23.249  24.691  1.00 182.54 ? 501  TYR A CD1 1 
ATOM   3838  C  CD2 . TYR A 1 501  ? -17.070 24.663  25.650  1.00 188.79 ? 501  TYR A CD2 1 
ATOM   3839  C  CE1 . TYR A 1 501  ? -16.188 22.129  24.976  1.00 184.95 ? 501  TYR A CE1 1 
ATOM   3840  C  CE2 . TYR A 1 501  ? -17.863 23.546  25.944  1.00 191.35 ? 501  TYR A CE2 1 
ATOM   3841  C  CZ  . TYR A 1 501  ? -17.415 22.286  25.603  1.00 189.61 ? 501  TYR A CZ  1 
ATOM   3842  O  OH  . TYR A 1 501  ? -18.191 21.183  25.888  1.00 191.70 ? 501  TYR A OH  1 
ATOM   3843  N  N   . LEU A 1 502  ? -13.653 25.084  22.259  1.00 149.69 ? 502  LEU A N   1 
ATOM   3844  C  CA  . LEU A 1 502  ? -13.185 24.279  21.162  1.00 146.86 ? 502  LEU A CA  1 
ATOM   3845  C  C   . LEU A 1 502  ? -11.938 23.548  21.611  1.00 143.35 ? 502  LEU A C   1 
ATOM   3846  O  O   . LEU A 1 502  ? -10.961 24.183  21.983  1.00 139.86 ? 502  LEU A O   1 
ATOM   3847  C  CB  . LEU A 1 502  ? -12.865 25.194  19.999  1.00 145.22 ? 502  LEU A CB  1 
ATOM   3848  C  CG  . LEU A 1 502  ? -13.280 24.706  18.623  1.00 144.03 ? 502  LEU A CG  1 
ATOM   3849  C  CD1 . LEU A 1 502  ? -14.556 23.868  18.686  1.00 143.70 ? 502  LEU A CD1 1 
ATOM   3850  C  CD2 . LEU A 1 502  ? -13.444 25.906  17.698  1.00 146.47 ? 502  LEU A CD2 1 
ATOM   3851  N  N   . ILE A 1 503  ? -11.964 22.216  21.570  1.00 145.47 ? 503  ILE A N   1 
ATOM   3852  C  CA  . ILE A 1 503  ? -10.821 21.416  22.014  1.00 142.21 ? 503  ILE A CA  1 
ATOM   3853  C  C   . ILE A 1 503  ? -10.290 20.443  20.954  1.00 141.38 ? 503  ILE A C   1 
ATOM   3854  O  O   . ILE A 1 503  ? -10.898 19.398  20.692  1.00 142.21 ? 503  ILE A O   1 
ATOM   3855  C  CB  . ILE A 1 503  ? -11.159 20.590  23.256  1.00 140.48 ? 503  ILE A CB  1 
ATOM   3856  C  CG1 . ILE A 1 503  ? -11.777 21.464  24.348  1.00 142.50 ? 503  ILE A CG1 1 
ATOM   3857  C  CG2 . ILE A 1 503  ? -9.906  19.918  23.777  1.00 135.84 ? 503  ILE A CG2 1 
ATOM   3858  C  CD1 . ILE A 1 503  ? -12.503 20.676  25.429  1.00 140.43 ? 503  ILE A CD1 1 
ATOM   3859  N  N   . LEU A 1 504  ? -9.148  20.806  20.362  1.00 143.06 ? 504  LEU A N   1 
ATOM   3860  C  CA  . LEU A 1 504  ? -8.436  20.001  19.367  1.00 142.85 ? 504  LEU A CA  1 
ATOM   3861  C  C   . LEU A 1 504  ? -7.473  19.079  20.062  1.00 143.44 ? 504  LEU A C   1 
ATOM   3862  O  O   . LEU A 1 504  ? -7.064  19.333  21.191  1.00 143.72 ? 504  LEU A O   1 
ATOM   3863  C  CB  . LEU A 1 504  ? -7.605  20.891  18.452  1.00 138.68 ? 504  LEU A CB  1 
ATOM   3864  C  CG  . LEU A 1 504  ? -8.317  21.724  17.398  1.00 139.89 ? 504  LEU A CG  1 
ATOM   3865  C  CD1 . LEU A 1 504  ? -9.631  22.211  17.904  1.00 142.05 ? 504  LEU A CD1 1 
ATOM   3866  C  CD2 . LEU A 1 504  ? -7.441  22.888  17.018  1.00 147.77 ? 504  LEU A CD2 1 
ATOM   3867  N  N   . SER A 1 505  ? -7.066  18.030  19.370  1.00 234.86 ? 505  SER A N   1 
ATOM   3868  C  CA  . SER A 1 505  ? -6.189  17.046  19.963  1.00 232.90 ? 505  SER A CA  1 
ATOM   3869  C  C   . SER A 1 505  ? -5.644  16.197  18.865  1.00 235.59 ? 505  SER A C   1 
ATOM   3870  O  O   . SER A 1 505  ? -6.397  15.492  18.195  1.00 235.97 ? 505  SER A O   1 
ATOM   3871  C  CB  . SER A 1 505  ? -6.979  16.145  20.899  1.00 231.55 ? 505  SER A CB  1 
ATOM   3872  O  OG  . SER A 1 505  ? -6.247  14.969  21.183  1.00 228.05 ? 505  SER A OG  1 
ATOM   3873  N  N   . LYS A 1 506  ? -4.335  16.237  18.687  1.00 169.11 ? 506  LYS A N   1 
ATOM   3874  C  CA  . LYS A 1 506  ? -3.762  15.541  17.564  1.00 170.50 ? 506  LYS A CA  1 
ATOM   3875  C  C   . LYS A 1 506  ? -4.307  16.170  16.301  1.00 176.68 ? 506  LYS A C   1 
ATOM   3876  O  O   . LYS A 1 506  ? -4.866  15.473  15.463  1.00 179.89 ? 506  LYS A O   1 
ATOM   3877  C  CB  . LYS A 1 506  ? -4.178  14.080  17.591  1.00 168.80 ? 506  LYS A CB  1 
ATOM   3878  C  CG  . LYS A 1 506  ? -3.873  13.405  18.896  1.00 163.14 ? 506  LYS A CG  1 
ATOM   3879  C  CD  . LYS A 1 506  ? -4.486  12.031  18.925  1.00 161.35 ? 506  LYS A CD  1 
ATOM   3880  C  CE  . LYS A 1 506  ? -5.979  12.118  19.070  1.00 163.16 ? 506  LYS A CE  1 
ATOM   3881  N  NZ  . LYS A 1 506  ? -6.317  12.637  20.403  1.00 161.52 ? 506  LYS A NZ  1 
ATOM   3882  N  N   . GLY A 1 507  ? -4.182  17.490  16.184  1.00 206.50 ? 507  GLY A N   1 
ATOM   3883  C  CA  . GLY A 1 507  ? -4.601  18.206  14.987  1.00 211.83 ? 507  GLY A CA  1 
ATOM   3884  C  C   . GLY A 1 507  ? -6.081  18.126  14.649  1.00 217.99 ? 507  GLY A C   1 
ATOM   3885  O  O   . GLY A 1 507  ? -6.511  18.657  13.621  1.00 220.77 ? 507  GLY A O   1 
ATOM   3886  N  N   . LYS A 1 508  ? -6.858  17.465  15.509  1.00 226.52 ? 508  LYS A N   1 
ATOM   3887  C  CA  . LYS A 1 508  ? -8.289  17.257  15.275  1.00 229.64 ? 508  LYS A CA  1 
ATOM   3888  C  C   . LYS A 1 508  ? -9.168  17.863  16.369  1.00 224.85 ? 508  LYS A C   1 
ATOM   3889  O  O   . LYS A 1 508  ? -8.977  17.600  17.559  1.00 221.07 ? 508  LYS A O   1 
ATOM   3890  C  CB  . LYS A 1 508  ? -8.593  15.759  15.169  1.00 230.47 ? 508  LYS A CB  1 
ATOM   3891  C  CG  . LYS A 1 508  ? -9.265  15.337  13.885  1.00 234.61 ? 508  LYS A CG  1 
ATOM   3892  C  CD  . LYS A 1 508  ? -9.179  13.839  13.729  1.00 233.45 ? 508  LYS A CD  1 
ATOM   3893  C  CE  . LYS A 1 508  ? -8.994  13.475  12.273  1.00 235.36 ? 508  LYS A CE  1 
ATOM   3894  N  NZ  . LYS A 1 508  ? -8.405  12.123  12.131  1.00 233.13 ? 508  LYS A NZ  1 
ATOM   3895  N  N   . ILE A 1 509  ? -10.139 18.672  15.963  1.00 154.25 ? 509  ILE A N   1 
ATOM   3896  C  CA  . ILE A 1 509  ? -11.154 19.115  16.897  1.00 150.75 ? 509  ILE A CA  1 
ATOM   3897  C  C   . ILE A 1 509  ? -11.902 17.868  17.336  1.00 147.56 ? 509  ILE A C   1 
ATOM   3898  O  O   . ILE A 1 509  ? -12.089 16.939  16.549  1.00 148.99 ? 509  ILE A O   1 
ATOM   3899  C  CB  . ILE A 1 509  ? -12.150 20.101  16.256  1.00 152.98 ? 509  ILE A CB  1 
ATOM   3900  C  CG1 . ILE A 1 509  ? -11.420 21.192  15.491  1.00 152.49 ? 509  ILE A CG1 1 
ATOM   3901  C  CG2 . ILE A 1 509  ? -13.018 20.753  17.311  1.00 155.32 ? 509  ILE A CG2 1 
ATOM   3902  C  CD1 . ILE A 1 509  ? -12.094 22.537  15.618  1.00 155.86 ? 509  ILE A CD1 1 
ATOM   3903  N  N   . ILE A 1 510  ? -12.322 17.842  18.594  1.00 175.70 ? 510  ILE A N   1 
ATOM   3904  C  CA  . ILE A 1 510  ? -13.068 16.709  19.112  1.00 174.60 ? 510  ILE A CA  1 
ATOM   3905  C  C   . ILE A 1 510  ? -14.038 17.161  20.180  1.00 176.95 ? 510  ILE A C   1 
ATOM   3906  O  O   . ILE A 1 510  ? -14.955 16.430  20.538  1.00 176.28 ? 510  ILE A O   1 
ATOM   3907  C  CB  . ILE A 1 510  ? -12.141 15.672  19.716  1.00 179.15 ? 510  ILE A CB  1 
ATOM   3908  C  CG1 . ILE A 1 510  ? -10.979 16.383  20.407  1.00 175.89 ? 510  ILE A CG1 1 
ATOM   3909  C  CG2 . ILE A 1 510  ? -11.624 14.731  18.648  1.00 178.35 ? 510  ILE A CG2 1 
ATOM   3910  C  CD1 . ILE A 1 510  ? -10.032 15.442  21.123  1.00 171.31 ? 510  ILE A CD1 1 
ATOM   3911  N  N   . HIS A 1 511  ? -13.846 18.371  20.687  1.00 177.35 ? 511  HIS A N   1 
ATOM   3912  C  CA  . HIS A 1 511  ? -14.810 18.916  21.620  1.00 184.26 ? 511  HIS A CA  1 
ATOM   3913  C  C   . HIS A 1 511  ? -15.126 20.373  21.363  1.00 189.38 ? 511  HIS A C   1 
ATOM   3914  O  O   . HIS A 1 511  ? -14.295 21.135  20.875  1.00 189.28 ? 511  HIS A O   1 
ATOM   3915  C  CB  . HIS A 1 511  ? -14.352 18.688  23.049  1.00 184.74 ? 511  HIS A CB  1 
ATOM   3916  C  CG  . HIS A 1 511  ? -14.118 17.246  23.364  1.00 183.93 ? 511  HIS A CG  1 
ATOM   3917  N  ND1 . HIS A 1 511  ? -15.143 16.372  23.652  1.00 185.93 ? 511  HIS A ND1 1 
ATOM   3918  C  CD2 . HIS A 1 511  ? -12.978 16.515  23.402  1.00 180.61 ? 511  HIS A CD2 1 
ATOM   3919  C  CE1 . HIS A 1 511  ? -14.645 15.167  23.870  1.00 182.52 ? 511  HIS A CE1 1 
ATOM   3920  N  NE2 . HIS A 1 511  ? -13.334 15.226  23.724  1.00 179.27 ? 511  HIS A NE2 1 
ATOM   3921  N  N   . PHE A 1 512  ? -16.358 20.736  21.691  1.00 169.48 ? 512  PHE A N   1 
ATOM   3922  C  CA  . PHE A 1 512  ? -16.863 22.083  21.496  1.00 175.65 ? 512  PHE A CA  1 
ATOM   3923  C  C   . PHE A 1 512  ? -18.262 22.112  22.105  1.00 176.82 ? 512  PHE A C   1 
ATOM   3924  O  O   . PHE A 1 512  ? -18.883 21.064  22.285  1.00 174.66 ? 512  PHE A O   1 
ATOM   3925  C  CB  . PHE A 1 512  ? -16.950 22.412  20.009  1.00 184.45 ? 512  PHE A CB  1 
ATOM   3926  C  CG  . PHE A 1 512  ? -18.119 21.780  19.340  1.00 192.43 ? 512  PHE A CG  1 
ATOM   3927  C  CD1 . PHE A 1 512  ? -19.152 22.550  18.828  1.00 198.74 ? 512  PHE A CD1 1 
ATOM   3928  C  CD2 . PHE A 1 512  ? -18.212 20.401  19.278  1.00 191.46 ? 512  PHE A CD2 1 
ATOM   3929  C  CE1 . PHE A 1 512  ? -20.242 21.948  18.235  1.00 202.90 ? 512  PHE A CE1 1 
ATOM   3930  C  CE2 . PHE A 1 512  ? -19.293 19.793  18.690  1.00 195.05 ? 512  PHE A CE2 1 
ATOM   3931  C  CZ  . PHE A 1 512  ? -20.314 20.565  18.167  1.00 200.58 ? 512  PHE A CZ  1 
ATOM   3932  N  N   . GLY A 1 513  ? -18.758 23.303  22.428  1.00 169.38 ? 513  GLY A N   1 
ATOM   3933  C  CA  . GLY A 1 513  ? -20.088 23.448  23.001  1.00 173.71 ? 513  GLY A CA  1 
ATOM   3934  C  C   . GLY A 1 513  ? -20.372 24.878  23.418  1.00 176.76 ? 513  GLY A C   1 
ATOM   3935  O  O   . GLY A 1 513  ? -19.697 25.799  22.958  1.00 175.29 ? 513  GLY A O   1 
ATOM   3936  N  N   . THR A 1 514  ? -21.362 25.077  24.286  1.00 179.87 ? 514  THR A N   1 
ATOM   3937  C  CA  . THR A 1 514  ? -21.585 26.406  24.866  1.00 183.99 ? 514  THR A CA  1 
ATOM   3938  C  C   . THR A 1 514  ? -22.180 26.416  26.275  1.00 182.76 ? 514  THR A C   1 
ATOM   3939  O  O   . THR A 1 514  ? -23.120 25.681  26.583  1.00 184.10 ? 514  THR A O   1 
ATOM   3940  C  CB  . THR A 1 514  ? -22.444 27.291  23.966  1.00 191.27 ? 514  THR A CB  1 
ATOM   3941  O  OG1 . THR A 1 514  ? -21.701 27.626  22.793  1.00 191.63 ? 514  THR A OG1 1 
ATOM   3942  C  CG2 . THR A 1 514  ? -22.807 28.570  24.690  1.00 196.04 ? 514  THR A CG2 1 
ATOM   3943  N  N   . ARG A 1 515  ? -21.616 27.267  27.124  1.00 224.00 ? 515  ARG A N   1 
ATOM   3944  C  CA  . ARG A 1 515  ? -22.133 27.477  28.460  1.00 228.31 ? 515  ARG A CA  1 
ATOM   3945  C  C   . ARG A 1 515  ? -22.765 28.861  28.495  1.00 231.36 ? 515  ARG A C   1 
ATOM   3946  O  O   . ARG A 1 515  ? -22.095 29.850  28.194  1.00 231.35 ? 515  ARG A O   1 
ATOM   3947  C  CB  . ARG A 1 515  ? -20.988 27.415  29.470  1.00 229.02 ? 515  ARG A CB  1 
ATOM   3948  C  CG  . ARG A 1 515  ? -20.050 26.233  29.294  1.00 228.91 ? 515  ARG A CG  1 
ATOM   3949  C  CD  . ARG A 1 515  ? -20.758 24.918  29.540  1.00 234.08 ? 515  ARG A CD  1 
ATOM   3950  N  NE  . ARG A 1 515  ? -19.806 23.821  29.675  1.00 233.56 ? 515  ARG A NE  1 
ATOM   3951  C  CZ  . ARG A 1 515  ? -19.079 23.590  30.768  1.00 234.76 ? 515  ARG A CZ  1 
ATOM   3952  N  NH1 . ARG A 1 515  ? -19.183 24.385  31.829  1.00 236.88 ? 515  ARG A NH1 1 
ATOM   3953  N  NH2 . ARG A 1 515  ? -18.235 22.564  30.805  1.00 232.46 ? 515  ARG A NH2 1 
ATOM   3954  N  N   . GLU A 1 516  ? -24.045 28.936  28.855  1.00 223.82 ? 516  GLU A N   1 
ATOM   3955  C  CA  . GLU A 1 516  ? -24.718 30.230  28.973  1.00 225.92 ? 516  GLU A CA  1 
ATOM   3956  C  C   . GLU A 1 516  ? -24.012 31.104  30.002  1.00 221.60 ? 516  GLU A C   1 
ATOM   3957  O  O   . GLU A 1 516  ? -23.740 30.667  31.121  1.00 216.39 ? 516  GLU A O   1 
ATOM   3958  C  CB  . GLU A 1 516  ? -26.205 30.067  29.327  1.00 232.29 ? 516  GLU A CB  1 
ATOM   3959  C  CG  . GLU A 1 516  ? -26.910 31.376  29.756  1.00 238.57 ? 516  GLU A CG  1 
ATOM   3960  C  CD  . GLU A 1 516  ? -28.306 31.558  29.146  1.00 245.66 ? 516  GLU A CD  1 
ATOM   3961  O  OE1 . GLU A 1 516  ? -29.131 32.294  29.739  1.00 249.82 ? 516  GLU A OE1 1 
ATOM   3962  O  OE2 . GLU A 1 516  ? -28.570 30.976  28.068  1.00 247.47 ? 516  GLU A OE2 1 
ATOM   3963  N  N   . LYS A 1 517  ? -23.710 32.339  29.616  1.00 180.96 ? 517  LYS A N   1 
ATOM   3964  C  CA  . LYS A 1 517  ? -22.993 33.250  30.493  1.00 180.76 ? 517  LYS A CA  1 
ATOM   3965  C  C   . LYS A 1 517  ? -23.773 33.617  31.756  1.00 189.68 ? 517  LYS A C   1 
ATOM   3966  O  O   . LYS A 1 517  ? -24.993 33.802  31.720  1.00 196.94 ? 517  LYS A O   1 
ATOM   3967  C  CB  . LYS A 1 517  ? -22.595 34.513  29.745  1.00 178.51 ? 517  LYS A CB  1 
ATOM   3968  C  CG  . LYS A 1 517  ? -21.504 35.282  30.452  1.00 173.24 ? 517  LYS A CG  1 
ATOM   3969  C  CD  . LYS A 1 517  ? -22.015 36.564  31.050  1.00 175.13 ? 517  LYS A CD  1 
ATOM   3970  C  CE  . LYS A 1 517  ? -20.886 37.343  31.692  1.00 170.79 ? 517  LYS A CE  1 
ATOM   3971  N  NZ  . LYS A 1 517  ? -21.088 38.801  31.474  1.00 174.08 ? 517  LYS A NZ  1 
ATOM   3972  N  N   . PHE A 1 518  ? -23.043 33.723  32.867  1.00 238.52 ? 518  PHE A N   1 
ATOM   3973  C  CA  . PHE A 1 518  ? -23.603 34.082  34.169  1.00 245.49 ? 518  PHE A CA  1 
ATOM   3974  C  C   . PHE A 1 518  ? -23.933 35.558  34.267  1.00 252.23 ? 518  PHE A C   1 
ATOM   3975  O  O   . PHE A 1 518  ? -23.058 36.396  34.498  1.00 248.28 ? 518  PHE A O   1 
ATOM   3976  C  CB  . PHE A 1 518  ? -22.656 33.669  35.293  1.00 244.62 ? 518  PHE A CB  1 
ATOM   3977  C  CG  . PHE A 1 518  ? -23.026 32.364  35.930  1.00 247.50 ? 518  PHE A CG  1 
ATOM   3978  C  CD1 . PHE A 1 518  ? -24.018 31.575  35.368  1.00 251.59 ? 518  PHE A CD1 1 
ATOM   3979  C  CD2 . PHE A 1 518  ? -22.394 31.925  37.091  1.00 246.06 ? 518  PHE A CD2 1 
ATOM   3980  C  CE1 . PHE A 1 518  ? -24.378 30.373  35.945  1.00 251.71 ? 518  PHE A CE1 1 
ATOM   3981  C  CE2 . PHE A 1 518  ? -22.747 30.717  37.681  1.00 246.26 ? 518  PHE A CE2 1 
ATOM   3982  C  CZ  . PHE A 1 518  ? -23.740 29.940  37.106  1.00 248.67 ? 518  PHE A CZ  1 
ATOM   3983  N  N   . SER A 1 519  ? -25.220 35.845  34.113  1.00 175.27 ? 519  SER A N   1 
ATOM   3984  C  CA  . SER A 1 519  ? -25.713 37.199  33.959  1.00 184.34 ? 519  SER A CA  1 
ATOM   3985  C  C   . SER A 1 519  ? -24.947 38.145  34.849  1.00 186.66 ? 519  SER A C   1 
ATOM   3986  O  O   . SER A 1 519  ? -23.894 38.646  34.466  1.00 188.61 ? 519  SER A O   1 
ATOM   3987  C  CB  . SER A 1 519  ? -27.205 37.248  34.276  1.00 189.40 ? 519  SER A CB  1 
ATOM   3988  O  OG  . SER A 1 519  ? -27.901 36.261  33.532  1.00 189.21 ? 519  SER A OG  1 
ATOM   3989  N  N   . ASP A 1 520  ? -25.474 38.369  36.044  1.00 282.70 ? 520  ASP A N   1 
ATOM   3990  C  CA  . ASP A 1 520  ? -24.865 39.286  36.994  1.00 284.92 ? 520  ASP A CA  1 
ATOM   3991  C  C   . ASP A 1 520  ? -23.352 39.353  36.860  1.00 277.37 ? 520  ASP A C   1 
ATOM   3992  O  O   . ASP A 1 520  ? -22.817 40.104  36.048  1.00 277.79 ? 520  ASP A O   1 
ATOM   3993  C  CB  . ASP A 1 520  ? -25.215 38.864  38.421  1.00 293.32 ? 520  ASP A CB  1 
ATOM   3994  C  CG  . ASP A 1 520  ? -24.863 37.412  38.700  1.00 299.65 ? 520  ASP A CG  1 
ATOM   3995  O  OD1 . ASP A 1 520  ? -24.583 36.676  37.726  1.00 300.59 ? 520  ASP A OD1 1 
ATOM   3996  O  OD2 . ASP A 1 520  ? -24.861 37.006  39.885  1.00 301.73 ? 520  ASP A OD2 1 
ATOM   3997  N  N   . ALA A 1 521  ? -22.673 38.545  37.660  1.00 220.14 ? 521  ALA A N   1 
ATOM   3998  C  CA  . ALA A 1 521  ? -21.240 38.682  37.867  1.00 209.10 ? 521  ALA A CA  1 
ATOM   3999  C  C   . ALA A 1 521  ? -20.384 38.436  36.629  1.00 194.05 ? 521  ALA A C   1 
ATOM   4000  O  O   . ALA A 1 521  ? -20.858 37.985  35.577  1.00 193.01 ? 521  ALA A O   1 
ATOM   4001  C  CB  . ALA A 1 521  ? -20.773 37.794  39.042  1.00 207.99 ? 521  ALA A CB  1 
ATOM   4002  N  N   . SER A 1 522  ? -19.105 38.745  36.812  1.00 240.63 ? 522  SER A N   1 
ATOM   4003  C  CA  . SER A 1 522  ? -18.076 38.650  35.797  1.00 230.35 ? 522  SER A CA  1 
ATOM   4004  C  C   . SER A 1 522  ? -17.921 37.231  35.285  1.00 221.48 ? 522  SER A C   1 
ATOM   4005  O  O   . SER A 1 522  ? -18.828 36.652  34.676  1.00 223.19 ? 522  SER A O   1 
ATOM   4006  C  CB  . SER A 1 522  ? -16.743 39.116  36.406  1.00 225.89 ? 522  SER A CB  1 
ATOM   4007  O  OG  . SER A 1 522  ? -15.663 39.008  35.493  1.00 222.63 ? 522  SER A OG  1 
ATOM   4008  N  N   . TYR A 1 523  ? -16.745 36.688  35.566  1.00 166.73 ? 523  TYR A N   1 
ATOM   4009  C  CA  . TYR A 1 523  ? -16.320 35.392  35.083  1.00 156.51 ? 523  TYR A CA  1 
ATOM   4010  C  C   . TYR A 1 523  ? -17.238 34.257  35.464  1.00 152.80 ? 523  TYR A C   1 
ATOM   4011  O  O   . TYR A 1 523  ? -18.308 34.456  36.021  1.00 153.37 ? 523  TYR A O   1 
ATOM   4012  C  CB  . TYR A 1 523  ? -14.934 35.095  35.630  1.00 151.54 ? 523  TYR A CB  1 
ATOM   4013  C  CG  . TYR A 1 523  ? -14.815 35.256  37.129  1.00 149.98 ? 523  TYR A CG  1 
ATOM   4014  C  CD1 . TYR A 1 523  ? -14.993 34.169  37.978  1.00 148.12 ? 523  TYR A CD1 1 
ATOM   4015  C  CD2 . TYR A 1 523  ? -14.495 36.488  37.695  1.00 149.32 ? 523  TYR A CD2 1 
ATOM   4016  C  CE1 . TYR A 1 523  ? -14.861 34.301  39.341  1.00 146.79 ? 523  TYR A CE1 1 
ATOM   4017  C  CE2 . TYR A 1 523  ? -14.364 36.628  39.057  1.00 147.30 ? 523  TYR A CE2 1 
ATOM   4018  C  CZ  . TYR A 1 523  ? -14.548 35.527  39.874  1.00 146.97 ? 523  TYR A CZ  1 
ATOM   4019  O  OH  . TYR A 1 523  ? -14.430 35.635  41.233  1.00 148.45 ? 523  TYR A OH  1 
ATOM   4020  N  N   . GLN A 1 524  ? -16.800 33.052  35.143  1.00 146.07 ? 524  GLN A N   1 
ATOM   4021  C  CA  . GLN A 1 524  ? -17.455 31.869  35.650  1.00 149.03 ? 524  GLN A CA  1 
ATOM   4022  C  C   . GLN A 1 524  ? -16.744 30.614  35.201  1.00 147.77 ? 524  GLN A C   1 
ATOM   4023  O  O   . GLN A 1 524  ? -15.997 30.615  34.227  1.00 145.90 ? 524  GLN A O   1 
ATOM   4024  C  CB  . GLN A 1 524  ? -18.897 31.815  35.196  1.00 153.51 ? 524  GLN A CB  1 
ATOM   4025  C  CG  . GLN A 1 524  ? -19.055 31.306  33.803  1.00 153.53 ? 524  GLN A CG  1 
ATOM   4026  C  CD  . GLN A 1 524  ? -20.126 32.069  33.083  1.00 160.34 ? 524  GLN A CD  1 
ATOM   4027  O  OE1 . GLN A 1 524  ? -20.216 33.289  33.218  1.00 163.19 ? 524  GLN A OE1 1 
ATOM   4028  N  NE2 . GLN A 1 524  ? -20.954 31.367  32.319  1.00 162.86 ? 524  GLN A NE2 1 
ATOM   4029  N  N   . SER A 1 525  ? -17.000 29.537  35.930  1.00 214.20 ? 525  SER A N   1 
ATOM   4030  C  CA  . SER A 1 525  ? -16.324 28.275  35.710  1.00 210.98 ? 525  SER A CA  1 
ATOM   4031  C  C   . SER A 1 525  ? -16.871 27.529  34.485  1.00 212.43 ? 525  SER A C   1 
ATOM   4032  O  O   . SER A 1 525  ? -18.065 27.605  34.168  1.00 213.75 ? 525  SER A O   1 
ATOM   4033  C  CB  . SER A 1 525  ? -16.430 27.416  36.975  1.00 213.29 ? 525  SER A CB  1 
ATOM   4034  O  OG  . SER A 1 525  ? -16.179 28.187  38.140  1.00 214.95 ? 525  SER A OG  1 
ATOM   4035  N  N   . ILE A 1 526  ? -15.975 26.834  33.786  1.00 179.29 ? 526  ILE A N   1 
ATOM   4036  C  CA  . ILE A 1 526  ? -16.364 25.868  32.763  1.00 175.98 ? 526  ILE A CA  1 
ATOM   4037  C  C   . ILE A 1 526  ? -15.765 24.509  33.132  1.00 171.00 ? 526  ILE A C   1 
ATOM   4038  O  O   . ILE A 1 526  ? -14.591 24.421  33.516  1.00 161.71 ? 526  ILE A O   1 
ATOM   4039  C  CB  . ILE A 1 526  ? -15.894 26.288  31.350  1.00 169.50 ? 526  ILE A CB  1 
ATOM   4040  C  CG1 . ILE A 1 526  ? -16.425 27.670  30.995  1.00 166.95 ? 526  ILE A CG1 1 
ATOM   4041  C  CG2 . ILE A 1 526  ? -16.386 25.307  30.318  1.00 170.33 ? 526  ILE A CG2 1 
ATOM   4042  C  CD1 . ILE A 1 526  ? -16.196 28.045  29.566  1.00 167.69 ? 526  ILE A CD1 1 
ATOM   4043  N  N   . ASN A 1 527  ? -16.566 23.451  33.035  1.00 225.66 ? 527  ASN A N   1 
ATOM   4044  C  CA  . ASN A 1 527  ? -16.063 22.139  33.420  1.00 228.57 ? 527  ASN A CA  1 
ATOM   4045  C  C   . ASN A 1 527  ? -16.173 21.019  32.403  1.00 232.43 ? 527  ASN A C   1 
ATOM   4046  O  O   . ASN A 1 527  ? -17.205 20.352  32.292  1.00 235.96 ? 527  ASN A O   1 
ATOM   4047  C  CB  . ASN A 1 527  ? -16.643 21.676  34.744  1.00 231.90 ? 527  ASN A CB  1 
ATOM   4048  C  CG  . ASN A 1 527  ? -15.732 20.692  35.439  1.00 230.63 ? 527  ASN A CG  1 
ATOM   4049  O  OD1 . ASN A 1 527  ? -15.345 19.675  34.860  1.00 228.18 ? 527  ASN A OD1 1 
ATOM   4050  N  ND2 . ASN A 1 527  ? -15.358 21.001  36.675  1.00 232.80 ? 527  ASN A ND2 1 
ATOM   4051  N  N   . ILE A 1 528  ? -15.059 20.800  31.713  1.00 168.14 ? 528  ILE A N   1 
ATOM   4052  C  CA  . ILE A 1 528  ? -14.952 19.787  30.680  1.00 169.50 ? 528  ILE A CA  1 
ATOM   4053  C  C   . ILE A 1 528  ? -14.187 18.561  31.174  1.00 168.33 ? 528  ILE A C   1 
ATOM   4054  O  O   . ILE A 1 528  ? -13.020 18.656  31.584  1.00 165.45 ? 528  ILE A O   1 
ATOM   4055  C  CB  . ILE A 1 528  ? -14.289 20.346  29.407  1.00 172.14 ? 528  ILE A CB  1 
ATOM   4056  C  CG1 . ILE A 1 528  ? -14.468 21.866  29.338  1.00 175.24 ? 528  ILE A CG1 1 
ATOM   4057  C  CG2 . ILE A 1 528  ? -14.861 19.659  28.162  1.00 173.34 ? 528  ILE A CG2 1 
ATOM   4058  C  CD1 . ILE A 1 528  ? -13.551 22.660  30.264  1.00 174.68 ? 528  ILE A CD1 1 
ATOM   4059  N  N   . PRO A 1 529  ? -14.875 17.407  31.166  1.00 208.23 ? 529  PRO A N   1 
ATOM   4060  C  CA  . PRO A 1 529  ? -14.334 16.069  31.405  1.00 207.62 ? 529  PRO A CA  1 
ATOM   4061  C  C   . PRO A 1 529  ? -13.190 15.799  30.458  1.00 204.91 ? 529  PRO A C   1 
ATOM   4062  O  O   . PRO A 1 529  ? -13.415 15.709  29.250  1.00 207.18 ? 529  PRO A O   1 
ATOM   4063  C  CB  . PRO A 1 529  ? -15.500 15.155  31.018  1.00 208.73 ? 529  PRO A CB  1 
ATOM   4064  C  CG  . PRO A 1 529  ? -16.694 15.945  31.335  1.00 212.96 ? 529  PRO A CG  1 
ATOM   4065  C  CD  . PRO A 1 529  ? -16.345 17.384  31.058  1.00 212.82 ? 529  PRO A CD  1 
ATOM   4066  N  N   . VAL A 1 530  ? -11.983 15.677  30.991  1.00 170.99 ? 530  VAL A N   1 
ATOM   4067  C  CA  . VAL A 1 530  ? -10.883 15.262  30.161  1.00 166.81 ? 530  VAL A CA  1 
ATOM   4068  C  C   . VAL A 1 530  ? -11.240 13.887  29.609  1.00 165.13 ? 530  VAL A C   1 
ATOM   4069  O  O   . VAL A 1 530  ? -11.626 12.983  30.343  1.00 164.62 ? 530  VAL A O   1 
ATOM   4070  C  CB  . VAL A 1 530  ? -9.563  15.237  30.940  1.00 140.21 ? 530  VAL A CB  1 
ATOM   4071  C  CG1 . VAL A 1 530  ? -9.427  13.978  31.754  1.00 138.36 ? 530  VAL A CG1 1 
ATOM   4072  C  CG2 . VAL A 1 530  ? -8.407  15.355  30.002  1.00 137.96 ? 530  VAL A CG2 1 
ATOM   4073  N  N   . THR A 1 531  ? -11.169 13.732  28.304  1.00 194.66 ? 531  THR A N   1 
ATOM   4074  C  CA  . THR A 1 531  ? -11.544 12.460  27.751  1.00 195.82 ? 531  THR A CA  1 
ATOM   4075  C  C   . THR A 1 531  ? -10.341 11.741  27.201  1.00 193.36 ? 531  THR A C   1 
ATOM   4076  O  O   . THR A 1 531  ? -9.409  12.352  26.668  1.00 191.15 ? 531  THR A O   1 
ATOM   4077  C  CB  . THR A 1 531  ? -12.594 12.605  26.647  1.00 199.61 ? 531  THR A CB  1 
ATOM   4078  O  OG1 . THR A 1 531  ? -13.074 11.306  26.282  1.00 200.08 ? 531  THR A OG1 1 
ATOM   4079  C  CG2 . THR A 1 531  ? -11.997 13.280  25.422  1.00 199.81 ? 531  THR A CG2 1 
ATOM   4080  N  N   . GLN A 1 532  ? -10.376 10.425  27.328  1.00 170.08 ? 532  GLN A N   1 
ATOM   4081  C  CA  . GLN A 1 532  ? -9.363  9.588   26.721  1.00 170.02 ? 532  GLN A CA  1 
ATOM   4082  C  C   . GLN A 1 532  ? -8.984  10.146  25.335  1.00 171.12 ? 532  GLN A C   1 
ATOM   4083  O  O   . GLN A 1 532  ? -7.831  10.063  24.923  1.00 169.79 ? 532  GLN A O   1 
ATOM   4084  C  CB  . GLN A 1 532  ? -9.896  8.154   26.652  1.00 171.60 ? 532  GLN A CB  1 
ATOM   4085  C  CG  . GLN A 1 532  ? -9.024  7.166   25.907  1.00 170.69 ? 532  GLN A CG  1 
ATOM   4086  C  CD  . GLN A 1 532  ? -7.741  6.843   26.631  1.00 167.31 ? 532  GLN A CD  1 
ATOM   4087  O  OE1 . GLN A 1 532  ? -7.354  7.526   27.574  1.00 167.39 ? 532  GLN A OE1 1 
ATOM   4088  N  NE2 . GLN A 1 532  ? -7.067  5.796   26.188  1.00 163.72 ? 532  GLN A NE2 1 
ATOM   4089  N  N   . ASN A 1 533  ? -9.949  10.770  24.656  1.00 194.14 ? 533  ASN A N   1 
ATOM   4090  C  CA  . ASN A 1 533  ? -9.760  11.280  23.297  1.00 194.93 ? 533  ASN A CA  1 
ATOM   4091  C  C   . ASN A 1 533  ? -8.812  12.452  23.178  1.00 192.48 ? 533  ASN A C   1 
ATOM   4092  O  O   . ASN A 1 533  ? -8.658  13.018  22.100  1.00 193.43 ? 533  ASN A O   1 
ATOM   4093  C  CB  . ASN A 1 533  ? -11.090 11.712  22.685  1.00 201.10 ? 533  ASN A CB  1 
ATOM   4094  C  CG  . ASN A 1 533  ? -12.007 10.555  22.400  1.00 205.90 ? 533  ASN A CG  1 
ATOM   4095  O  OD1 . ASN A 1 533  ? -13.149 10.545  22.859  1.00 210.19 ? 533  ASN A OD1 1 
ATOM   4096  N  ND2 . ASN A 1 533  ? -11.524 9.574   21.634  1.00 205.07 ? 533  ASN A ND2 1 
ATOM   4097  N  N   . MET A 1 534  ? -8.198  12.840  24.279  1.00 156.88 ? 534  MET A N   1 
ATOM   4098  C  CA  . MET A 1 534  ? -7.260  13.937  24.228  1.00 152.35 ? 534  MET A CA  1 
ATOM   4099  C  C   . MET A 1 534  ? -5.940  13.378  24.667  1.00 146.90 ? 534  MET A C   1 
ATOM   4100  O  O   . MET A 1 534  ? -4.974  14.098  24.897  1.00 144.19 ? 534  MET A O   1 
ATOM   4101  C  CB  . MET A 1 534  ? -7.738  15.006  25.163  1.00 152.68 ? 534  MET A CB  1 
ATOM   4102  C  CG  . MET A 1 534  ? -9.232  15.048  25.180  1.00 155.49 ? 534  MET A CG  1 
ATOM   4103  S  SD  . MET A 1 534  ? -9.878  15.766  26.686  1.00 153.00 ? 534  MET A SD  1 
ATOM   4104  C  CE  . MET A 1 534  ? -9.169  17.417  26.592  1.00 139.00 ? 534  MET A CE  1 
ATOM   4105  N  N   . VAL A 1 535  ? -5.918  12.056  24.742  1.00 160.57 ? 535  VAL A N   1 
ATOM   4106  C  CA  . VAL A 1 535  ? -4.820  11.322  25.343  1.00 157.38 ? 535  VAL A CA  1 
ATOM   4107  C  C   . VAL A 1 535  ? -3.451  12.004  25.279  1.00 155.23 ? 535  VAL A C   1 
ATOM   4108  O  O   . VAL A 1 535  ? -2.817  12.227  26.297  1.00 155.19 ? 535  VAL A O   1 
ATOM   4109  C  CB  . VAL A 1 535  ? -4.735  9.871   24.796  1.00 157.37 ? 535  VAL A CB  1 
ATOM   4110  C  CG1 . VAL A 1 535  ? -5.466  8.910   25.724  1.00 158.58 ? 535  VAL A CG1 1 
ATOM   4111  C  CG2 . VAL A 1 535  ? -5.298  9.791   23.378  1.00 163.03 ? 535  VAL A CG2 1 
ATOM   4112  N  N   . PRO A 1 536  ? -2.978  12.341  24.095  1.00 134.72 ? 536  PRO A N   1 
ATOM   4113  C  CA  . PRO A 1 536  ? -1.567  12.689  24.257  1.00 130.27 ? 536  PRO A CA  1 
ATOM   4114  C  C   . PRO A 1 536  ? -1.374  14.126  24.706  1.00 126.65 ? 536  PRO A C   1 
ATOM   4115  O  O   . PRO A 1 536  ? -0.625  14.397  25.636  1.00 125.45 ? 536  PRO A O   1 
ATOM   4116  C  CB  . PRO A 1 536  ? -0.991  12.460  22.859  1.00 133.21 ? 536  PRO A CB  1 
ATOM   4117  C  CG  . PRO A 1 536  ? -1.987  11.509  22.189  1.00 136.85 ? 536  PRO A CG  1 
ATOM   4118  C  CD  . PRO A 1 536  ? -3.312  11.976  22.717  1.00 137.95 ? 536  PRO A CD  1 
ATOM   4119  N  N   . SER A 1 537  ? -2.042  15.048  24.041  1.00 139.15 ? 537  SER A N   1 
ATOM   4120  C  CA  . SER A 1 537  ? -2.042  16.426  24.485  1.00 137.36 ? 537  SER A CA  1 
ATOM   4121  C  C   . SER A 1 537  ? -3.386  16.983  24.069  1.00 141.67 ? 537  SER A C   1 
ATOM   4122  O  O   . SER A 1 537  ? -4.334  16.219  23.866  1.00 144.39 ? 537  SER A O   1 
ATOM   4123  C  CB  . SER A 1 537  ? -0.875  17.226  23.904  1.00 132.96 ? 537  SER A CB  1 
ATOM   4124  O  OG  . SER A 1 537  ? -1.100  17.581  22.559  1.00 133.42 ? 537  SER A OG  1 
ATOM   4125  N  N   . SER A 1 538  ? -3.476  18.302  23.964  1.00 145.30 ? 538  SER A N   1 
ATOM   4126  C  CA  . SER A 1 538  ? -4.726  18.959  23.610  1.00 143.12 ? 538  SER A CA  1 
ATOM   4127  C  C   . SER A 1 538  ? -4.543  20.460  23.752  1.00 143.89 ? 538  SER A C   1 
ATOM   4128  O  O   . SER A 1 538  ? -3.741  20.926  24.563  1.00 142.34 ? 538  SER A O   1 
ATOM   4129  C  CB  . SER A 1 538  ? -5.891  18.489  24.505  1.00 142.84 ? 538  SER A CB  1 
ATOM   4130  O  OG  . SER A 1 538  ? -6.413  17.224  24.125  1.00 139.29 ? 538  SER A OG  1 
ATOM   4131  N  N   . ARG A 1 539  ? -5.256  21.216  22.929  1.00 122.50 ? 539  ARG A N   1 
ATOM   4132  C  CA  . ARG A 1 539  ? -5.482  22.612  23.235  1.00 123.11 ? 539  ARG A CA  1 
ATOM   4133  C  C   . ARG A 1 539  ? -6.965  22.869  23.144  1.00 124.55 ? 539  ARG A C   1 
ATOM   4134  O  O   . ARG A 1 539  ? -7.731  22.079  22.584  1.00 125.92 ? 539  ARG A O   1 
ATOM   4135  C  CB  . ARG A 1 539  ? -4.716  23.582  22.324  1.00 124.73 ? 539  ARG A CB  1 
ATOM   4136  C  CG  . ARG A 1 539  ? -3.897  22.971  21.193  1.00 125.63 ? 539  ARG A CG  1 
ATOM   4137  C  CD  . ARG A 1 539  ? -3.324  24.059  20.256  1.00 127.63 ? 539  ARG A CD  1 
ATOM   4138  N  NE  . ARG A 1 539  ? -2.252  24.861  20.849  1.00 126.50 ? 539  ARG A NE  1 
ATOM   4139  C  CZ  . ARG A 1 539  ? -0.956  24.553  20.778  1.00 125.61 ? 539  ARG A CZ  1 
ATOM   4140  N  NH1 . ARG A 1 539  ? -0.544  23.456  20.148  1.00 125.70 ? 539  ARG A NH1 1 
ATOM   4141  N  NH2 . ARG A 1 539  ? -0.062  25.340  21.351  1.00 124.65 ? 539  ARG A NH2 1 
ATOM   4142  N  N   . LEU A 1 540  ? -7.363  23.970  23.749  1.00 124.68 ? 540  LEU A N   1 
ATOM   4143  C  CA  . LEU A 1 540  ? -8.707  24.455  23.607  1.00 126.36 ? 540  LEU A CA  1 
ATOM   4144  C  C   . LEU A 1 540  ? -8.638  25.958  23.582  1.00 127.51 ? 540  LEU A C   1 
ATOM   4145  O  O   . LEU A 1 540  ? -7.635  26.561  23.977  1.00 126.64 ? 540  LEU A O   1 
ATOM   4146  C  CB  . LEU A 1 540  ? -9.607  23.988  24.749  1.00 127.26 ? 540  LEU A CB  1 
ATOM   4147  C  CG  . LEU A 1 540  ? -9.463  24.468  26.204  1.00 130.37 ? 540  LEU A CG  1 
ATOM   4148  C  CD1 . LEU A 1 540  ? -8.814  25.835  26.416  1.00 133.30 ? 540  LEU A CD1 1 
ATOM   4149  C  CD2 . LEU A 1 540  ? -10.842 24.448  26.820  1.00 133.20 ? 540  LEU A CD2 1 
ATOM   4150  N  N   . LEU A 1 541  ? -9.731  26.553  23.135  1.00 154.12 ? 541  LEU A N   1 
ATOM   4151  C  CA  . LEU A 1 541  ? -9.821  27.979  22.973  1.00 157.48 ? 541  LEU A CA  1 
ATOM   4152  C  C   . LEU A 1 541  ? -11.275 28.318  23.165  1.00 165.58 ? 541  LEU A C   1 
ATOM   4153  O  O   . LEU A 1 541  ? -12.143 27.442  23.131  1.00 166.28 ? 541  LEU A O   1 
ATOM   4154  C  CB  . LEU A 1 541  ? -9.334  28.355  21.588  1.00 156.53 ? 541  LEU A CB  1 
ATOM   4155  C  CG  . LEU A 1 541  ? -10.006 29.448  20.771  1.00 164.14 ? 541  LEU A CG  1 
ATOM   4156  C  CD1 . LEU A 1 541  ? -9.038  29.931  19.677  1.00 161.15 ? 541  LEU A CD1 1 
ATOM   4157  C  CD2 . LEU A 1 541  ? -11.310 28.924  20.176  1.00 167.06 ? 541  LEU A CD2 1 
ATOM   4158  N  N   . VAL A 1 542  ? -11.553 29.588  23.376  1.00 133.52 ? 542  VAL A N   1 
ATOM   4159  C  CA  . VAL A 1 542  ? -12.845 29.931  23.899  1.00 134.98 ? 542  VAL A CA  1 
ATOM   4160  C  C   . VAL A 1 542  ? -13.180 31.353  23.551  1.00 144.45 ? 542  VAL A C   1 
ATOM   4161  O  O   . VAL A 1 542  ? -12.542 32.284  24.034  1.00 143.88 ? 542  VAL A O   1 
ATOM   4162  C  CB  . VAL A 1 542  ? -12.828 29.775  25.403  1.00 131.77 ? 542  VAL A CB  1 
ATOM   4163  C  CG1 . VAL A 1 542  ? -13.899 30.622  26.009  1.00 134.47 ? 542  VAL A CG1 1 
ATOM   4164  C  CG2 . VAL A 1 542  ? -12.980 28.312  25.773  1.00 130.06 ? 542  VAL A CG2 1 
ATOM   4165  N  N   . TYR A 1 543  ? -14.188 31.512  22.704  1.00 167.20 ? 543  TYR A N   1 
ATOM   4166  C  CA  . TYR A 1 543  ? -14.551 32.819  22.190  1.00 175.37 ? 543  TYR A CA  1 
ATOM   4167  C  C   . TYR A 1 543  ? -15.959 33.217  22.593  1.00 180.99 ? 543  TYR A C   1 
ATOM   4168  O  O   . TYR A 1 543  ? -16.867 32.388  22.608  1.00 181.90 ? 543  TYR A O   1 
ATOM   4169  C  CB  . TYR A 1 543  ? -14.416 32.843  20.668  1.00 179.20 ? 543  TYR A CB  1 
ATOM   4170  C  CG  . TYR A 1 543  ? -15.312 31.858  19.921  1.00 182.70 ? 543  TYR A CG  1 
ATOM   4171  C  CD1 . TYR A 1 543  ? -14.887 30.557  19.659  1.00 180.86 ? 543  TYR A CD1 1 
ATOM   4172  C  CD2 . TYR A 1 543  ? -16.568 32.241  19.444  1.00 188.05 ? 543  TYR A CD2 1 
ATOM   4173  C  CE1 . TYR A 1 543  ? -15.692 29.663  18.963  1.00 182.66 ? 543  TYR A CE1 1 
ATOM   4174  C  CE2 . TYR A 1 543  ? -17.378 31.351  18.749  1.00 189.68 ? 543  TYR A CE2 1 
ATOM   4175  C  CZ  . TYR A 1 543  ? -16.933 30.066  18.516  1.00 185.94 ? 543  TYR A CZ  1 
ATOM   4176  O  OH  . TYR A 1 543  ? -17.727 29.177  17.839  1.00 185.45 ? 543  TYR A OH  1 
ATOM   4177  N  N   . TYR A 1 544  ? -16.122 34.489  22.942  1.00 198.44 ? 544  TYR A N   1 
ATOM   4178  C  CA  . TYR A 1 544  ? -17.442 35.084  23.116  1.00 204.45 ? 544  TYR A CA  1 
ATOM   4179  C  C   . TYR A 1 544  ? -17.635 36.111  22.000  1.00 208.93 ? 544  TYR A C   1 
ATOM   4180  O  O   . TYR A 1 544  ? -16.737 36.918  21.736  1.00 208.74 ? 544  TYR A O   1 
ATOM   4181  C  CB  . TYR A 1 544  ? -17.568 35.750  24.488  1.00 205.17 ? 544  TYR A CB  1 
ATOM   4182  C  CG  . TYR A 1 544  ? -16.585 36.875  24.696  1.00 204.77 ? 544  TYR A CG  1 
ATOM   4183  C  CD1 . TYR A 1 544  ? -15.235 36.689  24.450  1.00 200.33 ? 544  TYR A CD1 1 
ATOM   4184  C  CD2 . TYR A 1 544  ? -17.000 38.121  25.139  1.00 207.49 ? 544  TYR A CD2 1 
ATOM   4185  C  CE1 . TYR A 1 544  ? -14.332 37.700  24.638  1.00 200.02 ? 544  TYR A CE1 1 
ATOM   4186  C  CE2 . TYR A 1 544  ? -16.093 39.147  25.332  1.00 206.72 ? 544  TYR A CE2 1 
ATOM   4187  C  CZ  . TYR A 1 544  ? -14.760 38.926  25.076  1.00 203.35 ? 544  TYR A CZ  1 
ATOM   4188  O  OH  . TYR A 1 544  ? -13.843 39.927  25.263  1.00 203.32 ? 544  TYR A OH  1 
ATOM   4189  N  N   . ILE A 1 545  ? -18.794 36.051  21.336  1.00 168.25 ? 545  ILE A N   1 
ATOM   4190  C  CA  . ILE A 1 545  ? -19.127 36.944  20.222  1.00 171.86 ? 545  ILE A CA  1 
ATOM   4191  C  C   . ILE A 1 545  ? -19.619 38.312  20.745  1.00 176.73 ? 545  ILE A C   1 
ATOM   4192  O  O   . ILE A 1 545  ? -20.710 38.418  21.316  1.00 177.51 ? 545  ILE A O   1 
ATOM   4193  C  CB  . ILE A 1 545  ? -20.159 36.280  19.252  1.00 170.71 ? 545  ILE A CB  1 
ATOM   4194  C  CG1 . ILE A 1 545  ? -19.867 34.780  19.084  1.00 164.20 ? 545  ILE A CG1 1 
ATOM   4195  C  CG2 . ILE A 1 545  ? -20.137 36.962  17.904  1.00 176.85 ? 545  ILE A CG2 1 
ATOM   4196  C  CD1 . ILE A 1 545  ? -20.987 33.971  18.446  1.00 156.27 ? 545  ILE A CD1 1 
ATOM   4197  N  N   . VAL A 1 546  ? -18.782 39.339  20.555  1.00 204.81 ? 546  VAL A N   1 
ATOM   4198  C  CA  . VAL A 1 546  ? -19.021 40.708  21.036  1.00 213.75 ? 546  VAL A CA  1 
ATOM   4199  C  C   . VAL A 1 546  ? -19.640 41.620  19.976  1.00 230.98 ? 546  VAL A C   1 
ATOM   4200  O  O   . VAL A 1 546  ? -19.040 41.882  18.929  1.00 232.94 ? 546  VAL A O   1 
ATOM   4201  C  CB  . VAL A 1 546  ? -17.705 41.384  21.530  1.00 204.88 ? 546  VAL A CB  1 
ATOM   4202  C  CG1 . VAL A 1 546  ? -17.817 42.910  21.483  1.00 207.82 ? 546  VAL A CG1 1 
ATOM   4203  C  CG2 . VAL A 1 546  ? -17.341 40.912  22.922  1.00 199.31 ? 546  VAL A CG2 1 
ATOM   4204  N  N   . THR A 1 547  ? -20.842 42.107  20.266  1.00 211.03 ? 547  THR A N   1 
ATOM   4205  C  CA  . THR A 1 547  ? -21.538 43.046  19.398  1.00 230.64 ? 547  THR A CA  1 
ATOM   4206  C  C   . THR A 1 547  ? -21.164 44.492  19.736  1.00 247.60 ? 547  THR A C   1 
ATOM   4207  O  O   . THR A 1 547  ? -21.936 45.212  20.372  1.00 252.44 ? 547  THR A O   1 
ATOM   4208  C  CB  . THR A 1 547  ? -23.075 42.870  19.511  1.00 234.58 ? 547  THR A CB  1 
ATOM   4209  O  OG1 . THR A 1 547  ? -23.434 41.539  19.125  1.00 231.38 ? 547  THR A OG1 1 
ATOM   4210  C  CG2 . THR A 1 547  ? -23.810 43.858  18.621  1.00 242.25 ? 547  THR A CG2 1 
ATOM   4211  N  N   . GLY A 1 548  ? -19.971 44.912  19.328  1.00 327.59 ? 548  GLY A N   1 
ATOM   4212  C  CA  . GLY A 1 548  ? -19.632 46.321  19.379  1.00 344.80 ? 548  GLY A CA  1 
ATOM   4213  C  C   . GLY A 1 548  ? -20.623 47.033  18.479  1.00 367.61 ? 548  GLY A C   1 
ATOM   4214  O  O   . GLY A 1 548  ? -21.066 46.462  17.482  1.00 371.93 ? 548  GLY A O   1 
ATOM   4215  N  N   . GLU A 1 549  ? -20.987 48.266  18.820  1.00 360.50 ? 549  GLU A N   1 
ATOM   4216  C  CA  . GLU A 1 549  ? -21.990 48.983  18.035  1.00 378.41 ? 549  GLU A CA  1 
ATOM   4217  C  C   . GLU A 1 549  ? -21.550 49.139  16.585  1.00 382.15 ? 549  GLU A C   1 
ATOM   4218  O  O   . GLU A 1 549  ? -22.381 49.270  15.687  1.00 386.25 ? 549  GLU A O   1 
ATOM   4219  C  CB  . GLU A 1 549  ? -22.315 50.354  18.641  1.00 390.75 ? 549  GLU A CB  1 
ATOM   4220  C  CG  . GLU A 1 549  ? -21.191 51.371  18.554  1.00 395.43 ? 549  GLU A CG  1 
ATOM   4221  C  CD  . GLU A 1 549  ? -20.128 51.147  19.606  1.00 396.24 ? 549  GLU A CD  1 
ATOM   4222  O  OE1 . GLU A 1 549  ? -20.355 50.317  20.510  1.00 394.98 ? 549  GLU A OE1 1 
ATOM   4223  O  OE2 . GLU A 1 549  ? -19.069 51.803  19.532  1.00 396.93 ? 549  GLU A OE2 1 
ATOM   4224  N  N   . GLN A 1 550  ? -20.239 49.113  16.361  1.00 362.63 ? 550  GLN A N   1 
ATOM   4225  C  CA  . GLN A 1 550  ? -19.693 49.305  15.020  1.00 362.48 ? 550  GLN A CA  1 
ATOM   4226  C  C   . GLN A 1 550  ? -19.644 48.026  14.184  1.00 351.96 ? 550  GLN A C   1 
ATOM   4227  O  O   . GLN A 1 550  ? -19.944 48.055  12.993  1.00 357.98 ? 550  GLN A O   1 
ATOM   4228  C  CB  . GLN A 1 550  ? -18.305 49.957  15.069  1.00 363.99 ? 550  GLN A CB  1 
ATOM   4229  C  CG  . GLN A 1 550  ? -17.208 49.100  15.677  1.00 357.92 ? 550  GLN A CG  1 
ATOM   4230  C  CD  . GLN A 1 550  ? -17.129 49.246  17.178  1.00 354.98 ? 550  GLN A CD  1 
ATOM   4231  O  OE1 . GLN A 1 550  ? -17.799 50.094  17.765  1.00 359.06 ? 550  GLN A OE1 1 
ATOM   4232  N  NE2 . GLN A 1 550  ? -16.304 48.420  17.811  1.00 347.46 ? 550  GLN A NE2 1 
ATOM   4233  N  N   . THR A 1 551  ? -19.276 46.908  14.802  1.00 351.36 ? 551  THR A N   1 
ATOM   4234  C  CA  . THR A 1 551  ? -19.064 45.676  14.048  1.00 339.35 ? 551  THR A CA  1 
ATOM   4235  C  C   . THR A 1 551  ? -19.046 44.429  14.923  1.00 320.55 ? 551  THR A C   1 
ATOM   4236  O  O   . THR A 1 551  ? -18.606 44.470  16.072  1.00 315.52 ? 551  THR A O   1 
ATOM   4237  C  CB  . THR A 1 551  ? -17.735 45.732  13.278  1.00 339.63 ? 551  THR A CB  1 
ATOM   4238  O  OG1 . THR A 1 551  ? -17.755 46.832  12.360  1.00 348.33 ? 551  THR A OG1 1 
ATOM   4239  C  CG2 . THR A 1 551  ? -17.502 44.435  12.515  1.00 336.92 ? 551  THR A CG2 1 
ATOM   4240  N  N   . ALA A 1 552  ? -19.524 43.320  14.363  1.00 349.16 ? 552  ALA A N   1 
ATOM   4241  C  CA  . ALA A 1 552  ? -19.498 42.035  15.048  1.00 331.28 ? 552  ALA A CA  1 
ATOM   4242  C  C   . ALA A 1 552  ? -18.056 41.640  15.354  1.00 312.52 ? 552  ALA A C   1 
ATOM   4243  O  O   . ALA A 1 552  ? -17.288 41.352  14.434  1.00 310.83 ? 552  ALA A O   1 
ATOM   4244  C  CB  . ALA A 1 552  ? -20.171 40.971  14.185  1.00 332.34 ? 552  ALA A CB  1 
ATOM   4245  N  N   . GLU A 1 553  ? -17.687 41.627  16.638  1.00 237.69 ? 553  GLU A N   1 
ATOM   4246  C  CA  . GLU A 1 553  ? -16.315 41.294  17.026  1.00 219.98 ? 553  GLU A CA  1 
ATOM   4247  C  C   . GLU A 1 553  ? -16.179 39.961  17.762  1.00 206.47 ? 553  GLU A C   1 
ATOM   4248  O  O   . GLU A 1 553  ? -16.742 39.768  18.834  1.00 203.20 ? 553  GLU A O   1 
ATOM   4249  C  CB  . GLU A 1 553  ? -15.670 42.414  17.852  1.00 213.99 ? 553  GLU A CB  1 
ATOM   4250  C  CG  . GLU A 1 553  ? -14.184 42.577  17.556  1.00 208.83 ? 553  GLU A CG  1 
ATOM   4251  C  CD  . GLU A 1 553  ? -13.355 42.909  18.775  1.00 202.28 ? 553  GLU A CD  1 
ATOM   4252  O  OE1 . GLU A 1 553  ? -13.457 42.176  19.772  1.00 198.24 ? 553  GLU A OE1 1 
ATOM   4253  O  OE2 . GLU A 1 553  ? -12.585 43.893  18.728  1.00 201.78 ? 553  GLU A OE2 1 
ATOM   4254  N  N   . LEU A 1 554  ? -15.436 39.036  17.166  1.00 186.77 ? 554  LEU A N   1 
ATOM   4255  C  CA  . LEU A 1 554  ? -15.085 37.804  17.856  1.00 177.81 ? 554  LEU A CA  1 
ATOM   4256  C  C   . LEU A 1 554  ? -13.878 38.097  18.743  1.00 171.36 ? 554  LEU A C   1 
ATOM   4257  O  O   . LEU A 1 554  ? -13.039 38.942  18.418  1.00 172.25 ? 554  LEU A O   1 
ATOM   4258  C  CB  . LEU A 1 554  ? -14.788 36.645  16.876  1.00 176.52 ? 554  LEU A CB  1 
ATOM   4259  C  CG  . LEU A 1 554  ? -15.842 35.562  16.552  1.00 179.53 ? 554  LEU A CG  1 
ATOM   4260  C  CD1 . LEU A 1 554  ? -15.231 34.302  15.922  1.00 175.88 ? 554  LEU A CD1 1 
ATOM   4261  C  CD2 . LEU A 1 554  ? -16.661 35.183  17.782  1.00 179.84 ? 554  LEU A CD2 1 
ATOM   4262  N  N   . VAL A 1 555  ? -13.806 37.396  19.871  1.00 230.58 ? 555  VAL A N   1 
ATOM   4263  C  CA  . VAL A 1 555  ? -12.682 37.515  20.789  1.00 224.27 ? 555  VAL A CA  1 
ATOM   4264  C  C   . VAL A 1 555  ? -12.433 36.191  21.502  1.00 214.51 ? 555  VAL A C   1 
ATOM   4265  O  O   . VAL A 1 555  ? -13.382 35.507  21.890  1.00 213.30 ? 555  VAL A O   1 
ATOM   4266  C  CB  . VAL A 1 555  ? -12.923 38.619  21.834  1.00 227.66 ? 555  VAL A CB  1 
ATOM   4267  C  CG1 . VAL A 1 555  ? -11.966 38.468  22.992  1.00 224.09 ? 555  VAL A CG1 1 
ATOM   4268  C  CG2 . VAL A 1 555  ? -12.764 39.986  21.207  1.00 232.00 ? 555  VAL A CG2 1 
ATOM   4269  N  N   . SER A 1 556  ? -11.162 35.830  21.676  1.00 144.02 ? 556  SER A N   1 
ATOM   4270  C  CA  . SER A 1 556  ? -10.844 34.604  22.403  1.00 139.22 ? 556  SER A CA  1 
ATOM   4271  C  C   . SER A 1 556  ? -9.430  34.443  22.994  1.00 147.04 ? 556  SER A C   1 
ATOM   4272  O  O   . SER A 1 556  ? -8.558  35.324  22.914  1.00 138.78 ? 556  SER A O   1 
ATOM   4273  C  CB  . SER A 1 556  ? -11.211 33.376  21.559  1.00 148.02 ? 556  SER A CB  1 
ATOM   4274  O  OG  . SER A 1 556  ? -10.197 32.399  21.617  1.00 144.63 ? 556  SER A OG  1 
ATOM   4275  N  N   . ASP A 1 557  ? -9.261  33.294  23.636  1.00 191.61 ? 557  ASP A N   1 
ATOM   4276  C  CA  . ASP A 1 557  ? -7.968  32.825  24.080  1.00 181.39 ? 557  ASP A CA  1 
ATOM   4277  C  C   . ASP A 1 557  ? -8.017  31.307  24.168  1.00 173.82 ? 557  ASP A C   1 
ATOM   4278  O  O   . ASP A 1 557  ? -9.052  30.682  23.926  1.00 172.28 ? 557  ASP A O   1 
ATOM   4279  C  CB  . ASP A 1 557  ? -7.564  33.447  25.417  1.00 181.36 ? 557  ASP A CB  1 
ATOM   4280  C  CG  . ASP A 1 557  ? -6.130  33.116  25.808  1.00 178.97 ? 557  ASP A CG  1 
ATOM   4281  O  OD1 . ASP A 1 557  ? -5.306  32.940  24.894  1.00 179.88 ? 557  ASP A OD1 1 
ATOM   4282  O  OD2 . ASP A 1 557  ? -5.832  33.037  27.025  1.00 175.76 ? 557  ASP A OD2 1 
ATOM   4283  N  N   . SER A 1 558  ? -6.890  30.715  24.522  1.00 152.91 ? 558  SER A N   1 
ATOM   4284  C  CA  . SER A 1 558  ? -6.747  29.285  24.420  1.00 150.84 ? 558  SER A CA  1 
ATOM   4285  C  C   . SER A 1 558  ? -5.542  28.856  25.206  1.00 146.40 ? 558  SER A C   1 
ATOM   4286  O  O   . SER A 1 558  ? -4.677  29.672  25.523  1.00 144.52 ? 558  SER A O   1 
ATOM   4287  C  CB  . SER A 1 558  ? -6.473  28.933  22.978  1.00 152.48 ? 558  SER A CB  1 
ATOM   4288  O  OG  . SER A 1 558  ? -5.199  29.432  22.605  1.00 152.29 ? 558  SER A OG  1 
ATOM   4289  N  N   . VAL A 1 559  ? -5.455  27.565  25.488  1.00 185.01 ? 559  VAL A N   1 
ATOM   4290  C  CA  . VAL A 1 559  ? -4.292  27.067  26.194  1.00 179.76 ? 559  VAL A CA  1 
ATOM   4291  C  C   . VAL A 1 559  ? -3.818  25.749  25.646  1.00 180.03 ? 559  VAL A C   1 
ATOM   4292  O  O   . VAL A 1 559  ? -4.563  25.021  24.986  1.00 184.52 ? 559  VAL A O   1 
ATOM   4293  C  CB  . VAL A 1 559  ? -4.588  26.885  27.678  1.00 172.93 ? 559  VAL A CB  1 
ATOM   4294  C  CG1 . VAL A 1 559  ? -4.585  28.237  28.385  1.00 170.15 ? 559  VAL A CG1 1 
ATOM   4295  C  CG2 . VAL A 1 559  ? -5.912  26.181  27.840  1.00 169.14 ? 559  VAL A CG2 1 
ATOM   4296  N  N   . TRP A 1 560  ? -2.557  25.446  25.911  1.00 187.75 ? 560  TRP A N   1 
ATOM   4297  C  CA  . TRP A 1 560  ? -2.047  24.129  25.591  1.00 185.19 ? 560  TRP A CA  1 
ATOM   4298  C  C   . TRP A 1 560  ? -2.152  23.264  26.840  1.00 179.45 ? 560  TRP A C   1 
ATOM   4299  O  O   . TRP A 1 560  ? -1.935  23.751  27.956  1.00 179.23 ? 560  TRP A O   1 
ATOM   4300  C  CB  . TRP A 1 560  ? -0.616  24.207  25.054  1.00 189.89 ? 560  TRP A CB  1 
ATOM   4301  C  CG  . TRP A 1 560  ? -0.136  22.876  24.627  1.00 194.07 ? 560  TRP A CG  1 
ATOM   4302  C  CD1 . TRP A 1 560  ? -0.307  22.286  23.413  1.00 198.60 ? 560  TRP A CD1 1 
ATOM   4303  C  CD2 . TRP A 1 560  ? 0.566   21.943  25.428  1.00 193.80 ? 560  TRP A CD2 1 
ATOM   4304  N  NE1 . TRP A 1 560  ? 0.256   21.036  23.408  1.00 197.43 ? 560  TRP A NE1 1 
ATOM   4305  C  CE2 . TRP A 1 560  ? 0.799   20.801  24.639  1.00 193.95 ? 560  TRP A CE2 1 
ATOM   4306  C  CE3 . TRP A 1 560  ? 1.025   21.961  26.741  1.00 194.12 ? 560  TRP A CE3 1 
ATOM   4307  C  CZ2 . TRP A 1 560  ? 1.476   19.687  25.120  1.00 191.90 ? 560  TRP A CZ2 1 
ATOM   4308  C  CZ3 . TRP A 1 560  ? 1.704   20.858  27.219  1.00 192.72 ? 560  TRP A CZ3 1 
ATOM   4309  C  CH2 . TRP A 1 560  ? 1.926   19.735  26.409  1.00 190.82 ? 560  TRP A CH2 1 
ATOM   4310  N  N   . LEU A 1 561  ? -2.474  21.983  26.651  1.00 115.18 ? 561  LEU A N   1 
ATOM   4311  C  CA  . LEU A 1 561  ? -2.927  21.126  27.771  1.00 113.24 ? 561  LEU A CA  1 
ATOM   4312  C  C   . LEU A 1 561  ? -2.266  19.756  27.993  1.00 111.63 ? 561  LEU A C   1 
ATOM   4313  O  O   . LEU A 1 561  ? -2.952  18.727  27.855  1.00 111.69 ? 561  LEU A O   1 
ATOM   4314  C  CB  . LEU A 1 561  ? -4.397  20.796  27.608  1.00 114.30 ? 561  LEU A CB  1 
ATOM   4315  C  CG  . LEU A 1 561  ? -5.508  21.820  27.611  1.00 115.77 ? 561  LEU A CG  1 
ATOM   4316  C  CD1 . LEU A 1 561  ? -6.817  21.055  27.850  1.00 115.92 ? 561  LEU A CD1 1 
ATOM   4317  C  CD2 . LEU A 1 561  ? -5.268  22.890  28.675  1.00 114.73 ? 561  LEU A CD2 1 
ATOM   4318  N  N   . ASN A 1 562  ? -0.989  19.714  28.383  1.00 134.14 ? 562  ASN A N   1 
ATOM   4319  C  CA  . ASN A 1 562  ? -0.308  18.417  28.468  1.00 132.54 ? 562  ASN A CA  1 
ATOM   4320  C  C   . ASN A 1 562  ? -1.090  17.493  29.341  1.00 130.41 ? 562  ASN A C   1 
ATOM   4321  O  O   . ASN A 1 562  ? -1.698  17.926  30.301  1.00 131.71 ? 562  ASN A O   1 
ATOM   4322  C  CB  . ASN A 1 562  ? 1.120   18.499  29.004  1.00 126.87 ? 562  ASN A CB  1 
ATOM   4323  C  CG  . ASN A 1 562  ? 1.916   17.216  28.719  1.00 140.08 ? 562  ASN A CG  1 
ATOM   4324  O  OD1 . ASN A 1 562  ? 1.420   16.105  28.942  1.00 138.44 ? 562  ASN A OD1 1 
ATOM   4325  N  ND2 . ASN A 1 562  ? 3.144   17.369  28.213  1.00 139.06 ? 562  ASN A ND2 1 
ATOM   4326  N  N   . ILE A 1 563  ? -1.118  16.226  28.981  1.00 124.60 ? 563  ILE A N   1 
ATOM   4327  C  CA  . ILE A 1 563  ? -1.811  15.304  29.819  1.00 124.83 ? 563  ILE A CA  1 
ATOM   4328  C  C   . ILE A 1 563  ? -1.155  13.921  29.894  1.00 126.54 ? 563  ILE A C   1 
ATOM   4329  O  O   . ILE A 1 563  ? -0.160  13.651  29.207  1.00 126.16 ? 563  ILE A O   1 
ATOM   4330  C  CB  . ILE A 1 563  ? -3.292  15.249  29.461  1.00 125.31 ? 563  ILE A CB  1 
ATOM   4331  C  CG1 . ILE A 1 563  ? -3.649  13.923  28.843  1.00 125.64 ? 563  ILE A CG1 1 
ATOM   4332  C  CG2 . ILE A 1 563  ? -3.670  16.374  28.530  1.00 132.46 ? 563  ILE A CG2 1 
ATOM   4333  C  CD1 . ILE A 1 563  ? -5.118  13.788  28.603  1.00 129.18 ? 563  ILE A CD1 1 
ATOM   4334  N  N   . GLU A 1 564  ? -1.724  13.063  30.744  1.00 172.50 ? 564  GLU A N   1 
ATOM   4335  C  CA  . GLU A 1 564  ? -1.170  11.744  31.053  1.00 173.11 ? 564  GLU A CA  1 
ATOM   4336  C  C   . GLU A 1 564  ? -1.128  10.831  29.848  1.00 176.52 ? 564  GLU A C   1 
ATOM   4337  O  O   . GLU A 1 564  ? -2.131  10.636  29.169  1.00 179.48 ? 564  GLU A O   1 
ATOM   4338  C  CB  . GLU A 1 564  ? -1.964  11.056  32.171  1.00 175.22 ? 564  GLU A CB  1 
ATOM   4339  C  CG  . GLU A 1 564  ? -3.398  10.644  31.803  1.00 179.55 ? 564  GLU A CG  1 
ATOM   4340  C  CD  . GLU A 1 564  ? -3.872  9.430   32.597  1.00 183.42 ? 564  GLU A CD  1 
ATOM   4341  O  OE1 . GLU A 1 564  ? -5.096  9.220   32.706  1.00 186.55 ? 564  GLU A OE1 1 
ATOM   4342  O  OE2 . GLU A 1 564  ? -3.018  8.671   33.108  1.00 182.86 ? 564  GLU A OE2 1 
ATOM   4343  N  N   . GLU A 1 565  ? 0.034   10.250  29.595  1.00 131.10 ? 565  GLU A N   1 
ATOM   4344  C  CA  . GLU A 1 565  ? 0.188   9.408   28.426  1.00 136.30 ? 565  GLU A CA  1 
ATOM   4345  C  C   . GLU A 1 565  ? -0.425  8.031   28.647  1.00 135.76 ? 565  GLU A C   1 
ATOM   4346  O  O   . GLU A 1 565  ? 0.217   7.010   28.415  1.00 132.93 ? 565  GLU A O   1 
ATOM   4347  C  CB  . GLU A 1 565  ? 1.654   9.342   28.029  1.00 140.82 ? 565  GLU A CB  1 
ATOM   4348  C  CG  . GLU A 1 565  ? 2.221   10.735  27.852  1.00 146.21 ? 565  GLU A CG  1 
ATOM   4349  C  CD  . GLU A 1 565  ? 3.681   10.719  27.565  1.00 148.52 ? 565  GLU A CD  1 
ATOM   4350  O  OE1 . GLU A 1 565  ? 4.258   9.617   27.563  1.00 148.24 ? 565  GLU A OE1 1 
ATOM   4351  O  OE2 . GLU A 1 565  ? 4.250   11.803  27.341  1.00 149.48 ? 565  GLU A OE2 1 
ATOM   4352  N  N   . LYS A 1 566  ? -1.674  8.019   29.106  1.00 142.11 ? 566  LYS A N   1 
ATOM   4353  C  CA  . LYS A 1 566  ? -2.453  6.792   29.224  1.00 144.90 ? 566  LYS A CA  1 
ATOM   4354  C  C   . LYS A 1 566  ? -2.759  6.274   27.827  1.00 147.12 ? 566  LYS A C   1 
ATOM   4355  O  O   . LYS A 1 566  ? -3.384  6.973   27.034  1.00 147.25 ? 566  LYS A O   1 
ATOM   4356  C  CB  . LYS A 1 566  ? -3.756  7.074   29.982  1.00 146.80 ? 566  LYS A CB  1 
ATOM   4357  C  CG  . LYS A 1 566  ? -4.558  5.843   30.424  1.00 148.14 ? 566  LYS A CG  1 
ATOM   4358  C  CD  . LYS A 1 566  ? -5.565  6.233   31.519  1.00 151.46 ? 566  LYS A CD  1 
ATOM   4359  C  CE  . LYS A 1 566  ? -6.341  5.045   32.098  1.00 154.58 ? 566  LYS A CE  1 
ATOM   4360  N  NZ  . LYS A 1 566  ? -7.664  4.806   31.442  1.00 156.47 ? 566  LYS A NZ  1 
ATOM   4361  N  N   . CYS A 1 567  ? -2.304  5.058   27.528  1.00 190.80 ? 567  CYS A N   1 
ATOM   4362  C  CA  . CYS A 1 567  ? -2.522  4.436   26.217  1.00 193.11 ? 567  CYS A CA  1 
ATOM   4363  C  C   . CYS A 1 567  ? -3.971  3.989   26.037  1.00 195.49 ? 567  CYS A C   1 
ATOM   4364  O  O   . CYS A 1 567  ? -4.769  4.028   26.979  1.00 195.66 ? 567  CYS A O   1 
ATOM   4365  C  CB  . CYS A 1 567  ? -1.588  3.236   26.002  1.00 193.46 ? 567  CYS A CB  1 
ATOM   4366  S  SG  . CYS A 1 567  ? 0.181   3.608   25.808  1.00 256.36 ? 567  CYS A SG  1 
ATOM   4367  N  N   . GLY A 1 568  ? -4.304  3.567   24.820  1.00 185.54 ? 568  GLY A N   1 
ATOM   4368  C  CA  . GLY A 1 568  ? -5.639  3.089   24.527  1.00 188.02 ? 568  GLY A CA  1 
ATOM   4369  C  C   . GLY A 1 568  ? -5.792  1.698   25.083  1.00 187.90 ? 568  GLY A C   1 
ATOM   4370  O  O   . GLY A 1 568  ? -6.504  1.480   26.060  1.00 188.29 ? 568  GLY A O   1 
ATOM   4371  N  N   . ASN A 1 569  ? -5.113  0.748   24.461  1.00 207.78 ? 569  ASN A N   1 
ATOM   4372  C  CA  . ASN A 1 569  ? -5.092  -0.603  24.983  1.00 207.34 ? 569  ASN A CA  1 
ATOM   4373  C  C   . ASN A 1 569  ? -3.939  -0.805  25.960  1.00 203.54 ? 569  ASN A C   1 
ATOM   4374  O  O   . ASN A 1 569  ? -2.773  -0.692  25.582  1.00 204.30 ? 569  ASN A O   1 
ATOM   4375  C  CB  . ASN A 1 569  ? -5.018  -1.610  23.841  1.00 209.59 ? 569  ASN A CB  1 
ATOM   4376  C  CG  . ASN A 1 569  ? -6.376  -2.137  23.452  1.00 212.64 ? 569  ASN A CG  1 
ATOM   4377  O  OD1 . ASN A 1 569  ? -7.325  -2.065  24.234  1.00 213.31 ? 569  ASN A OD1 1 
ATOM   4378  N  ND2 . ASN A 1 569  ? -6.481  -2.675  22.243  1.00 213.99 ? 569  ASN A ND2 1 
ATOM   4379  N  N   . GLN A 1 570  ? -4.261  -1.083  27.221  1.00 283.03 ? 570  GLN A N   1 
ATOM   4380  C  CA  . GLN A 1 570  ? -3.229  -1.408  28.200  1.00 280.23 ? 570  GLN A CA  1 
ATOM   4381  C  C   . GLN A 1 570  ? -2.624  -2.754  27.839  1.00 284.03 ? 570  GLN A C   1 
ATOM   4382  O  O   . GLN A 1 570  ? -3.196  -3.806  28.130  1.00 284.48 ? 570  GLN A O   1 
ATOM   4383  C  CB  . GLN A 1 570  ? -3.793  -1.453  29.627  1.00 275.81 ? 570  GLN A CB  1 
ATOM   4384  C  CG  . GLN A 1 570  ? -3.219  -0.407  30.587  1.00 309.80 ? 570  GLN A CG  1 
ATOM   4385  C  CD  . GLN A 1 570  ? -4.106  0.816   30.712  1.00 308.93 ? 570  GLN A CD  1 
ATOM   4386  O  OE1 . GLN A 1 570  ? -4.744  1.234   29.747  1.00 308.96 ? 570  GLN A OE1 1 
ATOM   4387  N  NE2 . GLN A 1 570  ? -4.153  1.396   31.906  1.00 307.67 ? 570  GLN A NE2 1 
ATOM   4388  N  N   . LEU A 1 571  ? -1.476  -2.715  27.177  1.00 190.91 ? 571  LEU A N   1 
ATOM   4389  C  CA  . LEU A 1 571  ? -0.748  -3.932  26.882  1.00 191.74 ? 571  LEU A CA  1 
ATOM   4390  C  C   . LEU A 1 571  ? 0.344   -4.136  27.892  1.00 193.82 ? 571  LEU A C   1 
ATOM   4391  O  O   . LEU A 1 571  ? 1.256   -3.322  27.985  1.00 194.51 ? 571  LEU A O   1 
ATOM   4392  C  CB  . LEU A 1 571  ? -0.088  -3.851  25.517  1.00 185.05 ? 571  LEU A CB  1 
ATOM   4393  C  CG  . LEU A 1 571  ? 1.042   -4.880  25.370  1.00 177.73 ? 571  LEU A CG  1 
ATOM   4394  C  CD1 . LEU A 1 571  ? 0.657   -6.233  25.974  1.00 171.26 ? 571  LEU A CD1 1 
ATOM   4395  C  CD2 . LEU A 1 571  ? 1.472   -5.050  23.914  1.00 173.51 ? 571  LEU A CD2 1 
ATOM   4396  N  N   . GLN A 1 572  ? 0.284   -5.244  28.617  1.00 215.31 ? 572  GLN A N   1 
ATOM   4397  C  CA  . GLN A 1 572  ? 1.343   -5.572  29.552  1.00 216.27 ? 572  GLN A CA  1 
ATOM   4398  C  C   . GLN A 1 572  ? 1.842   -6.996  29.288  1.00 212.63 ? 572  GLN A C   1 
ATOM   4399  O  O   . GLN A 1 572  ? 1.075   -7.879  28.907  1.00 211.54 ? 572  GLN A O   1 
ATOM   4400  C  CB  . GLN A 1 572  ? 0.847   -5.377  30.997  1.00 226.13 ? 572  GLN A CB  1 
ATOM   4401  C  CG  . GLN A 1 572  ? 1.921   -5.439  32.095  1.00 235.27 ? 572  GLN A CG  1 
ATOM   4402  C  CD  . GLN A 1 572  ? 2.937   -4.303  32.033  1.00 242.96 ? 572  GLN A CD  1 
ATOM   4403  O  OE1 . GLN A 1 572  ? 2.637   -3.203  31.564  1.00 245.57 ? 572  GLN A OE1 1 
ATOM   4404  N  NE2 . GLN A 1 572  ? 4.145   -4.567  32.524  1.00 245.83 ? 572  GLN A NE2 1 
ATOM   4405  N  N   . VAL A 1 573  ? 3.141   -7.193  29.469  1.00 174.25 ? 573  VAL A N   1 
ATOM   4406  C  CA  . VAL A 1 573  ? 3.776   -8.495  29.331  1.00 171.04 ? 573  VAL A CA  1 
ATOM   4407  C  C   . VAL A 1 573  ? 4.432   -8.966  30.638  1.00 172.00 ? 573  VAL A C   1 
ATOM   4408  O  O   . VAL A 1 573  ? 5.307   -8.280  31.182  1.00 172.15 ? 573  VAL A O   1 
ATOM   4409  C  CB  . VAL A 1 573  ? 4.879   -8.388  28.316  1.00 161.82 ? 573  VAL A CB  1 
ATOM   4410  C  CG1 . VAL A 1 573  ? 4.400   -8.911  27.013  1.00 160.57 ? 573  VAL A CG1 1 
ATOM   4411  C  CG2 . VAL A 1 573  ? 5.316   -6.929  28.206  1.00 157.17 ? 573  VAL A CG2 1 
ATOM   4412  N  N   . HIS A 1 574  ? 4.043   -10.137 31.139  1.00 208.07 ? 574  HIS A N   1 
ATOM   4413  C  CA  . HIS A 1 574  ? 4.637   -10.641 32.379  1.00 208.38 ? 574  HIS A CA  1 
ATOM   4414  C  C   . HIS A 1 574  ? 5.264   -12.018 32.213  1.00 212.90 ? 574  HIS A C   1 
ATOM   4415  O  O   . HIS A 1 574  ? 4.707   -12.896 31.560  1.00 212.78 ? 574  HIS A O   1 
ATOM   4416  C  CB  . HIS A 1 574  ? 3.615   -10.669 33.524  1.00 210.84 ? 574  HIS A CB  1 
ATOM   4417  C  CG  . HIS A 1 574  ? 3.243   -9.315  34.049  1.00 213.47 ? 574  HIS A CG  1 
ATOM   4418  N  ND1 . HIS A 1 574  ? 4.179   -8.359  34.383  1.00 213.25 ? 574  HIS A ND1 1 
ATOM   4419  C  CD2 . HIS A 1 574  ? 2.032   -8.768  34.323  1.00 215.12 ? 574  HIS A CD2 1 
ATOM   4420  C  CE1 . HIS A 1 574  ? 3.561   -7.276  34.819  1.00 213.33 ? 574  HIS A CE1 1 
ATOM   4421  N  NE2 . HIS A 1 574  ? 2.259   -7.498  34.796  1.00 214.70 ? 574  HIS A NE2 1 
ATOM   4422  N  N   . LEU A 1 575  ? 6.424   -12.194 32.830  1.00 166.08 ? 575  LEU A N   1 
ATOM   4423  C  CA  . LEU A 1 575  ? 7.144   -13.458 32.787  1.00 174.77 ? 575  LEU A CA  1 
ATOM   4424  C  C   . LEU A 1 575  ? 6.674   -14.455 33.838  1.00 185.92 ? 575  LEU A C   1 
ATOM   4425  O  O   . LEU A 1 575  ? 6.647   -14.125 35.018  1.00 189.28 ? 575  LEU A O   1 
ATOM   4426  C  CB  . LEU A 1 575  ? 8.616   -13.179 32.996  1.00 169.10 ? 575  LEU A CB  1 
ATOM   4427  C  CG  . LEU A 1 575  ? 9.150   -12.524 31.747  1.00 163.02 ? 575  LEU A CG  1 
ATOM   4428  C  CD1 . LEU A 1 575  ? 10.593  -12.194 31.939  1.00 159.95 ? 575  LEU A CD1 1 
ATOM   4429  C  CD2 . LEU A 1 575  ? 8.965   -13.520 30.635  1.00 164.23 ? 575  LEU A CD2 1 
ATOM   4430  N  N   . SER A 1 576  ? 6.352   -15.681 33.420  1.00 260.09 ? 576  SER A N   1 
ATOM   4431  C  CA  . SER A 1 576  ? 5.785   -16.691 34.326  1.00 268.55 ? 576  SER A CA  1 
ATOM   4432  C  C   . SER A 1 576  ? 6.561   -16.843 35.630  1.00 269.77 ? 576  SER A C   1 
ATOM   4433  O  O   . SER A 1 576  ? 6.006   -16.616 36.704  1.00 269.22 ? 576  SER A O   1 
ATOM   4434  C  CB  . SER A 1 576  ? 5.619   -18.046 33.633  1.00 275.25 ? 576  SER A CB  1 
ATOM   4435  O  OG  . SER A 1 576  ? 4.342   -18.154 33.041  1.00 279.78 ? 576  SER A OG  1 
ATOM   4436  N  N   . PRO A 1 577  ? 7.833   -17.263 35.549  1.00 196.84 ? 577  PRO A N   1 
ATOM   4437  C  CA  . PRO A 1 577  ? 8.703   -17.047 36.709  1.00 196.94 ? 577  PRO A CA  1 
ATOM   4438  C  C   . PRO A 1 577  ? 9.157   -15.579 36.813  1.00 194.30 ? 577  PRO A C   1 
ATOM   4439  O  O   . PRO A 1 577  ? 9.977   -15.156 36.006  1.00 195.20 ? 577  PRO A O   1 
ATOM   4440  C  CB  . PRO A 1 577  ? 9.904   -17.961 36.415  1.00 200.77 ? 577  PRO A CB  1 
ATOM   4441  C  CG  . PRO A 1 577  ? 9.372   -19.001 35.490  1.00 202.73 ? 577  PRO A CG  1 
ATOM   4442  C  CD  . PRO A 1 577  ? 8.390   -18.272 34.632  1.00 199.73 ? 577  PRO A CD  1 
ATOM   4443  N  N   . ASP A 1 578  ? 8.643   -14.826 37.788  1.00 217.57 ? 578  ASP A N   1 
ATOM   4444  C  CA  . ASP A 1 578  ? 8.960   -13.397 37.909  1.00 212.31 ? 578  ASP A CA  1 
ATOM   4445  C  C   . ASP A 1 578  ? 10.309  -13.128 38.566  1.00 208.52 ? 578  ASP A C   1 
ATOM   4446  O  O   . ASP A 1 578  ? 10.684  -11.976 38.805  1.00 204.33 ? 578  ASP A O   1 
ATOM   4447  C  CB  . ASP A 1 578  ? 7.860   -12.643 38.655  1.00 213.93 ? 578  ASP A CB  1 
ATOM   4448  C  CG  . ASP A 1 578  ? 7.773   -11.191 38.232  1.00 215.49 ? 578  ASP A CG  1 
ATOM   4449  O  OD1 . ASP A 1 578  ? 8.798   -10.647 37.765  1.00 215.09 ? 578  ASP A OD1 1 
ATOM   4450  O  OD2 . ASP A 1 578  ? 6.681   -10.595 38.348  1.00 216.63 ? 578  ASP A OD2 1 
ATOM   4451  N  N   . ALA A 1 579  ? 11.023  -14.208 38.860  1.00 216.24 ? 579  ALA A N   1 
ATOM   4452  C  CA  . ALA A 1 579  ? 12.391  -14.134 39.351  1.00 215.23 ? 579  ALA A CA  1 
ATOM   4453  C  C   . ALA A 1 579  ? 13.185  -13.174 38.486  1.00 209.46 ? 579  ALA A C   1 
ATOM   4454  O  O   . ALA A 1 579  ? 12.932  -13.056 37.288  1.00 210.73 ? 579  ALA A O   1 
ATOM   4455  C  CB  . ALA A 1 579  ? 13.033  -15.507 39.319  1.00 219.05 ? 579  ALA A CB  1 
ATOM   4456  N  N   . ASP A 1 580  ? 14.150  -12.497 39.098  1.00 214.02 ? 580  ASP A N   1 
ATOM   4457  C  CA  . ASP A 1 580  ? 14.936  -11.479 38.413  1.00 211.11 ? 580  ASP A CA  1 
ATOM   4458  C  C   . ASP A 1 580  ? 16.230  -12.052 37.839  1.00 209.49 ? 580  ASP A C   1 
ATOM   4459  O  O   . ASP A 1 580  ? 17.259  -11.377 37.785  1.00 208.29 ? 580  ASP A O   1 
ATOM   4460  C  CB  . ASP A 1 580  ? 15.228  -10.324 39.369  1.00 214.27 ? 580  ASP A CB  1 
ATOM   4461  C  CG  . ASP A 1 580  ? 15.826  -10.798 40.674  1.00 221.64 ? 580  ASP A CG  1 
ATOM   4462  O  OD1 . ASP A 1 580  ? 16.774  -11.612 40.622  1.00 225.31 ? 580  ASP A OD1 1 
ATOM   4463  O  OD2 . ASP A 1 580  ? 15.348  -10.364 41.745  1.00 223.79 ? 580  ASP A OD2 1 
ATOM   4464  N  N   . ALA A 1 581  ? 16.159  -13.307 37.415  1.00 212.45 ? 581  ALA A N   1 
ATOM   4465  C  CA  . ALA A 1 581  ? 17.289  -13.984 36.803  1.00 211.00 ? 581  ALA A CA  1 
ATOM   4466  C  C   . ALA A 1 581  ? 16.835  -15.370 36.365  1.00 211.30 ? 581  ALA A C   1 
ATOM   4467  O  O   . ALA A 1 581  ? 15.982  -15.968 37.021  1.00 211.95 ? 581  ALA A O   1 
ATOM   4468  C  CB  . ALA A 1 581  ? 18.429  -14.079 37.786  1.00 212.62 ? 581  ALA A CB  1 
ATOM   4469  N  N   . TYR A 1 582  ? 17.396  -15.884 35.268  1.00 178.17 ? 582  TYR A N   1 
ATOM   4470  C  CA  . TYR A 1 582  ? 16.939  -17.164 34.722  1.00 176.00 ? 582  TYR A CA  1 
ATOM   4471  C  C   . TYR A 1 582  ? 18.028  -18.192 34.462  1.00 173.48 ? 582  TYR A C   1 
ATOM   4472  O  O   . TYR A 1 582  ? 19.163  -17.851 34.145  1.00 173.63 ? 582  TYR A O   1 
ATOM   4473  C  CB  . TYR A 1 582  ? 16.141  -16.945 33.441  1.00 173.89 ? 582  TYR A CB  1 
ATOM   4474  C  CG  . TYR A 1 582  ? 14.840  -16.227 33.677  1.00 171.06 ? 582  TYR A CG  1 
ATOM   4475  C  CD1 . TYR A 1 582  ? 13.667  -16.937 33.907  1.00 172.25 ? 582  TYR A CD1 1 
ATOM   4476  C  CD2 . TYR A 1 582  ? 14.784  -14.839 33.689  1.00 167.51 ? 582  TYR A CD2 1 
ATOM   4477  C  CE1 . TYR A 1 582  ? 12.469  -16.281 34.134  1.00 171.09 ? 582  TYR A CE1 1 
ATOM   4478  C  CE2 . TYR A 1 582  ? 13.594  -14.175 33.913  1.00 166.19 ? 582  TYR A CE2 1 
ATOM   4479  C  CZ  . TYR A 1 582  ? 12.440  -14.899 34.136  1.00 168.13 ? 582  TYR A CZ  1 
ATOM   4480  O  OH  . TYR A 1 582  ? 11.252  -14.238 34.357  1.00 167.17 ? 582  TYR A OH  1 
ATOM   4481  N  N   . SER A 1 583  ? 17.653  -19.457 34.609  1.00 242.06 ? 583  SER A N   1 
ATOM   4482  C  CA  . SER A 1 583  ? 18.513  -20.577 34.267  1.00 242.04 ? 583  SER A CA  1 
ATOM   4483  C  C   . SER A 1 583  ? 18.546  -20.722 32.756  1.00 241.58 ? 583  SER A C   1 
ATOM   4484  O  O   . SER A 1 583  ? 17.501  -20.813 32.121  1.00 237.32 ? 583  SER A O   1 
ATOM   4485  C  CB  . SER A 1 583  ? 17.955  -21.849 34.885  1.00 249.28 ? 583  SER A CB  1 
ATOM   4486  O  OG  . SER A 1 583  ? 16.543  -21.853 34.771  1.00 251.40 ? 583  SER A OG  1 
ATOM   4487  N  N   . PRO A 1 584  ? 19.750  -20.771 32.178  1.00 164.91 ? 584  PRO A N   1 
ATOM   4488  C  CA  . PRO A 1 584  ? 19.934  -20.650 30.727  1.00 166.26 ? 584  PRO A CA  1 
ATOM   4489  C  C   . PRO A 1 584  ? 19.350  -21.843 29.988  1.00 165.01 ? 584  PRO A C   1 
ATOM   4490  O  O   . PRO A 1 584  ? 20.041  -22.842 29.849  1.00 167.85 ? 584  PRO A O   1 
ATOM   4491  C  CB  . PRO A 1 584  ? 21.461  -20.637 30.566  1.00 166.42 ? 584  PRO A CB  1 
ATOM   4492  C  CG  . PRO A 1 584  ? 22.018  -20.477 31.971  1.00 167.01 ? 584  PRO A CG  1 
ATOM   4493  C  CD  . PRO A 1 584  ? 21.006  -21.083 32.871  1.00 168.47 ? 584  PRO A CD  1 
ATOM   4494  N  N   . GLY A 1 585  ? 18.111  -21.743 29.519  1.00 225.13 ? 585  GLY A N   1 
ATOM   4495  C  CA  . GLY A 1 585  ? 17.465  -22.853 28.840  1.00 228.64 ? 585  GLY A CA  1 
ATOM   4496  C  C   . GLY A 1 585  ? 16.167  -23.263 29.507  1.00 229.62 ? 585  GLY A C   1 
ATOM   4497  O  O   . GLY A 1 585  ? 15.398  -24.058 28.969  1.00 231.76 ? 585  GLY A O   1 
ATOM   4498  N  N   . GLN A 1 586  ? 15.933  -22.721 30.696  1.00 202.86 ? 586  GLN A N   1 
ATOM   4499  C  CA  . GLN A 1 586  ? 14.692  -22.947 31.420  1.00 205.84 ? 586  GLN A CA  1 
ATOM   4500  C  C   . GLN A 1 586  ? 13.513  -22.670 30.509  1.00 208.04 ? 586  GLN A C   1 
ATOM   4501  O  O   . GLN A 1 586  ? 13.480  -21.666 29.805  1.00 205.88 ? 586  GLN A O   1 
ATOM   4502  C  CB  . GLN A 1 586  ? 14.621  -22.015 32.637  1.00 202.84 ? 586  GLN A CB  1 
ATOM   4503  C  CG  . GLN A 1 586  ? 13.308  -22.038 33.418  1.00 204.95 ? 586  GLN A CG  1 
ATOM   4504  C  CD  . GLN A 1 586  ? 13.291  -21.021 34.550  1.00 205.60 ? 586  GLN A CD  1 
ATOM   4505  O  OE1 . GLN A 1 586  ? 14.293  -20.359 34.820  1.00 204.49 ? 586  GLN A OE1 1 
ATOM   4506  N  NE2 . GLN A 1 586  ? 12.149  -20.893 35.215  1.00 207.24 ? 586  GLN A NE2 1 
ATOM   4507  N  N   . THR A 1 587  ? 12.549  -23.574 30.507  1.00 193.37 ? 587  THR A N   1 
ATOM   4508  C  CA  . THR A 1 587  ? 11.277  -23.277 29.882  1.00 198.57 ? 587  THR A CA  1 
ATOM   4509  C  C   . THR A 1 587  ? 10.547  -22.305 30.815  1.00 198.26 ? 587  THR A C   1 
ATOM   4510  O  O   . THR A 1 587  ? 10.531  -22.511 32.033  1.00 195.63 ? 587  THR A O   1 
ATOM   4511  C  CB  . THR A 1 587  ? 10.483  -24.559 29.674  1.00 205.38 ? 587  THR A CB  1 
ATOM   4512  O  OG1 . THR A 1 587  ? 10.553  -25.341 30.869  1.00 207.45 ? 587  THR A OG1 1 
ATOM   4513  C  CG2 . THR A 1 587  ? 11.093  -25.371 28.545  1.00 209.59 ? 587  THR A CG2 1 
ATOM   4514  N  N   . VAL A 1 588  ? 9.974   -21.240 30.251  1.00 184.81 ? 588  VAL A N   1 
ATOM   4515  C  CA  . VAL A 1 588  ? 9.306   -20.195 31.039  1.00 184.22 ? 588  VAL A CA  1 
ATOM   4516  C  C   . VAL A 1 588  ? 8.170   -19.533 30.278  1.00 183.63 ? 588  VAL A C   1 
ATOM   4517  O  O   . VAL A 1 588  ? 8.375   -18.983 29.203  1.00 185.48 ? 588  VAL A O   1 
ATOM   4518  C  CB  . VAL A 1 588  ? 10.272  -19.072 31.449  1.00 182.02 ? 588  VAL A CB  1 
ATOM   4519  C  CG1 . VAL A 1 588  ? 11.360  -18.922 30.423  1.00 180.92 ? 588  VAL A CG1 1 
ATOM   4520  C  CG2 . VAL A 1 588  ? 9.513   -17.760 31.600  1.00 179.65 ? 588  VAL A CG2 1 
ATOM   4521  N  N   . SER A 1 589  ? 6.978   -19.549 30.859  1.00 235.85 ? 589  SER A N   1 
ATOM   4522  C  CA  . SER A 1 589  ? 5.798   -19.039 30.174  1.00 236.33 ? 589  SER A CA  1 
ATOM   4523  C  C   . SER A 1 589  ? 5.720   -17.506 30.177  1.00 231.28 ? 589  SER A C   1 
ATOM   4524  O  O   . SER A 1 589  ? 6.059   -16.861 31.167  1.00 228.16 ? 589  SER A O   1 
ATOM   4525  C  CB  . SER A 1 589  ? 4.549   -19.666 30.789  1.00 241.82 ? 589  SER A CB  1 
ATOM   4526  O  OG  . SER A 1 589  ? 4.851   -20.955 31.299  1.00 246.86 ? 589  SER A OG  1 
ATOM   4527  N  N   . LEU A 1 590  ? 5.286   -16.930 29.059  1.00 180.04 ? 590  LEU A N   1 
ATOM   4528  C  CA  . LEU A 1 590  ? 5.152   -15.480 28.941  1.00 174.02 ? 590  LEU A CA  1 
ATOM   4529  C  C   . LEU A 1 590  ? 3.691   -15.070 28.777  1.00 172.61 ? 590  LEU A C   1 
ATOM   4530  O  O   . LEU A 1 590  ? 2.926   -15.740 28.085  1.00 177.08 ? 590  LEU A O   1 
ATOM   4531  C  CB  . LEU A 1 590  ? 5.971   -14.965 27.761  1.00 168.81 ? 590  LEU A CB  1 
ATOM   4532  C  CG  . LEU A 1 590  ? 5.501   -13.627 27.194  1.00 160.43 ? 590  LEU A CG  1 
ATOM   4533  C  CD1 . LEU A 1 590  ? 5.741   -12.500 28.182  1.00 155.51 ? 590  LEU A CD1 1 
ATOM   4534  C  CD2 . LEU A 1 590  ? 6.187   -13.342 25.875  1.00 157.62 ? 590  LEU A CD2 1 
ATOM   4535  N  N   . ASN A 1 591  ? 3.310   -13.961 29.405  1.00 204.84 ? 591  ASN A N   1 
ATOM   4536  C  CA  . ASN A 1 591  ? 1.916   -13.523 29.404  1.00 202.77 ? 591  ASN A CA  1 
ATOM   4537  C  C   . ASN A 1 591  ? 1.643   -12.235 28.638  1.00 199.84 ? 591  ASN A C   1 
ATOM   4538  O  O   . ASN A 1 591  ? 2.404   -11.271 28.724  1.00 197.72 ? 591  ASN A O   1 
ATOM   4539  C  CB  . ASN A 1 591  ? 1.399   -13.364 30.840  1.00 202.70 ? 591  ASN A CB  1 
ATOM   4540  C  CG  . ASN A 1 591  ? 1.032   -14.686 31.478  1.00 207.49 ? 591  ASN A CG  1 
ATOM   4541  O  OD1 . ASN A 1 591  ? -0.062  -15.219 31.260  1.00 210.54 ? 591  ASN A OD1 1 
ATOM   4542  N  ND2 . ASN A 1 591  ? 1.948   -15.226 32.274  1.00 208.33 ? 591  ASN A ND2 1 
ATOM   4543  N  N   . MET A 1 592  ? 0.542   -12.229 27.896  1.00 214.34 ? 592  MET A N   1 
ATOM   4544  C  CA  . MET A 1 592  ? 0.017   -11.000 27.321  1.00 210.91 ? 592  MET A CA  1 
ATOM   4545  C  C   . MET A 1 592  ? -1.292  -10.596 28.003  1.00 212.12 ? 592  MET A C   1 
ATOM   4546  O  O   . MET A 1 592  ? -1.942  -11.410 28.675  1.00 213.28 ? 592  MET A O   1 
ATOM   4547  C  CB  . MET A 1 592  ? -0.193  -11.131 25.808  1.00 211.53 ? 592  MET A CB  1 
ATOM   4548  C  CG  . MET A 1 592  ? 1.030   -10.793 24.968  1.00 209.42 ? 592  MET A CG  1 
ATOM   4549  S  SD  . MET A 1 592  ? 2.081   -12.225 24.684  1.00 231.12 ? 592  MET A SD  1 
ATOM   4550  C  CE  . MET A 1 592  ? 0.878   -13.325 23.944  1.00 221.79 ? 592  MET A CE  1 
ATOM   4551  N  N   . ALA A 1 593  ? -1.676  -9.334  27.824  1.00 173.41 ? 593  ALA A N   1 
ATOM   4552  C  CA  . ALA A 1 593  ? -2.929  -8.832  28.384  1.00 176.15 ? 593  ALA A CA  1 
ATOM   4553  C  C   . ALA A 1 593  ? -3.388  -7.483  27.813  1.00 179.55 ? 593  ALA A C   1 
ATOM   4554  O  O   . ALA A 1 593  ? -2.574  -6.620  27.453  1.00 176.84 ? 593  ALA A O   1 
ATOM   4555  C  CB  . ALA A 1 593  ? -2.839  -8.759  29.902  1.00 172.85 ? 593  ALA A CB  1 
ATOM   4556  N  N   . THR A 1 594  ? -4.709  -7.313  27.759  1.00 158.94 ? 594  THR A N   1 
ATOM   4557  C  CA  . THR A 1 594  ? -5.322  -6.087  27.264  1.00 163.66 ? 594  THR A CA  1 
ATOM   4558  C  C   . THR A 1 594  ? -6.796  -5.939  27.642  1.00 168.57 ? 594  THR A C   1 
ATOM   4559  O  O   . THR A 1 594  ? -7.583  -6.884  27.542  1.00 172.95 ? 594  THR A O   1 
ATOM   4560  C  CB  . THR A 1 594  ? -5.246  -6.022  25.754  1.00 166.10 ? 594  THR A CB  1 
ATOM   4561  O  OG1 . THR A 1 594  ? -4.222  -6.909  25.283  1.00 166.33 ? 594  THR A OG1 1 
ATOM   4562  C  CG2 . THR A 1 594  ? -4.962  -4.607  25.323  1.00 164.50 ? 594  THR A CG2 1 
ATOM   4563  N  N   . GLY A 1 595  ? -7.165  -4.733  28.060  1.00 250.83 ? 595  GLY A N   1 
ATOM   4564  C  CA  . GLY A 1 595  ? -8.550  -4.419  28.353  1.00 256.21 ? 595  GLY A CA  1 
ATOM   4565  C  C   . GLY A 1 595  ? -9.429  -4.589  27.127  1.00 265.51 ? 595  GLY A C   1 
ATOM   4566  O  O   . GLY A 1 595  ? -10.649 -4.650  27.250  1.00 266.22 ? 595  GLY A O   1 
ATOM   4567  N  N   . MET A 1 596  ? -8.801  -4.669  25.951  1.00 196.60 ? 596  MET A N   1 
ATOM   4568  C  CA  . MET A 1 596  ? -9.491  -4.850  24.665  1.00 202.79 ? 596  MET A CA  1 
ATOM   4569  C  C   . MET A 1 596  ? -8.719  -5.821  23.747  1.00 203.56 ? 596  MET A C   1 
ATOM   4570  O  O   . MET A 1 596  ? -7.497  -5.902  23.831  1.00 203.91 ? 596  MET A O   1 
ATOM   4571  C  CB  . MET A 1 596  ? -9.620  -3.504  23.942  1.00 203.21 ? 596  MET A CB  1 
ATOM   4572  C  CG  . MET A 1 596  ? -10.536 -2.495  24.595  1.00 203.40 ? 596  MET A CG  1 
ATOM   4573  S  SD  . MET A 1 596  ? -12.245 -2.913  24.257  1.00 230.70 ? 596  MET A SD  1 
ATOM   4574  C  CE  . MET A 1 596  ? -12.138 -3.313  22.505  1.00 182.94 ? 596  MET A CE  1 
ATOM   4575  N  N   . ASP A 1 597  ? -9.415  -6.542  22.864  1.00 232.52 ? 597  ASP A N   1 
ATOM   4576  C  CA  . ASP A 1 597  ? -8.734  -7.400  21.889  1.00 232.17 ? 597  ASP A CA  1 
ATOM   4577  C  C   . ASP A 1 597  ? -7.634  -6.594  21.222  1.00 223.56 ? 597  ASP A C   1 
ATOM   4578  O  O   . ASP A 1 597  ? -7.854  -5.430  20.886  1.00 220.76 ? 597  ASP A O   1 
ATOM   4579  C  CB  . ASP A 1 597  ? -9.698  -7.875  20.802  1.00 241.26 ? 597  ASP A CB  1 
ATOM   4580  C  CG  . ASP A 1 597  ? -10.845 -8.682  21.347  1.00 249.98 ? 597  ASP A CG  1 
ATOM   4581  O  OD1 . ASP A 1 597  ? -10.618 -9.482  22.277  1.00 252.16 ? 597  ASP A OD1 1 
ATOM   4582  O  OD2 . ASP A 1 597  ? -11.973 -8.518  20.832  1.00 253.81 ? 597  ASP A OD2 1 
ATOM   4583  N  N   . SER A 1 598  ? -6.463  -7.199  21.010  1.00 182.97 ? 598  SER A N   1 
ATOM   4584  C  CA  . SER A 1 598  ? -5.345  -6.457  20.406  1.00 174.63 ? 598  SER A CA  1 
ATOM   4585  C  C   . SER A 1 598  ? -4.212  -7.264  19.730  1.00 166.48 ? 598  SER A C   1 
ATOM   4586  O  O   . SER A 1 598  ? -4.004  -8.450  19.995  1.00 166.46 ? 598  SER A O   1 
ATOM   4587  C  CB  . SER A 1 598  ? -4.752  -5.462  21.415  1.00 170.57 ? 598  SER A CB  1 
ATOM   4588  O  OG  . SER A 1 598  ? -3.994  -4.450  20.770  1.00 168.07 ? 598  SER A OG  1 
ATOM   4589  N  N   . TRP A 1 599  ? -3.494  -6.573  18.847  1.00 209.94 ? 599  TRP A N   1 
ATOM   4590  C  CA  . TRP A 1 599  ? -2.373  -7.126  18.098  1.00 205.65 ? 599  TRP A CA  1 
ATOM   4591  C  C   . TRP A 1 599  ? -1.052  -6.804  18.757  1.00 199.22 ? 599  TRP A C   1 
ATOM   4592  O  O   . TRP A 1 599  ? -0.635  -5.651  18.757  1.00 198.81 ? 599  TRP A O   1 
ATOM   4593  C  CB  . TRP A 1 599  ? -2.339  -6.522  16.697  1.00 208.75 ? 599  TRP A CB  1 
ATOM   4594  C  CG  . TRP A 1 599  ? -3.266  -7.178  15.748  1.00 216.68 ? 599  TRP A CG  1 
ATOM   4595  C  CD1 . TRP A 1 599  ? -4.303  -6.601  15.076  1.00 220.32 ? 599  TRP A CD1 1 
ATOM   4596  C  CD2 . TRP A 1 599  ? -3.253  -8.557  15.367  1.00 220.76 ? 599  TRP A CD2 1 
ATOM   4597  N  NE1 . TRP A 1 599  ? -4.937  -7.538  14.296  1.00 223.67 ? 599  TRP A NE1 1 
ATOM   4598  C  CE2 . TRP A 1 599  ? -4.309  -8.745  14.456  1.00 223.45 ? 599  TRP A CE2 1 
ATOM   4599  C  CE3 . TRP A 1 599  ? -2.448  -9.649  15.708  1.00 221.58 ? 599  TRP A CE3 1 
ATOM   4600  C  CZ2 . TRP A 1 599  ? -4.580  -9.983  13.884  1.00 225.38 ? 599  TRP A CZ2 1 
ATOM   4601  C  CZ3 . TRP A 1 599  ? -2.720  -10.873 15.138  1.00 223.67 ? 599  TRP A CZ3 1 
ATOM   4602  C  CH2 . TRP A 1 599  ? -3.776  -11.031 14.236  1.00 225.53 ? 599  TRP A CH2 1 
ATOM   4603  N  N   . VAL A 1 600  ? -0.375  -7.814  19.290  1.00 170.96 ? 600  VAL A N   1 
ATOM   4604  C  CA  . VAL A 1 600  ? 0.900   -7.576  19.968  1.00 162.79 ? 600  VAL A CA  1 
ATOM   4605  C  C   . VAL A 1 600  ? 2.049   -7.744  18.978  1.00 160.13 ? 600  VAL A C   1 
ATOM   4606  O  O   . VAL A 1 600  ? 1.831   -8.138  17.835  1.00 162.88 ? 600  VAL A O   1 
ATOM   4607  C  CB  . VAL A 1 600  ? 1.085   -8.505  21.213  1.00 161.36 ? 600  VAL A CB  1 
ATOM   4608  C  CG1 . VAL A 1 600  ? 2.050   -7.888  22.246  1.00 158.71 ? 600  VAL A CG1 1 
ATOM   4609  C  CG2 . VAL A 1 600  ? -0.263  -8.800  21.875  1.00 161.06 ? 600  VAL A CG2 1 
ATOM   4610  N  N   . ALA A 1 601  ? 3.264   -7.437  19.420  1.00 148.24 ? 601  ALA A N   1 
ATOM   4611  C  CA  . ALA A 1 601  ? 4.452   -7.604  18.589  1.00 147.58 ? 601  ALA A CA  1 
ATOM   4612  C  C   . ALA A 1 601  ? 5.744   -7.737  19.404  1.00 146.27 ? 601  ALA A C   1 
ATOM   4613  O  O   . ALA A 1 601  ? 6.487   -6.773  19.584  1.00 146.38 ? 601  ALA A O   1 
ATOM   4614  C  CB  . ALA A 1 601  ? 4.567   -6.464  17.601  1.00 146.04 ? 601  ALA A CB  1 
ATOM   4615  N  N   . LEU A 1 602  ? 6.022   -8.951  19.864  1.00 170.94 ? 602  LEU A N   1 
ATOM   4616  C  CA  . LEU A 1 602  ? 7.183   -9.218  20.705  1.00 168.89 ? 602  LEU A CA  1 
ATOM   4617  C  C   . LEU A 1 602  ? 8.512   -8.985  19.968  1.00 171.38 ? 602  LEU A C   1 
ATOM   4618  O  O   . LEU A 1 602  ? 8.551   -8.934  18.738  1.00 173.18 ? 602  LEU A O   1 
ATOM   4619  C  CB  . LEU A 1 602  ? 7.095   -10.645 21.247  1.00 167.53 ? 602  LEU A CB  1 
ATOM   4620  C  CG  . LEU A 1 602  ? 5.693   -11.092 21.708  1.00 166.30 ? 602  LEU A CG  1 
ATOM   4621  C  CD1 . LEU A 1 602  ? 5.734   -12.426 22.473  1.00 164.35 ? 602  LEU A CD1 1 
ATOM   4622  C  CD2 . LEU A 1 602  ? 4.966   -10.015 22.537  1.00 162.25 ? 602  LEU A CD2 1 
ATOM   4623  N  N   . ALA A 1 603  ? 9.596   -8.828  20.725  1.00 190.23 ? 603  ALA A N   1 
ATOM   4624  C  CA  . ALA A 1 603  ? 10.908  -8.523  20.149  1.00 185.63 ? 603  ALA A CA  1 
ATOM   4625  C  C   . ALA A 1 603  ? 12.036  -8.576  21.183  1.00 182.61 ? 603  ALA A C   1 
ATOM   4626  O  O   . ALA A 1 603  ? 12.304  -7.580  21.854  1.00 179.37 ? 603  ALA A O   1 
ATOM   4627  C  CB  . ALA A 1 603  ? 10.872  -7.148  19.514  1.00 183.49 ? 603  ALA A CB  1 
ATOM   4628  N  N   . ALA A 1 604  ? 12.718  -9.716  21.286  1.00 191.15 ? 604  ALA A N   1 
ATOM   4629  C  CA  . ALA A 1 604  ? 13.699  -9.935  22.355  1.00 189.21 ? 604  ALA A CA  1 
ATOM   4630  C  C   . ALA A 1 604  ? 15.134  -9.579  21.979  1.00 188.81 ? 604  ALA A C   1 
ATOM   4631  O  O   . ALA A 1 604  ? 15.865  -10.425 21.476  1.00 191.49 ? 604  ALA A O   1 
ATOM   4632  C  CB  . ALA A 1 604  ? 13.635  -11.374 22.838  1.00 188.24 ? 604  ALA A CB  1 
ATOM   4633  N  N   . VAL A 1 605  ? 15.535  -8.339  22.253  1.00 135.85 ? 605  VAL A N   1 
ATOM   4634  C  CA  . VAL A 1 605  ? 16.899  -7.864  21.997  1.00 136.97 ? 605  VAL A CA  1 
ATOM   4635  C  C   . VAL A 1 605  ? 17.909  -8.364  23.035  1.00 135.33 ? 605  VAL A C   1 
ATOM   4636  O  O   . VAL A 1 605  ? 17.531  -8.771  24.129  1.00 135.46 ? 605  VAL A O   1 
ATOM   4637  C  CB  . VAL A 1 605  ? 16.952  -6.318  22.015  1.00 133.87 ? 605  VAL A CB  1 
ATOM   4638  C  CG1 . VAL A 1 605  ? 18.343  -5.827  21.666  1.00 134.18 ? 605  VAL A CG1 1 
ATOM   4639  C  CG2 . VAL A 1 605  ? 15.904  -5.722  21.070  1.00 135.04 ? 605  VAL A CG2 1 
ATOM   4640  N  N   . ASP A 1 606  ? 19.193  -8.347  22.692  1.00 175.41 ? 606  ASP A N   1 
ATOM   4641  C  CA  . ASP A 1 606  ? 20.216  -8.399  23.724  1.00 175.09 ? 606  ASP A CA  1 
ATOM   4642  C  C   . ASP A 1 606  ? 20.416  -6.984  24.222  1.00 171.69 ? 606  ASP A C   1 
ATOM   4643  O  O   . ASP A 1 606  ? 21.048  -6.158  23.548  1.00 172.94 ? 606  ASP A O   1 
ATOM   4644  C  CB  . ASP A 1 606  ? 21.545  -8.939  23.215  1.00 178.91 ? 606  ASP A CB  1 
ATOM   4645  C  CG  . ASP A 1 606  ? 22.629  -8.924  24.293  1.00 177.02 ? 606  ASP A CG  1 
ATOM   4646  O  OD1 . ASP A 1 606  ? 22.283  -8.856  25.496  1.00 176.04 ? 606  ASP A OD1 1 
ATOM   4647  O  OD2 . ASP A 1 606  ? 23.828  -8.983  23.940  1.00 177.07 ? 606  ASP A OD2 1 
ATOM   4648  N  N   . SER A 1 607  ? 19.878  -6.729  25.413  1.00 172.80 ? 607  SER A N   1 
ATOM   4649  C  CA  . SER A 1 607  ? 19.829  -5.402  26.018  1.00 169.24 ? 607  SER A CA  1 
ATOM   4650  C  C   . SER A 1 607  ? 21.175  -4.716  25.982  1.00 164.99 ? 607  SER A C   1 
ATOM   4651  O  O   . SER A 1 607  ? 21.292  -3.535  26.296  1.00 160.72 ? 607  SER A O   1 
ATOM   4652  C  CB  . SER A 1 607  ? 19.382  -5.516  27.468  1.00 174.00 ? 607  SER A CB  1 
ATOM   4653  O  OG  . SER A 1 607  ? 20.300  -6.324  28.184  1.00 178.55 ? 607  SER A OG  1 
ATOM   4654  N  N   . ALA A 1 608  ? 22.193  -5.469  25.607  1.00 153.14 ? 608  ALA A N   1 
ATOM   4655  C  CA  . ALA A 1 608  ? 23.534  -4.950  25.609  1.00 150.78 ? 608  ALA A CA  1 
ATOM   4656  C  C   . ALA A 1 608  ? 23.586  -3.674  24.793  1.00 145.99 ? 608  ALA A C   1 
ATOM   4657  O  O   . ALA A 1 608  ? 24.007  -2.626  25.271  1.00 141.96 ? 608  ALA A O   1 
ATOM   4658  C  CB  . ALA A 1 608  ? 24.476  -5.981  25.038  1.00 158.60 ? 608  ALA A CB  1 
ATOM   4659  N  N   . VAL A 1 609  ? 23.131  -3.781  23.558  1.00 146.71 ? 609  VAL A N   1 
ATOM   4660  C  CA  . VAL A 1 609  ? 23.154  -2.694  22.593  1.00 142.99 ? 609  VAL A CA  1 
ATOM   4661  C  C   . VAL A 1 609  ? 23.010  -1.289  23.181  1.00 138.44 ? 609  VAL A C   1 
ATOM   4662  O  O   . VAL A 1 609  ? 24.011  -0.613  23.426  1.00 136.61 ? 609  VAL A O   1 
ATOM   4663  C  CB  . VAL A 1 609  ? 22.068  -2.946  21.557  1.00 142.54 ? 609  VAL A CB  1 
ATOM   4664  C  CG1 . VAL A 1 609  ? 22.171  -4.375  21.113  1.00 149.49 ? 609  VAL A CG1 1 
ATOM   4665  C  CG2 . VAL A 1 609  ? 20.698  -2.740  22.140  1.00 139.54 ? 609  VAL A CG2 1 
ATOM   4666  N  N   . TYR A 1 610  ? 21.772  -0.853  23.395  1.00 172.35 ? 610  TYR A N   1 
ATOM   4667  C  CA  . TYR A 1 610  ? 21.494  0.430   24.017  1.00 166.00 ? 610  TYR A CA  1 
ATOM   4668  C  C   . TYR A 1 610  ? 22.496  0.648   25.164  1.00 220.12 ? 610  TYR A C   1 
ATOM   4669  O  O   . TYR A 1 610  ? 23.582  1.195   24.948  1.00 214.12 ? 610  TYR A O   1 
ATOM   4670  C  CB  . TYR A 1 610  ? 20.051  0.446   24.544  1.00 161.90 ? 610  TYR A CB  1 
ATOM   4671  C  CG  . TYR A 1 610  ? 19.021  -0.303  23.695  1.00 167.81 ? 610  TYR A CG  1 
ATOM   4672  C  CD1 . TYR A 1 610  ? 18.409  0.301   22.606  1.00 171.03 ? 610  TYR A CD1 1 
ATOM   4673  C  CD2 . TYR A 1 610  ? 18.634  -1.600  24.013  1.00 167.93 ? 610  TYR A CD2 1 
ATOM   4674  C  CE1 . TYR A 1 610  ? 17.454  -0.376  21.838  1.00 177.79 ? 610  TYR A CE1 1 
ATOM   4675  C  CE2 . TYR A 1 610  ? 17.684  -2.290  23.248  1.00 175.03 ? 610  TYR A CE2 1 
ATOM   4676  C  CZ  . TYR A 1 610  ? 17.095  -1.673  22.160  1.00 178.82 ? 610  TYR A CZ  1 
ATOM   4677  O  OH  . TYR A 1 610  ? 16.148  -2.332  21.388  1.00 179.34 ? 610  TYR A OH  1 
ATOM   4678  N  N   . GLY A 1 611  ? 22.110  0.229   26.373  1.00 218.52 ? 611  GLY A N   1 
ATOM   4679  C  CA  . GLY A 1 611  ? 23.020  -0.002  27.498  1.00 223.61 ? 611  GLY A CA  1 
ATOM   4680  C  C   . GLY A 1 611  ? 23.657  1.103   28.343  1.00 226.74 ? 611  GLY A C   1 
ATOM   4681  O  O   . GLY A 1 611  ? 23.018  1.694   29.221  1.00 224.52 ? 611  GLY A O   1 
ATOM   4682  N  N   . VAL A 1 612  ? 24.949  1.328   28.094  1.00 193.19 ? 612  VAL A N   1 
ATOM   4683  C  CA  . VAL A 1 612  ? 25.764  2.323   28.786  1.00 197.39 ? 612  VAL A CA  1 
ATOM   4684  C  C   . VAL A 1 612  ? 25.058  3.662   28.831  1.00 204.26 ? 612  VAL A C   1 
ATOM   4685  O  O   . VAL A 1 612  ? 25.039  4.404   27.852  1.00 206.36 ? 612  VAL A O   1 
ATOM   4686  C  CB  . VAL A 1 612  ? 27.136  2.518   28.087  1.00 280.19 ? 612  VAL A CB  1 
ATOM   4687  C  CG1 . VAL A 1 612  ? 28.094  1.386   28.437  1.00 283.55 ? 612  VAL A CG1 1 
ATOM   4688  C  CG2 . VAL A 1 612  ? 26.962  2.627   26.574  1.00 283.68 ? 612  VAL A CG2 1 
ATOM   4689  N  N   . GLN A 1 613  ? 24.494  3.972   29.987  1.00 272.95 ? 613  GLN A N   1 
ATOM   4690  C  CA  . GLN A 1 613  ? 23.625  5.125   30.118  1.00 279.45 ? 613  GLN A CA  1 
ATOM   4691  C  C   . GLN A 1 613  ? 22.621  5.126   28.969  1.00 290.98 ? 613  GLN A C   1 
ATOM   4692  O  O   . GLN A 1 613  ? 22.791  5.825   27.969  1.00 290.87 ? 613  GLN A O   1 
ATOM   4693  C  CB  . GLN A 1 613  ? 24.417  6.440   30.175  1.00 277.78 ? 613  GLN A CB  1 
ATOM   4694  C  CG  . GLN A 1 613  ? 23.521  7.664   30.374  1.00 272.05 ? 613  GLN A CG  1 
ATOM   4695  C  CD  . GLN A 1 613  ? 24.175  8.789   31.155  1.00 266.31 ? 613  GLN A CD  1 
ATOM   4696  O  OE1 . GLN A 1 613  ? 25.079  8.566   31.957  1.00 264.81 ? 613  GLN A OE1 1 
ATOM   4697  N  NE2 . GLN A 1 613  ? 23.701  10.009  30.933  1.00 263.08 ? 613  GLN A NE2 1 
ATOM   4698  N  N   . ARG A 1 614  ? 21.584  4.309   29.109  1.00 230.42 ? 614  ARG A N   1 
ATOM   4699  C  CA  . ARG A 1 614  ? 20.485  4.312   28.159  1.00 238.24 ? 614  ARG A CA  1 
ATOM   4700  C  C   . ARG A 1 614  ? 19.650  5.558   28.403  1.00 238.99 ? 614  ARG A C   1 
ATOM   4701  O  O   . ARG A 1 614  ? 18.680  5.525   29.162  1.00 238.54 ? 614  ARG A O   1 
ATOM   4702  C  CB  . ARG A 1 614  ? 19.637  3.059   28.338  1.00 241.24 ? 614  ARG A CB  1 
ATOM   4703  C  CG  . ARG A 1 614  ? 18.532  2.911   27.321  1.00 242.68 ? 614  ARG A CG  1 
ATOM   4704  C  CD  . ARG A 1 614  ? 18.243  1.448   27.100  1.00 246.52 ? 614  ARG A CD  1 
ATOM   4705  N  NE  . ARG A 1 614  ? 16.831  1.209   26.861  1.00 248.27 ? 614  ARG A NE  1 
ATOM   4706  C  CZ  . ARG A 1 614  ? 16.177  0.152   27.318  1.00 252.90 ? 614  ARG A CZ  1 
ATOM   4707  N  NH1 . ARG A 1 614  ? 16.816  -0.759  28.038  1.00 254.88 ? 614  ARG A NH1 1 
ATOM   4708  N  NH2 . ARG A 1 614  ? 14.887  0.016   27.061  1.00 256.34 ? 614  ARG A NH2 1 
ATOM   4709  N  N   . GLY A 1 615  ? 20.036  6.650   27.749  1.00 422.94 ? 615  GLY A N   1 
ATOM   4710  C  CA  . GLY A 1 615  ? 19.501  7.971   28.035  1.00 421.24 ? 615  GLY A CA  1 
ATOM   4711  C  C   . GLY A 1 615  ? 18.113  7.995   28.646  1.00 423.44 ? 615  GLY A C   1 
ATOM   4712  O  O   . GLY A 1 615  ? 17.219  7.274   28.199  1.00 427.69 ? 615  GLY A O   1 
ATOM   4713  N  N   . ALA A 1 616  ? 17.935  8.829   29.668  1.00 272.75 ? 616  ALA A N   1 
ATOM   4714  C  CA  . ALA A 1 616  ? 16.631  9.001   30.289  1.00 273.13 ? 616  ALA A CA  1 
ATOM   4715  C  C   . ALA A 1 616  ? 15.546  9.124   29.214  1.00 276.21 ? 616  ALA A C   1 
ATOM   4716  O  O   . ALA A 1 616  ? 14.737  8.213   29.048  1.00 280.32 ? 616  ALA A O   1 
ATOM   4717  C  CB  . ALA A 1 616  ? 16.635  10.219  31.210  1.00 268.26 ? 616  ALA A CB  1 
ATOM   4718  N  N   . LYS A 1 617  ? 15.556  10.229  28.471  1.00 289.35 ? 617  LYS A N   1 
ATOM   4719  C  CA  . LYS A 1 617  ? 14.555  10.481  27.431  1.00 289.82 ? 617  LYS A CA  1 
ATOM   4720  C  C   . LYS A 1 617  ? 13.214  9.876   27.820  1.00 286.67 ? 617  LYS A C   1 
ATOM   4721  O  O   . LYS A 1 617  ? 12.607  10.317  28.790  1.00 284.32 ? 617  LYS A O   1 
ATOM   4722  C  CB  . LYS A 1 617  ? 15.007  9.942   26.074  1.00 296.33 ? 617  LYS A CB  1 
ATOM   4723  C  CG  . LYS A 1 617  ? 14.240  10.537  24.905  1.00 300.09 ? 617  LYS A CG  1 
ATOM   4724  C  CD  . LYS A 1 617  ? 14.165  12.045  25.049  1.00 296.88 ? 617  LYS A CD  1 
ATOM   4725  C  CE  . LYS A 1 617  ? 13.761  12.712  23.754  1.00 300.77 ? 617  LYS A CE  1 
ATOM   4726  N  NZ  . LYS A 1 617  ? 13.624  14.178  23.953  1.00 297.28 ? 617  LYS A NZ  1 
ATOM   4727  N  N   . LYS A 1 618  ? 12.769  8.867   27.067  1.00 258.31 ? 618  LYS A N   1 
ATOM   4728  C  CA  . LYS A 1 618  ? 11.607  8.047   27.440  1.00 254.97 ? 618  LYS A CA  1 
ATOM   4729  C  C   . LYS A 1 618  ? 11.434  6.819   26.533  1.00 248.90 ? 618  LYS A C   1 
ATOM   4730  O  O   . LYS A 1 618  ? 11.858  6.828   25.372  1.00 248.71 ? 618  LYS A O   1 
ATOM   4731  C  CB  . LYS A 1 618  ? 10.316  8.864   27.426  1.00 260.17 ? 618  LYS A CB  1 
ATOM   4732  C  CG  . LYS A 1 618  ? 10.191  9.937   28.494  1.00 259.58 ? 618  LYS A CG  1 
ATOM   4733  C  CD  . LYS A 1 618  ? 9.663   9.430   29.814  1.00 262.21 ? 618  LYS A CD  1 
ATOM   4734  C  CE  . LYS A 1 618  ? 9.208   10.600  30.684  1.00 258.28 ? 618  LYS A CE  1 
ATOM   4735  N  NZ  . LYS A 1 618  ? 10.102  11.793  30.584  1.00 253.51 ? 618  LYS A NZ  1 
ATOM   4736  N  N   . PRO A 1 619  ? 10.811  5.752   27.070  1.00 378.80 ? 619  PRO A N   1 
ATOM   4737  C  CA  . PRO A 1 619  ? 10.492  4.533   26.313  1.00 379.50 ? 619  PRO A CA  1 
ATOM   4738  C  C   . PRO A 1 619  ? 9.279   4.707   25.394  1.00 377.48 ? 619  PRO A C   1 
ATOM   4739  O  O   . PRO A 1 619  ? 9.446   4.765   24.174  1.00 378.93 ? 619  PRO A O   1 
ATOM   4740  C  CB  . PRO A 1 619  ? 10.168  3.508   27.411  1.00 383.84 ? 619  PRO A CB  1 
ATOM   4741  C  CG  . PRO A 1 619  ? 10.656  4.115   28.695  1.00 379.63 ? 619  PRO A CG  1 
ATOM   4742  C  CD  . PRO A 1 619  ? 10.520  5.590   28.504  1.00 375.59 ? 619  PRO A CD  1 
ATOM   4743  N  N   . LEU A 1 620  ? 8.081   4.776   25.978  1.00 309.57 ? 620  LEU A N   1 
ATOM   4744  C  CA  . LEU A 1 620  ? 6.839   4.943   25.215  1.00 308.11 ? 620  LEU A CA  1 
ATOM   4745  C  C   . LEU A 1 620  ? 6.649   6.373   24.696  1.00 304.30 ? 620  LEU A C   1 
ATOM   4746  O  O   . LEU A 1 620  ? 5.894   6.608   23.749  1.00 308.28 ? 620  LEU A O   1 
ATOM   4747  C  CB  . LEU A 1 620  ? 5.627   4.526   26.060  1.00 305.84 ? 620  LEU A CB  1 
ATOM   4748  C  CG  . LEU A 1 620  ? 4.243   4.972   25.571  1.00 305.31 ? 620  LEU A CG  1 
ATOM   4749  C  CD1 . LEU A 1 620  ? 3.825   4.215   24.324  1.00 311.74 ? 620  LEU A CD1 1 
ATOM   4750  C  CD2 . LEU A 1 620  ? 3.209   4.803   26.667  1.00 304.91 ? 620  LEU A CD2 1 
ATOM   4751  N  N   . GLU A 1 621  ? 7.335   7.321   25.330  1.00 238.29 ? 621  GLU A N   1 
ATOM   4752  C  CA  . GLU A 1 621  ? 7.300   8.729   24.932  1.00 235.26 ? 621  GLU A CA  1 
ATOM   4753  C  C   . GLU A 1 621  ? 8.055   8.953   23.609  1.00 232.95 ? 621  GLU A C   1 
ATOM   4754  O  O   . GLU A 1 621  ? 7.643   9.776   22.786  1.00 233.78 ? 621  GLU A O   1 
ATOM   4755  C  CB  . GLU A 1 621  ? 7.843   9.602   26.079  1.00 234.56 ? 621  GLU A CB  1 
ATOM   4756  C  CG  . GLU A 1 621  ? 8.208   11.052  25.754  1.00 237.23 ? 621  GLU A CG  1 
ATOM   4757  C  CD  . GLU A 1 621  ? 8.819   11.798  26.951  1.00 234.46 ? 621  GLU A CD  1 
ATOM   4758  O  OE1 . GLU A 1 621  ? 8.234   11.748  28.056  1.00 233.14 ? 621  GLU A OE1 1 
ATOM   4759  O  OE2 . GLU A 1 621  ? 9.891   12.425  26.794  1.00 232.84 ? 621  GLU A OE2 1 
ATOM   4760  N  N   . ARG A 1 622  ? 9.137   8.195   23.409  1.00 218.58 ? 622  ARG A N   1 
ATOM   4761  C  CA  . ARG A 1 622  ? 9.893   8.185   22.152  1.00 215.52 ? 622  ARG A CA  1 
ATOM   4762  C  C   . ARG A 1 622  ? 8.908   8.317   20.995  1.00 213.93 ? 622  ARG A C   1 
ATOM   4763  O  O   . ARG A 1 622  ? 9.009   9.218   20.159  1.00 214.81 ? 622  ARG A O   1 
ATOM   4764  C  CB  . ARG A 1 622  ? 10.683  6.873   22.035  1.00 218.99 ? 622  ARG A CB  1 
ATOM   4765  C  CG  . ARG A 1 622  ? 11.907  6.927   21.147  1.00 220.52 ? 622  ARG A CG  1 
ATOM   4766  C  CD  . ARG A 1 622  ? 12.755  5.670   21.318  1.00 205.99 ? 622  ARG A CD  1 
ATOM   4767  N  NE  . ARG A 1 622  ? 12.121  4.488   20.740  1.00 212.90 ? 622  ARG A NE  1 
ATOM   4768  C  CZ  . ARG A 1 622  ? 12.735  3.322   20.552  1.00 215.76 ? 622  ARG A CZ  1 
ATOM   4769  N  NH1 . ARG A 1 622  ? 14.007  3.173   20.896  1.00 213.94 ? 622  ARG A NH1 1 
ATOM   4770  N  NH2 . ARG A 1 622  ? 12.079  2.303   20.014  1.00 220.24 ? 622  ARG A NH2 1 
ATOM   4771  N  N   . VAL A 1 623  ? 7.929   7.425   20.979  1.00 253.18 ? 623  VAL A N   1 
ATOM   4772  C  CA  . VAL A 1 623  ? 6.857   7.494   20.008  1.00 253.55 ? 623  VAL A CA  1 
ATOM   4773  C  C   . VAL A 1 623  ? 5.926   8.680   20.275  1.00 246.48 ? 623  VAL A C   1 
ATOM   4774  O  O   . VAL A 1 623  ? 5.743   9.530   19.410  1.00 247.69 ? 623  VAL A O   1 
ATOM   4775  C  CB  . VAL A 1 623  ? 6.078   6.173   19.970  1.00 214.72 ? 623  VAL A CB  1 
ATOM   4776  C  CG1 . VAL A 1 623  ? 4.706   6.381   19.358  1.00 217.46 ? 623  VAL A CG1 1 
ATOM   4777  C  CG2 . VAL A 1 623  ? 6.887   5.105   19.211  1.00 216.85 ? 623  VAL A CG2 1 
ATOM   4778  N  N   . PHE A 1 624  ? 5.362   8.751   21.475  1.00 251.84 ? 624  PHE A N   1 
ATOM   4779  C  CA  . PHE A 1 624  ? 4.430   9.828   21.808  1.00 245.02 ? 624  PHE A CA  1 
ATOM   4780  C  C   . PHE A 1 624  ? 4.974   11.229  21.496  1.00 246.47 ? 624  PHE A C   1 
ATOM   4781  O  O   . PHE A 1 624  ? 4.199   12.141  21.229  1.00 247.70 ? 624  PHE A O   1 
ATOM   4782  C  CB  . PHE A 1 624  ? 3.967   9.748   23.273  1.00 230.72 ? 624  PHE A CB  1 
ATOM   4783  C  CG  . PHE A 1 624  ? 2.555   9.213   23.453  1.00 224.35 ? 624  PHE A CG  1 
ATOM   4784  C  CD1 . PHE A 1 624  ? 2.296   8.170   24.344  1.00 221.71 ? 624  PHE A CD1 1 
ATOM   4785  C  CD2 . PHE A 1 624  ? 1.490   9.758   22.743  1.00 222.38 ? 624  PHE A CD2 1 
ATOM   4786  C  CE1 . PHE A 1 624  ? 1.004   7.680   24.516  1.00 223.53 ? 624  PHE A CE1 1 
ATOM   4787  C  CE2 . PHE A 1 624  ? 0.197   9.269   22.908  1.00 223.90 ? 624  PHE A CE2 1 
ATOM   4788  C  CZ  . PHE A 1 624  ? -0.046  8.232   23.793  1.00 225.13 ? 624  PHE A CZ  1 
ATOM   4789  N  N   . GLN A 1 625  ? 6.292   11.408  21.536  1.00 223.17 ? 625  GLN A N   1 
ATOM   4790  C  CA  . GLN A 1 625  ? 6.879   12.683  21.136  1.00 226.70 ? 625  GLN A CA  1 
ATOM   4791  C  C   . GLN A 1 625  ? 6.589   12.893  19.672  1.00 230.66 ? 625  GLN A C   1 
ATOM   4792  O  O   . GLN A 1 625  ? 5.614   13.540  19.300  1.00 232.00 ? 625  GLN A O   1 
ATOM   4793  C  CB  . GLN A 1 625  ? 8.385   12.676  21.323  1.00 232.52 ? 625  GLN A CB  1 
ATOM   4794  C  CG  . GLN A 1 625  ? 8.825   12.490  22.748  1.00 235.58 ? 625  GLN A CG  1 
ATOM   4795  C  CD  . GLN A 1 625  ? 10.255  12.937  22.963  1.00 240.27 ? 625  GLN A CD  1 
ATOM   4796  O  OE1 . GLN A 1 625  ? 10.774  13.748  22.198  1.00 243.47 ? 625  GLN A OE1 1 
ATOM   4797  N  NE2 . GLN A 1 625  ? 10.900  12.417  24.008  1.00 240.12 ? 625  GLN A NE2 1 
ATOM   4798  N  N   . PHE A 1 626  ? 7.452   12.328  18.842  1.00 204.94 ? 626  PHE A N   1 
ATOM   4799  C  CA  . PHE A 1 626  ? 7.218   12.293  17.415  1.00 208.69 ? 626  PHE A CA  1 
ATOM   4800  C  C   . PHE A 1 626  ? 5.707   12.272  17.137  1.00 202.35 ? 626  PHE A C   1 
ATOM   4801  O  O   . PHE A 1 626  ? 5.131   13.243  16.652  1.00 200.08 ? 626  PHE A O   1 
ATOM   4802  C  CB  . PHE A 1 626  ? 7.904   11.051  16.840  1.00 218.01 ? 626  PHE A CB  1 
ATOM   4803  C  CG  . PHE A 1 626  ? 7.554   10.764  15.412  1.00 231.01 ? 626  PHE A CG  1 
ATOM   4804  C  CD1 . PHE A 1 626  ? 8.359   11.225  14.381  1.00 236.31 ? 626  PHE A CD1 1 
ATOM   4805  C  CD2 . PHE A 1 626  ? 6.425   10.016  15.097  1.00 237.46 ? 626  PHE A CD2 1 
ATOM   4806  C  CE1 . PHE A 1 626  ? 8.036   10.952  13.053  1.00 244.37 ? 626  PHE A CE1 1 
ATOM   4807  C  CE2 . PHE A 1 626  ? 6.094   9.740   13.777  1.00 245.65 ? 626  PHE A CE2 1 
ATOM   4808  C  CZ  . PHE A 1 626  ? 6.900   10.207  12.751  1.00 248.88 ? 626  PHE A CZ  1 
ATOM   4809  N  N   . LEU A 1 627  ? 5.066   11.179  17.518  1.00 168.44 ? 627  LEU A N   1 
ATOM   4810  C  CA  . LEU A 1 627  ? 3.696   10.884  17.123  1.00 167.24 ? 627  LEU A CA  1 
ATOM   4811  C  C   . LEU A 1 627  ? 2.694   12.039  17.208  1.00 164.94 ? 627  LEU A C   1 
ATOM   4812  O  O   . LEU A 1 627  ? 1.650   12.003  16.576  1.00 172.39 ? 627  LEU A O   1 
ATOM   4813  C  CB  . LEU A 1 627  ? 3.213   9.678   17.924  1.00 162.26 ? 627  LEU A CB  1 
ATOM   4814  C  CG  . LEU A 1 627  ? 1.784   9.166   17.853  1.00 160.45 ? 627  LEU A CG  1 
ATOM   4815  C  CD1 . LEU A 1 627  ? 1.769   7.666   18.149  1.00 162.40 ? 627  LEU A CD1 1 
ATOM   4816  C  CD2 . LEU A 1 627  ? 0.914   9.950   18.825  1.00 154.22 ? 627  LEU A CD2 1 
ATOM   4817  N  N   . GLU A 1 628  ? 2.994   13.061  17.985  1.00 214.70 ? 628  GLU A N   1 
ATOM   4818  C  CA  . GLU A 1 628  ? 2.083   14.187  18.049  1.00 212.74 ? 628  GLU A CA  1 
ATOM   4819  C  C   . GLU A 1 628  ? 2.787   15.440  17.598  1.00 210.38 ? 628  GLU A C   1 
ATOM   4820  O  O   . GLU A 1 628  ? 2.847   16.432  18.321  1.00 206.42 ? 628  GLU A O   1 
ATOM   4821  C  CB  . GLU A 1 628  ? 1.492   14.383  19.448  1.00 211.34 ? 628  GLU A CB  1 
ATOM   4822  C  CG  . GLU A 1 628  ? 2.487   14.848  20.517  1.00 234.77 ? 628  GLU A CG  1 
ATOM   4823  C  CD  . GLU A 1 628  ? 1.812   15.532  21.707  1.00 232.85 ? 628  GLU A CD  1 
ATOM   4824  O  OE1 . GLU A 1 628  ? 0.982   16.444  21.474  1.00 235.44 ? 628  GLU A OE1 1 
ATOM   4825  O  OE2 . GLU A 1 628  ? 2.121   15.160  22.867  1.00 228.23 ? 628  GLU A OE2 1 
ATOM   4826  N  N   . LYS A 1 629  ? 3.345   15.385  16.401  1.00 170.77 ? 629  LYS A N   1 
ATOM   4827  C  CA  . LYS A 1 629  ? 3.837   16.594  15.769  1.00 169.02 ? 629  LYS A CA  1 
ATOM   4828  C  C   . LYS A 1 629  ? 2.783   16.994  14.759  1.00 171.46 ? 629  LYS A C   1 
ATOM   4829  O  O   . LYS A 1 629  ? 2.944   17.930  13.979  1.00 168.94 ? 629  LYS A O   1 
ATOM   4830  C  CB  . LYS A 1 629  ? 5.216   16.362  15.177  1.00 170.44 ? 629  LYS A CB  1 
ATOM   4831  C  CG  . LYS A 1 629  ? 6.194   15.940  16.275  1.00 164.89 ? 629  LYS A CG  1 
ATOM   4832  C  CD  . LYS A 1 629  ? 5.700   16.470  17.630  1.00 183.46 ? 629  LYS A CD  1 
ATOM   4833  C  CE  . LYS A 1 629  ? 6.554   16.050  18.815  1.00 163.24 ? 629  LYS A CE  1 
ATOM   4834  N  NZ  . LYS A 1 629  ? 5.890   16.495  20.079  1.00 156.96 ? 629  LYS A NZ  1 
ATOM   4835  N  N   . SER A 1 630  ? 1.689   16.247  14.836  1.00 131.83 ? 630  SER A N   1 
ATOM   4836  C  CA  . SER A 1 630  ? 0.466   16.503  14.118  1.00 136.50 ? 630  SER A CA  1 
ATOM   4837  C  C   . SER A 1 630  ? -0.336  17.559  14.843  1.00 135.64 ? 630  SER A C   1 
ATOM   4838  O  O   . SER A 1 630  ? -1.472  17.868  14.496  1.00 143.48 ? 630  SER A O   1 
ATOM   4839  C  CB  . SER A 1 630  ? -0.353  15.213  14.000  1.00 136.85 ? 630  SER A CB  1 
ATOM   4840  O  OG  . SER A 1 630  ? -0.705  14.692  15.267  1.00 129.69 ? 630  SER A OG  1 
ATOM   4841  N  N   . ASP A 1 631  ? 0.249   18.094  15.895  1.00 199.45 ? 631  ASP A N   1 
ATOM   4842  C  CA  . ASP A 1 631  ? -0.370  19.226  16.537  1.00 197.55 ? 631  ASP A CA  1 
ATOM   4843  C  C   . ASP A 1 631  ? -0.105  20.362  15.575  1.00 200.49 ? 631  ASP A C   1 
ATOM   4844  O  O   . ASP A 1 631  ? 1.015   20.862  15.464  1.00 197.25 ? 631  ASP A O   1 
ATOM   4845  C  CB  . ASP A 1 631  ? 0.223   19.474  17.931  1.00 195.90 ? 631  ASP A CB  1 
ATOM   4846  C  CG  . ASP A 1 631  ? -0.795  20.039  18.914  1.00 205.35 ? 631  ASP A CG  1 
ATOM   4847  O  OD1 . ASP A 1 631  ? -0.886  21.277  19.003  1.00 207.06 ? 631  ASP A OD1 1 
ATOM   4848  O  OD2 . ASP A 1 631  ? -1.498  19.250  19.592  1.00 208.23 ? 631  ASP A OD2 1 
ATOM   4849  N  N   . LEU A 1 632  ? -1.147  20.712  14.835  1.00 183.92 ? 632  LEU A N   1 
ATOM   4850  C  CA  . LEU A 1 632  ? -1.064  21.734  13.807  1.00 187.30 ? 632  LEU A CA  1 
ATOM   4851  C  C   . LEU A 1 632  ? -0.662  23.078  14.432  1.00 181.22 ? 632  LEU A C   1 
ATOM   4852  O  O   . LEU A 1 632  ? 0.254   23.743  13.953  1.00 182.14 ? 632  LEU A O   1 
ATOM   4853  C  CB  . LEU A 1 632  ? -2.400  21.828  13.044  1.00 195.17 ? 632  LEU A CB  1 
ATOM   4854  C  CG  . LEU A 1 632  ? -2.969  20.552  12.394  1.00 199.68 ? 632  LEU A CG  1 
ATOM   4855  C  CD1 . LEU A 1 632  ? -4.460  20.671  12.101  1.00 202.31 ? 632  LEU A CD1 1 
ATOM   4856  C  CD2 . LEU A 1 632  ? -2.202  20.172  11.136  1.00 204.72 ? 632  LEU A CD2 1 
ATOM   4857  N  N   . GLY A 1 633  ? -1.324  23.455  15.522  1.00 214.55 ? 633  GLY A N   1 
ATOM   4858  C  CA  . GLY A 1 633  ? -1.079  24.738  16.155  1.00 206.34 ? 633  GLY A CA  1 
ATOM   4859  C  C   . GLY A 1 633  ? 0.264   24.845  16.838  1.00 195.18 ? 633  GLY A C   1 
ATOM   4860  O  O   . GLY A 1 633  ? 1.188   24.099  16.524  1.00 195.57 ? 633  GLY A O   1 
ATOM   4861  N  N   . CYS A 1 634  ? 0.363   25.774  17.785  1.00 179.24 ? 634  CYS A N   1 
ATOM   4862  C  CA  . CYS A 1 634  ? 1.606   25.981  18.518  1.00 175.22 ? 634  CYS A CA  1 
ATOM   4863  C  C   . CYS A 1 634  ? 1.511   26.859  19.777  1.00 171.59 ? 634  CYS A C   1 
ATOM   4864  O  O   . CYS A 1 634  ? 0.546   27.600  19.963  1.00 176.33 ? 634  CYS A O   1 
ATOM   4865  C  CB  . CYS A 1 634  ? 2.658   26.562  17.586  1.00 178.68 ? 634  CYS A CB  1 
ATOM   4866  S  SG  . CYS A 1 634  ? 4.187   26.961  18.425  1.00 209.55 ? 634  CYS A SG  1 
ATOM   4867  N  N   . GLY A 1 635  ? 2.523   26.752  20.638  1.00 179.80 ? 635  GLY A N   1 
ATOM   4868  C  CA  . GLY A 1 635  ? 2.673   27.625  21.791  1.00 172.76 ? 635  GLY A CA  1 
ATOM   4869  C  C   . GLY A 1 635  ? 2.297   27.095  23.172  1.00 169.14 ? 635  GLY A C   1 
ATOM   4870  O  O   . GLY A 1 635  ? 2.054   25.891  23.383  1.00 168.80 ? 635  GLY A O   1 
ATOM   4871  N  N   . ALA A 1 636  ? 2.299   28.024  24.126  1.00 163.81 ? 636  ALA A N   1 
ATOM   4872  C  CA  . ALA A 1 636  ? 1.701   27.819  25.431  1.00 160.45 ? 636  ALA A CA  1 
ATOM   4873  C  C   . ALA A 1 636  ? 0.204   28.040  25.265  1.00 160.98 ? 636  ALA A C   1 
ATOM   4874  O  O   . ALA A 1 636  ? -0.608  27.691  26.127  1.00 159.86 ? 636  ALA A O   1 
ATOM   4875  C  CB  . ALA A 1 636  ? 2.277   28.812  26.414  1.00 160.67 ? 636  ALA A CB  1 
ATOM   4876  N  N   . GLY A 1 637  ? -0.140  28.649  24.136  1.00 157.23 ? 637  GLY A N   1 
ATOM   4877  C  CA  . GLY A 1 637  ? -1.522  28.833  23.728  1.00 162.04 ? 637  GLY A CA  1 
ATOM   4878  C  C   . GLY A 1 637  ? -1.804  30.250  23.255  1.00 169.88 ? 637  GLY A C   1 
ATOM   4879  O  O   . GLY A 1 637  ? -0.953  31.128  23.400  1.00 166.47 ? 637  GLY A O   1 
ATOM   4880  N  N   . GLY A 1 638  ? -2.982  30.454  22.663  1.00 163.75 ? 638  GLY A N   1 
ATOM   4881  C  CA  . GLY A 1 638  ? -3.566  31.775  22.472  1.00 167.62 ? 638  GLY A CA  1 
ATOM   4882  C  C   . GLY A 1 638  ? -2.714  32.836  21.807  1.00 168.56 ? 638  GLY A C   1 
ATOM   4883  O  O   . GLY A 1 638  ? -1.531  32.964  22.096  1.00 170.69 ? 638  GLY A O   1 
ATOM   4884  N  N   . GLY A 1 639  ? -3.337  33.638  20.951  1.00 206.68 ? 639  GLY A N   1 
ATOM   4885  C  CA  . GLY A 1 639  ? -2.599  34.523  20.070  1.00 207.23 ? 639  GLY A CA  1 
ATOM   4886  C  C   . GLY A 1 639  ? -2.465  36.015  20.358  1.00 208.55 ? 639  GLY A C   1 
ATOM   4887  O  O   . GLY A 1 639  ? -1.994  36.434  21.426  1.00 201.04 ? 639  GLY A O   1 
ATOM   4888  N  N   . LEU A 1 640  ? -2.886  36.809  19.368  1.00 133.10 ? 640  LEU A N   1 
ATOM   4889  C  CA  . LEU A 1 640  ? -2.560  38.236  19.250  1.00 135.50 ? 640  LEU A CA  1 
ATOM   4890  C  C   . LEU A 1 640  ? -3.767  38.942  18.617  1.00 138.96 ? 640  LEU A C   1 
ATOM   4891  O  O   . LEU A 1 640  ? -3.945  40.154  18.766  1.00 139.79 ? 640  LEU A O   1 
ATOM   4892  C  CB  . LEU A 1 640  ? -1.275  38.402  18.397  1.00 136.55 ? 640  LEU A CB  1 
ATOM   4893  C  CG  . LEU A 1 640  ? -0.392  39.649  18.150  1.00 128.90 ? 640  LEU A CG  1 
ATOM   4894  C  CD1 . LEU A 1 640  ? -0.759  40.833  19.030  1.00 127.61 ? 640  LEU A CD1 1 
ATOM   4895  C  CD2 . LEU A 1 640  ? 1.107   39.289  18.251  1.00 129.24 ? 640  LEU A CD2 1 
ATOM   4896  N  N   . ASN A 1 641  ? -4.588  38.149  17.923  1.00 177.90 ? 641  ASN A N   1 
ATOM   4897  C  CA  . ASN A 1 641  ? -5.903  38.538  17.414  1.00 181.11 ? 641  ASN A CA  1 
ATOM   4898  C  C   . ASN A 1 641  ? -6.741  37.298  17.455  1.00 182.76 ? 641  ASN A C   1 
ATOM   4899  O  O   . ASN A 1 641  ? -6.216  36.203  17.271  1.00 183.33 ? 641  ASN A O   1 
ATOM   4900  C  CB  . ASN A 1 641  ? -5.817  38.932  15.961  1.00 190.15 ? 641  ASN A CB  1 
ATOM   4901  C  CG  . ASN A 1 641  ? -4.424  39.287  15.559  1.00 194.02 ? 641  ASN A CG  1 
ATOM   4902  O  OD1 . ASN A 1 641  ? -3.807  40.155  16.174  1.00 193.84 ? 641  ASN A OD1 1 
ATOM   4903  N  ND2 . ASN A 1 641  ? -3.897  38.610  14.537  1.00 198.79 ? 641  ASN A ND2 1 
ATOM   4904  N  N   . ASN A 1 642  ? -8.043  37.455  17.664  1.00 203.55 ? 642  ASN A N   1 
ATOM   4905  C  CA  . ASN A 1 642  ? -8.906  36.289  17.725  1.00 205.49 ? 642  ASN A CA  1 
ATOM   4906  C  C   . ASN A 1 642  ? -8.547  35.391  16.564  1.00 208.31 ? 642  ASN A C   1 
ATOM   4907  O  O   . ASN A 1 642  ? -8.654  34.166  16.623  1.00 204.44 ? 642  ASN A O   1 
ATOM   4908  C  CB  . ASN A 1 642  ? -10.377 36.672  17.641  1.00 214.62 ? 642  ASN A CB  1 
ATOM   4909  C  CG  . ASN A 1 642  ? -11.272 35.457  17.524  1.00 221.58 ? 642  ASN A CG  1 
ATOM   4910  O  OD1 . ASN A 1 642  ? -12.276 35.470  16.817  1.00 230.31 ? 642  ASN A OD1 1 
ATOM   4911  N  ND2 . ASN A 1 642  ? -10.894 34.383  18.205  1.00 218.14 ? 642  ASN A ND2 1 
ATOM   4912  N  N   . ALA A 1 643  ? -8.112  36.038  15.497  1.00 181.61 ? 643  ALA A N   1 
ATOM   4913  C  CA  . ALA A 1 643  ? -7.557  35.336  14.373  1.00 187.11 ? 643  ALA A CA  1 
ATOM   4914  C  C   . ALA A 1 643  ? -6.289  34.604  14.826  1.00 176.57 ? 643  ALA A C   1 
ATOM   4915  O  O   . ALA A 1 643  ? -6.232  33.376  14.781  1.00 173.05 ? 643  ALA A O   1 
ATOM   4916  C  CB  . ALA A 1 643  ? -7.262  36.315  13.253  1.00 197.63 ? 643  ALA A CB  1 
ATOM   4917  N  N   . ASN A 1 644  ? -5.284  35.350  15.277  1.00 165.79 ? 644  ASN A N   1 
ATOM   4918  C  CA  . ASN A 1 644  ? -4.026  34.746  15.707  1.00 160.64 ? 644  ASN A CA  1 
ATOM   4919  C  C   . ASN A 1 644  ? -4.270  33.582  16.671  1.00 158.02 ? 644  ASN A C   1 
ATOM   4920  O  O   . ASN A 1 644  ? -3.696  32.506  16.503  1.00 161.37 ? 644  ASN A O   1 
ATOM   4921  C  CB  . ASN A 1 644  ? -3.101  35.813  16.325  1.00 153.49 ? 644  ASN A CB  1 
ATOM   4922  C  CG  . ASN A 1 644  ? -1.703  35.273  16.686  1.00 148.73 ? 644  ASN A CG  1 
ATOM   4923  O  OD1 . ASN A 1 644  ? -0.777  36.037  17.002  1.00 145.23 ? 644  ASN A OD1 1 
ATOM   4924  N  ND2 . ASN A 1 644  ? -1.554  33.957  16.643  1.00 150.07 ? 644  ASN A ND2 1 
ATOM   4925  N  N   . VAL A 1 645  ? -5.131  33.795  17.665  1.00 219.40 ? 645  VAL A N   1 
ATOM   4926  C  CA  . VAL A 1 645  ? -5.438  32.779  18.677  1.00 214.93 ? 645  VAL A CA  1 
ATOM   4927  C  C   . VAL A 1 645  ? -5.958  31.481  18.057  1.00 219.73 ? 645  VAL A C   1 
ATOM   4928  O  O   . VAL A 1 645  ? -5.550  30.381  18.446  1.00 216.51 ? 645  VAL A O   1 
ATOM   4929  C  CB  . VAL A 1 645  ? -6.499  33.290  19.655  1.00 214.58 ? 645  VAL A CB  1 
ATOM   4930  C  CG1 . VAL A 1 645  ? -6.679  32.305  20.787  1.00 210.96 ? 645  VAL A CG1 1 
ATOM   4931  C  CG2 . VAL A 1 645  ? -6.105  34.654  20.186  1.00 210.30 ? 645  VAL A CG2 1 
ATOM   4932  N  N   . PHE A 1 646  ? -6.872  31.638  17.101  1.00 155.60 ? 646  PHE A N   1 
ATOM   4933  C  CA  . PHE A 1 646  ? -7.423  30.550  16.291  1.00 158.16 ? 646  PHE A CA  1 
ATOM   4934  C  C   . PHE A 1 646  ? -6.395  29.936  15.362  1.00 162.68 ? 646  PHE A C   1 
ATOM   4935  O  O   . PHE A 1 646  ? -6.458  28.752  15.012  1.00 163.86 ? 646  PHE A O   1 
ATOM   4936  C  CB  . PHE A 1 646  ? -8.549  31.110  15.442  1.00 162.60 ? 646  PHE A CB  1 
ATOM   4937  C  CG  . PHE A 1 646  ? -9.890  30.879  16.016  1.00 158.34 ? 646  PHE A CG  1 
ATOM   4938  C  CD1 . PHE A 1 646  ? -10.646 31.932  16.487  1.00 154.35 ? 646  PHE A CD1 1 
ATOM   4939  C  CD2 . PHE A 1 646  ? -10.393 29.593  16.104  1.00 156.63 ? 646  PHE A CD2 1 
ATOM   4940  C  CE1 . PHE A 1 646  ? -11.898 31.703  17.020  1.00 153.04 ? 646  PHE A CE1 1 
ATOM   4941  C  CE2 . PHE A 1 646  ? -11.638 29.354  16.633  1.00 154.98 ? 646  PHE A CE2 1 
ATOM   4942  C  CZ  . PHE A 1 646  ? -12.394 30.410  17.095  1.00 153.35 ? 646  PHE A CZ  1 
ATOM   4943  N  N   . HIS A 1 647  ? -5.465  30.772  14.936  1.00 199.66 ? 647  HIS A N   1 
ATOM   4944  C  CA  . HIS A 1 647  ? -4.383  30.288  14.140  1.00 203.88 ? 647  HIS A CA  1 
ATOM   4945  C  C   . HIS A 1 647  ? -3.588  29.347  15.024  1.00 188.76 ? 647  HIS A C   1 
ATOM   4946  O  O   . HIS A 1 647  ? -3.740  28.133  14.921  1.00 187.20 ? 647  HIS A O   1 
ATOM   4947  C  CB  . HIS A 1 647  ? -3.519  31.430  13.629  1.00 215.06 ? 647  HIS A CB  1 
ATOM   4948  C  CG  . HIS A 1 647  ? -2.748  31.089  12.406  1.00 231.48 ? 647  HIS A CG  1 
ATOM   4949  N  ND1 . HIS A 1 647  ? -2.237  29.811  12.169  1.00 235.49 ? 647  HIS A ND1 1 
ATOM   4950  C  CD2 . HIS A 1 647  ? -2.376  31.817  11.329  1.00 242.63 ? 647  HIS A CD2 1 
ATOM   4951  C  CE1 . HIS A 1 647  ? -1.607  29.789  11.029  1.00 242.74 ? 647  HIS A CE1 1 
ATOM   4952  N  NE2 . HIS A 1 647  ? -1.673  31.003  10.483  1.00 247.66 ? 647  HIS A NE2 1 
ATOM   4953  N  N   . LEU A 1 648  ? -2.782  29.904  15.927  1.00 162.41 ? 648  LEU A N   1 
ATOM   4954  C  CA  . LEU A 1 648  ? -1.878  29.106  16.769  1.00 154.86 ? 648  LEU A CA  1 
ATOM   4955  C  C   . LEU A 1 648  ? -2.564  27.882  17.330  1.00 151.11 ? 648  LEU A C   1 
ATOM   4956  O  O   . LEU A 1 648  ? -1.920  26.958  17.818  1.00 148.19 ? 648  LEU A O   1 
ATOM   4957  C  CB  . LEU A 1 648  ? -1.312  29.952  17.903  1.00 145.45 ? 648  LEU A CB  1 
ATOM   4958  C  CG  . LEU A 1 648  ? 0.005   30.615  17.498  1.00 142.75 ? 648  LEU A CG  1 
ATOM   4959  C  CD1 . LEU A 1 648  ? 0.126   32.019  18.050  1.00 137.97 ? 648  LEU A CD1 1 
ATOM   4960  C  CD2 . LEU A 1 648  ? 1.186   29.753  17.917  1.00 138.70 ? 648  LEU A CD2 1 
ATOM   4961  N  N   . ALA A 1 649  ? -3.885  27.893  17.248  1.00 151.09 ? 649  ALA A N   1 
ATOM   4962  C  CA  . ALA A 1 649  ? -4.702  26.765  17.634  1.00 148.94 ? 649  ALA A CA  1 
ATOM   4963  C  C   . ALA A 1 649  ? -4.524  25.609  16.671  1.00 151.17 ? 649  ALA A C   1 
ATOM   4964  O  O   . ALA A 1 649  ? -5.022  24.518  16.907  1.00 149.14 ? 649  ALA A O   1 
ATOM   4965  C  CB  . ALA A 1 649  ? -6.151  27.186  17.653  1.00 154.72 ? 649  ALA A CB  1 
ATOM   4966  N  N   . GLY A 1 650  ? -3.821  25.847  15.577  1.00 193.39 ? 650  GLY A N   1 
ATOM   4967  C  CA  . GLY A 1 650  ? -3.780  24.867  14.513  1.00 200.46 ? 650  GLY A CA  1 
ATOM   4968  C  C   . GLY A 1 650  ? -5.095  24.840  13.760  1.00 208.46 ? 650  GLY A C   1 
ATOM   4969  O  O   . GLY A 1 650  ? -5.390  23.896  13.019  1.00 211.35 ? 650  GLY A O   1 
ATOM   4970  N  N   . LEU A 1 651  ? -5.892  25.882  13.961  1.00 165.93 ? 651  LEU A N   1 
ATOM   4971  C  CA  . LEU A 1 651  ? -7.106  26.043  13.199  1.00 175.35 ? 651  LEU A CA  1 
ATOM   4972  C  C   . LEU A 1 651  ? -7.004  27.151  12.166  1.00 181.72 ? 651  LEU A C   1 
ATOM   4973  O  O   . LEU A 1 651  ? -6.050  27.931  12.149  1.00 179.63 ? 651  LEU A O   1 
ATOM   4974  C  CB  . LEU A 1 651  ? -8.266  26.396  14.130  1.00 172.13 ? 651  LEU A CB  1 
ATOM   4975  C  CG  . LEU A 1 651  ? -8.828  25.300  15.016  1.00 167.85 ? 651  LEU A CG  1 
ATOM   4976  C  CD1 . LEU A 1 651  ? -10.037 25.836  15.746  1.00 165.20 ? 651  LEU A CD1 1 
ATOM   4977  C  CD2 . LEU A 1 651  ? -9.194  24.104  14.167  1.00 174.22 ? 651  LEU A CD2 1 
ATOM   4978  N  N   . THR A 1 652  ? -8.000  27.171  11.286  1.00 160.20 ? 652  THR A N   1 
ATOM   4979  C  CA  . THR A 1 652  ? -8.616  28.422  10.853  1.00 162.71 ? 652  THR A CA  1 
ATOM   4980  C  C   . THR A 1 652  ? -10.129 28.153  10.710  1.00 163.62 ? 652  THR A C   1 
ATOM   4981  O  O   . THR A 1 652  ? -10.556 27.031  10.457  1.00 164.76 ? 652  THR A O   1 
ATOM   4982  C  CB  . THR A 1 652  ? -7.893  29.119  9.653   1.00 166.54 ? 652  THR A CB  1 
ATOM   4983  O  OG1 . THR A 1 652  ? -8.035  30.545  9.755   1.00 166.60 ? 652  THR A OG1 1 
ATOM   4984  C  CG2 . THR A 1 652  ? -8.425  28.639  8.330   1.00 175.56 ? 652  THR A CG2 1 
ATOM   4985  N  N   . PHE A 1 653  ? -10.922 29.185  10.937  1.00 174.08 ? 653  PHE A N   1 
ATOM   4986  C  CA  . PHE A 1 653  ? -12.327 29.059  11.269  1.00 179.53 ? 653  PHE A CA  1 
ATOM   4987  C  C   . PHE A 1 653  ? -13.086 29.823  10.219  1.00 191.11 ? 653  PHE A C   1 
ATOM   4988  O  O   . PHE A 1 653  ? -12.509 30.685  9.553   1.00 191.87 ? 653  PHE A O   1 
ATOM   4989  C  CB  . PHE A 1 653  ? -12.525 29.798  12.557  1.00 175.77 ? 653  PHE A CB  1 
ATOM   4990  C  CG  . PHE A 1 653  ? -11.853 31.136  12.555  1.00 178.41 ? 653  PHE A CG  1 
ATOM   4991  C  CD1 . PHE A 1 653  ? -12.564 32.288  12.796  1.00 181.24 ? 653  PHE A CD1 1 
ATOM   4992  C  CD2 . PHE A 1 653  ? -10.509 31.244  12.256  1.00 177.12 ? 653  PHE A CD2 1 
ATOM   4993  C  CE1 . PHE A 1 653  ? -11.937 33.518  12.779  1.00 180.45 ? 653  PHE A CE1 1 
ATOM   4994  C  CE2 . PHE A 1 653  ? -9.882  32.465  12.234  1.00 176.35 ? 653  PHE A CE2 1 
ATOM   4995  C  CZ  . PHE A 1 653  ? -10.592 33.603  12.506  1.00 177.77 ? 653  PHE A CZ  1 
ATOM   4996  N  N   . LEU A 1 654  ? -14.383 29.557  10.089  1.00 203.04 ? 654  LEU A N   1 
ATOM   4997  C  CA  . LEU A 1 654  ? -15.172 30.140  9.004   1.00 217.43 ? 654  LEU A CA  1 
ATOM   4998  C  C   . LEU A 1 654  ? -16.294 31.034  9.512   1.00 228.09 ? 654  LEU A C   1 
ATOM   4999  O  O   . LEU A 1 654  ? -17.395 30.554  9.764   1.00 234.68 ? 654  LEU A O   1 
ATOM   5000  C  CB  . LEU A 1 654  ? -15.756 29.028  8.147   1.00 218.88 ? 654  LEU A CB  1 
ATOM   5001  C  CG  . LEU A 1 654  ? -15.784 29.425  6.689   1.00 226.35 ? 654  LEU A CG  1 
ATOM   5002  C  CD1 . LEU A 1 654  ? -14.623 30.369  6.428   1.00 225.09 ? 654  LEU A CD1 1 
ATOM   5003  C  CD2 . LEU A 1 654  ? -15.714 28.191  5.804   1.00 230.42 ? 654  LEU A CD2 1 
ATOM   5004  N  N   . THR A 1 655  ? -16.025 32.333  9.647   1.00 222.47 ? 655  THR A N   1 
ATOM   5005  C  CA  . THR A 1 655  ? -17.003 33.238  10.251  1.00 225.82 ? 655  THR A CA  1 
ATOM   5006  C  C   . THR A 1 655  ? -17.038 34.618  9.618   1.00 238.10 ? 655  THR A C   1 
ATOM   5007  O  O   . THR A 1 655  ? -16.027 35.320  9.509   1.00 234.02 ? 655  THR A O   1 
ATOM   5008  C  CB  . THR A 1 655  ? -16.816 33.388  11.794  1.00 241.70 ? 655  THR A CB  1 
ATOM   5009  O  OG1 . THR A 1 655  ? -17.164 32.162  12.451  1.00 236.37 ? 655  THR A OG1 1 
ATOM   5010  C  CG2 . THR A 1 655  ? -17.691 34.517  12.340  1.00 240.89 ? 655  THR A CG2 1 
ATOM   5011  N  N   . ASN A 1 656  ? -18.233 34.985  9.187   1.00 236.38 ? 656  ASN A N   1 
ATOM   5012  C  CA  . ASN A 1 656  ? -18.477 36.346  8.808   1.00 250.69 ? 656  ASN A CA  1 
ATOM   5013  C  C   . ASN A 1 656  ? -18.787 37.151  10.049  1.00 245.80 ? 656  ASN A C   1 
ATOM   5014  O  O   . ASN A 1 656  ? -19.795 36.942  10.734  1.00 246.56 ? 656  ASN A O   1 
ATOM   5015  C  CB  . ASN A 1 656  ? -19.559 36.445  7.733   1.00 265.51 ? 656  ASN A CB  1 
ATOM   5016  C  CG  . ASN A 1 656  ? -19.011 36.149  6.341   1.00 271.12 ? 656  ASN A CG  1 
ATOM   5017  O  OD1 . ASN A 1 656  ? -19.724 36.211  5.335   1.00 279.94 ? 656  ASN A OD1 1 
ATOM   5018  N  ND2 . ASN A 1 656  ? -17.726 35.835  6.282   1.00 265.27 ? 656  ASN A ND2 1 
ATOM   5019  N  N   . ALA A 1 657  ? -17.848 38.041  10.334  1.00 287.21 ? 657  ALA A N   1 
ATOM   5020  C  CA  . ALA A 1 657  ? -17.917 38.992  11.421  1.00 279.86 ? 657  ALA A CA  1 
ATOM   5021  C  C   . ALA A 1 657  ? -16.498 39.515  11.541  1.00 274.55 ? 657  ALA A C   1 
ATOM   5022  O  O   . ALA A 1 657  ? -16.244 40.712  11.428  1.00 276.06 ? 657  ALA A O   1 
ATOM   5023  C  CB  . ALA A 1 657  ? -18.360 38.323  12.705  1.00 270.89 ? 657  ALA A CB  1 
ATOM   5024  N  N   . ASN A 1 658  ? -15.564 38.596  11.733  1.00 285.67 ? 658  ASN A N   1 
ATOM   5025  C  CA  . ASN A 1 658  ? -14.164 38.963  11.825  1.00 280.34 ? 658  ASN A CA  1 
ATOM   5026  C  C   . ASN A 1 658  ? -13.356 38.384  10.687  1.00 282.77 ? 658  ASN A C   1 
ATOM   5027  O  O   . ASN A 1 658  ? -13.817 37.474  9.998   1.00 286.32 ? 658  ASN A O   1 
ATOM   5028  C  CB  . ASN A 1 658  ? -13.579 38.491  13.149  1.00 268.39 ? 658  ASN A CB  1 
ATOM   5029  C  CG  . ASN A 1 658  ? -13.868 39.440  14.277  1.00 259.15 ? 658  ASN A CG  1 
ATOM   5030  O  OD1 . ASN A 1 658  ? -13.443 39.220  15.411  1.00 249.69 ? 658  ASN A OD1 1 
ATOM   5031  N  ND2 . ASN A 1 658  ? -14.590 40.512  13.974  1.00 261.92 ? 658  ASN A ND2 1 
ATOM   5032  N  N   . ALA A 1 659  ? -12.148 38.916  10.507  1.00 236.64 ? 659  ALA A N   1 
ATOM   5033  C  CA  . ALA A 1 659  ? -11.196 38.406  9.517   1.00 240.17 ? 659  ALA A CA  1 
ATOM   5034  C  C   . ALA A 1 659  ? -10.609 37.052  9.914   1.00 234.06 ? 659  ALA A C   1 
ATOM   5035  O  O   . ALA A 1 659  ? -9.567  36.996  10.576  1.00 228.73 ? 659  ALA A O   1 
ATOM   5036  C  CB  . ALA A 1 659  ? -10.073 39.415  9.280   1.00 240.38 ? 659  ALA A CB  1 
ATOM   5037  N  N   . ASP A 1 660  ? -11.270 35.970  9.492   1.00 214.60 ? 660  ASP A N   1 
ATOM   5038  C  CA  . ASP A 1 660  ? -10.799 34.610  9.777   1.00 209.18 ? 660  ASP A CA  1 
ATOM   5039  C  C   . ASP A 1 660  ? -9.478  34.240  9.092   1.00 207.67 ? 660  ASP A C   1 
ATOM   5040  O  O   . ASP A 1 660  ? -9.154  33.060  8.926   1.00 203.21 ? 660  ASP A O   1 
ATOM   5041  C  CB  . ASP A 1 660  ? -11.892 33.532  9.577   1.00 215.47 ? 660  ASP A CB  1 
ATOM   5042  C  CG  . ASP A 1 660  ? -12.680 33.692  8.294   1.00 229.59 ? 660  ASP A CG  1 
ATOM   5043  O  OD1 . ASP A 1 660  ? -12.062 33.773  7.217   1.00 235.28 ? 660  ASP A OD1 1 
ATOM   5044  O  OD2 . ASP A 1 660  ? -13.929 33.697  8.364   1.00 234.39 ? 660  ASP A OD2 1 
ATOM   5045  N  N   . ASP A 1 661  ? -8.706  35.267  8.745   1.00 198.96 ? 661  ASP A N   1 
ATOM   5046  C  CA  . ASP A 1 661  ? -7.469  35.102  7.990   1.00 198.98 ? 661  ASP A CA  1 
ATOM   5047  C  C   . ASP A 1 661  ? -6.411  34.244  8.698   1.00 193.99 ? 661  ASP A C   1 
ATOM   5048  O  O   . ASP A 1 661  ? -6.716  33.425  9.563   1.00 188.73 ? 661  ASP A O   1 
ATOM   5049  C  CB  . ASP A 1 661  ? -6.894  36.472  7.595   1.00 195.19 ? 661  ASP A CB  1 
ATOM   5050  C  CG  . ASP A 1 661  ? -6.307  37.222  8.767   1.00 177.83 ? 661  ASP A CG  1 
ATOM   5051  O  OD1 . ASP A 1 661  ? -7.007  38.073  9.360   1.00 170.45 ? 661  ASP A OD1 1 
ATOM   5052  O  OD2 . ASP A 1 661  ? -5.132  36.955  9.085   1.00 172.01 ? 661  ASP A OD2 1 
ATOM   5053  N  N   . SER A 1 662  ? -5.163  34.427  8.299   1.00 261.40 ? 662  SER A N   1 
ATOM   5054  C  CA  . SER A 1 662  ? -4.064  33.654  8.853   1.00 257.99 ? 662  SER A CA  1 
ATOM   5055  C  C   . SER A 1 662  ? -2.792  34.015  8.099   1.00 264.20 ? 662  SER A C   1 
ATOM   5056  O  O   . SER A 1 662  ? -2.211  33.188  7.386   1.00 263.60 ? 662  SER A O   1 
ATOM   5057  C  CB  . SER A 1 662  ? -4.361  32.150  8.778   1.00 260.56 ? 662  SER A CB  1 
ATOM   5058  O  OG  . SER A 1 662  ? -4.880  31.802  7.506   1.00 269.25 ? 662  SER A OG  1 
ATOM   5059  N  N   . GLN A 1 663  ? -2.370  35.259  8.303   1.00 177.74 ? 663  GLN A N   1 
ATOM   5060  C  CA  . GLN A 1 663  ? -1.344  35.936  7.514   1.00 187.47 ? 663  GLN A CA  1 
ATOM   5061  C  C   . GLN A 1 663  ? -0.361  35.112  6.658   1.00 200.21 ? 663  GLN A C   1 
ATOM   5062  O  O   . GLN A 1 663  ? 0.500   34.387  7.140   1.00 194.31 ? 663  GLN A O   1 
ATOM   5063  C  CB  . GLN A 1 663  ? -0.624  36.972  8.381   1.00 175.69 ? 663  GLN A CB  1 
ATOM   5064  C  CG  . GLN A 1 663  ? -1.515  37.618  9.439   1.00 166.10 ? 663  GLN A CG  1 
ATOM   5065  C  CD  . GLN A 1 663  ? -2.803  38.281  8.889   1.00 168.21 ? 663  GLN A CD  1 
ATOM   5066  O  OE1 . GLN A 1 663  ? -2.999  38.360  7.684   1.00 174.35 ? 663  GLN A OE1 1 
ATOM   5067  N  NE2 . GLN A 1 663  ? -3.662  38.757  9.775   1.00 163.91 ? 663  GLN A NE2 1 
ATOM   5068  N  N   . GLU A 1 664  ? -0.545  35.280  5.351   1.00 322.20 ? 664  GLU A N   1 
ATOM   5069  C  CA  . GLU A 1 664  ? 0.349   34.825  4.278   1.00 338.13 ? 664  GLU A CA  1 
ATOM   5070  C  C   . GLU A 1 664  ? 0.398   33.323  4.052   1.00 343.38 ? 664  GLU A C   1 
ATOM   5071  O  O   . GLU A 1 664  ? -0.149  32.791  3.087   1.00 338.90 ? 664  GLU A O   1 
ATOM   5072  C  CB  . GLU A 1 664  ? 1.759   35.348  4.530   1.00 341.63 ? 664  GLU A CB  1 
ATOM   5073  C  CG  . GLU A 1 664  ? 1.779   36.847  4.828   1.00 338.97 ? 664  GLU A CG  1 
ATOM   5074  C  CD  . GLU A 1 664  ? 3.037   37.537  4.336   1.00 346.49 ? 664  GLU A CD  1 
ATOM   5075  O  OE1 . GLU A 1 664  ? 3.813   36.926  3.571   1.00 351.93 ? 664  GLU A OE1 1 
ATOM   5076  O  OE2 . GLU A 1 664  ? 3.240   38.709  4.716   1.00 347.20 ? 664  GLU A OE2 1 
ATOM   5077  N  N   . ASN A 1 665  ? 1.048   32.658  4.989   1.00 195.76 ? 665  ASN A N   1 
ATOM   5078  C  CA  . ASN A 1 665  ? 1.560   31.330  4.777   1.00 200.99 ? 665  ASN A CA  1 
ATOM   5079  C  C   . ASN A 1 665  ? 0.986   30.487  5.896   1.00 199.26 ? 665  ASN A C   1 
ATOM   5080  O  O   . ASN A 1 665  ? -0.235  30.364  6.039   1.00 201.56 ? 665  ASN A O   1 
ATOM   5081  C  CB  . ASN A 1 665  ? 3.095   31.421  4.846   1.00 199.23 ? 665  ASN A CB  1 
ATOM   5082  C  CG  . ASN A 1 665  ? 3.794   30.109  4.582   1.00 196.77 ? 665  ASN A CG  1 
ATOM   5083  O  OD1 . ASN A 1 665  ? 4.486   29.579  5.462   1.00 188.90 ? 665  ASN A OD1 1 
ATOM   5084  N  ND2 . ASN A 1 665  ? 3.662   29.598  3.373   1.00 203.86 ? 665  ASN A ND2 1 
ATOM   5085  N  N   . ASP A 1 666  ? 1.883   29.933  6.703   1.00 341.29 ? 666  ASP A N   1 
ATOM   5086  C  CA  . ASP A 1 666  ? 1.527   29.336  7.984   1.00 336.43 ? 666  ASP A CA  1 
ATOM   5087  C  C   . ASP A 1 666  ? 2.731   28.906  8.829   1.00 324.74 ? 666  ASP A C   1 
ATOM   5088  O  O   . ASP A 1 666  ? 3.087   27.733  8.880   1.00 322.61 ? 666  ASP A O   1 
ATOM   5089  C  CB  . ASP A 1 666  ? 0.513   28.191  7.838   1.00 347.00 ? 666  ASP A CB  1 
ATOM   5090  C  CG  . ASP A 1 666  ? 1.087   26.969  7.158   1.00 358.11 ? 666  ASP A CG  1 
ATOM   5091  O  OD1 . ASP A 1 666  ? 2.110   27.101  6.459   1.00 363.95 ? 666  ASP A OD1 1 
ATOM   5092  O  OD2 . ASP A 1 666  ? 0.512   25.870  7.324   1.00 360.18 ? 666  ASP A OD2 1 
ATOM   5093  N  N   . GLU A 1 667  ? 3.377   29.891  9.441   1.00 383.14 ? 667  GLU A N   1 
ATOM   5094  C  CA  . GLU A 1 667  ? 4.183   29.706  10.649  1.00 369.75 ? 667  GLU A CA  1 
ATOM   5095  C  C   . GLU A 1 667  ? 4.888   28.360  10.828  1.00 367.25 ? 667  GLU A C   1 
ATOM   5096  O  O   . GLU A 1 667  ? 4.303   27.429  11.382  1.00 365.17 ? 667  GLU A O   1 
ATOM   5097  C  CB  . GLU A 1 667  ? 3.288   29.958  11.864  1.00 357.04 ? 667  GLU A CB  1 
ATOM   5098  C  CG  . GLU A 1 667  ? 1.846   30.308  11.500  1.00 354.52 ? 667  GLU A CG  1 
ATOM   5099  C  CD  . GLU A 1 667  ? 1.719   31.665  10.814  1.00 352.73 ? 667  GLU A CD  1 
ATOM   5100  O  OE1 . GLU A 1 667  ? 2.735   32.184  10.303  1.00 351.81 ? 667  GLU A OE1 1 
ATOM   5101  O  OE2 . GLU A 1 667  ? 0.600   32.219  10.787  1.00 352.98 ? 667  GLU A OE2 1 
ATOM   5102  N  N   . PRO A 1 668  ? 6.158   28.267  10.388  1.00 334.99 ? 668  PRO A N   1 
ATOM   5103  C  CA  . PRO A 1 668  ? 7.031   27.107  10.641  1.00 331.85 ? 668  PRO A CA  1 
ATOM   5104  C  C   . PRO A 1 668  ? 7.356   26.886  12.131  1.00 322.63 ? 668  PRO A C   1 
ATOM   5105  O  O   . PRO A 1 668  ? 8.475   26.477  12.453  1.00 319.48 ? 668  PRO A O   1 
ATOM   5106  C  CB  . PRO A 1 668  ? 8.307   27.455  9.863   1.00 334.18 ? 668  PRO A CB  1 
ATOM   5107  C  CG  . PRO A 1 668  ? 7.857   28.394  8.796   1.00 341.34 ? 668  PRO A CG  1 
ATOM   5108  C  CD  . PRO A 1 668  ? 6.755   29.201  9.417   1.00 339.59 ? 668  PRO A CD  1 
ATOM   5109  N  N   . CYS A 1 669  ? 6.381   27.146  13.005  1.00 312.12 ? 669  CYS A N   1 
ATOM   5110  C  CA  . CYS A 1 669  ? 6.514   26.999  14.458  1.00 304.54 ? 669  CYS A CA  1 
ATOM   5111  C  C   . CYS A 1 669  ? 7.497   25.903  14.882  1.00 301.75 ? 669  CYS A C   1 
ATOM   5112  O  O   . CYS A 1 669  ? 7.565   24.845  14.257  1.00 305.04 ? 669  CYS A O   1 
ATOM   5113  C  CB  . CYS A 1 669  ? 5.133   26.740  15.069  1.00 303.24 ? 669  CYS A CB  1 
ATOM   5114  S  SG  . CYS A 1 669  ? 5.135   26.198  16.789  1.00 344.48 ? 669  CYS A SG  1 
ATOM   5115  N  N   . LYS A 1 670  ? 8.252   26.154  15.949  1.00 276.90 ? 670  LYS A N   1 
ATOM   5116  C  CA  . LYS A 1 670  ? 9.297   25.223  16.374  1.00 272.64 ? 670  LYS A CA  1 
ATOM   5117  C  C   . LYS A 1 670  ? 9.652   25.362  17.859  1.00 261.78 ? 670  LYS A C   1 
ATOM   5118  O  O   . LYS A 1 670  ? 10.566  26.106  18.211  1.00 258.55 ? 670  LYS A O   1 
ATOM   5119  C  CB  . LYS A 1 670  ? 10.557  25.407  15.511  1.00 277.36 ? 670  LYS A CB  1 
ATOM   5120  C  CG  . LYS A 1 670  ? 11.741  24.519  15.892  1.00 275.66 ? 670  LYS A CG  1 
ATOM   5121  C  CD  . LYS A 1 670  ? 11.464  23.052  15.594  1.00 278.66 ? 670  LYS A CD  1 
ATOM   5122  C  CE  . LYS A 1 670  ? 12.605  22.148  16.056  1.00 276.30 ? 670  LYS A CE  1 
ATOM   5123  N  NZ  . LYS A 1 670  ? 13.861  22.346  15.278  1.00 279.69 ? 670  LYS A NZ  1 
ATOM   5124  N  N   . GLU A 1 671  ? 8.912   24.653  18.714  1.00 295.96 ? 671  GLU A N   1 
ATOM   5125  C  CA  . GLU A 1 671  ? 9.248   24.468  20.142  1.00 285.79 ? 671  GLU A CA  1 
ATOM   5126  C  C   . GLU A 1 671  ? 9.099   25.673  21.129  1.00 260.27 ? 671  GLU A C   1 
ATOM   5127  O  O   . GLU A 1 671  ? 10.012  25.934  21.914  1.00 259.25 ? 671  GLU A O   1 
ATOM   5128  C  CB  . GLU A 1 671  ? 10.641  23.821  20.286  1.00 284.25 ? 671  GLU A CB  1 
ATOM   5129  C  CG  . GLU A 1 671  ? 10.757  22.403  19.709  1.00 285.90 ? 671  GLU A CG  1 
ATOM   5130  C  CD  . GLU A 1 671  ? 12.136  21.794  19.907  1.00 282.58 ? 671  GLU A CD  1 
ATOM   5131  O  OE1 . GLU A 1 671  ? 12.910  22.326  20.728  1.00 277.28 ? 671  GLU A OE1 1 
ATOM   5132  O  OE2 . GLU A 1 671  ? 12.445  20.779  19.244  1.00 285.21 ? 671  GLU A OE2 1 
ATOM   5133  N  N   . ILE A 1 672  ? 7.955   26.372  21.106  1.00 246.05 ? 672  ILE A N   1 
ATOM   5134  C  CA  . ILE A 1 672  ? 7.657   27.493  22.031  1.00 234.71 ? 672  ILE A CA  1 
ATOM   5135  C  C   . ILE A 1 672  ? 6.664   27.064  23.120  1.00 223.04 ? 672  ILE A C   1 
ATOM   5136  O  O   . ILE A 1 672  ? 6.276   27.863  23.979  1.00 218.34 ? 672  ILE A O   1 
ATOM   5137  C  CB  . ILE A 1 672  ? 7.054   28.744  21.269  1.00 257.29 ? 672  ILE A CB  1 
ATOM   5138  C  CG1 . ILE A 1 672  ? 7.127   30.035  22.092  1.00 253.79 ? 672  ILE A CG1 1 
ATOM   5139  C  CG2 . ILE A 1 672  ? 5.603   28.516  20.884  1.00 259.62 ? 672  ILE A CG2 1 
ATOM   5140  C  CD1 . ILE A 1 672  ? 6.414   31.228  21.432  1.00 257.77 ? 672  ILE A CD1 1 
ATOM   5141  N  N   . LEU A 1 673  ? 6.274   25.792  23.084  1.00 154.02 ? 673  LEU A N   1 
ATOM   5142  C  CA  . LEU A 1 673  ? 4.998   25.373  23.657  1.00 143.55 ? 673  LEU A CA  1 
ATOM   5143  C  C   . LEU A 1 673  ? 4.948   25.242  25.158  1.00 135.13 ? 673  LEU A C   1 
ATOM   5144  O  O   . LEU A 1 673  ? 3.910   24.849  25.683  1.00 132.69 ? 673  LEU A O   1 
ATOM   5145  C  CB  . LEU A 1 673  ? 4.495   24.082  23.016  1.00 140.27 ? 673  LEU A CB  1 
ATOM   5146  C  CG  . LEU A 1 673  ? 4.772   22.738  23.675  1.00 129.59 ? 673  LEU A CG  1 
ATOM   5147  C  CD1 . LEU A 1 673  ? 3.682   21.799  23.231  1.00 130.48 ? 673  LEU A CD1 1 
ATOM   5148  C  CD2 . LEU A 1 673  ? 6.169   22.175  23.363  1.00 127.57 ? 673  LEU A CD2 1 
ATOM   5149  N  N   . LEU A 1 679  ? 55.996  14.874  20.596  1.00 336.20 ? 679  LEU A N   1 
ATOM   5150  C  CA  . LEU A 1 679  ? 56.957  14.614  19.529  1.00 335.14 ? 679  LEU A CA  1 
ATOM   5151  C  C   . LEU A 1 679  ? 56.270  14.111  18.253  1.00 337.24 ? 679  LEU A C   1 
ATOM   5152  O  O   . LEU A 1 679  ? 56.832  14.201  17.161  1.00 337.11 ? 679  LEU A O   1 
ATOM   5153  C  CB  . LEU A 1 679  ? 58.040  13.643  20.007  1.00 334.02 ? 679  LEU A CB  1 
ATOM   5154  C  CG  . LEU A 1 679  ? 58.959  14.213  21.094  1.00 331.22 ? 679  LEU A CG  1 
ATOM   5155  C  CD1 . LEU A 1 679  ? 59.644  13.103  21.876  1.00 329.09 ? 679  LEU A CD1 1 
ATOM   5156  C  CD2 . LEU A 1 679  ? 59.978  15.191  20.508  1.00 329.07 ? 679  LEU A CD2 1 
ATOM   5157  N  N   . GLN A 1 680  ? 55.055  13.584  18.396  1.00 290.23 ? 680  GLN A N   1 
ATOM   5158  C  CA  . GLN A 1 680  ? 54.197  13.309  17.243  1.00 292.33 ? 680  GLN A CA  1 
ATOM   5159  C  C   . GLN A 1 680  ? 53.358  14.547  16.883  1.00 289.72 ? 680  GLN A C   1 
ATOM   5160  O  O   . GLN A 1 680  ? 52.586  14.526  15.920  1.00 291.03 ? 680  GLN A O   1 
ATOM   5161  C  CB  . GLN A 1 680  ? 53.311  12.081  17.495  1.00 298.03 ? 680  GLN A CB  1 
ATOM   5162  C  CG  . GLN A 1 680  ? 51.814  12.361  17.565  1.00 301.98 ? 680  GLN A CG  1 
ATOM   5163  C  CD  . GLN A 1 680  ? 51.393  13.011  18.864  1.00 302.72 ? 680  GLN A CD  1 
ATOM   5164  O  OE1 . GLN A 1 680  ? 52.168  13.086  19.818  1.00 301.90 ? 680  GLN A OE1 1 
ATOM   5165  N  NE2 . GLN A 1 680  ? 50.153  13.484  18.910  1.00 304.47 ? 680  GLN A NE2 1 
ATOM   5166  N  N   . LYS A 1 681  ? 53.517  15.613  17.679  1.00 359.23 ? 681  LYS A N   1 
ATOM   5167  C  CA  . LYS A 1 681  ? 52.880  16.916  17.431  1.00 355.08 ? 681  LYS A CA  1 
ATOM   5168  C  C   . LYS A 1 681  ? 53.673  17.733  16.411  1.00 353.58 ? 681  LYS A C   1 
ATOM   5169  O  O   . LYS A 1 681  ? 53.105  18.517  15.649  1.00 354.05 ? 681  LYS A O   1 
ATOM   5170  C  CB  . LYS A 1 681  ? 52.781  17.755  18.718  1.00 350.62 ? 681  LYS A CB  1 
ATOM   5171  C  CG  . LYS A 1 681  ? 52.284  17.046  19.968  1.00 348.30 ? 681  LYS A CG  1 
ATOM   5172  C  CD  . LYS A 1 681  ? 52.325  17.996  21.156  1.00 344.57 ? 681  LYS A CD  1 
ATOM   5173  C  CE  . LYS A 1 681  ? 52.375  17.240  22.463  1.00 343.54 ? 681  LYS A CE  1 
ATOM   5174  N  NZ  . LYS A 1 681  ? 52.655  18.151  23.604  1.00 342.45 ? 681  LYS A NZ  1 
ATOM   5175  N  N   . LYS A 1 682  ? 54.993  17.568  16.435  1.00 339.94 ? 682  LYS A N   1 
ATOM   5176  C  CA  . LYS A 1 682  ? 55.887  18.257  15.509  1.00 338.92 ? 682  LYS A CA  1 
ATOM   5177  C  C   . LYS A 1 682  ? 55.546  17.916  14.062  1.00 343.54 ? 682  LYS A C   1 
ATOM   5178  O  O   . LYS A 1 682  ? 55.830  18.689  13.145  1.00 341.68 ? 682  LYS A O   1 
ATOM   5179  C  CB  . LYS A 1 682  ? 57.342  17.891  15.815  1.00 335.11 ? 682  LYS A CB  1 
ATOM   5180  C  CG  . LYS A 1 682  ? 58.279  17.987  14.623  1.00 332.72 ? 682  LYS A CG  1 
ATOM   5181  C  CD  . LYS A 1 682  ? 58.411  19.417  14.126  1.00 330.14 ? 682  LYS A CD  1 
ATOM   5182  C  CE  . LYS A 1 682  ? 59.135  19.464  12.790  1.00 328.67 ? 682  LYS A CE  1 
ATOM   5183  N  NZ  . LYS A 1 682  ? 59.218  20.847  12.241  1.00 327.22 ? 682  LYS A NZ  1 
ATOM   5184  N  N   . ILE A 1 683  ? 54.932  16.753  13.868  1.00 414.73 ? 683  ILE A N   1 
ATOM   5185  C  CA  . ILE A 1 683  ? 54.520  16.303  12.541  1.00 420.91 ? 683  ILE A CA  1 
ATOM   5186  C  C   . ILE A 1 683  ? 53.117  16.814  12.167  1.00 426.43 ? 683  ILE A C   1 
ATOM   5187  O  O   . ILE A 1 683  ? 52.879  17.196  11.018  1.00 429.21 ? 683  ILE A O   1 
ATOM   5188  C  CB  . ILE A 1 683  ? 54.568  14.756  12.430  1.00 384.56 ? 683  ILE A CB  1 
ATOM   5189  C  CG1 . ILE A 1 683  ? 55.707  14.185  13.284  1.00 381.29 ? 683  ILE A CG1 1 
ATOM   5190  C  CG2 . ILE A 1 683  ? 54.708  14.328  10.976  1.00 386.93 ? 683  ILE A CG2 1 
ATOM   5191  C  CD1 . ILE A 1 683  ? 55.665  12.675  13.437  1.00 381.23 ? 683  ILE A CD1 1 
ATOM   5192  N  N   . GLU A 1 684  ? 52.201  16.833  13.139  1.00 350.68 ? 684  GLU A N   1 
ATOM   5193  C  CA  . GLU A 1 684  ? 50.799  17.218  12.900  1.00 354.20 ? 684  GLU A CA  1 
ATOM   5194  C  C   . GLU A 1 684  ? 50.584  18.705  12.559  1.00 350.21 ? 684  GLU A C   1 
ATOM   5195  O  O   . GLU A 1 684  ? 49.483  19.111  12.173  1.00 351.00 ? 684  GLU A O   1 
ATOM   5196  C  CB  . GLU A 1 684  ? 49.896  16.790  14.073  1.00 360.51 ? 684  GLU A CB  1 
ATOM   5197  C  CG  . GLU A 1 684  ? 49.699  15.275  14.205  1.00 367.12 ? 684  GLU A CG  1 
ATOM   5198  C  CD  . GLU A 1 684  ? 48.465  14.908  15.009  1.00 372.95 ? 684  GLU A CD  1 
ATOM   5199  O  OE1 . GLU A 1 684  ? 47.817  15.821  15.560  1.00 373.97 ? 684  GLU A OE1 1 
ATOM   5200  O  OE2 . GLU A 1 684  ? 48.138  13.706  15.086  1.00 376.34 ? 684  GLU A OE2 1 
ATOM   5201  N  N   . GLU A 1 685  ? 51.637  19.507  12.710  1.00 293.79 ? 685  GLU A N   1 
ATOM   5202  C  CA  . GLU A 1 685  ? 51.625  20.910  12.300  1.00 291.33 ? 685  GLU A CA  1 
ATOM   5203  C  C   . GLU A 1 685  ? 51.610  21.001  10.778  1.00 288.36 ? 685  GLU A C   1 
ATOM   5204  O  O   . GLU A 1 685  ? 50.945  21.853  10.183  1.00 289.45 ? 685  GLU A O   1 
ATOM   5205  C  CB  . GLU A 1 685  ? 52.872  21.622  12.838  1.00 290.54 ? 685  GLU A CB  1 
ATOM   5206  C  CG  . GLU A 1 685  ? 54.184  21.059  12.292  1.00 290.16 ? 685  GLU A CG  1 
ATOM   5207  C  CD  . GLU A 1 685  ? 55.414  21.608  12.987  1.00 289.12 ? 685  GLU A CD  1 
ATOM   5208  O  OE1 . GLU A 1 685  ? 55.262  22.312  14.003  1.00 288.82 ? 685  GLU A OE1 1 
ATOM   5209  O  OE2 . GLU A 1 685  ? 56.536  21.329  12.516  1.00 288.63 ? 685  GLU A OE2 1 
ATOM   5210  N  N   . ILE A 1 686  ? 52.358  20.100  10.159  1.00 252.94 ? 686  ILE A N   1 
ATOM   5211  C  CA  . ILE A 1 686  ? 52.498  20.074  8.721   1.00 250.30 ? 686  ILE A CA  1 
ATOM   5212  C  C   . ILE A 1 686  ? 51.195  19.601  8.078   1.00 249.16 ? 686  ILE A C   1 
ATOM   5213  O  O   . ILE A 1 686  ? 51.179  19.170  6.926   1.00 251.33 ? 686  ILE A O   1 
ATOM   5214  C  CB  . ILE A 1 686  ? 53.688  19.198  8.312   1.00 249.60 ? 686  ILE A CB  1 
ATOM   5215  C  CG1 . ILE A 1 686  ? 54.877  19.475  9.233   1.00 246.86 ? 686  ILE A CG1 1 
ATOM   5216  C  CG2 . ILE A 1 686  ? 54.079  19.463  6.876   1.00 250.61 ? 686  ILE A CG2 1 
ATOM   5217  C  CD1 . ILE A 1 686  ? 55.385  20.904  9.170   1.00 245.21 ? 686  ILE A CD1 1 
ATOM   5218  N  N   . ALA A 1 687  ? 50.104  19.674  8.840   1.00 291.61 ? 687  ALA A N   1 
ATOM   5219  C  CA  . ALA A 1 687  ? 48.764  19.600  8.269   1.00 287.98 ? 687  ALA A CA  1 
ATOM   5220  C  C   . ALA A 1 687  ? 48.604  20.895  7.505   1.00 282.93 ? 687  ALA A C   1 
ATOM   5221  O  O   . ALA A 1 687  ? 47.570  21.154  6.881   1.00 283.23 ? 687  ALA A O   1 
ATOM   5222  C  CB  . ALA A 1 687  ? 47.723  19.498  9.354   1.00 288.15 ? 687  ALA A CB  1 
ATOM   5223  N  N   . ALA A 1 688  ? 49.661  21.704  7.597   1.00 289.72 ? 688  ALA A N   1 
ATOM   5224  C  CA  . ALA A 1 688  ? 49.834  22.949  6.857   1.00 285.99 ? 688  ALA A CA  1 
ATOM   5225  C  C   . ALA A 1 688  ? 49.894  22.745  5.337   1.00 284.79 ? 688  ALA A C   1 
ATOM   5226  O  O   . ALA A 1 688  ? 49.721  23.697  4.570   1.00 283.67 ? 688  ALA A O   1 
ATOM   5227  C  CB  . ALA A 1 688  ? 51.097  23.664  7.345   1.00 283.52 ? 688  ALA A CB  1 
ATOM   5228  N  N   . LYS A 1 689  ? 50.159  21.514  4.906   1.00 251.67 ? 689  LYS A N   1 
ATOM   5229  C  CA  . LYS A 1 689  ? 50.145  21.187  3.480   1.00 254.28 ? 689  LYS A CA  1 
ATOM   5230  C  C   . LYS A 1 689  ? 48.776  20.689  2.999   1.00 263.48 ? 689  LYS A C   1 
ATOM   5231  O  O   . LYS A 1 689  ? 48.682  20.034  1.957   1.00 266.68 ? 689  LYS A O   1 
ATOM   5232  C  CB  . LYS A 1 689  ? 51.264  20.195  3.114   1.00 246.82 ? 689  LYS A CB  1 
ATOM   5233  C  CG  . LYS A 1 689  ? 51.416  19.011  4.056   1.00 240.63 ? 689  LYS A CG  1 
ATOM   5234  C  CD  . LYS A 1 689  ? 52.686  18.237  3.755   1.00 235.37 ? 689  LYS A CD  1 
ATOM   5235  C  CE  . LYS A 1 689  ? 53.883  19.166  3.680   1.00 229.76 ? 689  LYS A CE  1 
ATOM   5236  N  NZ  . LYS A 1 689  ? 55.123  18.429  3.321   1.00 226.94 ? 689  LYS A NZ  1 
ATOM   5237  N  N   . TYR A 1 690  ? 47.721  20.995  3.756   1.00 334.50 ? 690  TYR A N   1 
ATOM   5238  C  CA  . TYR A 1 690  ? 46.364  20.650  3.333   1.00 345.43 ? 690  TYR A CA  1 
ATOM   5239  C  C   . TYR A 1 690  ? 46.021  21.333  2.014   1.00 349.73 ? 690  TYR A C   1 
ATOM   5240  O  O   . TYR A 1 690  ? 46.305  22.512  1.811   1.00 348.29 ? 690  TYR A O   1 
ATOM   5241  C  CB  . TYR A 1 690  ? 45.311  21.006  4.390   1.00 352.59 ? 690  TYR A CB  1 
ATOM   5242  C  CG  . TYR A 1 690  ? 43.929  21.175  3.789   1.00 363.31 ? 690  TYR A CG  1 
ATOM   5243  C  CD1 . TYR A 1 690  ? 43.225  20.084  3.299   1.00 368.67 ? 690  TYR A CD1 1 
ATOM   5244  C  CD2 . TYR A 1 690  ? 43.341  22.429  3.688   1.00 367.20 ? 690  TYR A CD2 1 
ATOM   5245  C  CE1 . TYR A 1 690  ? 41.971  20.235  2.736   1.00 374.72 ? 690  TYR A CE1 1 
ATOM   5246  C  CE2 . TYR A 1 690  ? 42.087  22.589  3.128   1.00 373.21 ? 690  TYR A CE2 1 
ATOM   5247  C  CZ  . TYR A 1 690  ? 41.406  21.490  2.654   1.00 376.95 ? 690  TYR A CZ  1 
ATOM   5248  O  OH  . TYR A 1 690  ? 40.156  21.645  2.097   1.00 382.11 ? 690  TYR A OH  1 
ATOM   5249  N  N   . LYS A 1 691  ? 45.402  20.573  1.124   1.00 304.57 ? 691  LYS A N   1 
ATOM   5250  C  CA  . LYS A 1 691  ? 45.035  21.048  -0.197  1.00 308.31 ? 691  LYS A CA  1 
ATOM   5251  C  C   . LYS A 1 691  ? 44.097  19.981  -0.708  1.00 313.57 ? 691  LYS A C   1 
ATOM   5252  O  O   . LYS A 1 691  ? 43.572  20.046  -1.818  1.00 316.60 ? 691  LYS A O   1 
ATOM   5253  C  CB  . LYS A 1 691  ? 46.274  21.192  -1.090  1.00 306.82 ? 691  LYS A CB  1 
ATOM   5254  C  CG  . LYS A 1 691  ? 47.280  20.046  -0.971  1.00 303.33 ? 691  LYS A CG  1 
ATOM   5255  C  CD  . LYS A 1 691  ? 48.643  20.410  -1.559  1.00 299.67 ? 691  LYS A CD  1 
ATOM   5256  C  CE  . LYS A 1 691  ? 49.685  19.348  -1.225  1.00 296.49 ? 691  LYS A CE  1 
ATOM   5257  N  NZ  . LYS A 1 691  ? 51.063  19.770  -1.594  1.00 293.83 ? 691  LYS A NZ  1 
ATOM   5258  N  N   . HIS A 1 692  ? 43.901  18.991  0.150   1.00 262.72 ? 692  HIS A N   1 
ATOM   5259  C  CA  . HIS A 1 692  ? 42.996  17.892  -0.097  1.00 265.85 ? 692  HIS A CA  1 
ATOM   5260  C  C   . HIS A 1 692  ? 43.120  16.945  1.073   1.00 259.43 ? 692  HIS A C   1 
ATOM   5261  O  O   . HIS A 1 692  ? 44.161  16.880  1.729   1.00 254.01 ? 692  HIS A O   1 
ATOM   5262  C  CB  . HIS A 1 692  ? 43.356  17.165  -1.388  1.00 272.63 ? 692  HIS A CB  1 
ATOM   5263  C  CG  . HIS A 1 692  ? 42.405  16.061  -1.743  1.00 282.53 ? 692  HIS A CG  1 
ATOM   5264  N  ND1 . HIS A 1 692  ? 41.071  16.284  -2.001  1.00 289.15 ? 692  HIS A ND1 1 
ATOM   5265  C  CD2 . HIS A 1 692  ? 42.603  14.730  -1.901  1.00 286.69 ? 692  HIS A CD2 1 
ATOM   5266  C  CE1 . HIS A 1 692  ? 40.483  15.137  -2.294  1.00 294.34 ? 692  HIS A CE1 1 
ATOM   5267  N  NE2 . HIS A 1 692  ? 41.390  14.179  -2.241  1.00 292.91 ? 692  HIS A NE2 1 
ATOM   5268  N  N   . SER A 1 693  ? 42.051  16.209  1.333   1.00 298.34 ? 693  SER A N   1 
ATOM   5269  C  CA  . SER A 1 693  ? 42.051  15.237  2.407   1.00 293.28 ? 693  SER A CA  1 
ATOM   5270  C  C   . SER A 1 693  ? 43.165  14.217  2.218   1.00 285.38 ? 693  SER A C   1 
ATOM   5271  O  O   . SER A 1 693  ? 44.004  14.029  3.100   1.00 281.83 ? 693  SER A O   1 
ATOM   5272  C  CB  . SER A 1 693  ? 40.705  14.519  2.452   1.00 298.31 ? 693  SER A CB  1 
ATOM   5273  O  OG  . SER A 1 693  ? 40.757  13.421  3.344   1.00 298.08 ? 693  SER A OG  1 
ATOM   5274  N  N   . VAL A 1 694  ? 43.168  13.574  1.053   1.00 393.14 ? 694  VAL A N   1 
ATOM   5275  C  CA  . VAL A 1 694  ? 44.064  12.453  0.784   1.00 388.26 ? 694  VAL A CA  1 
ATOM   5276  C  C   . VAL A 1 694  ? 45.530  12.794  1.038   1.00 379.97 ? 694  VAL A C   1 
ATOM   5277  O  O   . VAL A 1 694  ? 46.313  11.918  1.400   1.00 378.80 ? 694  VAL A O   1 
ATOM   5278  C  CB  . VAL A 1 694  ? 43.903  11.911  -0.659  1.00 385.59 ? 694  VAL A CB  1 
ATOM   5279  C  CG1 . VAL A 1 694  ? 44.741  10.658  -0.852  1.00 385.66 ? 694  VAL A CG1 1 
ATOM   5280  C  CG2 . VAL A 1 694  ? 42.442  11.618  -0.961  1.00 390.37 ? 694  VAL A CG2 1 
ATOM   5281  N  N   . VAL A 1 695  ? 45.907  14.057  0.851   1.00 245.17 ? 695  VAL A N   1 
ATOM   5282  C  CA  . VAL A 1 695  ? 47.284  14.448  1.116   1.00 238.19 ? 695  VAL A CA  1 
ATOM   5283  C  C   . VAL A 1 695  ? 47.525  14.365  2.608   1.00 233.31 ? 695  VAL A C   1 
ATOM   5284  O  O   . VAL A 1 695  ? 48.604  13.969  3.037   1.00 230.07 ? 695  VAL A O   1 
ATOM   5285  C  CB  . VAL A 1 695  ? 47.634  15.853  0.583   1.00 237.07 ? 695  VAL A CB  1 
ATOM   5286  C  CG1 . VAL A 1 695  ? 49.023  16.258  1.041   1.00 232.51 ? 695  VAL A CG1 1 
ATOM   5287  C  CG2 . VAL A 1 695  ? 47.561  15.883  -0.942  1.00 239.52 ? 695  VAL A CG2 1 
ATOM   5288  N  N   . LYS A 1 696  ? 46.511  14.726  3.392   1.00 357.69 ? 696  LYS A N   1 
ATOM   5289  C  CA  . LYS A 1 696  ? 46.556  14.522  4.834   1.00 354.69 ? 696  LYS A CA  1 
ATOM   5290  C  C   . LYS A 1 696  ? 46.788  13.041  5.119   1.00 355.47 ? 696  LYS A C   1 
ATOM   5291  O  O   . LYS A 1 696  ? 47.551  12.693  6.022   1.00 353.18 ? 696  LYS A O   1 
ATOM   5292  C  CB  . LYS A 1 696  ? 45.267  15.013  5.504   1.00 356.35 ? 696  LYS A CB  1 
ATOM   5293  C  CG  . LYS A 1 696  ? 44.982  14.409  6.885   1.00 356.76 ? 696  LYS A CG  1 
ATOM   5294  C  CD  . LYS A 1 696  ? 45.835  15.012  8.002   1.00 348.15 ? 696  LYS A CD  1 
ATOM   5295  C  CE  . LYS A 1 696  ? 45.400  14.479  9.373   1.00 347.31 ? 696  LYS A CE  1 
ATOM   5296  N  NZ  . LYS A 1 696  ? 46.153  15.092  10.510  1.00 341.96 ? 696  LYS A NZ  1 
ATOM   5297  N  N   . LYS A 1 697  ? 46.139  12.175  4.337   1.00 204.73 ? 697  LYS A N   1 
ATOM   5298  C  CA  . LYS A 1 697  ? 46.381  10.727  4.416   1.00 205.32 ? 697  LYS A CA  1 
ATOM   5299  C  C   . LYS A 1 697  ? 47.766  10.354  3.873   1.00 202.36 ? 697  LYS A C   1 
ATOM   5300  O  O   . LYS A 1 697  ? 48.349  9.350   4.282   1.00 203.20 ? 697  LYS A O   1 
ATOM   5301  C  CB  . LYS A 1 697  ? 45.295  9.930   3.677   1.00 210.35 ? 697  LYS A CB  1 
ATOM   5302  C  CG  . LYS A 1 697  ? 45.438  8.405   3.779   1.00 212.80 ? 697  LYS A CG  1 
ATOM   5303  C  CD  . LYS A 1 697  ? 45.027  7.909   5.160   1.00 212.29 ? 697  LYS A CD  1 
ATOM   5304  C  CE  . LYS A 1 697  ? 45.155  6.395   5.314   1.00 210.81 ? 697  LYS A CE  1 
ATOM   5305  N  NZ  . LYS A 1 697  ? 44.563  5.905   6.608   1.00 210.29 ? 697  LYS A NZ  1 
ATOM   5306  N  N   . CYS A 1 698  ? 48.286  11.163  2.950   1.00 235.03 ? 698  CYS A N   1 
ATOM   5307  C  CA  . CYS A 1 698  ? 49.611  10.927  2.373   1.00 232.41 ? 698  CYS A CA  1 
ATOM   5308  C  C   . CYS A 1 698  ? 50.690  11.146  3.423   1.00 226.89 ? 698  CYS A C   1 
ATOM   5309  O  O   . CYS A 1 698  ? 51.727  10.479  3.444   1.00 224.06 ? 698  CYS A O   1 
ATOM   5310  C  CB  . CYS A 1 698  ? 49.850  11.844  1.162   1.00 231.46 ? 698  CYS A CB  1 
ATOM   5311  S  SG  . CYS A 1 698  ? 48.562  11.790  -0.164  1.00 268.45 ? 698  CYS A SG  1 
ATOM   5312  N  N   . CYS A 1 699  ? 50.418  12.094  4.303   1.00 262.96 ? 699  CYS A N   1 
ATOM   5313  C  CA  . CYS A 1 699  ? 51.348  12.452  5.351   1.00 263.02 ? 699  CYS A CA  1 
ATOM   5314  C  C   . CYS A 1 699  ? 51.130  11.608  6.602   1.00 266.90 ? 699  CYS A C   1 
ATOM   5315  O  O   . CYS A 1 699  ? 52.083  11.064  7.153   1.00 265.41 ? 699  CYS A O   1 
ATOM   5316  C  CB  . CYS A 1 699  ? 51.189  13.928  5.690   1.00 262.31 ? 699  CYS A CB  1 
ATOM   5317  S  SG  . CYS A 1 699  ? 52.708  14.719  6.180   1.00 257.48 ? 699  CYS A SG  1 
ATOM   5318  N  N   . TYR A 1 700  ? 49.875  11.506  7.039   1.00 201.74 ? 700  TYR A N   1 
ATOM   5319  C  CA  . TYR A 1 700  ? 49.538  10.830  8.295   1.00 209.75 ? 700  TYR A CA  1 
ATOM   5320  C  C   . TYR A 1 700  ? 50.182  9.445   8.331   1.00 214.78 ? 700  TYR A C   1 
ATOM   5321  O  O   . TYR A 1 700  ? 51.312  9.291   8.789   1.00 212.96 ? 700  TYR A O   1 
ATOM   5322  C  CB  . TYR A 1 700  ? 48.007  10.767  8.514   1.00 218.97 ? 700  TYR A CB  1 
ATOM   5323  C  CG  . TYR A 1 700  ? 47.545  10.985  9.959   1.00 225.81 ? 700  TYR A CG  1 
ATOM   5324  C  CD1 . TYR A 1 700  ? 46.949  9.959   10.682  1.00 232.19 ? 700  TYR A CD1 1 
ATOM   5325  C  CD2 . TYR A 1 700  ? 47.708  12.223  10.596  1.00 226.05 ? 700  TYR A CD2 1 
ATOM   5326  C  CE1 . TYR A 1 700  ? 46.536  10.156  12.002  1.00 234.41 ? 700  TYR A CE1 1 
ATOM   5327  C  CE2 . TYR A 1 700  ? 47.295  12.426  11.919  1.00 228.44 ? 700  TYR A CE2 1 
ATOM   5328  C  CZ  . TYR A 1 700  ? 46.709  11.390  12.612  1.00 232.48 ? 700  TYR A CZ  1 
ATOM   5329  O  OH  . TYR A 1 700  ? 46.298  11.585  13.913  1.00 233.30 ? 700  TYR A OH  1 
ATOM   5330  N  N   . ASP A 1 701  ? 49.487  8.440   7.821   1.00 250.33 ? 701  ASP A N   1 
ATOM   5331  C  CA  . ASP A 1 701  ? 50.102  7.131   7.668   1.00 248.99 ? 701  ASP A CA  1 
ATOM   5332  C  C   . ASP A 1 701  ? 51.485  7.308   7.065   1.00 245.00 ? 701  ASP A C   1 
ATOM   5333  O  O   . ASP A 1 701  ? 52.343  6.432   7.171   1.00 242.99 ? 701  ASP A O   1 
ATOM   5334  C  CB  . ASP A 1 701  ? 49.247  6.228   6.766   1.00 252.07 ? 701  ASP A CB  1 
ATOM   5335  C  CG  . ASP A 1 701  ? 49.140  6.745   5.321   1.00 254.71 ? 701  ASP A CG  1 
ATOM   5336  O  OD1 . ASP A 1 701  ? 49.998  7.556   4.902   1.00 254.63 ? 701  ASP A OD1 1 
ATOM   5337  O  OD2 . ASP A 1 701  ? 48.199  6.326   4.598   1.00 256.87 ? 701  ASP A OD2 1 
ATOM   5338  N  N   . GLY A 1 702  ? 51.679  8.458   6.425   1.00 279.93 ? 702  GLY A N   1 
ATOM   5339  C  CA  . GLY A 1 702  ? 52.906  8.762   5.725   1.00 274.61 ? 702  GLY A CA  1 
ATOM   5340  C  C   . GLY A 1 702  ? 54.108  8.277   6.499   1.00 267.94 ? 702  GLY A C   1 
ATOM   5341  O  O   . GLY A 1 702  ? 54.743  7.301   6.110   1.00 264.87 ? 702  GLY A O   1 
ATOM   5342  N  N   . ALA A 1 703  ? 54.414  8.942   7.607   1.00 171.85 ? 703  ALA A N   1 
ATOM   5343  C  CA  . ALA A 1 703  ? 55.549  8.539   8.418   1.00 174.02 ? 703  ALA A CA  1 
ATOM   5344  C  C   . ALA A 1 703  ? 55.319  7.160   9.039   1.00 169.84 ? 703  ALA A C   1 
ATOM   5345  O  O   . ALA A 1 703  ? 56.274  6.392   9.228   1.00 169.13 ? 703  ALA A O   1 
ATOM   5346  C  CB  . ALA A 1 703  ? 55.798  9.566   9.488   1.00 175.12 ? 703  ALA A CB  1 
ATOM   5347  N  N   . CYS A 1 704  ? 54.041  6.852   9.294   1.00 215.52 ? 704  CYS A N   1 
ATOM   5348  C  CA  . CYS A 1 704  ? 53.587  5.760   10.184  1.00 211.92 ? 704  CYS A CA  1 
ATOM   5349  C  C   . CYS A 1 704  ? 54.674  5.074   11.036  1.00 208.55 ? 704  CYS A C   1 
ATOM   5350  O  O   . CYS A 1 704  ? 55.062  5.598   12.080  1.00 207.71 ? 704  CYS A O   1 
ATOM   5351  C  CB  . CYS A 1 704  ? 52.684  4.742   9.465   1.00 211.50 ? 704  CYS A CB  1 
ATOM   5352  S  SG  . CYS A 1 704  ? 51.431  3.973   10.544  1.00 187.16 ? 704  CYS A SG  1 
ATOM   5353  N  N   . VAL A 1 705  ? 55.156  3.908   10.622  1.00 222.58 ? 705  VAL A N   1 
ATOM   5354  C  CA  . VAL A 1 705  ? 56.184  3.213   11.401  1.00 220.38 ? 705  VAL A CA  1 
ATOM   5355  C  C   . VAL A 1 705  ? 56.947  2.191   10.571  1.00 221.58 ? 705  VAL A C   1 
ATOM   5356  O  O   . VAL A 1 705  ? 56.865  0.989   10.830  1.00 223.08 ? 705  VAL A O   1 
ATOM   5357  C  CB  . VAL A 1 705  ? 55.596  2.501   12.659  1.00 217.12 ? 705  VAL A CB  1 
ATOM   5358  C  CG1 . VAL A 1 705  ? 55.772  3.358   13.908  1.00 217.36 ? 705  VAL A CG1 1 
ATOM   5359  C  CG2 . VAL A 1 705  ? 54.134  2.132   12.448  1.00 217.72 ? 705  VAL A CG2 1 
ATOM   5360  N  N   . ASN A 1 706  ? 57.691  2.660   9.575   1.00 289.56 ? 706  ASN A N   1 
ATOM   5361  C  CA  . ASN A 1 706  ? 58.392  1.730   8.703   1.00 290.32 ? 706  ASN A CA  1 
ATOM   5362  C  C   . ASN A 1 706  ? 59.902  1.873   8.733   1.00 286.43 ? 706  ASN A C   1 
ATOM   5363  O  O   . ASN A 1 706  ? 60.465  2.868   8.273   1.00 286.92 ? 706  ASN A O   1 
ATOM   5364  C  CB  . ASN A 1 706  ? 57.858  1.798   7.272   1.00 295.83 ? 706  ASN A CB  1 
ATOM   5365  C  CG  . ASN A 1 706  ? 57.547  0.427   6.704   1.00 298.83 ? 706  ASN A CG  1 
ATOM   5366  O  OD1 . ASN A 1 706  ? 57.977  -0.593  7.247   1.00 298.27 ? 706  ASN A OD1 1 
ATOM   5367  N  ND2 . ASN A 1 706  ? 56.793  0.394   5.610   1.00 302.32 ? 706  ASN A ND2 1 
ATOM   5368  N  N   . ASN A 1 707  ? 60.540  0.845   9.280   1.00 265.31 ? 707  ASN A N   1 
ATOM   5369  C  CA  . ASN A 1 707  ? 61.984  0.801   9.439   1.00 262.23 ? 707  ASN A CA  1 
ATOM   5370  C  C   . ASN A 1 707  ? 62.681  -0.238  8.557   1.00 258.13 ? 707  ASN A C   1 
ATOM   5371  O  O   . ASN A 1 707  ? 63.904  -0.341  8.577   1.00 254.11 ? 707  ASN A O   1 
ATOM   5372  C  CB  . ASN A 1 707  ? 62.368  0.598   10.916  1.00 262.85 ? 707  ASN A CB  1 
ATOM   5373  C  CG  . ASN A 1 707  ? 61.372  -0.273  11.681  1.00 263.27 ? 707  ASN A CG  1 
ATOM   5374  O  OD1 . ASN A 1 707  ? 60.325  -0.655  11.158  1.00 264.27 ? 707  ASN A OD1 1 
ATOM   5375  N  ND2 . ASN A 1 707  ? 61.698  -0.579  12.936  1.00 262.08 ? 707  ASN A ND2 1 
ATOM   5376  N  N   . ASP A 1 708  ? 61.911  -1.006  7.789   1.00 241.96 ? 708  ASP A N   1 
ATOM   5377  C  CA  . ASP A 1 708  ? 62.485  -2.041  6.917   1.00 238.72 ? 708  ASP A CA  1 
ATOM   5378  C  C   . ASP A 1 708  ? 62.797  -1.540  5.501   1.00 239.53 ? 708  ASP A C   1 
ATOM   5379  O  O   . ASP A 1 708  ? 63.268  -2.295  4.653   1.00 238.40 ? 708  ASP A O   1 
ATOM   5380  C  CB  . ASP A 1 708  ? 61.574  -3.273  6.846   1.00 234.00 ? 708  ASP A CB  1 
ATOM   5381  C  CG  . ASP A 1 708  ? 61.962  -4.356  7.846   1.00 224.88 ? 708  ASP A CG  1 
ATOM   5382  O  OD1 . ASP A 1 708  ? 62.816  -4.094  8.714   1.00 218.89 ? 708  ASP A OD1 1 
ATOM   5383  O  OD2 . ASP A 1 708  ? 61.414  -5.475  7.761   1.00 222.60 ? 708  ASP A OD2 1 
ATOM   5384  N  N   . GLU A 1 709  ? 62.530  -0.270  5.244   1.00 226.00 ? 709  GLU A N   1 
ATOM   5385  C  CA  . GLU A 1 709  ? 62.770  0.277   3.926   1.00 229.69 ? 709  GLU A CA  1 
ATOM   5386  C  C   . GLU A 1 709  ? 62.712  1.790   3.981   1.00 231.99 ? 709  GLU A C   1 
ATOM   5387  O  O   . GLU A 1 709  ? 61.913  2.355   4.720   1.00 235.60 ? 709  GLU A O   1 
ATOM   5388  C  CB  . GLU A 1 709  ? 61.754  -0.280  2.925   1.00 233.46 ? 709  GLU A CB  1 
ATOM   5389  C  CG  . GLU A 1 709  ? 60.306  -0.297  3.416   1.00 235.18 ? 709  GLU A CG  1 
ATOM   5390  C  CD  . GLU A 1 709  ? 59.306  -0.781  2.353   1.00 237.07 ? 709  GLU A CD  1 
ATOM   5391  O  OE1 . GLU A 1 709  ? 59.609  -0.680  1.141   1.00 237.46 ? 709  GLU A OE1 1 
ATOM   5392  O  OE2 . GLU A 1 709  ? 58.210  -1.255  2.732   1.00 237.45 ? 709  GLU A OE2 1 
ATOM   5393  N  N   . THR A 1 710  ? 63.565  2.441   3.198   1.00 238.66 ? 710  THR A N   1 
ATOM   5394  C  CA  . THR A 1 710  ? 63.728  3.884   3.275   1.00 241.29 ? 710  THR A CA  1 
ATOM   5395  C  C   . THR A 1 710  ? 62.420  4.602   3.053   1.00 246.97 ? 710  THR A C   1 
ATOM   5396  O  O   . THR A 1 710  ? 61.383  3.985   2.840   1.00 247.44 ? 710  THR A O   1 
ATOM   5397  C  CB  . THR A 1 710  ? 64.724  4.416   2.243   1.00 262.94 ? 710  THR A CB  1 
ATOM   5398  O  OG1 . THR A 1 710  ? 64.022  4.795   1.052   1.00 264.89 ? 710  THR A OG1 1 
ATOM   5399  C  CG2 . THR A 1 710  ? 65.776  3.370   1.924   1.00 261.93 ? 710  THR A CG2 1 
ATOM   5400  N  N   . CYS A 1 711  ? 62.474  5.922   3.108   1.00 231.19 ? 711  CYS A N   1 
ATOM   5401  C  CA  . CYS A 1 711  ? 61.260  6.692   2.956   1.00 236.95 ? 711  CYS A CA  1 
ATOM   5402  C  C   . CYS A 1 711  ? 60.933  6.978   1.494   1.00 239.76 ? 711  CYS A C   1 
ATOM   5403  O  O   . CYS A 1 711  ? 59.791  7.290   1.177   1.00 243.29 ? 711  CYS A O   1 
ATOM   5404  C  CB  . CYS A 1 711  ? 61.295  7.972   3.798   1.00 239.73 ? 711  CYS A CB  1 
ATOM   5405  S  SG  . CYS A 1 711  ? 60.286  7.883   5.317   1.00 238.08 ? 711  CYS A SG  1 
ATOM   5406  N  N   . GLU A 1 712  ? 61.911  6.859   0.601   1.00 237.61 ? 712  GLU A N   1 
ATOM   5407  C  CA  . GLU A 1 712  ? 61.623  7.006   -0.830  1.00 239.83 ? 712  GLU A CA  1 
ATOM   5408  C  C   . GLU A 1 712  ? 61.514  5.661   -1.544  1.00 234.50 ? 712  GLU A C   1 
ATOM   5409  O  O   . GLU A 1 712  ? 61.214  5.592   -2.739  1.00 234.64 ? 712  GLU A O   1 
ATOM   5410  C  CB  . GLU A 1 712  ? 62.640  7.910   -1.502  1.00 247.59 ? 712  GLU A CB  1 
ATOM   5411  C  CG  . GLU A 1 712  ? 63.944  7.977   -0.770  1.00 251.51 ? 712  GLU A CG  1 
ATOM   5412  C  CD  . GLU A 1 712  ? 64.844  9.017   -1.358  1.00 257.96 ? 712  GLU A CD  1 
ATOM   5413  O  OE1 . GLU A 1 712  ? 64.750  10.181  -0.928  1.00 259.80 ? 712  GLU A OE1 1 
ATOM   5414  O  OE2 . GLU A 1 712  ? 65.627  8.672   -2.263  1.00 259.54 ? 712  GLU A OE2 1 
ATOM   5415  N  N   . GLN A 1 713  ? 61.772  4.599   -0.786  1.00 276.70 ? 713  GLN A N   1 
ATOM   5416  C  CA  . GLN A 1 713  ? 61.430  3.240   -1.189  1.00 273.63 ? 713  GLN A CA  1 
ATOM   5417  C  C   . GLN A 1 713  ? 59.909  3.055   -1.088  1.00 271.26 ? 713  GLN A C   1 
ATOM   5418  O  O   . GLN A 1 713  ? 59.267  2.610   -2.035  1.00 273.43 ? 713  GLN A O   1 
ATOM   5419  C  CB  . GLN A 1 713  ? 62.150  2.213   -0.301  1.00 271.21 ? 713  GLN A CB  1 
ATOM   5420  C  CG  . GLN A 1 713  ? 63.668  2.134   -0.491  1.00 270.15 ? 713  GLN A CG  1 
ATOM   5421  C  CD  . GLN A 1 713  ? 64.337  1.122   0.438   1.00 267.67 ? 713  GLN A CD  1 
ATOM   5422  O  OE1 . GLN A 1 713  ? 63.879  0.881   1.548   1.00 266.27 ? 713  GLN A OE1 1 
ATOM   5423  N  NE2 . GLN A 1 713  ? 65.434  0.540   -0.017  1.00 267.26 ? 713  GLN A NE2 1 
ATOM   5424  N  N   . ARG A 1 714  ? 59.343  3.407   0.068   1.00 278.68 ? 714  ARG A N   1 
ATOM   5425  C  CA  . ARG A 1 714  ? 57.893  3.398   0.276   1.00 277.26 ? 714  ARG A CA  1 
ATOM   5426  C  C   . ARG A 1 714  ? 57.214  4.403   -0.655  1.00 275.85 ? 714  ARG A C   1 
ATOM   5427  O  O   . ARG A 1 714  ? 56.055  4.231   -1.033  1.00 275.98 ? 714  ARG A O   1 
ATOM   5428  C  CB  . ARG A 1 714  ? 57.558  3.765   1.729   1.00 277.64 ? 714  ARG A CB  1 
ATOM   5429  C  CG  . ARG A 1 714  ? 58.179  2.866   2.794   1.00 277.01 ? 714  ARG A CG  1 
ATOM   5430  C  CD  . ARG A 1 714  ? 58.467  3.633   4.096   1.00 278.66 ? 714  ARG A CD  1 
ATOM   5431  N  NE  . ARG A 1 714  ? 57.252  4.027   4.807   1.00 283.44 ? 714  ARG A NE  1 
ATOM   5432  C  CZ  . ARG A 1 714  ? 57.232  4.558   6.029   1.00 286.12 ? 714  ARG A CZ  1 
ATOM   5433  N  NH1 . ARG A 1 714  ? 58.361  4.759   6.704   1.00 284.57 ? 714  ARG A NH1 1 
ATOM   5434  N  NH2 . ARG A 1 714  ? 56.073  4.879   6.586   1.00 288.77 ? 714  ARG A NH2 1 
ATOM   5435  N  N   . ALA A 1 715  ? 57.957  5.454   -0.998  1.00 215.09 ? 715  ALA A N   1 
ATOM   5436  C  CA  . ALA A 1 715  ? 57.478  6.567   -1.817  1.00 215.31 ? 715  ALA A CA  1 
ATOM   5437  C  C   . ALA A 1 715  ? 57.432  6.189   -3.287  1.00 214.96 ? 715  ALA A C   1 
ATOM   5438  O  O   . ALA A 1 715  ? 56.930  6.940   -4.130  1.00 218.94 ? 715  ALA A O   1 
ATOM   5439  C  CB  . ALA A 1 715  ? 58.363  7.780   -1.621  1.00 211.53 ? 715  ALA A CB  1 
ATOM   5440  N  N   . ALA A 1 716  ? 57.975  5.020   -3.592  1.00 222.91 ? 716  ALA A N   1 
ATOM   5441  C  CA  . ALA A 1 716  ? 57.884  4.478   -4.934  1.00 226.46 ? 716  ALA A CA  1 
ATOM   5442  C  C   . ALA A 1 716  ? 56.488  3.895   -5.157  1.00 228.56 ? 716  ALA A C   1 
ATOM   5443  O  O   . ALA A 1 716  ? 55.751  4.331   -6.042  1.00 231.40 ? 716  ALA A O   1 
ATOM   5444  C  CB  . ALA A 1 716  ? 58.947  3.418   -5.131  1.00 224.93 ? 716  ALA A CB  1 
ATOM   5445  N  N   . ARG A 1 717  ? 56.134  2.931   -4.310  1.00 207.75 ? 717  ARG A N   1 
ATOM   5446  C  CA  . ARG A 1 717  ? 54.870  2.202   -4.371  1.00 211.39 ? 717  ARG A CA  1 
ATOM   5447  C  C   . ARG A 1 717  ? 53.662  3.126   -4.378  1.00 213.32 ? 717  ARG A C   1 
ATOM   5448  O  O   . ARG A 1 717  ? 52.517  2.670   -4.459  1.00 214.31 ? 717  ARG A O   1 
ATOM   5449  C  CB  . ARG A 1 717  ? 54.783  1.277   -3.162  1.00 205.47 ? 717  ARG A CB  1 
ATOM   5450  C  CG  . ARG A 1 717  ? 54.034  -0.014  -3.366  1.00 209.30 ? 717  ARG A CG  1 
ATOM   5451  C  CD  . ARG A 1 717  ? 54.264  -0.899  -2.163  1.00 208.10 ? 717  ARG A CD  1 
ATOM   5452  N  NE  . ARG A 1 717  ? 55.657  -0.853  -1.713  1.00 204.35 ? 717  ARG A NE  1 
ATOM   5453  C  CZ  . ARG A 1 717  ? 56.106  -0.107  -0.698  1.00 200.38 ? 717  ARG A CZ  1 
ATOM   5454  N  NH1 . ARG A 1 717  ? 55.276  0.667   -0.010  1.00 199.73 ? 717  ARG A NH1 1 
ATOM   5455  N  NH2 . ARG A 1 717  ? 57.393  -0.130  -0.365  1.00 198.17 ? 717  ARG A NH2 1 
ATOM   5456  N  N   . ILE A 1 718  ? 53.928  4.424   -4.269  1.00 238.02 ? 718  ILE A N   1 
ATOM   5457  C  CA  . ILE A 1 718  ? 52.880  5.436   -4.217  1.00 243.34 ? 718  ILE A CA  1 
ATOM   5458  C  C   . ILE A 1 718  ? 52.333  5.801   -5.596  1.00 251.88 ? 718  ILE A C   1 
ATOM   5459  O  O   . ILE A 1 718  ? 53.058  6.283   -6.474  1.00 250.62 ? 718  ILE A O   1 
ATOM   5460  C  CB  . ILE A 1 718  ? 53.326  6.698   -3.433  1.00 239.95 ? 718  ILE A CB  1 
ATOM   5461  C  CG1 . ILE A 1 718  ? 53.172  6.461   -1.927  1.00 239.14 ? 718  ILE A CG1 1 
ATOM   5462  C  CG2 . ILE A 1 718  ? 52.519  7.915   -3.849  1.00 242.27 ? 718  ILE A CG2 1 
ATOM   5463  C  CD1 . ILE A 1 718  ? 53.259  7.716   -1.102  1.00 240.30 ? 718  ILE A CD1 1 
ATOM   5464  N  N   . SER A 1 719  ? 51.033  5.558   -5.738  1.00 197.03 ? 719  SER A N   1 
ATOM   5465  C  CA  . SER A 1 719  ? 50.284  5.727   -6.967  1.00 199.87 ? 719  SER A CA  1 
ATOM   5466  C  C   . SER A 1 719  ? 49.514  7.038   -6.980  1.00 199.77 ? 719  SER A C   1 
ATOM   5467  O  O   . SER A 1 719  ? 49.982  8.044   -7.513  1.00 198.75 ? 719  SER A O   1 
ATOM   5468  C  CB  . SER A 1 719  ? 49.285  4.579   -7.084  1.00 203.15 ? 719  SER A CB  1 
ATOM   5469  O  OG  . SER A 1 719  ? 48.499  4.690   -8.256  1.00 206.13 ? 719  SER A OG  1 
ATOM   5470  N  N   . LEU A 1 720  ? 48.327  6.989   -6.381  1.00 233.88 ? 720  LEU A N   1 
ATOM   5471  C  CA  . LEU A 1 720  ? 47.366  8.096   -6.322  1.00 245.51 ? 720  LEU A CA  1 
ATOM   5472  C  C   . LEU A 1 720  ? 47.803  9.423   -6.957  1.00 251.60 ? 720  LEU A C   1 
ATOM   5473  O  O   . LEU A 1 720  ? 47.035  10.042  -7.689  1.00 252.51 ? 720  LEU A O   1 
ATOM   5474  C  CB  . LEU A 1 720  ? 46.931  8.345   -4.874  1.00 248.90 ? 720  LEU A CB  1 
ATOM   5475  C  CG  . LEU A 1 720  ? 46.557  7.189   -3.931  1.00 253.68 ? 720  LEU A CG  1 
ATOM   5476  C  CD1 . LEU A 1 720  ? 46.334  7.718   -2.503  1.00 254.70 ? 720  LEU A CD1 1 
ATOM   5477  C  CD2 . LEU A 1 720  ? 45.337  6.411   -4.417  1.00 259.89 ? 720  LEU A CD2 1 
ATOM   5478  N  N   . GLY A 1 721  ? 49.011  9.881   -6.650  1.00 312.65 ? 721  GLY A N   1 
ATOM   5479  C  CA  . GLY A 1 721  ? 49.521  11.086  -7.272  1.00 317.17 ? 721  GLY A CA  1 
ATOM   5480  C  C   . GLY A 1 721  ? 50.740  11.683  -6.601  1.00 316.29 ? 721  GLY A C   1 
ATOM   5481  O  O   . GLY A 1 721  ? 50.839  11.710  -5.373  1.00 315.71 ? 721  GLY A O   1 
ATOM   5482  N  N   . PRO A 1 722  ? 51.682  12.169  -7.418  1.00 267.86 ? 722  PRO A N   1 
ATOM   5483  C  CA  . PRO A 1 722  ? 52.877  12.902  -6.987  1.00 261.75 ? 722  PRO A CA  1 
ATOM   5484  C  C   . PRO A 1 722  ? 52.530  14.125  -6.129  1.00 255.84 ? 722  PRO A C   1 
ATOM   5485  O  O   . PRO A 1 722  ? 53.383  14.665  -5.422  1.00 250.91 ? 722  PRO A O   1 
ATOM   5486  C  CB  . PRO A 1 722  ? 53.508  13.332  -8.315  1.00 263.38 ? 722  PRO A CB  1 
ATOM   5487  C  CG  . PRO A 1 722  ? 53.087  12.282  -9.273  1.00 266.90 ? 722  PRO A CG  1 
ATOM   5488  C  CD  . PRO A 1 722  ? 51.696  11.898  -8.865  1.00 269.86 ? 722  PRO A CD  1 
ATOM   5489  N  N   . ARG A 1 723  ? 51.275  14.553  -6.189  1.00 282.13 ? 723  ARG A N   1 
ATOM   5490  C  CA  . ARG A 1 723  ? 50.825  15.672  -5.382  1.00 277.29 ? 723  ARG A CA  1 
ATOM   5491  C  C   . ARG A 1 723  ? 51.100  15.377  -3.919  1.00 273.10 ? 723  ARG A C   1 
ATOM   5492  O  O   . ARG A 1 723  ? 51.437  16.270  -3.146  1.00 271.26 ? 723  ARG A O   1 
ATOM   5493  C  CB  . ARG A 1 723  ? 49.328  15.876  -5.576  1.00 276.77 ? 723  ARG A CB  1 
ATOM   5494  C  CG  . ARG A 1 723  ? 48.844  15.564  -6.978  1.00 276.03 ? 723  ARG A CG  1 
ATOM   5495  C  CD  . ARG A 1 723  ? 47.331  15.615  -7.044  1.00 275.57 ? 723  ARG A CD  1 
ATOM   5496  N  NE  . ARG A 1 723  ? 46.833  15.224  -8.355  1.00 276.68 ? 723  ARG A NE  1 
ATOM   5497  C  CZ  . ARG A 1 723  ? 46.441  13.995  -8.667  1.00 278.76 ? 723  ARG A CZ  1 
ATOM   5498  N  NH1 . ARG A 1 723  ? 46.482  13.029  -7.759  1.00 278.23 ? 723  ARG A NH1 1 
ATOM   5499  N  NH2 . ARG A 1 723  ? 46.003  13.735  -9.889  1.00 282.09 ? 723  ARG A NH2 1 
ATOM   5500  N  N   . CYS A 1 724  ? 50.956  14.112  -3.547  1.00 260.10 ? 724  CYS A N   1 
ATOM   5501  C  CA  . CYS A 1 724  ? 51.101  13.720  -2.153  1.00 255.83 ? 724  CYS A CA  1 
ATOM   5502  C  C   . CYS A 1 724  ? 52.493  13.175  -1.803  1.00 253.51 ? 724  CYS A C   1 
ATOM   5503  O  O   . CYS A 1 724  ? 52.953  13.307  -0.665  1.00 249.66 ? 724  CYS A O   1 
ATOM   5504  C  CB  . CYS A 1 724  ? 49.987  12.741  -1.740  1.00 257.16 ? 724  CYS A CB  1 
ATOM   5505  S  SG  . CYS A 1 724  ? 50.494  11.089  -1.159  1.00 228.35 ? 724  CYS A SG  1 
ATOM   5506  N  N   . ILE A 1 725  ? 53.182  12.613  -2.789  1.00 267.40 ? 725  ILE A N   1 
ATOM   5507  C  CA  . ILE A 1 725  ? 54.489  12.013  -2.542  1.00 265.76 ? 725  ILE A CA  1 
ATOM   5508  C  C   . ILE A 1 725  ? 55.362  12.936  -1.684  1.00 263.24 ? 725  ILE A C   1 
ATOM   5509  O  O   . ILE A 1 725  ? 56.098  12.478  -0.808  1.00 262.54 ? 725  ILE A O   1 
ATOM   5510  C  CB  . ILE A 1 725  ? 55.206  11.632  -3.866  1.00 265.70 ? 725  ILE A CB  1 
ATOM   5511  C  CG1 . ILE A 1 725  ? 54.391  10.577  -4.630  1.00 268.79 ? 725  ILE A CG1 1 
ATOM   5512  C  CG2 . ILE A 1 725  ? 56.617  11.129  -3.592  1.00 263.88 ? 725  ILE A CG2 1 
ATOM   5513  C  CD1 . ILE A 1 725  ? 55.115  9.945   -5.819  1.00 270.59 ? 725  ILE A CD1 1 
ATOM   5514  N  N   . LYS A 1 726  ? 55.256  14.238  -1.922  1.00 294.40 ? 726  LYS A N   1 
ATOM   5515  C  CA  . LYS A 1 726  ? 55.970  15.204  -1.108  1.00 291.85 ? 726  LYS A CA  1 
ATOM   5516  C  C   . LYS A 1 726  ? 55.525  15.112  0.345   1.00 284.42 ? 726  LYS A C   1 
ATOM   5517  O  O   . LYS A 1 726  ? 56.359  15.051  1.245   1.00 279.54 ? 726  LYS A O   1 
ATOM   5518  C  CB  . LYS A 1 726  ? 55.760  16.623  -1.628  1.00 299.16 ? 726  LYS A CB  1 
ATOM   5519  C  CG  . LYS A 1 726  ? 56.875  17.119  -2.520  1.00 306.44 ? 726  LYS A CG  1 
ATOM   5520  C  CD  . LYS A 1 726  ? 56.993  18.632  -2.454  1.00 310.81 ? 726  LYS A CD  1 
ATOM   5521  C  CE  . LYS A 1 726  ? 58.216  19.125  -3.212  1.00 313.69 ? 726  LYS A CE  1 
ATOM   5522  N  NZ  . LYS A 1 726  ? 58.440  20.586  -3.025  1.00 313.61 ? 726  LYS A NZ  1 
ATOM   5523  N  N   . ALA A 1 727  ? 54.210  15.102  0.564   1.00 314.84 ? 727  ALA A N   1 
ATOM   5524  C  CA  . ALA A 1 727  ? 53.632  15.053  1.912   1.00 311.52 ? 727  ALA A CA  1 
ATOM   5525  C  C   . ALA A 1 727  ? 53.965  13.744  2.611   1.00 305.95 ? 727  ALA A C   1 
ATOM   5526  O  O   . ALA A 1 727  ? 53.827  13.612  3.825   1.00 303.99 ? 727  ALA A O   1 
ATOM   5527  C  CB  . ALA A 1 727  ? 52.128  15.245  1.850   1.00 314.37 ? 727  ALA A CB  1 
ATOM   5528  N  N   . PHE A 1 728  ? 54.393  12.769  1.823   1.00 222.23 ? 728  PHE A N   1 
ATOM   5529  C  CA  . PHE A 1 728  ? 54.872  11.511  2.363   1.00 217.85 ? 728  PHE A CA  1 
ATOM   5530  C  C   . PHE A 1 728  ? 56.298  11.652  2.946   1.00 217.95 ? 728  PHE A C   1 
ATOM   5531  O  O   . PHE A 1 728  ? 56.476  11.798  4.170   1.00 218.08 ? 728  PHE A O   1 
ATOM   5532  C  CB  . PHE A 1 728  ? 54.834  10.451  1.268   1.00 211.67 ? 728  PHE A CB  1 
ATOM   5533  C  CG  . PHE A 1 728  ? 55.019  9.070   1.775   1.00 210.83 ? 728  PHE A CG  1 
ATOM   5534  C  CD1 . PHE A 1 728  ? 54.206  8.580   2.783   1.00 210.29 ? 728  PHE A CD1 1 
ATOM   5535  C  CD2 . PHE A 1 728  ? 56.003  8.258   1.253   1.00 214.14 ? 728  PHE A CD2 1 
ATOM   5536  C  CE1 . PHE A 1 728  ? 54.373  7.302   3.263   1.00 211.83 ? 728  PHE A CE1 1 
ATOM   5537  C  CE2 . PHE A 1 728  ? 56.177  6.981   1.726   1.00 210.19 ? 728  PHE A CE2 1 
ATOM   5538  C  CZ  . PHE A 1 728  ? 55.361  6.500   2.737   1.00 209.54 ? 728  PHE A CZ  1 
ATOM   5539  N  N   . THR A 1 729  ? 57.297  11.640  2.056   1.00 255.74 ? 729  THR A N   1 
ATOM   5540  C  CA  . THR A 1 729  ? 58.730  11.672  2.411   1.00 253.58 ? 729  THR A CA  1 
ATOM   5541  C  C   . THR A 1 729  ? 59.173  12.854  3.281   1.00 251.89 ? 729  THR A C   1 
ATOM   5542  O  O   . THR A 1 729  ? 60.175  12.774  3.992   1.00 250.01 ? 729  THR A O   1 
ATOM   5543  C  CB  . THR A 1 729  ? 59.611  11.657  1.133   1.00 281.76 ? 729  THR A CB  1 
ATOM   5544  O  OG1 . THR A 1 729  ? 58.819  12.041  0.001   1.00 283.00 ? 729  THR A OG1 1 
ATOM   5545  C  CG2 . THR A 1 729  ? 60.191  10.272  0.882   1.00 283.93 ? 729  THR A CG2 1 
ATOM   5546  N  N   . GLU A 1 730  ? 58.433  13.952  3.190   1.00 297.25 ? 730  GLU A N   1 
ATOM   5547  C  CA  . GLU A 1 730  ? 58.654  15.109  4.038   1.00 297.24 ? 730  GLU A CA  1 
ATOM   5548  C  C   . GLU A 1 730  ? 58.405  14.711  5.471   1.00 297.60 ? 730  GLU A C   1 
ATOM   5549  O  O   . GLU A 1 730  ? 59.215  14.965  6.366   1.00 295.41 ? 730  GLU A O   1 
ATOM   5550  C  CB  . GLU A 1 730  ? 57.658  16.209  3.679   1.00 298.30 ? 730  GLU A CB  1 
ATOM   5551  C  CG  . GLU A 1 730  ? 58.089  17.093  2.531   1.00 297.54 ? 730  GLU A CG  1 
ATOM   5552  C  CD  . GLU A 1 730  ? 58.960  18.233  2.990   1.00 293.80 ? 730  GLU A CD  1 
ATOM   5553  O  OE1 . GLU A 1 730  ? 58.801  18.664  4.156   1.00 290.68 ? 730  GLU A OE1 1 
ATOM   5554  O  OE2 . GLU A 1 730  ? 59.791  18.697  2.180   1.00 293.55 ? 730  GLU A OE2 1 
ATOM   5555  N  N   . CYS A 1 731  ? 57.261  14.071  5.664   1.00 429.35 ? 731  CYS A N   1 
ATOM   5556  C  CA  . CYS A 1 731  ? 56.709  13.831  6.983   1.00 431.19 ? 731  CYS A CA  1 
ATOM   5557  C  C   . CYS A 1 731  ? 57.217  12.536  7.607   1.00 434.28 ? 731  CYS A C   1 
ATOM   5558  O  O   . CYS A 1 731  ? 57.225  12.391  8.830   1.00 434.07 ? 731  CYS A O   1 
ATOM   5559  C  CB  . CYS A 1 731  ? 55.187  13.859  6.882   1.00 432.19 ? 731  CYS A CB  1 
ATOM   5560  S  SG  . CYS A 1 731  ? 54.636  15.234  5.833   1.00 476.50 ? 731  CYS A SG  1 
ATOM   5561  N  N   . CYS A 1 732  ? 57.647  11.599  6.767   1.00 323.90 ? 732  CYS A N   1 
ATOM   5562  C  CA  . CYS A 1 732  ? 58.297  10.394  7.266   1.00 326.40 ? 732  CYS A CA  1 
ATOM   5563  C  C   . CYS A 1 732  ? 59.677  10.742  7.830   1.00 324.67 ? 732  CYS A C   1 
ATOM   5564  O  O   . CYS A 1 732  ? 60.010  10.357  8.956   1.00 325.13 ? 732  CYS A O   1 
ATOM   5565  C  CB  . CYS A 1 732  ? 58.414  9.335   6.167   1.00 327.06 ? 732  CYS A CB  1 
ATOM   5566  S  SG  . CYS A 1 732  ? 58.867  7.679   6.758   1.00 316.62 ? 732  CYS A SG  1 
ATOM   5567  N  N   . VAL A 1 733  ? 60.468  11.483  7.051   1.00 280.43 ? 733  VAL A N   1 
ATOM   5568  C  CA  . VAL A 1 733  ? 61.806  11.890  7.478   1.00 276.90 ? 733  VAL A CA  1 
ATOM   5569  C  C   . VAL A 1 733  ? 61.727  12.563  8.834   1.00 272.91 ? 733  VAL A C   1 
ATOM   5570  O  O   . VAL A 1 733  ? 62.498  12.256  9.737   1.00 268.91 ? 733  VAL A O   1 
ATOM   5571  C  CB  . VAL A 1 733  ? 62.465  12.868  6.481   1.00 275.28 ? 733  VAL A CB  1 
ATOM   5572  C  CG1 . VAL A 1 733  ? 63.720  13.479  7.098   1.00 273.59 ? 733  VAL A CG1 1 
ATOM   5573  C  CG2 . VAL A 1 733  ? 62.780  12.168  5.158   1.00 276.32 ? 733  VAL A CG2 1 
ATOM   5574  N  N   . VAL A 1 734  ? 60.774  13.475  8.965   1.00 355.50 ? 734  VAL A N   1 
ATOM   5575  C  CA  . VAL A 1 734  ? 60.554  14.176  10.214  1.00 354.26 ? 734  VAL A CA  1 
ATOM   5576  C  C   . VAL A 1 734  ? 60.365  13.203  11.379  1.00 356.36 ? 734  VAL A C   1 
ATOM   5577  O  O   . VAL A 1 734  ? 60.936  13.388  12.457  1.00 356.97 ? 734  VAL A O   1 
ATOM   5578  C  CB  . VAL A 1 734  ? 59.324  15.093  10.108  1.00 353.19 ? 734  VAL A CB  1 
ATOM   5579  C  CG1 . VAL A 1 734  ? 59.033  15.758  11.446  1.00 350.85 ? 734  VAL A CG1 1 
ATOM   5580  C  CG2 . VAL A 1 734  ? 59.539  16.129  9.014   1.00 352.50 ? 734  VAL A CG2 1 
ATOM   5581  N  N   . ALA A 1 735  ? 59.570  12.162  11.151  1.00 363.56 ? 735  ALA A N   1 
ATOM   5582  C  CA  . ALA A 1 735  ? 59.221  11.211  12.203  1.00 364.41 ? 735  ALA A CA  1 
ATOM   5583  C  C   . ALA A 1 735  ? 60.304  10.157  12.416  1.00 363.17 ? 735  ALA A C   1 
ATOM   5584  O  O   . ALA A 1 735  ? 60.347  9.499   13.456  1.00 362.38 ? 735  ALA A O   1 
ATOM   5585  C  CB  . ALA A 1 735  ? 57.886  10.553  11.897  1.00 366.09 ? 735  ALA A CB  1 
ATOM   5586  N  N   . SER A 1 736  ? 61.179  10.008  11.428  1.00 274.77 ? 736  SER A N   1 
ATOM   5587  C  CA  . SER A 1 736  ? 62.271  9.046   11.513  1.00 274.04 ? 736  SER A CA  1 
ATOM   5588  C  C   . SER A 1 736  ? 63.489  9.570   12.287  1.00 270.83 ? 736  SER A C   1 
ATOM   5589  O  O   . SER A 1 736  ? 64.049  8.856   13.126  1.00 269.92 ? 736  SER A O   1 
ATOM   5590  C  CB  . SER A 1 736  ? 62.656  8.573   10.118  1.00 274.89 ? 736  SER A CB  1 
ATOM   5591  O  OG  . SER A 1 736  ? 61.523  8.012   9.478   1.00 276.55 ? 736  SER A OG  1 
ATOM   5592  N  N   . GLN A 1 737  ? 63.894  10.811  12.020  1.00 243.38 ? 737  GLN A N   1 
ATOM   5593  C  CA  . GLN A 1 737  ? 64.939  11.449  12.818  1.00 239.39 ? 737  GLN A CA  1 
ATOM   5594  C  C   . GLN A 1 737  ? 64.489  11.493  14.278  1.00 238.64 ? 737  GLN A C   1 
ATOM   5595  O  O   . GLN A 1 737  ? 65.310  11.513  15.196  1.00 234.61 ? 737  GLN A O   1 
ATOM   5596  C  CB  . GLN A 1 737  ? 65.225  12.873  12.319  1.00 238.21 ? 737  GLN A CB  1 
ATOM   5597  C  CG  . GLN A 1 737  ? 64.994  13.104  10.820  1.00 239.98 ? 737  GLN A CG  1 
ATOM   5598  C  CD  . GLN A 1 737  ? 66.036  12.451  9.927   1.00 239.69 ? 737  GLN A CD  1 
ATOM   5599  O  OE1 . GLN A 1 737  ? 67.222  12.767  9.996   1.00 238.69 ? 737  GLN A OE1 1 
ATOM   5600  N  NE2 . GLN A 1 737  ? 65.589  11.551  9.066   1.00 240.71 ? 737  GLN A NE2 1 
ATOM   5601  N  N   . LEU A 1 738  ? 63.171  11.487  14.470  1.00 313.03 ? 738  LEU A N   1 
ATOM   5602  C  CA  . LEU A 1 738  ? 62.543  11.616  15.786  1.00 316.56 ? 738  LEU A CA  1 
ATOM   5603  C  C   . LEU A 1 738  ? 62.696  10.397  16.701  1.00 322.21 ? 738  LEU A C   1 
ATOM   5604  O  O   . LEU A 1 738  ? 62.922  10.548  17.901  1.00 322.18 ? 738  LEU A O   1 
ATOM   5605  C  CB  . LEU A 1 738  ? 61.055  11.947  15.627  1.00 317.31 ? 738  LEU A CB  1 
ATOM   5606  C  CG  . LEU A 1 738  ? 60.261  12.236  16.904  1.00 315.07 ? 738  LEU A CG  1 
ATOM   5607  C  CD1 . LEU A 1 738  ? 60.550  13.644  17.414  1.00 312.75 ? 738  LEU A CD1 1 
ATOM   5608  C  CD2 . LEU A 1 738  ? 58.771  12.052  16.663  1.00 317.00 ? 738  LEU A CD2 1 
ATOM   5609  N  N   . ARG A 1 739  ? 62.549  9.195   16.151  1.00 279.90 ? 739  ARG A N   1 
ATOM   5610  C  CA  . ARG A 1 739  ? 62.667  7.986   16.964  1.00 286.73 ? 739  ARG A CA  1 
ATOM   5611  C  C   . ARG A 1 739  ? 64.113  7.742   17.371  1.00 285.47 ? 739  ARG A C   1 
ATOM   5612  O  O   . ARG A 1 739  ? 64.401  6.857   18.178  1.00 285.45 ? 739  ARG A O   1 
ATOM   5613  C  CB  . ARG A 1 739  ? 62.129  6.766   16.227  1.00 294.76 ? 739  ARG A CB  1 
ATOM   5614  C  CG  . ARG A 1 739  ? 63.006  6.296   15.093  1.00 300.90 ? 739  ARG A CG  1 
ATOM   5615  C  CD  . ARG A 1 739  ? 62.371  5.107   14.408  1.00 307.13 ? 739  ARG A CD  1 
ATOM   5616  N  NE  . ARG A 1 739  ? 63.055  4.755   13.168  1.00 313.03 ? 739  ARG A NE  1 
ATOM   5617  C  CZ  . ARG A 1 739  ? 62.618  3.837   12.309  1.00 316.65 ? 739  ARG A CZ  1 
ATOM   5618  N  NH1 . ARG A 1 739  ? 61.493  3.177   12.556  1.00 317.70 ? 739  ARG A NH1 1 
ATOM   5619  N  NH2 . ARG A 1 739  ? 63.303  3.578   11.200  1.00 317.87 ? 739  ARG A NH2 1 
ATOM   5620  N  N   . ALA A 1 740  ? 65.021  8.520   16.791  1.00 301.29 ? 740  ALA A N   1 
ATOM   5621  C  CA  . ALA A 1 740  ? 66.423  8.471   17.180  1.00 299.80 ? 740  ALA A CA  1 
ATOM   5622  C  C   . ALA A 1 740  ? 66.667  9.327   18.419  1.00 296.81 ? 740  ALA A C   1 
ATOM   5623  O  O   . ALA A 1 740  ? 67.770  9.336   18.962  1.00 297.81 ? 740  ALA A O   1 
ATOM   5624  C  CB  . ALA A 1 740  ? 67.315  8.925   16.030  1.00 299.41 ? 740  ALA A CB  1 
ATOM   5625  N  N   . ASN A 1 741  ? 65.633  10.039  18.866  1.00 348.85 ? 741  ASN A N   1 
ATOM   5626  C  CA  . ASN A 1 741  ? 65.779  10.993  19.967  1.00 343.18 ? 741  ASN A CA  1 
ATOM   5627  C  C   . ASN A 1 741  ? 64.797  10.838  21.148  1.00 353.68 ? 741  ASN A C   1 
ATOM   5628  O  O   . ASN A 1 741  ? 65.116  11.241  22.272  1.00 353.36 ? 741  ASN A O   1 
ATOM   5629  C  CB  . ASN A 1 741  ? 65.769  12.433  19.430  1.00 330.32 ? 741  ASN A CB  1 
ATOM   5630  C  CG  . ASN A 1 741  ? 67.066  12.802  18.716  1.00 319.77 ? 741  ASN A CG  1 
ATOM   5631  O  OD1 . ASN A 1 741  ? 67.073  13.070  17.512  1.00 318.02 ? 741  ASN A OD1 1 
ATOM   5632  N  ND2 . ASN A 1 741  ? 68.177  12.801  19.460  1.00 312.61 ? 741  ASN A ND2 1 
ATOM   5633  N  N   . ILE A 1 742  ? 63.613  10.271  20.899  1.00 329.62 ? 742  ILE A N   1 
ATOM   5634  C  CA  . ILE A 1 742  ? 62.672  9.952   21.981  1.00 339.61 ? 742  ILE A CA  1 
ATOM   5635  C  C   . ILE A 1 742  ? 63.276  8.859   22.854  1.00 343.25 ? 742  ILE A C   1 
ATOM   5636  O  O   . ILE A 1 742  ? 62.856  8.647   23.992  1.00 343.96 ? 742  ILE A O   1 
ATOM   5637  C  CB  . ILE A 1 742  ? 61.297  9.436   21.461  1.00 345.19 ? 742  ILE A CB  1 
ATOM   5638  C  CG1 . ILE A 1 742  ? 60.738  10.332  20.353  1.00 346.88 ? 742  ILE A CG1 1 
ATOM   5639  C  CG2 . ILE A 1 742  ? 60.293  9.312   22.608  1.00 347.16 ? 742  ILE A CG2 1 
ATOM   5640  C  CD1 . ILE A 1 742  ? 59.371  9.893   19.849  1.00 349.98 ? 742  ILE A CD1 1 
ATOM   5641  N  N   . SER A 1 743  ? 64.269  8.168   22.299  1.00 342.69 ? 743  SER A N   1 
ATOM   5642  C  CA  . SER A 1 743  ? 64.886  7.022   22.951  1.00 344.14 ? 743  SER A CA  1 
ATOM   5643  C  C   . SER A 1 743  ? 66.273  6.760   22.373  1.00 342.67 ? 743  SER A C   1 
ATOM   5644  O  O   . SER A 1 743  ? 66.458  6.751   21.155  1.00 342.14 ? 743  SER A O   1 
ATOM   5645  C  CB  . SER A 1 743  ? 64.012  5.785   22.762  1.00 347.79 ? 743  SER A CB  1 
ATOM   5646  O  OG  . SER A 1 743  ? 63.892  5.467   21.388  1.00 348.72 ? 743  SER A OG  1 
ATOM   5647  N  N   . GLY A 1 750  ? 65.358  -2.460  24.374  1.00 243.09 ? 750  GLY A N   1 
ATOM   5648  C  CA  . GLY A 1 750  ? 65.171  -2.513  22.934  1.00 246.24 ? 750  GLY A CA  1 
ATOM   5649  C  C   . GLY A 1 750  ? 63.742  -2.267  22.462  1.00 249.17 ? 750  GLY A C   1 
ATOM   5650  O  O   . GLY A 1 750  ? 63.348  -2.731  21.389  1.00 249.08 ? 750  GLY A O   1 
ATOM   5651  N  N   . ARG A 1 751  ? 62.961  -1.544  23.267  1.00 306.80 ? 751  ARG A N   1 
ATOM   5652  C  CA  . ARG A 1 751  ? 61.567  -1.221  22.932  1.00 309.26 ? 751  ARG A CA  1 
ATOM   5653  C  C   . ARG A 1 751  ? 61.378  0.226   22.482  1.00 317.39 ? 751  ARG A C   1 
ATOM   5654  O  O   . ARG A 1 751  ? 61.448  1.150   23.297  1.00 318.06 ? 751  ARG A O   1 
ATOM   5655  C  CB  . ARG A 1 751  ? 60.639  -1.484  24.129  1.00 303.02 ? 751  ARG A CB  1 
ATOM   5656  C  CG  . ARG A 1 751  ? 60.399  -2.945  24.451  1.00 295.93 ? 751  ARG A CG  1 
ATOM   5657  C  CD  . ARG A 1 751  ? 59.482  -3.111  25.662  1.00 286.23 ? 751  ARG A CD  1 
ATOM   5658  N  NE  . ARG A 1 751  ? 59.344  -4.515  26.042  1.00 280.13 ? 751  ARG A NE  1 
ATOM   5659  C  CZ  . ARG A 1 751  ? 58.521  -5.370  25.446  1.00 276.88 ? 751  ARG A CZ  1 
ATOM   5660  N  NH1 . ARG A 1 751  ? 57.761  -4.959  24.441  1.00 277.13 ? 751  ARG A NH1 1 
ATOM   5661  N  NH2 . ARG A 1 751  ? 58.460  -6.632  25.850  1.00 275.27 ? 751  ARG A NH2 1 
ATOM   5662  N  N   . LEU A 1 752  ? 61.123  0.420   21.191  1.00 416.16 ? 752  LEU A N   1 
ATOM   5663  C  CA  . LEU A 1 752  ? 60.769  1.740   20.661  1.00 421.50 ? 752  LEU A CA  1 
ATOM   5664  C  C   . LEU A 1 752  ? 59.798  1.560   19.498  1.00 421.94 ? 752  LEU A C   1 
ATOM   5665  O  O   . LEU A 1 752  ? 60.025  0.734   18.615  1.00 422.46 ? 752  LEU A O   1 
ATOM   5666  C  CB  . LEU A 1 752  ? 62.010  2.510   20.190  1.00 425.92 ? 752  LEU A CB  1 
ATOM   5667  C  CG  . LEU A 1 752  ? 61.752  3.852   19.487  1.00 430.95 ? 752  LEU A CG  1 
ATOM   5668  C  CD1 . LEU A 1 752  ? 61.217  4.907   20.456  1.00 433.44 ? 752  LEU A CD1 1 
ATOM   5669  C  CD2 . LEU A 1 752  ? 63.013  4.337   18.797  1.00 432.15 ? 752  LEU A CD2 1 
ATOM   5670  N  N   . HIS A 1 753  ? 58.725  2.340   19.498  1.00 436.64 ? 753  HIS A N   1 
ATOM   5671  C  CA  . HIS A 1 753  ? 57.667  2.165   18.521  1.00 434.09 ? 753  HIS A CA  1 
ATOM   5672  C  C   . HIS A 1 753  ? 56.814  3.432   18.400  1.00 425.58 ? 753  HIS A C   1 
ATOM   5673  O  O   . HIS A 1 753  ? 55.817  3.579   19.068  1.00 425.07 ? 753  HIS A O   1 
ATOM   5674  C  CB  . HIS A 1 753  ? 56.809  0.941   18.846  1.00 440.73 ? 753  HIS A CB  1 
ATOM   5675  C  CG  . HIS A 1 753  ? 57.244  0.183   20.088  1.00 445.09 ? 753  HIS A CG  1 
ATOM   5676  N  ND1 . HIS A 1 753  ? 57.095  0.730   21.357  1.00 447.37 ? 753  HIS A ND1 1 
ATOM   5677  C  CD2 . HIS A 1 753  ? 57.810  -1.055  20.246  1.00 446.23 ? 753  HIS A CD2 1 
ATOM   5678  C  CE1 . HIS A 1 753  ? 57.526  -0.176  22.246  1.00 447.37 ? 753  HIS A CE1 1 
ATOM   5679  N  NE2 . HIS A 1 753  ? 57.978  -1.232  21.605  1.00 446.66 ? 753  HIS A NE2 1 
ATOM   5680  N  N   . MET A 1 754  ? 57.210  4.341   17.516  1.00 295.63 ? 754  MET A N   1 
ATOM   5681  C  CA  . MET A 1 754  ? 56.509  5.611   17.308  1.00 289.66 ? 754  MET A CA  1 
ATOM   5682  C  C   . MET A 1 754  ? 55.059  5.338   16.918  1.00 286.23 ? 754  MET A C   1 
ATOM   5683  O  O   . MET A 1 754  ? 54.707  4.205   16.563  1.00 286.01 ? 754  MET A O   1 
ATOM   5684  C  CB  . MET A 1 754  ? 57.160  6.432   16.177  1.00 286.86 ? 754  MET A CB  1 
ATOM   5685  C  CG  . MET A 1 754  ? 58.659  6.637   16.313  1.00 283.51 ? 754  MET A CG  1 
ATOM   5686  S  SD  . MET A 1 754  ? 59.307  7.290   14.762  1.00 259.86 ? 754  MET A SD  1 
ATOM   5687  C  CE  . MET A 1 754  ? 57.830  8.042   14.086  1.00 200.55 ? 754  MET A CE  1 
ATOM   5688  N  N   . LYS A 1 755  ? 54.219  6.372   16.999  1.00 282.86 ? 755  LYS A N   1 
ATOM   5689  C  CA  . LYS A 1 755  ? 52.821  6.305   16.550  1.00 282.49 ? 755  LYS A CA  1 
ATOM   5690  C  C   . LYS A 1 755  ? 52.167  7.692   16.561  1.00 287.48 ? 755  LYS A C   1 
ATOM   5691  O  O   . LYS A 1 755  ? 52.701  8.649   17.122  1.00 285.74 ? 755  LYS A O   1 
ATOM   5692  C  CB  . LYS A 1 755  ? 51.985  5.352   17.416  1.00 279.37 ? 755  LYS A CB  1 
ATOM   5693  C  CG  . LYS A 1 755  ? 52.148  3.856   17.138  1.00 275.24 ? 755  LYS A CG  1 
ATOM   5694  C  CD  . LYS A 1 755  ? 52.146  3.520   15.643  1.00 274.00 ? 755  LYS A CD  1 
ATOM   5695  C  CE  . LYS A 1 755  ? 50.826  3.859   14.973  1.00 276.10 ? 755  LYS A CE  1 
ATOM   5696  N  NZ  . LYS A 1 755  ? 50.778  3.424   13.542  1.00 275.65 ? 755  LYS A NZ  1 
ATOM   5697  N  N   . THR A 1 756  ? 51.002  7.782   15.930  1.00 265.12 ? 756  THR A N   1 
ATOM   5698  C  CA  . THR A 1 756  ? 50.142  8.962   15.995  1.00 272.57 ? 756  THR A CA  1 
ATOM   5699  C  C   . THR A 1 756  ? 48.738  8.500   15.616  1.00 281.42 ? 756  THR A C   1 
ATOM   5700  O  O   . THR A 1 756  ? 48.398  8.424   14.435  1.00 284.14 ? 756  THR A O   1 
ATOM   5701  C  CB  . THR A 1 756  ? 50.606  10.077  15.035  1.00 269.89 ? 756  THR A CB  1 
ATOM   5702  O  OG1 . THR A 1 756  ? 51.871  10.592  15.469  1.00 265.70 ? 756  THR A OG1 1 
ATOM   5703  C  CG2 . THR A 1 756  ? 49.595  11.211  15.003  1.00 268.47 ? 756  THR A CG2 1 
ATOM   5704  N  N   . LEU A 1 757  ? 47.932  8.183   16.626  1.00 221.56 ? 757  LEU A N   1 
ATOM   5705  C  CA  . LEU A 1 757  ? 46.680  7.445   16.421  1.00 230.07 ? 757  LEU A CA  1 
ATOM   5706  C  C   . LEU A 1 757  ? 45.647  8.147   15.514  1.00 237.70 ? 757  LEU A C   1 
ATOM   5707  O  O   . LEU A 1 757  ? 45.612  9.376   15.408  1.00 237.30 ? 757  LEU A O   1 
ATOM   5708  C  CB  . LEU A 1 757  ? 46.056  7.040   17.774  1.00 234.33 ? 757  LEU A CB  1 
ATOM   5709  C  CG  . LEU A 1 757  ? 44.878  6.049   17.834  1.00 240.77 ? 757  LEU A CG  1 
ATOM   5710  C  CD1 . LEU A 1 757  ? 45.334  4.594   17.725  1.00 239.28 ? 757  LEU A CD1 1 
ATOM   5711  C  CD2 . LEU A 1 757  ? 44.077  6.249   19.111  1.00 243.66 ? 757  LEU A CD2 1 
ATOM   5712  N  N   . LEU A 1 758  ? 44.834  7.330   14.848  1.00 352.13 ? 758  LEU A N   1 
ATOM   5713  C  CA  . LEU A 1 758  ? 43.677  7.767   14.066  1.00 360.74 ? 758  LEU A CA  1 
ATOM   5714  C  C   . LEU A 1 758  ? 43.064  6.522   13.432  1.00 374.59 ? 758  LEU A C   1 
ATOM   5715  O  O   . LEU A 1 758  ? 43.545  6.054   12.396  1.00 374.22 ? 758  LEU A O   1 
ATOM   5716  C  CB  . LEU A 1 758  ? 44.072  8.763   12.967  1.00 351.70 ? 758  LEU A CB  1 
ATOM   5717  C  CG  . LEU A 1 758  ? 43.040  9.793   12.476  1.00 342.80 ? 758  LEU A CG  1 
ATOM   5718  C  CD1 . LEU A 1 758  ? 43.449  10.411  11.140  1.00 337.86 ? 758  LEU A CD1 1 
ATOM   5719  C  CD2 . LEU A 1 758  ? 41.649  9.194   12.362  1.00 343.98 ? 758  LEU A CD2 1 
ATOM   5720  N  N   . PRO A 1 759  ? 42.013  5.965   14.062  1.00 433.96 ? 759  PRO A N   1 
ATOM   5721  C  CA  . PRO A 1 759  ? 41.333  4.774   13.538  1.00 443.06 ? 759  PRO A CA  1 
ATOM   5722  C  C   . PRO A 1 759  ? 40.780  4.995   12.132  1.00 453.21 ? 759  PRO A C   1 
ATOM   5723  O  O   . PRO A 1 759  ? 39.970  4.195   11.664  1.00 458.47 ? 759  PRO A O   1 
ATOM   5724  C  CB  . PRO A 1 759  ? 40.184  4.562   14.530  1.00 444.01 ? 759  PRO A CB  1 
ATOM   5725  C  CG  . PRO A 1 759  ? 40.659  5.185   15.792  1.00 440.33 ? 759  PRO A CG  1 
ATOM   5726  C  CD  . PRO A 1 759  ? 41.471  6.377   15.369  1.00 437.16 ? 759  PRO A CD  1 
ATOM   5727  N  N   . VAL A 1 760  ? 41.216  6.071   11.479  1.00 382.88 ? 760  VAL A N   1 
ATOM   5728  C  CA  . VAL A 1 760  ? 40.773  6.416   10.132  1.00 390.09 ? 760  VAL A CA  1 
ATOM   5729  C  C   . VAL A 1 760  ? 39.264  6.671   10.132  1.00 379.02 ? 760  VAL A C   1 
ATOM   5730  O  O   . VAL A 1 760  ? 38.635  6.772   9.078   1.00 381.79 ? 760  VAL A O   1 
ATOM   5731  C  CB  . VAL A 1 760  ? 41.157  5.326   9.104   1.00 411.87 ? 760  VAL A CB  1 
ATOM   5732  C  CG1 . VAL A 1 760  ? 41.030  5.862   7.691   1.00 421.30 ? 760  VAL A CG1 1 
ATOM   5733  C  CG2 . VAL A 1 760  ? 42.580  4.841   9.351   1.00 417.74 ? 760  VAL A CG2 1 
ATOM   5734  N  N   . SER A 1 761  ? 38.704  6.780   11.337  1.00 328.22 ? 761  SER A N   1 
ATOM   5735  C  CA  . SER A 1 761  ? 37.282  7.041   11.545  1.00 313.02 ? 761  SER A CA  1 
ATOM   5736  C  C   . SER A 1 761  ? 36.411  5.788   11.367  1.00 296.90 ? 761  SER A C   1 
ATOM   5737  O  O   . SER A 1 761  ? 35.197  5.893   11.191  1.00 295.11 ? 761  SER A O   1 
ATOM   5738  C  CB  . SER A 1 761  ? 36.804  8.182   10.636  1.00 317.60 ? 761  SER A CB  1 
ATOM   5739  O  OG  . SER A 1 761  ? 35.461  8.542   10.914  1.00 315.42 ? 761  SER A OG  1 
ATOM   5740  N  N   . LYS A 1 762  ? 37.031  4.609   11.427  1.00 234.50 ? 762  LYS A N   1 
ATOM   5741  C  CA  . LYS A 1 762  ? 36.324  3.345   11.181  1.00 215.75 ? 762  LYS A CA  1 
ATOM   5742  C  C   . LYS A 1 762  ? 35.558  2.817   12.393  1.00 203.22 ? 762  LYS A C   1 
ATOM   5743  O  O   . LYS A 1 762  ? 36.118  2.697   13.485  1.00 201.65 ? 762  LYS A O   1 
ATOM   5744  C  CB  . LYS A 1 762  ? 37.286  2.256   10.676  1.00 208.46 ? 762  LYS A CB  1 
ATOM   5745  C  CG  . LYS A 1 762  ? 37.672  2.325   9.182   1.00 202.53 ? 762  LYS A CG  1 
ATOM   5746  C  CD  . LYS A 1 762  ? 38.576  1.144   8.797   1.00 196.01 ? 762  LYS A CD  1 
ATOM   5747  C  CE  . LYS A 1 762  ? 39.473  1.441   7.610   1.00 194.04 ? 762  LYS A CE  1 
ATOM   5748  N  NZ  . LYS A 1 762  ? 40.649  0.526   7.613   1.00 192.86 ? 762  LYS A NZ  1 
ATOM   5749  N  N   . PRO A 1 763  ? 34.272  2.485   12.193  1.00 246.21 ? 763  PRO A N   1 
ATOM   5750  C  CA  . PRO A 1 763  ? 33.422  1.885   13.226  1.00 236.74 ? 763  PRO A CA  1 
ATOM   5751  C  C   . PRO A 1 763  ? 33.886  0.488   13.635  1.00 228.46 ? 763  PRO A C   1 
ATOM   5752  O  O   . PRO A 1 763  ? 33.497  -0.495  12.999  1.00 230.22 ? 763  PRO A O   1 
ATOM   5753  C  CB  . PRO A 1 763  ? 32.047  1.805   12.547  1.00 235.41 ? 763  PRO A CB  1 
ATOM   5754  C  CG  . PRO A 1 763  ? 32.090  2.830   11.469  1.00 239.27 ? 763  PRO A CG  1 
ATOM   5755  C  CD  . PRO A 1 763  ? 33.506  2.817   10.980  1.00 245.40 ? 763  PRO A CD  1 
ATOM   5756  N  N   . GLU A 1 764  ? 34.717  0.410   14.674  1.00 222.02 ? 764  GLU A N   1 
ATOM   5757  C  CA  . GLU A 1 764  ? 35.039  -0.870  15.300  1.00 212.49 ? 764  GLU A CA  1 
ATOM   5758  C  C   . GLU A 1 764  ? 34.505  -0.942  16.715  1.00 200.26 ? 764  GLU A C   1 
ATOM   5759  O  O   . GLU A 1 764  ? 34.231  0.072   17.347  1.00 197.30 ? 764  GLU A O   1 
ATOM   5760  C  CB  . GLU A 1 764  ? 36.537  -1.161  15.283  1.00 214.18 ? 764  GLU A CB  1 
ATOM   5761  C  CG  . GLU A 1 764  ? 37.399  -0.104  15.918  1.00 213.59 ? 764  GLU A CG  1 
ATOM   5762  C  CD  . GLU A 1 764  ? 38.804  -0.140  15.359  1.00 217.29 ? 764  GLU A CD  1 
ATOM   5763  O  OE1 . GLU A 1 764  ? 39.348  -1.256  15.195  1.00 218.16 ? 764  GLU A OE1 1 
ATOM   5764  O  OE2 . GLU A 1 764  ? 39.355  0.944   15.070  1.00 218.86 ? 764  GLU A OE2 1 
ATOM   5765  N  N   . ILE A 1 765  ? 34.383  -2.161  17.208  1.00 183.45 ? 765  ILE A N   1 
ATOM   5766  C  CA  . ILE A 1 765  ? 33.572  -2.414  18.368  1.00 175.68 ? 765  ILE A CA  1 
ATOM   5767  C  C   . ILE A 1 765  ? 33.924  -3.781  18.886  1.00 175.43 ? 765  ILE A C   1 
ATOM   5768  O  O   . ILE A 1 765  ? 33.718  -4.784  18.213  1.00 179.25 ? 765  ILE A O   1 
ATOM   5769  C  CB  . ILE A 1 765  ? 32.097  -2.406  17.977  1.00 169.84 ? 765  ILE A CB  1 
ATOM   5770  C  CG1 . ILE A 1 765  ? 31.237  -2.830  19.160  1.00 166.43 ? 765  ILE A CG1 1 
ATOM   5771  C  CG2 . ILE A 1 765  ? 31.850  -3.346  16.810  1.00 170.99 ? 765  ILE A CG2 1 
ATOM   5772  C  CD1 . ILE A 1 765  ? 29.807  -2.344  19.048  1.00 164.31 ? 765  ILE A CD1 1 
ATOM   5773  N  N   . ARG A 1 766  ? 34.470  -3.826  20.085  1.00 185.99 ? 766  ARG A N   1 
ATOM   5774  C  CA  . ARG A 1 766  ? 35.033  -5.066  20.566  1.00 184.17 ? 766  ARG A CA  1 
ATOM   5775  C  C   . ARG A 1 766  ? 34.009  -5.957  21.244  1.00 184.82 ? 766  ARG A C   1 
ATOM   5776  O  O   . ARG A 1 766  ? 34.286  -6.550  22.282  1.00 183.89 ? 766  ARG A O   1 
ATOM   5777  C  CB  . ARG A 1 766  ? 36.175  -4.750  21.505  1.00 180.34 ? 766  ARG A CB  1 
ATOM   5778  C  CG  . ARG A 1 766  ? 37.078  -3.704  20.922  1.00 179.52 ? 766  ARG A CG  1 
ATOM   5779  C  CD  . ARG A 1 766  ? 37.650  -4.230  19.634  1.00 183.08 ? 766  ARG A CD  1 
ATOM   5780  N  NE  . ARG A 1 766  ? 38.682  -3.363  19.080  1.00 187.18 ? 766  ARG A NE  1 
ATOM   5781  C  CZ  . ARG A 1 766  ? 39.893  -3.782  18.720  1.00 193.50 ? 766  ARG A CZ  1 
ATOM   5782  N  NH1 . ARG A 1 766  ? 40.232  -5.060  18.862  1.00 197.82 ? 766  ARG A NH1 1 
ATOM   5783  N  NH2 . ARG A 1 766  ? 40.770  -2.923  18.215  1.00 194.57 ? 766  ARG A NH2 1 
ATOM   5784  N  N   . SER A 1 767  ? 32.825  -6.061  20.654  1.00 153.83 ? 767  SER A N   1 
ATOM   5785  C  CA  . SER A 1 767  ? 31.778  -6.895  21.233  1.00 157.57 ? 767  SER A CA  1 
ATOM   5786  C  C   . SER A 1 767  ? 30.730  -7.366  20.221  1.00 160.65 ? 767  SER A C   1 
ATOM   5787  O  O   . SER A 1 767  ? 30.288  -6.610  19.353  1.00 160.94 ? 767  SER A O   1 
ATOM   5788  C  CB  . SER A 1 767  ? 31.125  -6.182  22.426  1.00 158.09 ? 767  SER A CB  1 
ATOM   5789  O  OG  . SER A 1 767  ? 31.273  -4.774  22.329  1.00 157.49 ? 767  SER A OG  1 
ATOM   5790  N  N   . TYR A 1 768  ? 30.361  -8.638  20.328  1.00 247.21 ? 768  TYR A N   1 
ATOM   5791  C  CA  . TYR A 1 768  ? 29.324  -9.210  19.481  1.00 251.66 ? 768  TYR A CA  1 
ATOM   5792  C  C   . TYR A 1 768  ? 27.998  -8.954  20.161  1.00 243.63 ? 768  TYR A C   1 
ATOM   5793  O  O   . TYR A 1 768  ? 27.946  -8.692  21.363  1.00 242.50 ? 768  TYR A O   1 
ATOM   5794  C  CB  . TYR A 1 768  ? 29.546  -10.716 19.285  1.00 263.01 ? 768  TYR A CB  1 
ATOM   5795  C  CG  . TYR A 1 768  ? 28.486  -11.424 18.451  1.00 271.24 ? 768  TYR A CG  1 
ATOM   5796  C  CD1 . TYR A 1 768  ? 28.572  -11.468 17.060  1.00 278.05 ? 768  TYR A CD1 1 
ATOM   5797  C  CD2 . TYR A 1 768  ? 27.412  -12.073 19.057  1.00 273.40 ? 768  TYR A CD2 1 
ATOM   5798  C  CE1 . TYR A 1 768  ? 27.607  -12.124 16.296  1.00 282.49 ? 768  TYR A CE1 1 
ATOM   5799  C  CE2 . TYR A 1 768  ? 26.447  -12.731 18.301  1.00 278.01 ? 768  TYR A CE2 1 
ATOM   5800  C  CZ  . TYR A 1 768  ? 26.546  -12.753 16.922  1.00 282.92 ? 768  TYR A CZ  1 
ATOM   5801  O  OH  . TYR A 1 768  ? 25.586  -13.403 16.173  1.00 286.16 ? 768  TYR A OH  1 
ATOM   5802  N  N   . PHE A 1 769  ? 26.926  -9.038  19.390  1.00 172.39 ? 769  PHE A N   1 
ATOM   5803  C  CA  . PHE A 1 769  ? 25.605  -8.708  19.890  1.00 166.59 ? 769  PHE A CA  1 
ATOM   5804  C  C   . PHE A 1 769  ? 24.569  -9.630  19.277  1.00 167.37 ? 769  PHE A C   1 
ATOM   5805  O  O   . PHE A 1 769  ? 23.946  -9.271  18.277  1.00 170.22 ? 769  PHE A O   1 
ATOM   5806  C  CB  . PHE A 1 769  ? 25.246  -7.302  19.456  1.00 163.15 ? 769  PHE A CB  1 
ATOM   5807  C  CG  . PHE A 1 769  ? 25.852  -6.213  20.295  1.00 158.74 ? 769  PHE A CG  1 
ATOM   5808  C  CD1 . PHE A 1 769  ? 25.378  -5.944  21.570  1.00 174.02 ? 769  PHE A CD1 1 
ATOM   5809  C  CD2 . PHE A 1 769  ? 26.851  -5.408  19.779  1.00 174.98 ? 769  PHE A CD2 1 
ATOM   5810  C  CE1 . PHE A 1 769  ? 25.913  -4.909  22.314  1.00 154.89 ? 769  PHE A CE1 1 
ATOM   5811  C  CE2 . PHE A 1 769  ? 27.388  -4.374  20.527  1.00 168.86 ? 769  PHE A CE2 1 
ATOM   5812  C  CZ  . PHE A 1 769  ? 26.920  -4.125  21.788  1.00 172.32 ? 769  PHE A CZ  1 
ATOM   5813  N  N   . PRO A 1 770  ? 24.351  -10.799 19.892  1.00 173.20 ? 770  PRO A N   1 
ATOM   5814  C  CA  . PRO A 1 770  ? 23.562  -11.908 19.334  1.00 178.81 ? 770  PRO A CA  1 
ATOM   5815  C  C   . PRO A 1 770  ? 22.297  -11.510 18.571  1.00 184.52 ? 770  PRO A C   1 
ATOM   5816  O  O   . PRO A 1 770  ? 21.652  -10.505 18.866  1.00 184.56 ? 770  PRO A O   1 
ATOM   5817  C  CB  . PRO A 1 770  ? 23.188  -12.719 20.574  1.00 176.92 ? 770  PRO A CB  1 
ATOM   5818  C  CG  . PRO A 1 770  ? 24.324  -12.480 21.525  1.00 175.08 ? 770  PRO A CG  1 
ATOM   5819  C  CD  . PRO A 1 770  ? 24.836  -11.089 21.254  1.00 172.32 ? 770  PRO A CD  1 
ATOM   5820  N  N   . GLU A 1 771  ? 21.954  -12.308 17.572  1.00 208.50 ? 771  GLU A N   1 
ATOM   5821  C  CA  . GLU A 1 771  ? 20.697  -12.116 16.891  1.00 213.11 ? 771  GLU A CA  1 
ATOM   5822  C  C   . GLU A 1 771  ? 19.604  -12.274 17.931  1.00 208.56 ? 771  GLU A C   1 
ATOM   5823  O  O   . GLU A 1 771  ? 19.655  -13.185 18.759  1.00 206.96 ? 771  GLU A O   1 
ATOM   5824  C  CB  . GLU A 1 771  ? 20.539  -13.163 15.807  1.00 223.60 ? 771  GLU A CB  1 
ATOM   5825  C  CG  . GLU A 1 771  ? 19.233  -13.079 15.055  1.00 231.15 ? 771  GLU A CG  1 
ATOM   5826  C  CD  . GLU A 1 771  ? 19.032  -14.267 14.136  1.00 239.65 ? 771  GLU A CD  1 
ATOM   5827  O  OE1 . GLU A 1 771  ? 18.659  -14.052 12.961  1.00 242.33 ? 771  GLU A OE1 1 
ATOM   5828  O  OE2 . GLU A 1 771  ? 19.258  -15.414 14.588  1.00 242.96 ? 771  GLU A OE2 1 
ATOM   5829  N  N   . SER A 1 772  ? 18.626  -11.376 17.888  1.00 187.47 ? 772  SER A N   1 
ATOM   5830  C  CA  . SER A 1 772  ? 17.541  -11.335 18.874  1.00 183.52 ? 772  SER A CA  1 
ATOM   5831  C  C   . SER A 1 772  ? 16.544  -12.484 18.701  1.00 181.65 ? 772  SER A C   1 
ATOM   5832  O  O   . SER A 1 772  ? 16.894  -13.488 18.089  1.00 183.84 ? 772  SER A O   1 
ATOM   5833  C  CB  . SER A 1 772  ? 16.836  -9.987  18.795  1.00 182.32 ? 772  SER A CB  1 
ATOM   5834  O  OG  . SER A 1 772  ? 17.791  -8.941  18.831  1.00 181.16 ? 772  SER A OG  1 
ATOM   5835  N  N   . TRP A 1 773  ? 15.328  -12.352 19.246  1.00 177.51 ? 773  TRP A N   1 
ATOM   5836  C  CA  . TRP A 1 773  ? 14.293  -13.391 19.101  1.00 180.88 ? 773  TRP A CA  1 
ATOM   5837  C  C   . TRP A 1 773  ? 12.913  -13.001 19.620  1.00 183.95 ? 773  TRP A C   1 
ATOM   5838  O  O   . TRP A 1 773  ? 12.696  -11.860 20.006  1.00 185.25 ? 773  TRP A O   1 
ATOM   5839  C  CB  . TRP A 1 773  ? 14.725  -14.683 19.772  1.00 181.02 ? 773  TRP A CB  1 
ATOM   5840  C  CG  . TRP A 1 773  ? 15.168  -14.476 21.169  1.00 178.74 ? 773  TRP A CG  1 
ATOM   5841  C  CD1 . TRP A 1 773  ? 16.369  -13.965 21.585  1.00 177.63 ? 773  TRP A CD1 1 
ATOM   5842  C  CD2 . TRP A 1 773  ? 14.429  -14.772 22.358  1.00 179.11 ? 773  TRP A CD2 1 
ATOM   5843  N  NE1 . TRP A 1 773  ? 16.421  -13.928 22.957  1.00 175.68 ? 773  TRP A NE1 1 
ATOM   5844  C  CE2 . TRP A 1 773  ? 15.240  -14.422 23.455  1.00 176.56 ? 773  TRP A CE2 1 
ATOM   5845  C  CE3 . TRP A 1 773  ? 13.153  -15.309 22.599  1.00 179.66 ? 773  TRP A CE3 1 
ATOM   5846  C  CZ2 . TRP A 1 773  ? 14.820  -14.590 24.781  1.00 175.99 ? 773  TRP A CZ2 1 
ATOM   5847  C  CZ3 . TRP A 1 773  ? 12.736  -15.473 23.926  1.00 178.68 ? 773  TRP A CZ3 1 
ATOM   5848  C  CH2 . TRP A 1 773  ? 13.566  -15.116 24.992  1.00 177.03 ? 773  TRP A CH2 1 
ATOM   5849  N  N   . LEU A 1 774  ? 11.992  -13.967 19.625  1.00 242.89 ? 774  LEU A N   1 
ATOM   5850  C  CA  . LEU A 1 774  ? 10.571  -13.721 19.910  1.00 243.90 ? 774  LEU A CA  1 
ATOM   5851  C  C   . LEU A 1 774  ? 9.973   -12.604 19.046  1.00 241.78 ? 774  LEU A C   1 
ATOM   5852  O  O   . LEU A 1 774  ? 9.228   -11.753 19.536  1.00 237.74 ? 774  LEU A O   1 
ATOM   5853  C  CB  . LEU A 1 774  ? 10.339  -13.436 21.396  1.00 244.33 ? 774  LEU A CB  1 
ATOM   5854  C  CG  . LEU A 1 774  ? 9.686   -14.581 22.168  1.00 249.16 ? 774  LEU A CG  1 
ATOM   5855  C  CD1 . LEU A 1 774  ? 9.559   -14.234 23.641  1.00 247.25 ? 774  LEU A CD1 1 
ATOM   5856  C  CD2 . LEU A 1 774  ? 8.326   -14.921 21.573  1.00 252.70 ? 774  LEU A CD2 1 
ATOM   5857  N  N   . TRP A 1 775  ? 10.291  -12.635 17.754  1.00 171.20 ? 775  TRP A N   1 
ATOM   5858  C  CA  . TRP A 1 775  ? 9.979   -11.545 16.847  1.00 169.00 ? 775  TRP A CA  1 
ATOM   5859  C  C   . TRP A 1 775  ? 8.612   -11.722 16.204  1.00 172.23 ? 775  TRP A C   1 
ATOM   5860  O  O   . TRP A 1 775  ? 8.176   -10.874 15.439  1.00 171.93 ? 775  TRP A O   1 
ATOM   5861  C  CB  . TRP A 1 775  ? 11.076  -11.454 15.796  1.00 167.66 ? 775  TRP A CB  1 
ATOM   5862  C  CG  . TRP A 1 775  ? 10.975  -10.278 14.910  1.00 167.76 ? 775  TRP A CG  1 
ATOM   5863  C  CD1 . TRP A 1 775  ? 10.427  -10.253 13.676  1.00 172.47 ? 775  TRP A CD1 1 
ATOM   5864  C  CD2 . TRP A 1 775  ? 11.446  -8.944  15.164  1.00 165.43 ? 775  TRP A CD2 1 
ATOM   5865  N  NE1 . TRP A 1 775  ? 10.517  -8.991  13.134  1.00 171.66 ? 775  TRP A NE1 1 
ATOM   5866  C  CE2 . TRP A 1 775  ? 11.143  -8.172  14.029  1.00 166.81 ? 775  TRP A CE2 1 
ATOM   5867  C  CE3 . TRP A 1 775  ? 12.093  -8.332  16.235  1.00 162.39 ? 775  TRP A CE3 1 
ATOM   5868  C  CZ2 . TRP A 1 775  ? 11.462  -6.821  13.936  1.00 164.42 ? 775  TRP A CZ2 1 
ATOM   5869  C  CZ3 . TRP A 1 775  ? 12.410  -6.983  16.134  1.00 160.61 ? 775  TRP A CZ3 1 
ATOM   5870  C  CH2 . TRP A 1 775  ? 12.093  -6.248  14.996  1.00 161.84 ? 775  TRP A CH2 1 
ATOM   5871  N  N   . GLU A 1 776  ? 7.945   -12.829 16.527  1.00 238.53 ? 776  GLU A N   1 
ATOM   5872  C  CA  . GLU A 1 776  ? 6.602   -13.137 16.025  1.00 244.36 ? 776  GLU A CA  1 
ATOM   5873  C  C   . GLU A 1 776  ? 5.557   -12.089 16.439  1.00 243.18 ? 776  GLU A C   1 
ATOM   5874  O  O   . GLU A 1 776  ? 5.694   -11.461 17.488  1.00 239.69 ? 776  GLU A O   1 
ATOM   5875  C  CB  . GLU A 1 776  ? 6.184   -14.523 16.532  1.00 250.92 ? 776  GLU A CB  1 
ATOM   5876  C  CG  . GLU A 1 776  ? 6.529   -14.763 18.006  1.00 253.56 ? 776  GLU A CG  1 
ATOM   5877  C  CD  . GLU A 1 776  ? 6.372   -16.213 18.432  1.00 261.27 ? 776  GLU A CD  1 
ATOM   5878  O  OE1 . GLU A 1 776  ? 7.220   -16.706 19.204  1.00 261.58 ? 776  GLU A OE1 1 
ATOM   5879  O  OE2 . GLU A 1 776  ? 5.404   -16.864 17.994  1.00 266.65 ? 776  GLU A OE2 1 
ATOM   5880  N  N   . VAL A 1 777  ? 4.522   -11.889 15.620  1.00 151.77 ? 777  VAL A N   1 
ATOM   5881  C  CA  . VAL A 1 777  ? 3.386   -11.046 16.022  1.00 149.37 ? 777  VAL A CA  1 
ATOM   5882  C  C   . VAL A 1 777  ? 2.292   -11.916 16.680  1.00 139.94 ? 777  VAL A C   1 
ATOM   5883  O  O   . VAL A 1 777  ? 2.375   -13.141 16.612  1.00 139.90 ? 777  VAL A O   1 
ATOM   5884  C  CB  . VAL A 1 777  ? 2.849   -10.217 14.831  1.00 142.10 ? 777  VAL A CB  1 
ATOM   5885  C  CG1 . VAL A 1 777  ? 1.556   -9.523  15.189  1.00 144.41 ? 777  VAL A CG1 1 
ATOM   5886  C  CG2 . VAL A 1 777  ? 3.887   -9.203  14.400  1.00 145.62 ? 777  VAL A CG2 1 
ATOM   5887  N  N   . HIS A 1 778  ? 1.299   -11.317 17.342  1.00 180.53 ? 778  HIS A N   1 
ATOM   5888  C  CA  . HIS A 1 778  ? 0.220   -12.121 17.935  1.00 188.31 ? 778  HIS A CA  1 
ATOM   5889  C  C   . HIS A 1 778  ? -1.152  -11.451 18.048  1.00 200.31 ? 778  HIS A C   1 
ATOM   5890  O  O   . HIS A 1 778  ? -1.274  -10.230 18.145  1.00 198.21 ? 778  HIS A O   1 
ATOM   5891  C  CB  . HIS A 1 778  ? 0.625   -12.679 19.307  1.00 184.42 ? 778  HIS A CB  1 
ATOM   5892  C  CG  . HIS A 1 778  ? 1.369   -13.972 19.242  1.00 183.90 ? 778  HIS A CG  1 
ATOM   5893  N  ND1 . HIS A 1 778  ? 0.735   -15.195 19.134  1.00 185.94 ? 778  HIS A ND1 1 
ATOM   5894  C  CD2 . HIS A 1 778  ? 2.695   -14.244 19.276  1.00 181.95 ? 778  HIS A CD2 1 
ATOM   5895  C  CE1 . HIS A 1 778  ? 1.637   -16.155 19.101  1.00 186.09 ? 778  HIS A CE1 1 
ATOM   5896  N  NE2 . HIS A 1 778  ? 2.839   -15.605 19.186  1.00 183.65 ? 778  HIS A NE2 1 
ATOM   5897  N  N   . LEU A 1 779  ? -2.181  -12.290 18.032  1.00 207.29 ? 779  LEU A N   1 
ATOM   5898  C  CA  . LEU A 1 779  ? -3.542  -11.867 18.297  1.00 218.09 ? 779  LEU A CA  1 
ATOM   5899  C  C   . LEU A 1 779  ? -3.886  -12.199 19.745  1.00 224.73 ? 779  LEU A C   1 
ATOM   5900  O  O   . LEU A 1 779  ? -4.011  -13.372 20.101  1.00 228.65 ? 779  LEU A O   1 
ATOM   5901  C  CB  . LEU A 1 779  ? -4.498  -12.598 17.357  1.00 223.40 ? 779  LEU A CB  1 
ATOM   5902  C  CG  . LEU A 1 779  ? -5.974  -12.242 17.497  1.00 224.71 ? 779  LEU A CG  1 
ATOM   5903  C  CD1 . LEU A 1 779  ? -6.134  -10.738 17.424  1.00 223.14 ? 779  LEU A CD1 1 
ATOM   5904  C  CD2 . LEU A 1 779  ? -6.811  -12.934 16.428  1.00 229.15 ? 779  LEU A CD2 1 
ATOM   5905  N  N   . VAL A 1 780  ? -4.043  -11.174 20.579  1.00 239.73 ? 780  VAL A N   1 
ATOM   5906  C  CA  . VAL A 1 780  ? -4.342  -11.395 21.996  1.00 244.92 ? 780  VAL A CA  1 
ATOM   5907  C  C   . VAL A 1 780  ? -5.642  -10.728 22.459  1.00 242.82 ? 780  VAL A C   1 
ATOM   5908  O  O   . VAL A 1 780  ? -5.689  -9.516  22.671  1.00 239.23 ? 780  VAL A O   1 
ATOM   5909  C  CB  . VAL A 1 780  ? -3.176  -10.936 22.900  1.00 248.23 ? 780  VAL A CB  1 
ATOM   5910  C  CG1 . VAL A 1 780  ? -3.557  -11.067 24.366  1.00 252.54 ? 780  VAL A CG1 1 
ATOM   5911  C  CG2 . VAL A 1 780  ? -1.922  -11.737 22.595  1.00 252.15 ? 780  VAL A CG2 1 
ATOM   5912  N  N   . PRO A 1 781  ? -6.709  -11.527 22.599  1.00 221.50 ? 781  PRO A N   1 
ATOM   5913  C  CA  . PRO A 1 781  ? -7.986  -11.069 23.158  1.00 221.42 ? 781  PRO A CA  1 
ATOM   5914  C  C   . PRO A 1 781  ? -7.935  -10.960 24.683  1.00 219.35 ? 781  PRO A C   1 
ATOM   5915  O  O   . PRO A 1 781  ? -8.618  -11.718 25.377  1.00 222.04 ? 781  PRO A O   1 
ATOM   5916  C  CB  . PRO A 1 781  ? -8.968  -12.173 22.741  1.00 227.14 ? 781  PRO A CB  1 
ATOM   5917  C  CG  . PRO A 1 781  ? -8.272  -12.931 21.645  1.00 229.74 ? 781  PRO A CG  1 
ATOM   5918  C  CD  . PRO A 1 781  ? -6.826  -12.866 21.999  1.00 226.44 ? 781  PRO A CD  1 
ATOM   5919  N  N   . ARG A 1 782  ? -7.124  -10.035 25.188  1.00 245.06 ? 782  ARG A N   1 
ATOM   5920  C  CA  . ARG A 1 782  ? -7.025  -9.774  26.622  1.00 244.03 ? 782  ARG A CA  1 
ATOM   5921  C  C   . ARG A 1 782  ? -6.070  -10.708 27.382  1.00 239.88 ? 782  ARG A C   1 
ATOM   5922  O  O   . ARG A 1 782  ? -5.487  -10.314 28.390  1.00 238.76 ? 782  ARG A O   1 
ATOM   5923  C  CB  . ARG A 1 782  ? -8.408  -9.788  27.276  1.00 251.20 ? 782  ARG A CB  1 
ATOM   5924  C  CG  . ARG A 1 782  ? -9.417  -8.843  26.650  1.00 258.18 ? 782  ARG A CG  1 
ATOM   5925  C  CD  . ARG A 1 782  ? -10.727 -8.863  27.419  1.00 265.92 ? 782  ARG A CD  1 
ATOM   5926  N  NE  . ARG A 1 782  ? -11.404 -10.151 27.298  1.00 273.86 ? 782  ARG A NE  1 
ATOM   5927  C  CZ  . ARG A 1 782  ? -12.537 -10.466 27.920  1.00 279.17 ? 782  ARG A CZ  1 
ATOM   5928  N  NH1 . ARG A 1 782  ? -13.130 -9.588  28.720  1.00 279.55 ? 782  ARG A NH1 1 
ATOM   5929  N  NH2 . ARG A 1 782  ? -13.079 -11.665 27.743  1.00 283.13 ? 782  ARG A NH2 1 
ATOM   5930  N  N   . ARG A 1 783  ? -5.916  -11.944 26.920  1.00 219.72 ? 783  ARG A N   1 
ATOM   5931  C  CA  . ARG A 1 783  ? -4.975  -12.873 27.554  1.00 216.16 ? 783  ARG A CA  1 
ATOM   5932  C  C   . ARG A 1 783  ? -4.397  -13.851 26.533  1.00 212.87 ? 783  ARG A C   1 
ATOM   5933  O  O   . ARG A 1 783  ? -5.113  -14.335 25.655  1.00 214.88 ? 783  ARG A O   1 
ATOM   5934  C  CB  . ARG A 1 783  ? -5.638  -13.661 28.695  1.00 219.28 ? 783  ARG A CB  1 
ATOM   5935  C  CG  . ARG A 1 783  ? -5.780  -12.921 30.015  1.00 218.68 ? 783  ARG A CG  1 
ATOM   5936  C  CD  . ARG A 1 783  ? -6.718  -13.674 30.954  1.00 222.14 ? 783  ARG A CD  1 
ATOM   5937  N  NE  . ARG A 1 783  ? -7.679  -12.779 31.596  1.00 223.11 ? 783  ARG A NE  1 
ATOM   5938  C  CZ  . ARG A 1 783  ? -8.994  -12.983 31.642  1.00 225.82 ? 783  ARG A CZ  1 
ATOM   5939  N  NH1 . ARG A 1 783  ? -9.523  -14.065 31.093  1.00 228.27 ? 783  ARG A NH1 1 
ATOM   5940  N  NH2 . ARG A 1 783  ? -9.787  -12.106 32.242  1.00 224.81 ? 783  ARG A NH2 1 
ATOM   5941  N  N   . LYS A 1 784  ? -3.101  -14.132 26.656  1.00 174.08 ? 784  LYS A N   1 
ATOM   5942  C  CA  . LYS A 1 784  ? -2.422  -15.122 25.816  1.00 171.74 ? 784  LYS A CA  1 
ATOM   5943  C  C   . LYS A 1 784  ? -1.074  -15.479 26.435  1.00 168.10 ? 784  LYS A C   1 
ATOM   5944  O  O   . LYS A 1 784  ? -0.213  -14.626 26.647  1.00 165.96 ? 784  LYS A O   1 
ATOM   5945  C  CB  . LYS A 1 784  ? -2.265  -14.638 24.352  1.00 170.60 ? 784  LYS A CB  1 
ATOM   5946  C  CG  . LYS A 1 784  ? -1.744  -15.711 23.348  1.00 171.75 ? 784  LYS A CG  1 
ATOM   5947  C  CD  . LYS A 1 784  ? -1.945  -15.332 21.857  1.00 170.46 ? 784  LYS A CD  1 
ATOM   5948  C  CE  . LYS A 1 784  ? -1.689  -16.541 20.931  1.00 170.10 ? 784  LYS A CE  1 
ATOM   5949  N  NZ  . LYS A 1 784  ? -1.890  -16.290 19.467  1.00 169.34 ? 784  LYS A NZ  1 
ATOM   5950  N  N   . GLN A 1 785  ? -0.921  -16.753 26.750  1.00 206.68 ? 785  GLN A N   1 
ATOM   5951  C  CA  . GLN A 1 785  ? 0.319   -17.257 27.295  1.00 203.18 ? 785  GLN A CA  1 
ATOM   5952  C  C   . GLN A 1 785  ? 0.965   -18.139 26.237  1.00 202.05 ? 785  GLN A C   1 
ATOM   5953  O  O   . GLN A 1 785  ? 0.279   -18.886 25.540  1.00 201.82 ? 785  GLN A O   1 
ATOM   5954  C  CB  . GLN A 1 785  ? 0.028   -18.054 28.563  1.00 205.42 ? 785  GLN A CB  1 
ATOM   5955  C  CG  . GLN A 1 785  ? 1.241   -18.456 29.366  1.00 207.48 ? 785  GLN A CG  1 
ATOM   5956  C  CD  . GLN A 1 785  ? 0.852   -19.185 30.627  1.00 210.91 ? 785  GLN A CD  1 
ATOM   5957  O  OE1 . GLN A 1 785  ? -0.231  -19.757 30.714  1.00 212.79 ? 785  GLN A OE1 1 
ATOM   5958  N  NE2 . GLN A 1 785  ? 1.729   -19.165 31.615  1.00 211.06 ? 785  GLN A NE2 1 
ATOM   5959  N  N   . LEU A 1 786  ? 2.283   -18.030 26.104  1.00 184.56 ? 786  LEU A N   1 
ATOM   5960  C  CA  . LEU A 1 786  ? 3.038   -18.858 25.165  1.00 186.64 ? 786  LEU A CA  1 
ATOM   5961  C  C   . LEU A 1 786  ? 4.388   -19.253 25.743  1.00 188.07 ? 786  LEU A C   1 
ATOM   5962  O  O   . LEU A 1 786  ? 5.352   -18.489 25.700  1.00 187.73 ? 786  LEU A O   1 
ATOM   5963  C  CB  . LEU A 1 786  ? 3.207   -18.183 23.793  1.00 183.50 ? 786  LEU A CB  1 
ATOM   5964  C  CG  . LEU A 1 786  ? 3.676   -16.737 23.664  1.00 176.99 ? 786  LEU A CG  1 
ATOM   5965  C  CD1 . LEU A 1 786  ? 3.822   -16.386 22.203  1.00 175.68 ? 786  LEU A CD1 1 
ATOM   5966  C  CD2 . LEU A 1 786  ? 2.677   -15.824 24.319  1.00 174.30 ? 786  LEU A CD2 1 
ATOM   5967  N  N   . GLN A 1 787  ? 4.442   -20.461 26.287  1.00 231.54 ? 787  GLN A N   1 
ATOM   5968  C  CA  . GLN A 1 787  ? 5.656   -20.947 26.921  1.00 231.11 ? 787  GLN A CA  1 
ATOM   5969  C  C   . GLN A 1 787  ? 6.764   -21.217 25.900  1.00 227.79 ? 787  GLN A C   1 
ATOM   5970  O  O   . GLN A 1 787  ? 6.492   -21.408 24.710  1.00 228.20 ? 787  GLN A O   1 
ATOM   5971  C  CB  . GLN A 1 787  ? 5.361   -22.182 27.783  1.00 236.79 ? 787  GLN A CB  1 
ATOM   5972  C  CG  . GLN A 1 787  ? 4.383   -23.169 27.164  1.00 243.13 ? 787  GLN A CG  1 
ATOM   5973  C  CD  . GLN A 1 787  ? 3.927   -24.235 28.146  1.00 248.83 ? 787  GLN A CD  1 
ATOM   5974  O  OE1 . GLN A 1 787  ? 3.588   -25.348 27.754  1.00 252.52 ? 787  GLN A OE1 1 
ATOM   5975  N  NE2 . GLN A 1 787  ? 3.918   -23.898 29.430  1.00 249.10 ? 787  GLN A NE2 1 
ATOM   5976  N  N   . PHE A 1 788  ? 8.007   -21.210 26.381  1.00 232.14 ? 788  PHE A N   1 
ATOM   5977  C  CA  . PHE A 1 788  ? 9.194   -21.419 25.551  1.00 228.37 ? 788  PHE A CA  1 
ATOM   5978  C  C   . PHE A 1 788  ? 10.455  -21.359 26.405  1.00 224.00 ? 788  PHE A C   1 
ATOM   5979  O  O   . PHE A 1 788  ? 10.498  -20.649 27.409  1.00 223.84 ? 788  PHE A O   1 
ATOM   5980  C  CB  . PHE A 1 788  ? 9.280   -20.362 24.448  1.00 224.14 ? 788  PHE A CB  1 
ATOM   5981  C  CG  . PHE A 1 788  ? 9.346   -18.947 24.961  1.00 217.57 ? 788  PHE A CG  1 
ATOM   5982  C  CD1 . PHE A 1 788  ? 10.567  -18.327 25.185  1.00 214.38 ? 788  PHE A CD1 1 
ATOM   5983  C  CD2 . PHE A 1 788  ? 8.184   -18.237 25.215  1.00 214.16 ? 788  PHE A CD2 1 
ATOM   5984  C  CE1 . PHE A 1 788  ? 10.624  -17.031 25.650  1.00 209.13 ? 788  PHE A CE1 1 
ATOM   5985  C  CE2 . PHE A 1 788  ? 8.236   -16.941 25.680  1.00 209.24 ? 788  PHE A CE2 1 
ATOM   5986  C  CZ  . PHE A 1 788  ? 9.458   -16.340 25.899  1.00 206.77 ? 788  PHE A CZ  1 
ATOM   5987  N  N   . ALA A 1 789  ? 11.482  -22.101 26.009  1.00 224.27 ? 789  ALA A N   1 
ATOM   5988  C  CA  . ALA A 1 789  ? 12.740  -22.078 26.740  1.00 217.99 ? 789  ALA A CA  1 
ATOM   5989  C  C   . ALA A 1 789  ? 13.669  -21.007 26.178  1.00 212.97 ? 789  ALA A C   1 
ATOM   5990  O  O   . ALA A 1 789  ? 13.709  -20.789 24.968  1.00 213.00 ? 789  ALA A O   1 
ATOM   5991  C  CB  . ALA A 1 789  ? 13.398  -23.437 26.695  1.00 221.55 ? 789  ALA A CB  1 
ATOM   5992  N  N   . LEU A 1 790  ? 14.409  -20.340 27.059  1.00 186.46 ? 790  LEU A N   1 
ATOM   5993  C  CA  . LEU A 1 790  ? 15.319  -19.284 26.640  1.00 184.43 ? 790  LEU A CA  1 
ATOM   5994  C  C   . LEU A 1 790  ? 16.646  -19.865 26.207  1.00 187.99 ? 790  LEU A C   1 
ATOM   5995  O  O   . LEU A 1 790  ? 17.102  -20.869 26.750  1.00 187.34 ? 790  LEU A O   1 
ATOM   5996  C  CB  . LEU A 1 790  ? 15.541  -18.282 27.757  1.00 178.06 ? 790  LEU A CB  1 
ATOM   5997  C  CG  . LEU A 1 790  ? 14.347  -18.172 28.687  1.00 174.65 ? 790  LEU A CG  1 
ATOM   5998  C  CD1 . LEU A 1 790  ? 14.566  -19.009 29.934  1.00 174.95 ? 790  LEU A CD1 1 
ATOM   5999  C  CD2 . LEU A 1 790  ? 14.149  -16.730 29.050  1.00 169.08 ? 790  LEU A CD2 1 
ATOM   6000  N  N   . PRO A 1 791  ? 17.289  -19.199 25.249  1.00 173.97 ? 791  PRO A N   1 
ATOM   6001  C  CA  . PRO A 1 791  ? 18.423  -19.756 24.520  1.00 182.13 ? 791  PRO A CA  1 
ATOM   6002  C  C   . PRO A 1 791  ? 19.559  -19.912 25.467  1.00 189.68 ? 791  PRO A C   1 
ATOM   6003  O  O   . PRO A 1 791  ? 19.800  -19.004 26.253  1.00 190.89 ? 791  PRO A O   1 
ATOM   6004  C  CB  . PRO A 1 791  ? 18.794  -18.644 23.538  1.00 179.10 ? 791  PRO A CB  1 
ATOM   6005  C  CG  . PRO A 1 791  ? 17.721  -17.599 23.659  1.00 175.07 ? 791  PRO A CG  1 
ATOM   6006  C  CD  . PRO A 1 791  ? 17.140  -17.757 25.011  1.00 171.94 ? 791  PRO A CD  1 
ATOM   6007  N  N   . ASP A 1 792  ? 20.254  -21.032 25.405  1.00 218.86 ? 792  ASP A N   1 
ATOM   6008  C  CA  . ASP A 1 792  ? 21.496  -21.108 26.129  1.00 224.90 ? 792  ASP A CA  1 
ATOM   6009  C  C   . ASP A 1 792  ? 22.272  -19.896 25.624  1.00 218.36 ? 792  ASP A C   1 
ATOM   6010  O  O   . ASP A 1 792  ? 22.352  -19.672 24.415  1.00 218.32 ? 792  ASP A O   1 
ATOM   6011  C  CB  . ASP A 1 792  ? 22.224  -22.416 25.811  1.00 242.38 ? 792  ASP A CB  1 
ATOM   6012  C  CG  . ASP A 1 792  ? 23.278  -22.778 26.854  1.00 260.33 ? 792  ASP A CG  1 
ATOM   6013  O  OD1 . ASP A 1 792  ? 23.716  -21.882 27.611  1.00 265.94 ? 792  ASP A OD1 1 
ATOM   6014  O  OD2 . ASP A 1 792  ? 23.674  -23.965 26.909  1.00 272.21 ? 792  ASP A OD2 1 
ATOM   6015  N  N   . SER A 1 793  ? 22.783  -19.088 26.551  1.00 214.81 ? 793  SER A N   1 
ATOM   6016  C  CA  . SER A 1 793  ? 23.631  -17.939 26.225  1.00 207.46 ? 793  SER A CA  1 
ATOM   6017  C  C   . SER A 1 793  ? 23.818  -16.990 27.410  1.00 197.69 ? 793  SER A C   1 
ATOM   6018  O  O   . SER A 1 793  ? 22.932  -16.839 28.252  1.00 195.92 ? 793  SER A O   1 
ATOM   6019  C  CB  . SER A 1 793  ? 23.081  -17.155 25.034  1.00 206.21 ? 793  SER A CB  1 
ATOM   6020  O  OG  . SER A 1 793  ? 23.866  -15.995 24.808  1.00 202.47 ? 793  SER A OG  1 
ATOM   6021  N  N   . LEU A 1 794  ? 24.975  -16.345 27.468  1.00 226.24 ? 794  LEU A N   1 
ATOM   6022  C  CA  . LEU A 1 794  ? 25.222  -15.371 28.516  1.00 217.41 ? 794  LEU A CA  1 
ATOM   6023  C  C   . LEU A 1 794  ? 24.856  -13.975 28.056  1.00 214.53 ? 794  LEU A C   1 
ATOM   6024  O  O   . LEU A 1 794  ? 25.591  -13.349 27.295  1.00 217.37 ? 794  LEU A O   1 
ATOM   6025  C  CB  . LEU A 1 794  ? 26.674  -15.418 28.967  1.00 215.81 ? 794  LEU A CB  1 
ATOM   6026  C  CG  . LEU A 1 794  ? 26.936  -16.457 30.051  1.00 217.63 ? 794  LEU A CG  1 
ATOM   6027  C  CD1 . LEU A 1 794  ? 26.692  -17.862 29.515  1.00 221.05 ? 794  LEU A CD1 1 
ATOM   6028  C  CD2 . LEU A 1 794  ? 28.348  -16.306 30.585  1.00 218.04 ? 794  LEU A CD2 1 
ATOM   6029  N  N   . THR A 1 795  ? 23.717  -13.487 28.527  1.00 198.29 ? 795  THR A N   1 
ATOM   6030  C  CA  . THR A 1 795  ? 23.252  -12.160 28.159  1.00 192.18 ? 795  THR A CA  1 
ATOM   6031  C  C   . THR A 1 795  ? 22.133  -11.729 29.071  1.00 187.68 ? 795  THR A C   1 
ATOM   6032  O  O   . THR A 1 795  ? 21.658  -12.495 29.914  1.00 184.40 ? 795  THR A O   1 
ATOM   6033  C  CB  . THR A 1 795  ? 22.688  -12.123 26.726  1.00 250.09 ? 795  THR A CB  1 
ATOM   6034  O  OG1 . THR A 1 795  ? 21.982  -13.341 26.451  1.00 252.54 ? 795  THR A OG1 1 
ATOM   6035  C  CG2 . THR A 1 795  ? 23.794  -11.936 25.707  1.00 250.90 ? 795  THR A CG2 1 
ATOM   6036  N  N   . THR A 1 796  ? 21.715  -10.485 28.899  1.00 197.39 ? 796  THR A N   1 
ATOM   6037  C  CA  . THR A 1 796  ? 20.489  -10.031 29.522  1.00 195.40 ? 796  THR A CA  1 
ATOM   6038  C  C   . THR A 1 796  ? 19.521  -9.617  28.427  1.00 199.34 ? 796  THR A C   1 
ATOM   6039  O  O   . THR A 1 796  ? 19.753  -8.646  27.703  1.00 200.52 ? 796  THR A O   1 
ATOM   6040  C  CB  . THR A 1 796  ? 20.728  -8.875  30.495  1.00 190.35 ? 796  THR A CB  1 
ATOM   6041  O  OG1 . THR A 1 796  ? 21.617  -9.305  31.533  1.00 190.57 ? 796  THR A OG1 1 
ATOM   6042  C  CG2 . THR A 1 796  ? 19.416  -8.451  31.119  1.00 187.11 ? 796  THR A CG2 1 
ATOM   6043  N  N   . TRP A 1 797  ? 18.445  -10.386 28.300  1.00 182.02 ? 797  TRP A N   1 
ATOM   6044  C  CA  . TRP A 1 797  ? 17.451  -10.174 27.257  1.00 180.56 ? 797  TRP A CA  1 
ATOM   6045  C  C   . TRP A 1 797  ? 16.478  -9.054  27.628  1.00 173.72 ? 797  TRP A C   1 
ATOM   6046  O  O   . TRP A 1 797  ? 15.869  -9.089  28.700  1.00 172.20 ? 797  TRP A O   1 
ATOM   6047  C  CB  . TRP A 1 797  ? 16.679  -11.479 27.002  1.00 186.03 ? 797  TRP A CB  1 
ATOM   6048  C  CG  . TRP A 1 797  ? 17.510  -12.583 26.403  1.00 193.53 ? 797  TRP A CG  1 
ATOM   6049  C  CD1 . TRP A 1 797  ? 17.613  -13.878 26.838  1.00 197.98 ? 797  TRP A CD1 1 
ATOM   6050  C  CD2 . TRP A 1 797  ? 18.355  -12.477 25.260  1.00 197.68 ? 797  TRP A CD2 1 
ATOM   6051  N  NE1 . TRP A 1 797  ? 18.470  -14.580 26.027  1.00 202.77 ? 797  TRP A NE1 1 
ATOM   6052  C  CE2 . TRP A 1 797  ? 18.939  -13.738 25.053  1.00 202.88 ? 797  TRP A CE2 1 
ATOM   6053  C  CE3 . TRP A 1 797  ? 18.674  -11.435 24.392  1.00 198.12 ? 797  TRP A CE3 1 
ATOM   6054  C  CZ2 . TRP A 1 797  ? 19.819  -13.980 24.020  1.00 205.60 ? 797  TRP A CZ2 1 
ATOM   6055  C  CZ3 . TRP A 1 797  ? 19.542  -11.677 23.373  1.00 201.17 ? 797  TRP A CZ3 1 
ATOM   6056  C  CH2 . TRP A 1 797  ? 20.108  -12.938 23.190  1.00 204.68 ? 797  TRP A CH2 1 
ATOM   6057  N  N   . GLU A 1 798  ? 16.329  -8.064  26.751  1.00 172.60 ? 798  GLU A N   1 
ATOM   6058  C  CA  . GLU A 1 798  ? 15.282  -7.061  26.941  1.00 169.87 ? 798  GLU A CA  1 
ATOM   6059  C  C   . GLU A 1 798  ? 14.105  -7.238  25.990  1.00 170.30 ? 798  GLU A C   1 
ATOM   6060  O  O   . GLU A 1 798  ? 14.045  -6.611  24.939  1.00 170.24 ? 798  GLU A O   1 
ATOM   6061  C  CB  . GLU A 1 798  ? 15.819  -5.642  26.813  1.00 168.50 ? 798  GLU A CB  1 
ATOM   6062  C  CG  . GLU A 1 798  ? 14.704  -4.621  26.867  1.00 168.45 ? 798  GLU A CG  1 
ATOM   6063  C  CD  . GLU A 1 798  ? 15.209  -3.203  26.830  1.00 169.59 ? 798  GLU A CD  1 
ATOM   6064  O  OE1 . GLU A 1 798  ? 16.440  -3.003  26.880  1.00 170.60 ? 798  GLU A OE1 1 
ATOM   6065  O  OE2 . GLU A 1 798  ? 14.369  -2.288  26.756  1.00 170.05 ? 798  GLU A OE2 1 
ATOM   6066  N  N   . ILE A 1 799  ? 13.162  -8.080  26.376  1.00 130.66 ? 799  ILE A N   1 
ATOM   6067  C  CA  . ILE A 1 799  ? 12.049  -8.391  25.515  1.00 134.30 ? 799  ILE A CA  1 
ATOM   6068  C  C   . ILE A 1 799  ? 11.007  -7.273  25.588  1.00 134.62 ? 799  ILE A C   1 
ATOM   6069  O  O   . ILE A 1 799  ? 10.279  -7.174  26.557  1.00 134.83 ? 799  ILE A O   1 
ATOM   6070  C  CB  . ILE A 1 799  ? 11.528  -9.838  25.802  1.00 127.66 ? 799  ILE A CB  1 
ATOM   6071  C  CG1 . ILE A 1 799  ? 10.146  -9.900  26.433  1.00 127.49 ? 799  ILE A CG1 1 
ATOM   6072  C  CG2 . ILE A 1 799  ? 12.485  -10.557 26.712  1.00 126.57 ? 799  ILE A CG2 1 
ATOM   6073  C  CD1 . ILE A 1 799  ? 9.780   -11.332 26.833  1.00 127.26 ? 799  ILE A CD1 1 
ATOM   6074  N  N   . GLN A 1 800  ? 10.988  -6.400  24.576  1.00 147.52 ? 800  GLN A N   1 
ATOM   6075  C  CA  . GLN A 1 800  ? 9.984   -5.324  24.459  1.00 148.31 ? 800  GLN A CA  1 
ATOM   6076  C  C   . GLN A 1 800  ? 8.919   -5.656  23.429  1.00 150.60 ? 800  GLN A C   1 
ATOM   6077  O  O   . GLN A 1 800  ? 9.209   -6.173  22.351  1.00 152.68 ? 800  GLN A O   1 
ATOM   6078  C  CB  . GLN A 1 800  ? 10.615  -3.973  24.087  1.00 149.05 ? 800  GLN A CB  1 
ATOM   6079  C  CG  . GLN A 1 800  ? 10.784  -3.713  22.581  1.00 152.58 ? 800  GLN A CG  1 
ATOM   6080  C  CD  . GLN A 1 800  ? 12.252  -3.634  22.157  1.00 153.31 ? 800  GLN A CD  1 
ATOM   6081  O  OE1 . GLN A 1 800  ? 13.150  -3.741  22.986  1.00 153.38 ? 800  GLN A OE1 1 
ATOM   6082  N  NE2 . GLN A 1 800  ? 12.497  -3.445  20.868  1.00 153.70 ? 800  GLN A NE2 1 
ATOM   6083  N  N   . GLY A 1 801  ? 7.676   -5.345  23.743  1.00 132.36 ? 801  GLY A N   1 
ATOM   6084  C  CA  . GLY A 1 801  ? 6.608   -5.756  22.861  1.00 134.05 ? 801  GLY A CA  1 
ATOM   6085  C  C   . GLY A 1 801  ? 5.605   -4.655  22.632  1.00 133.73 ? 801  GLY A C   1 
ATOM   6086  O  O   . GLY A 1 801  ? 4.839   -4.324  23.530  1.00 132.64 ? 801  GLY A O   1 
ATOM   6087  N  N   . ILE A 1 802  ? 5.623   -4.077  21.433  1.00 166.34 ? 802  ILE A N   1 
ATOM   6088  C  CA  . ILE A 1 802  ? 4.611   -3.107  21.028  1.00 166.99 ? 802  ILE A CA  1 
ATOM   6089  C  C   . ILE A 1 802  ? 3.342   -3.820  20.538  1.00 169.25 ? 802  ILE A C   1 
ATOM   6090  O  O   . ILE A 1 802  ? 3.410   -4.892  19.938  1.00 174.74 ? 802  ILE A O   1 
ATOM   6091  C  CB  . ILE A 1 802  ? 5.169   -2.096  19.980  1.00 169.72 ? 802  ILE A CB  1 
ATOM   6092  C  CG1 . ILE A 1 802  ? 4.148   -1.800  18.888  1.00 171.17 ? 802  ILE A CG1 1 
ATOM   6093  C  CG2 . ILE A 1 802  ? 6.463   -2.599  19.353  1.00 170.40 ? 802  ILE A CG2 1 
ATOM   6094  C  CD1 . ILE A 1 802  ? 3.146   -0.745  19.261  1.00 170.90 ? 802  ILE A CD1 1 
ATOM   6095  N  N   . GLY A 1 803  ? 2.186   -3.228  20.824  1.00 179.11 ? 803  GLY A N   1 
ATOM   6096  C  CA  . GLY A 1 803  ? 0.911   -3.766  20.384  1.00 178.98 ? 803  GLY A CA  1 
ATOM   6097  C  C   . GLY A 1 803  ? 0.036   -2.678  19.791  1.00 183.13 ? 803  GLY A C   1 
ATOM   6098  O  O   . GLY A 1 803  ? 0.082   -1.531  20.236  1.00 179.40 ? 803  GLY A O   1 
ATOM   6099  N  N   . ILE A 1 804  ? -0.759  -3.030  18.784  1.00 142.83 ? 804  ILE A N   1 
ATOM   6100  C  CA  . ILE A 1 804  ? -1.601  -2.046  18.119  1.00 143.79 ? 804  ILE A CA  1 
ATOM   6101  C  C   . ILE A 1 804  ? -2.932  -2.639  17.701  1.00 147.35 ? 804  ILE A C   1 
ATOM   6102  O  O   . ILE A 1 804  ? -3.002  -3.784  17.259  1.00 144.85 ? 804  ILE A O   1 
ATOM   6103  C  CB  . ILE A 1 804  ? -0.899  -1.412  16.907  1.00 144.82 ? 804  ILE A CB  1 
ATOM   6104  C  CG1 . ILE A 1 804  ? -0.268  -2.484  16.035  1.00 143.39 ? 804  ILE A CG1 1 
ATOM   6105  C  CG2 . ILE A 1 804  ? 0.197   -0.479  17.356  1.00 141.79 ? 804  ILE A CG2 1 
ATOM   6106  C  CD1 . ILE A 1 804  ? 0.923   -1.967  15.251  1.00 143.30 ? 804  ILE A CD1 1 
ATOM   6107  N  N   . SER A 1 805  ? -3.976  -1.830  17.867  1.00 218.75 ? 805  SER A N   1 
ATOM   6108  C  CA  . SER A 1 805  ? -5.354  -2.189  17.558  1.00 227.96 ? 805  SER A CA  1 
ATOM   6109  C  C   . SER A 1 805  ? -6.131  -0.937  17.210  1.00 230.06 ? 805  SER A C   1 
ATOM   6110  O  O   . SER A 1 805  ? -5.566  0.063   16.770  1.00 231.08 ? 805  SER A O   1 
ATOM   6111  C  CB  . SER A 1 805  ? -6.031  -2.863  18.748  1.00 225.82 ? 805  SER A CB  1 
ATOM   6112  O  OG  . SER A 1 805  ? -5.769  -4.249  18.755  1.00 227.58 ? 805  SER A OG  1 
ATOM   6113  N  N   . ASN A 1 806  ? -7.434  -0.992  17.434  1.00 235.44 ? 806  ASN A N   1 
ATOM   6114  C  CA  . ASN A 1 806  ? -8.315  0.073   16.998  1.00 244.07 ? 806  ASN A CA  1 
ATOM   6115  C  C   . ASN A 1 806  ? -8.219  1.336   17.851  1.00 245.18 ? 806  ASN A C   1 
ATOM   6116  O  O   . ASN A 1 806  ? -8.715  2.395   17.471  1.00 246.07 ? 806  ASN A O   1 
ATOM   6117  C  CB  . ASN A 1 806  ? -9.739  -0.462  16.869  1.00 251.83 ? 806  ASN A CB  1 
ATOM   6118  C  CG  . ASN A 1 806  ? -9.839  -1.566  15.826  1.00 259.92 ? 806  ASN A CG  1 
ATOM   6119  O  OD1 . ASN A 1 806  ? -10.048 -2.736  16.150  1.00 262.76 ? 806  ASN A OD1 1 
ATOM   6120  N  ND2 . ASN A 1 806  ? -9.653  -1.198  14.564  1.00 263.80 ? 806  ASN A ND2 1 
ATOM   6121  N  N   . THR A 1 807  ? -7.551  1.232   18.991  1.00 236.67 ? 807  THR A N   1 
ATOM   6122  C  CA  . THR A 1 807  ? -7.272  2.424   19.776  1.00 234.46 ? 807  THR A CA  1 
ATOM   6123  C  C   . THR A 1 807  ? -6.132  3.260   19.159  1.00 228.56 ? 807  THR A C   1 
ATOM   6124  O  O   . THR A 1 807  ? -6.203  4.489   19.137  1.00 231.20 ? 807  THR A O   1 
ATOM   6125  C  CB  . THR A 1 807  ? -7.036  2.093   21.272  1.00 234.98 ? 807  THR A CB  1 
ATOM   6126  O  OG1 . THR A 1 807  ? -6.150  0.972   21.392  1.00 235.33 ? 807  THR A OG1 1 
ATOM   6127  C  CG2 . THR A 1 807  ? -8.364  1.751   21.951  1.00 236.30 ? 807  THR A CG2 1 
ATOM   6128  N  N   . GLY A 1 808  ? -5.107  2.588   18.634  1.00 188.34 ? 808  GLY A N   1 
ATOM   6129  C  CA  . GLY A 1 808  ? -3.940  3.253   18.069  1.00 181.00 ? 808  GLY A CA  1 
ATOM   6130  C  C   . GLY A 1 808  ? -2.658  2.440   18.232  1.00 177.45 ? 808  GLY A C   1 
ATOM   6131  O  O   . GLY A 1 808  ? -2.630  1.252   17.912  1.00 176.16 ? 808  GLY A O   1 
ATOM   6132  N  N   . ILE A 1 809  ? -1.600  3.080   18.734  1.00 142.55 ? 809  ILE A N   1 
ATOM   6133  C  CA  . ILE A 1 809  ? -0.306  2.428   18.990  1.00 141.35 ? 809  ILE A CA  1 
ATOM   6134  C  C   . ILE A 1 809  ? 0.037   2.625   20.469  1.00 139.78 ? 809  ILE A C   1 
ATOM   6135  O  O   . ILE A 1 809  ? -0.174  3.730   20.962  1.00 139.85 ? 809  ILE A O   1 
ATOM   6136  C  CB  . ILE A 1 809  ? 0.811   3.064   18.100  1.00 141.92 ? 809  ILE A CB  1 
ATOM   6137  C  CG1 . ILE A 1 809  ? 2.147   2.345   18.244  1.00 140.84 ? 809  ILE A CG1 1 
ATOM   6138  C  CG2 . ILE A 1 809  ? 0.997   4.542   18.407  1.00 142.09 ? 809  ILE A CG2 1 
ATOM   6139  C  CD1 . ILE A 1 809  ? 3.338   3.217   17.892  1.00 140.96 ? 809  ILE A CD1 1 
ATOM   6140  N  N   . CYS A 1 810  ? 0.525   1.585   21.178  1.00 228.00 ? 810  CYS A N   1 
ATOM   6141  C  CA  . CYS A 1 810  ? 0.924   1.681   22.622  1.00 223.84 ? 810  CYS A CA  1 
ATOM   6142  C  C   . CYS A 1 810  ? 2.017   0.706   23.117  1.00 223.16 ? 810  CYS A C   1 
ATOM   6143  O  O   . CYS A 1 810  ? 1.805   -0.506  23.171  1.00 222.65 ? 810  CYS A O   1 
ATOM   6144  C  CB  . CYS A 1 810  ? -0.283  1.547   23.568  1.00 221.63 ? 810  CYS A CB  1 
ATOM   6145  S  SG  . CYS A 1 810  ? 0.124   1.625   25.350  1.00 250.72 ? 810  CYS A SG  1 
ATOM   6146  N  N   . VAL A 1 811  ? 3.160   1.247   23.532  1.00 183.74 ? 811  VAL A N   1 
ATOM   6147  C  CA  . VAL A 1 811  ? 4.289   0.428   23.978  1.00 182.53 ? 811  VAL A CA  1 
ATOM   6148  C  C   . VAL A 1 811  ? 4.075   -0.166  25.362  1.00 181.78 ? 811  VAL A C   1 
ATOM   6149  O  O   . VAL A 1 811  ? 3.696   0.546   26.281  1.00 181.46 ? 811  VAL A O   1 
ATOM   6150  C  CB  . VAL A 1 811  ? 5.575   1.263   24.051  1.00 181.91 ? 811  VAL A CB  1 
ATOM   6151  C  CG1 . VAL A 1 811  ? 6.756   0.400   24.513  1.00 182.13 ? 811  VAL A CG1 1 
ATOM   6152  C  CG2 . VAL A 1 811  ? 5.849   1.909   22.711  1.00 181.70 ? 811  VAL A CG2 1 
ATOM   6153  N  N   . ALA A 1 812  ? 4.334   -1.460  25.526  1.00 250.22 ? 812  ALA A N   1 
ATOM   6154  C  CA  . ALA A 1 812  ? 4.318   -2.046  26.865  1.00 247.96 ? 812  ALA A CA  1 
ATOM   6155  C  C   . ALA A 1 812  ? 5.628   -1.748  27.583  1.00 245.31 ? 812  ALA A C   1 
ATOM   6156  O  O   . ALA A 1 812  ? 6.669   -1.551  26.947  1.00 244.87 ? 812  ALA A O   1 
ATOM   6157  C  CB  . ALA A 1 812  ? 4.068   -3.549  26.812  1.00 251.38 ? 812  ALA A CB  1 
ATOM   6158  N  N   . ASP A 1 813  ? 5.562   -1.702  28.908  1.00 194.49 ? 813  ASP A N   1 
ATOM   6159  C  CA  . ASP A 1 813  ? 6.754   -1.591  29.719  1.00 191.28 ? 813  ASP A CA  1 
ATOM   6160  C  C   . ASP A 1 813  ? 7.577   -2.812  29.402  1.00 187.56 ? 813  ASP A C   1 
ATOM   6161  O  O   . ASP A 1 813  ? 7.034   -3.920  29.353  1.00 186.36 ? 813  ASP A O   1 
ATOM   6162  C  CB  . ASP A 1 813  ? 6.379   -1.599  31.192  1.00 194.60 ? 813  ASP A CB  1 
ATOM   6163  C  CG  . ASP A 1 813  ? 5.498   -0.426  31.573  1.00 197.29 ? 813  ASP A CG  1 
ATOM   6164  O  OD1 . ASP A 1 813  ? 5.994   0.721   31.539  1.00 196.87 ? 813  ASP A OD1 1 
ATOM   6165  O  OD2 . ASP A 1 813  ? 4.313   -0.651  31.908  1.00 199.03 ? 813  ASP A OD2 1 
ATOM   6166  N  N   . THR A 1 814  ? 8.877   -2.612  29.183  1.00 134.70 ? 814  THR A N   1 
ATOM   6167  C  CA  . THR A 1 814  ? 9.791   -3.715  28.868  1.00 133.95 ? 814  THR A CA  1 
ATOM   6168  C  C   . THR A 1 814  ? 9.722   -4.800  29.936  1.00 133.03 ? 814  THR A C   1 
ATOM   6169  O  O   . THR A 1 814  ? 8.907   -4.708  30.849  1.00 132.79 ? 814  THR A O   1 
ATOM   6170  C  CB  . THR A 1 814  ? 11.261  -3.236  28.673  1.00 131.13 ? 814  THR A CB  1 
ATOM   6171  O  OG1 . THR A 1 814  ? 12.177  -4.275  29.051  1.00 131.38 ? 814  THR A OG1 1 
ATOM   6172  C  CG2 . THR A 1 814  ? 11.538  -1.977  29.485  1.00 129.73 ? 814  THR A CG2 1 
ATOM   6173  N  N   . VAL A 1 815  ? 10.548  -5.834  29.800  1.00 187.71 ? 815  VAL A N   1 
ATOM   6174  C  CA  . VAL A 1 815  ? 10.714  -6.853  30.835  1.00 190.41 ? 815  VAL A CA  1 
ATOM   6175  C  C   . VAL A 1 815  ? 12.067  -7.540  30.638  1.00 191.84 ? 815  VAL A C   1 
ATOM   6176  O  O   . VAL A 1 815  ? 12.153  -8.561  29.955  1.00 196.56 ? 815  VAL A O   1 
ATOM   6177  C  CB  . VAL A 1 815  ? 9.571   -7.914  30.823  1.00 193.99 ? 815  VAL A CB  1 
ATOM   6178  C  CG1 . VAL A 1 815  ? 9.898   -9.077  31.737  1.00 194.67 ? 815  VAL A CG1 1 
ATOM   6179  C  CG2 . VAL A 1 815  ? 8.240   -7.299  31.233  1.00 193.78 ? 815  VAL A CG2 1 
ATOM   6180  N  N   . LYS A 1 816  ? 13.124  -6.966  31.220  1.00 201.31 ? 816  LYS A N   1 
ATOM   6181  C  CA  . LYS A 1 816  ? 14.460  -7.572  31.177  1.00 204.36 ? 816  LYS A CA  1 
ATOM   6182  C  C   . LYS A 1 816  ? 14.362  -8.975  31.726  1.00 209.00 ? 816  LYS A C   1 
ATOM   6183  O  O   . LYS A 1 816  ? 13.356  -9.335  32.332  1.00 207.40 ? 816  LYS A O   1 
ATOM   6184  C  CB  . LYS A 1 816  ? 15.481  -6.785  32.010  1.00 227.22 ? 816  LYS A CB  1 
ATOM   6185  C  CG  . LYS A 1 816  ? 15.916  -5.457  31.428  1.00 243.88 ? 816  LYS A CG  1 
ATOM   6186  C  CD  . LYS A 1 816  ? 14.868  -4.383  31.650  1.00 241.73 ? 816  LYS A CD  1 
ATOM   6187  C  CE  . LYS A 1 816  ? 15.353  -3.040  31.134  1.00 238.29 ? 816  LYS A CE  1 
ATOM   6188  N  NZ  . LYS A 1 816  ? 14.349  -1.961  31.351  1.00 235.50 ? 816  LYS A NZ  1 
ATOM   6189  N  N   . ALA A 1 817  ? 15.403  -9.769  31.527  1.00 183.35 ? 817  ALA A N   1 
ATOM   6190  C  CA  . ALA A 1 817  ? 15.346  -11.151 31.966  1.00 191.42 ? 817  ALA A CA  1 
ATOM   6191  C  C   . ALA A 1 817  ? 16.648  -11.888 31.681  1.00 192.79 ? 817  ALA A C   1 
ATOM   6192  O  O   . ALA A 1 817  ? 16.668  -12.885 30.958  1.00 195.60 ? 817  ALA A O   1 
ATOM   6193  C  CB  . ALA A 1 817  ? 14.173  -11.858 31.309  1.00 196.72 ? 817  ALA A CB  1 
ATOM   6194  N  N   . LYS A 1 818  ? 17.732  -11.384 32.263  1.00 223.13 ? 818  LYS A N   1 
ATOM   6195  C  CA  . LYS A 1 818  ? 19.046  -12.001 32.141  1.00 224.53 ? 818  LYS A CA  1 
ATOM   6196  C  C   . LYS A 1 818  ? 18.988  -13.487 32.461  1.00 223.99 ? 818  LYS A C   1 
ATOM   6197  O  O   . LYS A 1 818  ? 18.363  -13.911 33.438  1.00 221.41 ? 818  LYS A O   1 
ATOM   6198  C  CB  . LYS A 1 818  ? 20.056  -11.315 33.073  1.00 226.57 ? 818  LYS A CB  1 
ATOM   6199  C  CG  . LYS A 1 818  ? 19.765  -11.505 34.572  1.00 231.47 ? 818  LYS A CG  1 
ATOM   6200  C  CD  . LYS A 1 818  ? 20.733  -10.727 35.479  1.00 235.39 ? 818  LYS A CD  1 
ATOM   6201  C  CE  . LYS A 1 818  ? 20.418  -10.940 36.967  1.00 239.39 ? 818  LYS A CE  1 
ATOM   6202  N  NZ  . LYS A 1 818  ? 21.489  -10.422 37.870  1.00 239.71 ? 818  LYS A NZ  1 
ATOM   6203  N  N   . VAL A 1 819  ? 19.630  -14.278 31.616  1.00 193.72 ? 819  VAL A N   1 
ATOM   6204  C  CA  . VAL A 1 819  ? 19.809  -15.682 31.897  1.00 195.61 ? 819  VAL A CA  1 
ATOM   6205  C  C   . VAL A 1 819  ? 21.281  -15.851 32.147  1.00 196.52 ? 819  VAL A C   1 
ATOM   6206  O  O   . VAL A 1 819  ? 22.099  -15.143 31.560  1.00 195.90 ? 819  VAL A O   1 
ATOM   6207  C  CB  . VAL A 1 819  ? 19.421  -16.551 30.700  1.00 196.38 ? 819  VAL A CB  1 
ATOM   6208  C  CG1 . VAL A 1 819  ? 17.987  -16.262 30.286  1.00 196.06 ? 819  VAL A CG1 1 
ATOM   6209  C  CG2 . VAL A 1 819  ? 20.373  -16.312 29.540  1.00 195.38 ? 819  VAL A CG2 1 
ATOM   6210  N  N   . PHE A 1 820  ? 21.627  -16.789 33.011  1.00 208.10 ? 820  PHE A N   1 
ATOM   6211  C  CA  . PHE A 1 820  ? 23.021  -16.973 33.329  1.00 213.28 ? 820  PHE A CA  1 
ATOM   6212  C  C   . PHE A 1 820  ? 23.277  -18.057 34.377  1.00 214.93 ? 820  PHE A C   1 
ATOM   6213  O  O   . PHE A 1 820  ? 22.539  -18.188 35.353  1.00 211.89 ? 820  PHE A O   1 
ATOM   6214  C  CB  . PHE A 1 820  ? 23.602  -15.653 33.801  1.00 219.79 ? 820  PHE A CB  1 
ATOM   6215  C  CG  . PHE A 1 820  ? 24.772  -15.824 34.674  1.00 231.80 ? 820  PHE A CG  1 
ATOM   6216  C  CD1 . PHE A 1 820  ? 24.615  -15.886 36.045  1.00 237.23 ? 820  PHE A CD1 1 
ATOM   6217  C  CD2 . PHE A 1 820  ? 26.029  -15.977 34.132  1.00 238.11 ? 820  PHE A CD2 1 
ATOM   6218  C  CE1 . PHE A 1 820  ? 25.695  -16.068 36.864  1.00 241.83 ? 820  PHE A CE1 1 
ATOM   6219  C  CE2 . PHE A 1 820  ? 27.114  -16.158 34.942  1.00 241.95 ? 820  PHE A CE2 1 
ATOM   6220  C  CZ  . PHE A 1 820  ? 26.948  -16.205 36.316  1.00 243.34 ? 820  PHE A CZ  1 
ATOM   6221  N  N   . LYS A 1 821  ? 24.345  -18.819 34.166  1.00 246.58 ? 821  LYS A N   1 
ATOM   6222  C  CA  . LYS A 1 821  ? 24.718  -19.921 35.049  1.00 250.66 ? 821  LYS A CA  1 
ATOM   6223  C  C   . LYS A 1 821  ? 25.796  -19.475 36.045  1.00 250.94 ? 821  LYS A C   1 
ATOM   6224  O  O   . LYS A 1 821  ? 26.768  -18.836 35.656  1.00 252.02 ? 821  LYS A O   1 
ATOM   6225  C  CB  . LYS A 1 821  ? 25.219  -21.093 34.197  1.00 252.06 ? 821  LYS A CB  1 
ATOM   6226  C  CG  . LYS A 1 821  ? 25.617  -22.341 34.966  1.00 250.96 ? 821  LYS A CG  1 
ATOM   6227  C  CD  . LYS A 1 821  ? 24.671  -23.507 34.680  1.00 250.64 ? 821  LYS A CD  1 
ATOM   6228  C  CE  . LYS A 1 821  ? 25.286  -24.840 35.108  1.00 252.45 ? 821  LYS A CE  1 
ATOM   6229  N  NZ  . LYS A 1 821  ? 24.368  -26.003 34.908  1.00 254.80 ? 821  LYS A NZ  1 
ATOM   6230  N  N   . ASP A 1 822  ? 25.631  -19.825 37.321  1.00 257.23 ? 822  ASP A N   1 
ATOM   6231  C  CA  . ASP A 1 822  ? 26.546  -19.377 38.380  1.00 256.88 ? 822  ASP A CA  1 
ATOM   6232  C  C   . ASP A 1 822  ? 28.025  -19.556 38.029  1.00 256.29 ? 822  ASP A C   1 
ATOM   6233  O  O   . ASP A 1 822  ? 28.781  -18.587 37.933  1.00 248.71 ? 822  ASP A O   1 
ATOM   6234  C  CB  . ASP A 1 822  ? 26.259  -20.116 39.699  1.00 267.19 ? 822  ASP A CB  1 
ATOM   6235  C  CG  . ASP A 1 822  ? 24.967  -19.661 40.374  1.00 274.09 ? 822  ASP A CG  1 
ATOM   6236  O  OD1 . ASP A 1 822  ? 24.015  -19.286 39.654  1.00 274.78 ? 822  ASP A OD1 1 
ATOM   6237  O  OD2 . ASP A 1 822  ? 24.904  -19.695 41.629  1.00 278.70 ? 822  ASP A OD2 1 
ATOM   6238  N  N   . VAL A 1 823  ? 28.430  -20.809 37.857  1.00 180.79 ? 823  VAL A N   1 
ATOM   6239  C  CA  . VAL A 1 823  ? 29.809  -21.140 37.514  1.00 182.52 ? 823  VAL A CA  1 
ATOM   6240  C  C   . VAL A 1 823  ? 29.894  -22.117 36.353  1.00 189.39 ? 823  VAL A C   1 
ATOM   6241  O  O   . VAL A 1 823  ? 29.082  -23.036 36.233  1.00 197.39 ? 823  VAL A O   1 
ATOM   6242  C  CB  . VAL A 1 823  ? 30.522  -21.780 38.675  1.00 182.21 ? 823  VAL A CB  1 
ATOM   6243  C  CG1 . VAL A 1 823  ? 31.854  -22.346 38.222  1.00 181.91 ? 823  VAL A CG1 1 
ATOM   6244  C  CG2 . VAL A 1 823  ? 30.708  -20.761 39.753  1.00 177.79 ? 823  VAL A CG2 1 
ATOM   6245  N  N   . PHE A 1 824  ? 30.901  -21.940 35.509  1.00 186.87 ? 824  PHE A N   1 
ATOM   6246  C  CA  . PHE A 1 824  ? 30.963  -22.701 34.278  1.00 187.86 ? 824  PHE A CA  1 
ATOM   6247  C  C   . PHE A 1 824  ? 32.341  -22.603 33.664  1.00 182.30 ? 824  PHE A C   1 
ATOM   6248  O  O   . PHE A 1 824  ? 32.973  -21.554 33.689  1.00 175.42 ? 824  PHE A O   1 
ATOM   6249  C  CB  . PHE A 1 824  ? 29.904  -22.184 33.305  1.00 187.78 ? 824  PHE A CB  1 
ATOM   6250  C  CG  . PHE A 1 824  ? 29.988  -20.696 33.035  1.00 184.25 ? 824  PHE A CG  1 
ATOM   6251  C  CD1 . PHE A 1 824  ? 30.801  -20.207 32.028  1.00 185.06 ? 824  PHE A CD1 1 
ATOM   6252  C  CD2 . PHE A 1 824  ? 29.237  -19.788 33.771  1.00 181.94 ? 824  PHE A CD2 1 
ATOM   6253  C  CE1 . PHE A 1 824  ? 30.870  -18.841 31.766  1.00 180.48 ? 824  PHE A CE1 1 
ATOM   6254  C  CE2 . PHE A 1 824  ? 29.308  -18.417 33.510  1.00 177.40 ? 824  PHE A CE2 1 
ATOM   6255  C  CZ  . PHE A 1 824  ? 30.127  -17.948 32.512  1.00 176.39 ? 824  PHE A CZ  1 
ATOM   6256  N  N   . LEU A 1 825  ? 32.810  -23.716 33.126  1.00 194.88 ? 825  LEU A N   1 
ATOM   6257  C  CA  . LEU A 1 825  ? 34.105  -23.746 32.479  1.00 189.02 ? 825  LEU A CA  1 
ATOM   6258  C  C   . LEU A 1 825  ? 33.983  -23.496 30.986  1.00 187.85 ? 825  LEU A C   1 
ATOM   6259  O  O   . LEU A 1 825  ? 33.000  -23.897 30.359  1.00 190.39 ? 825  LEU A O   1 
ATOM   6260  C  CB  . LEU A 1 825  ? 34.756  -25.108 32.684  1.00 188.99 ? 825  LEU A CB  1 
ATOM   6261  C  CG  . LEU A 1 825  ? 35.680  -25.465 31.519  1.00 182.15 ? 825  LEU A CG  1 
ATOM   6262  C  CD1 . LEU A 1 825  ? 37.005  -24.757 31.691  1.00 175.17 ? 825  LEU A CD1 1 
ATOM   6263  C  CD2 . LEU A 1 825  ? 35.874  -26.964 31.387  1.00 186.89 ? 825  LEU A CD2 1 
ATOM   6264  N  N   . GLU A 1 826  ? 34.990  -22.844 30.413  1.00 231.13 ? 826  GLU A N   1 
ATOM   6265  C  CA  . GLU A 1 826  ? 35.141  -22.821 28.964  1.00 230.49 ? 826  GLU A CA  1 
ATOM   6266  C  C   . GLU A 1 826  ? 36.515  -23.371 28.601  1.00 231.58 ? 826  GLU A C   1 
ATOM   6267  O  O   . GLU A 1 826  ? 37.461  -23.283 29.384  1.00 228.82 ? 826  GLU A O   1 
ATOM   6268  C  CB  . GLU A 1 826  ? 34.988  -21.409 28.405  1.00 225.61 ? 826  GLU A CB  1 
ATOM   6269  C  CG  . GLU A 1 826  ? 36.308  -20.686 28.225  1.00 225.14 ? 826  GLU A CG  1 
ATOM   6270  C  CD  . GLU A 1 826  ? 36.221  -19.576 27.210  1.00 223.47 ? 826  GLU A CD  1 
ATOM   6271  O  OE1 . GLU A 1 826  ? 37.265  -19.224 26.621  1.00 222.28 ? 826  GLU A OE1 1 
ATOM   6272  O  OE2 . GLU A 1 826  ? 35.103  -19.067 26.997  1.00 222.72 ? 826  GLU A OE2 1 
ATOM   6273  N  N   . MET A 1 827  ? 36.629  -23.941 27.413  1.00 165.79 ? 827  MET A N   1 
ATOM   6274  C  CA  . MET A 1 827  ? 37.888  -24.515 26.997  1.00 166.53 ? 827  MET A CA  1 
ATOM   6275  C  C   . MET A 1 827  ? 38.233  -23.899 25.661  1.00 161.32 ? 827  MET A C   1 
ATOM   6276  O  O   . MET A 1 827  ? 37.452  -23.996 24.727  1.00 163.88 ? 827  MET A O   1 
ATOM   6277  C  CB  . MET A 1 827  ? 37.756  -26.036 26.872  1.00 174.29 ? 827  MET A CB  1 
ATOM   6278  C  CG  . MET A 1 827  ? 37.520  -26.786 28.197  1.00 177.80 ? 827  MET A CG  1 
ATOM   6279  S  SD  . MET A 1 827  ? 38.956  -26.878 29.303  1.00 166.10 ? 827  MET A SD  1 
ATOM   6280  C  CE  . MET A 1 827  ? 40.177  -27.747 28.316  1.00 154.75 ? 827  MET A CE  1 
ATOM   6281  N  N   . ASN A 1 828  ? 39.381  -23.242 25.561  1.00 207.15 ? 828  ASN A N   1 
ATOM   6282  C  CA  . ASN A 1 828  ? 39.809  -22.723 24.267  1.00 203.73 ? 828  ASN A CA  1 
ATOM   6283  C  C   . ASN A 1 828  ? 40.612  -23.771 23.465  1.00 202.84 ? 828  ASN A C   1 
ATOM   6284  O  O   . ASN A 1 828  ? 41.843  -23.784 23.524  1.00 202.40 ? 828  ASN A O   1 
ATOM   6285  C  CB  . ASN A 1 828  ? 40.604  -21.415 24.432  1.00 206.07 ? 828  ASN A CB  1 
ATOM   6286  C  CG  . ASN A 1 828  ? 40.690  -20.600 23.137  1.00 211.22 ? 828  ASN A CG  1 
ATOM   6287  O  OD1 . ASN A 1 828  ? 39.745  -19.903 22.770  1.00 212.36 ? 828  ASN A OD1 1 
ATOM   6288  N  ND2 . ASN A 1 828  ? 41.833  -20.673 22.456  1.00 214.32 ? 828  ASN A ND2 1 
ATOM   6289  N  N   . ILE A 1 829  ? 39.908  -24.652 22.739  1.00 158.82 ? 829  ILE A N   1 
ATOM   6290  C  CA  . ILE A 1 829  ? 40.528  -25.627 21.824  1.00 154.58 ? 829  ILE A CA  1 
ATOM   6291  C  C   . ILE A 1 829  ? 41.085  -24.885 20.608  1.00 150.77 ? 829  ILE A C   1 
ATOM   6292  O  O   . ILE A 1 829  ? 40.608  -23.802 20.288  1.00 149.60 ? 829  ILE A O   1 
ATOM   6293  C  CB  . ILE A 1 829  ? 39.501  -26.681 21.339  1.00 156.37 ? 829  ILE A CB  1 
ATOM   6294  C  CG1 . ILE A 1 829  ? 38.574  -27.083 22.473  1.00 155.78 ? 829  ILE A CG1 1 
ATOM   6295  C  CG2 . ILE A 1 829  ? 40.193  -27.918 20.776  1.00 160.35 ? 829  ILE A CG2 1 
ATOM   6296  C  CD1 . ILE A 1 829  ? 39.273  -27.824 23.581  1.00 161.02 ? 829  ILE A CD1 1 
ATOM   6297  N  N   . PRO A 1 830  ? 42.111  -25.448 19.944  1.00 183.75 ? 830  PRO A N   1 
ATOM   6298  C  CA  . PRO A 1 830  ? 42.671  -24.842 18.726  1.00 185.57 ? 830  PRO A CA  1 
ATOM   6299  C  C   . PRO A 1 830  ? 41.874  -25.187 17.484  1.00 202.59 ? 830  PRO A C   1 
ATOM   6300  O  O   . PRO A 1 830  ? 40.996  -26.049 17.544  1.00 218.31 ? 830  PRO A O   1 
ATOM   6301  C  CB  . PRO A 1 830  ? 44.043  -25.503 18.596  1.00 180.29 ? 830  PRO A CB  1 
ATOM   6302  C  CG  . PRO A 1 830  ? 44.273  -26.237 19.871  1.00 179.65 ? 830  PRO A CG  1 
ATOM   6303  C  CD  . PRO A 1 830  ? 42.944  -26.554 20.439  1.00 182.29 ? 830  PRO A CD  1 
ATOM   6304  N  N   . TYR A 1 831  ? 42.176  -24.540 16.363  1.00 224.14 ? 831  TYR A N   1 
ATOM   6305  C  CA  . TYR A 1 831  ? 41.575  -24.994 15.125  1.00 227.73 ? 831  TYR A CA  1 
ATOM   6306  C  C   . TYR A 1 831  ? 42.084  -26.413 14.927  1.00 230.24 ? 831  TYR A C   1 
ATOM   6307  O  O   . TYR A 1 831  ? 41.346  -27.376 15.123  1.00 235.27 ? 831  TYR A O   1 
ATOM   6308  C  CB  . TYR A 1 831  ? 41.904  -24.084 13.925  1.00 228.60 ? 831  TYR A CB  1 
ATOM   6309  C  CG  . TYR A 1 831  ? 41.269  -24.548 12.616  1.00 235.85 ? 831  TYR A CG  1 
ATOM   6310  C  CD1 . TYR A 1 831  ? 41.988  -24.561 11.429  1.00 237.38 ? 831  TYR A CD1 1 
ATOM   6311  C  CD2 . TYR A 1 831  ? 39.952  -24.993 12.579  1.00 238.93 ? 831  TYR A CD2 1 
ATOM   6312  C  CE1 . TYR A 1 831  ? 41.411  -24.996 10.249  1.00 241.98 ? 831  TYR A CE1 1 
ATOM   6313  C  CE2 . TYR A 1 831  ? 39.371  -25.429 11.405  1.00 243.77 ? 831  TYR A CE2 1 
ATOM   6314  C  CZ  . TYR A 1 831  ? 40.105  -25.430 10.245  1.00 245.39 ? 831  TYR A CZ  1 
ATOM   6315  O  OH  . TYR A 1 831  ? 39.527  -25.866 9.077   1.00 250.33 ? 831  TYR A OH  1 
ATOM   6316  N  N   . SER A 1 832  ? 43.366  -26.546 14.611  1.00 163.46 ? 832  SER A N   1 
ATOM   6317  C  CA  . SER A 1 832  ? 43.893  -27.847 14.237  1.00 170.81 ? 832  SER A CA  1 
ATOM   6318  C  C   . SER A 1 832  ? 45.170  -28.162 14.973  1.00 170.00 ? 832  SER A C   1 
ATOM   6319  O  O   . SER A 1 832  ? 45.802  -27.275 15.546  1.00 165.45 ? 832  SER A O   1 
ATOM   6320  C  CB  . SER A 1 832  ? 44.193  -27.883 12.748  1.00 175.47 ? 832  SER A CB  1 
ATOM   6321  O  OG  . SER A 1 832  ? 45.417  -27.222 12.481  1.00 174.58 ? 832  SER A OG  1 
ATOM   6322  N  N   . VAL A 1 833  ? 45.554  -29.436 14.904  1.00 175.53 ? 833  VAL A N   1 
ATOM   6323  C  CA  . VAL A 1 833  ? 46.731  -29.976 15.568  1.00 174.76 ? 833  VAL A CA  1 
ATOM   6324  C  C   . VAL A 1 833  ? 47.322  -31.087 14.707  1.00 177.48 ? 833  VAL A C   1 
ATOM   6325  O  O   . VAL A 1 833  ? 46.605  -32.006 14.294  1.00 181.62 ? 833  VAL A O   1 
ATOM   6326  C  CB  . VAL A 1 833  ? 46.345  -30.651 16.872  1.00 176.58 ? 833  VAL A CB  1 
ATOM   6327  C  CG1 . VAL A 1 833  ? 47.583  -31.018 17.628  1.00 176.57 ? 833  VAL A CG1 1 
ATOM   6328  C  CG2 . VAL A 1 833  ? 45.444  -29.755 17.686  1.00 173.68 ? 833  VAL A CG2 1 
ATOM   6329  N  N   . VAL A 1 834  ? 48.624  -31.012 14.447  1.00 187.86 ? 834  VAL A N   1 
ATOM   6330  C  CA  . VAL A 1 834  ? 49.337  -32.059 13.719  1.00 193.03 ? 834  VAL A CA  1 
ATOM   6331  C  C   . VAL A 1 834  ? 49.548  -33.302 14.598  1.00 201.87 ? 834  VAL A C   1 
ATOM   6332  O  O   . VAL A 1 834  ? 50.066  -33.187 15.709  1.00 201.36 ? 834  VAL A O   1 
ATOM   6333  C  CB  . VAL A 1 834  ? 50.717  -31.523 13.239  1.00 189.51 ? 834  VAL A CB  1 
ATOM   6334  C  CG1 . VAL A 1 834  ? 51.587  -32.631 12.695  1.00 195.25 ? 834  VAL A CG1 1 
ATOM   6335  C  CG2 . VAL A 1 834  ? 50.537  -30.406 12.215  1.00 184.00 ? 834  VAL A CG2 1 
ATOM   6336  N  N   . ARG A 1 835  ? 49.151  -34.482 14.116  1.00 196.36 ? 835  ARG A N   1 
ATOM   6337  C  CA  . ARG A 1 835  ? 49.479  -35.727 14.817  1.00 206.96 ? 835  ARG A CA  1 
ATOM   6338  C  C   . ARG A 1 835  ? 50.863  -35.558 15.424  1.00 206.25 ? 835  ARG A C   1 
ATOM   6339  O  O   . ARG A 1 835  ? 51.741  -34.944 14.813  1.00 203.85 ? 835  ARG A O   1 
ATOM   6340  C  CB  . ARG A 1 835  ? 49.446  -36.946 13.860  1.00 216.18 ? 835  ARG A CB  1 
ATOM   6341  C  CG  . ARG A 1 835  ? 50.393  -38.124 14.213  1.00 224.63 ? 835  ARG A CG  1 
ATOM   6342  C  CD  . ARG A 1 835  ? 50.002  -39.461 13.547  1.00 234.81 ? 835  ARG A CD  1 
ATOM   6343  N  NE  . ARG A 1 835  ? 49.901  -39.388 12.095  1.00 235.54 ? 835  ARG A NE  1 
ATOM   6344  C  CZ  . ARG A 1 835  ? 50.772  -38.760 11.317  1.00 231.41 ? 835  ARG A CZ  1 
ATOM   6345  N  NH1 . ARG A 1 835  ? 51.822  -38.146 11.836  1.00 225.68 ? 835  ARG A NH1 1 
ATOM   6346  N  NH2 . ARG A 1 835  ? 50.595  -38.746 10.011  1.00 232.41 ? 835  ARG A NH2 1 
ATOM   6347  N  N   . GLY A 1 836  ? 51.046  -36.058 16.640  1.00 225.07 ? 836  GLY A N   1 
ATOM   6348  C  CA  . GLY A 1 836  ? 52.370  -36.130 17.233  1.00 226.65 ? 836  GLY A CA  1 
ATOM   6349  C  C   . GLY A 1 836  ? 52.923  -34.861 17.851  1.00 221.36 ? 836  GLY A C   1 
ATOM   6350  O  O   . GLY A 1 836  ? 53.958  -34.891 18.511  1.00 220.08 ? 836  GLY A O   1 
ATOM   6351  N  N   . GLU A 1 837  ? 52.268  -33.735 17.628  1.00 222.37 ? 837  GLU A N   1 
ATOM   6352  C  CA  . GLU A 1 837  ? 52.654  -32.544 18.356  1.00 217.21 ? 837  GLU A CA  1 
ATOM   6353  C  C   . GLU A 1 837  ? 52.049  -32.646 19.751  1.00 221.29 ? 837  GLU A C   1 
ATOM   6354  O  O   . GLU A 1 837  ? 51.026  -33.307 19.943  1.00 225.01 ? 837  GLU A O   1 
ATOM   6355  C  CB  . GLU A 1 837  ? 52.169  -31.288 17.641  1.00 210.15 ? 837  GLU A CB  1 
ATOM   6356  C  CG  . GLU A 1 837  ? 52.941  -30.941 16.368  1.00 196.52 ? 837  GLU A CG  1 
ATOM   6357  C  CD  . GLU A 1 837  ? 52.445  -29.651 15.717  1.00 186.87 ? 837  GLU A CD  1 
ATOM   6358  O  OE1 . GLU A 1 837  ? 51.215  -29.481 15.563  1.00 186.29 ? 837  GLU A OE1 1 
ATOM   6359  O  OE2 . GLU A 1 837  ? 53.278  -28.800 15.347  1.00 180.13 ? 837  GLU A OE2 1 
ATOM   6360  N  N   . GLN A 1 838  ? 52.702  -32.025 20.727  1.00 206.17 ? 838  GLN A N   1 
ATOM   6361  C  CA  . GLN A 1 838  ? 52.189  -31.965 22.089  1.00 206.43 ? 838  GLN A CA  1 
ATOM   6362  C  C   . GLN A 1 838  ? 51.459  -30.635 22.234  1.00 199.26 ? 838  GLN A C   1 
ATOM   6363  O  O   . GLN A 1 838  ? 52.057  -29.578 22.069  1.00 191.57 ? 838  GLN A O   1 
ATOM   6364  C  CB  . GLN A 1 838  ? 53.358  -32.066 23.081  1.00 209.15 ? 838  GLN A CB  1 
ATOM   6365  C  CG  . GLN A 1 838  ? 52.991  -32.158 24.585  1.00 214.44 ? 838  GLN A CG  1 
ATOM   6366  C  CD  . GLN A 1 838  ? 54.228  -32.139 25.538  1.00 224.47 ? 838  GLN A CD  1 
ATOM   6367  O  OE1 . GLN A 1 838  ? 54.719  -33.190 25.974  1.00 232.70 ? 838  GLN A OE1 1 
ATOM   6368  N  NE2 . GLN A 1 838  ? 54.710  -30.939 25.869  1.00 220.26 ? 838  GLN A NE2 1 
ATOM   6369  N  N   . ILE A 1 839  ? 50.164  -30.672 22.516  1.00 239.66 ? 839  ILE A N   1 
ATOM   6370  C  CA  . ILE A 1 839  ? 49.399  -29.429 22.590  1.00 234.31 ? 839  ILE A CA  1 
ATOM   6371  C  C   . ILE A 1 839  ? 49.124  -28.980 24.024  1.00 235.60 ? 839  ILE A C   1 
ATOM   6372  O  O   . ILE A 1 839  ? 49.104  -29.800 24.936  1.00 242.00 ? 839  ILE A O   1 
ATOM   6373  C  CB  . ILE A 1 839  ? 48.054  -29.558 21.863  1.00 234.78 ? 839  ILE A CB  1 
ATOM   6374  C  CG1 . ILE A 1 839  ? 47.462  -28.175 21.589  1.00 227.92 ? 839  ILE A CG1 1 
ATOM   6375  C  CG2 . ILE A 1 839  ? 47.092  -30.391 22.678  1.00 238.67 ? 839  ILE A CG2 1 
ATOM   6376  C  CD1 . ILE A 1 839  ? 48.264  -27.357 20.597  1.00 224.45 ? 839  ILE A CD1 1 
ATOM   6377  N  N   . GLN A 1 840  ? 48.907  -27.681 24.225  1.00 183.10 ? 840  GLN A N   1 
ATOM   6378  C  CA  . GLN A 1 840  ? 48.458  -27.197 25.527  1.00 181.01 ? 840  GLN A CA  1 
ATOM   6379  C  C   . GLN A 1 840  ? 47.042  -26.624 25.469  1.00 171.65 ? 840  GLN A C   1 
ATOM   6380  O  O   . GLN A 1 840  ? 46.834  -25.462 25.119  1.00 164.44 ? 840  GLN A O   1 
ATOM   6381  C  CB  . GLN A 1 840  ? 49.436  -26.179 26.120  1.00 183.05 ? 840  GLN A CB  1 
ATOM   6382  C  CG  . GLN A 1 840  ? 49.821  -26.463 27.598  1.00 193.74 ? 840  GLN A CG  1 
ATOM   6383  C  CD  . GLN A 1 840  ? 49.311  -25.414 28.627  1.00 196.16 ? 840  GLN A CD  1 
ATOM   6384  O  OE1 . GLN A 1 840  ? 49.705  -25.440 29.797  1.00 200.32 ? 840  GLN A OE1 1 
ATOM   6385  N  NE2 . GLN A 1 840  ? 48.440  -24.503 28.189  1.00 192.42 ? 840  GLN A NE2 1 
ATOM   6386  N  N   . LEU A 1 841  ? 46.079  -27.467 25.832  1.00 220.95 ? 841  LEU A N   1 
ATOM   6387  C  CA  . LEU A 1 841  ? 44.662  -27.113 25.836  1.00 215.15 ? 841  LEU A CA  1 
ATOM   6388  C  C   . LEU A 1 841  ? 44.286  -26.194 26.989  1.00 209.41 ? 841  LEU A C   1 
ATOM   6389  O  O   . LEU A 1 841  ? 44.023  -26.663 28.094  1.00 210.39 ? 841  LEU A O   1 
ATOM   6390  C  CB  . LEU A 1 841  ? 43.802  -28.376 25.939  1.00 218.61 ? 841  LEU A CB  1 
ATOM   6391  C  CG  . LEU A 1 841  ? 43.813  -29.364 24.774  1.00 217.63 ? 841  LEU A CG  1 
ATOM   6392  C  CD1 . LEU A 1 841  ? 42.789  -30.460 25.028  1.00 221.80 ? 841  LEU A CD1 1 
ATOM   6393  C  CD2 . LEU A 1 841  ? 43.520  -28.642 23.466  1.00 211.34 ? 841  LEU A CD2 1 
ATOM   6394  N  N   . LYS A 1 842  ? 44.217  -24.894 26.733  1.00 198.89 ? 842  LYS A N   1 
ATOM   6395  C  CA  . LYS A 1 842  ? 43.878  -23.949 27.789  1.00 196.05 ? 842  LYS A CA  1 
ATOM   6396  C  C   . LYS A 1 842  ? 42.372  -23.803 28.011  1.00 197.11 ? 842  LYS A C   1 
ATOM   6397  O  O   . LYS A 1 842  ? 41.571  -24.567 27.476  1.00 200.01 ? 842  LYS A O   1 
ATOM   6398  C  CB  . LYS A 1 842  ? 44.503  -22.583 27.512  1.00 189.49 ? 842  LYS A CB  1 
ATOM   6399  C  CG  . LYS A 1 842  ? 46.015  -22.570 27.572  1.00 190.20 ? 842  LYS A CG  1 
ATOM   6400  C  CD  . LYS A 1 842  ? 46.536  -21.149 27.679  1.00 185.46 ? 842  LYS A CD  1 
ATOM   6401  C  CE  . LYS A 1 842  ? 48.039  -21.137 27.907  1.00 187.07 ? 842  LYS A CE  1 
ATOM   6402  N  NZ  . LYS A 1 842  ? 48.568  -19.754 28.065  1.00 183.89 ? 842  LYS A NZ  1 
ATOM   6403  N  N   . GLY A 1 843  ? 42.007  -22.813 28.818  1.00 161.60 ? 843  GLY A N   1 
ATOM   6404  C  CA  . GLY A 1 843  ? 40.621  -22.545 29.158  1.00 163.39 ? 843  GLY A CA  1 
ATOM   6405  C  C   . GLY A 1 843  ? 40.566  -21.839 30.501  1.00 162.98 ? 843  GLY A C   1 
ATOM   6406  O  O   . GLY A 1 843  ? 41.603  -21.637 31.131  1.00 163.61 ? 843  GLY A O   1 
ATOM   6407  N  N   . THR A 1 844  ? 39.372  -21.460 30.950  1.00 203.12 ? 844  THR A N   1 
ATOM   6408  C  CA  . THR A 1 844  ? 39.222  -20.802 32.250  1.00 204.29 ? 844  THR A CA  1 
ATOM   6409  C  C   . THR A 1 844  ? 37.819  -21.034 32.831  1.00 203.34 ? 844  THR A C   1 
ATOM   6410  O  O   . THR A 1 844  ? 36.818  -20.791 32.156  1.00 201.28 ? 844  THR A O   1 
ATOM   6411  C  CB  . THR A 1 844  ? 39.493  -19.277 32.156  1.00 179.85 ? 844  THR A CB  1 
ATOM   6412  O  OG1 . THR A 1 844  ? 38.344  -18.611 31.624  1.00 176.08 ? 844  THR A OG1 1 
ATOM   6413  C  CG2 . THR A 1 844  ? 40.703  -18.968 31.269  1.00 171.71 ? 844  THR A CG2 1 
ATOM   6414  N  N   . VAL A 1 845  ? 37.746  -21.503 34.078  1.00 170.95 ? 845  VAL A N   1 
ATOM   6415  C  CA  . VAL A 1 845  ? 36.454  -21.771 34.726  1.00 173.81 ? 845  VAL A CA  1 
ATOM   6416  C  C   . VAL A 1 845  ? 35.840  -20.532 35.374  1.00 168.15 ? 845  VAL A C   1 
ATOM   6417  O  O   . VAL A 1 845  ? 36.519  -19.797 36.077  1.00 163.62 ? 845  VAL A O   1 
ATOM   6418  C  CB  . VAL A 1 845  ? 36.567  -22.868 35.797  1.00 144.23 ? 845  VAL A CB  1 
ATOM   6419  C  CG1 . VAL A 1 845  ? 37.848  -22.701 36.591  1.00 143.76 ? 845  VAL A CG1 1 
ATOM   6420  C  CG2 . VAL A 1 845  ? 35.340  -22.842 36.702  1.00 144.99 ? 845  VAL A CG2 1 
ATOM   6421  N  N   . TYR A 1 846  ? 34.552  -20.300 35.155  1.00 216.83 ? 846  TYR A N   1 
ATOM   6422  C  CA  . TYR A 1 846  ? 33.979  -19.032 35.587  1.00 212.10 ? 846  TYR A CA  1 
ATOM   6423  C  C   . TYR A 1 846  ? 33.216  -19.050 36.899  1.00 219.38 ? 846  TYR A C   1 
ATOM   6424  O  O   . TYR A 1 846  ? 32.232  -19.768 37.058  1.00 222.12 ? 846  TYR A O   1 
ATOM   6425  C  CB  . TYR A 1 846  ? 33.143  -18.387 34.478  1.00 202.44 ? 846  TYR A CB  1 
ATOM   6426  C  CG  . TYR A 1 846  ? 33.992  -17.768 33.394  1.00 193.03 ? 846  TYR A CG  1 
ATOM   6427  C  CD1 . TYR A 1 846  ? 33.555  -17.715 32.080  1.00 190.04 ? 846  TYR A CD1 1 
ATOM   6428  C  CD2 . TYR A 1 846  ? 35.245  -17.251 33.688  1.00 188.60 ? 846  TYR A CD2 1 
ATOM   6429  C  CE1 . TYR A 1 846  ? 34.337  -17.154 31.082  1.00 184.93 ? 846  TYR A CE1 1 
ATOM   6430  C  CE2 . TYR A 1 846  ? 36.039  -16.690 32.699  1.00 182.98 ? 846  TYR A CE2 1 
ATOM   6431  C  CZ  . TYR A 1 846  ? 35.583  -16.642 31.394  1.00 181.13 ? 846  TYR A CZ  1 
ATOM   6432  O  OH  . TYR A 1 846  ? 36.378  -16.081 30.409  1.00 177.07 ? 846  TYR A OH  1 
ATOM   6433  N  N   . ASN A 1 847  ? 33.699  -18.234 37.832  1.00 187.90 ? 847  ASN A N   1 
ATOM   6434  C  CA  . ASN A 1 847  ? 32.992  -17.965 39.078  1.00 195.46 ? 847  ASN A CA  1 
ATOM   6435  C  C   . ASN A 1 847  ? 32.240  -16.648 39.011  1.00 192.38 ? 847  ASN A C   1 
ATOM   6436  O  O   . ASN A 1 847  ? 32.834  -15.588 38.808  1.00 184.82 ? 847  ASN A O   1 
ATOM   6437  C  CB  . ASN A 1 847  ? 33.953  -17.933 40.273  1.00 200.28 ? 847  ASN A CB  1 
ATOM   6438  C  CG  . ASN A 1 847  ? 33.224  -17.867 41.610  1.00 201.94 ? 847  ASN A CG  1 
ATOM   6439  O  OD1 . ASN A 1 847  ? 32.266  -17.109 41.775  1.00 202.65 ? 847  ASN A OD1 1 
ATOM   6440  N  ND2 . ASN A 1 847  ? 33.676  -18.668 42.568  1.00 199.83 ? 847  ASN A ND2 1 
ATOM   6441  N  N   . TYR A 1 848  ? 30.929  -16.723 39.192  1.00 255.19 ? 848  TYR A N   1 
ATOM   6442  C  CA  . TYR A 1 848  ? 30.118  -15.526 39.294  1.00 253.95 ? 848  TYR A CA  1 
ATOM   6443  C  C   . TYR A 1 848  ? 29.189  -15.602 40.498  1.00 257.62 ? 848  TYR A C   1 
ATOM   6444  O  O   . TYR A 1 848  ? 28.301  -14.772 40.663  1.00 253.70 ? 848  TYR A O   1 
ATOM   6445  C  CB  . TYR A 1 848  ? 29.345  -15.275 38.003  1.00 253.26 ? 848  TYR A CB  1 
ATOM   6446  C  CG  . TYR A 1 848  ? 30.214  -14.786 36.870  1.00 249.65 ? 848  TYR A CG  1 
ATOM   6447  C  CD1 . TYR A 1 848  ? 31.371  -14.061 37.120  1.00 245.62 ? 848  TYR A CD1 1 
ATOM   6448  C  CD2 . TYR A 1 848  ? 29.870  -15.034 35.550  1.00 249.18 ? 848  TYR A CD2 1 
ATOM   6449  C  CE1 . TYR A 1 848  ? 32.167  -13.610 36.090  1.00 242.57 ? 848  TYR A CE1 1 
ATOM   6450  C  CE2 . TYR A 1 848  ? 30.653  -14.587 34.514  1.00 246.06 ? 848  TYR A CE2 1 
ATOM   6451  C  CZ  . TYR A 1 848  ? 31.800  -13.876 34.788  1.00 243.83 ? 848  TYR A CZ  1 
ATOM   6452  O  OH  . TYR A 1 848  ? 32.582  -13.433 33.749  1.00 243.51 ? 848  TYR A OH  1 
ATOM   6453  N  N   . ARG A 1 849  ? 29.395  -16.609 41.336  1.00 224.35 ? 849  ARG A N   1 
ATOM   6454  C  CA  . ARG A 1 849  ? 28.764  -16.635 42.646  1.00 227.86 ? 849  ARG A CA  1 
ATOM   6455  C  C   . ARG A 1 849  ? 29.520  -15.618 43.526  1.00 221.55 ? 849  ARG A C   1 
ATOM   6456  O  O   . ARG A 1 849  ? 30.726  -15.421 43.334  1.00 219.48 ? 849  ARG A O   1 
ATOM   6457  C  CB  . ARG A 1 849  ? 28.803  -18.062 43.203  1.00 231.80 ? 849  ARG A CB  1 
ATOM   6458  C  CG  . ARG A 1 849  ? 28.196  -18.252 44.573  1.00 232.01 ? 849  ARG A CG  1 
ATOM   6459  C  CD  . ARG A 1 849  ? 26.730  -17.867 44.638  1.00 237.98 ? 849  ARG A CD  1 
ATOM   6460  N  NE  . ARG A 1 849  ? 26.257  -17.911 46.022  1.00 236.54 ? 849  ARG A NE  1 
ATOM   6461  C  CZ  . ARG A 1 849  ? 25.209  -17.235 46.489  1.00 236.63 ? 849  ARG A CZ  1 
ATOM   6462  N  NH1 . ARG A 1 849  ? 24.509  -16.451 45.683  1.00 240.29 ? 849  ARG A NH1 1 
ATOM   6463  N  NH2 . ARG A 1 849  ? 24.859  -17.338 47.765  1.00 232.03 ? 849  ARG A NH2 1 
ATOM   6464  N  N   . THR A 1 850  ? 28.811  -14.962 44.458  1.00 209.56 ? 850  THR A N   1 
ATOM   6465  C  CA  . THR A 1 850  ? 29.364  -13.860 45.285  1.00 203.03 ? 850  THR A CA  1 
ATOM   6466  C  C   . THR A 1 850  ? 30.638  -14.236 46.040  1.00 199.55 ? 850  THR A C   1 
ATOM   6467  O  O   . THR A 1 850  ? 31.670  -13.568 45.936  1.00 199.77 ? 850  THR A O   1 
ATOM   6468  C  CB  . THR A 1 850  ? 28.326  -13.290 46.332  1.00 196.76 ? 850  THR A CB  1 
ATOM   6469  O  OG1 . THR A 1 850  ? 27.890  -14.326 47.221  1.00 194.49 ? 850  THR A OG1 1 
ATOM   6470  C  CG2 . THR A 1 850  ? 27.110  -12.660 45.654  1.00 199.27 ? 850  THR A CG2 1 
ATOM   6471  N  N   . SER A 1 851  ? 30.537  -15.303 46.817  1.00 209.70 ? 851  SER A N   1 
ATOM   6472  C  CA  . SER A 1 851  ? 31.667  -15.873 47.522  1.00 207.91 ? 851  SER A CA  1 
ATOM   6473  C  C   . SER A 1 851  ? 32.507  -16.698 46.562  1.00 213.72 ? 851  SER A C   1 
ATOM   6474  O  O   . SER A 1 851  ? 32.083  -16.965 45.443  1.00 216.93 ? 851  SER A O   1 
ATOM   6475  C  CB  . SER A 1 851  ? 31.138  -16.802 48.599  1.00 207.26 ? 851  SER A CB  1 
ATOM   6476  O  OG  . SER A 1 851  ? 30.278  -17.767 48.015  1.00 214.18 ? 851  SER A OG  1 
ATOM   6477  N  N   . GLY A 1 852  ? 33.688  -17.121 47.009  1.00 171.59 ? 852  GLY A N   1 
ATOM   6478  C  CA  . GLY A 1 852  ? 34.513  -18.055 46.254  1.00 174.86 ? 852  GLY A CA  1 
ATOM   6479  C  C   . GLY A 1 852  ? 34.032  -19.499 46.339  1.00 172.25 ? 852  GLY A C   1 
ATOM   6480  O  O   . GLY A 1 852  ? 32.986  -19.764 46.936  1.00 171.81 ? 852  GLY A O   1 
ATOM   6481  N  N   . MET A 1 853  ? 34.778  -20.431 45.737  1.00 153.32 ? 853  MET A N   1 
ATOM   6482  C  CA  . MET A 1 853  ? 34.448  -21.861 45.857  1.00 150.80 ? 853  MET A CA  1 
ATOM   6483  C  C   . MET A 1 853  ? 35.469  -22.888 45.339  1.00 149.88 ? 853  MET A C   1 
ATOM   6484  O  O   . MET A 1 853  ? 36.557  -22.553 44.870  1.00 149.06 ? 853  MET A O   1 
ATOM   6485  C  CB  . MET A 1 853  ? 33.051  -22.172 45.298  1.00 155.69 ? 853  MET A CB  1 
ATOM   6486  C  CG  . MET A 1 853  ? 32.780  -21.739 43.871  1.00 161.92 ? 853  MET A CG  1 
ATOM   6487  S  SD  . MET A 1 853  ? 30.997  -21.777 43.596  1.00 191.93 ? 853  MET A SD  1 
ATOM   6488  C  CE  . MET A 1 853  ? 30.463  -20.426 44.639  1.00 196.33 ? 853  MET A CE  1 
ATOM   6489  N  N   . GLN A 1 854  ? 35.097  -24.154 45.453  1.00 262.57 ? 854  GLN A N   1 
ATOM   6490  C  CA  . GLN A 1 854  ? 35.981  -25.235 45.072  1.00 263.94 ? 854  GLN A CA  1 
ATOM   6491  C  C   . GLN A 1 854  ? 35.466  -25.972 43.849  1.00 269.21 ? 854  GLN A C   1 
ATOM   6492  O  O   . GLN A 1 854  ? 34.272  -26.266 43.752  1.00 271.41 ? 854  GLN A O   1 
ATOM   6493  C  CB  . GLN A 1 854  ? 36.134  -26.199 46.233  1.00 262.03 ? 854  GLN A CB  1 
ATOM   6494  C  CG  . GLN A 1 854  ? 36.549  -25.510 47.508  1.00 255.43 ? 854  GLN A CG  1 
ATOM   6495  C  CD  . GLN A 1 854  ? 36.672  -26.482 48.652  1.00 253.39 ? 854  GLN A CD  1 
ATOM   6496  O  OE1 . GLN A 1 854  ? 36.277  -27.645 48.531  1.00 256.44 ? 854  GLN A OE1 1 
ATOM   6497  N  NE2 . GLN A 1 854  ? 37.219  -26.017 49.775  1.00 247.82 ? 854  GLN A NE2 1 
ATOM   6498  N  N   . PHE A 1 855  ? 36.379  -26.275 42.926  1.00 188.20 ? 855  PHE A N   1 
ATOM   6499  C  CA  . PHE A 1 855  ? 36.047  -26.953 41.672  1.00 192.00 ? 855  PHE A CA  1 
ATOM   6500  C  C   . PHE A 1 855  ? 36.891  -28.183 41.462  1.00 195.98 ? 855  PHE A C   1 
ATOM   6501  O  O   . PHE A 1 855  ? 37.631  -28.602 42.337  1.00 193.98 ? 855  PHE A O   1 
ATOM   6502  C  CB  . PHE A 1 855  ? 36.259  -26.034 40.480  1.00 190.90 ? 855  PHE A CB  1 
ATOM   6503  C  CG  . PHE A 1 855  ? 37.701  -25.635 40.255  1.00 185.10 ? 855  PHE A CG  1 
ATOM   6504  C  CD1 . PHE A 1 855  ? 38.668  -26.577 39.908  1.00 186.80 ? 855  PHE A CD1 1 
ATOM   6505  C  CD2 . PHE A 1 855  ? 38.075  -24.300 40.345  1.00 178.90 ? 855  PHE A CD2 1 
ATOM   6506  C  CE1 . PHE A 1 855  ? 39.974  -26.191 39.682  1.00 184.90 ? 855  PHE A CE1 1 
ATOM   6507  C  CE2 . PHE A 1 855  ? 39.378  -23.905 40.122  1.00 176.96 ? 855  PHE A CE2 1 
ATOM   6508  C  CZ  . PHE A 1 855  ? 40.325  -24.845 39.781  1.00 179.80 ? 855  PHE A CZ  1 
ATOM   6509  N  N   . CYS A 1 856  ? 36.812  -28.740 40.269  1.00 231.09 ? 856  CYS A N   1 
ATOM   6510  C  CA  . CYS A 1 856  ? 37.496  -29.981 40.017  1.00 235.10 ? 856  CYS A CA  1 
ATOM   6511  C  C   . CYS A 1 856  ? 37.298  -30.335 38.547  1.00 244.93 ? 856  CYS A C   1 
ATOM   6512  O  O   . CYS A 1 856  ? 36.362  -31.059 38.204  1.00 249.32 ? 856  CYS A O   1 
ATOM   6513  C  CB  . CYS A 1 856  ? 36.900  -31.062 40.929  1.00 234.13 ? 856  CYS A CB  1 
ATOM   6514  S  SG  . CYS A 1 856  ? 37.966  -32.461 41.358  1.00 273.29 ? 856  CYS A SG  1 
ATOM   6515  N  N   . VAL A 1 857  ? 38.156  -29.805 37.674  1.00 184.83 ? 857  VAL A N   1 
ATOM   6516  C  CA  . VAL A 1 857  ? 38.069  -30.103 36.244  1.00 191.58 ? 857  VAL A CA  1 
ATOM   6517  C  C   . VAL A 1 857  ? 38.952  -31.292 35.896  1.00 196.07 ? 857  VAL A C   1 
ATOM   6518  O  O   . VAL A 1 857  ? 40.123  -31.330 36.269  1.00 194.33 ? 857  VAL A O   1 
ATOM   6519  C  CB  . VAL A 1 857  ? 38.456  -28.889 35.362  1.00 190.56 ? 857  VAL A CB  1 
ATOM   6520  C  CG1 . VAL A 1 857  ? 37.406  -27.781 35.464  1.00 188.06 ? 857  VAL A CG1 1 
ATOM   6521  C  CG2 . VAL A 1 857  ? 39.842  -28.375 35.732  1.00 185.44 ? 857  VAL A CG2 1 
ATOM   6522  N  N   . LYS A 1 858  ? 38.380  -32.264 35.194  1.00 237.89 ? 858  LYS A N   1 
ATOM   6523  C  CA  . LYS A 1 858  ? 39.138  -33.414 34.717  1.00 243.19 ? 858  LYS A CA  1 
ATOM   6524  C  C   . LYS A 1 858  ? 38.815  -33.714 33.253  1.00 249.28 ? 858  LYS A C   1 
ATOM   6525  O  O   . LYS A 1 858  ? 37.654  -33.672 32.834  1.00 253.06 ? 858  LYS A O   1 
ATOM   6526  C  CB  . LYS A 1 858  ? 38.883  -34.641 35.599  1.00 247.08 ? 858  LYS A CB  1 
ATOM   6527  C  CG  . LYS A 1 858  ? 37.415  -34.925 35.861  1.00 253.60 ? 858  LYS A CG  1 
ATOM   6528  C  CD  . LYS A 1 858  ? 37.225  -36.148 36.744  1.00 257.12 ? 858  LYS A CD  1 
ATOM   6529  C  CE  . LYS A 1 858  ? 35.749  -36.468 36.902  1.00 262.67 ? 858  LYS A CE  1 
ATOM   6530  N  NZ  . LYS A 1 858  ? 35.525  -37.597 37.839  1.00 262.93 ? 858  LYS A NZ  1 
ATOM   6531  N  N   . MET A 1 859  ? 39.855  -34.005 32.478  1.00 250.36 ? 859  MET A N   1 
ATOM   6532  C  CA  . MET A 1 859  ? 39.704  -34.309 31.062  1.00 254.08 ? 859  MET A CA  1 
ATOM   6533  C  C   . MET A 1 859  ? 39.553  -35.805 30.821  1.00 258.20 ? 859  MET A C   1 
ATOM   6534  O  O   . MET A 1 859  ? 40.305  -36.613 31.363  1.00 256.34 ? 859  MET A O   1 
ATOM   6535  C  CB  . MET A 1 859  ? 40.904  -33.777 30.287  1.00 248.17 ? 859  MET A CB  1 
ATOM   6536  C  CG  . MET A 1 859  ? 41.182  -34.512 29.000  1.00 250.63 ? 859  MET A CG  1 
ATOM   6537  S  SD  . MET A 1 859  ? 42.730  -33.972 28.258  1.00 208.64 ? 859  MET A SD  1 
ATOM   6538  C  CE  . MET A 1 859  ? 42.242  -32.430 27.496  1.00 273.27 ? 859  MET A CE  1 
ATOM   6539  N  N   . SER A 1 860  ? 38.575  -36.166 30.000  1.00 280.60 ? 860  SER A N   1 
ATOM   6540  C  CA  . SER A 1 860  ? 38.326  -37.562 29.666  1.00 289.85 ? 860  SER A CA  1 
ATOM   6541  C  C   . SER A 1 860  ? 39.355  -38.085 28.670  1.00 292.69 ? 860  SER A C   1 
ATOM   6542  O  O   . SER A 1 860  ? 39.570  -37.484 27.622  1.00 289.63 ? 860  SER A O   1 
ATOM   6543  C  CB  . SER A 1 860  ? 36.919  -37.716 29.089  1.00 292.66 ? 860  SER A CB  1 
ATOM   6544  O  OG  . SER A 1 860  ? 36.831  -38.859 28.259  1.00 300.50 ? 860  SER A OG  1 
ATOM   6545  N  N   . ALA A 1 861  ? 39.985  -39.208 29.000  1.00 228.99 ? 861  ALA A N   1 
ATOM   6546  C  CA  . ALA A 1 861  ? 40.962  -39.835 28.112  1.00 231.83 ? 861  ALA A CA  1 
ATOM   6547  C  C   . ALA A 1 861  ? 40.302  -40.605 26.967  1.00 234.55 ? 861  ALA A C   1 
ATOM   6548  O  O   . ALA A 1 861  ? 39.817  -41.718 27.171  1.00 239.38 ? 861  ALA A O   1 
ATOM   6549  C  CB  . ALA A 1 861  ? 41.857  -40.765 28.905  1.00 228.82 ? 861  ALA A CB  1 
ATOM   6550  N  N   . VAL A 1 862  ? 40.295  -40.022 25.767  1.00 265.62 ? 862  VAL A N   1 
ATOM   6551  C  CA  . VAL A 1 862  ? 39.761  -40.693 24.574  1.00 269.96 ? 862  VAL A CA  1 
ATOM   6552  C  C   . VAL A 1 862  ? 40.838  -41.475 23.796  1.00 273.21 ? 862  VAL A C   1 
ATOM   6553  O  O   . VAL A 1 862  ? 41.904  -40.940 23.473  1.00 271.21 ? 862  VAL A O   1 
ATOM   6554  C  CB  . VAL A 1 862  ? 39.032  -39.697 23.630  1.00 265.76 ? 862  VAL A CB  1 
ATOM   6555  C  CG1 . VAL A 1 862  ? 38.609  -40.388 22.346  1.00 270.59 ? 862  VAL A CG1 1 
ATOM   6556  C  CG2 . VAL A 1 862  ? 37.822  -39.076 24.324  1.00 262.38 ? 862  VAL A CG2 1 
ATOM   6557  N  N   . GLU A 1 863  ? 40.535  -42.741 23.504  1.00 272.93 ? 863  GLU A N   1 
ATOM   6558  C  CA  . GLU A 1 863  ? 41.435  -43.669 22.799  1.00 275.39 ? 863  GLU A CA  1 
ATOM   6559  C  C   . GLU A 1 863  ? 42.824  -43.121 22.460  1.00 266.96 ? 863  GLU A C   1 
ATOM   6560  O  O   . GLU A 1 863  ? 43.790  -43.325 23.192  1.00 265.98 ? 863  GLU A O   1 
ATOM   6561  C  CB  . GLU A 1 863  ? 40.778  -44.199 21.506  1.00 285.35 ? 863  GLU A CB  1 
ATOM   6562  C  CG  . GLU A 1 863  ? 39.968  -45.513 21.623  1.00 304.90 ? 863  GLU A CG  1 
ATOM   6563  C  CD  . GLU A 1 863  ? 40.839  -46.766 21.657  1.00 316.58 ? 863  GLU A CD  1 
ATOM   6564  O  OE1 . GLU A 1 863  ? 41.921  -46.726 22.279  1.00 316.02 ? 863  GLU A OE1 1 
ATOM   6565  O  OE2 . GLU A 1 863  ? 40.439  -47.796 21.068  1.00 323.58 ? 863  GLU A OE2 1 
ATOM   6566  N  N   . GLY A 1 864  ? 42.908  -42.435 21.329  1.00 230.14 ? 864  GLY A N   1 
ATOM   6567  C  CA  . GLY A 1 864  ? 44.181  -42.160 20.697  1.00 227.38 ? 864  GLY A CA  1 
ATOM   6568  C  C   . GLY A 1 864  ? 44.851  -40.887 21.133  1.00 216.80 ? 864  GLY A C   1 
ATOM   6569  O  O   . GLY A 1 864  ? 45.895  -40.511 20.606  1.00 214.94 ? 864  GLY A O   1 
ATOM   6570  N  N   . ILE A 1 865  ? 44.249  -40.197 22.082  1.00 228.75 ? 865  ILE A N   1 
ATOM   6571  C  CA  . ILE A 1 865  ? 44.921  -39.039 22.631  1.00 218.36 ? 865  ILE A CA  1 
ATOM   6572  C  C   . ILE A 1 865  ? 45.796  -39.449 23.815  1.00 221.11 ? 865  ILE A C   1 
ATOM   6573  O  O   . ILE A 1 865  ? 45.476  -40.388 24.545  1.00 225.08 ? 865  ILE A O   1 
ATOM   6574  C  CB  . ILE A 1 865  ? 43.935  -37.939 23.002  1.00 208.90 ? 865  ILE A CB  1 
ATOM   6575  C  CG1 . ILE A 1 865  ? 42.780  -37.939 22.013  1.00 207.24 ? 865  ILE A CG1 1 
ATOM   6576  C  CG2 . ILE A 1 865  ? 44.630  -36.594 22.973  1.00 200.67 ? 865  ILE A CG2 1 
ATOM   6577  C  CD1 . ILE A 1 865  ? 41.906  -36.719 22.115  1.00 200.25 ? 865  ILE A CD1 1 
ATOM   6578  N  N   . CYS A 1 866  ? 46.918  -38.756 23.975  1.00 225.32 ? 866  CYS A N   1 
ATOM   6579  C  CA  . CYS A 1 866  ? 47.874  -39.065 25.021  1.00 232.63 ? 866  CYS A CA  1 
ATOM   6580  C  C   . CYS A 1 866  ? 47.685  -38.152 26.221  1.00 236.34 ? 866  CYS A C   1 
ATOM   6581  O  O   . CYS A 1 866  ? 47.225  -37.022 26.070  1.00 226.41 ? 866  CYS A O   1 
ATOM   6582  C  CB  . CYS A 1 866  ? 49.281  -38.908 24.477  1.00 229.77 ? 866  CYS A CB  1 
ATOM   6583  S  SG  . CYS A 1 866  ? 50.335  -40.226 25.003  1.00 241.13 ? 866  CYS A SG  1 
ATOM   6584  N  N   . THR A 1 867  ? 48.046  -38.635 27.408  1.00 279.08 ? 867  THR A N   1 
ATOM   6585  C  CA  . THR A 1 867  ? 47.928  -37.819 28.615  1.00 281.69 ? 867  THR A CA  1 
ATOM   6586  C  C   . THR A 1 867  ? 48.795  -38.263 29.785  1.00 288.53 ? 867  THR A C   1 
ATOM   6587  O  O   . THR A 1 867  ? 49.674  -39.116 29.658  1.00 291.16 ? 867  THR A O   1 
ATOM   6588  C  CB  . THR A 1 867  ? 46.475  -37.732 29.114  1.00 269.13 ? 867  THR A CB  1 
ATOM   6589  O  OG1 . THR A 1 867  ? 45.643  -38.586 28.322  1.00 274.98 ? 867  THR A OG1 1 
ATOM   6590  C  CG2 . THR A 1 867  ? 45.968  -36.301 29.024  1.00 265.43 ? 867  THR A CG2 1 
ATOM   6591  N  N   . SER A 1 868  ? 48.519  -37.663 30.934  1.00 255.04 ? 868  SER A N   1 
ATOM   6592  C  CA  . SER A 1 868  ? 49.356  -37.830 32.106  1.00 262.49 ? 868  SER A CA  1 
ATOM   6593  C  C   . SER A 1 868  ? 48.722  -38.734 33.179  1.00 273.97 ? 868  SER A C   1 
ATOM   6594  O  O   . SER A 1 868  ? 49.423  -39.261 34.046  1.00 270.65 ? 868  SER A O   1 
ATOM   6595  C  CB  . SER A 1 868  ? 49.713  -36.451 32.657  1.00 256.47 ? 868  SER A CB  1 
ATOM   6596  O  OG  . SER A 1 868  ? 50.040  -35.576 31.585  1.00 259.33 ? 868  SER A OG  1 
ATOM   6597  N  N   . GLU A 1 869  ? 47.401  -38.909 33.116  1.00 330.52 ? 869  GLU A N   1 
ATOM   6598  C  CA  . GLU A 1 869  ? 46.701  -39.901 33.940  1.00 342.27 ? 869  GLU A CA  1 
ATOM   6599  C  C   . GLU A 1 869  ? 46.977  -41.298 33.362  1.00 349.21 ? 869  GLU A C   1 
ATOM   6600  O  O   . GLU A 1 869  ? 47.275  -41.425 32.173  1.00 352.95 ? 869  GLU A O   1 
ATOM   6601  C  CB  . GLU A 1 869  ? 45.192  -39.596 33.972  1.00 344.69 ? 869  GLU A CB  1 
ATOM   6602  C  CG  . GLU A 1 869  ? 44.374  -40.364 35.016  1.00 344.02 ? 869  GLU A CG  1 
ATOM   6603  C  CD  . GLU A 1 869  ? 43.730  -41.628 34.463  1.00 348.76 ? 869  GLU A CD  1 
ATOM   6604  O  OE1 . GLU A 1 869  ? 43.660  -41.773 33.227  1.00 352.82 ? 869  GLU A OE1 1 
ATOM   6605  O  OE2 . GLU A 1 869  ? 43.285  -42.477 35.263  1.00 347.31 ? 869  GLU A OE2 1 
ATOM   6606  N  N   . SER A 1 870  ? 46.902  -42.340 34.191  1.00 269.72 ? 870  SER A N   1 
ATOM   6607  C  CA  . SER A 1 870  ? 47.175  -43.697 33.712  1.00 279.69 ? 870  SER A CA  1 
ATOM   6608  C  C   . SER A 1 870  ? 46.130  -44.106 32.685  1.00 288.73 ? 870  SER A C   1 
ATOM   6609  O  O   . SER A 1 870  ? 44.931  -44.071 32.963  1.00 290.15 ? 870  SER A O   1 
ATOM   6610  C  CB  . SER A 1 870  ? 47.201  -44.711 34.860  1.00 279.92 ? 870  SER A CB  1 
ATOM   6611  O  OG  . SER A 1 870  ? 45.898  -45.169 35.168  1.00 282.42 ? 870  SER A OG  1 
ATOM   6612  N  N   . LYS A 1 882  ? 41.606  -37.320 36.270  1.00 290.18 ? 882  LYS A N   1 
ATOM   6613  C  CA  . LYS A 1 882  ? 41.974  -37.229 37.685  1.00 284.53 ? 882  LYS A CA  1 
ATOM   6614  C  C   . LYS A 1 882  ? 41.429  -35.960 38.362  1.00 276.23 ? 882  LYS A C   1 
ATOM   6615  O  O   . LYS A 1 882  ? 41.226  -34.942 37.705  1.00 275.89 ? 882  LYS A O   1 
ATOM   6616  C  CB  . LYS A 1 882  ? 43.496  -37.313 37.850  1.00 284.50 ? 882  LYS A CB  1 
ATOM   6617  C  CG  . LYS A 1 882  ? 44.263  -36.089 37.366  1.00 284.52 ? 882  LYS A CG  1 
ATOM   6618  C  CD  . LYS A 1 882  ? 45.764  -36.237 37.601  1.00 284.08 ? 882  LYS A CD  1 
ATOM   6619  C  CE  . LYS A 1 882  ? 46.339  -37.408 36.814  1.00 291.58 ? 882  LYS A CE  1 
ATOM   6620  N  NZ  . LYS A 1 882  ? 47.799  -37.591 37.054  1.00 290.16 ? 882  LYS A NZ  1 
ATOM   6621  N  N   . CYS A 1 883  ? 41.201  -36.025 39.675  1.00 342.14 ? 883  CYS A N   1 
ATOM   6622  C  CA  . CYS A 1 883  ? 40.582  -34.918 40.418  1.00 334.70 ? 883  CYS A CA  1 
ATOM   6623  C  C   . CYS A 1 883  ? 41.583  -34.014 41.152  1.00 325.38 ? 883  CYS A C   1 
ATOM   6624  O  O   . CYS A 1 883  ? 41.924  -34.255 42.313  1.00 321.14 ? 883  CYS A O   1 
ATOM   6625  C  CB  . CYS A 1 883  ? 39.540  -35.459 41.406  1.00 333.16 ? 883  CYS A CB  1 
ATOM   6626  S  SG  . CYS A 1 883  ? 38.543  -34.197 42.243  1.00 381.19 ? 883  CYS A SG  1 
ATOM   6627  N  N   . VAL A 1 884  ? 42.032  -32.966 40.468  1.00 298.00 ? 884  VAL A N   1 
ATOM   6628  C  CA  . VAL A 1 884  ? 42.974  -32.000 41.028  1.00 290.94 ? 884  VAL A CA  1 
ATOM   6629  C  C   . VAL A 1 884  ? 42.254  -30.761 41.572  1.00 287.78 ? 884  VAL A C   1 
ATOM   6630  O  O   . VAL A 1 884  ? 42.309  -29.691 40.959  1.00 287.91 ? 884  VAL A O   1 
ATOM   6631  C  CB  . VAL A 1 884  ? 43.980  -31.555 39.951  1.00 257.78 ? 884  VAL A CB  1 
ATOM   6632  C  CG1 . VAL A 1 884  ? 44.972  -32.663 39.659  1.00 260.64 ? 884  VAL A CG1 1 
ATOM   6633  C  CG2 . VAL A 1 884  ? 43.245  -31.170 38.677  1.00 263.08 ? 884  VAL A CG2 1 
ATOM   6634  N  N   . ARG A 1 885  ? 41.590  -30.895 42.721  1.00 270.86 ? 885  ARG A N   1 
ATOM   6635  C  CA  . ARG A 1 885  ? 40.702  -29.824 43.190  1.00 266.47 ? 885  ARG A CA  1 
ATOM   6636  C  C   . ARG A 1 885  ? 41.417  -28.527 43.536  1.00 260.10 ? 885  ARG A C   1 
ATOM   6637  O  O   . ARG A 1 885  ? 42.463  -28.523 44.171  1.00 255.58 ? 885  ARG A O   1 
ATOM   6638  C  CB  . ARG A 1 885  ? 39.744  -30.269 44.317  1.00 263.88 ? 885  ARG A CB  1 
ATOM   6639  C  CG  . ARG A 1 885  ? 40.366  -30.658 45.649  1.00 259.07 ? 885  ARG A CG  1 
ATOM   6640  C  CD  . ARG A 1 885  ? 39.291  -30.813 46.756  1.00 256.47 ? 885  ARG A CD  1 
ATOM   6641  N  NE  . ARG A 1 885  ? 38.136  -31.611 46.331  1.00 261.77 ? 885  ARG A NE  1 
ATOM   6642  C  CZ  . ARG A 1 885  ? 37.096  -31.920 47.106  1.00 261.67 ? 885  ARG A CZ  1 
ATOM   6643  N  NH1 . ARG A 1 885  ? 37.051  -31.509 48.364  1.00 256.64 ? 885  ARG A NH1 1 
ATOM   6644  N  NH2 . ARG A 1 885  ? 36.096  -32.646 46.620  1.00 266.48 ? 885  ARG A NH2 1 
ATOM   6645  N  N   . GLN A 1 886  ? 40.823  -27.425 43.101  1.00 227.84 ? 886  GLN A N   1 
ATOM   6646  C  CA  . GLN A 1 886  ? 41.419  -26.111 43.253  1.00 225.32 ? 886  GLN A CA  1 
ATOM   6647  C  C   . GLN A 1 886  ? 40.371  -25.166 43.854  1.00 216.96 ? 886  GLN A C   1 
ATOM   6648  O  O   . GLN A 1 886  ? 39.257  -25.582 44.187  1.00 217.20 ? 886  GLN A O   1 
ATOM   6649  C  CB  . GLN A 1 886  ? 41.886  -25.609 41.888  1.00 235.74 ? 886  GLN A CB  1 
ATOM   6650  C  CG  . GLN A 1 886  ? 42.967  -24.564 41.888  1.00 239.58 ? 886  GLN A CG  1 
ATOM   6651  C  CD  . GLN A 1 886  ? 44.322  -25.170 41.671  1.00 244.80 ? 886  GLN A CD  1 
ATOM   6652  O  OE1 . GLN A 1 886  ? 45.293  -24.460 41.437  1.00 246.35 ? 886  GLN A OE1 1 
ATOM   6653  N  NE2 . GLN A 1 886  ? 44.398  -26.496 41.737  1.00 247.08 ? 886  GLN A NE2 1 
ATOM   6654  N  N   . LYS A 1 887  ? 40.729  -23.897 44.002  1.00 244.54 ? 887  LYS A N   1 
ATOM   6655  C  CA  . LYS A 1 887  ? 39.829  -22.932 44.612  1.00 238.98 ? 887  LYS A CA  1 
ATOM   6656  C  C   . LYS A 1 887  ? 39.763  -21.678 43.756  1.00 237.03 ? 887  LYS A C   1 
ATOM   6657  O  O   . LYS A 1 887  ? 40.775  -21.206 43.229  1.00 233.83 ? 887  LYS A O   1 
ATOM   6658  C  CB  . LYS A 1 887  ? 40.275  -22.590 46.041  1.00 233.29 ? 887  LYS A CB  1 
ATOM   6659  C  CG  . LYS A 1 887  ? 40.856  -23.764 46.849  1.00 233.16 ? 887  LYS A CG  1 
ATOM   6660  C  CD  . LYS A 1 887  ? 42.369  -23.924 46.612  1.00 234.81 ? 887  LYS A CD  1 
ATOM   6661  C  CE  . LYS A 1 887  ? 42.980  -25.131 47.336  1.00 234.13 ? 887  LYS A CE  1 
ATOM   6662  N  NZ  . LYS A 1 887  ? 43.391  -24.853 48.743  1.00 228.04 ? 887  LYS A NZ  1 
ATOM   6663  N  N   . VAL A 1 888  ? 38.557  -21.150 43.617  1.00 186.10 ? 888  VAL A N   1 
ATOM   6664  C  CA  . VAL A 1 888  ? 38.339  -19.944 42.842  1.00 186.99 ? 888  VAL A CA  1 
ATOM   6665  C  C   . VAL A 1 888  ? 37.884  -18.800 43.717  1.00 184.72 ? 888  VAL A C   1 
ATOM   6666  O  O   . VAL A 1 888  ? 36.836  -18.878 44.358  1.00 185.49 ? 888  VAL A O   1 
ATOM   6667  C  CB  . VAL A 1 888  ? 37.256  -20.158 41.802  1.00 188.73 ? 888  VAL A CB  1 
ATOM   6668  C  CG1 . VAL A 1 888  ? 37.836  -20.876 40.606  1.00 194.05 ? 888  VAL A CG1 1 
ATOM   6669  C  CG2 . VAL A 1 888  ? 36.089  -20.931 42.416  1.00 187.21 ? 888  VAL A CG2 1 
ATOM   6670  N  N   . GLU A 1 889  ? 38.669  -17.731 43.733  1.00 185.39 ? 889  GLU A N   1 
ATOM   6671  C  CA  . GLU A 1 889  ? 38.256  -16.528 44.427  1.00 186.02 ? 889  GLU A CA  1 
ATOM   6672  C  C   . GLU A 1 889  ? 36.934  -16.071 43.826  1.00 185.66 ? 889  GLU A C   1 
ATOM   6673  O  O   . GLU A 1 889  ? 36.726  -16.171 42.617  1.00 187.29 ? 889  GLU A O   1 
ATOM   6674  C  CB  . GLU A 1 889  ? 39.329  -15.438 44.333  1.00 195.26 ? 889  GLU A CB  1 
ATOM   6675  C  CG  . GLU A 1 889  ? 39.859  -15.164 42.933  1.00 211.91 ? 889  GLU A CG  1 
ATOM   6676  C  CD  . GLU A 1 889  ? 40.945  -16.130 42.503  1.00 224.38 ? 889  GLU A CD  1 
ATOM   6677  O  OE1 . GLU A 1 889  ? 41.360  -16.985 43.313  1.00 225.67 ? 889  GLU A OE1 1 
ATOM   6678  O  OE2 . GLU A 1 889  ? 41.389  -16.029 41.345  1.00 232.01 ? 889  GLU A OE2 1 
ATOM   6679  N  N   . GLY A 1 890  ? 36.039  -15.586 44.680  1.00 240.88 ? 890  GLY A N   1 
ATOM   6680  C  CA  . GLY A 1 890  ? 34.682  -15.268 44.276  1.00 240.08 ? 890  GLY A CA  1 
ATOM   6681  C  C   . GLY A 1 890  ? 34.583  -14.291 43.127  1.00 235.60 ? 890  GLY A C   1 
ATOM   6682  O  O   . GLY A 1 890  ? 35.360  -13.343 43.031  1.00 233.21 ? 890  GLY A O   1 
ATOM   6683  N  N   . SER A 1 891  ? 33.625  -14.522 42.241  1.00 240.22 ? 891  SER A N   1 
ATOM   6684  C  CA  . SER A 1 891  ? 33.365  -13.549 41.207  1.00 229.77 ? 891  SER A CA  1 
ATOM   6685  C  C   . SER A 1 891  ? 34.623  -13.317 40.380  1.00 226.32 ? 891  SER A C   1 
ATOM   6686  O  O   . SER A 1 891  ? 35.060  -12.178 40.226  1.00 222.37 ? 891  SER A O   1 
ATOM   6687  C  CB  . SER A 1 891  ? 32.949  -12.233 41.862  1.00 221.82 ? 891  SER A CB  1 
ATOM   6688  O  OG  . SER A 1 891  ? 32.417  -12.459 43.156  1.00 224.63 ? 891  SER A OG  1 
ATOM   6689  N  N   . SER A 1 892  ? 35.217  -14.387 39.861  1.00 203.69 ? 892  SER A N   1 
ATOM   6690  C  CA  . SER A 1 892  ? 36.399  -14.246 39.012  1.00 201.07 ? 892  SER A CA  1 
ATOM   6691  C  C   . SER A 1 892  ? 36.629  -15.467 38.135  1.00 204.87 ? 892  SER A C   1 
ATOM   6692  O  O   . SER A 1 892  ? 35.694  -16.007 37.542  1.00 204.50 ? 892  SER A O   1 
ATOM   6693  C  CB  . SER A 1 892  ? 37.655  -13.959 39.849  1.00 201.26 ? 892  SER A CB  1 
ATOM   6694  O  OG  . SER A 1 892  ? 37.621  -12.663 40.432  1.00 196.69 ? 892  SER A OG  1 
ATOM   6695  N  N   . SER A 1 893  ? 37.884  -15.894 38.053  1.00 195.38 ? 893  SER A N   1 
ATOM   6696  C  CA  . SER A 1 893  ? 38.221  -17.063 37.260  1.00 200.13 ? 893  SER A CA  1 
ATOM   6697  C  C   . SER A 1 893  ? 39.631  -17.616 37.528  1.00 204.94 ? 893  SER A C   1 
ATOM   6698  O  O   . SER A 1 893  ? 40.596  -16.871 37.670  1.00 202.86 ? 893  SER A O   1 
ATOM   6699  C  CB  . SER A 1 893  ? 38.034  -16.754 35.774  1.00 196.54 ? 893  SER A CB  1 
ATOM   6700  O  OG  . SER A 1 893  ? 37.943  -17.947 35.020  1.00 199.83 ? 893  SER A OG  1 
ATOM   6701  N  N   . HIS A 1 894  ? 39.729  -18.939 37.611  1.00 163.58 ? 894  HIS A N   1 
ATOM   6702  C  CA  . HIS A 1 894  ? 41.009  -19.626 37.755  1.00 176.56 ? 894  HIS A CA  1 
ATOM   6703  C  C   . HIS A 1 894  ? 41.313  -20.355 36.446  1.00 162.19 ? 894  HIS A C   1 
ATOM   6704  O  O   . HIS A 1 894  ? 40.582  -21.268 36.029  1.00 162.63 ? 894  HIS A O   1 
ATOM   6705  C  CB  . HIS A 1 894  ? 40.968  -20.605 38.933  1.00 215.40 ? 894  HIS A CB  1 
ATOM   6706  C  CG  . HIS A 1 894  ? 42.248  -20.685 39.699  1.00 259.31 ? 894  HIS A CG  1 
ATOM   6707  N  ND1 . HIS A 1 894  ? 42.937  -21.866 39.873  1.00 286.19 ? 894  HIS A ND1 1 
ATOM   6708  C  CD2 . HIS A 1 894  ? 42.966  -19.733 40.335  1.00 276.08 ? 894  HIS A CD2 1 
ATOM   6709  C  CE1 . HIS A 1 894  ? 44.023  -21.635 40.586  1.00 305.07 ? 894  HIS A CE1 1 
ATOM   6710  N  NE2 . HIS A 1 894  ? 44.064  -20.348 40.878  1.00 290.71 ? 894  HIS A NE2 1 
ATOM   6711  N  N   . LEU A 1 895  ? 42.382  -19.921 35.788  1.00 239.99 ? 895  LEU A N   1 
ATOM   6712  C  CA  . LEU A 1 895  ? 42.822  -20.526 34.542  1.00 235.63 ? 895  LEU A CA  1 
ATOM   6713  C  C   . LEU A 1 895  ? 42.914  -22.021 34.723  1.00 232.98 ? 895  LEU A C   1 
ATOM   6714  O  O   . LEU A 1 895  ? 43.031  -22.509 35.840  1.00 236.10 ? 895  LEU A O   1 
ATOM   6715  C  CB  . LEU A 1 895  ? 44.190  -19.983 34.152  1.00 236.32 ? 895  LEU A CB  1 
ATOM   6716  C  CG  . LEU A 1 895  ? 44.208  -19.112 32.906  1.00 234.31 ? 895  LEU A CG  1 
ATOM   6717  C  CD1 . LEU A 1 895  ? 45.139  -17.932 33.096  1.00 230.86 ? 895  LEU A CD1 1 
ATOM   6718  C  CD2 . LEU A 1 895  ? 44.614  -19.951 31.715  1.00 236.95 ? 895  LEU A CD2 1 
ATOM   6719  N  N   . VAL A 1 896  ? 42.859  -22.754 33.627  1.00 187.12 ? 896  VAL A N   1 
ATOM   6720  C  CA  . VAL A 1 896  ? 43.006  -24.192 33.702  1.00 184.93 ? 896  VAL A CA  1 
ATOM   6721  C  C   . VAL A 1 896  ? 43.943  -24.599 32.584  1.00 184.41 ? 896  VAL A C   1 
ATOM   6722  O  O   . VAL A 1 896  ? 44.192  -23.808 31.680  1.00 181.00 ? 896  VAL A O   1 
ATOM   6723  C  CB  . VAL A 1 896  ? 41.644  -24.901 33.546  1.00 182.55 ? 896  VAL A CB  1 
ATOM   6724  C  CG1 . VAL A 1 896  ? 41.763  -26.363 33.936  1.00 189.28 ? 896  VAL A CG1 1 
ATOM   6725  C  CG2 . VAL A 1 896  ? 40.572  -24.206 34.388  1.00 177.09 ? 896  VAL A CG2 1 
ATOM   6726  N  N   . THR A 1 897  ? 44.498  -25.805 32.658  1.00 185.54 ? 897  THR A N   1 
ATOM   6727  C  CA  . THR A 1 897  ? 45.271  -26.343 31.541  1.00 183.79 ? 897  THR A CA  1 
ATOM   6728  C  C   . THR A 1 897  ? 45.364  -27.867 31.580  1.00 191.71 ? 897  THR A C   1 
ATOM   6729  O  O   . THR A 1 897  ? 45.319  -28.482 32.643  1.00 196.36 ? 897  THR A O   1 
ATOM   6730  C  CB  . THR A 1 897  ? 46.718  -25.779 31.454  1.00 178.57 ? 897  THR A CB  1 
ATOM   6731  O  OG1 . THR A 1 897  ? 47.631  -26.702 32.064  1.00 184.18 ? 897  THR A OG1 1 
ATOM   6732  C  CG2 . THR A 1 897  ? 46.843  -24.395 32.105  1.00 172.15 ? 897  THR A CG2 1 
ATOM   6733  N  N   . PHE A 1 898  ? 45.492  -28.455 30.394  1.00 195.38 ? 898  PHE A N   1 
ATOM   6734  C  CA  . PHE A 1 898  ? 45.734  -29.883 30.209  1.00 200.85 ? 898  PHE A CA  1 
ATOM   6735  C  C   . PHE A 1 898  ? 46.574  -30.056 28.956  1.00 200.44 ? 898  PHE A C   1 
ATOM   6736  O  O   . PHE A 1 898  ? 46.252  -29.518 27.893  1.00 195.10 ? 898  PHE A O   1 
ATOM   6737  C  CB  . PHE A 1 898  ? 44.428  -30.648 29.998  1.00 203.94 ? 898  PHE A CB  1 
ATOM   6738  C  CG  . PHE A 1 898  ? 43.557  -30.714 31.206  1.00 203.90 ? 898  PHE A CG  1 
ATOM   6739  C  CD1 . PHE A 1 898  ? 43.319  -31.924 31.832  1.00 208.71 ? 898  PHE A CD1 1 
ATOM   6740  C  CD2 . PHE A 1 898  ? 42.965  -29.569 31.707  1.00 197.99 ? 898  PHE A CD2 1 
ATOM   6741  C  CE1 . PHE A 1 898  ? 42.515  -31.988 32.931  1.00 204.76 ? 898  PHE A CE1 1 
ATOM   6742  C  CE2 . PHE A 1 898  ? 42.169  -29.620 32.811  1.00 199.10 ? 898  PHE A CE2 1 
ATOM   6743  C  CZ  . PHE A 1 898  ? 41.937  -30.831 33.427  1.00 201.77 ? 898  PHE A CZ  1 
ATOM   6744  N  N   . THR A 1 899  ? 47.642  -30.826 29.069  1.00 173.25 ? 899  THR A N   1 
ATOM   6745  C  CA  . THR A 1 899  ? 48.460  -31.104 27.909  1.00 171.64 ? 899  THR A CA  1 
ATOM   6746  C  C   . THR A 1 899  ? 48.143  -32.495 27.353  1.00 174.57 ? 899  THR A C   1 
ATOM   6747  O  O   . THR A 1 899  ? 47.809  -33.409 28.117  1.00 177.86 ? 899  THR A O   1 
ATOM   6748  C  CB  . THR A 1 899  ? 49.946  -30.971 28.246  1.00 174.03 ? 899  THR A CB  1 
ATOM   6749  O  OG1 . THR A 1 899  ? 50.222  -31.685 29.459  1.00 180.11 ? 899  THR A OG1 1 
ATOM   6750  C  CG2 . THR A 1 899  ? 50.301  -29.504 28.433  1.00 163.53 ? 899  THR A CG2 1 
ATOM   6751  N  N   . VAL A 1 900  ? 48.235  -32.625 26.022  1.00 193.90 ? 900  VAL A N   1 
ATOM   6752  C  CA  . VAL A 1 900  ? 47.957  -33.861 25.278  1.00 198.54 ? 900  VAL A CA  1 
ATOM   6753  C  C   . VAL A 1 900  ? 48.768  -33.920 23.984  1.00 196.04 ? 900  VAL A C   1 
ATOM   6754  O  O   . VAL A 1 900  ? 49.480  -32.978 23.630  1.00 191.62 ? 900  VAL A O   1 
ATOM   6755  C  CB  . VAL A 1 900  ? 46.468  -33.986 24.885  1.00 182.36 ? 900  VAL A CB  1 
ATOM   6756  C  CG1 . VAL A 1 900  ? 45.650  -34.574 26.012  1.00 186.87 ? 900  VAL A CG1 1 
ATOM   6757  C  CG2 . VAL A 1 900  ? 45.920  -32.645 24.477  1.00 175.15 ? 900  VAL A CG2 1 
ATOM   6758  N  N   . LEU A 1 901  ? 48.640  -35.039 23.280  1.00 195.50 ? 901  LEU A N   1 
ATOM   6759  C  CA  . LEU A 1 901  ? 49.354  -35.265 22.026  1.00 201.08 ? 901  LEU A CA  1 
ATOM   6760  C  C   . LEU A 1 901  ? 48.782  -36.472 21.276  1.00 212.00 ? 901  LEU A C   1 
ATOM   6761  O  O   . LEU A 1 901  ? 48.991  -37.611 21.687  1.00 220.84 ? 901  LEU A O   1 
ATOM   6762  C  CB  . LEU A 1 901  ? 50.843  -35.457 22.303  1.00 200.67 ? 901  LEU A CB  1 
ATOM   6763  C  CG  . LEU A 1 901  ? 51.676  -36.208 21.270  1.00 204.81 ? 901  LEU A CG  1 
ATOM   6764  C  CD1 . LEU A 1 901  ? 52.997  -35.510 21.068  1.00 200.09 ? 901  LEU A CD1 1 
ATOM   6765  C  CD2 . LEU A 1 901  ? 51.889  -37.642 21.723  1.00 213.09 ? 901  LEU A CD2 1 
ATOM   6766  N  N   . PRO A 1 902  ? 48.044  -36.212 20.180  1.00 188.56 ? 902  PRO A N   1 
ATOM   6767  C  CA  . PRO A 1 902  ? 47.304  -37.175 19.357  1.00 194.52 ? 902  PRO A CA  1 
ATOM   6768  C  C   . PRO A 1 902  ? 48.145  -37.853 18.277  1.00 200.97 ? 902  PRO A C   1 
ATOM   6769  O  O   . PRO A 1 902  ? 49.027  -37.230 17.684  1.00 197.22 ? 902  PRO A O   1 
ATOM   6770  C  CB  . PRO A 1 902  ? 46.229  -36.308 18.686  1.00 191.00 ? 902  PRO A CB  1 
ATOM   6771  C  CG  . PRO A 1 902  ? 46.355  -34.923 19.294  1.00 176.96 ? 902  PRO A CG  1 
ATOM   6772  C  CD  . PRO A 1 902  ? 47.771  -34.836 19.750  1.00 177.49 ? 902  PRO A CD  1 
ATOM   6773  N  N   . LEU A 1 903  ? 47.838  -39.122 18.023  1.00 220.87 ? 903  LEU A N   1 
ATOM   6774  C  CA  . LEU A 1 903  ? 48.527  -39.930 17.025  1.00 227.52 ? 903  LEU A CA  1 
ATOM   6775  C  C   . LEU A 1 903  ? 47.505  -40.398 16.008  1.00 232.13 ? 903  LEU A C   1 
ATOM   6776  O  O   . LEU A 1 903  ? 47.850  -40.856 14.911  1.00 235.68 ? 903  LEU A O   1 
ATOM   6777  C  CB  . LEU A 1 903  ? 49.154  -41.155 17.682  1.00 233.58 ? 903  LEU A CB  1 
ATOM   6778  C  CG  . LEU A 1 903  ? 49.840  -40.902 19.018  1.00 232.00 ? 903  LEU A CG  1 
ATOM   6779  C  CD1 . LEU A 1 903  ? 50.662  -39.642 18.883  1.00 224.33 ? 903  LEU A CD1 1 
ATOM   6780  C  CD2 . LEU A 1 903  ? 48.836  -40.788 20.165  1.00 230.95 ? 903  LEU A CD2 1 
ATOM   6781  N  N   . GLU A 1 904  ? 46.241  -40.303 16.409  1.00 242.64 ? 904  GLU A N   1 
ATOM   6782  C  CA  . GLU A 1 904  ? 45.118  -40.592 15.531  1.00 249.54 ? 904  GLU A CA  1 
ATOM   6783  C  C   . GLU A 1 904  ? 44.598  -39.311 14.872  1.00 240.11 ? 904  GLU A C   1 
ATOM   6784  O  O   . GLU A 1 904  ? 43.979  -38.460 15.525  1.00 233.31 ? 904  GLU A O   1 
ATOM   6785  C  CB  . GLU A 1 904  ? 44.013  -41.331 16.293  1.00 260.08 ? 904  GLU A CB  1 
ATOM   6786  C  CG  . GLU A 1 904  ? 44.494  -42.647 16.905  1.00 273.14 ? 904  GLU A CG  1 
ATOM   6787  C  CD  . GLU A 1 904  ? 43.405  -43.703 17.022  1.00 286.60 ? 904  GLU A CD  1 
ATOM   6788  O  OE1 . GLU A 1 904  ? 42.227  -43.407 16.716  1.00 287.65 ? 904  GLU A OE1 1 
ATOM   6789  O  OE2 . GLU A 1 904  ? 43.738  -44.839 17.422  1.00 295.06 ? 904  GLU A OE2 1 
ATOM   6790  N  N   . ILE A 1 905  ? 44.867  -39.207 13.567  1.00 217.06 ? 905  ILE A N   1 
ATOM   6791  C  CA  . ILE A 1 905  ? 44.581  -38.021 12.752  1.00 202.88 ? 905  ILE A CA  1 
ATOM   6792  C  C   . ILE A 1 905  ? 43.094  -37.903 12.489  1.00 197.44 ? 905  ILE A C   1 
ATOM   6793  O  O   . ILE A 1 905  ? 42.451  -38.866 12.079  1.00 195.17 ? 905  ILE A O   1 
ATOM   6794  C  CB  . ILE A 1 905  ? 45.344  -38.049 11.392  1.00 188.43 ? 905  ILE A CB  1 
ATOM   6795  C  CG1 . ILE A 1 905  ? 46.810  -38.440 11.609  1.00 195.97 ? 905  ILE A CG1 1 
ATOM   6796  C  CG2 . ILE A 1 905  ? 45.246  -36.707 10.689  1.00 185.12 ? 905  ILE A CG2 1 
ATOM   6797  C  CD1 . ILE A 1 905  ? 47.749  -37.975 10.517  1.00 191.07 ? 905  ILE A CD1 1 
ATOM   6798  N  N   . GLY A 1 906  ? 42.552  -36.716 12.726  1.00 231.66 ? 906  GLY A N   1 
ATOM   6799  C  CA  . GLY A 1 906  ? 41.119  -36.527 12.666  1.00 237.68 ? 906  GLY A CA  1 
ATOM   6800  C  C   . GLY A 1 906  ? 40.434  -36.822 13.991  1.00 242.31 ? 906  GLY A C   1 
ATOM   6801  O  O   . GLY A 1 906  ? 39.357  -36.293 14.234  1.00 238.69 ? 906  GLY A O   1 
ATOM   6802  N  N   . LEU A 1 907  ? 41.055  -37.634 14.856  1.00 213.79 ? 907  LEU A N   1 
ATOM   6803  C  CA  . LEU A 1 907  ? 40.407  -38.060 16.113  1.00 219.31 ? 907  LEU A CA  1 
ATOM   6804  C  C   . LEU A 1 907  ? 39.940  -36.895 16.971  1.00 215.04 ? 907  LEU A C   1 
ATOM   6805  O  O   . LEU A 1 907  ? 40.707  -35.992 17.289  1.00 208.66 ? 907  LEU A O   1 
ATOM   6806  C  CB  . LEU A 1 907  ? 41.279  -39.003 16.954  1.00 226.15 ? 907  LEU A CB  1 
ATOM   6807  C  CG  . LEU A 1 907  ? 40.622  -39.431 18.280  1.00 234.45 ? 907  LEU A CG  1 
ATOM   6808  C  CD1 . LEU A 1 907  ? 39.211  -39.969 18.083  1.00 240.27 ? 907  LEU A CD1 1 
ATOM   6809  C  CD2 . LEU A 1 907  ? 41.468  -40.453 19.014  1.00 243.32 ? 907  LEU A CD2 1 
ATOM   6810  N  N   . HIS A 1 908  ? 38.673  -36.960 17.364  1.00 242.57 ? 908  HIS A N   1 
ATOM   6811  C  CA  . HIS A 1 908  ? 37.981  -35.848 17.989  1.00 240.02 ? 908  HIS A CA  1 
ATOM   6812  C  C   . HIS A 1 908  ? 37.512  -36.210 19.392  1.00 242.33 ? 908  HIS A C   1 
ATOM   6813  O  O   . HIS A 1 908  ? 38.033  -37.137 20.009  1.00 249.27 ? 908  HIS A O   1 
ATOM   6814  C  CB  . HIS A 1 908  ? 36.745  -35.475 17.163  1.00 240.56 ? 908  HIS A CB  1 
ATOM   6815  C  CG  . HIS A 1 908  ? 36.863  -35.763 15.691  1.00 238.84 ? 908  HIS A CG  1 
ATOM   6816  N  ND1 . HIS A 1 908  ? 36.909  -37.040 15.177  1.00 243.26 ? 908  HIS A ND1 1 
ATOM   6817  C  CD2 . HIS A 1 908  ? 36.884  -34.927 14.624  1.00 232.16 ? 908  HIS A CD2 1 
ATOM   6818  C  CE1 . HIS A 1 908  ? 36.982  -36.980 13.858  1.00 242.19 ? 908  HIS A CE1 1 
ATOM   6819  N  NE2 . HIS A 1 908  ? 36.971  -35.710 13.499  1.00 235.25 ? 908  HIS A NE2 1 
ATOM   6820  N  N   . ASN A 1 909  ? 36.510  -35.469 19.866  1.00 228.03 ? 909  ASN A N   1 
ATOM   6821  C  CA  . ASN A 1 909  ? 35.832  -35.720 21.142  1.00 228.87 ? 909  ASN A CA  1 
ATOM   6822  C  C   . ASN A 1 909  ? 36.713  -35.695 22.379  1.00 223.63 ? 909  ASN A C   1 
ATOM   6823  O  O   . ASN A 1 909  ? 37.626  -36.506 22.527  1.00 225.32 ? 909  ASN A O   1 
ATOM   6824  C  CB  . ASN A 1 909  ? 35.039  -37.034 21.124  1.00 241.96 ? 909  ASN A CB  1 
ATOM   6825  C  CG  . ASN A 1 909  ? 34.524  -37.429 22.514  1.00 249.85 ? 909  ASN A CG  1 
ATOM   6826  O  OD1 . ASN A 1 909  ? 34.508  -38.606 22.882  1.00 258.34 ? 909  ASN A OD1 1 
ATOM   6827  N  ND2 . ASN A 1 909  ? 34.108  -36.440 23.288  1.00 246.40 ? 909  ASN A ND2 1 
ATOM   6828  N  N   . ILE A 1 910  ? 36.402  -34.773 23.281  1.00 205.98 ? 910  ILE A N   1 
ATOM   6829  C  CA  . ILE A 1 910  ? 36.985  -34.758 24.610  1.00 199.75 ? 910  ILE A CA  1 
ATOM   6830  C  C   . ILE A 1 910  ? 35.940  -34.186 25.545  1.00 199.08 ? 910  ILE A C   1 
ATOM   6831  O  O   . ILE A 1 910  ? 35.543  -33.033 25.415  1.00 198.06 ? 910  ILE A O   1 
ATOM   6832  C  CB  . ILE A 1 910  ? 38.267  -33.920 24.672  1.00 186.48 ? 910  ILE A CB  1 
ATOM   6833  C  CG1 . ILE A 1 910  ? 39.426  -34.696 24.057  1.00 185.03 ? 910  ILE A CG1 1 
ATOM   6834  C  CG2 . ILE A 1 910  ? 38.618  -33.586 26.097  1.00 183.05 ? 910  ILE A CG2 1 
ATOM   6835  C  CD1 . ILE A 1 910  ? 40.722  -33.951 24.091  1.00 177.90 ? 910  ILE A CD1 1 
ATOM   6836  N  N   . ASN A 1 911  ? 35.470  -35.015 26.467  1.00 229.73 ? 911  ASN A N   1 
ATOM   6837  C  CA  . ASN A 1 911  ? 34.495  -34.578 27.456  1.00 224.08 ? 911  ASN A CA  1 
ATOM   6838  C  C   . ASN A 1 911  ? 35.189  -33.984 28.696  1.00 221.86 ? 911  ASN A C   1 
ATOM   6839  O  O   . ASN A 1 911  ? 35.993  -34.656 29.353  1.00 223.88 ? 911  ASN A O   1 
ATOM   6840  C  CB  . ASN A 1 911  ? 33.569  -35.742 27.851  1.00 228.29 ? 911  ASN A CB  1 
ATOM   6841  C  CG  . ASN A 1 911  ? 32.816  -36.350 26.656  1.00 227.90 ? 911  ASN A CG  1 
ATOM   6842  O  OD1 . ASN A 1 911  ? 33.418  -36.922 25.743  1.00 231.54 ? 911  ASN A OD1 1 
ATOM   6843  N  ND2 . ASN A 1 911  ? 31.488  -36.247 26.682  1.00 228.04 ? 911  ASN A ND2 1 
ATOM   6844  N  N   . PHE A 1 912  ? 34.889  -32.723 29.006  1.00 214.15 ? 912  PHE A N   1 
ATOM   6845  C  CA  . PHE A 1 912  ? 35.431  -32.071 30.200  1.00 210.03 ? 912  PHE A CA  1 
ATOM   6846  C  C   . PHE A 1 912  ? 34.374  -31.963 31.308  1.00 214.41 ? 912  PHE A C   1 
ATOM   6847  O  O   . PHE A 1 912  ? 33.179  -31.860 31.026  1.00 215.98 ? 912  PHE A O   1 
ATOM   6848  C  CB  . PHE A 1 912  ? 36.001  -30.687 29.860  1.00 197.72 ? 912  PHE A CB  1 
ATOM   6849  C  CG  . PHE A 1 912  ? 37.307  -30.731 29.115  1.00 191.17 ? 912  PHE A CG  1 
ATOM   6850  C  CD1 . PHE A 1 912  ? 38.483  -31.041 29.768  1.00 190.52 ? 912  PHE A CD1 1 
ATOM   6851  C  CD2 . PHE A 1 912  ? 37.358  -30.447 27.765  1.00 186.99 ? 912  PHE A CD2 1 
ATOM   6852  C  CE1 . PHE A 1 912  ? 39.678  -31.074 29.087  1.00 187.47 ? 912  PHE A CE1 1 
ATOM   6853  C  CE2 . PHE A 1 912  ? 38.558  -30.481 27.082  1.00 183.98 ? 912  PHE A CE2 1 
ATOM   6854  C  CZ  . PHE A 1 912  ? 39.715  -30.795 27.744  1.00 183.77 ? 912  PHE A CZ  1 
ATOM   6855  N  N   . SER A 1 913  ? 34.829  -31.972 32.563  1.00 217.94 ? 913  SER A N   1 
ATOM   6856  C  CA  . SER A 1 913  ? 33.941  -31.987 33.732  1.00 220.12 ? 913  SER A CA  1 
ATOM   6857  C  C   . SER A 1 913  ? 34.549  -31.276 34.949  1.00 217.27 ? 913  SER A C   1 
ATOM   6858  O  O   . SER A 1 913  ? 35.733  -31.450 35.247  1.00 213.50 ? 913  SER A O   1 
ATOM   6859  C  CB  . SER A 1 913  ? 33.593  -33.429 34.110  1.00 221.04 ? 913  SER A CB  1 
ATOM   6860  O  OG  . SER A 1 913  ? 32.837  -33.488 35.307  1.00 216.32 ? 913  SER A OG  1 
ATOM   6861  N  N   . LEU A 1 914  ? 33.731  -30.482 35.645  1.00 211.98 ? 914  LEU A N   1 
ATOM   6862  C  CA  . LEU A 1 914  ? 34.150  -29.805 36.874  1.00 208.41 ? 914  LEU A CA  1 
ATOM   6863  C  C   . LEU A 1 914  ? 33.225  -30.161 38.028  1.00 214.27 ? 914  LEU A C   1 
ATOM   6864  O  O   . LEU A 1 914  ? 32.075  -30.539 37.817  1.00 219.69 ? 914  LEU A O   1 
ATOM   6865  C  CB  . LEU A 1 914  ? 34.215  -28.281 36.687  1.00 198.64 ? 914  LEU A CB  1 
ATOM   6866  C  CG  . LEU A 1 914  ? 33.013  -27.512 36.124  1.00 194.39 ? 914  LEU A CG  1 
ATOM   6867  C  CD1 . LEU A 1 914  ? 31.803  -27.564 37.052  1.00 190.68 ? 914  LEU A CD1 1 
ATOM   6868  C  CD2 . LEU A 1 914  ? 33.400  -26.068 35.823  1.00 185.56 ? 914  LEU A CD2 1 
ATOM   6869  N  N   . GLU A 1 915  ? 33.728  -30.047 39.248  1.00 268.92 ? 915  GLU A N   1 
ATOM   6870  C  CA  . GLU A 1 915  ? 32.929  -30.421 40.401  1.00 273.50 ? 915  GLU A CA  1 
ATOM   6871  C  C   . GLU A 1 915  ? 32.882  -29.319 41.439  1.00 270.70 ? 915  GLU A C   1 
ATOM   6872  O  O   . GLU A 1 915  ? 33.883  -28.666 41.718  1.00 264.79 ? 915  GLU A O   1 
ATOM   6873  C  CB  . GLU A 1 915  ? 33.429  -31.730 41.022  1.00 275.54 ? 915  GLU A CB  1 
ATOM   6874  C  CG  . GLU A 1 915  ? 32.874  -32.979 40.344  1.00 286.02 ? 915  GLU A CG  1 
ATOM   6875  C  CD  . GLU A 1 915  ? 33.915  -33.729 39.532  1.00 293.48 ? 915  GLU A CD  1 
ATOM   6876  O  OE1 . GLU A 1 915  ? 35.087  -33.778 39.964  1.00 290.67 ? 915  GLU A OE1 1 
ATOM   6877  O  OE2 . GLU A 1 915  ? 33.561  -34.276 38.466  1.00 302.03 ? 915  GLU A OE2 1 
ATOM   6878  N  N   . THR A 1 916  ? 31.698  -29.123 42.002  1.00 252.22 ? 916  THR A N   1 
ATOM   6879  C  CA  . THR A 1 916  ? 31.488  -28.127 43.035  1.00 253.01 ? 916  THR A CA  1 
ATOM   6880  C  C   . THR A 1 916  ? 30.490  -28.670 44.035  1.00 261.02 ? 916  THR A C   1 
ATOM   6881  O  O   . THR A 1 916  ? 29.688  -29.547 43.712  1.00 266.29 ? 916  THR A O   1 
ATOM   6882  C  CB  . THR A 1 916  ? 30.945  -26.819 42.450  1.00 251.02 ? 916  THR A CB  1 
ATOM   6883  O  OG1 . THR A 1 916  ? 31.897  -26.283 41.525  1.00 250.99 ? 916  THR A OG1 1 
ATOM   6884  C  CG2 . THR A 1 916  ? 30.696  -25.803 43.555  1.00 243.32 ? 916  THR A CG2 1 
ATOM   6885  N  N   . TRP A 1 917  ? 30.549  -28.144 45.250  1.00 323.80 ? 917  TRP A N   1 
ATOM   6886  C  CA  . TRP A 1 917  ? 29.682  -28.591 46.323  1.00 329.78 ? 917  TRP A CA  1 
ATOM   6887  C  C   . TRP A 1 917  ? 28.286  -28.901 45.813  1.00 338.95 ? 917  TRP A C   1 
ATOM   6888  O  O   . TRP A 1 917  ? 27.767  -29.995 46.029  1.00 340.28 ? 917  TRP A O   1 
ATOM   6889  C  CB  . TRP A 1 917  ? 29.599  -27.521 47.404  1.00 327.58 ? 917  TRP A CB  1 
ATOM   6890  C  CG  . TRP A 1 917  ? 29.445  -28.091 48.763  1.00 328.68 ? 917  TRP A CG  1 
ATOM   6891  C  CD1 . TRP A 1 917  ? 28.316  -28.100 49.528  1.00 328.29 ? 917  TRP A CD1 1 
ATOM   6892  C  CD2 . TRP A 1 917  ? 30.455  -28.754 49.527  1.00 328.38 ? 917  TRP A CD2 1 
ATOM   6893  N  NE1 . TRP A 1 917  ? 28.564  -28.722 50.728  1.00 326.23 ? 917  TRP A NE1 1 
ATOM   6894  C  CE2 . TRP A 1 917  ? 29.872  -29.134 50.752  1.00 326.13 ? 917  TRP A CE2 1 
ATOM   6895  C  CE3 . TRP A 1 917  ? 31.799  -29.062 49.294  1.00 330.01 ? 917  TRP A CE3 1 
ATOM   6896  C  CZ2 . TRP A 1 917  ? 30.585  -29.806 51.742  1.00 323.78 ? 917  TRP A CZ2 1 
ATOM   6897  C  CZ3 . TRP A 1 917  ? 32.505  -29.728 50.278  1.00 327.38 ? 917  TRP A CZ3 1 
ATOM   6898  C  CH2 . TRP A 1 917  ? 31.897  -30.092 51.487  1.00 324.48 ? 917  TRP A CH2 1 
ATOM   6899  N  N   . PHE A 1 918  ? 27.681  -27.936 45.129  1.00 245.57 ? 918  PHE A N   1 
ATOM   6900  C  CA  . PHE A 1 918  ? 26.317  -28.110 44.646  1.00 253.79 ? 918  PHE A CA  1 
ATOM   6901  C  C   . PHE A 1 918  ? 26.196  -28.382 43.146  1.00 254.83 ? 918  PHE A C   1 
ATOM   6902  O  O   . PHE A 1 918  ? 25.130  -28.197 42.563  1.00 259.34 ? 918  PHE A O   1 
ATOM   6903  C  CB  . PHE A 1 918  ? 25.404  -26.950 45.089  1.00 257.99 ? 918  PHE A CB  1 
ATOM   6904  C  CG  . PHE A 1 918  ? 25.858  -25.580 44.642  1.00 260.89 ? 918  PHE A CG  1 
ATOM   6905  C  CD1 . PHE A 1 918  ? 25.406  -25.042 43.448  1.00 268.27 ? 918  PHE A CD1 1 
ATOM   6906  C  CD2 . PHE A 1 918  ? 26.689  -24.809 45.445  1.00 256.12 ? 918  PHE A CD2 1 
ATOM   6907  C  CE1 . PHE A 1 918  ? 25.798  -23.774 43.045  1.00 267.60 ? 918  PHE A CE1 1 
ATOM   6908  C  CE2 . PHE A 1 918  ? 27.086  -23.538 45.048  1.00 255.35 ? 918  PHE A CE2 1 
ATOM   6909  C  CZ  . PHE A 1 918  ? 26.639  -23.021 43.847  1.00 261.02 ? 918  PHE A CZ  1 
ATOM   6910  N  N   . GLY A 1 919  ? 27.271  -28.851 42.525  1.00 282.58 ? 919  GLY A N   1 
ATOM   6911  C  CA  . GLY A 1 919  ? 27.223  -29.108 41.099  1.00 282.45 ? 919  GLY A CA  1 
ATOM   6912  C  C   . GLY A 1 919  ? 28.330  -29.958 40.510  1.00 279.41 ? 919  GLY A C   1 
ATOM   6913  O  O   . GLY A 1 919  ? 29.408  -30.108 41.087  1.00 274.21 ? 919  GLY A O   1 
ATOM   6914  N  N   . LYS A 1 920  ? 28.042  -30.513 39.337  1.00 288.00 ? 920  LYS A N   1 
ATOM   6915  C  CA  . LYS A 1 920  ? 29.002  -31.286 38.559  1.00 285.47 ? 920  LYS A CA  1 
ATOM   6916  C  C   . LYS A 1 920  ? 28.552  -31.246 37.096  1.00 286.91 ? 920  LYS A C   1 
ATOM   6917  O  O   . LYS A 1 920  ? 27.456  -31.705 36.762  1.00 293.42 ? 920  LYS A O   1 
ATOM   6918  C  CB  . LYS A 1 920  ? 29.082  -32.724 39.081  1.00 284.97 ? 920  LYS A CB  1 
ATOM   6919  C  CG  . LYS A 1 920  ? 30.131  -33.595 38.403  1.00 286.71 ? 920  LYS A CG  1 
ATOM   6920  C  CD  . LYS A 1 920  ? 30.346  -34.889 39.179  1.00 284.09 ? 920  LYS A CD  1 
ATOM   6921  C  CE  . LYS A 1 920  ? 31.279  -35.835 38.446  1.00 286.42 ? 920  LYS A CE  1 
ATOM   6922  N  NZ  . LYS A 1 920  ? 31.757  -36.929 39.331  1.00 283.94 ? 920  LYS A NZ  1 
ATOM   6923  N  N   . GLU A 1 921  ? 29.402  -30.689 36.233  1.00 278.85 ? 921  GLU A N   1 
ATOM   6924  C  CA  . GLU A 1 921  ? 29.023  -30.340 34.857  1.00 276.85 ? 921  GLU A CA  1 
ATOM   6925  C  C   . GLU A 1 921  ? 29.973  -30.967 33.823  1.00 270.09 ? 921  GLU A C   1 
ATOM   6926  O  O   . GLU A 1 921  ? 31.152  -31.180 34.109  1.00 268.91 ? 921  GLU A O   1 
ATOM   6927  C  CB  . GLU A 1 921  ? 29.012  -28.809 34.708  1.00 271.86 ? 921  GLU A CB  1 
ATOM   6928  C  CG  . GLU A 1 921  ? 28.133  -28.261 33.592  1.00 272.60 ? 921  GLU A CG  1 
ATOM   6929  C  CD  . GLU A 1 921  ? 26.813  -27.704 34.099  1.00 275.45 ? 921  GLU A CD  1 
ATOM   6930  O  OE1 . GLU A 1 921  ? 26.374  -28.090 35.202  1.00 281.12 ? 921  GLU A OE1 1 
ATOM   6931  O  OE2 . GLU A 1 921  ? 26.211  -26.881 33.384  1.00 272.06 ? 921  GLU A OE2 1 
ATOM   6932  N  N   . ILE A 1 922  ? 29.464  -31.256 32.626  1.00 245.65 ? 922  ILE A N   1 
ATOM   6933  C  CA  . ILE A 1 922  ? 30.282  -31.874 31.581  1.00 238.64 ? 922  ILE A CA  1 
ATOM   6934  C  C   . ILE A 1 922  ? 30.186  -31.181 30.230  1.00 227.05 ? 922  ILE A C   1 
ATOM   6935  O  O   . ILE A 1 922  ? 29.206  -31.341 29.500  1.00 226.68 ? 922  ILE A O   1 
ATOM   6936  C  CB  . ILE A 1 922  ? 29.963  -33.372 31.394  1.00 244.19 ? 922  ILE A CB  1 
ATOM   6937  C  CG1 . ILE A 1 922  ? 30.700  -34.191 32.451  1.00 247.16 ? 922  ILE A CG1 1 
ATOM   6938  C  CG2 . ILE A 1 922  ? 30.390  -33.838 30.015  1.00 245.79 ? 922  ILE A CG2 1 
ATOM   6939  C  CD1 . ILE A 1 922  ? 30.815  -35.663 32.134  1.00 253.23 ? 922  ILE A CD1 1 
ATOM   6940  N  N   . LEU A 1 923  ? 31.221  -30.417 29.903  1.00 211.72 ? 923  LEU A N   1 
ATOM   6941  C  CA  . LEU A 1 923  ? 31.303  -29.746 28.613  1.00 205.76 ? 923  LEU A CA  1 
ATOM   6942  C  C   . LEU A 1 923  ? 32.095  -30.585 27.620  1.00 208.62 ? 923  LEU A C   1 
ATOM   6943  O  O   . LEU A 1 923  ? 33.285  -30.833 27.823  1.00 211.10 ? 923  LEU A O   1 
ATOM   6944  C  CB  . LEU A 1 923  ? 31.942  -28.365 28.779  1.00 196.46 ? 923  LEU A CB  1 
ATOM   6945  C  CG  . LEU A 1 923  ? 32.768  -27.791 27.627  1.00 191.44 ? 923  LEU A CG  1 
ATOM   6946  C  CD1 . LEU A 1 923  ? 31.927  -27.633 26.388  1.00 191.24 ? 923  LEU A CD1 1 
ATOM   6947  C  CD2 . LEU A 1 923  ? 33.352  -26.458 28.033  1.00 183.91 ? 923  LEU A CD2 1 
ATOM   6948  N  N   . VAL A 1 924  ? 31.433  -31.019 26.547  1.00 188.83 ? 924  VAL A N   1 
ATOM   6949  C  CA  . VAL A 1 924  ? 32.104  -31.819 25.525  1.00 189.26 ? 924  VAL A CA  1 
ATOM   6950  C  C   . VAL A 1 924  ? 32.699  -31.009 24.369  1.00 178.56 ? 924  VAL A C   1 
ATOM   6951  O  O   . VAL A 1 924  ? 32.087  -30.078 23.846  1.00 171.33 ? 924  VAL A O   1 
ATOM   6952  C  CB  . VAL A 1 924  ? 31.215  -32.946 24.971  1.00 195.44 ? 924  VAL A CB  1 
ATOM   6953  C  CG1 . VAL A 1 924  ? 32.084  -34.134 24.630  1.00 201.33 ? 924  VAL A CG1 1 
ATOM   6954  C  CG2 . VAL A 1 924  ? 30.151  -33.345 25.981  1.00 199.75 ? 924  VAL A CG2 1 
ATOM   6955  N  N   . LYS A 1 925  ? 33.903  -31.405 23.974  1.00 189.52 ? 925  LYS A N   1 
ATOM   6956  C  CA  . LYS A 1 925  ? 34.679  -30.682 22.983  1.00 180.89 ? 925  LYS A CA  1 
ATOM   6957  C  C   . LYS A 1 925  ? 35.256  -31.618 21.922  1.00 182.98 ? 925  LYS A C   1 
ATOM   6958  O  O   . LYS A 1 925  ? 35.184  -32.841 22.053  1.00 194.02 ? 925  LYS A O   1 
ATOM   6959  C  CB  . LYS A 1 925  ? 35.818  -29.947 23.667  1.00 173.68 ? 925  LYS A CB  1 
ATOM   6960  C  CG  . LYS A 1 925  ? 35.964  -28.535 23.217  1.00 163.84 ? 925  LYS A CG  1 
ATOM   6961  C  CD  . LYS A 1 925  ? 34.809  -27.717 23.686  1.00 160.41 ? 925  LYS A CD  1 
ATOM   6962  C  CE  . LYS A 1 925  ? 35.141  -26.250 23.558  1.00 153.56 ? 925  LYS A CE  1 
ATOM   6963  N  NZ  . LYS A 1 925  ? 34.025  -25.394 24.036  1.00 150.65 ? 925  LYS A NZ  1 
ATOM   6964  N  N   . THR A 1 926  ? 35.856  -31.036 20.885  1.00 187.76 ? 926  THR A N   1 
ATOM   6965  C  CA  . THR A 1 926  ? 36.290  -31.806 19.721  1.00 185.45 ? 926  THR A CA  1 
ATOM   6966  C  C   . THR A 1 926  ? 37.539  -31.253 19.022  1.00 179.43 ? 926  THR A C   1 
ATOM   6967  O  O   . THR A 1 926  ? 37.598  -30.080 18.639  1.00 173.23 ? 926  THR A O   1 
ATOM   6968  C  CB  . THR A 1 926  ? 35.139  -31.912 18.727  1.00 214.85 ? 926  THR A CB  1 
ATOM   6969  O  OG1 . THR A 1 926  ? 34.306  -30.749 18.857  1.00 209.70 ? 926  THR A OG1 1 
ATOM   6970  C  CG2 . THR A 1 926  ? 34.309  -33.153 19.034  1.00 219.26 ? 926  THR A CG2 1 
ATOM   6971  N  N   . LEU A 1 927  ? 38.522  -32.129 18.844  1.00 161.75 ? 927  LEU A N   1 
ATOM   6972  C  CA  . LEU A 1 927  ? 39.861  -31.733 18.428  1.00 162.40 ? 927  LEU A CA  1 
ATOM   6973  C  C   . LEU A 1 927  ? 40.160  -32.129 16.988  1.00 165.31 ? 927  LEU A C   1 
ATOM   6974  O  O   . LEU A 1 927  ? 40.115  -33.309 16.650  1.00 167.64 ? 927  LEU A O   1 
ATOM   6975  C  CB  . LEU A 1 927  ? 40.877  -32.409 19.352  1.00 162.66 ? 927  LEU A CB  1 
ATOM   6976  C  CG  . LEU A 1 927  ? 42.392  -32.143 19.324  1.00 163.84 ? 927  LEU A CG  1 
ATOM   6977  C  CD1 . LEU A 1 927  ? 43.106  -33.245 20.091  1.00 167.78 ? 927  LEU A CD1 1 
ATOM   6978  C  CD2 . LEU A 1 927  ? 42.956  -32.058 17.925  1.00 165.31 ? 927  LEU A CD2 1 
ATOM   6979  N  N   . ARG A 1 928  ? 40.497  -31.150 16.150  1.00 223.01 ? 928  ARG A N   1 
ATOM   6980  C  CA  . ARG A 1 928  ? 40.848  -31.417 14.752  1.00 224.23 ? 928  ARG A CA  1 
ATOM   6981  C  C   . ARG A 1 928  ? 42.327  -31.826 14.602  1.00 226.89 ? 928  ARG A C   1 
ATOM   6982  O  O   . ARG A 1 928  ? 43.223  -31.042 14.902  1.00 223.15 ? 928  ARG A O   1 
ATOM   6983  C  CB  . ARG A 1 928  ? 40.482  -30.207 13.857  1.00 219.36 ? 928  ARG A CB  1 
ATOM   6984  C  CG  . ARG A 1 928  ? 38.972  -30.113 13.452  1.00 224.19 ? 928  ARG A CG  1 
ATOM   6985  C  CD  . ARG A 1 928  ? 38.420  -28.660 13.394  1.00 224.40 ? 928  ARG A CD  1 
ATOM   6986  N  NE  . ARG A 1 928  ? 38.394  -28.000 14.711  1.00 228.99 ? 928  ARG A NE  1 
ATOM   6987  C  CZ  . ARG A 1 928  ? 37.289  -27.665 15.383  1.00 231.34 ? 928  ARG A CZ  1 
ATOM   6988  N  NH1 . ARG A 1 928  ? 36.091  -27.912 14.868  1.00 234.72 ? 928  ARG A NH1 1 
ATOM   6989  N  NH2 . ARG A 1 928  ? 37.379  -27.075 16.573  1.00 226.21 ? 928  ARG A NH2 1 
ATOM   6990  N  N   . VAL A 1 929  ? 42.575  -33.054 14.146  1.00 172.40 ? 929  VAL A N   1 
ATOM   6991  C  CA  . VAL A 1 929  ? 43.947  -33.566 14.018  1.00 174.06 ? 929  VAL A CA  1 
ATOM   6992  C  C   . VAL A 1 929  ? 44.395  -33.735 12.542  1.00 176.99 ? 929  VAL A C   1 
ATOM   6993  O  O   . VAL A 1 929  ? 43.695  -34.358 11.748  1.00 178.96 ? 929  VAL A O   1 
ATOM   6994  C  CB  . VAL A 1 929  ? 44.125  -34.882 14.840  1.00 176.83 ? 929  VAL A CB  1 
ATOM   6995  C  CG1 . VAL A 1 929  ? 45.590  -35.260 14.987  1.00 177.90 ? 929  VAL A CG1 1 
ATOM   6996  C  CG2 . VAL A 1 929  ? 43.506  -34.722 16.216  1.00 174.72 ? 929  VAL A CG2 1 
ATOM   6997  N  N   . VAL A 1 930  ? 45.569  -33.190 12.200  1.00 190.13 ? 930  VAL A N   1 
ATOM   6998  C  CA  . VAL A 1 930  ? 46.051  -33.056 10.813  1.00 192.85 ? 930  VAL A CA  1 
ATOM   6999  C  C   . VAL A 1 930  ? 47.429  -33.675 10.625  1.00 200.47 ? 930  VAL A C   1 
ATOM   7000  O  O   . VAL A 1 930  ? 48.060  -34.040 11.597  1.00 205.25 ? 930  VAL A O   1 
ATOM   7001  C  CB  . VAL A 1 930  ? 46.240  -31.573 10.467  1.00 187.56 ? 930  VAL A CB  1 
ATOM   7002  C  CG1 . VAL A 1 930  ? 46.250  -31.344 8.945   1.00 187.40 ? 930  VAL A CG1 1 
ATOM   7003  C  CG2 . VAL A 1 930  ? 45.178  -30.732 11.150  1.00 184.31 ? 930  VAL A CG2 1 
ATOM   7004  N  N   . PRO A 1 931  ? 47.887  -33.831 9.368   1.00 178.15 ? 931  PRO A N   1 
ATOM   7005  C  CA  . PRO A 1 931  ? 49.288  -34.084 9.016   1.00 181.53 ? 931  PRO A CA  1 
ATOM   7006  C  C   . PRO A 1 931  ? 49.891  -32.934 8.216   1.00 176.13 ? 931  PRO A C   1 
ATOM   7007  O  O   . PRO A 1 931  ? 49.378  -31.820 8.289   1.00 176.79 ? 931  PRO A O   1 
ATOM   7008  C  CB  . PRO A 1 931  ? 49.217  -35.335 8.132   1.00 178.66 ? 931  PRO A CB  1 
ATOM   7009  C  CG  . PRO A 1 931  ? 47.759  -35.702 8.060   1.00 174.74 ? 931  PRO A CG  1 
ATOM   7010  C  CD  . PRO A 1 931  ? 47.015  -34.441 8.371   1.00 172.91 ? 931  PRO A CD  1 
ATOM   7011  N  N   . GLU A 1 932  ? 50.924  -33.218 7.424   1.00 187.31 ? 932  GLU A N   1 
ATOM   7012  C  CA  . GLU A 1 932  ? 51.902  -32.212 7.010   1.00 188.21 ? 932  GLU A CA  1 
ATOM   7013  C  C   . GLU A 1 932  ? 52.250  -32.196 5.504   1.00 181.14 ? 932  GLU A C   1 
ATOM   7014  O  O   . GLU A 1 932  ? 53.021  -33.039 5.059   1.00 177.74 ? 932  GLU A O   1 
ATOM   7015  C  CB  . GLU A 1 932  ? 53.195  -32.506 7.784   1.00 194.95 ? 932  GLU A CB  1 
ATOM   7016  C  CG  . GLU A 1 932  ? 52.994  -33.168 9.171   1.00 200.43 ? 932  GLU A CG  1 
ATOM   7017  C  CD  . GLU A 1 932  ? 52.634  -34.654 9.121   1.00 200.42 ? 932  GLU A CD  1 
ATOM   7018  O  OE1 . GLU A 1 932  ? 52.096  -35.108 8.104   1.00 196.44 ? 932  GLU A OE1 1 
ATOM   7019  O  OE2 . GLU A 1 932  ? 52.874  -35.374 10.111  1.00 204.53 ? 932  GLU A OE2 1 
ATOM   7020  N  N   . GLY A 1 933  ? 51.736  -31.236 4.727   1.00 186.64 ? 933  GLY A N   1 
ATOM   7021  C  CA  . GLY A 1 933  ? 51.991  -31.184 3.279   1.00 184.50 ? 933  GLY A CA  1 
ATOM   7022  C  C   . GLY A 1 933  ? 50.878  -31.661 2.332   1.00 178.95 ? 933  GLY A C   1 
ATOM   7023  O  O   . GLY A 1 933  ? 51.096  -32.546 1.501   1.00 175.28 ? 933  GLY A O   1 
ATOM   7024  N  N   . VAL A 1 934  ? 49.689  -31.064 2.457   1.00 203.64 ? 934  VAL A N   1 
ATOM   7025  C  CA  . VAL A 1 934  ? 48.493  -31.452 1.693   1.00 205.71 ? 934  VAL A CA  1 
ATOM   7026  C  C   . VAL A 1 934  ? 48.552  -31.069 0.225   1.00 199.90 ? 934  VAL A C   1 
ATOM   7027  O  O   . VAL A 1 934  ? 48.684  -29.890 -0.103  1.00 196.92 ? 934  VAL A O   1 
ATOM   7028  C  CB  . VAL A 1 934  ? 47.207  -30.787 2.270   1.00 212.13 ? 934  VAL A CB  1 
ATOM   7029  C  CG1 . VAL A 1 934  ? 45.998  -31.050 1.374   1.00 173.61 ? 934  VAL A CG1 1 
ATOM   7030  C  CG2 . VAL A 1 934  ? 46.938  -31.269 3.672   1.00 219.66 ? 934  VAL A CG2 1 
ATOM   7031  N  N   . LYS A 1 935  ? 48.441  -32.068 -0.650  1.00 199.28 ? 935  LYS A N   1 
ATOM   7032  C  CA  . LYS A 1 935  ? 48.266  -31.846 -2.085  1.00 197.03 ? 935  LYS A CA  1 
ATOM   7033  C  C   . LYS A 1 935  ? 47.095  -32.730 -2.567  1.00 197.82 ? 935  LYS A C   1 
ATOM   7034  O  O   . LYS A 1 935  ? 46.994  -33.896 -2.181  1.00 197.70 ? 935  LYS A O   1 
ATOM   7035  C  CB  . LYS A 1 935  ? 49.577  -32.149 -2.833  1.00 198.67 ? 935  LYS A CB  1 
ATOM   7036  C  CG  . LYS A 1 935  ? 50.088  -31.043 -3.791  1.00 167.13 ? 935  LYS A CG  1 
ATOM   7037  C  CD  . LYS A 1 935  ? 50.001  -29.629 -3.220  1.00 175.29 ? 935  LYS A CD  1 
ATOM   7038  C  CE  . LYS A 1 935  ? 49.994  -28.537 -4.314  1.00 175.78 ? 935  LYS A CE  1 
ATOM   7039  N  NZ  . LYS A 1 935  ? 51.322  -27.920 -4.650  1.00 180.53 ? 935  LYS A NZ  1 
ATOM   7040  N  N   . ARG A 1 936  ? 46.184  -32.177 -3.368  1.00 160.05 ? 936  ARG A N   1 
ATOM   7041  C  CA  . ARG A 1 936  ? 45.135  -33.009 -3.959  1.00 159.43 ? 936  ARG A CA  1 
ATOM   7042  C  C   . ARG A 1 936  ? 45.217  -33.098 -5.494  1.00 158.53 ? 936  ARG A C   1 
ATOM   7043  O  O   . ARG A 1 936  ? 45.186  -32.080 -6.192  1.00 159.70 ? 936  ARG A O   1 
ATOM   7044  C  CB  . ARG A 1 936  ? 43.752  -32.550 -3.514  1.00 158.16 ? 936  ARG A CB  1 
ATOM   7045  C  CG  . ARG A 1 936  ? 43.438  -31.117 -3.853  1.00 157.51 ? 936  ARG A CG  1 
ATOM   7046  C  CD  . ARG A 1 936  ? 42.393  -30.568 -2.909  1.00 162.58 ? 936  ARG A CD  1 
ATOM   7047  N  NE  . ARG A 1 936  ? 41.076  -30.424 -3.522  1.00 163.51 ? 936  ARG A NE  1 
ATOM   7048  C  CZ  . ARG A 1 936  ? 40.010  -29.936 -2.892  1.00 166.69 ? 936  ARG A CZ  1 
ATOM   7049  N  NH1 . ARG A 1 936  ? 40.105  -29.546 -1.630  1.00 170.02 ? 936  ARG A NH1 1 
ATOM   7050  N  NH2 . ARG A 1 936  ? 38.847  -29.834 -3.522  1.00 164.54 ? 936  ARG A NH2 1 
ATOM   7051  N  N   . GLU A 1 937  ? 45.322  -34.332 -5.997  1.00 214.68 ? 937  GLU A N   1 
ATOM   7052  C  CA  . GLU A 1 937  ? 45.365  -34.627 -7.434  1.00 220.42 ? 937  GLU A CA  1 
ATOM   7053  C  C   . GLU A 1 937  ? 44.138  -35.427 -7.903  1.00 222.43 ? 937  GLU A C   1 
ATOM   7054  O  O   . GLU A 1 937  ? 44.008  -36.622 -7.611  1.00 217.83 ? 937  GLU A O   1 
ATOM   7055  C  CB  . GLU A 1 937  ? 46.651  -35.381 -7.776  1.00 234.29 ? 937  GLU A CB  1 
ATOM   7056  C  CG  . GLU A 1 937  ? 46.749  -36.790 -7.186  1.00 286.03 ? 937  GLU A CG  1 
ATOM   7057  C  CD  . GLU A 1 937  ? 48.177  -37.328 -7.165  1.00 300.10 ? 937  GLU A CD  1 
ATOM   7058  O  OE1 . GLU A 1 937  ? 49.020  -36.732 -6.457  1.00 302.47 ? 937  GLU A OE1 1 
ATOM   7059  O  OE2 . GLU A 1 937  ? 48.457  -38.347 -7.843  1.00 299.76 ? 937  GLU A OE2 1 
ATOM   7060  N  N   . SER A 1 938  ? 43.272  -34.760 -8.671  1.00 140.30 ? 938  SER A N   1 
ATOM   7061  C  CA  . SER A 1 938  ? 41.909  -35.229 -8.936  1.00 142.13 ? 938  SER A CA  1 
ATOM   7062  C  C   . SER A 1 938  ? 41.608  -35.645 -10.386 1.00 150.13 ? 938  SER A C   1 
ATOM   7063  O  O   . SER A 1 938  ? 40.458  -35.975 -10.707 1.00 155.85 ? 938  SER A O   1 
ATOM   7064  C  CB  . SER A 1 938  ? 40.932  -34.130 -8.528  1.00 123.83 ? 938  SER A CB  1 
ATOM   7065  O  OG  . SER A 1 938  ? 41.242  -32.953 -9.235  1.00 162.92 ? 938  SER A OG  1 
ATOM   7066  N  N   . TYR A 1 939  ? 42.634  -35.651 -11.242 1.00 239.47 ? 939  TYR A N   1 
ATOM   7067  C  CA  . TYR A 1 939  ? 42.459  -35.727 -12.710 1.00 246.37 ? 939  TYR A CA  1 
ATOM   7068  C  C   . TYR A 1 939  ? 41.738  -36.955 -13.274 1.00 233.11 ? 939  TYR A C   1 
ATOM   7069  O  O   . TYR A 1 939  ? 41.427  -37.022 -14.473 1.00 223.27 ? 939  TYR A O   1 
ATOM   7070  C  CB  . TYR A 1 939  ? 43.787  -35.510 -13.451 1.00 277.12 ? 939  TYR A CB  1 
ATOM   7071  C  CG  . TYR A 1 939  ? 44.793  -36.625 -13.305 1.00 296.23 ? 939  TYR A CG  1 
ATOM   7072  C  CD1 . TYR A 1 939  ? 44.722  -37.765 -14.090 1.00 301.40 ? 939  TYR A CD1 1 
ATOM   7073  C  CD2 . TYR A 1 939  ? 45.828  -36.523 -12.395 1.00 305.67 ? 939  TYR A CD2 1 
ATOM   7074  C  CE1 . TYR A 1 939  ? 45.648  -38.775 -13.957 1.00 306.14 ? 939  TYR A CE1 1 
ATOM   7075  C  CE2 . TYR A 1 939  ? 46.756  -37.522 -12.257 1.00 310.47 ? 939  TYR A CE2 1 
ATOM   7076  C  CZ  . TYR A 1 939  ? 46.665  -38.645 -13.036 1.00 310.49 ? 939  TYR A CZ  1 
ATOM   7077  O  OH  . TYR A 1 939  ? 47.603  -39.637 -12.883 1.00 314.15 ? 939  TYR A OH  1 
ATOM   7078  N  N   . SER A 1 940  ? 41.491  -37.929 -12.412 1.00 212.84 ? 940  SER A N   1 
ATOM   7079  C  CA  . SER A 1 940  ? 40.583  -39.001 -12.748 1.00 206.22 ? 940  SER A CA  1 
ATOM   7080  C  C   . SER A 1 940  ? 39.203  -38.399 -12.971 1.00 193.49 ? 940  SER A C   1 
ATOM   7081  O  O   . SER A 1 940  ? 38.767  -37.507 -12.238 1.00 193.07 ? 940  SER A O   1 
ATOM   7082  C  CB  . SER A 1 940  ? 40.529  -40.002 -11.608 1.00 211.85 ? 940  SER A CB  1 
ATOM   7083  O  OG  . SER A 1 940  ? 40.091  -39.369 -10.422 1.00 213.44 ? 940  SER A OG  1 
ATOM   7084  N  N   . GLY A 1 941  ? 38.523  -38.887 -13.996 1.00 179.18 ? 941  GLY A N   1 
ATOM   7085  C  CA  . GLY A 1 941  ? 37.194  -38.418 -14.318 1.00 168.25 ? 941  GLY A CA  1 
ATOM   7086  C  C   . GLY A 1 941  ? 36.744  -39.124 -15.571 1.00 160.11 ? 941  GLY A C   1 
ATOM   7087  O  O   . GLY A 1 941  ? 37.578  -39.471 -16.409 1.00 158.90 ? 941  GLY A O   1 
ATOM   7088  N  N   . VAL A 1 942  ? 35.437  -39.344 -15.695 1.00 165.82 ? 942  VAL A N   1 
ATOM   7089  C  CA  . VAL A 1 942  ? 34.861  -39.949 -16.891 1.00 156.00 ? 942  VAL A CA  1 
ATOM   7090  C  C   . VAL A 1 942  ? 33.603  -39.204 -17.325 1.00 148.81 ? 942  VAL A C   1 
ATOM   7091  O  O   . VAL A 1 942  ? 33.133  -38.290 -16.636 1.00 150.63 ? 942  VAL A O   1 
ATOM   7092  C  CB  . VAL A 1 942  ? 34.463  -41.409 -16.635 1.00 155.55 ? 942  VAL A CB  1 
ATOM   7093  C  CG1 . VAL A 1 942  ? 34.701  -42.240 -17.882 1.00 155.19 ? 942  VAL A CG1 1 
ATOM   7094  C  CG2 . VAL A 1 942  ? 35.237  -41.968 -15.469 1.00 159.53 ? 942  VAL A CG2 1 
ATOM   7095  N  N   . THR A 1 943  ? 33.086  -39.577 -18.491 1.00 99.59  ? 943  THR A N   1 
ATOM   7096  C  CA  . THR A 1 943  ? 31.679  -39.365 -18.780 1.00 102.82 ? 943  THR A CA  1 
ATOM   7097  C  C   . THR A 1 943  ? 31.093  -40.732 -19.052 1.00 103.18 ? 943  THR A C   1 
ATOM   7098  O  O   . THR A 1 943  ? 31.618  -41.485 -19.856 1.00 104.38 ? 943  THR A O   1 
ATOM   7099  C  CB  . THR A 1 943  ? 31.417  -38.453 -19.995 1.00 98.04  ? 943  THR A CB  1 
ATOM   7100  O  OG1 . THR A 1 943  ? 32.294  -37.321 -19.962 1.00 98.79  ? 943  THR A OG1 1 
ATOM   7101  C  CG2 . THR A 1 943  ? 29.957  -37.976 -19.989 1.00 98.22  ? 943  THR A CG2 1 
ATOM   7102  N  N   . LEU A 1 944  ? 30.002  -41.027 -18.387 1.00 176.23 ? 944  LEU A N   1 
ATOM   7103  C  CA  . LEU A 1 944  ? 29.343  -42.259 -18.740 1.00 174.66 ? 944  LEU A CA  1 
ATOM   7104  C  C   . LEU A 1 944  ? 28.481  -41.953 -19.963 1.00 175.78 ? 944  LEU A C   1 
ATOM   7105  O  O   . LEU A 1 944  ? 27.607  -41.081 -19.927 1.00 175.36 ? 944  LEU A O   1 
ATOM   7106  C  CB  . LEU A 1 944  ? 28.524  -42.798 -17.596 1.00 174.21 ? 944  LEU A CB  1 
ATOM   7107  C  CG  . LEU A 1 944  ? 29.375  -43.508 -16.554 1.00 175.51 ? 944  LEU A CG  1 
ATOM   7108  C  CD1 . LEU A 1 944  ? 28.517  -44.320 -15.606 1.00 177.41 ? 944  LEU A CD1 1 
ATOM   7109  C  CD2 . LEU A 1 944  ? 30.404  -44.400 -17.226 1.00 174.49 ? 944  LEU A CD2 1 
ATOM   7110  N  N   . ASP A 1 945  ? 28.758  -42.686 -21.055 1.00 139.76 ? 945  ASP A N   1 
ATOM   7111  C  CA  . ASP A 1 945  ? 27.980  -42.552 -22.292 1.00 136.48 ? 945  ASP A CA  1 
ATOM   7112  C  C   . ASP A 1 945  ? 27.679  -43.914 -22.856 1.00 135.07 ? 945  ASP A C   1 
ATOM   7113  O  O   . ASP A 1 945  ? 28.457  -44.432 -23.664 1.00 136.41 ? 945  ASP A O   1 
ATOM   7114  C  CB  . ASP A 1 945  ? 28.709  -41.707 -23.322 1.00 135.47 ? 945  ASP A CB  1 
ATOM   7115  C  CG  . ASP A 1 945  ? 27.755  -41.040 -24.282 1.00 131.91 ? 945  ASP A CG  1 
ATOM   7116  O  OD1 . ASP A 1 945  ? 26.525  -41.237 -24.150 1.00 131.67 ? 945  ASP A OD1 1 
ATOM   7117  O  OD2 . ASP A 1 945  ? 28.242  -40.323 -25.183 1.00 128.36 ? 945  ASP A OD2 1 
ATOM   7118  N  N   . PRO A 1 946  ? 26.576  -44.480 -22.438 1.00 113.96 ? 946  PRO A N   1 
ATOM   7119  C  CA  . PRO A 1 946  ? 26.217  -45.812 -22.896 1.00 116.76 ? 946  PRO A CA  1 
ATOM   7120  C  C   . PRO A 1 946  ? 25.983  -45.800 -24.378 1.00 115.49 ? 946  PRO A C   1 
ATOM   7121  O  O   . PRO A 1 946  ? 26.423  -46.680 -25.111 1.00 116.00 ? 946  PRO A O   1 
ATOM   7122  C  CB  . PRO A 1 946  ? 24.925  -46.140 -22.139 1.00 117.39 ? 946  PRO A CB  1 
ATOM   7123  C  CG  . PRO A 1 946  ? 24.521  -44.861 -21.476 1.00 115.23 ? 946  PRO A CG  1 
ATOM   7124  C  CD  . PRO A 1 946  ? 25.355  -43.759 -22.075 1.00 115.77 ? 946  PRO A CD  1 
ATOM   7125  N  N   . ARG A 1 947  ? 25.242  -44.778 -24.813 1.00 122.61 ? 947  ARG A N   1 
ATOM   7126  C  CA  . ARG A 1 947  ? 24.822  -44.649 -26.239 1.00 120.70 ? 947  ARG A CA  1 
ATOM   7127  C  C   . ARG A 1 947  ? 25.852  -44.089 -27.259 1.00 118.02 ? 947  ARG A C   1 
ATOM   7128  O  O   . ARG A 1 947  ? 25.475  -43.736 -28.377 1.00 118.29 ? 947  ARG A O   1 
ATOM   7129  C  CB  . ARG A 1 947  ? 23.607  -43.750 -26.317 1.00 120.12 ? 947  ARG A CB  1 
ATOM   7130  C  CG  . ARG A 1 947  ? 22.572  -44.024 -25.251 1.00 122.58 ? 947  ARG A CG  1 
ATOM   7131  C  CD  . ARG A 1 947  ? 21.515  -44.974 -25.764 1.00 123.19 ? 947  ARG A CD  1 
ATOM   7132  N  NE  . ARG A 1 947  ? 20.377  -44.219 -26.253 1.00 121.75 ? 947  ARG A NE  1 
ATOM   7133  C  CZ  . ARG A 1 947  ? 19.123  -44.495 -25.895 1.00 125.79 ? 947  ARG A CZ  1 
ATOM   7134  N  NH1 . ARG A 1 947  ? 18.879  -45.507 -25.057 1.00 129.09 ? 947  ARG A NH1 1 
ATOM   7135  N  NH2 . ARG A 1 947  ? 18.110  -43.770 -26.374 1.00 125.72 ? 947  ARG A NH2 1 
ATOM   7136  N  N   . GLY A 1 948  ? 27.135  -44.007 -26.892 1.00 119.25 ? 948  GLY A N   1 
ATOM   7137  C  CA  . GLY A 1 948  ? 28.183  -43.536 -27.802 1.00 116.37 ? 948  GLY A CA  1 
ATOM   7138  C  C   . GLY A 1 948  ? 27.725  -42.304 -28.570 1.00 111.10 ? 948  GLY A C   1 
ATOM   7139  O  O   . GLY A 1 948  ? 27.866  -42.185 -29.783 1.00 108.55 ? 948  GLY A O   1 
ATOM   7140  N  N   . ILE A 1 949  ? 27.158  -41.403 -27.767 1.00 124.18 ? 949  ILE A N   1 
ATOM   7141  C  CA  . ILE A 1 949  ? 26.612  -40.125 -28.208 1.00 111.95 ? 949  ILE A CA  1 
ATOM   7142  C  C   . ILE A 1 949  ? 27.711  -39.060 -28.362 1.00 110.54 ? 949  ILE A C   1 
ATOM   7143  O  O   . ILE A 1 949  ? 27.479  -38.062 -29.031 1.00 113.09 ? 949  ILE A O   1 
ATOM   7144  C  CB  . ILE A 1 949  ? 25.520  -39.618 -27.229 1.00 116.95 ? 949  ILE A CB  1 
ATOM   7145  C  CG1 . ILE A 1 949  ? 24.302  -40.547 -27.220 1.00 122.52 ? 949  ILE A CG1 1 
ATOM   7146  C  CG2 . ILE A 1 949  ? 25.092  -38.204 -27.602 1.00 113.98 ? 949  ILE A CG2 1 
ATOM   7147  C  CD1 . ILE A 1 949  ? 22.966  -39.821 -27.192 1.00 119.68 ? 949  ILE A CD1 1 
ATOM   7148  N  N   . TYR A 1 950  ? 28.871  -39.229 -27.763 1.00 158.81 ? 950  TYR A N   1 
ATOM   7149  C  CA  . TYR A 1 950  ? 29.749  -38.094 -27.929 1.00 161.01 ? 950  TYR A CA  1 
ATOM   7150  C  C   . TYR A 1 950  ? 31.063  -38.396 -28.625 1.00 161.46 ? 950  TYR A C   1 
ATOM   7151  O  O   . TYR A 1 950  ? 31.836  -37.478 -28.897 1.00 162.55 ? 950  TYR A O   1 
ATOM   7152  C  CB  . TYR A 1 950  ? 30.002  -37.419 -26.563 1.00 153.79 ? 950  TYR A CB  1 
ATOM   7153  C  CG  . TYR A 1 950  ? 28.962  -36.355 -26.267 1.00 151.73 ? 950  TYR A CG  1 
ATOM   7154  C  CD1 . TYR A 1 950  ? 29.238  -35.009 -26.464 1.00 145.96 ? 950  TYR A CD1 1 
ATOM   7155  C  CD2 . TYR A 1 950  ? 27.682  -36.703 -25.840 1.00 151.83 ? 950  TYR A CD2 1 
ATOM   7156  C  CE1 . TYR A 1 950  ? 28.274  -34.038 -26.220 1.00 145.05 ? 950  TYR A CE1 1 
ATOM   7157  C  CE2 . TYR A 1 950  ? 26.712  -35.738 -25.594 1.00 152.71 ? 950  TYR A CE2 1 
ATOM   7158  C  CZ  . TYR A 1 950  ? 27.013  -34.412 -25.784 1.00 151.64 ? 950  TYR A CZ  1 
ATOM   7159  O  OH  . TYR A 1 950  ? 26.050  -33.464 -25.539 1.00 150.25 ? 950  TYR A OH  1 
ATOM   7160  N  N   . GLY A 1 951  ? 31.331  -39.667 -28.909 1.00 123.62 ? 951  GLY A N   1 
ATOM   7161  C  CA  . GLY A 1 951  ? 32.621  -40.048 -29.500 1.00 127.00 ? 951  GLY A CA  1 
ATOM   7162  C  C   . GLY A 1 951  ? 32.877  -41.552 -29.363 1.00 132.88 ? 951  GLY A C   1 
ATOM   7163  O  O   . GLY A 1 951  ? 33.696  -42.122 -30.080 1.00 134.54 ? 951  GLY A O   1 
ATOM   7164  N  N   . THR A 1 952  ? 32.194  -42.199 -28.434 1.00 119.49 ? 952  THR A N   1 
ATOM   7165  C  CA  . THR A 1 952  ? 32.310  -43.662 -28.246 1.00 120.29 ? 952  THR A CA  1 
ATOM   7166  C  C   . THR A 1 952  ? 31.406  -44.110 -27.130 1.00 120.29 ? 952  THR A C   1 
ATOM   7167  O  O   . THR A 1 952  ? 30.806  -43.286 -26.447 1.00 118.70 ? 952  THR A O   1 
ATOM   7168  C  CB  . THR A 1 952  ? 33.722  -44.172 -27.901 1.00 121.40 ? 952  THR A CB  1 
ATOM   7169  O  OG1 . THR A 1 952  ? 33.593  -45.317 -27.052 1.00 126.72 ? 952  THR A OG1 1 
ATOM   7170  C  CG2 . THR A 1 952  ? 34.529  -43.104 -27.178 1.00 119.05 ? 952  THR A CG2 1 
ATOM   7171  N  N   . ILE A 1 953  ? 31.305  -45.419 -26.938 1.00 131.82 ? 953  ILE A N   1 
ATOM   7172  C  CA  . ILE A 1 953  ? 30.561  -45.930 -25.801 1.00 136.83 ? 953  ILE A CA  1 
ATOM   7173  C  C   . ILE A 1 953  ? 31.465  -45.989 -24.571 1.00 148.76 ? 953  ILE A C   1 
ATOM   7174  O  O   . ILE A 1 953  ? 32.580  -46.526 -24.640 1.00 152.87 ? 953  ILE A O   1 
ATOM   7175  C  CB  . ILE A 1 953  ? 29.926  -47.286 -26.095 1.00 141.39 ? 953  ILE A CB  1 
ATOM   7176  C  CG1 . ILE A 1 953  ? 30.894  -48.425 -25.817 1.00 144.55 ? 953  ILE A CG1 1 
ATOM   7177  C  CG2 . ILE A 1 953  ? 29.475  -47.341 -27.535 1.00 143.12 ? 953  ILE A CG2 1 
ATOM   7178  C  CD1 . ILE A 1 953  ? 30.294  -49.772 -26.092 1.00 145.74 ? 953  ILE A CD1 1 
ATOM   7179  N  N   . SER A 1 954  ? 30.983  -45.421 -23.456 1.00 175.38 ? 954  SER A N   1 
ATOM   7180  C  CA  . SER A 1 954  ? 31.742  -45.345 -22.201 1.00 171.84 ? 954  SER A CA  1 
ATOM   7181  C  C   . SER A 1 954  ? 30.944  -45.968 -21.077 1.00 172.34 ? 954  SER A C   1 
ATOM   7182  O  O   . SER A 1 954  ? 30.047  -45.341 -20.516 1.00 172.91 ? 954  SER A O   1 
ATOM   7183  C  CB  . SER A 1 954  ? 32.066  -43.898 -21.841 1.00 165.16 ? 954  SER A CB  1 
ATOM   7184  O  OG  . SER A 1 954  ? 33.099  -43.850 -20.880 1.00 165.32 ? 954  SER A OG  1 
ATOM   7185  N  N   . ARG A 1 955  ? 31.273  -47.210 -20.758 1.00 145.26 ? 955  ARG A N   1 
ATOM   7186  C  CA  . ARG A 1 955  ? 30.536  -47.940 -19.748 1.00 147.73 ? 955  ARG A CA  1 
ATOM   7187  C  C   . ARG A 1 955  ? 31.462  -48.588 -18.725 1.00 154.27 ? 955  ARG A C   1 
ATOM   7188  O  O   . ARG A 1 955  ? 30.997  -49.405 -17.924 1.00 159.26 ? 955  ARG A O   1 
ATOM   7189  C  CB  . ARG A 1 955  ? 29.669  -49.029 -20.366 1.00 148.22 ? 955  ARG A CB  1 
ATOM   7190  C  CG  . ARG A 1 955  ? 28.511  -48.583 -21.226 1.00 146.30 ? 955  ARG A CG  1 
ATOM   7191  C  CD  . ARG A 1 955  ? 27.799  -49.852 -21.699 1.00 146.53 ? 955  ARG A CD  1 
ATOM   7192  N  NE  . ARG A 1 955  ? 27.133  -49.753 -22.995 1.00 140.61 ? 955  ARG A NE  1 
ATOM   7193  C  CZ  . ARG A 1 955  ? 26.931  -50.800 -23.795 1.00 140.47 ? 955  ARG A CZ  1 
ATOM   7194  N  NH1 . ARG A 1 955  ? 27.365  -52.007 -23.437 1.00 144.10 ? 955  ARG A NH1 1 
ATOM   7195  N  NH2 . ARG A 1 955  ? 26.307  -50.647 -24.956 1.00 142.90 ? 955  ARG A NH2 1 
ATOM   7196  N  N   . ARG A 1 956  ? 32.759  -48.254 -18.769 1.00 136.25 ? 956  ARG A N   1 
ATOM   7197  C  CA  . ARG A 1 956  ? 33.719  -48.655 -17.711 1.00 139.04 ? 956  ARG A CA  1 
ATOM   7198  C  C   . ARG A 1 956  ? 35.070  -47.888 -17.732 1.00 144.50 ? 956  ARG A C   1 
ATOM   7199  O  O   . ARG A 1 956  ? 35.904  -48.079 -18.641 1.00 142.85 ? 956  ARG A O   1 
ATOM   7200  C  CB  . ARG A 1 956  ? 33.951  -50.188 -17.684 1.00 139.80 ? 956  ARG A CB  1 
ATOM   7201  C  CG  . ARG A 1 956  ? 34.079  -50.771 -16.266 1.00 144.19 ? 956  ARG A CG  1 
ATOM   7202  C  CD  . ARG A 1 956  ? 34.271  -52.286 -16.227 1.00 150.65 ? 956  ARG A CD  1 
ATOM   7203  N  NE  . ARG A 1 956  ? 35.688  -52.636 -16.213 1.00 154.68 ? 956  ARG A NE  1 
ATOM   7204  C  CZ  . ARG A 1 956  ? 36.175  -53.796 -15.792 1.00 160.37 ? 956  ARG A CZ  1 
ATOM   7205  N  NH1 . ARG A 1 956  ? 35.359  -54.734 -15.335 1.00 163.03 ? 956  ARG A NH1 1 
ATOM   7206  N  NH2 . ARG A 1 956  ? 37.482  -54.012 -15.829 1.00 162.20 ? 956  ARG A NH2 1 
ATOM   7207  N  N   . LYS A 1 957  ? 35.253  -47.011 -16.732 1.00 146.71 ? 957  LYS A N   1 
ATOM   7208  C  CA  . LYS A 1 957  ? 36.530  -46.333 -16.472 1.00 148.42 ? 957  LYS A CA  1 
ATOM   7209  C  C   . LYS A 1 957  ? 37.059  -46.817 -15.148 1.00 149.43 ? 957  LYS A C   1 
ATOM   7210  O  O   . LYS A 1 957  ? 36.295  -47.223 -14.278 1.00 147.70 ? 957  LYS A O   1 
ATOM   7211  C  CB  . LYS A 1 957  ? 36.406  -44.805 -16.445 1.00 147.25 ? 957  LYS A CB  1 
ATOM   7212  C  CG  . LYS A 1 957  ? 37.721  -44.081 -16.076 1.00 152.76 ? 957  LYS A CG  1 
ATOM   7213  C  CD  . LYS A 1 957  ? 38.207  -43.087 -17.155 1.00 154.36 ? 957  LYS A CD  1 
ATOM   7214  C  CE  . LYS A 1 957  ? 39.717  -43.237 -17.525 1.00 159.70 ? 957  LYS A CE  1 
ATOM   7215  N  NZ  . LYS A 1 957  ? 40.692  -43.253 -16.380 1.00 165.23 ? 957  LYS A NZ  1 
ATOM   7216  N  N   . GLU A 1 958  ? 38.374  -46.753 -14.997 1.00 155.57 ? 958  GLU A N   1 
ATOM   7217  C  CA  . GLU A 1 958  ? 39.029  -47.353 -13.857 1.00 164.25 ? 958  GLU A CA  1 
ATOM   7218  C  C   . GLU A 1 958  ? 40.048  -46.423 -13.188 1.00 165.79 ? 958  GLU A C   1 
ATOM   7219  O  O   . GLU A 1 958  ? 41.122  -46.149 -13.732 1.00 166.00 ? 958  GLU A O   1 
ATOM   7220  C  CB  . GLU A 1 958  ? 39.693  -48.644 -14.303 1.00 172.47 ? 958  GLU A CB  1 
ATOM   7221  C  CG  . GLU A 1 958  ? 40.361  -49.397 -13.198 1.00 183.09 ? 958  GLU A CG  1 
ATOM   7222  C  CD  . GLU A 1 958  ? 40.999  -50.663 -13.701 1.00 191.61 ? 958  GLU A CD  1 
ATOM   7223  O  OE1 . GLU A 1 958  ? 40.367  -51.340 -14.543 1.00 193.60 ? 958  GLU A OE1 1 
ATOM   7224  O  OE2 . GLU A 1 958  ? 42.124  -50.980 -13.258 1.00 195.39 ? 958  GLU A OE2 1 
ATOM   7225  N  N   . PHE A 1 959  ? 39.675  -45.935 -12.004 1.00 188.76 ? 959  PHE A N   1 
ATOM   7226  C  CA  . PHE A 1 959  ? 40.569  -45.204 -11.109 1.00 191.17 ? 959  PHE A CA  1 
ATOM   7227  C  C   . PHE A 1 959  ? 41.175  -46.166 -10.115 1.00 200.06 ? 959  PHE A C   1 
ATOM   7228  O  O   . PHE A 1 959  ? 40.463  -46.716 -9.272  1.00 203.34 ? 959  PHE A O   1 
ATOM   7229  C  CB  . PHE A 1 959  ? 39.769  -44.202 -10.315 1.00 184.10 ? 959  PHE A CB  1 
ATOM   7230  C  CG  . PHE A 1 959  ? 38.667  -43.615 -11.081 1.00 176.77 ? 959  PHE A CG  1 
ATOM   7231  C  CD1 . PHE A 1 959  ? 38.861  -42.453 -11.784 1.00 173.55 ? 959  PHE A CD1 1 
ATOM   7232  C  CD2 . PHE A 1 959  ? 37.445  -44.244 -11.143 1.00 174.03 ? 959  PHE A CD2 1 
ATOM   7233  C  CE1 . PHE A 1 959  ? 37.855  -41.899 -12.514 1.00 169.42 ? 959  PHE A CE1 1 
ATOM   7234  C  CE2 . PHE A 1 959  ? 36.428  -43.701 -11.880 1.00 170.20 ? 959  PHE A CE2 1 
ATOM   7235  C  CZ  . PHE A 1 959  ? 36.633  -42.522 -12.568 1.00 167.85 ? 959  PHE A CZ  1 
ATOM   7236  N  N   . PRO A 1 960  ? 42.495  -46.369 -10.198 1.00 174.06 ? 960  PRO A N   1 
ATOM   7237  C  CA  . PRO A 1 960  ? 43.221  -47.283 -9.317  1.00 183.33 ? 960  PRO A CA  1 
ATOM   7238  C  C   . PRO A 1 960  ? 43.870  -46.577 -8.134  1.00 193.22 ? 960  PRO A C   1 
ATOM   7239  O  O   . PRO A 1 960  ? 43.611  -45.405 -7.844  1.00 191.92 ? 960  PRO A O   1 
ATOM   7240  C  CB  . PRO A 1 960  ? 44.336  -47.829 -10.225 1.00 183.31 ? 960  PRO A CB  1 
ATOM   7241  C  CG  . PRO A 1 960  ? 44.167  -47.131 -11.574 1.00 166.71 ? 960  PRO A CG  1 
ATOM   7242  C  CD  . PRO A 1 960  ? 43.343  -45.915 -11.306 1.00 167.04 ? 960  PRO A CD  1 
ATOM   7243  N  N   . TYR A 1 961  ? 44.737  -47.329 -7.466  1.00 232.22 ? 961  TYR A N   1 
ATOM   7244  C  CA  . TYR A 1 961  ? 45.615  -46.816 -6.429  1.00 241.73 ? 961  TYR A CA  1 
ATOM   7245  C  C   . TYR A 1 961  ? 46.908  -46.288 -7.024  1.00 244.70 ? 961  TYR A C   1 
ATOM   7246  O  O   . TYR A 1 961  ? 47.566  -46.975 -7.812  1.00 246.64 ? 961  TYR A O   1 
ATOM   7247  C  CB  . TYR A 1 961  ? 45.961  -47.942 -5.465  1.00 250.23 ? 961  TYR A CB  1 
ATOM   7248  C  CG  . TYR A 1 961  ? 45.383  -47.733 -4.110  1.00 255.62 ? 961  TYR A CG  1 
ATOM   7249  C  CD1 . TYR A 1 961  ? 46.192  -47.414 -3.036  1.00 260.16 ? 961  TYR A CD1 1 
ATOM   7250  C  CD2 . TYR A 1 961  ? 44.021  -47.828 -3.906  1.00 255.81 ? 961  TYR A CD2 1 
ATOM   7251  C  CE1 . TYR A 1 961  ? 45.660  -47.210 -1.793  1.00 263.03 ? 961  TYR A CE1 1 
ATOM   7252  C  CE2 . TYR A 1 961  ? 43.479  -47.625 -2.672  1.00 259.40 ? 961  TYR A CE2 1 
ATOM   7253  C  CZ  . TYR A 1 961  ? 44.300  -47.317 -1.617  1.00 263.35 ? 961  TYR A CZ  1 
ATOM   7254  O  OH  . TYR A 1 961  ? 43.752  -47.106 -0.381  1.00 267.16 ? 961  TYR A OH  1 
ATOM   7255  N  N   . ARG A 1 962  ? 47.281  -45.075 -6.640  1.00 236.59 ? 962  ARG A N   1 
ATOM   7256  C  CA  . ARG A 1 962  ? 48.602  -44.565 -6.975  1.00 241.69 ? 962  ARG A CA  1 
ATOM   7257  C  C   . ARG A 1 962  ? 49.194  -43.787 -5.804  1.00 240.75 ? 962  ARG A C   1 
ATOM   7258  O  O   . ARG A 1 962  ? 49.094  -42.559 -5.749  1.00 236.54 ? 962  ARG A O   1 
ATOM   7259  C  CB  . ARG A 1 962  ? 48.590  -43.708 -8.247  1.00 247.14 ? 962  ARG A CB  1 
ATOM   7260  C  CG  . ARG A 1 962  ? 49.866  -42.891 -8.426  1.00 257.77 ? 962  ARG A CG  1 
ATOM   7261  C  CD  . ARG A 1 962  ? 50.463  -43.027 -9.807  1.00 264.10 ? 962  ARG A CD  1 
ATOM   7262  N  NE  . ARG A 1 962  ? 50.268  -41.803 -10.567 1.00 266.38 ? 962  ARG A NE  1 
ATOM   7263  C  CZ  . ARG A 1 962  ? 51.006  -41.449 -11.610 1.00 268.87 ? 962  ARG A CZ  1 
ATOM   7264  N  NH1 . ARG A 1 962  ? 52.001  -42.227 -12.020 1.00 272.25 ? 962  ARG A NH1 1 
ATOM   7265  N  NH2 . ARG A 1 962  ? 50.749  -40.310 -12.237 1.00 266.60 ? 962  ARG A NH2 1 
ATOM   7266  N  N   . ILE A 1 963  ? 49.805  -44.516 -4.869  1.00 214.58 ? 963  ILE A N   1 
ATOM   7267  C  CA  . ILE A 1 963  ? 50.462  -43.920 -3.710  1.00 210.36 ? 963  ILE A CA  1 
ATOM   7268  C  C   . ILE A 1 963  ? 51.747  -43.203 -4.125  1.00 210.98 ? 963  ILE A C   1 
ATOM   7269  O  O   . ILE A 1 963  ? 52.749  -43.848 -4.472  1.00 212.51 ? 963  ILE A O   1 
ATOM   7270  C  CB  . ILE A 1 963  ? 50.787  -44.985 -2.638  1.00 204.89 ? 963  ILE A CB  1 
ATOM   7271  C  CG1 . ILE A 1 963  ? 49.755  -46.117 -2.656  1.00 199.47 ? 963  ILE A CG1 1 
ATOM   7272  C  CG2 . ILE A 1 963  ? 50.810  -44.349 -1.276  1.00 206.74 ? 963  ILE A CG2 1 
ATOM   7273  C  CD1 . ILE A 1 963  ? 50.072  -47.267 -1.707  1.00 201.73 ? 963  ILE A CD1 1 
ATOM   7274  N  N   . PRO A 1 964  ? 51.720  -41.860 -4.086  1.00 220.94 ? 964  PRO A N   1 
ATOM   7275  C  CA  . PRO A 1 964  ? 52.864  -41.042 -4.495  1.00 223.58 ? 964  PRO A CA  1 
ATOM   7276  C  C   . PRO A 1 964  ? 54.020  -41.349 -3.562  1.00 232.55 ? 964  PRO A C   1 
ATOM   7277  O  O   . PRO A 1 964  ? 53.803  -41.347 -2.351  1.00 235.34 ? 964  PRO A O   1 
ATOM   7278  C  CB  . PRO A 1 964  ? 52.377  -39.605 -4.255  1.00 221.52 ? 964  PRO A CB  1 
ATOM   7279  C  CG  . PRO A 1 964  ? 50.894  -39.699 -4.067  1.00 215.44 ? 964  PRO A CG  1 
ATOM   7280  C  CD  . PRO A 1 964  ? 50.640  -41.050 -3.499  1.00 217.31 ? 964  PRO A CD  1 
ATOM   7281  N  N   . LEU A 1 965  ? 55.215  -41.604 -4.086  1.00 253.74 ? 965  LEU A N   1 
ATOM   7282  C  CA  . LEU A 1 965  ? 56.330  -42.010 -3.219  1.00 264.86 ? 965  LEU A CA  1 
ATOM   7283  C  C   . LEU A 1 965  ? 56.761  -40.936 -2.187  1.00 270.09 ? 965  LEU A C   1 
ATOM   7284  O  O   . LEU A 1 965  ? 57.781  -41.080 -1.507  1.00 275.70 ? 965  LEU A O   1 
ATOM   7285  C  CB  . LEU A 1 965  ? 57.522  -42.524 -4.043  1.00 268.91 ? 965  LEU A CB  1 
ATOM   7286  C  CG  . LEU A 1 965  ? 57.317  -43.792 -4.889  1.00 282.34 ? 965  LEU A CG  1 
ATOM   7287  C  CD1 . LEU A 1 965  ? 58.649  -44.298 -5.438  1.00 285.44 ? 965  LEU A CD1 1 
ATOM   7288  C  CD2 . LEU A 1 965  ? 56.612  -44.902 -4.112  1.00 284.69 ? 965  LEU A CD2 1 
ATOM   7289  N  N   . ASP A 1 966  ? 55.971  -39.872 -2.073  1.00 241.89 ? 966  ASP A N   1 
ATOM   7290  C  CA  . ASP A 1 966  ? 56.204  -38.833 -1.081  1.00 241.71 ? 966  ASP A CA  1 
ATOM   7291  C  C   . ASP A 1 966  ? 55.139  -38.870 0.003   1.00 234.24 ? 966  ASP A C   1 
ATOM   7292  O  O   . ASP A 1 966  ? 54.941  -37.881 0.707   1.00 235.30 ? 966  ASP A O   1 
ATOM   7293  C  CB  . ASP A 1 966  ? 56.185  -37.449 -1.728  1.00 242.57 ? 966  ASP A CB  1 
ATOM   7294  C  CG  . ASP A 1 966  ? 57.537  -37.037 -2.259  1.00 246.18 ? 966  ASP A CG  1 
ATOM   7295  O  OD1 . ASP A 1 966  ? 58.531  -37.730 -1.956  1.00 250.49 ? 966  ASP A OD1 1 
ATOM   7296  O  OD2 . ASP A 1 966  ? 57.607  -36.017 -2.973  1.00 243.94 ? 966  ASP A OD2 1 
ATOM   7297  N  N   . LEU A 1 967  ? 54.436  -39.990 0.131   1.00 209.19 ? 967  LEU A N   1 
ATOM   7298  C  CA  . LEU A 1 967  ? 53.322  -40.050 1.075   1.00 203.72 ? 967  LEU A CA  1 
ATOM   7299  C  C   . LEU A 1 967  ? 53.816  -39.799 2.499   1.00 203.91 ? 967  LEU A C   1 
ATOM   7300  O  O   . LEU A 1 967  ? 54.873  -40.302 2.880   1.00 208.47 ? 967  LEU A O   1 
ATOM   7301  C  CB  . LEU A 1 967  ? 52.591  -41.399 1.000   1.00 202.69 ? 967  LEU A CB  1 
ATOM   7302  C  CG  . LEU A 1 967  ? 51.563  -41.656 2.115   1.00 204.92 ? 967  LEU A CG  1 
ATOM   7303  C  CD1 . LEU A 1 967  ? 50.531  -40.530 2.247   1.00 203.34 ? 967  LEU A CD1 1 
ATOM   7304  C  CD2 . LEU A 1 967  ? 50.883  -43.004 1.941   1.00 204.09 ? 967  LEU A CD2 1 
ATOM   7305  N  N   . VAL A 1 968  ? 53.069  -39.024 3.282   1.00 201.36 ? 968  VAL A N   1 
ATOM   7306  C  CA  . VAL A 1 968  ? 53.388  -38.860 4.699   1.00 200.49 ? 968  VAL A CA  1 
ATOM   7307  C  C   . VAL A 1 968  ? 52.903  -40.071 5.511   1.00 202.03 ? 968  VAL A C   1 
ATOM   7308  O  O   . VAL A 1 968  ? 51.727  -40.166 5.842   1.00 198.95 ? 968  VAL A O   1 
ATOM   7309  C  CB  . VAL A 1 968  ? 52.750  -37.597 5.230   1.00 196.11 ? 968  VAL A CB  1 
ATOM   7310  C  CG1 . VAL A 1 968  ? 53.286  -36.415 4.482   1.00 192.54 ? 968  VAL A CG1 1 
ATOM   7311  C  CG2 . VAL A 1 968  ? 51.262  -37.661 5.031   1.00 192.57 ? 968  VAL A CG2 1 
ATOM   7312  N  N   . PRO A 1 969  ? 53.819  -40.994 5.852   1.00 201.25 ? 969  PRO A N   1 
ATOM   7313  C  CA  . PRO A 1 969  ? 53.461  -42.366 6.247   1.00 205.46 ? 969  PRO A CA  1 
ATOM   7314  C  C   . PRO A 1 969  ? 52.256  -42.480 7.179   1.00 210.66 ? 969  PRO A C   1 
ATOM   7315  O  O   . PRO A 1 969  ? 51.850  -41.505 7.793   1.00 211.30 ? 969  PRO A O   1 
ATOM   7316  C  CB  . PRO A 1 969  ? 54.729  -42.877 6.918   1.00 209.79 ? 969  PRO A CB  1 
ATOM   7317  C  CG  . PRO A 1 969  ? 55.819  -42.129 6.234   1.00 208.31 ? 969  PRO A CG  1 
ATOM   7318  C  CD  . PRO A 1 969  ? 55.263  -40.752 5.984   1.00 204.31 ? 969  PRO A CD  1 
ATOM   7319  N  N   . LYS A 1 970  ? 51.677  -43.672 7.251   1.00 243.87 ? 970  LYS A N   1 
ATOM   7320  C  CA  . LYS A 1 970  ? 50.505  -43.928 8.087   1.00 252.06 ? 970  LYS A CA  1 
ATOM   7321  C  C   . LYS A 1 970  ? 49.351  -42.936 7.947   1.00 251.56 ? 970  LYS A C   1 
ATOM   7322  O  O   . LYS A 1 970  ? 48.595  -42.743 8.890   1.00 252.13 ? 970  LYS A O   1 
ATOM   7323  C  CB  . LYS A 1 970  ? 50.899  -44.041 9.558   1.00 263.31 ? 970  LYS A CB  1 
ATOM   7324  C  CG  . LYS A 1 970  ? 51.437  -45.401 9.960   1.00 274.44 ? 970  LYS A CG  1 
ATOM   7325  C  CD  . LYS A 1 970  ? 51.349  -45.599 11.474  1.00 285.23 ? 970  LYS A CD  1 
ATOM   7326  C  CE  . LYS A 1 970  ? 51.822  -46.991 11.889  1.00 292.80 ? 970  LYS A CE  1 
ATOM   7327  N  NZ  . LYS A 1 970  ? 51.523  -47.307 13.319  1.00 298.23 ? 970  LYS A NZ  1 
ATOM   7328  N  N   . THR A 1 971  ? 49.215  -42.309 6.785   1.00 236.09 ? 971  THR A N   1 
ATOM   7329  C  CA  . THR A 1 971  ? 48.058  -41.462 6.512   1.00 235.64 ? 971  THR A CA  1 
ATOM   7330  C  C   . THR A 1 971  ? 47.317  -41.949 5.286   1.00 230.94 ? 971  THR A C   1 
ATOM   7331  O  O   . THR A 1 971  ? 47.828  -41.857 4.173   1.00 231.03 ? 971  THR A O   1 
ATOM   7332  C  CB  . THR A 1 971  ? 48.475  -40.026 6.228   1.00 236.86 ? 971  THR A CB  1 
ATOM   7333  O  OG1 . THR A 1 971  ? 48.990  -39.929 4.893   1.00 232.51 ? 971  THR A OG1 1 
ATOM   7334  C  CG2 . THR A 1 971  ? 49.531  -39.602 7.217   1.00 243.62 ? 971  THR A CG2 1 
ATOM   7335  N  N   . GLU A 1 972  ? 46.108  -42.450 5.489   1.00 295.24 ? 972  GLU A N   1 
ATOM   7336  C  CA  . GLU A 1 972  ? 45.307  -42.991 4.397   1.00 289.21 ? 972  GLU A CA  1 
ATOM   7337  C  C   . GLU A 1 972  ? 45.014  -41.991 3.264   1.00 275.56 ? 972  GLU A C   1 
ATOM   7338  O  O   . GLU A 1 972  ? 44.844  -40.792 3.514   1.00 270.94 ? 972  GLU A O   1 
ATOM   7339  C  CB  . GLU A 1 972  ? 44.004  -43.546 4.964   1.00 297.79 ? 972  GLU A CB  1 
ATOM   7340  C  CG  . GLU A 1 972  ? 43.564  -42.849 6.244   1.00 307.85 ? 972  GLU A CG  1 
ATOM   7341  C  CD  . GLU A 1 972  ? 42.401  -43.550 6.915   1.00 314.79 ? 972  GLU A CD  1 
ATOM   7342  O  OE1 . GLU A 1 972  ? 41.672  -44.288 6.220   1.00 314.09 ? 972  GLU A OE1 1 
ATOM   7343  O  OE2 . GLU A 1 972  ? 42.212  -43.364 8.135   1.00 320.14 ? 972  GLU A OE2 1 
ATOM   7344  N  N   . ILE A 1 973  ? 44.963  -42.502 2.025   1.00 171.73 ? 973  ILE A N   1 
ATOM   7345  C  CA  . ILE A 1 973  ? 44.585  -41.709 0.848   1.00 160.48 ? 973  ILE A CA  1 
ATOM   7346  C  C   . ILE A 1 973  ? 43.063  -41.572 0.734   1.00 161.77 ? 973  ILE A C   1 
ATOM   7347  O  O   . ILE A 1 973  ? 42.368  -42.531 0.381   1.00 163.49 ? 973  ILE A O   1 
ATOM   7348  C  CB  . ILE A 1 973  ? 45.119  -42.287 -0.502  1.00 146.80 ? 973  ILE A CB  1 
ATOM   7349  C  CG1 . ILE A 1 973  ? 46.249  -43.298 -0.326  1.00 146.99 ? 973  ILE A CG1 1 
ATOM   7350  C  CG2 . ILE A 1 973  ? 45.591  -41.163 -1.367  1.00 139.82 ? 973  ILE A CG2 1 
ATOM   7351  C  CD1 . ILE A 1 973  ? 47.388  -43.095 -1.332  1.00 144.94 ? 973  ILE A CD1 1 
ATOM   7352  N  N   . LYS A 1 974  ? 42.563  -40.371 1.019   1.00 222.02 ? 974  LYS A N   1 
ATOM   7353  C  CA  . LYS A 1 974  ? 41.135  -40.071 0.988   1.00 218.05 ? 974  LYS A CA  1 
ATOM   7354  C  C   . LYS A 1 974  ? 40.684  -39.543 -0.373  1.00 207.63 ? 974  LYS A C   1 
ATOM   7355  O  O   . LYS A 1 974  ? 41.296  -38.610 -0.895  1.00 205.89 ? 974  LYS A O   1 
ATOM   7356  C  CB  . LYS A 1 974  ? 40.833  -39.023 2.047   1.00 223.41 ? 974  LYS A CB  1 
ATOM   7357  C  CG  . LYS A 1 974  ? 39.481  -38.365 1.912   1.00 226.96 ? 974  LYS A CG  1 
ATOM   7358  C  CD  . LYS A 1 974  ? 39.245  -37.420 3.071   1.00 235.77 ? 974  LYS A CD  1 
ATOM   7359  C  CE  . LYS A 1 974  ? 37.919  -36.700 2.941   1.00 237.05 ? 974  LYS A CE  1 
ATOM   7360  N  NZ  . LYS A 1 974  ? 37.713  -35.770 4.087   1.00 239.91 ? 974  LYS A NZ  1 
ATOM   7361  N  N   . ARG A 1 975  ? 39.610  -40.116 -0.933  1.00 134.58 ? 975  ARG A N   1 
ATOM   7362  C  CA  . ARG A 1 975  ? 39.128  -39.727 -2.270  1.00 137.80 ? 975  ARG A CA  1 
ATOM   7363  C  C   . ARG A 1 975  ? 37.608  -39.785 -2.496  1.00 130.88 ? 975  ARG A C   1 
ATOM   7364  O  O   . ARG A 1 975  ? 36.912  -40.699 -2.037  1.00 132.86 ? 975  ARG A O   1 
ATOM   7365  C  CB  . ARG A 1 975  ? 39.851  -40.545 -3.316  1.00 135.02 ? 975  ARG A CB  1 
ATOM   7366  C  CG  . ARG A 1 975  ? 39.976  -41.962 -2.909  1.00 135.52 ? 975  ARG A CG  1 
ATOM   7367  C  CD  . ARG A 1 975  ? 41.117  -42.611 -3.637  1.00 135.09 ? 975  ARG A CD  1 
ATOM   7368  N  NE  . ARG A 1 975  ? 40.862  -44.034 -3.776  1.00 136.16 ? 975  ARG A NE  1 
ATOM   7369  C  CZ  . ARG A 1 975  ? 41.410  -44.815 -4.707  1.00 134.01 ? 975  ARG A CZ  1 
ATOM   7370  N  NH1 . ARG A 1 975  ? 42.266  -44.324 -5.607  1.00 130.34 ? 975  ARG A NH1 1 
ATOM   7371  N  NH2 . ARG A 1 975  ? 41.094  -46.102 -4.742  1.00 135.70 ? 975  ARG A NH2 1 
ATOM   7372  N  N   . ILE A 1 976  ? 37.123  -38.780 -3.220  1.00 154.71 ? 976  ILE A N   1 
ATOM   7373  C  CA  . ILE A 1 976  ? 35.704  -38.601 -3.467  1.00 148.75 ? 976  ILE A CA  1 
ATOM   7374  C  C   . ILE A 1 976  ? 35.362  -39.002 -4.880  1.00 143.16 ? 976  ILE A C   1 
ATOM   7375  O  O   . ILE A 1 976  ? 36.231  -39.012 -5.748  1.00 143.81 ? 976  ILE A O   1 
ATOM   7376  C  CB  . ILE A 1 976  ? 35.310  -37.149 -3.303  1.00 147.49 ? 976  ILE A CB  1 
ATOM   7377  C  CG1 . ILE A 1 976  ? 36.240  -36.537 -2.275  1.00 154.22 ? 976  ILE A CG1 1 
ATOM   7378  C  CG2 . ILE A 1 976  ? 33.840  -37.053 -2.904  1.00 145.33 ? 976  ILE A CG2 1 
ATOM   7379  C  CD1 . ILE A 1 976  ? 36.334  -35.042 -2.288  1.00 156.77 ? 976  ILE A CD1 1 
ATOM   7380  N  N   . LEU A 1 977  ? 34.076  -39.283 -5.103  1.00 145.27 ? 977  LEU A N   1 
ATOM   7381  C  CA  . LEU A 1 977  ? 33.561  -39.906 -6.323  1.00 136.31 ? 977  LEU A CA  1 
ATOM   7382  C  C   . LEU A 1 977  ? 32.193  -39.318 -6.617  1.00 133.27 ? 977  LEU A C   1 
ATOM   7383  O  O   . LEU A 1 977  ? 31.196  -39.781 -6.069  1.00 135.88 ? 977  LEU A O   1 
ATOM   7384  C  CB  . LEU A 1 977  ? 33.418  -41.384 -6.036  1.00 136.48 ? 977  LEU A CB  1 
ATOM   7385  C  CG  . LEU A 1 977  ? 32.859  -42.372 -7.019  1.00 136.09 ? 977  LEU A CG  1 
ATOM   7386  C  CD1 . LEU A 1 977  ? 34.023  -43.133 -7.571  1.00 135.63 ? 977  LEU A CD1 1 
ATOM   7387  C  CD2 . LEU A 1 977  ? 31.945  -43.285 -6.233  1.00 141.16 ? 977  LEU A CD2 1 
ATOM   7388  N  N   . SER A 1 978  ? 32.154  -38.288 -7.463  1.00 127.62 ? 978  SER A N   1 
ATOM   7389  C  CA  . SER A 1 978  ? 30.923  -37.527 -7.717  1.00 128.07 ? 978  SER A CA  1 
ATOM   7390  C  C   . SER A 1 978  ? 30.222  -37.963 -9.012  1.00 134.46 ? 978  SER A C   1 
ATOM   7391  O  O   . SER A 1 978  ? 30.668  -37.638 -10.118 1.00 137.19 ? 978  SER A O   1 
ATOM   7392  C  CB  . SER A 1 978  ? 31.215  -36.025 -7.762  1.00 126.11 ? 978  SER A CB  1 
ATOM   7393  O  OG  . SER A 1 978  ? 30.035  -35.268 -7.627  1.00 122.90 ? 978  SER A OG  1 
ATOM   7394  N  N   . VAL A 1 979  ? 29.120  -38.696 -8.864  1.00 124.38 ? 979  VAL A N   1 
ATOM   7395  C  CA  . VAL A 1 979  ? 28.390  -39.227 -10.002 1.00 119.04 ? 979  VAL A CA  1 
ATOM   7396  C  C   . VAL A 1 979  ? 27.068  -38.476 -10.157 1.00 116.95 ? 979  VAL A C   1 
ATOM   7397  O  O   . VAL A 1 979  ? 26.165  -38.619 -9.328  1.00 120.84 ? 979  VAL A O   1 
ATOM   7398  C  CB  . VAL A 1 979  ? 28.095  -40.739 -9.824  1.00 118.46 ? 979  VAL A CB  1 
ATOM   7399  C  CG1 . VAL A 1 979  ? 28.411  -41.469 -11.076 1.00 115.05 ? 979  VAL A CG1 1 
ATOM   7400  C  CG2 . VAL A 1 979  ? 28.922  -41.327 -8.724  1.00 121.43 ? 979  VAL A CG2 1 
ATOM   7401  N  N   . LYS A 1 980  ? 26.953  -37.686 -11.224 1.00 164.80 ? 980  LYS A N   1 
ATOM   7402  C  CA  . LYS A 1 980  ? 25.713  -36.958 -11.508 1.00 165.14 ? 980  LYS A CA  1 
ATOM   7403  C  C   . LYS A 1 980  ? 25.246  -37.059 -12.972 1.00 161.32 ? 980  LYS A C   1 
ATOM   7404  O  O   . LYS A 1 980  ? 26.057  -37.065 -13.898 1.00 161.09 ? 980  LYS A O   1 
ATOM   7405  C  CB  . LYS A 1 980  ? 25.850  -35.491 -11.094 1.00 166.19 ? 980  LYS A CB  1 
ATOM   7406  C  CG  . LYS A 1 980  ? 27.275  -35.058 -10.796 1.00 167.70 ? 980  LYS A CG  1 
ATOM   7407  C  CD  . LYS A 1 980  ? 27.674  -35.471 -9.392  1.00 169.74 ? 980  LYS A CD  1 
ATOM   7408  C  CE  . LYS A 1 980  ? 26.680  -34.930 -8.359  1.00 167.90 ? 980  LYS A CE  1 
ATOM   7409  N  NZ  . LYS A 1 980  ? 26.950  -35.337 -6.937  1.00 170.19 ? 980  LYS A NZ  1 
ATOM   7410  N  N   . GLY A 1 981  ? 23.933  -37.142 -13.174 1.00 127.34 ? 981  GLY A N   1 
ATOM   7411  C  CA  . GLY A 1 981  ? 23.366  -37.057 -14.507 1.00 122.37 ? 981  GLY A CA  1 
ATOM   7412  C  C   . GLY A 1 981  ? 23.455  -35.659 -15.087 1.00 118.23 ? 981  GLY A C   1 
ATOM   7413  O  O   . GLY A 1 981  ? 23.340  -34.676 -14.373 1.00 119.42 ? 981  GLY A O   1 
ATOM   7414  N  N   . LEU A 1 982  ? 23.663  -35.587 -16.393 1.00 95.42  ? 982  LEU A N   1 
ATOM   7415  C  CA  . LEU A 1 982  ? 23.759  -34.327 -17.125 1.00 103.82 ? 982  LEU A CA  1 
ATOM   7416  C  C   . LEU A 1 982  ? 25.152  -33.690 -17.138 1.00 96.67  ? 982  LEU A C   1 
ATOM   7417  O  O   . LEU A 1 982  ? 25.952  -33.908 -16.235 1.00 97.16  ? 982  LEU A O   1 
ATOM   7418  C  CB  . LEU A 1 982  ? 22.747  -33.319 -16.601 1.00 100.51 ? 982  LEU A CB  1 
ATOM   7419  C  CG  . LEU A 1 982  ? 21.233  -33.601 -16.676 1.00 98.88  ? 982  LEU A CG  1 
ATOM   7420  C  CD1 . LEU A 1 982  ? 20.534  -32.581 -17.595 1.00 97.22  ? 982  LEU A CD1 1 
ATOM   7421  C  CD2 . LEU A 1 982  ? 20.854  -35.042 -17.025 1.00 98.49  ? 982  LEU A CD2 1 
ATOM   7422  N  N   . LEU A 1 983  ? 25.436  -32.923 -18.191 1.00 163.88 ? 983  LEU A N   1 
ATOM   7423  C  CA  . LEU A 1 983  ? 26.724  -32.256 -18.349 1.00 165.79 ? 983  LEU A CA  1 
ATOM   7424  C  C   . LEU A 1 983  ? 26.663  -31.028 -17.511 1.00 173.58 ? 983  LEU A C   1 
ATOM   7425  O  O   . LEU A 1 983  ? 27.619  -30.266 -17.383 1.00 173.63 ? 983  LEU A O   1 
ATOM   7426  C  CB  . LEU A 1 983  ? 26.946  -31.847 -19.802 1.00 159.72 ? 983  LEU A CB  1 
ATOM   7427  C  CG  . LEU A 1 983  ? 27.617  -32.877 -20.723 1.00 158.59 ? 983  LEU A CG  1 
ATOM   7428  C  CD1 . LEU A 1 983  ? 27.458  -34.318 -20.229 1.00 158.80 ? 983  LEU A CD1 1 
ATOM   7429  C  CD2 . LEU A 1 983  ? 27.087  -32.752 -22.128 1.00 158.06 ? 983  LEU A CD2 1 
ATOM   7430  N  N   . VAL A 1 984  ? 25.497  -30.843 -16.934 1.00 119.34 ? 984  VAL A N   1 
ATOM   7431  C  CA  . VAL A 1 984  ? 25.227  -29.641 -16.210 1.00 122.30 ? 984  VAL A CA  1 
ATOM   7432  C  C   . VAL A 1 984  ? 24.673  -30.052 -14.839 1.00 136.21 ? 984  VAL A C   1 
ATOM   7433  O  O   . VAL A 1 984  ? 24.018  -29.272 -14.164 1.00 136.76 ? 984  VAL A O   1 
ATOM   7434  C  CB  . VAL A 1 984  ? 24.270  -28.769 -17.037 1.00 121.03 ? 984  VAL A CB  1 
ATOM   7435  C  CG1 . VAL A 1 984  ? 22.900  -29.419 -17.105 1.00 120.97 ? 984  VAL A CG1 1 
ATOM   7436  C  CG2 . VAL A 1 984  ? 24.237  -27.325 -16.521 1.00 120.23 ? 984  VAL A CG2 1 
ATOM   7437  N  N   . GLY A 1 985  ? 24.971  -31.289 -14.433 1.00 174.64 ? 985  GLY A N   1 
ATOM   7438  C  CA  . GLY A 1 985  ? 24.611  -31.811 -13.117 1.00 176.12 ? 985  GLY A CA  1 
ATOM   7439  C  C   . GLY A 1 985  ? 25.540  -31.501 -11.939 1.00 178.60 ? 985  GLY A C   1 
ATOM   7440  O  O   . GLY A 1 985  ? 25.099  -31.428 -10.793 1.00 185.11 ? 985  GLY A O   1 
ATOM   7441  N  N   . GLU A 1 986  ? 26.831  -31.344 -12.205 1.00 139.31 ? 986  GLU A N   1 
ATOM   7442  C  CA  . GLU A 1 986  ? 27.788  -30.930 -11.182 1.00 141.34 ? 986  GLU A CA  1 
ATOM   7443  C  C   . GLU A 1 986  ? 27.461  -29.515 -10.775 1.00 140.10 ? 986  GLU A C   1 
ATOM   7444  O  O   . GLU A 1 986  ? 27.376  -29.195 -9.604  1.00 145.90 ? 986  GLU A O   1 
ATOM   7445  C  CB  . GLU A 1 986  ? 29.213  -31.000 -11.738 1.00 142.25 ? 986  GLU A CB  1 
ATOM   7446  C  CG  . GLU A 1 986  ? 30.277  -31.495 -10.762 1.00 149.00 ? 986  GLU A CG  1 
ATOM   7447  C  CD  . GLU A 1 986  ? 29.788  -32.633 -9.864  1.00 154.76 ? 986  GLU A CD  1 
ATOM   7448  O  OE1 . GLU A 1 986  ? 30.602  -33.499 -9.456  1.00 156.97 ? 986  GLU A OE1 1 
ATOM   7449  O  OE2 . GLU A 1 986  ? 28.581  -32.657 -9.559  1.00 156.93 ? 986  GLU A OE2 1 
ATOM   7450  N  N   . ILE A 1 987  ? 27.260  -28.679 -11.782 1.00 132.45 ? 987  ILE A N   1 
ATOM   7451  C  CA  . ILE A 1 987  ? 26.816  -27.301 -11.619 1.00 130.77 ? 987  ILE A CA  1 
ATOM   7452  C  C   . ILE A 1 987  ? 25.385  -27.214 -11.050 1.00 134.83 ? 987  ILE A C   1 
ATOM   7453  O  O   . ILE A 1 987  ? 24.995  -26.169 -10.537 1.00 136.58 ? 987  ILE A O   1 
ATOM   7454  C  CB  . ILE A 1 987  ? 26.955  -26.505 -12.958 1.00 124.84 ? 987  ILE A CB  1 
ATOM   7455  C  CG1 . ILE A 1 987  ? 28.399  -26.567 -13.469 1.00 130.02 ? 987  ILE A CG1 1 
ATOM   7456  C  CG2 . ILE A 1 987  ? 26.525  -25.044 -12.813 1.00 119.50 ? 987  ILE A CG2 1 
ATOM   7457  C  CD1 . ILE A 1 987  ? 28.546  -26.162 -14.941 1.00 131.80 ? 987  ILE A CD1 1 
ATOM   7458  N  N   . LEU A 1 988  ? 24.606  -28.296 -11.127 1.00 106.85 ? 988  LEU A N   1 
ATOM   7459  C  CA  . LEU A 1 988  ? 23.304  -28.336 -10.443 1.00 109.38 ? 988  LEU A CA  1 
ATOM   7460  C  C   . LEU A 1 988  ? 23.467  -28.666 -8.948  1.00 116.17 ? 988  LEU A C   1 
ATOM   7461  O  O   . LEU A 1 988  ? 23.033  -27.893 -8.084  1.00 120.94 ? 988  LEU A O   1 
ATOM   7462  C  CB  . LEU A 1 988  ? 22.326  -29.320 -11.117 1.00 108.21 ? 988  LEU A CB  1 
ATOM   7463  C  CG  . LEU A 1 988  ? 21.198  -28.735 -11.974 1.00 104.98 ? 988  LEU A CG  1 
ATOM   7464  C  CD1 . LEU A 1 988  ? 20.184  -29.813 -12.360 1.00 105.52 ? 988  LEU A CD1 1 
ATOM   7465  C  CD2 . LEU A 1 988  ? 20.538  -27.594 -11.237 1.00 103.52 ? 988  LEU A CD2 1 
ATOM   7466  N  N   . SER A 1 989  ? 24.122  -29.794 -8.655  1.00 144.23 ? 989  SER A N   1 
ATOM   7467  C  CA  . SER A 1 989  ? 24.314  -30.272 -7.279  1.00 148.15 ? 989  SER A CA  1 
ATOM   7468  C  C   . SER A 1 989  ? 24.963  -29.210 -6.375  1.00 148.09 ? 989  SER A C   1 
ATOM   7469  O  O   . SER A 1 989  ? 24.499  -28.958 -5.259  1.00 150.16 ? 989  SER A O   1 
ATOM   7470  C  CB  . SER A 1 989  ? 25.122  -31.580 -7.279  1.00 152.56 ? 989  SER A CB  1 
ATOM   7471  O  OG  . SER A 1 989  ? 24.961  -32.312 -6.075  1.00 159.54 ? 989  SER A OG  1 
ATOM   7472  N  N   . ALA A 1 990  ? 26.025  -28.583 -6.870  1.00 183.72 ? 990  ALA A N   1 
ATOM   7473  C  CA  . ALA A 1 990  ? 26.666  -27.488 -6.157  1.00 187.04 ? 990  ALA A CA  1 
ATOM   7474  C  C   . ALA A 1 990  ? 25.619  -26.551 -5.536  1.00 187.62 ? 990  ALA A C   1 
ATOM   7475  O  O   . ALA A 1 990  ? 25.603  -26.347 -4.322  1.00 194.76 ? 990  ALA A O   1 
ATOM   7476  C  CB  . ALA A 1 990  ? 27.607  -26.726 -7.088  1.00 184.91 ? 990  ALA A CB  1 
ATOM   7477  N  N   . VAL A 1 991  ? 24.734  -26.008 -6.363  1.00 131.19 ? 991  VAL A N   1 
ATOM   7478  C  CA  . VAL A 1 991  ? 23.768  -25.012 -5.904  1.00 132.78 ? 991  VAL A CA  1 
ATOM   7479  C  C   . VAL A 1 991  ? 22.488  -25.576 -5.256  1.00 137.00 ? 991  VAL A C   1 
ATOM   7480  O  O   . VAL A 1 991  ? 21.687  -24.819 -4.717  1.00 139.85 ? 991  VAL A O   1 
ATOM   7481  C  CB  . VAL A 1 991  ? 23.460  -23.987 -7.048  1.00 104.68 ? 991  VAL A CB  1 
ATOM   7482  C  CG1 . VAL A 1 991  ? 22.070  -23.332 -6.930  1.00 103.88 ? 991  VAL A CG1 1 
ATOM   7483  C  CG2 . VAL A 1 991  ? 24.556  -22.943 -7.113  1.00 105.06 ? 991  VAL A CG2 1 
ATOM   7484  N  N   . LEU A 1 992  ? 22.296  -26.890 -5.261  1.00 131.03 ? 992  LEU A N   1 
ATOM   7485  C  CA  . LEU A 1 992  ? 21.092  -27.432 -4.621  1.00 138.79 ? 992  LEU A CA  1 
ATOM   7486  C  C   . LEU A 1 992  ? 21.337  -28.644 -3.744  1.00 158.63 ? 992  LEU A C   1 
ATOM   7487  O  O   . LEU A 1 992  ? 20.783  -29.725 -3.969  1.00 163.69 ? 992  LEU A O   1 
ATOM   7488  C  CB  . LEU A 1 992  ? 19.977  -27.720 -5.638  1.00 127.46 ? 992  LEU A CB  1 
ATOM   7489  C  CG  . LEU A 1 992  ? 19.430  -26.580 -6.528  1.00 118.29 ? 992  LEU A CG  1 
ATOM   7490  C  CD1 . LEU A 1 992  ? 18.608  -27.121 -7.707  1.00 112.05 ? 992  LEU A CD1 1 
ATOM   7491  C  CD2 . LEU A 1 992  ? 18.626  -25.470 -5.766  1.00 120.04 ? 992  LEU A CD2 1 
ATOM   7492  N  N   . SER A 1 993  ? 22.172  -28.442 -2.734  1.00 217.53 ? 993  SER A N   1 
ATOM   7493  C  CA  . SER A 1 993  ? 22.508  -29.487 -1.782  1.00 230.46 ? 993  SER A CA  1 
ATOM   7494  C  C   . SER A 1 993  ? 23.140  -28.826 -0.589  1.00 244.32 ? 993  SER A C   1 
ATOM   7495  O  O   . SER A 1 993  ? 23.025  -29.316 0.530   1.00 250.87 ? 993  SER A O   1 
ATOM   7496  C  CB  . SER A 1 993  ? 23.495  -30.471 -2.394  1.00 228.67 ? 993  SER A CB  1 
ATOM   7497  O  OG  . SER A 1 993  ? 22.919  -31.120 -3.515  1.00 224.17 ? 993  SER A OG  1 
ATOM   7498  N  N   . GLN A 1 994  ? 23.846  -27.730 -0.849  1.00 171.06 ? 994  GLN A N   1 
ATOM   7499  C  CA  . GLN A 1 994  ? 24.206  -26.791 0.201   1.00 182.94 ? 994  GLN A CA  1 
ATOM   7500  C  C   . GLN A 1 994  ? 23.246  -25.634 0.066   1.00 182.65 ? 994  GLN A C   1 
ATOM   7501  O  O   . GLN A 1 994  ? 22.575  -25.490 -0.954  1.00 175.31 ? 994  GLN A O   1 
ATOM   7502  C  CB  . GLN A 1 994  ? 25.657  -26.292 0.070   1.00 188.15 ? 994  GLN A CB  1 
ATOM   7503  C  CG  . GLN A 1 994  ? 25.933  -25.435 -1.171  1.00 186.63 ? 994  GLN A CG  1 
ATOM   7504  C  CD  . GLN A 1 994  ? 26.915  -24.291 -0.918  1.00 190.66 ? 994  GLN A CD  1 
ATOM   7505  O  OE1 . GLN A 1 994  ? 27.449  -24.132 0.182   1.00 197.02 ? 994  GLN A OE1 1 
ATOM   7506  N  NE2 . GLN A 1 994  ? 27.148  -23.488 -1.946  1.00 186.01 ? 994  GLN A NE2 1 
ATOM   7507  N  N   . GLU A 1 995  ? 23.154  -24.832 1.108   1.00 188.42 ? 995  GLU A N   1 
ATOM   7508  C  CA  . GLU A 1 995  ? 22.465  -23.580 0.984   1.00 192.42 ? 995  GLU A CA  1 
ATOM   7509  C  C   . GLU A 1 995  ? 23.545  -22.530 1.013   1.00 193.13 ? 995  GLU A C   1 
ATOM   7510  O  O   . GLU A 1 995  ? 24.731  -22.855 0.957   1.00 192.71 ? 995  GLU A O   1 
ATOM   7511  C  CB  . GLU A 1 995  ? 21.453  -23.400 2.111   1.00 201.27 ? 995  GLU A CB  1 
ATOM   7512  C  CG  . GLU A 1 995  ? 20.045  -23.897 1.766   1.00 203.42 ? 995  GLU A CG  1 
ATOM   7513  C  CD  . GLU A 1 995  ? 19.536  -25.000 2.693   1.00 209.59 ? 995  GLU A CD  1 
ATOM   7514  O  OE1 . GLU A 1 995  ? 20.327  -25.504 3.526   1.00 214.51 ? 995  GLU A OE1 1 
ATOM   7515  O  OE2 . GLU A 1 995  ? 18.338  -25.359 2.584   1.00 209.28 ? 995  GLU A OE2 1 
ATOM   7516  N  N   . GLY A 1 996  ? 23.136  -21.273 1.081   1.00 210.84 ? 996  GLY A N   1 
ATOM   7517  C  CA  . GLY A 1 996  ? 24.083  -20.183 1.146   1.00 213.95 ? 996  GLY A CA  1 
ATOM   7518  C  C   . GLY A 1 996  ? 25.012  -20.188 -0.046  1.00 211.56 ? 996  GLY A C   1 
ATOM   7519  O  O   . GLY A 1 996  ? 25.798  -21.122 -0.234  1.00 211.99 ? 996  GLY A O   1 
ATOM   7520  N  N   . ILE A 1 997  ? 24.926  -19.130 -0.846  1.00 254.01 ? 997  ILE A N   1 
ATOM   7521  C  CA  . ILE A 1 997  ? 25.777  -18.982 -2.018  1.00 250.61 ? 997  ILE A CA  1 
ATOM   7522  C  C   . ILE A 1 997  ? 27.229  -19.260 -1.612  1.00 256.76 ? 997  ILE A C   1 
ATOM   7523  O  O   . ILE A 1 997  ? 27.566  -19.205 -0.428  1.00 262.47 ? 997  ILE A O   1 
ATOM   7524  C  CB  . ILE A 1 997  ? 25.601  -17.585 -2.676  1.00 244.11 ? 997  ILE A CB  1 
ATOM   7525  C  CG1 . ILE A 1 997  ? 26.264  -16.493 -1.842  1.00 247.02 ? 997  ILE A CG1 1 
ATOM   7526  C  CG2 . ILE A 1 997  ? 24.117  -17.262 -2.867  1.00 242.38 ? 997  ILE A CG2 1 
ATOM   7527  C  CD1 . ILE A 1 997  ? 25.992  -15.096 -2.360  1.00 244.59 ? 997  ILE A CD1 1 
ATOM   7528  N  N   . ASN A 1 998  ? 28.085  -19.581 -2.576  1.00 227.37 ? 998  ASN A N   1 
ATOM   7529  C  CA  . ASN A 1 998  ? 29.402  -20.120 -2.244  1.00 231.01 ? 998  ASN A CA  1 
ATOM   7530  C  C   . ASN A 1 998  ? 30.371  -20.150 -3.434  1.00 221.57 ? 998  ASN A C   1 
ATOM   7531  O  O   . ASN A 1 998  ? 29.960  -20.448 -4.552  1.00 219.93 ? 998  ASN A O   1 
ATOM   7532  C  CB  . ASN A 1 998  ? 29.217  -21.517 -1.631  1.00 240.99 ? 998  ASN A CB  1 
ATOM   7533  C  CG  . ASN A 1 998  ? 30.343  -22.475 -1.972  1.00 247.77 ? 998  ASN A CG  1 
ATOM   7534  O  OD1 . ASN A 1 998  ? 31.512  -22.190 -1.729  1.00 252.74 ? 998  ASN A OD1 1 
ATOM   7535  N  ND2 . ASN A 1 998  ? 29.987  -23.637 -2.509  1.00 248.17 ? 998  ASN A ND2 1 
ATOM   7536  N  N   . ILE A 1 999  ? 31.648  -19.824 -3.191  1.00 226.16 ? 999  ILE A N   1 
ATOM   7537  C  CA  . ILE A 1 999  ? 32.696  -19.828 -4.234  1.00 214.05 ? 999  ILE A CA  1 
ATOM   7538  C  C   . ILE A 1 999  ? 33.091  -21.254 -4.601  1.00 204.81 ? 999  ILE A C   1 
ATOM   7539  O  O   . ILE A 1 999  ? 33.085  -22.148 -3.755  1.00 204.82 ? 999  ILE A O   1 
ATOM   7540  C  CB  . ILE A 1 999  ? 33.971  -19.062 -3.799  1.00 327.72 ? 999  ILE A CB  1 
ATOM   7541  C  CG1 . ILE A 1 999  ? 33.609  -17.666 -3.296  1.00 328.99 ? 999  ILE A CG1 1 
ATOM   7542  C  CG2 . ILE A 1 999  ? 34.969  -18.965 -4.954  1.00 324.33 ? 999  ILE A CG2 1 
ATOM   7543  C  CD1 . ILE A 1 999  ? 32.936  -16.817 -4.337  1.00 324.23 ? 999  ILE A CD1 1 
ATOM   7544  N  N   . LEU A 1 1000 ? 33.437  -21.483 -5.859  1.00 161.05 ? 1000 LEU A N   1 
ATOM   7545  C  CA  . LEU A 1 1000 ? 33.635  -22.862 -6.278  1.00 152.66 ? 1000 LEU A CA  1 
ATOM   7546  C  C   . LEU A 1 1000 ? 35.094  -23.269 -6.410  1.00 151.76 ? 1000 LEU A C   1 
ATOM   7547  O  O   . LEU A 1 1000 ? 35.444  -24.225 -7.097  1.00 150.54 ? 1000 LEU A O   1 
ATOM   7548  C  CB  . LEU A 1 1000 ? 32.786  -23.197 -7.508  1.00 140.63 ? 1000 LEU A CB  1 
ATOM   7549  C  CG  . LEU A 1 1000 ? 31.367  -23.626 -7.081  1.00 130.67 ? 1000 LEU A CG  1 
ATOM   7550  C  CD1 . LEU A 1 1000 ? 30.338  -23.503 -8.181  1.00 123.50 ? 1000 LEU A CD1 1 
ATOM   7551  C  CD2 . LEU A 1 1000 ? 31.368  -25.040 -6.522  1.00 130.83 ? 1000 LEU A CD2 1 
ATOM   7552  N  N   . THR A 1 1001 ? 35.946  -22.558 -5.700  1.00 192.90 ? 1001 THR A N   1 
ATOM   7553  C  CA  . THR A 1 1001 ? 37.321  -22.976 -5.616  1.00 194.51 ? 1001 THR A CA  1 
ATOM   7554  C  C   . THR A 1 1001 ? 37.791  -22.639 -4.235  1.00 203.98 ? 1001 THR A C   1 
ATOM   7555  O  O   . THR A 1 1001 ? 37.032  -22.109 -3.433  1.00 207.71 ? 1001 THR A O   1 
ATOM   7556  C  CB  . THR A 1 1001 ? 38.158  -22.213 -6.605  1.00 184.72 ? 1001 THR A CB  1 
ATOM   7557  O  OG1 . THR A 1 1001 ? 37.289  -21.652 -7.596  1.00 174.72 ? 1001 THR A OG1 1 
ATOM   7558  C  CG2 . THR A 1 1001 ? 39.172  -23.137 -7.247  1.00 184.57 ? 1001 THR A CG2 1 
ATOM   7559  N  N   . HIS A 1 1002 ? 39.042  -22.950 -3.945  1.00 167.48 ? 1002 HIS A N   1 
ATOM   7560  C  CA  . HIS A 1 1002 ? 39.608  -22.559 -2.676  1.00 176.66 ? 1002 HIS A CA  1 
ATOM   7561  C  C   . HIS A 1 1002 ? 40.118  -21.112 -2.736  1.00 151.10 ? 1002 HIS A C   1 
ATOM   7562  O  O   . HIS A 1 1002 ? 40.715  -20.610 -1.786  1.00 156.37 ? 1002 HIS A O   1 
ATOM   7563  C  CB  . HIS A 1 1002 ? 40.708  -23.540 -2.269  1.00 189.11 ? 1002 HIS A CB  1 
ATOM   7564  C  CG  . HIS A 1 1002 ? 40.201  -24.907 -1.909  1.00 198.33 ? 1002 HIS A CG  1 
ATOM   7565  N  ND1 . HIS A 1 1002 ? 39.948  -25.879 -2.849  1.00 198.24 ? 1002 HIS A ND1 1 
ATOM   7566  C  CD2 . HIS A 1 1002 ? 39.911  -25.464 -0.707  1.00 206.12 ? 1002 HIS A CD2 1 
ATOM   7567  C  CE1 . HIS A 1 1002 ? 39.517  -26.973 -2.247  1.00 201.97 ? 1002 HIS A CE1 1 
ATOM   7568  N  NE2 . HIS A 1 1002 ? 39.487  -26.749 -0.948  1.00 206.69 ? 1002 HIS A NE2 1 
ATOM   7569  N  N   . LEU A 1 1003 ? 39.863  -20.427 -3.844  1.00 174.24 ? 1003 LEU A N   1 
ATOM   7570  C  CA  . LEU A 1 1003 ? 40.340  -19.048 -3.986  1.00 168.88 ? 1003 LEU A CA  1 
ATOM   7571  C  C   . LEU A 1 1003 ? 39.790  -18.019 -2.979  1.00 173.14 ? 1003 LEU A C   1 
ATOM   7572  O  O   . LEU A 1 1003 ? 38.582  -17.891 -2.789  1.00 175.11 ? 1003 LEU A O   1 
ATOM   7573  C  CB  . LEU A 1 1003 ? 40.199  -18.574 -5.430  1.00 154.74 ? 1003 LEU A CB  1 
ATOM   7574  C  CG  . LEU A 1 1003 ? 41.308  -19.238 -6.229  1.00 147.18 ? 1003 LEU A CG  1 
ATOM   7575  C  CD1 . LEU A 1 1003 ? 41.984  -18.214 -7.079  1.00 140.21 ? 1003 LEU A CD1 1 
ATOM   7576  C  CD2 . LEU A 1 1003 ? 42.329  -19.896 -5.306  1.00 151.21 ? 1003 LEU A CD2 1 
ATOM   7577  N  N   . PRO A 1 1004 ? 40.708  -17.281 -2.350  1.00 167.09 ? 1004 PRO A N   1 
ATOM   7578  C  CA  . PRO A 1 1004 ? 40.649  -16.228 -1.340  1.00 167.64 ? 1004 PRO A CA  1 
ATOM   7579  C  C   . PRO A 1 1004 ? 39.680  -15.115 -1.678  1.00 162.73 ? 1004 PRO A C   1 
ATOM   7580  O  O   . PRO A 1 1004 ? 39.769  -14.534 -2.763  1.00 157.95 ? 1004 PRO A O   1 
ATOM   7581  C  CB  . PRO A 1 1004 ? 42.063  -15.651 -1.383  1.00 172.51 ? 1004 PRO A CB  1 
ATOM   7582  C  CG  . PRO A 1 1004 ? 42.686  -16.204 -2.636  1.00 167.38 ? 1004 PRO A CG  1 
ATOM   7583  C  CD  . PRO A 1 1004 ? 42.096  -17.541 -2.740  1.00 166.15 ? 1004 PRO A CD  1 
ATOM   7584  N  N   . LYS A 1 1005 ? 38.823  -14.779 -0.720  1.00 149.75 ? 1005 LYS A N   1 
ATOM   7585  C  CA  . LYS A 1 1005 ? 37.694  -13.878 -0.941  1.00 151.04 ? 1005 LYS A CA  1 
ATOM   7586  C  C   . LYS A 1 1005 ? 38.062  -12.415 -1.234  1.00 149.80 ? 1005 LYS A C   1 
ATOM   7587  O  O   . LYS A 1 1005 ? 37.182  -11.561 -1.455  1.00 145.26 ? 1005 LYS A O   1 
ATOM   7588  C  CB  . LYS A 1 1005 ? 36.758  -13.943 0.261   1.00 160.30 ? 1005 LYS A CB  1 
ATOM   7589  C  CG  . LYS A 1 1005 ? 36.030  -15.268 0.413   1.00 168.28 ? 1005 LYS A CG  1 
ATOM   7590  C  CD  . LYS A 1 1005 ? 34.868  -15.391 -0.583  1.00 169.39 ? 1005 LYS A CD  1 
ATOM   7591  C  CE  . LYS A 1 1005 ? 33.873  -14.223 -0.478  1.00 172.88 ? 1005 LYS A CE  1 
ATOM   7592  N  NZ  . LYS A 1 1005 ? 32.710  -14.384 -1.413  1.00 169.56 ? 1005 LYS A NZ  1 
ATOM   7593  N  N   . GLY A 1 1006 ? 39.362  -12.143 -1.268  1.00 169.30 ? 1006 GLY A N   1 
ATOM   7594  C  CA  . GLY A 1 1006 ? 39.878  -10.783 -1.278  1.00 172.10 ? 1006 GLY A CA  1 
ATOM   7595  C  C   . GLY A 1 1006 ? 39.229  -9.782  -2.215  1.00 163.42 ? 1006 GLY A C   1 
ATOM   7596  O  O   . GLY A 1 1006 ? 38.583  -8.823  -1.781  1.00 161.43 ? 1006 GLY A O   1 
ATOM   7597  N  N   . SER A 1 1007 ? 39.414  -10.011 -3.506  1.00 190.74 ? 1007 SER A N   1 
ATOM   7598  C  CA  . SER A 1 1007 ? 38.934  -9.100  -4.534  1.00 183.72 ? 1007 SER A CA  1 
ATOM   7599  C  C   . SER A 1 1007 ? 37.469  -8.773  -4.388  1.00 177.12 ? 1007 SER A C   1 
ATOM   7600  O  O   . SER A 1 1007 ? 36.795  -9.229  -3.462  1.00 175.77 ? 1007 SER A O   1 
ATOM   7601  C  CB  . SER A 1 1007 ? 39.153  -9.708  -5.924  1.00 181.57 ? 1007 SER A CB  1 
ATOM   7602  O  OG  . SER A 1 1007 ? 38.667  -8.851  -6.945  1.00 179.00 ? 1007 SER A OG  1 
ATOM   7603  N  N   . ALA A 1 1008 ? 37.000  -7.953  -5.318  1.00 146.24 ? 1008 ALA A N   1 
ATOM   7604  C  CA  . ALA A 1 1008 ? 35.588  -7.802  -5.583  1.00 144.40 ? 1008 ALA A CA  1 
ATOM   7605  C  C   . ALA A 1 1008 ? 35.182  -9.003  -6.414  1.00 139.36 ? 1008 ALA A C   1 
ATOM   7606  O  O   . ALA A 1 1008 ? 34.200  -9.687  -6.119  1.00 139.53 ? 1008 ALA A O   1 
ATOM   7607  C  CB  . ALA A 1 1008 ? 35.341  -6.516  -6.355  1.00 143.67 ? 1008 ALA A CB  1 
ATOM   7608  N  N   . GLU A 1 1009 ? 35.982  -9.255  -7.445  1.00 142.54 ? 1009 GLU A N   1 
ATOM   7609  C  CA  . GLU A 1 1009 ? 35.799  -10.382 -8.335  1.00 138.53 ? 1009 GLU A CA  1 
ATOM   7610  C  C   . GLU A 1 1009 ? 35.181  -11.520 -7.558  1.00 138.12 ? 1009 GLU A C   1 
ATOM   7611  O  O   . GLU A 1 1009 ? 34.071  -11.954 -7.849  1.00 136.56 ? 1009 GLU A O   1 
ATOM   7612  C  CB  . GLU A 1 1009 ? 37.162  -10.827 -8.887  1.00 136.84 ? 1009 GLU A CB  1 
ATOM   7613  C  CG  . GLU A 1 1009 ? 37.061  -11.751 -10.105 1.00 128.91 ? 1009 GLU A CG  1 
ATOM   7614  C  CD  . GLU A 1 1009 ? 38.386  -12.055 -10.754 1.00 126.47 ? 1009 GLU A CD  1 
ATOM   7615  O  OE1 . GLU A 1 1009 ? 39.419  -11.511 -10.309 1.00 127.51 ? 1009 GLU A OE1 1 
ATOM   7616  O  OE2 . GLU A 1 1009 ? 38.377  -12.842 -11.715 1.00 123.92 ? 1009 GLU A OE2 1 
ATOM   7617  N  N   . ALA A 1 1010 ? 35.908  -11.984 -6.552  1.00 178.61 ? 1010 ALA A N   1 
ATOM   7618  C  CA  . ALA A 1 1010 ? 35.485  -13.126 -5.764  1.00 183.40 ? 1010 ALA A CA  1 
ATOM   7619  C  C   . ALA A 1 1010 ? 34.071  -12.971 -5.218  1.00 181.18 ? 1010 ALA A C   1 
ATOM   7620  O  O   . ALA A 1 1010 ? 33.291  -13.920 -5.217  1.00 176.92 ? 1010 ALA A O   1 
ATOM   7621  C  CB  . ALA A 1 1010 ? 36.460  -13.352 -4.638  1.00 192.46 ? 1010 ALA A CB  1 
ATOM   7622  N  N   . GLU A 1 1011 ? 33.741  -11.776 -4.750  1.00 219.12 ? 1011 GLU A N   1 
ATOM   7623  C  CA  . GLU A 1 1011 ? 32.404  -11.522 -4.234  1.00 222.42 ? 1011 GLU A CA  1 
ATOM   7624  C  C   . GLU A 1 1011 ? 31.371  -11.603 -5.355  1.00 217.26 ? 1011 GLU A C   1 
ATOM   7625  O  O   . GLU A 1 1011 ? 30.173  -11.718 -5.080  1.00 218.02 ? 1011 GLU A O   1 
ATOM   7626  C  CB  . GLU A 1 1011 ? 32.336  -10.155 -3.546  1.00 227.48 ? 1011 GLU A CB  1 
ATOM   7627  C  CG  . GLU A 1 1011 ? 31.579  -10.128 -2.208  1.00 232.75 ? 1011 GLU A CG  1 
ATOM   7628  C  CD  . GLU A 1 1011 ? 32.300  -10.865 -1.087  1.00 239.16 ? 1011 GLU A CD  1 
ATOM   7629  O  OE1 . GLU A 1 1011 ? 33.488  -10.578 -0.829  1.00 242.69 ? 1011 GLU A OE1 1 
ATOM   7630  O  OE2 . GLU A 1 1011 ? 31.670  -11.733 -0.454  1.00 241.21 ? 1011 GLU A OE2 1 
ATOM   7631  N  N   . LEU A 1 1012 ? 31.830  -11.525 -6.610  1.00 117.54 ? 1012 LEU A N   1 
ATOM   7632  C  CA  . LEU A 1 1012 ? 30.961  -11.753 -7.783  1.00 108.66 ? 1012 LEU A CA  1 
ATOM   7633  C  C   . LEU A 1 1012 ? 30.898  -13.229 -8.142  1.00 110.37 ? 1012 LEU A C   1 
ATOM   7634  O  O   . LEU A 1 1012 ? 29.849  -13.737 -8.515  1.00 110.17 ? 1012 LEU A O   1 
ATOM   7635  C  CB  . LEU A 1 1012 ? 31.407  -10.907 -8.979  1.00 98.99  ? 1012 LEU A CB  1 
ATOM   7636  C  CG  . LEU A 1 1012 ? 30.901  -9.454  -8.931  1.00 96.12  ? 1012 LEU A CG  1 
ATOM   7637  C  CD1 . LEU A 1 1012 ? 31.812  -8.460  -9.643  1.00 93.25  ? 1012 LEU A CD1 1 
ATOM   7638  C  CD2 . LEU A 1 1012 ? 29.468  -9.371  -9.442  1.00 93.25  ? 1012 LEU A CD2 1 
ATOM   7639  N  N   . MET A 1 1013 ? 32.013  -13.929 -7.977  1.00 177.65 ? 1013 MET A N   1 
ATOM   7640  C  CA  . MET A 1 1013 ? 32.040  -15.354 -8.297  1.00 176.95 ? 1013 MET A CA  1 
ATOM   7641  C  C   . MET A 1 1013 ? 31.024  -16.151 -7.482  1.00 182.00 ? 1013 MET A C   1 
ATOM   7642  O  O   . MET A 1 1013 ? 30.854  -17.347 -7.701  1.00 183.29 ? 1013 MET A O   1 
ATOM   7643  C  CB  . MET A 1 1013 ? 33.439  -15.948 -8.125  1.00 177.78 ? 1013 MET A CB  1 
ATOM   7644  C  CG  . MET A 1 1013 ? 33.776  -16.935 -9.204  1.00 175.73 ? 1013 MET A CG  1 
ATOM   7645  S  SD  . MET A 1 1013 ? 33.560  -16.108 -10.789 1.00 191.68 ? 1013 MET A SD  1 
ATOM   7646  C  CE  . MET A 1 1013 ? 34.818  -14.825 -10.723 1.00 171.07 ? 1013 MET A CE  1 
ATOM   7647  N  N   . SER A 1 1014 ? 30.352  -15.476 -6.557  1.00 156.71 ? 1014 SER A N   1 
ATOM   7648  C  CA  . SER A 1 1014 ? 29.343  -16.093 -5.710  1.00 158.59 ? 1014 SER A CA  1 
ATOM   7649  C  C   . SER A 1 1014 ? 27.995  -16.155 -6.426  1.00 149.85 ? 1014 SER A C   1 
ATOM   7650  O  O   . SER A 1 1014 ? 27.239  -17.117 -6.246  1.00 147.20 ? 1014 SER A O   1 
ATOM   7651  C  CB  . SER A 1 1014 ? 29.185  -15.305 -4.391  1.00 169.11 ? 1014 SER A CB  1 
ATOM   7652  O  OG  . SER A 1 1014 ? 28.337  -14.168 -4.526  1.00 170.93 ? 1014 SER A OG  1 
ATOM   7653  N  N   . VAL A 1 1015 ? 27.701  -15.112 -7.215  1.00 129.18 ? 1015 VAL A N   1 
ATOM   7654  C  CA  . VAL A 1 1015 ? 26.410  -14.965 -7.906  1.00 127.66 ? 1015 VAL A CA  1 
ATOM   7655  C  C   . VAL A 1 1015 ? 26.295  -15.823 -9.166  1.00 124.78 ? 1015 VAL A C   1 
ATOM   7656  O  O   . VAL A 1 1015 ? 25.191  -16.190 -9.611  1.00 126.27 ? 1015 VAL A O   1 
ATOM   7657  C  CB  . VAL A 1 1015 ? 26.062  -13.475 -8.258  1.00 133.53 ? 1015 VAL A CB  1 
ATOM   7658  C  CG1 . VAL A 1 1015 ? 27.307  -12.597 -8.321  1.00 132.62 ? 1015 VAL A CG1 1 
ATOM   7659  C  CG2 . VAL A 1 1015 ? 25.237  -13.409 -9.564  1.00 131.00 ? 1015 VAL A CG2 1 
ATOM   7660  N  N   . VAL A 1 1016 ? 27.452  -16.151 -9.729  1.00 113.46 ? 1016 VAL A N   1 
ATOM   7661  C  CA  . VAL A 1 1016 ? 27.532  -17.034 -10.891 1.00 102.70 ? 1016 VAL A CA  1 
ATOM   7662  C  C   . VAL A 1 1016 ? 26.853  -18.392 -10.668 1.00 96.98  ? 1016 VAL A C   1 
ATOM   7663  O  O   . VAL A 1 1016 ? 25.714  -18.533 -11.067 1.00 91.37  ? 1016 VAL A O   1 
ATOM   7664  C  CB  . VAL A 1 1016 ? 28.983  -17.160 -11.406 1.00 99.92  ? 1016 VAL A CB  1 
ATOM   7665  C  CG1 . VAL A 1 1016 ? 29.157  -18.404 -12.256 1.00 96.89  ? 1016 VAL A CG1 1 
ATOM   7666  C  CG2 . VAL A 1 1016 ? 29.371  -15.924 -12.182 1.00 98.26  ? 1016 VAL A CG2 1 
ATOM   7667  N  N   . PRO A 1 1017 ? 27.518  -19.370 -10.000 1.00 102.75 ? 1017 PRO A N   1 
ATOM   7668  C  CA  . PRO A 1 1017 ? 26.915  -20.713 -10.008 1.00 104.25 ? 1017 PRO A CA  1 
ATOM   7669  C  C   . PRO A 1 1017 ? 25.399  -20.766 -9.867  1.00 105.71 ? 1017 PRO A C   1 
ATOM   7670  O  O   . PRO A 1 1017 ? 24.800  -21.624 -10.511 1.00 102.46 ? 1017 PRO A O   1 
ATOM   7671  C  CB  . PRO A 1 1017 ? 27.569  -21.401 -8.803  1.00 107.21 ? 1017 PRO A CB  1 
ATOM   7672  C  CG  . PRO A 1 1017 ? 28.891  -20.816 -8.767  1.00 107.81 ? 1017 PRO A CG  1 
ATOM   7673  C  CD  . PRO A 1 1017 ? 28.760  -19.368 -9.199  1.00 106.34 ? 1017 PRO A CD  1 
ATOM   7674  N  N   . VAL A 1 1018 ? 24.776  -19.900 -9.072  1.00 106.32 ? 1018 VAL A N   1 
ATOM   7675  C  CA  . VAL A 1 1018 ? 23.317  -19.913 -9.069  1.00 113.50 ? 1018 VAL A CA  1 
ATOM   7676  C  C   . VAL A 1 1018 ? 22.738  -19.349 -10.344 1.00 112.51 ? 1018 VAL A C   1 
ATOM   7677  O  O   . VAL A 1 1018 ? 21.976  -20.048 -11.000 1.00 110.43 ? 1018 VAL A O   1 
ATOM   7678  C  CB  . VAL A 1 1018 ? 22.724  -19.157 -7.948  1.00 121.56 ? 1018 VAL A CB  1 
ATOM   7679  C  CG1 . VAL A 1 1018 ? 21.234  -19.501 -7.877  1.00 123.80 ? 1018 VAL A CG1 1 
ATOM   7680  C  CG2 . VAL A 1 1018 ? 23.457  -19.543 -6.691  1.00 127.27 ? 1018 VAL A CG2 1 
ATOM   7681  N  N   . PHE A 1 1019 ? 23.101  -18.115 -10.723 1.00 154.01 ? 1019 PHE A N   1 
ATOM   7682  C  CA  . PHE A 1 1019 ? 22.532  -17.519 -11.955 1.00 149.76 ? 1019 PHE A CA  1 
ATOM   7683  C  C   . PHE A 1 1019 ? 22.415  -18.462 -13.167 1.00 143.40 ? 1019 PHE A C   1 
ATOM   7684  O  O   . PHE A 1 1019 ? 21.345  -18.586 -13.772 1.00 142.53 ? 1019 PHE A O   1 
ATOM   7685  C  CB  . PHE A 1 1019 ? 23.248  -16.243 -12.423 1.00 150.06 ? 1019 PHE A CB  1 
ATOM   7686  C  CG  . PHE A 1 1019 ? 22.957  -15.895 -13.885 1.00 144.95 ? 1019 PHE A CG  1 
ATOM   7687  C  CD1 . PHE A 1 1019 ? 21.713  -15.408 -14.269 1.00 142.60 ? 1019 PHE A CD1 1 
ATOM   7688  C  CD2 . PHE A 1 1019 ? 23.927  -16.079 -14.869 1.00 141.50 ? 1019 PHE A CD2 1 
ATOM   7689  C  CE1 . PHE A 1 1019 ? 21.458  -15.105 -15.590 1.00 139.49 ? 1019 PHE A CE1 1 
ATOM   7690  C  CE2 . PHE A 1 1019 ? 23.676  -15.774 -16.190 1.00 138.69 ? 1019 PHE A CE2 1 
ATOM   7691  C  CZ  . PHE A 1 1019 ? 22.449  -15.288 -16.549 1.00 138.44 ? 1019 PHE A CZ  1 
ATOM   7692  N  N   . TYR A 1 1020 ? 23.517  -19.097 -13.545 1.00 110.00 ? 1020 TYR A N   1 
ATOM   7693  C  CA  . TYR A 1 1020 ? 23.462  -20.053 -14.637 1.00 106.04 ? 1020 TYR A CA  1 
ATOM   7694  C  C   . TYR A 1 1020 ? 22.427  -21.127 -14.325 1.00 104.33 ? 1020 TYR A C   1 
ATOM   7695  O  O   . TYR A 1 1020 ? 21.536  -21.399 -15.132 1.00 103.25 ? 1020 TYR A O   1 
ATOM   7696  C  CB  . TYR A 1 1020 ? 24.840  -20.649 -14.910 1.00 107.39 ? 1020 TYR A CB  1 
ATOM   7697  C  CG  . TYR A 1 1020 ? 25.710  -19.618 -15.565 1.00 110.04 ? 1020 TYR A CG  1 
ATOM   7698  C  CD1 . TYR A 1 1020 ? 25.142  -18.480 -16.138 1.00 111.31 ? 1020 TYR A CD1 1 
ATOM   7699  C  CD2 . TYR A 1 1020 ? 27.076  -19.755 -15.607 1.00 113.89 ? 1020 TYR A CD2 1 
ATOM   7700  C  CE1 . TYR A 1 1020 ? 25.910  -17.512 -16.742 1.00 113.82 ? 1020 TYR A CE1 1 
ATOM   7701  C  CE2 . TYR A 1 1020 ? 27.864  -18.789 -16.210 1.00 115.94 ? 1020 TYR A CE2 1 
ATOM   7702  C  CZ  . TYR A 1 1020 ? 27.274  -17.663 -16.780 1.00 117.09 ? 1020 TYR A CZ  1 
ATOM   7703  O  OH  . TYR A 1 1020 ? 28.051  -16.688 -17.388 1.00 119.91 ? 1020 TYR A OH  1 
ATOM   7704  N  N   . VAL A 1 1021 ? 22.516  -21.700 -13.132 1.00 83.48  ? 1021 VAL A N   1 
ATOM   7705  C  CA  . VAL A 1 1021 ? 21.605  -22.752 -12.720 1.00 83.60  ? 1021 VAL A CA  1 
ATOM   7706  C  C   . VAL A 1 1021 ? 20.120  -22.305 -12.705 1.00 82.25  ? 1021 VAL A C   1 
ATOM   7707  O  O   . VAL A 1 1021 ? 19.213  -23.133 -12.691 1.00 80.56  ? 1021 VAL A O   1 
ATOM   7708  C  CB  . VAL A 1 1021 ? 22.117  -23.379 -11.407 1.00 77.33  ? 1021 VAL A CB  1 
ATOM   7709  C  CG1 . VAL A 1 1021 ? 21.101  -24.351 -10.795 1.00 87.49  ? 1021 VAL A CG1 1 
ATOM   7710  C  CG2 . VAL A 1 1021 ? 23.422  -24.064 -11.683 1.00 77.84  ? 1021 VAL A CG2 1 
ATOM   7711  N  N   . PHE A 1 1022 ? 19.861  -21.004 -12.748 1.00 116.28 ? 1022 PHE A N   1 
ATOM   7712  C  CA  . PHE A 1 1022 ? 18.479  -20.553 -12.743 1.00 120.99 ? 1022 PHE A CA  1 
ATOM   7713  C  C   . PHE A 1 1022 ? 18.108  -20.306 -14.178 1.00 121.02 ? 1022 PHE A C   1 
ATOM   7714  O  O   . PHE A 1 1022 ? 16.963  -20.476 -14.588 1.00 122.71 ? 1022 PHE A O   1 
ATOM   7715  C  CB  . PHE A 1 1022 ? 18.320  -19.272 -11.946 1.00 124.11 ? 1022 PHE A CB  1 
ATOM   7716  C  CG  . PHE A 1 1022 ? 16.933  -18.759 -11.935 1.00 124.02 ? 1022 PHE A CG  1 
ATOM   7717  C  CD1 . PHE A 1 1022 ? 15.991  -19.297 -11.069 1.00 125.69 ? 1022 PHE A CD1 1 
ATOM   7718  C  CD2 . PHE A 1 1022 ? 16.561  -17.759 -12.808 1.00 122.72 ? 1022 PHE A CD2 1 
ATOM   7719  C  CE1 . PHE A 1 1022 ? 14.702  -18.835 -11.060 1.00 127.60 ? 1022 PHE A CE1 1 
ATOM   7720  C  CE2 . PHE A 1 1022 ? 15.282  -17.292 -12.819 1.00 124.93 ? 1022 PHE A CE2 1 
ATOM   7721  C  CZ  . PHE A 1 1022 ? 14.339  -17.826 -11.940 1.00 127.18 ? 1022 PHE A CZ  1 
ATOM   7722  N  N   . HIS A 1 1023 ? 19.109  -19.901 -14.945 1.00 126.62 ? 1023 HIS A N   1 
ATOM   7723  C  CA  . HIS A 1 1023 ? 18.940  -19.638 -16.360 1.00 124.05 ? 1023 HIS A CA  1 
ATOM   7724  C  C   . HIS A 1 1023 ? 18.695  -20.945 -17.083 1.00 119.39 ? 1023 HIS A C   1 
ATOM   7725  O  O   . HIS A 1 1023 ? 17.863  -21.032 -17.988 1.00 119.45 ? 1023 HIS A O   1 
ATOM   7726  C  CB  . HIS A 1 1023 ? 20.194  -18.975 -16.878 1.00 124.23 ? 1023 HIS A CB  1 
ATOM   7727  C  CG  . HIS A 1 1023 ? 20.189  -18.749 -18.352 1.00 123.80 ? 1023 HIS A CG  1 
ATOM   7728  N  ND1 . HIS A 1 1023 ? 20.926  -19.517 -19.216 1.00 124.19 ? 1023 HIS A ND1 1 
ATOM   7729  C  CD2 . HIS A 1 1023 ? 19.550  -17.821 -19.102 1.00 123.88 ? 1023 HIS A CD2 1 
ATOM   7730  C  CE1 . HIS A 1 1023 ? 20.757  -19.062 -20.452 1.00 124.47 ? 1023 HIS A CE1 1 
ATOM   7731  N  NE2 . HIS A 1 1023 ? 19.927  -18.040 -20.406 1.00 124.85 ? 1023 HIS A NE2 1 
ATOM   7732  N  N   . TYR A 1 1024 ? 19.439  -21.957 -16.647 1.00 89.22  ? 1024 TYR A N   1 
ATOM   7733  C  CA  . TYR A 1 1024 ? 19.191  -23.349 -16.993 1.00 87.87  ? 1024 TYR A CA  1 
ATOM   7734  C  C   . TYR A 1 1024 ? 17.836  -23.862 -16.507 1.00 89.92  ? 1024 TYR A C   1 
ATOM   7735  O  O   . TYR A 1 1024 ? 17.016  -24.343 -17.276 1.00 88.90  ? 1024 TYR A O   1 
ATOM   7736  C  CB  . TYR A 1 1024 ? 20.267  -24.248 -16.398 1.00 90.43  ? 1024 TYR A CB  1 
ATOM   7737  C  CG  . TYR A 1 1024 ? 20.010  -25.689 -16.715 1.00 94.23  ? 1024 TYR A CG  1 
ATOM   7738  C  CD1 . TYR A 1 1024 ? 20.945  -26.427 -17.418 1.00 97.37  ? 1024 TYR A CD1 1 
ATOM   7739  C  CD2 . TYR A 1 1024 ? 18.801  -26.306 -16.349 1.00 96.82  ? 1024 TYR A CD2 1 
ATOM   7740  C  CE1 . TYR A 1 1024 ? 20.698  -27.743 -17.742 1.00 100.55 ? 1024 TYR A CE1 1 
ATOM   7741  C  CE2 . TYR A 1 1024 ? 18.542  -27.615 -16.666 1.00 99.91  ? 1024 TYR A CE2 1 
ATOM   7742  C  CZ  . TYR A 1 1024 ? 19.492  -28.342 -17.363 1.00 104.02 ? 1024 TYR A CZ  1 
ATOM   7743  O  OH  . TYR A 1 1024 ? 19.218  -29.665 -17.678 1.00 109.39 ? 1024 TYR A OH  1 
ATOM   7744  N  N   . LEU A 1 1025 ? 17.615  -23.822 -15.212 1.00 119.34 ? 1025 LEU A N   1 
ATOM   7745  C  CA  . LEU A 1 1025 ? 16.361  -24.339 -14.724 1.00 122.65 ? 1025 LEU A CA  1 
ATOM   7746  C  C   . LEU A 1 1025 ? 15.190  -23.664 -15.437 1.00 122.26 ? 1025 LEU A C   1 
ATOM   7747  O  O   . LEU A 1 1025 ? 14.233  -24.319 -15.810 1.00 120.53 ? 1025 LEU A O   1 
ATOM   7748  C  CB  . LEU A 1 1025 ? 16.256  -24.137 -13.217 1.00 125.65 ? 1025 LEU A CB  1 
ATOM   7749  C  CG  . LEU A 1 1025 ? 17.146  -25.039 -12.358 1.00 127.51 ? 1025 LEU A CG  1 
ATOM   7750  C  CD1 . LEU A 1 1025 ? 17.117  -24.623 -10.880 1.00 130.69 ? 1025 LEU A CD1 1 
ATOM   7751  C  CD2 . LEU A 1 1025 ? 16.742  -26.508 -12.535 1.00 127.35 ? 1025 LEU A CD2 1 
ATOM   7752  N  N   . GLU A 1 1026 ? 15.281  -22.352 -15.632 1.00 137.53 ? 1026 GLU A N   1 
ATOM   7753  C  CA  . GLU A 1 1026 ? 14.155  -21.539 -16.096 1.00 143.66 ? 1026 GLU A CA  1 
ATOM   7754  C  C   . GLU A 1 1026 ? 14.004  -21.536 -17.604 1.00 145.85 ? 1026 GLU A C   1 
ATOM   7755  O  O   . GLU A 1 1026 ? 12.980  -21.960 -18.163 1.00 149.43 ? 1026 GLU A O   1 
ATOM   7756  C  CB  . GLU A 1 1026 ? 14.342  -20.090 -15.631 1.00 147.31 ? 1026 GLU A CB  1 
ATOM   7757  C  CG  . GLU A 1 1026 ? 13.410  -19.080 -16.269 1.00 151.35 ? 1026 GLU A CG  1 
ATOM   7758  C  CD  . GLU A 1 1026 ? 11.972  -19.251 -15.831 1.00 156.12 ? 1026 GLU A CD  1 
ATOM   7759  O  OE1 . GLU A 1 1026 ? 11.691  -20.168 -15.033 1.00 157.89 ? 1026 GLU A OE1 1 
ATOM   7760  O  OE2 . GLU A 1 1026 ? 11.117  -18.461 -16.284 1.00 156.98 ? 1026 GLU A OE2 1 
ATOM   7761  N  N   . THR A 1 1027 ? 15.038  -21.022 -18.256 1.00 136.30 ? 1027 THR A N   1 
ATOM   7762  C  CA  . THR A 1 1027 ? 14.982  -20.789 -19.679 1.00 134.72 ? 1027 THR A CA  1 
ATOM   7763  C  C   . THR A 1 1027 ? 14.801  -22.110 -20.401 1.00 135.17 ? 1027 THR A C   1 
ATOM   7764  O  O   . THR A 1 1027 ? 14.037  -22.186 -21.352 1.00 136.77 ? 1027 THR A O   1 
ATOM   7765  C  CB  . THR A 1 1027 ? 16.216  -20.060 -20.162 1.00 132.10 ? 1027 THR A CB  1 
ATOM   7766  O  OG1 . THR A 1 1027 ? 15.858  -18.710 -20.468 1.00 133.62 ? 1027 THR A OG1 1 
ATOM   7767  C  CG2 . THR A 1 1027 ? 16.760  -20.736 -21.391 1.00 130.10 ? 1027 THR A CG2 1 
ATOM   7768  N  N   . GLY A 1 1028 ? 15.486  -23.147 -19.928 1.00 103.12 ? 1028 GLY A N   1 
ATOM   7769  C  CA  . GLY A 1 1028 ? 15.251  -24.499 -20.394 1.00 105.66 ? 1028 GLY A CA  1 
ATOM   7770  C  C   . GLY A 1 1028 ? 14.142  -25.197 -19.622 1.00 108.94 ? 1028 GLY A C   1 
ATOM   7771  O  O   . GLY A 1 1028 ? 14.162  -26.416 -19.447 1.00 107.70 ? 1028 GLY A O   1 
ATOM   7772  N  N   . ASN A 1 1029 ? 13.153  -24.426 -19.189 1.00 131.13 ? 1029 ASN A N   1 
ATOM   7773  C  CA  . ASN A 1 1029 ? 12.249  -24.887 -18.151 1.00 138.92 ? 1029 ASN A CA  1 
ATOM   7774  C  C   . ASN A 1 1029 ? 12.470  -26.360 -17.747 1.00 136.90 ? 1029 ASN A C   1 
ATOM   7775  O  O   . ASN A 1 1029 ? 12.186  -27.320 -18.483 1.00 134.56 ? 1029 ASN A O   1 
ATOM   7776  C  CB  . ASN A 1 1029 ? 10.799  -24.595 -18.493 1.00 148.81 ? 1029 ASN A CB  1 
ATOM   7777  C  CG  . ASN A 1 1029 ? 10.093  -25.803 -19.021 1.00 158.18 ? 1029 ASN A CG  1 
ATOM   7778  O  OD1 . ASN A 1 1029 ? 9.015   -26.163 -18.548 1.00 163.66 ? 1029 ASN A OD1 1 
ATOM   7779  N  ND2 . ASN A 1 1029 ? 10.713  -26.469 -19.990 1.00 159.00 ? 1029 ASN A ND2 1 
ATOM   7780  N  N   . HIS A 1 1030 ? 13.022  -26.498 -16.548 1.00 165.27 ? 1030 HIS A N   1 
ATOM   7781  C  CA  . HIS A 1 1030 ? 13.392  -27.779 -15.963 1.00 164.61 ? 1030 HIS A CA  1 
ATOM   7782  C  C   . HIS A 1 1030 ? 13.034  -27.775 -14.486 1.00 164.84 ? 1030 HIS A C   1 
ATOM   7783  O  O   . HIS A 1 1030 ? 13.447  -28.643 -13.712 1.00 164.36 ? 1030 HIS A O   1 
ATOM   7784  C  CB  . HIS A 1 1030 ? 14.888  -28.008 -16.108 1.00 161.04 ? 1030 HIS A CB  1 
ATOM   7785  C  CG  . HIS A 1 1030 ? 15.295  -28.413 -17.478 1.00 157.10 ? 1030 HIS A CG  1 
ATOM   7786  N  ND1 . HIS A 1 1030 ? 14.781  -29.533 -18.101 1.00 155.70 ? 1030 HIS A ND1 1 
ATOM   7787  C  CD2 . HIS A 1 1030 ? 16.158  -27.854 -18.353 1.00 154.85 ? 1030 HIS A CD2 1 
ATOM   7788  C  CE1 . HIS A 1 1030 ? 15.313  -29.640 -19.297 1.00 153.74 ? 1030 HIS A CE1 1 
ATOM   7789  N  NE2 . HIS A 1 1030 ? 16.152  -28.632 -19.478 1.00 152.73 ? 1030 HIS A NE2 1 
ATOM   7790  N  N   . TRP A 1 1031 ? 12.261  -26.776 -14.100 1.00 159.17 ? 1031 TRP A N   1 
ATOM   7791  C  CA  . TRP A 1 1031 ? 11.753  -26.726 -12.754 1.00 157.89 ? 1031 TRP A CA  1 
ATOM   7792  C  C   . TRP A 1 1031 ? 11.275  -28.112 -12.285 1.00 159.86 ? 1031 TRP A C   1 
ATOM   7793  O  O   . TRP A 1 1031 ? 11.357  -28.436 -11.099 1.00 165.13 ? 1031 TRP A O   1 
ATOM   7794  C  CB  . TRP A 1 1031 ? 10.652  -25.665 -12.660 1.00 156.57 ? 1031 TRP A CB  1 
ATOM   7795  C  CG  . TRP A 1 1031 ? 11.212  -24.279 -12.746 1.00 152.97 ? 1031 TRP A CG  1 
ATOM   7796  C  CD1 . TRP A 1 1031 ? 10.772  -23.262 -13.541 1.00 151.96 ? 1031 TRP A CD1 1 
ATOM   7797  C  CD2 . TRP A 1 1031 ? 12.345  -23.761 -12.023 1.00 152.83 ? 1031 TRP A CD2 1 
ATOM   7798  N  NE1 . TRP A 1 1031 ? 11.550  -22.144 -13.349 1.00 151.57 ? 1031 TRP A NE1 1 
ATOM   7799  C  CE2 . TRP A 1 1031 ? 12.520  -22.430 -12.418 1.00 153.08 ? 1031 TRP A CE2 1 
ATOM   7800  C  CE3 . TRP A 1 1031 ? 13.220  -24.306 -11.068 1.00 154.68 ? 1031 TRP A CE3 1 
ATOM   7801  C  CZ2 . TRP A 1 1031 ? 13.540  -21.624 -11.895 1.00 155.74 ? 1031 TRP A CZ2 1 
ATOM   7802  C  CZ3 . TRP A 1 1031 ? 14.228  -23.503 -10.557 1.00 157.09 ? 1031 TRP A CZ3 1 
ATOM   7803  C  CH2 . TRP A 1 1031 ? 14.381  -22.184 -10.970 1.00 157.49 ? 1031 TRP A CH2 1 
ATOM   7804  N  N   . ASN A 1 1032 ? 10.819  -28.944 -13.212 1.00 180.80 ? 1032 ASN A N   1 
ATOM   7805  C  CA  . ASN A 1 1032 ? 10.227  -30.224 -12.846 1.00 183.46 ? 1032 ASN A CA  1 
ATOM   7806  C  C   . ASN A 1 1032 ? 11.228  -31.269 -12.375 1.00 181.18 ? 1032 ASN A C   1 
ATOM   7807  O  O   . ASN A 1 1032 ? 10.846  -32.428 -12.156 1.00 181.47 ? 1032 ASN A O   1 
ATOM   7808  C  CB  . ASN A 1 1032 ? 9.541   -30.794 -14.048 1.00 185.05 ? 1032 ASN A CB  1 
ATOM   7809  C  CG  . ASN A 1 1032 ? 10.527  -31.171 -15.104 1.00 182.49 ? 1032 ASN A CG  1 
ATOM   7810  O  OD1 . ASN A 1 1032 ? 11.157  -30.311 -15.727 1.00 179.07 ? 1032 ASN A OD1 1 
ATOM   7811  N  ND2 . ASN A 1 1032 ? 10.710  -32.467 -15.291 1.00 183.45 ? 1032 ASN A ND2 1 
ATOM   7812  N  N   . ILE A 1 1033 ? 12.504  -30.890 -12.260 1.00 109.14 ? 1033 ILE A N   1 
ATOM   7813  C  CA  . ILE A 1 1033 ? 13.477  -31.770 -11.594 1.00 108.84 ? 1033 ILE A CA  1 
ATOM   7814  C  C   . ILE A 1 1033 ? 13.033  -32.125 -10.169 1.00 113.72 ? 1033 ILE A C   1 
ATOM   7815  O  O   . ILE A 1 1033 ? 13.375  -33.204 -9.666  1.00 115.43 ? 1033 ILE A O   1 
ATOM   7816  C  CB  . ILE A 1 1033 ? 14.894  -31.162 -11.349 1.00 105.94 ? 1033 ILE A CB  1 
ATOM   7817  C  CG1 . ILE A 1 1033 ? 15.310  -30.084 -12.325 1.00 103.03 ? 1033 ILE A CG1 1 
ATOM   7818  C  CG2 . ILE A 1 1033 ? 15.943  -32.262 -11.333 1.00 106.26 ? 1033 ILE A CG2 1 
ATOM   7819  C  CD1 . ILE A 1 1033 ? 16.830  -29.944 -12.318 1.00 102.42 ? 1033 ILE A CD1 1 
ATOM   7820  N  N   . PHE A 1 1034 ? 12.329  -31.189 -9.512  1.00 164.60 ? 1034 PHE A N   1 
ATOM   7821  C  CA  . PHE A 1 1034 ? 11.975  -31.276 -8.084  1.00 169.23 ? 1034 PHE A CA  1 
ATOM   7822  C  C   . PHE A 1 1034 ? 10.738  -32.106 -7.766  1.00 177.59 ? 1034 PHE A C   1 
ATOM   7823  O  O   . PHE A 1 1034 ? 9.692   -31.960 -8.407  1.00 178.12 ? 1034 PHE A O   1 
ATOM   7824  C  CB  . PHE A 1 1034 ? 11.773  -29.881 -7.507  1.00 165.03 ? 1034 PHE A CB  1 
ATOM   7825  C  CG  . PHE A 1 1034 ? 12.908  -28.958 -7.776  1.00 158.87 ? 1034 PHE A CG  1 
ATOM   7826  C  CD1 . PHE A 1 1034 ? 14.155  -29.207 -7.241  1.00 158.70 ? 1034 PHE A CD1 1 
ATOM   7827  C  CD2 . PHE A 1 1034 ? 12.736  -27.843 -8.565  1.00 153.72 ? 1034 PHE A CD2 1 
ATOM   7828  C  CE1 . PHE A 1 1034 ? 15.211  -28.360 -7.489  1.00 155.75 ? 1034 PHE A CE1 1 
ATOM   7829  C  CE2 . PHE A 1 1034 ? 13.789  -26.995 -8.817  1.00 149.88 ? 1034 PHE A CE2 1 
ATOM   7830  C  CZ  . PHE A 1 1034 ? 15.027  -27.252 -8.278  1.00 150.99 ? 1034 PHE A CZ  1 
ATOM   7831  N  N   . HIS A 1 1035 ? 10.864  -32.957 -6.750  1.00 164.58 ? 1035 HIS A N   1 
ATOM   7832  C  CA  . HIS A 1 1035 ? 9.738   -33.721 -6.237  1.00 177.19 ? 1035 HIS A CA  1 
ATOM   7833  C  C   . HIS A 1 1035 ? 8.951   -32.833 -5.283  1.00 184.22 ? 1035 HIS A C   1 
ATOM   7834  O  O   . HIS A 1 1035 ? 7.767   -33.055 -5.049  1.00 187.98 ? 1035 HIS A O   1 
ATOM   7835  C  CB  . HIS A 1 1035 ? 10.232  -34.960 -5.499  1.00 188.65 ? 1035 HIS A CB  1 
ATOM   7836  C  CG  . HIS A 1 1035 ? 11.345  -35.672 -6.195  1.00 194.16 ? 1035 HIS A CG  1 
ATOM   7837  N  ND1 . HIS A 1 1035 ? 11.192  -36.921 -6.760  1.00 196.44 ? 1035 HIS A ND1 1 
ATOM   7838  C  CD2 . HIS A 1 1035 ? 12.631  -35.313 -6.421  1.00 195.53 ? 1035 HIS A CD2 1 
ATOM   7839  C  CE1 . HIS A 1 1035 ? 12.334  -37.299 -7.300  1.00 195.77 ? 1035 HIS A CE1 1 
ATOM   7840  N  NE2 . HIS A 1 1035 ? 13.226  -36.340 -7.110  1.00 195.53 ? 1035 HIS A NE2 1 
ATOM   7841  N  N   . SER A 1 1036 ? 9.624   -31.817 -4.746  1.00 179.37 ? 1036 SER A N   1 
ATOM   7842  C  CA  . SER A 1 1036 ? 9.029   -30.874 -3.791  1.00 182.80 ? 1036 SER A CA  1 
ATOM   7843  C  C   . SER A 1 1036 ? 7.988   -29.970 -4.444  1.00 179.14 ? 1036 SER A C   1 
ATOM   7844  O  O   . SER A 1 1036 ? 7.478   -30.281 -5.514  1.00 174.87 ? 1036 SER A O   1 
ATOM   7845  C  CB  . SER A 1 1036 ? 10.121  -30.019 -3.134  1.00 186.18 ? 1036 SER A CB  1 
ATOM   7846  O  OG  . SER A 1 1036 ? 10.616  -29.031 -4.022  1.00 183.08 ? 1036 SER A OG  1 
ATOM   7847  N  N   . ASP A 1 1037 ? 7.642   -28.870 -3.783  1.00 220.82 ? 1037 ASP A N   1 
ATOM   7848  C  CA  . ASP A 1 1037 ? 6.992   -27.792 -4.500  1.00 215.93 ? 1037 ASP A CA  1 
ATOM   7849  C  C   . ASP A 1 1037 ? 8.092   -27.027 -5.172  1.00 204.99 ? 1037 ASP A C   1 
ATOM   7850  O  O   . ASP A 1 1037 ? 9.066   -26.633 -4.532  1.00 206.14 ? 1037 ASP A O   1 
ATOM   7851  C  CB  . ASP A 1 1037 ? 6.223   -26.844 -3.598  1.00 222.33 ? 1037 ASP A CB  1 
ATOM   7852  C  CG  . ASP A 1 1037 ? 5.626   -25.665 -4.374  1.00 219.32 ? 1037 ASP A CG  1 
ATOM   7853  O  OD1 . ASP A 1 1037 ? 6.117   -25.339 -5.484  1.00 211.97 ? 1037 ASP A OD1 1 
ATOM   7854  O  OD2 . ASP A 1 1037 ? 4.654   -25.062 -3.876  1.00 223.54 ? 1037 ASP A OD2 1 
ATOM   7855  N  N   . PRO A 1 1038 ? 7.937   -26.814 -6.475  1.00 160.60 ? 1038 PRO A N   1 
ATOM   7856  C  CA  . PRO A 1 1038 ? 8.966   -26.177 -7.293  1.00 154.06 ? 1038 PRO A CA  1 
ATOM   7857  C  C   . PRO A 1 1038 ? 8.915   -24.649 -7.206  1.00 152.67 ? 1038 PRO A C   1 
ATOM   7858  O  O   . PRO A 1 1038 ? 9.956   -23.982 -7.107  1.00 152.21 ? 1038 PRO A O   1 
ATOM   7859  C  CB  . PRO A 1 1038 ? 8.620   -26.663 -8.709  1.00 151.82 ? 1038 PRO A CB  1 
ATOM   7860  C  CG  . PRO A 1 1038 ? 7.629   -27.790 -8.519  1.00 155.97 ? 1038 PRO A CG  1 
ATOM   7861  C  CD  . PRO A 1 1038 ? 6.878   -27.409 -7.299  1.00 160.65 ? 1038 PRO A CD  1 
ATOM   7862  N  N   . LEU A 1 1039 ? 7.709   -24.099 -7.232  1.00 200.68 ? 1039 LEU A N   1 
ATOM   7863  C  CA  . LEU A 1 1039 ? 7.568   -22.659 -7.318  1.00 199.36 ? 1039 LEU A CA  1 
ATOM   7864  C  C   . LEU A 1 1039 ? 8.390   -22.008 -6.216  1.00 197.74 ? 1039 LEU A C   1 
ATOM   7865  O  O   . LEU A 1 1039 ? 9.067   -21.004 -6.433  1.00 194.96 ? 1039 LEU A O   1 
ATOM   7866  C  CB  . LEU A 1 1039 ? 6.098   -22.261 -7.225  1.00 202.97 ? 1039 LEU A CB  1 
ATOM   7867  C  CG  . LEU A 1 1039 ? 5.786   -20.863 -7.767  1.00 204.55 ? 1039 LEU A CG  1 
ATOM   7868  C  CD1 . LEU A 1 1039 ? 6.877   -20.376 -8.721  1.00 199.63 ? 1039 LEU A CD1 1 
ATOM   7869  C  CD2 . LEU A 1 1039 ? 4.425   -20.866 -8.445  1.00 207.30 ? 1039 LEU A CD2 1 
ATOM   7870  N  N   . ILE A 1 1040 ? 8.348   -22.623 -5.041  1.00 156.68 ? 1040 ILE A N   1 
ATOM   7871  C  CA  . ILE A 1 1040 ? 9.069   -22.133 -3.878  1.00 158.41 ? 1040 ILE A CA  1 
ATOM   7872  C  C   . ILE A 1 1040 ? 10.569  -22.355 -4.076  1.00 157.82 ? 1040 ILE A C   1 
ATOM   7873  O  O   . ILE A 1 1040 ? 11.383  -21.501 -3.736  1.00 159.39 ? 1040 ILE A O   1 
ATOM   7874  C  CB  . ILE A 1 1040 ? 8.547   -22.825 -2.573  1.00 160.93 ? 1040 ILE A CB  1 
ATOM   7875  C  CG1 . ILE A 1 1040 ? 8.498   -21.859 -1.370  1.00 167.93 ? 1040 ILE A CG1 1 
ATOM   7876  C  CG2 . ILE A 1 1040 ? 9.316   -24.108 -2.269  1.00 158.12 ? 1040 ILE A CG2 1 
ATOM   7877  C  CD1 . ILE A 1 1040 ? 9.069   -20.475 -1.629  1.00 186.12 ? 1040 ILE A CD1 1 
ATOM   7878  N  N   . GLU A 1 1041 ? 10.929  -23.497 -4.650  1.00 156.88 ? 1041 GLU A N   1 
ATOM   7879  C  CA  . GLU A 1 1041 ? 12.324  -23.796 -4.913  1.00 157.88 ? 1041 GLU A CA  1 
ATOM   7880  C  C   . GLU A 1 1041 ? 12.871  -22.647 -5.736  1.00 156.08 ? 1041 GLU A C   1 
ATOM   7881  O  O   . GLU A 1 1041 ? 14.039  -22.259 -5.607  1.00 153.33 ? 1041 GLU A O   1 
ATOM   7882  C  CB  . GLU A 1 1041 ? 12.447  -25.102 -5.688  1.00 158.90 ? 1041 GLU A CB  1 
ATOM   7883  C  CG  . GLU A 1 1041 ? 13.599  -25.978 -5.251  1.00 164.00 ? 1041 GLU A CG  1 
ATOM   7884  C  CD  . GLU A 1 1041 ? 13.259  -26.813 -4.033  1.00 175.25 ? 1041 GLU A CD  1 
ATOM   7885  O  OE1 . GLU A 1 1041 ? 12.061  -27.096 -3.831  1.00 177.95 ? 1041 GLU A OE1 1 
ATOM   7886  O  OE2 . GLU A 1 1041 ? 14.183  -27.188 -3.280  1.00 181.73 ? 1041 GLU A OE2 1 
ATOM   7887  N  N   . LYS A 1 1042 ? 11.993  -22.094 -6.571  1.00 164.74 ? 1042 LYS A N   1 
ATOM   7888  C  CA  . LYS A 1 1042 ? 12.337  -20.959 -7.424  1.00 167.29 ? 1042 LYS A CA  1 
ATOM   7889  C  C   . LYS A 1 1042 ? 12.763  -19.789 -6.562  1.00 175.62 ? 1042 LYS A C   1 
ATOM   7890  O  O   . LYS A 1 1042 ? 13.908  -19.322 -6.625  1.00 176.40 ? 1042 LYS A O   1 
ATOM   7891  C  CB  . LYS A 1 1042 ? 11.147  -20.527 -8.287  1.00 167.02 ? 1042 LYS A CB  1 
ATOM   7892  C  CG  . LYS A 1 1042 ? 11.400  -19.237 -9.064  1.00 169.40 ? 1042 LYS A CG  1 
ATOM   7893  C  CD  . LYS A 1 1042 ? 10.287  -18.937 -10.056 1.00 172.13 ? 1042 LYS A CD  1 
ATOM   7894  C  CE  . LYS A 1 1042 ? 10.735  -19.159 -11.497 1.00 168.34 ? 1042 LYS A CE  1 
ATOM   7895  N  NZ  . LYS A 1 1042 ? 9.628   -18.882 -12.456 1.00 168.63 ? 1042 LYS A NZ  1 
ATOM   7896  N  N   . GLN A 1 1043 ? 11.820  -19.324 -5.749  1.00 170.43 ? 1043 GLN A N   1 
ATOM   7897  C  CA  . GLN A 1 1043 ? 12.046  -18.183 -4.878  1.00 176.30 ? 1043 GLN A CA  1 
ATOM   7898  C  C   . GLN A 1 1043 ? 13.423  -18.253 -4.274  1.00 172.21 ? 1043 GLN A C   1 
ATOM   7899  O  O   . GLN A 1 1043 ? 14.229  -17.341 -4.454  1.00 171.66 ? 1043 GLN A O   1 
ATOM   7900  C  CB  . GLN A 1 1043 ? 10.992  -18.156 -3.771  1.00 186.75 ? 1043 GLN A CB  1 
ATOM   7901  C  CG  . GLN A 1 1043 ? 9.609   -18.014 -4.318  1.00 192.56 ? 1043 GLN A CG  1 
ATOM   7902  C  CD  . GLN A 1 1043 ? 9.606   -17.043 -5.475  1.00 193.18 ? 1043 GLN A CD  1 
ATOM   7903  O  OE1 . GLN A 1 1043 ? 10.299  -16.020 -5.432  1.00 194.06 ? 1043 GLN A OE1 1 
ATOM   7904  N  NE2 . GLN A 1 1043 ? 8.845   -17.359 -6.526  1.00 190.92 ? 1043 GLN A NE2 1 
ATOM   7905  N  N   . LYS A 1 1044 ? 13.680  -19.361 -3.575  1.00 155.62 ? 1044 LYS A N   1 
ATOM   7906  C  CA  . LYS A 1 1044 ? 14.920  -19.566 -2.819  1.00 154.81 ? 1044 LYS A CA  1 
ATOM   7907  C  C   . LYS A 1 1044 ? 16.143  -19.336 -3.702  1.00 150.11 ? 1044 LYS A C   1 
ATOM   7908  O  O   . LYS A 1 1044 ? 17.209  -18.910 -3.235  1.00 152.34 ? 1044 LYS A O   1 
ATOM   7909  C  CB  . LYS A 1 1044 ? 14.959  -20.966 -2.173  1.00 155.57 ? 1044 LYS A CB  1 
ATOM   7910  C  CG  . LYS A 1 1044 ? 14.168  -21.101 -0.869  1.00 195.30 ? 1044 LYS A CG  1 
ATOM   7911  C  CD  . LYS A 1 1044 ? 14.182  -22.529 -0.329  1.00 193.50 ? 1044 LYS A CD  1 
ATOM   7912  C  CE  . LYS A 1 1044 ? 15.553  -22.927 0.185   1.00 194.12 ? 1044 LYS A CE  1 
ATOM   7913  N  NZ  . LYS A 1 1044 ? 15.548  -24.331 0.662   1.00 193.95 ? 1044 LYS A NZ  1 
ATOM   7914  N  N   . LEU A 1 1045 ? 15.986  -19.617 -4.985  1.00 166.19 ? 1045 LEU A N   1 
ATOM   7915  C  CA  . LEU A 1 1045 ? 17.070  -19.384 -5.904  1.00 158.73 ? 1045 LEU A CA  1 
ATOM   7916  C  C   . LEU A 1 1045 ? 17.034  -17.914 -6.254  1.00 157.17 ? 1045 LEU A C   1 
ATOM   7917  O  O   . LEU A 1 1045 ? 18.066  -17.249 -6.306  1.00 156.00 ? 1045 LEU A O   1 
ATOM   7918  C  CB  . LEU A 1 1045 ? 16.912  -20.278 -7.121  1.00 151.24 ? 1045 LEU A CB  1 
ATOM   7919  C  CG  . LEU A 1 1045 ? 16.882  -21.763 -6.722  1.00 148.41 ? 1045 LEU A CG  1 
ATOM   7920  C  CD1 . LEU A 1 1045 ? 17.555  -22.577 -7.802  1.00 145.63 ? 1045 LEU A CD1 1 
ATOM   7921  C  CD2 . LEU A 1 1045 ? 17.551  -22.040 -5.383  1.00 148.60 ? 1045 LEU A CD2 1 
ATOM   7922  N  N   . LYS A 1 1046 ? 15.829  -17.397 -6.443  1.00 150.66 ? 1046 LYS A N   1 
ATOM   7923  C  CA  . LYS A 1 1046 ? 15.671  -15.984 -6.708  1.00 154.67 ? 1046 LYS A CA  1 
ATOM   7924  C  C   . LYS A 1 1046 ? 16.412  -15.194 -5.644  1.00 161.89 ? 1046 LYS A C   1 
ATOM   7925  O  O   . LYS A 1 1046 ? 17.349  -14.445 -5.926  1.00 162.81 ? 1046 LYS A O   1 
ATOM   7926  C  CB  . LYS A 1 1046 ? 14.191  -15.604 -6.741  1.00 157.10 ? 1046 LYS A CB  1 
ATOM   7927  C  CG  . LYS A 1 1046 ? 13.451  -16.028 -8.005  1.00 155.35 ? 1046 LYS A CG  1 
ATOM   7928  C  CD  . LYS A 1 1046 ? 12.266  -15.102 -8.208  1.00 160.46 ? 1046 LYS A CD  1 
ATOM   7929  C  CE  . LYS A 1 1046 ? 11.125  -15.713 -8.999  1.00 161.70 ? 1046 LYS A CE  1 
ATOM   7930  N  NZ  . LYS A 1 1046 ? 9.912   -14.825 -8.968  1.00 165.36 ? 1046 LYS A NZ  1 
ATOM   7931  N  N   . LYS A 1 1047 ? 15.985  -15.378 -4.409  1.00 122.85 ? 1047 LYS A N   1 
ATOM   7932  C  CA  . LYS A 1 1047 ? 16.704  -14.810 -3.285  1.00 127.52 ? 1047 LYS A CA  1 
ATOM   7933  C  C   . LYS A 1 1047 ? 18.189  -15.030 -3.502  1.00 119.52 ? 1047 LYS A C   1 
ATOM   7934  O  O   . LYS A 1 1047 ? 18.937  -14.072 -3.713  1.00 117.17 ? 1047 LYS A O   1 
ATOM   7935  C  CB  . LYS A 1 1047 ? 16.278  -15.484 -1.971  1.00 139.31 ? 1047 LYS A CB  1 
ATOM   7936  C  CG  . LYS A 1 1047 ? 16.711  -14.769 -0.677  1.00 152.58 ? 1047 LYS A CG  1 
ATOM   7937  C  CD  . LYS A 1 1047 ? 15.868  -15.210 0.527   1.00 165.70 ? 1047 LYS A CD  1 
ATOM   7938  C  CE  . LYS A 1 1047 ? 16.038  -14.241 1.668   1.00 176.99 ? 1047 LYS A CE  1 
ATOM   7939  N  NZ  . LYS A 1 1047 ? 17.461  -14.034 2.040   1.00 180.48 ? 1047 LYS A NZ  1 
ATOM   7940  N  N   . LYS A 1 1048 ? 18.604  -16.293 -3.461  1.00 129.73 ? 1048 LYS A N   1 
ATOM   7941  C  CA  . LYS A 1 1048 ? 20.018  -16.611 -3.424  1.00 123.62 ? 1048 LYS A CA  1 
ATOM   7942  C  C   . LYS A 1 1048 ? 20.773  -15.730 -4.371  1.00 116.65 ? 1048 LYS A C   1 
ATOM   7943  O  O   . LYS A 1 1048 ? 21.954  -15.459 -4.164  1.00 115.64 ? 1048 LYS A O   1 
ATOM   7944  C  CB  . LYS A 1 1048 ? 20.250  -18.065 -3.766  1.00 119.09 ? 1048 LYS A CB  1 
ATOM   7945  C  CG  . LYS A 1 1048 ? 20.241  -18.919 -2.566  1.00 122.17 ? 1048 LYS A CG  1 
ATOM   7946  C  CD  . LYS A 1 1048 ? 21.455  -19.755 -2.531  1.00 122.47 ? 1048 LYS A CD  1 
ATOM   7947  C  CE  . LYS A 1 1048 ? 21.031  -21.190 -2.400  1.00 123.59 ? 1048 LYS A CE  1 
ATOM   7948  N  NZ  . LYS A 1 1048 ? 22.227  -22.059 -2.310  1.00 123.96 ? 1048 LYS A NZ  1 
ATOM   7949  N  N   . LEU A 1 1049 ? 20.062  -15.296 -5.407  1.00 156.90 ? 1049 LEU A N   1 
ATOM   7950  C  CA  . LEU A 1 1049 ? 20.573  -14.380 -6.409  1.00 153.14 ? 1049 LEU A CA  1 
ATOM   7951  C  C   . LEU A 1 1049 ? 20.635  -12.936 -5.893  1.00 158.47 ? 1049 LEU A C   1 
ATOM   7952  O  O   . LEU A 1 1049 ? 21.716  -12.388 -5.684  1.00 160.94 ? 1049 LEU A O   1 
ATOM   7953  C  CB  . LEU A 1 1049 ? 19.738  -14.488 -7.701  1.00 144.61 ? 1049 LEU A CB  1 
ATOM   7954  C  CG  . LEU A 1 1049 ? 20.510  -14.668 -9.025  1.00 136.05 ? 1049 LEU A CG  1 
ATOM   7955  C  CD1 . LEU A 1 1049 ? 21.409  -15.907 -9.008  1.00 130.77 ? 1049 LEU A CD1 1 
ATOM   7956  C  CD2 . LEU A 1 1049 ? 19.607  -14.692 -10.260 1.00 132.93 ? 1049 LEU A CD2 1 
ATOM   7957  N  N   . LYS A 1 1050 ? 19.491  -12.316 -5.661  1.00 150.99 ? 1050 LYS A N   1 
ATOM   7958  C  CA  . LYS A 1 1050 ? 19.552  -10.948 -5.187  1.00 154.56 ? 1050 LYS A CA  1 
ATOM   7959  C  C   . LYS A 1 1050 ? 20.567  -10.805 -4.057  1.00 161.99 ? 1050 LYS A C   1 
ATOM   7960  O  O   . LYS A 1 1050 ? 21.475  -10.002 -4.154  1.00 161.07 ? 1050 LYS A O   1 
ATOM   7961  C  CB  . LYS A 1 1050 ? 18.189  -10.440 -4.739  1.00 155.79 ? 1050 LYS A CB  1 
ATOM   7962  C  CG  . LYS A 1 1050 ? 18.249  -9.028  -4.210  1.00 157.17 ? 1050 LYS A CG  1 
ATOM   7963  C  CD  . LYS A 1 1050 ? 16.960  -8.312  -4.483  1.00 158.86 ? 1050 LYS A CD  1 
ATOM   7964  C  CE  . LYS A 1 1050 ? 17.145  -6.816  -4.420  1.00 163.32 ? 1050 LYS A CE  1 
ATOM   7965  N  NZ  . LYS A 1 1050 ? 15.858  -6.165  -4.785  1.00 166.29 ? 1050 LYS A NZ  1 
ATOM   7966  N  N   . GLU A 1 1051 ? 20.445  -11.587 -2.993  1.00 199.34 ? 1051 GLU A N   1 
ATOM   7967  C  CA  . GLU A 1 1051 ? 21.330  -11.370 -1.848  1.00 211.33 ? 1051 GLU A CA  1 
ATOM   7968  C  C   . GLU A 1 1051 ? 22.811  -11.480 -2.225  1.00 208.99 ? 1051 GLU A C   1 
ATOM   7969  O  O   . GLU A 1 1051 ? 23.651  -10.729 -1.722  1.00 211.65 ? 1051 GLU A O   1 
ATOM   7970  C  CB  . GLU A 1 1051 ? 21.005  -12.335 -0.719  1.00 224.05 ? 1051 GLU A CB  1 
ATOM   7971  C  CG  . GLU A 1 1051 ? 21.537  -13.723 -0.963  1.00 230.97 ? 1051 GLU A CG  1 
ATOM   7972  C  CD  . GLU A 1 1051 ? 21.005  -14.714 0.032   1.00 241.06 ? 1051 GLU A CD  1 
ATOM   7973  O  OE1 . GLU A 1 1051 ? 19.956  -14.416 0.644   1.00 245.41 ? 1051 GLU A OE1 1 
ATOM   7974  O  OE2 . GLU A 1 1051 ? 21.635  -15.782 0.199   1.00 244.00 ? 1051 GLU A OE2 1 
ATOM   7975  N  N   . GLY A 1 1052 ? 23.127  -12.428 -3.099  1.00 156.24 ? 1052 GLY A N   1 
ATOM   7976  C  CA  . GLY A 1 1052 ? 24.479  -12.555 -3.595  1.00 156.14 ? 1052 GLY A CA  1 
ATOM   7977  C  C   . GLY A 1 1052 ? 24.807  -11.270 -4.313  1.00 153.05 ? 1052 GLY A C   1 
ATOM   7978  O  O   . GLY A 1 1052 ? 25.943  -10.809 -4.306  1.00 153.86 ? 1052 GLY A O   1 
ATOM   7979  N  N   . MET A 1 1053 ? 23.776  -10.688 -4.915  1.00 190.03 ? 1053 MET A N   1 
ATOM   7980  C  CA  . MET A 1 1053 ? 23.901  -9.488  -5.726  1.00 188.99 ? 1053 MET A CA  1 
ATOM   7981  C  C   . MET A 1 1053 ? 24.323  -8.304  -4.895  1.00 191.80 ? 1053 MET A C   1 
ATOM   7982  O  O   . MET A 1 1053 ? 25.059  -7.440  -5.357  1.00 190.87 ? 1053 MET A O   1 
ATOM   7983  C  CB  . MET A 1 1053 ? 22.564  -9.175  -6.403  1.00 190.78 ? 1053 MET A CB  1 
ATOM   7984  C  CG  . MET A 1 1053 ? 22.653  -8.114  -7.486  1.00 188.15 ? 1053 MET A CG  1 
ATOM   7985  S  SD  . MET A 1 1053 ? 24.295  -8.078  -8.245  1.00 295.03 ? 1053 MET A SD  1 
ATOM   7986  C  CE  . MET A 1 1053 ? 23.939  -8.411  -9.986  1.00 119.74 ? 1053 MET A CE  1 
ATOM   7987  N  N   . LEU A 1 1054 ? 23.829  -8.242  -3.670  1.00 138.59 ? 1054 LEU A N   1 
ATOM   7988  C  CA  . LEU A 1 1054 ? 24.157  -7.099  -2.844  1.00 142.88 ? 1054 LEU A CA  1 
ATOM   7989  C  C   . LEU A 1 1054 ? 25.579  -7.328  -2.377  1.00 141.54 ? 1054 LEU A C   1 
ATOM   7990  O  O   . LEU A 1 1054 ? 26.369  -6.395  -2.284  1.00 141.88 ? 1054 LEU A O   1 
ATOM   7991  C  CB  . LEU A 1 1054 ? 23.175  -6.933  -1.675  1.00 151.88 ? 1054 LEU A CB  1 
ATOM   7992  C  CG  . LEU A 1 1054 ? 21.658  -6.908  -1.970  1.00 155.40 ? 1054 LEU A CG  1 
ATOM   7993  C  CD1 . LEU A 1 1054 ? 20.853  -6.844  -0.674  1.00 161.60 ? 1054 LEU A CD1 1 
ATOM   7994  C  CD2 . LEU A 1 1054 ? 21.192  -5.797  -2.941  1.00 155.34 ? 1054 LEU A CD2 1 
ATOM   7995  N  N   . SER A 1 1055 ? 25.912  -8.595  -2.158  1.00 165.48 ? 1055 SER A N   1 
ATOM   7996  C  CA  . SER A 1 1055 ? 27.198  -8.965  -1.582  1.00 165.95 ? 1055 SER A CA  1 
ATOM   7997  C  C   . SER A 1 1055 ? 28.351  -8.098  -2.095  1.00 158.85 ? 1055 SER A C   1 
ATOM   7998  O  O   . SER A 1 1055 ? 29.393  -7.980  -1.448  1.00 163.10 ? 1055 SER A O   1 
ATOM   7999  C  CB  . SER A 1 1055 ? 27.503  -10.451 -1.826  1.00 169.95 ? 1055 SER A CB  1 
ATOM   8000  O  OG  . SER A 1 1055 ? 28.779  -10.797 -1.306  1.00 174.87 ? 1055 SER A OG  1 
ATOM   8001  N  N   . ILE A 1 1056 ? 28.142  -7.479  -3.249  1.00 173.33 ? 1056 ILE A N   1 
ATOM   8002  C  CA  . ILE A 1 1056 ? 29.170  -6.713  -3.933  1.00 171.20 ? 1056 ILE A CA  1 
ATOM   8003  C  C   . ILE A 1 1056 ? 29.065  -5.207  -3.682  1.00 170.72 ? 1056 ILE A C   1 
ATOM   8004  O  O   . ILE A 1 1056 ? 30.070  -4.505  -3.644  1.00 170.73 ? 1056 ILE A O   1 
ATOM   8005  C  CB  . ILE A 1 1056 ? 29.127  -7.040  -5.441  1.00 154.87 ? 1056 ILE A CB  1 
ATOM   8006  C  CG1 . ILE A 1 1056 ? 29.454  -5.813  -6.296  1.00 149.51 ? 1056 ILE A CG1 1 
ATOM   8007  C  CG2 . ILE A 1 1056 ? 27.758  -7.611  -5.803  1.00 150.54 ? 1056 ILE A CG2 1 
ATOM   8008  C  CD1 . ILE A 1 1056 ? 28.377  -5.475  -7.320  1.00 146.55 ? 1056 ILE A CD1 1 
ATOM   8009  N  N   . MET A 1 1057 ? 27.849  -4.723  -3.494  1.00 173.03 ? 1057 MET A N   1 
ATOM   8010  C  CA  . MET A 1 1057 ? 27.625  -3.297  -3.349  1.00 180.83 ? 1057 MET A CA  1 
ATOM   8011  C  C   . MET A 1 1057 ? 28.828  -2.619  -2.746  1.00 187.25 ? 1057 MET A C   1 
ATOM   8012  O  O   . MET A 1 1057 ? 29.309  -1.610  -3.239  1.00 186.49 ? 1057 MET A O   1 
ATOM   8013  C  CB  . MET A 1 1057 ? 26.416  -3.043  -2.459  1.00 189.79 ? 1057 MET A CB  1 
ATOM   8014  C  CG  . MET A 1 1057 ? 25.572  -1.893  -2.961  1.00 192.54 ? 1057 MET A CG  1 
ATOM   8015  S  SD  . MET A 1 1057 ? 25.109  -2.134  -4.704  1.00 220.44 ? 1057 MET A SD  1 
ATOM   8016  C  CE  . MET A 1 1057 ? 23.578  -3.059  -4.555  1.00 251.17 ? 1057 MET A CE  1 
ATOM   8017  N  N   . SER A 1 1058 ? 29.315  -3.214  -1.674  1.00 212.64 ? 1058 SER A N   1 
ATOM   8018  C  CA  . SER A 1 1058 ? 30.442  -2.695  -0.935  1.00 213.07 ? 1058 SER A CA  1 
ATOM   8019  C  C   . SER A 1 1058 ? 31.586  -2.253  -1.827  1.00 207.72 ? 1058 SER A C   1 
ATOM   8020  O  O   . SER A 1 1058 ? 32.292  -1.300  -1.508  1.00 208.90 ? 1058 SER A O   1 
ATOM   8021  C  CB  . SER A 1 1058 ? 30.923  -3.756  0.049   1.00 213.91 ? 1058 SER A CB  1 
ATOM   8022  O  OG  . SER A 1 1058 ? 29.848  -4.193  0.869   1.00 213.48 ? 1058 SER A OG  1 
ATOM   8023  N  N   . TYR A 1 1059 ? 31.771  -2.942  -2.942  1.00 154.79 ? 1059 TYR A N   1 
ATOM   8024  C  CA  . TYR A 1 1059 ? 32.887  -2.634  -3.823  1.00 152.53 ? 1059 TYR A CA  1 
ATOM   8025  C  C   . TYR A 1 1059 ? 32.483  -1.622  -4.867  1.00 155.63 ? 1059 TYR A C   1 
ATOM   8026  O  O   . TYR A 1 1059 ? 33.298  -1.193  -5.681  1.00 155.93 ? 1059 TYR A O   1 
ATOM   8027  C  CB  . TYR A 1 1059 ? 33.391  -3.884  -4.525  1.00 144.62 ? 1059 TYR A CB  1 
ATOM   8028  C  CG  . TYR A 1 1059 ? 33.826  -4.997  -3.601  1.00 144.65 ? 1059 TYR A CG  1 
ATOM   8029  C  CD1 . TYR A 1 1059 ? 32.918  -5.632  -2.753  1.00 147.88 ? 1059 TYR A CD1 1 
ATOM   8030  C  CD2 . TYR A 1 1059 ? 35.141  -5.441  -3.599  1.00 147.61 ? 1059 TYR A CD2 1 
ATOM   8031  C  CE1 . TYR A 1 1059 ? 33.324  -6.684  -1.912  1.00 154.30 ? 1059 TYR A CE1 1 
ATOM   8032  C  CE2 . TYR A 1 1059 ? 35.561  -6.486  -2.771  1.00 155.17 ? 1059 TYR A CE2 1 
ATOM   8033  C  CZ  . TYR A 1 1059 ? 34.657  -7.106  -1.930  1.00 158.26 ? 1059 TYR A CZ  1 
ATOM   8034  O  OH  . TYR A 1 1059 ? 35.111  -8.138  -1.121  1.00 162.06 ? 1059 TYR A OH  1 
ATOM   8035  N  N   . ARG A 1 1060 ? 31.213  -1.250  -4.853  1.00 172.91 ? 1060 ARG A N   1 
ATOM   8036  C  CA  . ARG A 1 1060 ? 30.737  -0.244  -5.781  1.00 174.87 ? 1060 ARG A CA  1 
ATOM   8037  C  C   . ARG A 1 1060 ? 31.153  1.148   -5.363  1.00 179.97 ? 1060 ARG A C   1 
ATOM   8038  O  O   . ARG A 1 1060 ? 30.742  1.609   -4.304  1.00 183.90 ? 1060 ARG A O   1 
ATOM   8039  C  CB  . ARG A 1 1060 ? 29.226  -0.249  -5.833  1.00 177.17 ? 1060 ARG A CB  1 
ATOM   8040  C  CG  . ARG A 1 1060 ? 28.709  0.999   -6.497  1.00 170.02 ? 1060 ARG A CG  1 
ATOM   8041  C  CD  . ARG A 1 1060 ? 27.386  0.754   -7.153  1.00 170.75 ? 1060 ARG A CD  1 
ATOM   8042  N  NE  . ARG A 1 1060 ? 26.500  1.881   -6.923  1.00 177.97 ? 1060 ARG A NE  1 
ATOM   8043  C  CZ  . ARG A 1 1060 ? 25.199  1.863   -7.188  1.00 181.06 ? 1060 ARG A CZ  1 
ATOM   8044  N  NH1 . ARG A 1 1060 ? 24.632  0.768   -7.696  1.00 181.63 ? 1060 ARG A NH1 1 
ATOM   8045  N  NH2 . ARG A 1 1060 ? 24.466  2.941   -6.940  1.00 182.76 ? 1060 ARG A NH2 1 
ATOM   8046  N  N   . ASN A 1 1061 ? 31.914  1.847   -6.198  1.00 135.93 ? 1061 ASN A N   1 
ATOM   8047  C  CA  . ASN A 1 1061 ? 32.248  3.231   -5.873  1.00 144.40 ? 1061 ASN A CA  1 
ATOM   8048  C  C   . ASN A 1 1061 ? 31.108  4.240   -6.029  1.00 147.72 ? 1061 ASN A C   1 
ATOM   8049  O  O   . ASN A 1 1061 ? 29.926  3.885   -6.071  1.00 146.32 ? 1061 ASN A O   1 
ATOM   8050  C  CB  . ASN A 1 1061 ? 33.512  3.715   -6.595  1.00 147.70 ? 1061 ASN A CB  1 
ATOM   8051  C  CG  . ASN A 1 1061 ? 34.784  3.404   -5.808  1.00 155.28 ? 1061 ASN A CG  1 
ATOM   8052  O  OD1 . ASN A 1 1061 ? 34.964  2.279   -5.348  1.00 157.07 ? 1061 ASN A OD1 1 
ATOM   8053  N  ND2 . ASN A 1 1061 ? 35.665  4.399   -5.645  1.00 159.61 ? 1061 ASN A ND2 1 
ATOM   8054  N  N   . ALA A 1 1062 ? 31.490  5.509   -6.092  1.00 188.85 ? 1062 ALA A N   1 
ATOM   8055  C  CA  . ALA A 1 1062 ? 30.545  6.609   -5.982  1.00 192.15 ? 1062 ALA A CA  1 
ATOM   8056  C  C   . ALA A 1 1062 ? 29.915  6.958   -7.313  1.00 188.69 ? 1062 ALA A C   1 
ATOM   8057  O  O   . ALA A 1 1062 ? 28.687  6.986   -7.447  1.00 190.37 ? 1062 ALA A O   1 
ATOM   8058  C  CB  . ALA A 1 1062 ? 31.246  7.831   -5.404  1.00 197.42 ? 1062 ALA A CB  1 
ATOM   8059  N  N   . ASP A 1 1063 ? 30.785  7.238   -8.283  1.00 230.79 ? 1063 ASP A N   1 
ATOM   8060  C  CA  . ASP A 1 1063 ? 30.412  7.618   -9.644  1.00 226.47 ? 1063 ASP A CA  1 
ATOM   8061  C  C   . ASP A 1 1063 ? 29.846  6.432   -10.400 1.00 217.94 ? 1063 ASP A C   1 
ATOM   8062  O  O   . ASP A 1 1063 ? 29.689  6.476   -11.612 1.00 214.04 ? 1063 ASP A O   1 
ATOM   8063  C  CB  . ASP A 1 1063 ? 31.645  8.114   -10.381 1.00 227.90 ? 1063 ASP A CB  1 
ATOM   8064  C  CG  . ASP A 1 1063 ? 32.769  7.102   -10.355 1.00 229.06 ? 1063 ASP A CG  1 
ATOM   8065  O  OD1 . ASP A 1 1063 ? 32.511  5.937   -9.980  1.00 228.69 ? 1063 ASP A OD1 1 
ATOM   8066  O  OD2 . ASP A 1 1063 ? 33.908  7.470   -10.708 1.00 230.83 ? 1063 ASP A OD2 1 
ATOM   8067  N  N   . TYR A 1 1064 ? 29.573  5.363   -9.667  1.00 171.56 ? 1064 TYR A N   1 
ATOM   8068  C  CA  . TYR A 1 1064 ? 28.947  4.176   -10.218 1.00 165.92 ? 1064 TYR A CA  1 
ATOM   8069  C  C   . TYR A 1 1064 ? 29.972  3.246   -10.825 1.00 163.74 ? 1064 TYR A C   1 
ATOM   8070  O  O   . TYR A 1 1064 ? 29.652  2.125   -11.205 1.00 164.93 ? 1064 TYR A O   1 
ATOM   8071  C  CB  . TYR A 1 1064 ? 27.828  4.552   -11.190 1.00 161.72 ? 1064 TYR A CB  1 
ATOM   8072  C  CG  . TYR A 1 1064 ? 26.722  5.299   -10.484 1.00 164.41 ? 1064 TYR A CG  1 
ATOM   8073  C  CD1 . TYR A 1 1064 ? 25.800  4.620   -9.694  1.00 164.72 ? 1064 TYR A CD1 1 
ATOM   8074  C  CD2 . TYR A 1 1064 ? 26.617  6.685   -10.564 1.00 167.24 ? 1064 TYR A CD2 1 
ATOM   8075  C  CE1 . TYR A 1 1064 ? 24.780  5.299   -9.013  1.00 169.38 ? 1064 TYR A CE1 1 
ATOM   8076  C  CE2 . TYR A 1 1064 ? 25.597  7.376   -9.887  1.00 172.14 ? 1064 TYR A CE2 1 
ATOM   8077  C  CZ  . TYR A 1 1064 ? 24.677  6.676   -9.111  1.00 172.40 ? 1064 TYR A CZ  1 
ATOM   8078  O  OH  . TYR A 1 1064 ? 23.656  7.337   -8.439  1.00 176.17 ? 1064 TYR A OH  1 
ATOM   8079  N  N   . SER A 1 1065 ? 31.216  3.697   -10.885 1.00 206.40 ? 1065 SER A N   1 
ATOM   8080  C  CA  . SER A 1 1065 ? 32.291  2.787   -11.208 1.00 201.82 ? 1065 SER A CA  1 
ATOM   8081  C  C   . SER A 1 1065 ? 32.420  1.794   -10.065 1.00 200.96 ? 1065 SER A C   1 
ATOM   8082  O  O   . SER A 1 1065 ? 32.372  2.164   -8.894  1.00 204.44 ? 1065 SER A O   1 
ATOM   8083  C  CB  . SER A 1 1065 ? 33.607  3.533   -11.331 1.00 203.74 ? 1065 SER A CB  1 
ATOM   8084  O  OG  . SER A 1 1065 ? 34.188  3.674   -10.045 1.00 209.08 ? 1065 SER A OG  1 
ATOM   8085  N  N   . TYR A 1 1066 ? 32.590  0.529   -10.413 1.00 137.78 ? 1066 TYR A N   1 
ATOM   8086  C  CA  . TYR A 1 1066 ? 32.863  -0.509  -9.437  1.00 139.35 ? 1066 TYR A CA  1 
ATOM   8087  C  C   . TYR A 1 1066 ? 34.363  -0.467  -9.081  1.00 141.75 ? 1066 TYR A C   1 
ATOM   8088  O  O   . TYR A 1 1066 ? 35.066  0.431   -9.548  1.00 142.63 ? 1066 TYR A O   1 
ATOM   8089  C  CB  . TYR A 1 1066 ? 32.359  -1.837  -10.002 1.00 134.14 ? 1066 TYR A CB  1 
ATOM   8090  C  CG  . TYR A 1 1066 ? 30.847  -1.835  -10.014 1.00 133.75 ? 1066 TYR A CG  1 
ATOM   8091  C  CD1 . TYR A 1 1066 ? 30.142  -0.704  -10.429 1.00 133.53 ? 1066 TYR A CD1 1 
ATOM   8092  C  CD2 . TYR A 1 1066 ? 30.118  -2.929  -9.568  1.00 134.65 ? 1066 TYR A CD2 1 
ATOM   8093  C  CE1 . TYR A 1 1066 ? 28.739  -0.664  -10.417 1.00 136.01 ? 1066 TYR A CE1 1 
ATOM   8094  C  CE2 . TYR A 1 1066 ? 28.704  -2.903  -9.551  1.00 136.67 ? 1066 TYR A CE2 1 
ATOM   8095  C  CZ  . TYR A 1 1066 ? 28.018  -1.767  -9.977  1.00 138.11 ? 1066 TYR A CZ  1 
ATOM   8096  O  OH  . TYR A 1 1066 ? 26.626  -1.735  -9.963  1.00 140.61 ? 1066 TYR A OH  1 
ATOM   8097  N  N   . SER A 1 1067 ? 34.854  -1.379  -8.238  1.00 147.20 ? 1067 SER A N   1 
ATOM   8098  C  CA  . SER A 1 1067 ? 36.296  -1.422  -7.927  1.00 149.00 ? 1067 SER A CA  1 
ATOM   8099  C  C   . SER A 1 1067 ? 36.788  -2.780  -7.412  1.00 150.72 ? 1067 SER A C   1 
ATOM   8100  O  O   . SER A 1 1067 ? 36.037  -3.548  -6.809  1.00 151.66 ? 1067 SER A O   1 
ATOM   8101  C  CB  . SER A 1 1067 ? 36.712  -0.301  -6.960  1.00 152.71 ? 1067 SER A CB  1 
ATOM   8102  O  OG  . SER A 1 1067 ? 38.127  -0.211  -6.864  1.00 154.24 ? 1067 SER A OG  1 
ATOM   8103  N  N   . VAL A 1 1068 ? 38.066  -3.051  -7.662  1.00 153.39 ? 1068 VAL A N   1 
ATOM   8104  C  CA  . VAL A 1 1068 ? 38.685  -4.343  -7.367  1.00 155.20 ? 1068 VAL A CA  1 
ATOM   8105  C  C   . VAL A 1 1068 ? 38.602  -4.810  -5.919  1.00 163.67 ? 1068 VAL A C   1 
ATOM   8106  O  O   . VAL A 1 1068 ? 37.940  -5.802  -5.639  1.00 164.67 ? 1068 VAL A O   1 
ATOM   8107  C  CB  . VAL A 1 1068 ? 40.159  -4.331  -7.705  1.00 155.02 ? 1068 VAL A CB  1 
ATOM   8108  C  CG1 . VAL A 1 1068 ? 40.868  -3.156  -6.972  1.00 161.23 ? 1068 VAL A CG1 1 
ATOM   8109  C  CG2 . VAL A 1 1068 ? 40.761  -5.676  -7.323  1.00 154.96 ? 1068 VAL A CG2 1 
ATOM   8110  N  N   . TRP A 1 1069 ? 39.357  -4.152  -5.029  1.00 150.93 ? 1069 TRP A N   1 
ATOM   8111  C  CA  . TRP A 1 1069 ? 39.209  -4.323  -3.572  1.00 156.48 ? 1069 TRP A CA  1 
ATOM   8112  C  C   . TRP A 1 1069 ? 38.728  -3.025  -2.919  1.00 159.77 ? 1069 TRP A C   1 
ATOM   8113  O  O   . TRP A 1 1069 ? 39.087  -1.923  -3.362  1.00 158.69 ? 1069 TRP A O   1 
ATOM   8114  C  CB  . TRP A 1 1069 ? 40.506  -4.715  -2.875  1.00 159.18 ? 1069 TRP A CB  1 
ATOM   8115  C  CG  . TRP A 1 1069 ? 41.360  -5.644  -3.605  1.00 154.47 ? 1069 TRP A CG  1 
ATOM   8116  C  CD1 . TRP A 1 1069 ? 41.282  -7.005  -3.606  1.00 152.58 ? 1069 TRP A CD1 1 
ATOM   8117  C  CD2 . TRP A 1 1069 ? 42.480  -5.295  -4.412  1.00 149.65 ? 1069 TRP A CD2 1 
ATOM   8118  N  NE1 . TRP A 1 1069 ? 42.281  -7.523  -4.376  1.00 149.79 ? 1069 TRP A NE1 1 
ATOM   8119  C  CE2 . TRP A 1 1069 ? 43.034  -6.498  -4.889  1.00 149.59 ? 1069 TRP A CE2 1 
ATOM   8120  C  CE3 . TRP A 1 1069 ? 43.065  -4.083  -4.783  1.00 147.11 ? 1069 TRP A CE3 1 
ATOM   8121  C  CZ2 . TRP A 1 1069 ? 44.155  -6.528  -5.726  1.00 150.09 ? 1069 TRP A CZ2 1 
ATOM   8122  C  CZ3 . TRP A 1 1069 ? 44.164  -4.105  -5.607  1.00 148.50 ? 1069 TRP A CZ3 1 
ATOM   8123  C  CH2 . TRP A 1 1069 ? 44.705  -5.322  -6.074  1.00 150.49 ? 1069 TRP A CH2 1 
ATOM   8124  N  N   . LYS A 1 1070 ? 37.966  -3.170  -1.834  1.00 145.38 ? 1070 LYS A N   1 
ATOM   8125  C  CA  . LYS A 1 1070 ? 37.163  -2.072  -1.311  1.00 145.55 ? 1070 LYS A CA  1 
ATOM   8126  C  C   . LYS A 1 1070 ? 37.858  -0.728  -1.403  1.00 148.48 ? 1070 LYS A C   1 
ATOM   8127  O  O   . LYS A 1 1070 ? 39.007  -0.577  -0.997  1.00 151.65 ? 1070 LYS A O   1 
ATOM   8128  C  CB  . LYS A 1 1070 ? 36.667  -2.356  0.108   1.00 147.09 ? 1070 LYS A CB  1 
ATOM   8129  C  CG  . LYS A 1 1070 ? 35.273  -2.959  0.125   1.00 144.06 ? 1070 LYS A CG  1 
ATOM   8130  C  CD  . LYS A 1 1070 ? 34.418  -2.464  1.269   1.00 148.60 ? 1070 LYS A CD  1 
ATOM   8131  C  CE  . LYS A 1 1070 ? 34.685  -3.253  2.520   1.00 152.67 ? 1070 LYS A CE  1 
ATOM   8132  N  NZ  . LYS A 1 1070 ? 33.583  -3.048  3.473   1.00 157.28 ? 1070 LYS A NZ  1 
ATOM   8133  N  N   . GLY A 1 1071 ? 37.150  0.235   -1.982  1.00 166.96 ? 1071 GLY A N   1 
ATOM   8134  C  CA  . GLY A 1 1071 ? 37.623  1.604   -2.068  1.00 172.32 ? 1071 GLY A CA  1 
ATOM   8135  C  C   . GLY A 1 1071 ? 38.731  1.859   -3.067  1.00 172.93 ? 1071 GLY A C   1 
ATOM   8136  O  O   . GLY A 1 1071 ? 38.949  3.009   -3.465  1.00 177.71 ? 1071 GLY A O   1 
ATOM   8137  N  N   . GLY A 1 1072 ? 39.429  0.792   -3.459  1.00 353.41 ? 1072 GLY A N   1 
ATOM   8138  C  CA  . GLY A 1 1072 ? 40.514  0.878   -4.422  1.00 352.15 ? 1072 GLY A CA  1 
ATOM   8139  C  C   . GLY A 1 1072 ? 40.117  1.767   -5.582  1.00 349.78 ? 1072 GLY A C   1 
ATOM   8140  O  O   . GLY A 1 1072 ? 38.926  1.968   -5.832  1.00 348.05 ? 1072 GLY A O   1 
ATOM   8141  N  N   . SER A 1 1073 ? 41.107  2.319   -6.278  1.00 205.76 ? 1073 SER A N   1 
ATOM   8142  C  CA  . SER A 1 1073 ? 40.831  3.176   -7.417  1.00 202.60 ? 1073 SER A CA  1 
ATOM   8143  C  C   . SER A 1 1073 ? 39.969  2.359   -8.335  1.00 195.04 ? 1073 SER A C   1 
ATOM   8144  O  O   . SER A 1 1073 ? 40.273  1.198   -8.592  1.00 191.61 ? 1073 SER A O   1 
ATOM   8145  C  CB  . SER A 1 1073 ? 42.127  3.558   -8.123  1.00 203.82 ? 1073 SER A CB  1 
ATOM   8146  O  OG  . SER A 1 1073 ? 42.938  2.415   -8.344  1.00 204.75 ? 1073 SER A OG  1 
ATOM   8147  N  N   . ALA A 1 1074 ? 38.883  2.948   -8.814  1.00 189.50 ? 1074 ALA A N   1 
ATOM   8148  C  CA  . ALA A 1 1074 ? 37.968  2.229   -9.690  1.00 183.58 ? 1074 ALA A CA  1 
ATOM   8149  C  C   . ALA A 1 1074 ? 38.698  1.501   -10.840 1.00 178.38 ? 1074 ALA A C   1 
ATOM   8150  O  O   . ALA A 1 1074 ? 39.470  2.100   -11.592 1.00 179.24 ? 1074 ALA A O   1 
ATOM   8151  C  CB  . ALA A 1 1074 ? 36.918  3.180   -10.229 1.00 184.63 ? 1074 ALA A CB  1 
ATOM   8152  N  N   . SER A 1 1075 ? 38.472  0.198   -10.961 1.00 207.16 ? 1075 SER A N   1 
ATOM   8153  C  CA  . SER A 1 1075 ? 39.106  -0.578  -12.016 1.00 202.88 ? 1075 SER A CA  1 
ATOM   8154  C  C   . SER A 1 1075 ? 38.157  -0.677  -13.188 1.00 198.75 ? 1075 SER A C   1 
ATOM   8155  O  O   . SER A 1 1075 ? 37.016  -1.109  -13.025 1.00 195.78 ? 1075 SER A O   1 
ATOM   8156  C  CB  . SER A 1 1075 ? 39.427  -1.982  -11.522 1.00 203.94 ? 1075 SER A CB  1 
ATOM   8157  O  OG  . SER A 1 1075 ? 38.238  -2.699  -11.236 1.00 203.02 ? 1075 SER A OG  1 
ATOM   8158  N  N   . THR A 1 1076 ? 38.626  -0.299  -14.370 1.00 162.44 ? 1076 THR A N   1 
ATOM   8159  C  CA  . THR A 1 1076 ? 37.772  -0.307  -15.552 1.00 156.01 ? 1076 THR A CA  1 
ATOM   8160  C  C   . THR A 1 1076 ? 37.349  -1.758  -15.930 1.00 151.96 ? 1076 THR A C   1 
ATOM   8161  O  O   . THR A 1 1076 ? 36.169  -2.034  -16.196 1.00 150.38 ? 1076 THR A O   1 
ATOM   8162  C  CB  . THR A 1 1076 ? 38.471  0.471   -16.698 1.00 152.76 ? 1076 THR A CB  1 
ATOM   8163  O  OG1 . THR A 1 1076 ? 37.499  1.102   -17.544 1.00 153.12 ? 1076 THR A OG1 1 
ATOM   8164  C  CG2 . THR A 1 1076 ? 39.381  -0.432  -17.490 1.00 148.60 ? 1076 THR A CG2 1 
ATOM   8165  N  N   . TRP A 1 1077 ? 38.331  -2.662  -15.903 1.00 160.23 ? 1077 TRP A N   1 
ATOM   8166  C  CA  . TRP A 1 1077 ? 38.194  -4.121  -16.045 1.00 158.14 ? 1077 TRP A CA  1 
ATOM   8167  C  C   . TRP A 1 1077 ? 37.046  -4.761  -15.245 1.00 153.59 ? 1077 TRP A C   1 
ATOM   8168  O  O   . TRP A 1 1077 ? 36.172  -5.418  -15.805 1.00 147.61 ? 1077 TRP A O   1 
ATOM   8169  C  CB  . TRP A 1 1077 ? 39.516  -4.732  -15.569 1.00 162.24 ? 1077 TRP A CB  1 
ATOM   8170  C  CG  . TRP A 1 1077 ? 39.718  -6.188  -15.774 1.00 164.75 ? 1077 TRP A CG  1 
ATOM   8171  C  CD1 . TRP A 1 1077 ? 40.332  -6.765  -16.832 1.00 165.49 ? 1077 TRP A CD1 1 
ATOM   8172  C  CD2 . TRP A 1 1077 ? 39.369  -7.261  -14.878 1.00 167.95 ? 1077 TRP A CD2 1 
ATOM   8173  N  NE1 . TRP A 1 1077 ? 40.370  -8.125  -16.675 1.00 166.81 ? 1077 TRP A NE1 1 
ATOM   8174  C  CE2 . TRP A 1 1077 ? 39.786  -8.456  -15.482 1.00 168.06 ? 1077 TRP A CE2 1 
ATOM   8175  C  CE3 . TRP A 1 1077 ? 38.732  -7.327  -13.636 1.00 170.88 ? 1077 TRP A CE3 1 
ATOM   8176  C  CZ2 . TRP A 1 1077 ? 39.591  -9.706  -14.885 1.00 167.74 ? 1077 TRP A CZ2 1 
ATOM   8177  C  CZ3 . TRP A 1 1077 ? 38.539  -8.575  -13.046 1.00 172.09 ? 1077 TRP A CZ3 1 
ATOM   8178  C  CH2 . TRP A 1 1077 ? 38.967  -9.739  -13.668 1.00 169.38 ? 1077 TRP A CH2 1 
ATOM   8179  N  N   . LEU A 1 1078 ? 37.076  -4.592  -13.926 1.00 163.20 ? 1078 LEU A N   1 
ATOM   8180  C  CA  . LEU A 1 1078 ? 36.038  -5.134  -13.058 1.00 161.96 ? 1078 LEU A CA  1 
ATOM   8181  C  C   . LEU A 1 1078 ? 34.795  -4.263  -13.121 1.00 163.31 ? 1078 LEU A C   1 
ATOM   8182  O  O   . LEU A 1 1078 ? 33.707  -4.712  -12.777 1.00 164.42 ? 1078 LEU A O   1 
ATOM   8183  C  CB  . LEU A 1 1078 ? 36.536  -5.271  -11.610 1.00 161.32 ? 1078 LEU A CB  1 
ATOM   8184  C  CG  . LEU A 1 1078 ? 35.662  -6.147  -10.702 1.00 156.69 ? 1078 LEU A CG  1 
ATOM   8185  C  CD1 . LEU A 1 1078 ? 36.446  -6.775  -9.564  1.00 156.39 ? 1078 LEU A CD1 1 
ATOM   8186  C  CD2 . LEU A 1 1078 ? 34.504  -5.340  -10.163 1.00 157.65 ? 1078 LEU A CD2 1 
ATOM   8187  N  N   . THR A 1 1079 ? 34.950  -3.022  -13.572 1.00 202.37 ? 1079 THR A N   1 
ATOM   8188  C  CA  . THR A 1 1079 ? 33.803  -2.138  -13.732 1.00 202.54 ? 1079 THR A CA  1 
ATOM   8189  C  C   . THR A 1 1079 ? 32.885  -2.762  -14.736 1.00 198.06 ? 1079 THR A C   1 
ATOM   8190  O  O   . THR A 1 1079 ? 31.658  -2.632  -14.659 1.00 198.48 ? 1079 THR A O   1 
ATOM   8191  C  CB  . THR A 1 1079 ? 34.211  -0.771  -14.259 1.00 213.78 ? 1079 THR A CB  1 
ATOM   8192  O  OG1 . THR A 1 1079 ? 34.833  -0.022  -13.207 1.00 217.55 ? 1079 THR A OG1 1 
ATOM   8193  C  CG2 . THR A 1 1079 ? 32.984  -0.013  -14.765 1.00 211.85 ? 1079 THR A CG2 1 
ATOM   8194  N  N   . ALA A 1 1080 ? 33.497  -3.430  -15.701 1.00 106.69 ? 1080 ALA A N   1 
ATOM   8195  C  CA  . ALA A 1 1080 ? 32.728  -4.247  -16.623 1.00 100.76 ? 1080 ALA A CA  1 
ATOM   8196  C  C   . ALA A 1 1080 ? 32.398  -5.608  -16.029 1.00 98.53  ? 1080 ALA A C   1 
ATOM   8197  O  O   . ALA A 1 1080 ? 31.234  -5.973  -15.948 1.00 96.61  ? 1080 ALA A O   1 
ATOM   8198  C  CB  . ALA A 1 1080 ? 33.459  -4.430  -17.931 1.00 99.06  ? 1080 ALA A CB  1 
ATOM   8199  N  N   . PHE A 1 1081 ? 33.406  -6.383  -15.637 1.00 135.60 ? 1081 PHE A N   1 
ATOM   8200  C  CA  . PHE A 1 1081 ? 33.105  -7.752  -15.244 1.00 133.18 ? 1081 PHE A CA  1 
ATOM   8201  C  C   . PHE A 1 1081 ? 31.832  -7.824  -14.422 1.00 130.73 ? 1081 PHE A C   1 
ATOM   8202  O  O   . PHE A 1 1081 ? 31.049  -8.756  -14.575 1.00 126.05 ? 1081 PHE A O   1 
ATOM   8203  C  CB  . PHE A 1 1081 ? 34.238  -8.402  -14.479 1.00 137.78 ? 1081 PHE A CB  1 
ATOM   8204  C  CG  . PHE A 1 1081 ? 33.965  -9.843  -14.112 1.00 140.58 ? 1081 PHE A CG  1 
ATOM   8205  C  CD1 . PHE A 1 1081 ? 34.588  -10.872 -14.796 1.00 139.71 ? 1081 PHE A CD1 1 
ATOM   8206  C  CD2 . PHE A 1 1081 ? 33.090  -10.177 -13.091 1.00 146.15 ? 1081 PHE A CD2 1 
ATOM   8207  C  CE1 . PHE A 1 1081 ? 34.352  -12.210 -14.468 1.00 140.81 ? 1081 PHE A CE1 1 
ATOM   8208  C  CE2 . PHE A 1 1081 ? 32.854  -11.514 -12.761 1.00 147.47 ? 1081 PHE A CE2 1 
ATOM   8209  C  CZ  . PHE A 1 1081 ? 33.486  -12.528 -13.452 1.00 144.59 ? 1081 PHE A CZ  1 
ATOM   8210  N  N   . ALA A 1 1082 ? 31.624  -6.854  -13.537 1.00 205.40 ? 1082 ALA A N   1 
ATOM   8211  C  CA  . ALA A 1 1082 ? 30.330  -6.754  -12.862 1.00 207.55 ? 1082 ALA A CA  1 
ATOM   8212  C  C   . ALA A 1 1082 ? 29.255  -6.416  -13.897 1.00 204.63 ? 1082 ALA A C   1 
ATOM   8213  O  O   . ALA A 1 1082 ? 28.235  -7.101  -13.984 1.00 203.89 ? 1082 ALA A O   1 
ATOM   8214  C  CB  . ALA A 1 1082 ? 30.355  -5.722  -11.742 1.00 212.67 ? 1082 ALA A CB  1 
ATOM   8215  N  N   . LEU A 1 1083 ? 29.485  -5.367  -14.688 1.00 97.53  ? 1083 LEU A N   1 
ATOM   8216  C  CA  . LEU A 1 1083 ? 28.536  -4.997  -15.721 1.00 93.18  ? 1083 LEU A CA  1 
ATOM   8217  C  C   . LEU A 1 1083 ? 28.080  -6.280  -16.319 1.00 91.97  ? 1083 LEU A C   1 
ATOM   8218  O  O   . LEU A 1 1083 ? 26.906  -6.611  -16.261 1.00 93.70  ? 1083 LEU A O   1 
ATOM   8219  C  CB  . LEU A 1 1083 ? 29.210  -4.137  -16.768 1.00 88.70  ? 1083 LEU A CB  1 
ATOM   8220  C  CG  . LEU A 1 1083 ? 29.122  -2.659  -16.410 1.00 88.64  ? 1083 LEU A CG  1 
ATOM   8221  C  CD1 . LEU A 1 1083 ? 30.133  -1.828  -17.171 1.00 88.90  ? 1083 LEU A CD1 1 
ATOM   8222  C  CD2 . LEU A 1 1083 ? 27.709  -2.161  -16.671 1.00 86.44  ? 1083 LEU A CD2 1 
ATOM   8223  N  N   . ARG A 1 1084 ? 29.037  -7.025  -16.847 1.00 123.36 ? 1084 ARG A N   1 
ATOM   8224  C  CA  . ARG A 1 1084 ? 28.754  -8.343  -17.379 1.00 123.01 ? 1084 ARG A CA  1 
ATOM   8225  C  C   . ARG A 1 1084 ? 27.803  -9.171  -16.468 1.00 126.37 ? 1084 ARG A C   1 
ATOM   8226  O  O   . ARG A 1 1084 ? 26.640  -9.400  -16.827 1.00 126.14 ? 1084 ARG A O   1 
ATOM   8227  C  CB  . ARG A 1 1084 ? 30.062  -9.086  -17.741 1.00 124.28 ? 1084 ARG A CB  1 
ATOM   8228  C  CG  . ARG A 1 1084 ? 29.968  -10.604 -17.708 1.00 120.68 ? 1084 ARG A CG  1 
ATOM   8229  C  CD  . ARG A 1 1084 ? 30.262  -11.289 -19.022 1.00 121.06 ? 1084 ARG A CD  1 
ATOM   8230  N  NE  . ARG A 1 1084 ? 30.126  -12.735 -18.859 1.00 125.87 ? 1084 ARG A NE  1 
ATOM   8231  C  CZ  . ARG A 1 1084 ? 31.132  -13.601 -18.904 1.00 132.87 ? 1084 ARG A CZ  1 
ATOM   8232  N  NH1 . ARG A 1 1084 ? 32.369  -13.185 -19.154 1.00 137.31 ? 1084 ARG A NH1 1 
ATOM   8233  N  NH2 . ARG A 1 1084 ? 30.889  -14.892 -18.722 1.00 133.12 ? 1084 ARG A NH2 1 
ATOM   8234  N  N   . VAL A 1 1085 ? 28.244  -9.601  -15.289 1.00 126.89 ? 1085 VAL A N   1 
ATOM   8235  C  CA  . VAL A 1 1085 ? 27.386  -10.512 -14.520 1.00 130.74 ? 1085 VAL A CA  1 
ATOM   8236  C  C   . VAL A 1 1085 ? 26.161  -9.795  -13.937 1.00 131.96 ? 1085 VAL A C   1 
ATOM   8237  O  O   . VAL A 1 1085 ? 25.217  -10.430 -13.472 1.00 131.04 ? 1085 VAL A O   1 
ATOM   8238  C  CB  . VAL A 1 1085 ? 28.160  -11.317 -13.447 1.00 123.18 ? 1085 VAL A CB  1 
ATOM   8239  C  CG1 . VAL A 1 1085 ? 27.376  -12.573 -13.041 1.00 122.53 ? 1085 VAL A CG1 1 
ATOM   8240  C  CG2 . VAL A 1 1085 ? 29.546  -11.708 -13.962 1.00 119.98 ? 1085 VAL A CG2 1 
ATOM   8241  N  N   . LEU A 1 1086 ? 26.187  -8.468  -13.979 1.00 184.48 ? 1086 LEU A N   1 
ATOM   8242  C  CA  . LEU A 1 1086 ? 25.049  -7.651  -13.579 1.00 190.15 ? 1086 LEU A CA  1 
ATOM   8243  C  C   . LEU A 1 1086 ? 23.901  -7.733  -14.570 1.00 188.02 ? 1086 LEU A C   1 
ATOM   8244  O  O   . LEU A 1 1086 ? 22.734  -7.868  -14.174 1.00 190.18 ? 1086 LEU A O   1 
ATOM   8245  C  CB  . LEU A 1 1086 ? 25.476  -6.196  -13.465 1.00 195.11 ? 1086 LEU A CB  1 
ATOM   8246  C  CG  . LEU A 1 1086 ? 25.777  -5.740  -12.050 1.00 205.82 ? 1086 LEU A CG  1 
ATOM   8247  C  CD1 . LEU A 1 1086 ? 24.499  -5.644  -11.239 1.00 206.52 ? 1086 LEU A CD1 1 
ATOM   8248  C  CD2 . LEU A 1 1086 ? 26.755  -6.699  -11.414 1.00 207.52 ? 1086 LEU A CD2 1 
ATOM   8249  N  N   . GLY A 1 1087 ? 24.243  -7.616  -15.857 1.00 141.76 ? 1087 GLY A N   1 
ATOM   8250  C  CA  . GLY A 1 1087 ? 23.274  -7.656  -16.954 1.00 137.94 ? 1087 GLY A CA  1 
ATOM   8251  C  C   . GLY A 1 1087 ? 22.763  -9.054  -17.263 1.00 134.31 ? 1087 GLY A C   1 
ATOM   8252  O  O   . GLY A 1 1087 ? 21.690  -9.226  -17.865 1.00 135.85 ? 1087 GLY A O   1 
ATOM   8253  N  N   . GLN A 1 1088 ? 23.551  -10.048 -16.849 1.00 115.42 ? 1088 GLN A N   1 
ATOM   8254  C  CA  . GLN A 1 1088 ? 23.196  -11.449 -17.006 1.00 116.22 ? 1088 GLN A CA  1 
ATOM   8255  C  C   . GLN A 1 1088 ? 22.087  -11.784 -16.014 1.00 122.56 ? 1088 GLN A C   1 
ATOM   8256  O  O   . GLN A 1 1088 ? 21.017  -12.289 -16.367 1.00 122.72 ? 1088 GLN A O   1 
ATOM   8257  C  CB  . GLN A 1 1088 ? 24.413  -12.345 -16.744 1.00 115.12 ? 1088 GLN A CB  1 
ATOM   8258  C  CG  . GLN A 1 1088 ? 25.568  -12.170 -17.731 1.00 115.61 ? 1088 GLN A CG  1 
ATOM   8259  C  CD  . GLN A 1 1088 ? 26.610  -13.309 -17.677 1.00 116.38 ? 1088 GLN A CD  1 
ATOM   8260  O  OE1 . GLN A 1 1088 ? 27.814  -13.094 -17.893 1.00 115.26 ? 1088 GLN A OE1 1 
ATOM   8261  N  NE2 . GLN A 1 1088 ? 26.139  -14.525 -17.399 1.00 116.27 ? 1088 GLN A NE2 1 
ATOM   8262  N  N   . VAL A 1 1089 ? 22.343  -11.466 -14.758 1.00 165.42 ? 1089 VAL A N   1 
ATOM   8263  C  CA  . VAL A 1 1089 ? 21.361  -11.689 -13.718 1.00 168.13 ? 1089 VAL A CA  1 
ATOM   8264  C  C   . VAL A 1 1089 ? 20.175  -10.720 -13.838 1.00 171.30 ? 1089 VAL A C   1 
ATOM   8265  O  O   . VAL A 1 1089 ? 19.185  -10.857 -13.140 1.00 171.73 ? 1089 VAL A O   1 
ATOM   8266  C  CB  . VAL A 1 1089 ? 22.027  -11.604 -12.352 1.00 163.73 ? 1089 VAL A CB  1 
ATOM   8267  C  CG1 . VAL A 1 1089 ? 21.102  -12.116 -11.299 1.00 164.27 ? 1089 VAL A CG1 1 
ATOM   8268  C  CG2 . VAL A 1 1089 ? 23.307  -12.433 -12.366 1.00 163.40 ? 1089 VAL A CG2 1 
ATOM   8269  N  N   . ASN A 1 1090 ? 20.264  -9.747  -14.732 1.00 123.07 ? 1090 ASN A N   1 
ATOM   8270  C  CA  . ASN A 1 1090 ? 19.142  -8.865  -14.938 1.00 128.89 ? 1090 ASN A CA  1 
ATOM   8271  C  C   . ASN A 1 1090 ? 17.972  -9.646  -15.495 1.00 130.44 ? 1090 ASN A C   1 
ATOM   8272  O  O   . ASN A 1 1090 ? 16.829  -9.213  -15.438 1.00 132.07 ? 1090 ASN A O   1 
ATOM   8273  C  CB  . ASN A 1 1090 ? 19.505  -7.755  -15.903 1.00 130.52 ? 1090 ASN A CB  1 
ATOM   8274  C  CG  . ASN A 1 1090 ? 18.381  -6.763  -16.087 1.00 134.40 ? 1090 ASN A CG  1 
ATOM   8275  O  OD1 . ASN A 1 1090 ? 17.207  -7.122  -16.218 1.00 134.21 ? 1090 ASN A OD1 1 
ATOM   8276  N  ND2 . ASN A 1 1090 ? 18.734  -5.499  -16.096 1.00 138.46 ? 1090 ASN A ND2 1 
ATOM   8277  N  N   . LYS A 1 1091 ? 18.266  -10.809 -16.048 1.00 125.66 ? 1091 LYS A N   1 
ATOM   8278  C  CA  . LYS A 1 1091 ? 17.250  -11.592 -16.734 1.00 127.48 ? 1091 LYS A CA  1 
ATOM   8279  C  C   . LYS A 1 1091 ? 16.102  -11.933 -15.824 1.00 125.51 ? 1091 LYS A C   1 
ATOM   8280  O  O   . LYS A 1 1091 ? 14.952  -11.956 -16.246 1.00 127.14 ? 1091 LYS A O   1 
ATOM   8281  C  CB  . LYS A 1 1091 ? 17.842  -12.890 -17.292 1.00 133.72 ? 1091 LYS A CB  1 
ATOM   8282  C  CG  . LYS A 1 1091 ? 18.378  -12.803 -18.729 1.00 139.45 ? 1091 LYS A CG  1 
ATOM   8283  C  CD  . LYS A 1 1091 ? 18.171  -14.124 -19.462 1.00 144.19 ? 1091 LYS A CD  1 
ATOM   8284  C  CE  . LYS A 1 1091 ? 16.686  -14.465 -19.459 1.00 150.30 ? 1091 LYS A CE  1 
ATOM   8285  N  NZ  . LYS A 1 1091 ? 16.319  -15.565 -20.392 1.00 151.41 ? 1091 LYS A NZ  1 
ATOM   8286  N  N   . TYR A 1 1092 ? 16.421  -12.198 -14.567 1.00 141.56 ? 1092 TYR A N   1 
ATOM   8287  C  CA  . TYR A 1 1092 ? 15.438  -12.731 -13.632 1.00 142.47 ? 1092 TYR A CA  1 
ATOM   8288  C  C   . TYR A 1 1092 ? 15.378  -11.922 -12.335 1.00 151.21 ? 1092 TYR A C   1 
ATOM   8289  O  O   . TYR A 1 1092 ? 14.548  -12.165 -11.456 1.00 156.00 ? 1092 TYR A O   1 
ATOM   8290  C  CB  . TYR A 1 1092 ? 15.783  -14.182 -13.312 1.00 137.23 ? 1092 TYR A CB  1 
ATOM   8291  C  CG  . TYR A 1 1092 ? 16.217  -14.996 -14.505 1.00 132.75 ? 1092 TYR A CG  1 
ATOM   8292  C  CD1 . TYR A 1 1092 ? 15.294  -15.410 -15.452 1.00 132.14 ? 1092 TYR A CD1 1 
ATOM   8293  C  CD2 . TYR A 1 1092 ? 17.546  -15.367 -14.678 1.00 132.13 ? 1092 TYR A CD2 1 
ATOM   8294  C  CE1 . TYR A 1 1092 ? 15.677  -16.169 -16.543 1.00 131.19 ? 1092 TYR A CE1 1 
ATOM   8295  C  CE2 . TYR A 1 1092 ? 17.941  -16.127 -15.772 1.00 130.53 ? 1092 TYR A CE2 1 
ATOM   8296  C  CZ  . TYR A 1 1092 ? 17.001  -16.527 -16.702 1.00 130.07 ? 1092 TYR A CZ  1 
ATOM   8297  O  OH  . TYR A 1 1092 ? 17.374  -17.289 -17.795 1.00 128.15 ? 1092 TYR A OH  1 
ATOM   8298  N  N   . VAL A 1 1093 ? 16.285  -10.968 -12.212 1.00 168.12 ? 1093 VAL A N   1 
ATOM   8299  C  CA  . VAL A 1 1093 ? 16.358  -10.145 -11.023 1.00 171.52 ? 1093 VAL A CA  1 
ATOM   8300  C  C   . VAL A 1 1093 ? 16.574  -8.726  -11.517 1.00 169.08 ? 1093 VAL A C   1 
ATOM   8301  O  O   . VAL A 1 1093 ? 17.705  -8.291  -11.774 1.00 167.27 ? 1093 VAL A O   1 
ATOM   8302  C  CB  . VAL A 1 1093 ? 17.478  -10.643 -10.064 1.00 173.99 ? 1093 VAL A CB  1 
ATOM   8303  C  CG1 . VAL A 1 1093 ? 17.788  -9.625  -8.979  1.00 180.37 ? 1093 VAL A CG1 1 
ATOM   8304  C  CG2 . VAL A 1 1093 ? 17.084  -11.989 -9.450  1.00 173.38 ? 1093 VAL A CG2 1 
ATOM   8305  N  N   . GLU A 1 1094 ? 15.460  -8.023  -11.691 1.00 133.32 ? 1094 GLU A N   1 
ATOM   8306  C  CA  . GLU A 1 1094 ? 15.500  -6.703  -12.291 1.00 132.36 ? 1094 GLU A CA  1 
ATOM   8307  C  C   . GLU A 1 1094 ? 16.577  -5.930  -11.597 1.00 132.61 ? 1094 GLU A C   1 
ATOM   8308  O  O   . GLU A 1 1094 ? 16.604  -5.879  -10.389 1.00 138.92 ? 1094 GLU A O   1 
ATOM   8309  C  CB  . GLU A 1 1094 ? 14.180  -5.951  -12.140 1.00 138.27 ? 1094 GLU A CB  1 
ATOM   8310  C  CG  . GLU A 1 1094 ? 14.310  -4.495  -12.606 1.00 143.93 ? 1094 GLU A CG  1 
ATOM   8311  C  CD  . GLU A 1 1094 ? 12.991  -3.723  -12.655 1.00 152.40 ? 1094 GLU A CD  1 
ATOM   8312  O  OE1 . GLU A 1 1094 ? 12.007  -4.136  -11.988 1.00 156.58 ? 1094 GLU A OE1 1 
ATOM   8313  O  OE2 . GLU A 1 1094 ? 12.959  -2.684  -13.365 1.00 154.58 ? 1094 GLU A OE2 1 
ATOM   8314  N  N   . GLN A 1 1095 ? 17.482  -5.343  -12.351 1.00 103.14 ? 1095 GLN A N   1 
ATOM   8315  C  CA  . GLN A 1 1095 ? 18.518  -4.547  -11.745 1.00 105.72 ? 1095 GLN A CA  1 
ATOM   8316  C  C   . GLN A 1 1095 ? 18.204  -3.072  -11.881 1.00 113.47 ? 1095 GLN A C   1 
ATOM   8317  O  O   . GLN A 1 1095 ? 17.380  -2.669  -12.713 1.00 114.23 ? 1095 GLN A O   1 
ATOM   8318  C  CB  . GLN A 1 1095 ? 19.871  -4.901  -12.334 1.00 101.46 ? 1095 GLN A CB  1 
ATOM   8319  C  CG  . GLN A 1 1095 ? 20.271  -6.331  -12.040 1.00 104.50 ? 1095 GLN A CG  1 
ATOM   8320  C  CD  . GLN A 1 1095 ? 20.417  -6.610  -10.536 1.00 136.73 ? 1095 GLN A CD  1 
ATOM   8321  O  OE1 . GLN A 1 1095 ? 21.056  -5.849  -9.798  1.00 139.05 ? 1095 GLN A OE1 1 
ATOM   8322  N  NE2 . GLN A 1 1095 ? 19.827  -7.710  -10.082 1.00 136.70 ? 1095 GLN A NE2 1 
ATOM   8323  N  N   . ASN A 1 1096 ? 18.851  -2.283  -11.028 1.00 191.28 ? 1096 ASN A N   1 
ATOM   8324  C  CA  . ASN A 1 1096 ? 18.550  -0.869  -10.876 1.00 198.58 ? 1096 ASN A CA  1 
ATOM   8325  C  C   . ASN A 1 1096 ? 18.926  -0.119  -12.129 1.00 197.63 ? 1096 ASN A C   1 
ATOM   8326  O  O   . ASN A 1 1096 ? 20.104  -0.030  -12.463 1.00 195.59 ? 1096 ASN A O   1 
ATOM   8327  C  CB  . ASN A 1 1096 ? 19.293  -0.299  -9.657  1.00 206.19 ? 1096 ASN A CB  1 
ATOM   8328  C  CG  . ASN A 1 1096 ? 18.987  1.177   -9.406  1.00 214.09 ? 1096 ASN A CG  1 
ATOM   8329  O  OD1 . ASN A 1 1096 ? 18.639  1.569   -8.285  1.00 221.53 ? 1096 ASN A OD1 1 
ATOM   8330  N  ND2 . ASN A 1 1096 ? 19.123  2.001   -10.448 1.00 212.55 ? 1096 ASN A ND2 1 
ATOM   8331  N  N   . GLN A 1 1097 ? 17.935  0.430   -12.821 1.00 171.65 ? 1097 GLN A N   1 
ATOM   8332  C  CA  . GLN A 1 1097 ? 18.245  1.051   -14.088 1.00 171.77 ? 1097 GLN A CA  1 
ATOM   8333  C  C   . GLN A 1 1097 ? 19.354  2.076   -13.929 1.00 175.51 ? 1097 GLN A C   1 
ATOM   8334  O  O   . GLN A 1 1097 ? 20.514  1.771   -14.182 1.00 172.32 ? 1097 GLN A O   1 
ATOM   8335  C  CB  . GLN A 1 1097 ? 17.024  1.643   -14.803 1.00 171.29 ? 1097 GLN A CB  1 
ATOM   8336  C  CG  . GLN A 1 1097 ? 17.378  2.024   -16.260 1.00 167.50 ? 1097 GLN A CG  1 
ATOM   8337  C  CD  . GLN A 1 1097 ? 16.184  2.260   -17.182 1.00 168.94 ? 1097 GLN A CD  1 
ATOM   8338  O  OE1 . GLN A 1 1097 ? 15.038  2.294   -16.741 1.00 171.00 ? 1097 GLN A OE1 1 
ATOM   8339  N  NE2 . GLN A 1 1097 ? 16.461  2.432   -18.478 1.00 166.89 ? 1097 GLN A NE2 1 
ATOM   8340  N  N   . ASN A 1 1098 ? 19.024  3.278   -13.485 1.00 153.07 ? 1098 ASN A N   1 
ATOM   8341  C  CA  . ASN A 1 1098 ? 20.015  4.348   -13.538 1.00 157.21 ? 1098 ASN A CA  1 
ATOM   8342  C  C   . ASN A 1 1098 ? 21.368  3.974   -12.930 1.00 141.74 ? 1098 ASN A C   1 
ATOM   8343  O  O   . ASN A 1 1098 ? 22.372  4.635   -13.179 1.00 139.60 ? 1098 ASN A O   1 
ATOM   8344  C  CB  . ASN A 1 1098 ? 19.472  5.649   -12.948 1.00 165.48 ? 1098 ASN A CB  1 
ATOM   8345  C  CG  . ASN A 1 1098 ? 20.477  6.788   -13.029 1.00 171.48 ? 1098 ASN A CG  1 
ATOM   8346  O  OD1 . ASN A 1 1098 ? 21.191  7.065   -12.069 1.00 175.64 ? 1098 ASN A OD1 1 
ATOM   8347  N  ND2 . ASN A 1 1098 ? 20.540  7.448   -14.179 1.00 172.75 ? 1098 ASN A ND2 1 
ATOM   8348  N  N   . SER A 1 1099 ? 21.395  2.905   -12.146 1.00 172.53 ? 1099 SER A N   1 
ATOM   8349  C  CA  . SER A 1 1099 ? 22.664  2.385   -11.662 1.00 168.44 ? 1099 SER A CA  1 
ATOM   8350  C  C   . SER A 1 1099 ? 23.444  1.934   -12.869 1.00 160.64 ? 1099 SER A C   1 
ATOM   8351  O  O   . SER A 1 1099 ? 24.436  2.557   -13.262 1.00 161.67 ? 1099 SER A O   1 
ATOM   8352  C  CB  . SER A 1 1099 ? 22.452  1.184   -10.733 1.00 166.93 ? 1099 SER A CB  1 
ATOM   8353  O  OG  . SER A 1 1099 ? 23.663  0.469   -10.490 1.00 163.58 ? 1099 SER A OG  1 
ATOM   8354  N  N   . ILE A 1 1100 ? 22.968  0.841   -13.460 1.00 169.32 ? 1100 ILE A N   1 
ATOM   8355  C  CA  . ILE A 1 1100 ? 23.621  0.224   -14.599 1.00 159.96 ? 1100 ILE A CA  1 
ATOM   8356  C  C   . ILE A 1 1100 ? 23.919  1.289   -15.634 1.00 161.16 ? 1100 ILE A C   1 
ATOM   8357  O  O   . ILE A 1 1100 ? 25.006  1.325   -16.199 1.00 159.28 ? 1100 ILE A O   1 
ATOM   8358  C  CB  . ILE A 1 1100 ? 22.723  -0.847  -15.233 1.00 149.69 ? 1100 ILE A CB  1 
ATOM   8359  C  CG1 . ILE A 1 1100 ? 22.851  -2.175  -14.490 1.00 144.22 ? 1100 ILE A CG1 1 
ATOM   8360  C  CG2 . ILE A 1 1100 ? 23.117  -1.058  -16.662 1.00 145.14 ? 1100 ILE A CG2 1 
ATOM   8361  C  CD1 . ILE A 1 1100 ? 24.111  -2.935  -14.847 1.00 140.53 ? 1100 ILE A CD1 1 
ATOM   8362  N  N   . CYS A 1 1101 ? 22.947  2.168   -15.859 1.00 154.98 ? 1101 CYS A N   1 
ATOM   8363  C  CA  . CYS A 1 1101 ? 23.096  3.237   -16.835 1.00 155.39 ? 1101 CYS A CA  1 
ATOM   8364  C  C   . CYS A 1 1101 ? 24.432  3.933   -16.669 1.00 155.18 ? 1101 CYS A C   1 
ATOM   8365  O  O   . CYS A 1 1101 ? 25.337  3.724   -17.466 1.00 152.26 ? 1101 CYS A O   1 
ATOM   8366  C  CB  . CYS A 1 1101 ? 21.956  4.251   -16.723 1.00 159.76 ? 1101 CYS A CB  1 
ATOM   8367  S  SG  . CYS A 1 1101 ? 20.702  4.168   -18.048 1.00 183.44 ? 1101 CYS A SG  1 
ATOM   8368  N  N   . ASN A 1 1102 ? 24.563  4.750   -15.632 1.00 152.97 ? 1102 ASN A N   1 
ATOM   8369  C  CA  . ASN A 1 1102 ? 25.809  5.465   -15.396 1.00 153.38 ? 1102 ASN A CA  1 
ATOM   8370  C  C   . ASN A 1 1102 ? 26.969  4.501   -15.473 1.00 150.15 ? 1102 ASN A C   1 
ATOM   8371  O  O   . ASN A 1 1102 ? 28.018  4.832   -16.027 1.00 149.00 ? 1102 ASN A O   1 
ATOM   8372  C  CB  . ASN A 1 1102 ? 25.778  6.150   -14.037 1.00 157.01 ? 1102 ASN A CB  1 
ATOM   8373  C  CG  . ASN A 1 1102 ? 24.671  7.182   -13.936 1.00 159.85 ? 1102 ASN A CG  1 
ATOM   8374  O  OD1 . ASN A 1 1102 ? 24.517  8.036   -14.809 1.00 160.94 ? 1102 ASN A OD1 1 
ATOM   8375  N  ND2 . ASN A 1 1102 ? 23.890  7.106   -12.864 1.00 160.92 ? 1102 ASN A ND2 1 
ATOM   8376  N  N   . SER A 1 1103 ? 26.739  3.298   -14.942 1.00 170.16 ? 1103 SER A N   1 
ATOM   8377  C  CA  . SER A 1 1103 ? 27.732  2.220   -14.897 1.00 167.41 ? 1103 SER A CA  1 
ATOM   8378  C  C   . SER A 1 1103 ? 28.391  1.941   -16.262 1.00 165.38 ? 1103 SER A C   1 
ATOM   8379  O  O   . SER A 1 1103 ? 29.608  1.759   -16.346 1.00 164.25 ? 1103 SER A O   1 
ATOM   8380  C  CB  . SER A 1 1103 ? 27.124  0.945   -14.287 1.00 165.93 ? 1103 SER A CB  1 
ATOM   8381  O  OG  . SER A 1 1103 ? 26.853  1.113   -12.901 1.00 169.15 ? 1103 SER A OG  1 
ATOM   8382  N  N   . LEU A 1 1104 ? 27.584  1.909   -17.320 1.00 149.06 ? 1104 LEU A N   1 
ATOM   8383  C  CA  . LEU A 1 1104 ? 28.098  1.840   -18.686 1.00 147.30 ? 1104 LEU A CA  1 
ATOM   8384  C  C   . LEU A 1 1104 ? 28.786  3.172   -19.018 1.00 153.50 ? 1104 LEU A C   1 
ATOM   8385  O  O   . LEU A 1 1104 ? 30.000  3.234   -19.278 1.00 153.14 ? 1104 LEU A O   1 
ATOM   8386  C  CB  . LEU A 1 1104 ? 26.955  1.568   -19.689 1.00 142.93 ? 1104 LEU A CB  1 
ATOM   8387  C  CG  . LEU A 1 1104 ? 26.223  0.215   -19.630 1.00 138.44 ? 1104 LEU A CG  1 
ATOM   8388  C  CD1 . LEU A 1 1104 ? 24.912  0.265   -20.385 1.00 136.85 ? 1104 LEU A CD1 1 
ATOM   8389  C  CD2 . LEU A 1 1104 ? 27.081  -0.908  -20.159 1.00 133.34 ? 1104 LEU A CD2 1 
ATOM   8390  N  N   . LEU A 1 1105 ? 27.985  4.235   -18.963 1.00 147.72 ? 1105 LEU A N   1 
ATOM   8391  C  CA  . LEU A 1 1105 ? 28.392  5.591   -19.323 1.00 151.74 ? 1105 LEU A CA  1 
ATOM   8392  C  C   . LEU A 1 1105 ? 29.635  6.077   -18.586 1.00 154.03 ? 1105 LEU A C   1 
ATOM   8393  O  O   . LEU A 1 1105 ? 30.137  7.164   -18.850 1.00 156.94 ? 1105 LEU A O   1 
ATOM   8394  C  CB  . LEU A 1 1105 ? 27.220  6.571   -19.132 1.00 154.74 ? 1105 LEU A CB  1 
ATOM   8395  C  CG  . LEU A 1 1105 ? 26.043  6.524   -20.132 1.00 155.22 ? 1105 LEU A CG  1 
ATOM   8396  C  CD1 . LEU A 1 1105 ? 24.686  6.458   -19.428 1.00 158.86 ? 1105 LEU A CD1 1 
ATOM   8397  C  CD2 . LEU A 1 1105 ? 26.081  7.713   -21.080 1.00 156.95 ? 1105 LEU A CD2 1 
ATOM   8398  N  N   . TRP A 1 1106 ? 30.138  5.273   -17.664 1.00 165.22 ? 1106 TRP A N   1 
ATOM   8399  C  CA  . TRP A 1 1106 ? 31.433  5.582   -17.081 1.00 167.68 ? 1106 TRP A CA  1 
ATOM   8400  C  C   . TRP A 1 1106 ? 32.553  5.126   -18.009 1.00 164.68 ? 1106 TRP A C   1 
ATOM   8401  O  O   . TRP A 1 1106 ? 33.409  5.933   -18.397 1.00 166.29 ? 1106 TRP A O   1 
ATOM   8402  C  CB  . TRP A 1 1106 ? 31.608  4.950   -15.696 1.00 169.43 ? 1106 TRP A CB  1 
ATOM   8403  C  CG  . TRP A 1 1106 ? 32.940  5.255   -15.069 1.00 170.01 ? 1106 TRP A CG  1 
ATOM   8404  C  CD1 . TRP A 1 1106 ? 33.394  6.473   -14.661 1.00 171.58 ? 1106 TRP A CD1 1 
ATOM   8405  C  CD2 . TRP A 1 1106 ? 33.987  4.324   -14.783 1.00 169.83 ? 1106 TRP A CD2 1 
ATOM   8406  N  NE1 . TRP A 1 1106 ? 34.655  6.358   -14.146 1.00 172.31 ? 1106 TRP A NE1 1 
ATOM   8407  C  CE2 . TRP A 1 1106 ? 35.042  5.046   -14.212 1.00 171.94 ? 1106 TRP A CE2 1 
ATOM   8408  C  CE3 . TRP A 1 1106 ? 34.129  2.949   -14.963 1.00 169.57 ? 1106 TRP A CE3 1 
ATOM   8409  C  CZ2 . TRP A 1 1106 ? 36.229  4.442   -13.809 1.00 174.97 ? 1106 TRP A CZ2 1 
ATOM   8410  C  CZ3 . TRP A 1 1106 ? 35.305  2.352   -14.572 1.00 170.64 ? 1106 TRP A CZ3 1 
ATOM   8411  C  CH2 . TRP A 1 1106 ? 36.340  3.094   -13.998 1.00 173.37 ? 1106 TRP A CH2 1 
ATOM   8412  N  N   . LEU A 1 1107 ? 32.553  3.838   -18.364 1.00 164.67 ? 1107 LEU A N   1 
ATOM   8413  C  CA  . LEU A 1 1107 ? 33.665  3.283   -19.132 1.00 163.66 ? 1107 LEU A CA  1 
ATOM   8414  C  C   . LEU A 1 1107 ? 33.802  4.106   -20.374 1.00 169.39 ? 1107 LEU A C   1 
ATOM   8415  O  O   . LEU A 1 1107 ? 34.828  4.751   -20.595 1.00 171.63 ? 1107 LEU A O   1 
ATOM   8416  C  CB  . LEU A 1 1107 ? 33.411  1.837   -19.531 1.00 156.15 ? 1107 LEU A CB  1 
ATOM   8417  C  CG  . LEU A 1 1107 ? 33.033  0.935   -18.376 1.00 152.30 ? 1107 LEU A CG  1 
ATOM   8418  C  CD1 . LEU A 1 1107 ? 31.543  0.720   -18.459 1.00 151.20 ? 1107 LEU A CD1 1 
ATOM   8419  C  CD2 . LEU A 1 1107 ? 33.802  -0.372  -18.429 1.00 148.52 ? 1107 LEU A CD2 1 
ATOM   8420  N  N   . VAL A 1 1108 ? 32.736  4.088   -21.166 1.00 170.59 ? 1108 VAL A N   1 
ATOM   8421  C  CA  . VAL A 1 1108 ? 32.675  4.819   -22.418 1.00 171.85 ? 1108 VAL A CA  1 
ATOM   8422  C  C   . VAL A 1 1108 ? 33.212  6.241   -22.287 1.00 178.14 ? 1108 VAL A C   1 
ATOM   8423  O  O   . VAL A 1 1108 ? 34.287  6.553   -22.800 1.00 179.89 ? 1108 VAL A O   1 
ATOM   8424  C  CB  . VAL A 1 1108 ? 31.236  4.887   -22.918 1.00 170.25 ? 1108 VAL A CB  1 
ATOM   8425  C  CG1 . VAL A 1 1108 ? 30.318  5.169   -21.759 1.00 172.09 ? 1108 VAL A CG1 1 
ATOM   8426  C  CG2 . VAL A 1 1108 ? 31.091  5.952   -23.981 1.00 171.77 ? 1108 VAL A CG2 1 
ATOM   8427  N  N   . GLU A 1 1109 ? 32.479  7.095   -21.582 1.00 175.46 ? 1109 GLU A N   1 
ATOM   8428  C  CA  . GLU A 1 1109 ? 32.783  8.515   -21.584 1.00 181.20 ? 1109 GLU A CA  1 
ATOM   8429  C  C   . GLU A 1 1109 ? 34.179  8.859   -21.088 1.00 183.75 ? 1109 GLU A C   1 
ATOM   8430  O  O   . GLU A 1 1109 ? 34.681  9.939   -21.372 1.00 186.80 ? 1109 GLU A O   1 
ATOM   8431  C  CB  . GLU A 1 1109 ? 31.734  9.266   -20.787 1.00 184.62 ? 1109 GLU A CB  1 
ATOM   8432  C  CG  . GLU A 1 1109 ? 30.334  8.831   -21.138 1.00 183.60 ? 1109 GLU A CG  1 
ATOM   8433  C  CD  . GLU A 1 1109 ? 29.296  9.843   -20.708 1.00 186.11 ? 1109 GLU A CD  1 
ATOM   8434  O  OE1 . GLU A 1 1109 ? 28.143  9.451   -20.414 1.00 185.14 ? 1109 GLU A OE1 1 
ATOM   8435  O  OE2 . GLU A 1 1109 ? 29.640  11.042  -20.664 1.00 189.05 ? 1109 GLU A OE2 1 
ATOM   8436  N  N   . ASN A 1 1110 ? 34.818  7.932   -20.380 1.00 199.58 ? 1110 ASN A N   1 
ATOM   8437  C  CA  . ASN A 1 1110 ? 36.101  8.221   -19.752 1.00 201.14 ? 1110 ASN A CA  1 
ATOM   8438  C  C   . ASN A 1 1110 ? 37.255  7.305   -20.154 1.00 197.95 ? 1110 ASN A C   1 
ATOM   8439  O  O   . ASN A 1 1110 ? 38.384  7.754   -20.302 1.00 199.85 ? 1110 ASN A O   1 
ATOM   8440  C  CB  . ASN A 1 1110 ? 35.941  8.223   -18.230 1.00 204.11 ? 1110 ASN A CB  1 
ATOM   8441  C  CG  . ASN A 1 1110 ? 34.804  9.119   -17.764 1.00 207.70 ? 1110 ASN A CG  1 
ATOM   8442  O  OD1 . ASN A 1 1110 ? 33.843  8.649   -17.153 1.00 208.20 ? 1110 ASN A OD1 1 
ATOM   8443  N  ND2 . ASN A 1 1110 ? 34.904  10.414  -18.059 1.00 210.93 ? 1110 ASN A ND2 1 
ATOM   8444  N  N   . TYR A 1 1111 ? 36.980  6.025   -20.340 1.00 208.20 ? 1111 TYR A N   1 
ATOM   8445  C  CA  . TYR A 1 1111 ? 38.069  5.082   -20.537 1.00 206.33 ? 1111 TYR A CA  1 
ATOM   8446  C  C   . TYR A 1 1111 ? 38.107  4.365   -21.880 1.00 204.54 ? 1111 TYR A C   1 
ATOM   8447  O  O   . TYR A 1 1111 ? 38.450  3.186   -21.942 1.00 201.37 ? 1111 TYR A O   1 
ATOM   8448  C  CB  . TYR A 1 1111 ? 38.090  4.083   -19.395 1.00 204.98 ? 1111 TYR A CB  1 
ATOM   8449  C  CG  . TYR A 1 1111 ? 38.479  4.748   -18.116 1.00 208.30 ? 1111 TYR A CG  1 
ATOM   8450  C  CD1 . TYR A 1 1111 ? 39.792  4.721   -17.674 1.00 210.53 ? 1111 TYR A CD1 1 
ATOM   8451  C  CD2 . TYR A 1 1111 ? 37.546  5.441   -17.365 1.00 209.58 ? 1111 TYR A CD2 1 
ATOM   8452  C  CE1 . TYR A 1 1111 ? 40.168  5.348   -16.496 1.00 214.34 ? 1111 TYR A CE1 1 
ATOM   8453  C  CE2 . TYR A 1 1111 ? 37.907  6.072   -16.186 1.00 213.44 ? 1111 TYR A CE2 1 
ATOM   8454  C  CZ  . TYR A 1 1111 ? 39.223  6.022   -15.753 1.00 216.03 ? 1111 TYR A CZ  1 
ATOM   8455  O  OH  . TYR A 1 1111 ? 39.596  6.646   -14.578 1.00 220.32 ? 1111 TYR A OH  1 
ATOM   8456  N  N   . GLN A 1 1112 ? 37.777  5.082   -22.953 1.00 189.83 ? 1112 GLN A N   1 
ATOM   8457  C  CA  . GLN A 1 1112 ? 37.778  4.506   -24.305 1.00 190.70 ? 1112 GLN A CA  1 
ATOM   8458  C  C   . GLN A 1 1112 ? 38.591  5.334   -25.293 1.00 198.52 ? 1112 GLN A C   1 
ATOM   8459  O  O   . GLN A 1 1112 ? 38.082  6.282   -25.884 1.00 201.13 ? 1112 GLN A O   1 
ATOM   8460  C  CB  . GLN A 1 1112 ? 36.355  4.377   -24.825 1.00 186.09 ? 1112 GLN A CB  1 
ATOM   8461  C  CG  . GLN A 1 1112 ? 36.267  3.998   -26.272 1.00 183.19 ? 1112 GLN A CG  1 
ATOM   8462  C  CD  . GLN A 1 1112 ? 34.854  4.092   -26.774 1.00 179.21 ? 1112 GLN A CD  1 
ATOM   8463  O  OE1 . GLN A 1 1112 ? 34.147  5.063   -26.502 1.00 179.43 ? 1112 GLN A OE1 1 
ATOM   8464  N  NE2 . GLN A 1 1112 ? 34.425  3.082   -27.511 1.00 175.73 ? 1112 GLN A NE2 1 
ATOM   8465  N  N   . LEU A 1 1113 ? 39.843  4.942   -25.494 1.00 218.23 ? 1113 LEU A N   1 
ATOM   8466  C  CA  . LEU A 1 1113 ? 40.798  5.718   -26.276 1.00 224.16 ? 1113 LEU A CA  1 
ATOM   8467  C  C   . LEU A 1 1113 ? 40.268  6.228   -27.616 1.00 227.30 ? 1113 LEU A C   1 
ATOM   8468  O  O   . LEU A 1 1113 ? 39.242  5.762   -28.120 1.00 224.31 ? 1113 LEU A O   1 
ATOM   8469  C  CB  . LEU A 1 1113 ? 42.078  4.906   -26.489 1.00 223.66 ? 1113 LEU A CB  1 
ATOM   8470  C  CG  . LEU A 1 1113 ? 42.801  4.494   -25.205 1.00 220.84 ? 1113 LEU A CG  1 
ATOM   8471  C  CD1 . LEU A 1 1113 ? 43.875  3.443   -25.470 1.00 220.81 ? 1113 LEU A CD1 1 
ATOM   8472  C  CD2 . LEU A 1 1113 ? 43.394  5.717   -24.517 1.00 223.83 ? 1113 LEU A CD2 1 
ATOM   8473  N  N   . ASP A 1 1114 ? 40.985  7.198   -28.180 1.00 258.19 ? 1114 ASP A N   1 
ATOM   8474  C  CA  . ASP A 1 1114 ? 40.647  7.782   -29.472 1.00 262.81 ? 1114 ASP A CA  1 
ATOM   8475  C  C   . ASP A 1 1114 ? 40.840  6.790   -30.615 1.00 260.82 ? 1114 ASP A C   1 
ATOM   8476  O  O   . ASP A 1 1114 ? 41.314  7.153   -31.690 1.00 264.81 ? 1114 ASP A O   1 
ATOM   8477  C  CB  . ASP A 1 1114 ? 41.488  9.036   -29.720 1.00 272.30 ? 1114 ASP A CB  1 
ATOM   8478  C  CG  . ASP A 1 1114 ? 40.767  10.302  -29.334 1.00 277.71 ? 1114 ASP A CG  1 
ATOM   8479  O  OD1 . ASP A 1 1114 ? 39.520  10.313  -29.391 1.00 276.04 ? 1114 ASP A OD1 1 
ATOM   8480  O  OD2 . ASP A 1 1114 ? 41.445  11.287  -28.980 1.00 283.08 ? 1114 ASP A OD2 1 
ATOM   8481  N  N   . ASN A 1 1115 ? 40.476  5.535   -30.380 1.00 171.38 ? 1115 ASN A N   1 
ATOM   8482  C  CA  . ASN A 1 1115 ? 40.583  4.496   -31.397 1.00 168.05 ? 1115 ASN A CA  1 
ATOM   8483  C  C   . ASN A 1 1115 ? 39.684  3.352   -30.985 1.00 157.08 ? 1115 ASN A C   1 
ATOM   8484  O  O   . ASN A 1 1115 ? 39.872  2.205   -31.399 1.00 153.99 ? 1115 ASN A O   1 
ATOM   8485  C  CB  . ASN A 1 1115 ? 42.037  4.030   -31.602 1.00 172.57 ? 1115 ASN A CB  1 
ATOM   8486  C  CG  . ASN A 1 1115 ? 42.529  3.082   -30.508 1.00 171.29 ? 1115 ASN A CG  1 
ATOM   8487  O  OD1 . ASN A 1 1115 ? 43.592  2.465   -30.639 1.00 173.18 ? 1115 ASN A OD1 1 
ATOM   8488  N  ND2 . ASN A 1 1115 ? 41.766  2.963   -29.433 1.00 168.12 ? 1115 ASN A ND2 1 
ATOM   8489  N  N   . GLY A 1 1116 ? 38.720  3.689   -30.135 1.00 143.06 ? 1116 GLY A N   1 
ATOM   8490  C  CA  . GLY A 1 1116 ? 37.746  2.732   -29.657 1.00 135.54 ? 1116 GLY A CA  1 
ATOM   8491  C  C   . GLY A 1 1116 ? 38.248  1.721   -28.639 1.00 129.08 ? 1116 GLY A C   1 
ATOM   8492  O  O   . GLY A 1 1116 ? 37.467  0.901   -28.158 1.00 126.05 ? 1116 GLY A O   1 
ATOM   8493  N  N   . SER A 1 1117 ? 39.542  1.749   -28.318 1.00 189.94 ? 1117 SER A N   1 
ATOM   8494  C  CA  . SER A 1 1117 ? 40.086  0.835   -27.302 1.00 187.69 ? 1117 SER A CA  1 
ATOM   8495  C  C   . SER A 1 1117 ? 39.874  1.385   -25.887 1.00 188.26 ? 1117 SER A C   1 
ATOM   8496  O  O   . SER A 1 1117 ? 39.517  2.548   -25.724 1.00 191.16 ? 1117 SER A O   1 
ATOM   8497  C  CB  . SER A 1 1117 ? 41.558  0.462   -27.568 1.00 189.94 ? 1117 SER A CB  1 
ATOM   8498  O  OG  . SER A 1 1117 ? 42.462  1.407   -27.031 1.00 192.78 ? 1117 SER A OG  1 
ATOM   8499  N  N   . PHE A 1 1118 ? 40.077  0.541   -24.874 1.00 166.87 ? 1118 PHE A N   1 
ATOM   8500  C  CA  . PHE A 1 1118 ? 39.718  0.868   -23.482 1.00 164.24 ? 1118 PHE A CA  1 
ATOM   8501  C  C   . PHE A 1 1118 ? 40.921  0.867   -22.505 1.00 165.02 ? 1118 PHE A C   1 
ATOM   8502  O  O   . PHE A 1 1118 ? 41.471  -0.190  -22.206 1.00 165.25 ? 1118 PHE A O   1 
ATOM   8503  C  CB  . PHE A 1 1118 ? 38.622  -0.105  -22.987 1.00 161.24 ? 1118 PHE A CB  1 
ATOM   8504  C  CG  . PHE A 1 1118 ? 37.214  0.286   -23.390 1.00 160.53 ? 1118 PHE A CG  1 
ATOM   8505  C  CD1 . PHE A 1 1118 ? 36.953  0.813   -24.640 1.00 160.51 ? 1118 PHE A CD1 1 
ATOM   8506  C  CD2 . PHE A 1 1118 ? 36.152  0.119   -22.516 1.00 160.27 ? 1118 PHE A CD2 1 
ATOM   8507  C  CE1 . PHE A 1 1118 ? 35.664  1.173   -25.006 1.00 159.13 ? 1118 PHE A CE1 1 
ATOM   8508  C  CE2 . PHE A 1 1118 ? 34.858  0.476   -22.884 1.00 158.72 ? 1118 PHE A CE2 1 
ATOM   8509  C  CZ  . PHE A 1 1118 ? 34.619  1.002   -24.127 1.00 157.87 ? 1118 PHE A CZ  1 
ATOM   8510  N  N   . LYS A 1 1119 ? 41.329  2.040   -22.010 1.00 194.76 ? 1119 LYS A N   1 
ATOM   8511  C  CA  . LYS A 1 1119 ? 42.464  2.113   -21.080 1.00 196.72 ? 1119 LYS A CA  1 
ATOM   8512  C  C   . LYS A 1 1119 ? 42.027  1.735   -19.669 1.00 194.16 ? 1119 LYS A C   1 
ATOM   8513  O  O   . LYS A 1 1119 ? 41.019  2.246   -19.169 1.00 193.09 ? 1119 LYS A O   1 
ATOM   8514  C  CB  . LYS A 1 1119 ? 43.139  3.498   -21.092 1.00 209.70 ? 1119 LYS A CB  1 
ATOM   8515  C  CG  . LYS A 1 1119 ? 42.227  4.688   -20.749 1.00 217.49 ? 1119 LYS A CG  1 
ATOM   8516  C  CD  . LYS A 1 1119 ? 42.996  5.811   -20.020 1.00 249.89 ? 1119 LYS A CD  1 
ATOM   8517  C  CE  . LYS A 1 1119 ? 43.637  6.825   -20.964 1.00 252.18 ? 1119 LYS A CE  1 
ATOM   8518  N  NZ  . LYS A 1 1119 ? 42.699  7.911   -21.365 1.00 251.14 ? 1119 LYS A NZ  1 
ATOM   8519  N  N   . GLU A 1 1120 ? 42.772  0.827   -19.037 1.00 216.66 ? 1120 GLU A N   1 
ATOM   8520  C  CA  . GLU A 1 1120 ? 42.473  0.421   -17.665 1.00 219.77 ? 1120 GLU A CA  1 
ATOM   8521  C  C   . GLU A 1 1120 ? 43.000  1.456   -16.698 1.00 226.76 ? 1120 GLU A C   1 
ATOM   8522  O  O   . GLU A 1 1120 ? 44.159  1.858   -16.797 1.00 229.62 ? 1120 GLU A O   1 
ATOM   8523  C  CB  . GLU A 1 1120 ? 43.095  -0.931  -17.332 1.00 220.58 ? 1120 GLU A CB  1 
ATOM   8524  C  CG  . GLU A 1 1120 ? 43.116  -1.225  -15.841 1.00 224.39 ? 1120 GLU A CG  1 
ATOM   8525  C  CD  . GLU A 1 1120 ? 41.728  -1.319  -15.242 1.00 222.50 ? 1120 GLU A CD  1 
ATOM   8526  O  OE1 . GLU A 1 1120 ? 41.349  -2.432  -14.833 1.00 220.44 ? 1120 GLU A OE1 1 
ATOM   8527  O  OE2 . GLU A 1 1120 ? 41.016  -0.295  -15.183 1.00 222.85 ? 1120 GLU A OE2 1 
ATOM   8528  N  N   . ASN A 1 1121 ? 42.158  1.871   -15.754 1.00 196.17 ? 1121 ASN A N   1 
ATOM   8529  C  CA  . ASN A 1 1121 ? 42.520  2.948   -14.833 1.00 200.92 ? 1121 ASN A CA  1 
ATOM   8530  C  C   . ASN A 1 1121 ? 43.577  2.583   -13.795 1.00 207.28 ? 1121 ASN A C   1 
ATOM   8531  O  O   . ASN A 1 1121 ? 44.705  3.092   -13.817 1.00 209.24 ? 1121 ASN A O   1 
ATOM   8532  C  CB  . ASN A 1 1121 ? 41.284  3.464   -14.103 1.00 199.17 ? 1121 ASN A CB  1 
ATOM   8533  C  CG  . ASN A 1 1121 ? 41.579  4.705   -13.297 1.00 199.27 ? 1121 ASN A CG  1 
ATOM   8534  O  OD1 . ASN A 1 1121 ? 42.113  5.678   -13.821 1.00 199.87 ? 1121 ASN A OD1 1 
ATOM   8535  N  ND2 . ASN A 1 1121 ? 41.248  4.676   -12.015 1.00 198.22 ? 1121 ASN A ND2 1 
ATOM   8536  N  N   . SER A 1 1122 ? 43.179  1.708   -12.878 1.00 213.84 ? 1122 SER A N   1 
ATOM   8537  C  CA  . SER A 1 1122 ? 44.026  1.263   -11.784 1.00 219.24 ? 1122 SER A CA  1 
ATOM   8538  C  C   . SER A 1 1122 ? 45.301  0.612   -12.285 1.00 222.28 ? 1122 SER A C   1 
ATOM   8539  O  O   . SER A 1 1122 ? 45.542  0.532   -13.482 1.00 220.96 ? 1122 SER A O   1 
ATOM   8540  C  CB  . SER A 1 1122 ? 43.263  0.247   -10.936 1.00 216.49 ? 1122 SER A CB  1 
ATOM   8541  O  OG  . SER A 1 1122 ? 43.047  -0.944  -11.678 1.00 211.87 ? 1122 SER A OG  1 
ATOM   8542  N  N   . GLN A 1 1123 ? 46.113  0.132   -11.358 1.00 253.99 ? 1123 GLN A N   1 
ATOM   8543  C  CA  . GLN A 1 1123 ? 47.316  -0.577  -11.737 1.00 257.19 ? 1123 GLN A CA  1 
ATOM   8544  C  C   . GLN A 1 1123 ? 47.026  -2.063  -11.915 1.00 248.67 ? 1123 GLN A C   1 
ATOM   8545  O  O   . GLN A 1 1123 ? 47.920  -2.857  -12.188 1.00 249.31 ? 1123 GLN A O   1 
ATOM   8546  C  CB  . GLN A 1 1123 ? 48.403  -0.345  -10.694 1.00 271.10 ? 1123 GLN A CB  1 
ATOM   8547  C  CG  . GLN A 1 1123 ? 48.579  1.127   -10.340 1.00 282.41 ? 1123 GLN A CG  1 
ATOM   8548  C  CD  . GLN A 1 1123 ? 49.926  1.424   -9.709  1.00 296.47 ? 1123 GLN A CD  1 
ATOM   8549  O  OE1 . GLN A 1 1123 ? 50.925  0.775   -10.008 1.00 301.16 ? 1123 GLN A OE1 1 
ATOM   8550  N  NE2 . GLN A 1 1123 ? 49.959  2.417   -8.837  1.00 303.64 ? 1123 GLN A NE2 1 
ATOM   8551  N  N   . TYR A 1 1124 ? 45.763  -2.439  -11.783 1.00 183.36 ? 1124 TYR A N   1 
ATOM   8552  C  CA  . TYR A 1 1124 ? 45.426  -3.848  -11.773 1.00 174.41 ? 1124 TYR A CA  1 
ATOM   8553  C  C   . TYR A 1 1124 ? 45.935  -4.592  -13.003 1.00 169.64 ? 1124 TYR A C   1 
ATOM   8554  O  O   . TYR A 1 1124 ? 45.668  -4.197  -14.136 1.00 164.88 ? 1124 TYR A O   1 
ATOM   8555  C  CB  . TYR A 1 1124 ? 43.926  -4.026  -11.621 1.00 166.88 ? 1124 TYR A CB  1 
ATOM   8556  C  CG  . TYR A 1 1124 ? 43.523  -5.405  -11.157 1.00 161.09 ? 1124 TYR A CG  1 
ATOM   8557  C  CD1 . TYR A 1 1124 ? 44.021  -5.947  -9.978  1.00 162.45 ? 1124 TYR A CD1 1 
ATOM   8558  C  CD2 . TYR A 1 1124 ? 42.625  -6.157  -11.885 1.00 155.27 ? 1124 TYR A CD2 1 
ATOM   8559  C  CE1 . TYR A 1 1124 ? 43.634  -7.225  -9.545  1.00 159.66 ? 1124 TYR A CE1 1 
ATOM   8560  C  CE2 . TYR A 1 1124 ? 42.232  -7.426  -11.467 1.00 152.09 ? 1124 TYR A CE2 1 
ATOM   8561  C  CZ  . TYR A 1 1124 ? 42.733  -7.960  -10.296 1.00 152.26 ? 1124 TYR A CZ  1 
ATOM   8562  O  OH  . TYR A 1 1124 ? 42.328  -9.222  -9.896  1.00 146.70 ? 1124 TYR A OH  1 
ATOM   8563  N  N   . GLN A 1 1125 ? 46.720  -5.639  -12.753 1.00 185.25 ? 1125 GLN A N   1 
ATOM   8564  C  CA  . GLN A 1 1125 ? 47.057  -6.643  -13.753 1.00 182.06 ? 1125 GLN A CA  1 
ATOM   8565  C  C   . GLN A 1 1125 ? 46.208  -7.845  -13.381 1.00 174.02 ? 1125 GLN A C   1 
ATOM   8566  O  O   . GLN A 1 1125 ? 46.415  -8.437  -12.331 1.00 172.30 ? 1125 GLN A O   1 
ATOM   8567  C  CB  . GLN A 1 1125 ? 48.537  -7.060  -13.677 1.00 193.61 ? 1125 GLN A CB  1 
ATOM   8568  C  CG  . GLN A 1 1125 ? 49.597  -5.955  -13.471 1.00 204.78 ? 1125 GLN A CG  1 
ATOM   8569  C  CD  . GLN A 1 1125 ? 49.781  -5.034  -14.669 1.00 210.16 ? 1125 GLN A CD  1 
ATOM   8570  O  OE1 . GLN A 1 1125 ? 48.804  -4.585  -15.269 1.00 207.74 ? 1125 GLN A OE1 1 
ATOM   8571  N  NE2 . GLN A 1 1125 ? 51.041  -4.720  -14.998 1.00 216.12 ? 1125 GLN A NE2 1 
ATOM   8572  N  N   . PRO A 1 1126 ? 45.226  -8.200  -14.217 1.00 165.86 ? 1126 PRO A N   1 
ATOM   8573  C  CA  . PRO A 1 1126 ? 44.455  -9.405  -13.906 1.00 164.96 ? 1126 PRO A CA  1 
ATOM   8574  C  C   . PRO A 1 1126 ? 45.214  -10.625 -14.413 1.00 168.19 ? 1126 PRO A C   1 
ATOM   8575  O  O   . PRO A 1 1126 ? 45.428  -11.596 -13.684 1.00 172.27 ? 1126 PRO A O   1 
ATOM   8576  C  CB  . PRO A 1 1126 ? 43.160  -9.216  -14.714 1.00 158.31 ? 1126 PRO A CB  1 
ATOM   8577  C  CG  . PRO A 1 1126 ? 43.232  -7.814  -15.287 1.00 158.64 ? 1126 PRO A CG  1 
ATOM   8578  C  CD  . PRO A 1 1126 ? 44.688  -7.502  -15.391 1.00 162.81 ? 1126 PRO A CD  1 
ATOM   8579  N  N   . ILE A 1 1127 ? 45.656  -10.544 -15.664 1.00 190.75 ? 1127 ILE A N   1 
ATOM   8580  C  CA  . ILE A 1 1127 ? 46.267  -11.679 -16.355 1.00 193.34 ? 1127 ILE A CA  1 
ATOM   8581  C  C   . ILE A 1 1127 ? 47.670  -11.390 -16.869 1.00 198.02 ? 1127 ILE A C   1 
ATOM   8582  O  O   . ILE A 1 1127 ? 47.950  -10.286 -17.343 1.00 197.36 ? 1127 ILE A O   1 
ATOM   8583  C  CB  . ILE A 1 1127 ? 45.439  -12.059 -17.576 1.00 195.54 ? 1127 ILE A CB  1 
ATOM   8584  C  CG1 . ILE A 1 1127 ? 44.666  -10.829 -18.087 1.00 192.57 ? 1127 ILE A CG1 1 
ATOM   8585  C  CG2 . ILE A 1 1127 ? 44.481  -13.190 -17.224 1.00 193.80 ? 1127 ILE A CG2 1 
ATOM   8586  C  CD1 . ILE A 1 1127 ? 45.516  -9.592  -18.431 1.00 195.48 ? 1127 ILE A CD1 1 
ATOM   8587  N  N   . LYS A 1 1128 ? 48.549  -12.385 -16.797 1.00 188.39 ? 1128 LYS A N   1 
ATOM   8588  C  CA  . LYS A 1 1128 ? 49.891  -12.226 -17.346 1.00 194.75 ? 1128 LYS A CA  1 
ATOM   8589  C  C   . LYS A 1 1128 ? 49.881  -12.574 -18.825 1.00 198.59 ? 1128 LYS A C   1 
ATOM   8590  O  O   . LYS A 1 1128 ? 49.716  -13.736 -19.187 1.00 199.21 ? 1128 LYS A O   1 
ATOM   8591  C  CB  . LYS A 1 1128 ? 50.901  -13.112 -16.604 1.00 197.51 ? 1128 LYS A CB  1 
ATOM   8592  C  CG  . LYS A 1 1128 ? 52.319  -13.129 -17.205 1.00 201.14 ? 1128 LYS A CG  1 
ATOM   8593  C  CD  . LYS A 1 1128 ? 53.088  -11.802 -17.054 1.00 202.98 ? 1128 LYS A CD  1 
ATOM   8594  C  CE  . LYS A 1 1128 ? 53.184  -11.012 -18.372 1.00 200.96 ? 1128 LYS A CE  1 
ATOM   8595  N  NZ  . LYS A 1 1128 ? 54.437  -10.200 -18.563 1.00 205.09 ? 1128 LYS A NZ  1 
ATOM   8596  N  N   . LEU A 1 1129 ? 50.056  -11.576 -19.684 1.00 238.80 ? 1129 LEU A N   1 
ATOM   8597  C  CA  . LEU A 1 1129 ? 50.148  -11.839 -21.119 1.00 242.53 ? 1129 LEU A CA  1 
ATOM   8598  C  C   . LEU A 1 1129 ? 51.588  -12.066 -21.592 1.00 253.23 ? 1129 LEU A C   1 
ATOM   8599  O  O   . LEU A 1 1129 ? 52.516  -11.409 -21.116 1.00 259.60 ? 1129 LEU A O   1 
ATOM   8600  C  CB  . LEU A 1 1129 ? 49.509  -10.706 -21.924 1.00 236.68 ? 1129 LEU A CB  1 
ATOM   8601  C  CG  . LEU A 1 1129 ? 47.985  -10.592 -21.866 1.00 229.42 ? 1129 LEU A CG  1 
ATOM   8602  C  CD1 . LEU A 1 1129 ? 47.461  -9.886  -23.112 1.00 226.91 ? 1129 LEU A CD1 1 
ATOM   8603  C  CD2 . LEU A 1 1129 ? 47.343  -11.962 -21.723 1.00 226.99 ? 1129 LEU A CD2 1 
ATOM   8604  N  N   . GLN A 1 1130 ? 51.770  -12.990 -22.535 1.00 198.73 ? 1130 GLN A N   1 
ATOM   8605  C  CA  . GLN A 1 1130 ? 53.089  -13.241 -23.115 1.00 203.88 ? 1130 GLN A CA  1 
ATOM   8606  C  C   . GLN A 1 1130 ? 53.515  -12.141 -24.083 1.00 199.34 ? 1130 GLN A C   1 
ATOM   8607  O  O   . GLN A 1 1130 ? 52.717  -11.293 -24.477 1.00 193.35 ? 1130 GLN A O   1 
ATOM   8608  C  CB  . GLN A 1 1130 ? 53.108  -14.578 -23.844 1.00 211.23 ? 1130 GLN A CB  1 
ATOM   8609  C  CG  . GLN A 1 1130 ? 52.639  -15.743 -23.013 1.00 214.38 ? 1130 GLN A CG  1 
ATOM   8610  C  CD  . GLN A 1 1130 ? 53.142  -17.057 -23.563 1.00 220.58 ? 1130 GLN A CD  1 
ATOM   8611  O  OE1 . GLN A 1 1130 ? 54.349  -17.244 -23.754 1.00 226.95 ? 1130 GLN A OE1 1 
ATOM   8612  N  NE2 . GLN A 1 1130 ? 52.221  -17.979 -23.824 1.00 217.96 ? 1130 GLN A NE2 1 
ATOM   8613  N  N   . GLY A 1 1131 ? 54.783  -12.163 -24.466 1.00 234.31 ? 1131 GLY A N   1 
ATOM   8614  C  CA  . GLY A 1 1131 ? 55.269  -11.246 -25.474 1.00 237.23 ? 1131 GLY A CA  1 
ATOM   8615  C  C   . GLY A 1 1131 ? 56.157  -10.126 -24.977 1.00 244.01 ? 1131 GLY A C   1 
ATOM   8616  O  O   . GLY A 1 1131 ? 56.295  -9.884  -23.772 1.00 247.06 ? 1131 GLY A O   1 
ATOM   8617  N  N   . THR A 1 1132 ? 56.758  -9.439  -25.941 1.00 251.40 ? 1132 THR A N   1 
ATOM   8618  C  CA  . THR A 1 1132 ? 57.680  -8.352  -25.676 1.00 254.25 ? 1132 THR A CA  1 
ATOM   8619  C  C   . THR A 1 1132 ? 56.984  -7.257  -24.881 1.00 249.38 ? 1132 THR A C   1 
ATOM   8620  O  O   . THR A 1 1132 ? 55.760  -7.193  -24.840 1.00 242.62 ? 1132 THR A O   1 
ATOM   8621  C  CB  . THR A 1 1132 ? 58.199  -7.753  -26.997 1.00 259.14 ? 1132 THR A CB  1 
ATOM   8622  O  OG1 . THR A 1 1132 ? 58.121  -8.735  -28.037 1.00 259.21 ? 1132 THR A OG1 1 
ATOM   8623  C  CG2 . THR A 1 1132 ? 59.637  -7.289  -26.843 1.00 266.93 ? 1132 THR A CG2 1 
ATOM   8624  N  N   . LEU A 1 1133 ? 57.770  -6.398  -24.245 1.00 233.58 ? 1133 LEU A N   1 
ATOM   8625  C  CA  . LEU A 1 1133 ? 57.216  -5.245  -23.550 1.00 234.25 ? 1133 LEU A CA  1 
ATOM   8626  C  C   . LEU A 1 1133 ? 56.339  -4.381  -24.470 1.00 235.08 ? 1133 LEU A C   1 
ATOM   8627  O  O   . LEU A 1 1133 ? 55.352  -3.809  -24.008 1.00 233.96 ? 1133 LEU A O   1 
ATOM   8628  C  CB  . LEU A 1 1133 ? 58.326  -4.403  -22.910 1.00 237.89 ? 1133 LEU A CB  1 
ATOM   8629  C  CG  . LEU A 1 1133 ? 59.041  -5.011  -21.695 1.00 237.56 ? 1133 LEU A CG  1 
ATOM   8630  C  CD1 . LEU A 1 1133 ? 59.882  -6.228  -22.081 1.00 240.73 ? 1133 LEU A CD1 1 
ATOM   8631  C  CD2 . LEU A 1 1133 ? 59.897  -3.965  -20.976 1.00 240.78 ? 1133 LEU A CD2 1 
ATOM   8632  N  N   . PRO A 1 1134 ? 56.706  -4.275  -25.768 1.00 232.74 ? 1134 PRO A N   1 
ATOM   8633  C  CA  . PRO A 1 1134 ? 55.862  -3.630  -26.783 1.00 231.31 ? 1134 PRO A CA  1 
ATOM   8634  C  C   . PRO A 1 1134 ? 54.657  -4.490  -27.090 1.00 228.47 ? 1134 PRO A C   1 
ATOM   8635  O  O   . PRO A 1 1134 ? 53.516  -4.040  -26.974 1.00 223.36 ? 1134 PRO A O   1 
ATOM   8636  C  CB  . PRO A 1 1134 ? 56.756  -3.612  -28.027 1.00 235.36 ? 1134 PRO A CB  1 
ATOM   8637  C  CG  . PRO A 1 1134 ? 58.122  -3.800  -27.546 1.00 241.26 ? 1134 PRO A CG  1 
ATOM   8638  C  CD  . PRO A 1 1134 ? 58.029  -4.625  -26.311 1.00 239.20 ? 1134 PRO A CD  1 
ATOM   8639  N  N   . VAL A 1 1135 ? 54.925  -5.724  -27.499 1.00 197.29 ? 1135 VAL A N   1 
ATOM   8640  C  CA  . VAL A 1 1135 ? 53.861  -6.670  -27.772 1.00 191.18 ? 1135 VAL A CA  1 
ATOM   8641  C  C   . VAL A 1 1135 ? 52.841  -6.613  -26.652 1.00 185.39 ? 1135 VAL A C   1 
ATOM   8642  O  O   . VAL A 1 1135 ? 51.735  -6.131  -26.854 1.00 180.66 ? 1135 VAL A O   1 
ATOM   8643  C  CB  . VAL A 1 1135 ? 54.380  -8.106  -27.849 1.00 192.43 ? 1135 VAL A CB  1 
ATOM   8644  C  CG1 . VAL A 1 1135 ? 53.237  -9.076  -27.686 1.00 186.86 ? 1135 VAL A CG1 1 
ATOM   8645  C  CG2 . VAL A 1 1135 ? 55.090  -8.344  -29.161 1.00 196.19 ? 1135 VAL A CG2 1 
ATOM   8646  N  N   . GLU A 1 1136 ? 53.229  -7.086  -25.468 1.00 242.24 ? 1136 GLU A N   1 
ATOM   8647  C  CA  . GLU A 1 1136 ? 52.326  -7.187  -24.314 1.00 237.18 ? 1136 GLU A CA  1 
ATOM   8648  C  C   . GLU A 1 1136 ? 51.362  -6.005  -24.214 1.00 234.73 ? 1136 GLU A C   1 
ATOM   8649  O  O   . GLU A 1 1136 ? 50.177  -6.182  -23.946 1.00 231.22 ? 1136 GLU A O   1 
ATOM   8650  C  CB  . GLU A 1 1136 ? 53.128  -7.339  -23.005 1.00 238.04 ? 1136 GLU A CB  1 
ATOM   8651  C  CG  . GLU A 1 1136 ? 52.278  -7.364  -21.727 1.00 234.10 ? 1136 GLU A CG  1 
ATOM   8652  C  CD  . GLU A 1 1136 ? 53.077  -7.723  -20.474 1.00 235.98 ? 1136 GLU A CD  1 
ATOM   8653  O  OE1 . GLU A 1 1136 ? 54.322  -7.683  -20.520 1.00 238.69 ? 1136 GLU A OE1 1 
ATOM   8654  O  OE2 . GLU A 1 1136 ? 52.449  -8.045  -19.442 1.00 234.37 ? 1136 GLU A OE2 1 
ATOM   8655  N  N   . ALA A 1 1137 ? 51.881  -4.803  -24.439 1.00 230.92 ? 1137 ALA A N   1 
ATOM   8656  C  CA  . ALA A 1 1137 ? 51.074  -3.595  -24.363 1.00 229.41 ? 1137 ALA A CA  1 
ATOM   8657  C  C   . ALA A 1 1137 ? 49.933  -3.686  -25.356 1.00 225.77 ? 1137 ALA A C   1 
ATOM   8658  O  O   . ALA A 1 1137 ? 48.763  -3.590  -24.999 1.00 221.49 ? 1137 ALA A O   1 
ATOM   8659  C  CB  . ALA A 1 1137 ? 51.930  -2.379  -24.650 1.00 234.55 ? 1137 ALA A CB  1 
ATOM   8660  N  N   . ARG A 1 1138 ? 50.290  -3.877  -26.614 1.00 243.46 ? 1138 ARG A N   1 
ATOM   8661  C  CA  . ARG A 1 1138 ? 49.303  -4.062  -27.661 1.00 240.87 ? 1138 ARG A CA  1 
ATOM   8662  C  C   . ARG A 1 1138 ? 48.393  -5.248  -27.317 1.00 232.81 ? 1138 ARG A C   1 
ATOM   8663  O  O   . ARG A 1 1138 ? 47.190  -5.207  -27.568 1.00 228.06 ? 1138 ARG A O   1 
ATOM   8664  C  CB  . ARG A 1 1138 ? 50.018  -4.281  -28.995 1.00 249.46 ? 1138 ARG A CB  1 
ATOM   8665  C  CG  . ARG A 1 1138 ? 49.149  -4.159  -30.236 1.00 251.52 ? 1138 ARG A CG  1 
ATOM   8666  C  CD  . ARG A 1 1138 ? 50.029  -4.076  -31.488 1.00 259.97 ? 1138 ARG A CD  1 
ATOM   8667  N  NE  . ARG A 1 1138 ? 49.305  -4.364  -32.726 1.00 263.19 ? 1138 ARG A NE  1 
ATOM   8668  C  CZ  . ARG A 1 1138 ? 49.837  -4.245  -33.940 1.00 270.17 ? 1138 ARG A CZ  1 
ATOM   8669  N  NH1 . ARG A 1 1138 ? 51.092  -3.835  -34.071 1.00 276.01 ? 1138 ARG A NH1 1 
ATOM   8670  N  NH2 . ARG A 1 1138 ? 49.119  -4.528  -35.018 1.00 270.02 ? 1138 ARG A NH2 1 
ATOM   8671  N  N   . GLU A 1 1139 ? 48.979  -6.294  -26.733 1.00 230.72 ? 1139 GLU A N   1 
ATOM   8672  C  CA  . GLU A 1 1139 ? 48.233  -7.471  -26.280 1.00 222.83 ? 1139 GLU A CA  1 
ATOM   8673  C  C   . GLU A 1 1139 ? 47.306  -7.091  -25.146 1.00 219.62 ? 1139 GLU A C   1 
ATOM   8674  O  O   . GLU A 1 1139 ? 46.115  -7.389  -25.169 1.00 215.41 ? 1139 GLU A O   1 
ATOM   8675  C  CB  . GLU A 1 1139 ? 49.186  -8.556  -25.768 1.00 222.57 ? 1139 GLU A CB  1 
ATOM   8676  C  CG  . GLU A 1 1139 ? 49.776  -9.466  -26.828 1.00 222.07 ? 1139 GLU A CG  1 
ATOM   8677  C  CD  . GLU A 1 1139 ? 48.788  -10.500 -27.331 1.00 217.72 ? 1139 GLU A CD  1 
ATOM   8678  O  OE1 . GLU A 1 1139 ? 49.021  -11.709 -27.106 1.00 219.28 ? 1139 GLU A OE1 1 
ATOM   8679  O  OE2 . GLU A 1 1139 ? 47.784  -10.101 -27.959 1.00 214.38 ? 1139 GLU A OE2 1 
ATOM   8680  N  N   . ASN A 1 1140 ? 47.876  -6.432  -24.146 1.00 256.01 ? 1140 ASN A N   1 
ATOM   8681  C  CA  . ASN A 1 1140 ? 47.133  -6.022  -22.969 1.00 253.50 ? 1140 ASN A CA  1 
ATOM   8682  C  C   . ASN A 1 1140 ? 45.978  -5.084  -23.321 1.00 245.50 ? 1140 ASN A C   1 
ATOM   8683  O  O   . ASN A 1 1140 ? 44.932  -5.123  -22.675 1.00 241.05 ? 1140 ASN A O   1 
ATOM   8684  C  CB  . ASN A 1 1140 ? 48.074  -5.371  -21.958 1.00 262.82 ? 1140 ASN A CB  1 
ATOM   8685  C  CG  . ASN A 1 1140 ? 47.521  -5.394  -20.554 1.00 267.90 ? 1140 ASN A CG  1 
ATOM   8686  O  OD1 . ASN A 1 1140 ? 47.952  -4.629  -19.698 1.00 273.74 ? 1140 ASN A OD1 1 
ATOM   8687  N  ND2 . ASN A 1 1140 ? 46.558  -6.274  -20.307 1.00 266.45 ? 1140 ASN A ND2 1 
ATOM   8688  N  N   . SER A 1 1141 ? 46.167  -4.252  -24.346 1.00 245.14 ? 1141 SER A N   1 
ATOM   8689  C  CA  . SER A 1 1141 ? 45.119  -3.342  -24.825 1.00 240.74 ? 1141 SER A CA  1 
ATOM   8690  C  C   . SER A 1 1141 ? 43.973  -4.098  -25.465 1.00 232.58 ? 1141 SER A C   1 
ATOM   8691  O  O   . SER A 1 1141 ? 42.800  -3.804  -25.234 1.00 228.00 ? 1141 SER A O   1 
ATOM   8692  C  CB  . SER A 1 1141 ? 45.671  -2.352  -25.852 1.00 245.11 ? 1141 SER A CB  1 
ATOM   8693  O  OG  . SER A 1 1141 ? 44.618  -1.778  -26.619 1.00 244.35 ? 1141 SER A OG  1 
ATOM   8694  N  N   . LEU A 1 1142 ? 44.326  -5.064  -26.297 1.00 197.32 ? 1142 LEU A N   1 
ATOM   8695  C  CA  . LEU A 1 1142 ? 43.328  -5.880  -26.953 1.00 189.93 ? 1142 LEU A CA  1 
ATOM   8696  C  C   . LEU A 1 1142 ? 42.469  -6.558  -25.886 1.00 186.24 ? 1142 LEU A C   1 
ATOM   8697  O  O   . LEU A 1 1142 ? 41.240  -6.450  -25.911 1.00 182.93 ? 1142 LEU A O   1 
ATOM   8698  C  CB  . LEU A 1 1142 ? 44.003  -6.920  -27.843 1.00 188.04 ? 1142 LEU A CB  1 
ATOM   8699  C  CG  . LEU A 1 1142 ? 43.157  -7.412  -29.012 1.00 182.06 ? 1142 LEU A CG  1 
ATOM   8700  C  CD1 . LEU A 1 1142 ? 43.986  -8.331  -29.887 1.00 183.52 ? 1142 LEU A CD1 1 
ATOM   8701  C  CD2 . LEU A 1 1142 ? 41.906  -8.107  -28.516 1.00 175.39 ? 1142 LEU A CD2 1 
ATOM   8702  N  N   . TYR A 1 1143 ? 43.118  -7.229  -24.933 1.00 174.33 ? 1143 TYR A N   1 
ATOM   8703  C  CA  . TYR A 1 1143 ? 42.389  -7.999  -23.927 1.00 170.33 ? 1143 TYR A CA  1 
ATOM   8704  C  C   . TYR A 1 1143 ? 41.332  -7.151  -23.255 1.00 166.30 ? 1143 TYR A C   1 
ATOM   8705  O  O   . TYR A 1 1143 ? 40.154  -7.507  -23.265 1.00 162.16 ? 1143 TYR A O   1 
ATOM   8706  C  CB  . TYR A 1 1143 ? 43.324  -8.620  -22.875 1.00 170.81 ? 1143 TYR A CB  1 
ATOM   8707  C  CG  . TYR A 1 1143 ? 42.584  -9.455  -21.838 1.00 168.24 ? 1143 TYR A CG  1 
ATOM   8708  C  CD1 . TYR A 1 1143 ? 42.608  -10.851 -21.883 1.00 166.62 ? 1143 TYR A CD1 1 
ATOM   8709  C  CD2 . TYR A 1 1143 ? 41.844  -8.846  -20.821 1.00 167.68 ? 1143 TYR A CD2 1 
ATOM   8710  C  CE1 . TYR A 1 1143 ? 41.920  -11.617 -20.932 1.00 166.21 ? 1143 TYR A CE1 1 
ATOM   8711  C  CE2 . TYR A 1 1143 ? 41.152  -9.603  -19.866 1.00 166.02 ? 1143 TYR A CE2 1 
ATOM   8712  C  CZ  . TYR A 1 1143 ? 41.196  -10.990 -19.925 1.00 165.42 ? 1143 TYR A CZ  1 
ATOM   8713  O  OH  . TYR A 1 1143 ? 40.520  -11.754 -18.984 1.00 164.37 ? 1143 TYR A OH  1 
ATOM   8714  N  N   . LEU A 1 1144 ? 41.754  -6.026  -22.684 1.00 257.92 ? 1144 LEU A N   1 
ATOM   8715  C  CA  . LEU A 1 1144 ? 40.819  -5.137  -22.011 1.00 257.14 ? 1144 LEU A CA  1 
ATOM   8716  C  C   . LEU A 1 1144 ? 39.694  -4.833  -22.988 1.00 256.25 ? 1144 LEU A C   1 
ATOM   8717  O  O   . LEU A 1 1144 ? 38.541  -5.178  -22.736 1.00 254.26 ? 1144 LEU A O   1 
ATOM   8718  C  CB  . LEU A 1 1144 ? 41.500  -3.843  -21.541 1.00 257.37 ? 1144 LEU A CB  1 
ATOM   8719  C  CG  . LEU A 1 1144 ? 40.940  -3.163  -20.282 1.00 253.95 ? 1144 LEU A CG  1 
ATOM   8720  C  CD1 . LEU A 1 1144 ? 41.229  -3.977  -19.027 1.00 253.80 ? 1144 LEU A CD1 1 
ATOM   8721  C  CD2 . LEU A 1 1144 ? 41.504  -1.777  -20.118 1.00 255.27 ? 1144 LEU A CD2 1 
ATOM   8722  N  N   . THR A 1 1145 ? 40.038  -4.242  -24.129 1.00 171.28 ? 1145 THR A N   1 
ATOM   8723  C  CA  . THR A 1 1145 ? 39.024  -3.832  -25.090 1.00 169.14 ? 1145 THR A CA  1 
ATOM   8724  C  C   . THR A 1 1145 ? 38.159  -5.010  -25.517 1.00 166.99 ? 1145 THR A C   1 
ATOM   8725  O  O   . THR A 1 1145 ? 37.065  -4.816  -26.031 1.00 165.34 ? 1145 THR A O   1 
ATOM   8726  C  CB  . THR A 1 1145 ? 39.622  -3.164  -26.338 1.00 175.64 ? 1145 THR A CB  1 
ATOM   8727  O  OG1 . THR A 1 1145 ? 40.751  -2.359  -25.975 1.00 177.26 ? 1145 THR A OG1 1 
ATOM   8728  C  CG2 . THR A 1 1145 ? 38.574  -2.288  -27.004 1.00 175.39 ? 1145 THR A CG2 1 
ATOM   8729  N  N   . ALA A 1 1146 ? 38.643  -6.231  -25.313 1.00 132.67 ? 1146 ALA A N   1 
ATOM   8730  C  CA  . ALA A 1 1146 ? 37.830  -7.405  -25.621 1.00 134.71 ? 1146 ALA A CA  1 
ATOM   8731  C  C   . ALA A 1 1146 ? 36.765  -7.639  -24.540 1.00 134.08 ? 1146 ALA A C   1 
ATOM   8732  O  O   . ALA A 1 1146 ? 35.585  -7.918  -24.824 1.00 130.80 ? 1146 ALA A O   1 
ATOM   8733  C  CB  . ALA A 1 1146 ? 38.715  -8.627  -25.770 1.00 136.32 ? 1146 ALA A CB  1 
ATOM   8734  N  N   . PHE A 1 1147 ? 37.215  -7.488  -23.296 1.00 178.85 ? 1147 PHE A N   1 
ATOM   8735  C  CA  . PHE A 1 1147 ? 36.453  -7.788  -22.081 1.00 177.03 ? 1147 PHE A CA  1 
ATOM   8736  C  C   . PHE A 1 1147 ? 35.377  -6.751  -21.766 1.00 174.70 ? 1147 PHE A C   1 
ATOM   8737  O  O   . PHE A 1 1147 ? 34.276  -7.092  -21.328 1.00 173.78 ? 1147 PHE A O   1 
ATOM   8738  C  CB  . PHE A 1 1147 ? 37.426  -7.848  -20.908 1.00 178.46 ? 1147 PHE A CB  1 
ATOM   8739  C  CG  . PHE A 1 1147 ? 37.012  -8.786  -19.836 1.00 176.88 ? 1147 PHE A CG  1 
ATOM   8740  C  CD1 . PHE A 1 1147 ? 37.944  -9.611  -19.227 1.00 175.78 ? 1147 PHE A CD1 1 
ATOM   8741  C  CD2 . PHE A 1 1147 ? 35.683  -8.857  -19.447 1.00 176.02 ? 1147 PHE A CD2 1 
ATOM   8742  C  CE1 . PHE A 1 1147 ? 37.566  -10.486 -18.242 1.00 175.06 ? 1147 PHE A CE1 1 
ATOM   8743  C  CE2 . PHE A 1 1147 ? 35.287  -9.731  -18.462 1.00 175.88 ? 1147 PHE A CE2 1 
ATOM   8744  C  CZ  . PHE A 1 1147 ? 36.232  -10.550 -17.855 1.00 175.31 ? 1147 PHE A CZ  1 
ATOM   8745  N  N   . THR A 1 1148 ? 35.729  -5.482  -21.953 1.00 150.72 ? 1148 THR A N   1 
ATOM   8746  C  CA  . THR A 1 1148 ? 34.788  -4.386  -21.769 1.00 151.95 ? 1148 THR A CA  1 
ATOM   8747  C  C   . THR A 1 1148 ? 33.593  -4.512  -22.714 1.00 144.11 ? 1148 THR A C   1 
ATOM   8748  O  O   . THR A 1 1148 ? 32.443  -4.279  -22.328 1.00 142.98 ? 1148 THR A O   1 
ATOM   8749  C  CB  . THR A 1 1148 ? 35.475  -2.993  -21.942 1.00 146.09 ? 1148 THR A CB  1 
ATOM   8750  O  OG1 . THR A 1 1148 ? 34.666  -2.157  -22.777 1.00 147.67 ? 1148 THR A OG1 1 
ATOM   8751  C  CG2 . THR A 1 1148 ? 36.850  -3.123  -22.566 1.00 145.80 ? 1148 THR A CG2 1 
ATOM   8752  N  N   . VAL A 1 1149 ? 33.884  -4.896  -23.952 1.00 148.28 ? 1149 VAL A N   1 
ATOM   8753  C  CA  . VAL A 1 1149 ? 32.860  -5.142  -24.944 1.00 146.66 ? 1149 VAL A CA  1 
ATOM   8754  C  C   . VAL A 1 1149 ? 31.912  -6.151  -24.367 1.00 143.11 ? 1149 VAL A C   1 
ATOM   8755  O  O   . VAL A 1 1149 ? 30.723  -5.877  -24.231 1.00 141.95 ? 1149 VAL A O   1 
ATOM   8756  C  CB  . VAL A 1 1149 ? 33.466  -5.776  -26.195 1.00 131.06 ? 1149 VAL A CB  1 
ATOM   8757  C  CG1 . VAL A 1 1149 ? 32.382  -6.329  -27.101 1.00 130.43 ? 1149 VAL A CG1 1 
ATOM   8758  C  CG2 . VAL A 1 1149 ? 34.326  -4.766  -26.952 1.00 130.49 ? 1149 VAL A CG2 1 
ATOM   8759  N  N   . ILE A 1 1150 ? 32.457  -7.316  -24.012 1.00 119.74 ? 1150 ILE A N   1 
ATOM   8760  C  CA  . ILE A 1 1150 ? 31.644  -8.444  -23.568 1.00 114.24 ? 1150 ILE A CA  1 
ATOM   8761  C  C   . ILE A 1 1150 ? 30.654  -7.932  -22.550 1.00 113.08 ? 1150 ILE A C   1 
ATOM   8762  O  O   . ILE A 1 1150 ? 29.426  -8.096  -22.667 1.00 113.06 ? 1150 ILE A O   1 
ATOM   8763  C  CB  . ILE A 1 1150 ? 32.499  -9.505  -22.874 1.00 110.88 ? 1150 ILE A CB  1 
ATOM   8764  C  CG1 . ILE A 1 1150 ? 33.799  -9.729  -23.648 1.00 113.55 ? 1150 ILE A CG1 1 
ATOM   8765  C  CG2 . ILE A 1 1150 ? 31.702  -10.800 -22.695 1.00 104.97 ? 1150 ILE A CG2 1 
ATOM   8766  C  CD1 . ILE A 1 1150 ? 34.603  -10.888 -23.120 1.00 115.59 ? 1150 ILE A CD1 1 
ATOM   8767  N  N   . GLY A 1 1151 ? 31.231  -7.292  -21.543 1.00 251.55 ? 1151 GLY A N   1 
ATOM   8768  C  CA  . GLY A 1 1151 ? 30.467  -6.588  -20.544 1.00 253.39 ? 1151 GLY A CA  1 
ATOM   8769  C  C   . GLY A 1 1151 ? 29.401  -5.733  -21.199 1.00 254.50 ? 1151 GLY A C   1 
ATOM   8770  O  O   . GLY A 1 1151 ? 28.217  -6.097  -21.178 1.00 254.50 ? 1151 GLY A O   1 
ATOM   8771  N  N   . ILE A 1 1152 ? 29.811  -4.622  -21.813 1.00 113.95 ? 1152 ILE A N   1 
ATOM   8772  C  CA  . ILE A 1 1152 ? 28.841  -3.627  -22.272 1.00 116.23 ? 1152 ILE A CA  1 
ATOM   8773  C  C   . ILE A 1 1152 ? 27.781  -4.324  -23.063 1.00 119.44 ? 1152 ILE A C   1 
ATOM   8774  O  O   . ILE A 1 1152 ? 26.608  -3.969  -23.021 1.00 120.49 ? 1152 ILE A O   1 
ATOM   8775  C  CB  . ILE A 1 1152 ? 29.455  -2.572  -23.196 1.00 113.17 ? 1152 ILE A CB  1 
ATOM   8776  C  CG1 . ILE A 1 1152 ? 30.745  -1.995  -22.579 1.00 109.29 ? 1152 ILE A CG1 1 
ATOM   8777  C  CG2 . ILE A 1 1152 ? 28.366  -1.500  -23.527 1.00 83.18  ? 1152 ILE A CG2 1 
ATOM   8778  C  CD1 . ILE A 1 1152 ? 31.928  -1.933  -23.530 1.00 106.52 ? 1152 ILE A CD1 1 
ATOM   8779  N  N   . ARG A 1 1153 ? 28.224  -5.322  -23.805 1.00 192.02 ? 1153 ARG A N   1 
ATOM   8780  C  CA  . ARG A 1 1153 ? 27.296  -6.177  -24.485 1.00 193.28 ? 1153 ARG A CA  1 
ATOM   8781  C  C   . ARG A 1 1153 ? 26.377  -6.795  -23.439 1.00 190.39 ? 1153 ARG A C   1 
ATOM   8782  O  O   . ARG A 1 1153 ? 25.261  -6.315  -23.264 1.00 192.12 ? 1153 ARG A O   1 
ATOM   8783  C  CB  . ARG A 1 1153 ? 28.024  -7.217  -25.335 1.00 198.54 ? 1153 ARG A CB  1 
ATOM   8784  C  CG  . ARG A 1 1153 ? 28.741  -6.629  -26.565 1.00 205.47 ? 1153 ARG A CG  1 
ATOM   8785  C  CD  . ARG A 1 1153 ? 27.750  -6.272  -27.691 1.00 210.06 ? 1153 ARG A CD  1 
ATOM   8786  N  NE  . ARG A 1 1153 ? 28.408  -5.791  -28.911 1.00 212.37 ? 1153 ARG A NE  1 
ATOM   8787  C  CZ  . ARG A 1 1153 ? 27.775  -5.251  -29.955 1.00 213.59 ? 1153 ARG A CZ  1 
ATOM   8788  N  NH1 . ARG A 1 1153 ? 26.455  -5.110  -29.949 1.00 212.02 ? 1153 ARG A NH1 1 
ATOM   8789  N  NH2 . ARG A 1 1153 ? 28.464  -4.842  -31.010 1.00 217.26 ? 1153 ARG A NH2 1 
ATOM   8790  N  N   . LYS A 1 1154 ? 26.838  -7.812  -22.717 1.00 133.33 ? 1154 LYS A N   1 
ATOM   8791  C  CA  . LYS A 1 1154 ? 25.928  -8.602  -21.891 1.00 132.85 ? 1154 LYS A CA  1 
ATOM   8792  C  C   . LYS A 1 1154 ? 24.789  -7.789  -21.279 1.00 136.96 ? 1154 LYS A C   1 
ATOM   8793  O  O   . LYS A 1 1154 ? 23.625  -8.201  -21.270 1.00 135.94 ? 1154 LYS A O   1 
ATOM   8794  C  CB  . LYS A 1 1154 ? 26.711  -9.255  -20.770 1.00 131.49 ? 1154 LYS A CB  1 
ATOM   8795  C  CG  . LYS A 1 1154 ? 27.472  -10.459 -21.174 1.00 129.66 ? 1154 LYS A CG  1 
ATOM   8796  C  CD  . LYS A 1 1154 ? 26.542  -11.625 -21.248 1.00 129.66 ? 1154 LYS A CD  1 
ATOM   8797  C  CE  . LYS A 1 1154 ? 27.317  -12.900 -21.123 1.00 129.97 ? 1154 LYS A CE  1 
ATOM   8798  N  NZ  . LYS A 1 1154 ? 26.379  -14.043 -21.177 1.00 129.98 ? 1154 LYS A NZ  1 
ATOM   8799  N  N   . ALA A 1 1155 ? 25.152  -6.628  -20.756 1.00 175.33 ? 1155 ALA A N   1 
ATOM   8800  C  CA  . ALA A 1 1155 ? 24.242  -5.819  -19.968 1.00 179.91 ? 1155 ALA A CA  1 
ATOM   8801  C  C   . ALA A 1 1155 ? 23.503  -4.832  -20.842 1.00 186.73 ? 1155 ALA A C   1 
ATOM   8802  O  O   . ALA A 1 1155 ? 22.463  -4.307  -20.453 1.00 189.99 ? 1155 ALA A O   1 
ATOM   8803  C  CB  . ALA A 1 1155 ? 25.010  -5.075  -18.899 1.00 178.73 ? 1155 ALA A CB  1 
ATOM   8804  N  N   . PHE A 1 1156 ? 24.048  -4.575  -22.026 1.00 171.70 ? 1156 PHE A N   1 
ATOM   8805  C  CA  . PHE A 1 1156 ? 23.577  -3.473  -22.869 1.00 175.67 ? 1156 PHE A CA  1 
ATOM   8806  C  C   . PHE A 1 1156 ? 22.063  -3.235  -22.801 1.00 175.35 ? 1156 PHE A C   1 
ATOM   8807  O  O   . PHE A 1 1156 ? 21.598  -2.092  -22.813 1.00 176.81 ? 1156 PHE A O   1 
ATOM   8808  C  CB  . PHE A 1 1156 ? 24.018  -3.650  -24.339 1.00 177.06 ? 1156 PHE A CB  1 
ATOM   8809  C  CG  . PHE A 1 1156 ? 23.477  -2.595  -25.251 1.00 179.65 ? 1156 PHE A CG  1 
ATOM   8810  C  CD1 . PHE A 1 1156 ? 24.191  -1.435  -25.496 1.00 181.82 ? 1156 PHE A CD1 1 
ATOM   8811  C  CD2 . PHE A 1 1156 ? 22.229  -2.740  -25.819 1.00 180.41 ? 1156 PHE A CD2 1 
ATOM   8812  C  CE1 . PHE A 1 1156 ? 23.675  -0.451  -26.307 1.00 183.38 ? 1156 PHE A CE1 1 
ATOM   8813  C  CE2 . PHE A 1 1156 ? 21.715  -1.762  -26.628 1.00 182.28 ? 1156 PHE A CE2 1 
ATOM   8814  C  CZ  . PHE A 1 1156 ? 22.438  -0.617  -26.874 1.00 184.29 ? 1156 PHE A CZ  1 
ATOM   8815  N  N   . ASP A 1 1157 ? 21.289  -4.303  -22.716 1.00 184.87 ? 1157 ASP A N   1 
ATOM   8816  C  CA  . ASP A 1 1157 ? 19.866  -4.152  -22.935 1.00 186.82 ? 1157 ASP A CA  1 
ATOM   8817  C  C   . ASP A 1 1157 ? 19.089  -3.338  -21.923 1.00 188.25 ? 1157 ASP A C   1 
ATOM   8818  O  O   . ASP A 1 1157 ? 18.018  -2.843  -22.248 1.00 188.91 ? 1157 ASP A O   1 
ATOM   8819  C  CB  . ASP A 1 1157 ? 19.235  -5.502  -23.187 1.00 189.54 ? 1157 ASP A CB  1 
ATOM   8820  C  CG  . ASP A 1 1157 ? 19.745  -6.105  -24.452 1.00 194.97 ? 1157 ASP A CG  1 
ATOM   8821  O  OD1 . ASP A 1 1157 ? 20.522  -5.407  -25.142 1.00 197.73 ? 1157 ASP A OD1 1 
ATOM   8822  O  OD2 . ASP A 1 1157 ? 19.383  -7.254  -24.759 1.00 195.16 ? 1157 ASP A OD2 1 
ATOM   8823  N  N   . ILE A 1 1158 ? 19.614  -3.183  -20.712 1.00 155.06 ? 1158 ILE A N   1 
ATOM   8824  C  CA  . ILE A 1 1158 ? 18.908  -2.381  -19.707 1.00 152.74 ? 1158 ILE A CA  1 
ATOM   8825  C  C   . ILE A 1 1158 ? 19.242  -0.907  -19.799 1.00 158.27 ? 1158 ILE A C   1 
ATOM   8826  O  O   . ILE A 1 1158 ? 18.561  -0.069  -19.211 1.00 163.63 ? 1158 ILE A O   1 
ATOM   8827  C  CB  . ILE A 1 1158 ? 19.098  -2.873  -18.255 1.00 147.01 ? 1158 ILE A CB  1 
ATOM   8828  C  CG1 . ILE A 1 1158 ? 20.186  -3.952  -18.188 1.00 138.28 ? 1158 ILE A CG1 1 
ATOM   8829  C  CG2 . ILE A 1 1158 ? 17.740  -3.356  -17.695 1.00 146.88 ? 1158 ILE A CG2 1 
ATOM   8830  C  CD1 . ILE A 1 1158 ? 20.965  -4.018  -16.871 1.00 137.22 ? 1158 ILE A CD1 1 
ATOM   8831  N  N   . CYS A 1 1159 ? 20.285  -0.581  -20.541 1.00 197.58 ? 1159 CYS A N   1 
ATOM   8832  C  CA  . CYS A 1 1159 ? 20.484  0.812   -20.863 1.00 201.31 ? 1159 CYS A CA  1 
ATOM   8833  C  C   . CYS A 1 1159 ? 20.800  0.992   -22.331 1.00 203.48 ? 1159 CYS A C   1 
ATOM   8834  O  O   . CYS A 1 1159 ? 21.840  1.548   -22.679 1.00 206.20 ? 1159 CYS A O   1 
ATOM   8835  C  CB  . CYS A 1 1159 ? 21.557  1.441   -19.987 1.00 199.23 ? 1159 CYS A CB  1 
ATOM   8836  S  SG  . CYS A 1 1159 ? 21.292  3.216   -19.762 1.00 264.20 ? 1159 CYS A SG  1 
ATOM   8837  N  N   . PRO A 1 1160 ? 19.889  0.522   -23.198 1.00 168.23 ? 1160 PRO A N   1 
ATOM   8838  C  CA  . PRO A 1 1160 ? 20.003  0.790   -24.631 1.00 166.15 ? 1160 PRO A CA  1 
ATOM   8839  C  C   . PRO A 1 1160 ? 20.122  2.294   -24.826 1.00 168.28 ? 1160 PRO A C   1 
ATOM   8840  O  O   . PRO A 1 1160 ? 19.244  3.061   -24.409 1.00 169.15 ? 1160 PRO A O   1 
ATOM   8841  C  CB  . PRO A 1 1160 ? 18.672  0.272   -25.189 1.00 169.62 ? 1160 PRO A CB  1 
ATOM   8842  C  CG  . PRO A 1 1160 ? 17.762  0.117   -23.997 1.00 171.23 ? 1160 PRO A CG  1 
ATOM   8843  C  CD  . PRO A 1 1160 ? 18.678  -0.252  -22.886 1.00 168.97 ? 1160 PRO A CD  1 
ATOM   8844  N  N   . LEU A 1 1161 ? 21.209  2.719   -25.451 1.00 154.35 ? 1161 LEU A N   1 
ATOM   8845  C  CA  . LEU A 1 1161 ? 21.494  4.134   -25.479 1.00 157.80 ? 1161 LEU A CA  1 
ATOM   8846  C  C   . LEU A 1 1161 ? 22.323  4.527   -26.669 1.00 159.74 ? 1161 LEU A C   1 
ATOM   8847  O  O   . LEU A 1 1161 ? 23.357  3.922   -26.960 1.00 158.75 ? 1161 LEU A O   1 
ATOM   8848  C  CB  . LEU A 1 1161 ? 22.201  4.538   -24.188 1.00 155.03 ? 1161 LEU A CB  1 
ATOM   8849  C  CG  . LEU A 1 1161 ? 22.417  6.017   -23.841 1.00 155.09 ? 1161 LEU A CG  1 
ATOM   8850  C  CD1 . LEU A 1 1161 ? 21.594  6.967   -24.705 1.00 149.70 ? 1161 LEU A CD1 1 
ATOM   8851  C  CD2 . LEU A 1 1161 ? 22.140  6.231   -22.346 1.00 153.77 ? 1161 LEU A CD2 1 
ATOM   8852  N  N   . VAL A 1 1162 ? 21.836  5.553   -27.354 1.00 173.13 ? 1162 VAL A N   1 
ATOM   8853  C  CA  . VAL A 1 1162 ? 22.543  6.130   -28.471 1.00 175.57 ? 1162 VAL A CA  1 
ATOM   8854  C  C   . VAL A 1 1162 ? 23.996  6.209   -28.072 1.00 174.87 ? 1162 VAL A C   1 
ATOM   8855  O  O   . VAL A 1 1162 ? 24.839  5.472   -28.584 1.00 170.96 ? 1162 VAL A O   1 
ATOM   8856  C  CB  . VAL A 1 1162 ? 22.007  7.552   -28.795 1.00 184.15 ? 1162 VAL A CB  1 
ATOM   8857  C  CG1 . VAL A 1 1162 ? 20.713  7.482   -29.612 1.00 185.05 ? 1162 VAL A CG1 1 
ATOM   8858  C  CG2 . VAL A 1 1162 ? 21.800  8.359   -27.508 1.00 189.33 ? 1162 VAL A CG2 1 
ATOM   8859  N  N   . LYS A 1 1163 ? 24.271  7.068   -27.103 1.00 144.32 ? 1163 LYS A N   1 
ATOM   8860  C  CA  . LYS A 1 1163 ? 25.639  7.423   -26.798 1.00 145.84 ? 1163 LYS A CA  1 
ATOM   8861  C  C   . LYS A 1 1163 ? 26.506  6.201   -26.446 1.00 142.70 ? 1163 LYS A C   1 
ATOM   8862  O  O   . LYS A 1 1163 ? 27.735  6.293   -26.466 1.00 142.35 ? 1163 LYS A O   1 
ATOM   8863  C  CB  . LYS A 1 1163 ? 25.699  8.524   -25.719 1.00 148.31 ? 1163 LYS A CB  1 
ATOM   8864  C  CG  . LYS A 1 1163 ? 26.859  9.506   -25.935 1.00 149.10 ? 1163 LYS A CG  1 
ATOM   8865  C  CD  . LYS A 1 1163 ? 27.166  10.434  -24.753 1.00 151.27 ? 1163 LYS A CD  1 
ATOM   8866  C  CE  . LYS A 1 1163 ? 28.475  11.192  -25.036 1.00 152.21 ? 1163 LYS A CE  1 
ATOM   8867  N  NZ  . LYS A 1 1163 ? 29.185  11.757  -23.850 1.00 153.89 ? 1163 LYS A NZ  1 
ATOM   8868  N  N   . ILE A 1 1164 ? 25.888  5.059   -26.143 1.00 197.52 ? 1164 ILE A N   1 
ATOM   8869  C  CA  . ILE A 1 1164 ? 26.683  3.873   -25.814 1.00 196.88 ? 1164 ILE A CA  1 
ATOM   8870  C  C   . ILE A 1 1164 ? 26.634  2.827   -26.902 1.00 196.57 ? 1164 ILE A C   1 
ATOM   8871  O  O   . ILE A 1 1164 ? 27.461  1.916   -26.952 1.00 195.77 ? 1164 ILE A O   1 
ATOM   8872  C  CB  . ILE A 1 1164 ? 26.262  3.197   -24.504 1.00 173.03 ? 1164 ILE A CB  1 
ATOM   8873  C  CG1 . ILE A 1 1164 ? 25.328  2.022   -24.781 1.00 170.12 ? 1164 ILE A CG1 1 
ATOM   8874  C  CG2 . ILE A 1 1164 ? 25.669  4.199   -23.525 1.00 175.56 ? 1164 ILE A CG2 1 
ATOM   8875  C  CD1 . ILE A 1 1164 ? 25.367  0.981   -23.682 1.00 169.93 ? 1164 ILE A CD1 1 
ATOM   8876  N  N   . ASP A 1 1165 ? 25.650  2.941   -27.774 1.00 175.29 ? 1165 ASP A N   1 
ATOM   8877  C  CA  . ASP A 1 1165 ? 25.672  2.099   -28.944 1.00 176.08 ? 1165 ASP A CA  1 
ATOM   8878  C  C   . ASP A 1 1165 ? 26.869  2.506   -29.764 1.00 176.79 ? 1165 ASP A C   1 
ATOM   8879  O  O   . ASP A 1 1165 ? 27.665  1.675   -30.192 1.00 175.21 ? 1165 ASP A O   1 
ATOM   8880  C  CB  . ASP A 1 1165 ? 24.426  2.293   -29.781 1.00 179.32 ? 1165 ASP A CB  1 
ATOM   8881  C  CG  . ASP A 1 1165 ? 24.464  1.462   -31.028 1.00 179.83 ? 1165 ASP A CG  1 
ATOM   8882  O  OD1 . ASP A 1 1165 ? 25.371  0.598   -31.111 1.00 177.31 ? 1165 ASP A OD1 1 
ATOM   8883  O  OD2 . ASP A 1 1165 ? 23.603  1.667   -31.910 1.00 182.62 ? 1165 ASP A OD2 1 
ATOM   8884  N  N   . THR A 1 1166 ? 26.960  3.809   -29.987 1.00 169.54 ? 1166 THR A N   1 
ATOM   8885  C  CA  . THR A 1 1166 ? 28.117  4.417   -30.598 1.00 171.22 ? 1166 THR A CA  1 
ATOM   8886  C  C   . THR A 1 1166 ? 29.340  3.706   -30.099 1.00 168.96 ? 1166 THR A C   1 
ATOM   8887  O  O   . THR A 1 1166 ? 29.868  2.833   -30.774 1.00 169.81 ? 1166 THR A O   1 
ATOM   8888  C  CB  . THR A 1 1166 ? 28.232  5.889   -30.184 1.00 174.08 ? 1166 THR A CB  1 
ATOM   8889  O  OG1 . THR A 1 1166 ? 27.177  6.630   -30.805 1.00 177.03 ? 1166 THR A OG1 1 
ATOM   8890  C  CG2 . THR A 1 1166 ? 29.587  6.481   -30.589 1.00 175.92 ? 1166 THR A CG2 1 
ATOM   8891  N  N   . ALA A 1 1167 ? 29.780  4.065   -28.901 1.00 240.48 ? 1167 ALA A N   1 
ATOM   8892  C  CA  . ALA A 1 1167 ? 31.028  3.534   -28.387 1.00 236.06 ? 1167 ALA A CA  1 
ATOM   8893  C  C   . ALA A 1 1167 ? 31.133  2.037   -28.664 1.00 228.91 ? 1167 ALA A C   1 
ATOM   8894  O  O   . ALA A 1 1167 ? 32.231  1.530   -28.891 1.00 227.82 ? 1167 ALA A O   1 
ATOM   8895  C  CB  . ALA A 1 1167 ? 31.161  3.817   -26.908 1.00 235.14 ? 1167 ALA A CB  1 
ATOM   8896  N  N   . LEU A 1 1168 ? 30.001  1.333   -28.673 1.00 146.73 ? 1168 LEU A N   1 
ATOM   8897  C  CA  . LEU A 1 1168 ? 30.039  -0.117  -28.860 1.00 143.39 ? 1168 LEU A CA  1 
ATOM   8898  C  C   . LEU A 1 1168 ? 30.699  -0.536  -30.180 1.00 149.74 ? 1168 LEU A C   1 
ATOM   8899  O  O   . LEU A 1 1168 ? 31.360  -1.578  -30.262 1.00 150.94 ? 1168 LEU A O   1 
ATOM   8900  C  CB  . LEU A 1 1168 ? 28.641  -0.709  -28.747 1.00 137.08 ? 1168 LEU A CB  1 
ATOM   8901  C  CG  . LEU A 1 1168 ? 28.624  -1.849  -27.729 1.00 133.63 ? 1168 LEU A CG  1 
ATOM   8902  C  CD1 . LEU A 1 1168 ? 27.197  -2.229  -27.376 1.00 132.61 ? 1168 LEU A CD1 1 
ATOM   8903  C  CD2 . LEU A 1 1168 ? 29.442  -3.050  -28.203 1.00 131.00 ? 1168 LEU A CD2 1 
ATOM   8904  N  N   . ILE A 1 1169 ? 30.506  0.297   -31.199 1.00 144.24 ? 1169 ILE A N   1 
ATOM   8905  C  CA  . ILE A 1 1169 ? 31.045  0.095   -32.537 1.00 143.63 ? 1169 ILE A CA  1 
ATOM   8906  C  C   . ILE A 1 1169 ? 32.475  0.583   -32.612 1.00 145.99 ? 1169 ILE A C   1 
ATOM   8907  O  O   . ILE A 1 1169 ? 33.351  -0.135  -33.069 1.00 145.86 ? 1169 ILE A O   1 
ATOM   8908  C  CB  . ILE A 1 1169 ? 30.219  0.863   -33.558 1.00 143.94 ? 1169 ILE A CB  1 
ATOM   8909  C  CG1 . ILE A 1 1169 ? 28.902  0.135   -33.803 1.00 140.14 ? 1169 ILE A CG1 1 
ATOM   8910  C  CG2 . ILE A 1 1169 ? 30.992  1.026   -34.834 1.00 146.89 ? 1169 ILE A CG2 1 
ATOM   8911  C  CD1 . ILE A 1 1169 ? 27.697  1.009   -33.642 1.00 139.70 ? 1169 ILE A CD1 1 
ATOM   8912  N  N   . LYS A 1 1170 ? 32.715  1.806   -32.153 1.00 200.10 ? 1170 LYS A N   1 
ATOM   8913  C  CA  . LYS A 1 1170 ? 34.077  2.301   -32.054 1.00 204.88 ? 1170 LYS A CA  1 
ATOM   8914  C  C   . LYS A 1 1170 ? 34.905  1.167   -31.492 1.00 199.80 ? 1170 LYS A C   1 
ATOM   8915  O  O   . LYS A 1 1170 ? 36.077  1.024   -31.814 1.00 199.78 ? 1170 LYS A O   1 
ATOM   8916  C  CB  . LYS A 1 1170 ? 34.166  3.501   -31.110 1.00 212.00 ? 1170 LYS A CB  1 
ATOM   8917  C  CG  . LYS A 1 1170 ? 33.481  4.765   -31.604 1.00 221.17 ? 1170 LYS A CG  1 
ATOM   8918  C  CD  . LYS A 1 1170 ? 34.093  5.255   -32.907 1.00 231.41 ? 1170 LYS A CD  1 
ATOM   8919  C  CE  . LYS A 1 1170 ? 35.552  5.652   -32.729 1.00 238.85 ? 1170 LYS A CE  1 
ATOM   8920  N  NZ  . LYS A 1 1170 ? 36.179  6.048   -34.020 1.00 244.03 ? 1170 LYS A NZ  1 
ATOM   8921  N  N   . ALA A 1 1171 ? 34.273  0.352   -30.655 1.00 166.17 ? 1171 ALA A N   1 
ATOM   8922  C  CA  . ALA A 1 1171 ? 34.958  -0.734  -29.968 1.00 166.23 ? 1171 ALA A CA  1 
ATOM   8923  C  C   . ALA A 1 1171 ? 35.139  -1.954  -30.851 1.00 166.52 ? 1171 ALA A C   1 
ATOM   8924  O  O   . ALA A 1 1171 ? 36.258  -2.413  -31.074 1.00 168.00 ? 1171 ALA A O   1 
ATOM   8925  C  CB  . ALA A 1 1171 ? 34.204  -1.113  -28.727 1.00 164.91 ? 1171 ALA A CB  1 
ATOM   8926  N  N   . ASP A 1 1172 ? 34.033  -2.489  -31.347 1.00 189.86 ? 1172 ASP A N   1 
ATOM   8927  C  CA  . ASP A 1 1172 ? 34.114  -3.631  -32.240 1.00 190.50 ? 1172 ASP A CA  1 
ATOM   8928  C  C   . ASP A 1 1172 ? 35.100  -3.340  -33.386 1.00 193.86 ? 1172 ASP A C   1 
ATOM   8929  O  O   . ASP A 1 1172 ? 35.863  -4.210  -33.802 1.00 193.29 ? 1172 ASP A O   1 
ATOM   8930  C  CB  . ASP A 1 1172 ? 32.714  -4.017  -32.751 1.00 191.62 ? 1172 ASP A CB  1 
ATOM   8931  C  CG  . ASP A 1 1172 ? 31.908  -4.830  -31.725 1.00 191.15 ? 1172 ASP A CG  1 
ATOM   8932  O  OD1 . ASP A 1 1172 ? 32.267  -4.817  -30.530 1.00 190.09 ? 1172 ASP A OD1 1 
ATOM   8933  O  OD2 . ASP A 1 1172 ? 30.915  -5.489  -32.113 1.00 192.23 ? 1172 ASP A OD2 1 
ATOM   8934  N  N   . ASN A 1 1173 ? 35.109  -2.099  -33.862 1.00 209.93 ? 1173 ASN A N   1 
ATOM   8935  C  CA  . ASN A 1 1173 ? 36.007  -1.704  -34.942 1.00 215.20 ? 1173 ASN A CA  1 
ATOM   8936  C  C   . ASN A 1 1173 ? 37.457  -1.942  -34.625 1.00 214.19 ? 1173 ASN A C   1 
ATOM   8937  O  O   . ASN A 1 1173 ? 38.139  -2.655  -35.349 1.00 215.79 ? 1173 ASN A O   1 
ATOM   8938  C  CB  . ASN A 1 1173 ? 35.824  -0.236  -35.299 1.00 222.99 ? 1173 ASN A CB  1 
ATOM   8939  C  CG  . ASN A 1 1173 ? 34.728  -0.027  -36.306 1.00 229.95 ? 1173 ASN A CG  1 
ATOM   8940  O  OD1 . ASN A 1 1173 ? 34.914  0.651   -37.316 1.00 236.28 ? 1173 ASN A OD1 1 
ATOM   8941  N  ND2 . ASN A 1 1173 ? 33.573  -0.628  -36.049 1.00 228.17 ? 1173 ASN A ND2 1 
ATOM   8942  N  N   . PHE A 1 1174 ? 37.930  -1.320  -33.553 1.00 198.57 ? 1174 PHE A N   1 
ATOM   8943  C  CA  . PHE A 1 1174 ? 39.284  -1.558  -33.088 1.00 198.46 ? 1174 PHE A CA  1 
ATOM   8944  C  C   . PHE A 1 1174 ? 39.487  -3.051  -33.175 1.00 194.68 ? 1174 PHE A C   1 
ATOM   8945  O  O   . PHE A 1 1174 ? 40.522  -3.509  -33.648 1.00 197.96 ? 1174 PHE A O   1 
ATOM   8946  C  CB  . PHE A 1 1174 ? 39.445  -1.068  -31.639 1.00 196.70 ? 1174 PHE A CB  1 
ATOM   8947  C  CG  . PHE A 1 1174 ? 40.770  -1.430  -30.981 1.00 196.06 ? 1174 PHE A CG  1 
ATOM   8948  C  CD1 . PHE A 1 1174 ? 41.829  -0.531  -30.972 1.00 199.27 ? 1174 PHE A CD1 1 
ATOM   8949  C  CD2 . PHE A 1 1174 ? 40.929  -2.644  -30.317 1.00 193.55 ? 1174 PHE A CD2 1 
ATOM   8950  C  CE1 . PHE A 1 1174 ? 43.027  -0.853  -30.344 1.00 200.96 ? 1174 PHE A CE1 1 
ATOM   8951  C  CE2 . PHE A 1 1174 ? 42.126  -2.966  -29.688 1.00 194.78 ? 1174 PHE A CE2 1 
ATOM   8952  C  CZ  . PHE A 1 1174 ? 43.172  -2.069  -29.704 1.00 198.57 ? 1174 PHE A CZ  1 
ATOM   8953  N  N   . LEU A 1 1175 ? 38.471  -3.811  -32.776 1.00 195.62 ? 1175 LEU A N   1 
ATOM   8954  C  CA  . LEU A 1 1175 ? 38.639  -5.250  -32.653 1.00 193.89 ? 1175 LEU A CA  1 
ATOM   8955  C  C   . LEU A 1 1175 ? 38.961  -5.932  -33.976 1.00 195.28 ? 1175 LEU A C   1 
ATOM   8956  O  O   . LEU A 1 1175 ? 40.009  -6.562  -34.110 1.00 195.79 ? 1175 LEU A O   1 
ATOM   8957  C  CB  . LEU A 1 1175 ? 37.449  -5.893  -31.959 1.00 190.84 ? 1175 LEU A CB  1 
ATOM   8958  C  CG  . LEU A 1 1175 ? 37.586  -5.880  -30.438 1.00 189.21 ? 1175 LEU A CG  1 
ATOM   8959  C  CD1 . LEU A 1 1175 ? 36.487  -6.710  -29.837 1.00 185.76 ? 1175 LEU A CD1 1 
ATOM   8960  C  CD2 . LEU A 1 1175 ? 38.945  -6.404  -30.000 1.00 190.55 ? 1175 LEU A CD2 1 
ATOM   8961  N  N   . LEU A 1 1176 ? 38.087  -5.801  -34.962 1.00 175.27 ? 1176 LEU A N   1 
ATOM   8962  C  CA  . LEU A 1 1176 ? 38.407  -6.315  -36.287 1.00 178.10 ? 1176 LEU A CA  1 
ATOM   8963  C  C   . LEU A 1 1176 ? 39.754  -5.756  -36.747 1.00 187.25 ? 1176 LEU A C   1 
ATOM   8964  O  O   . LEU A 1 1176 ? 40.720  -6.500  -36.958 1.00 190.70 ? 1176 LEU A O   1 
ATOM   8965  C  CB  . LEU A 1 1176 ? 37.331  -5.857  -37.250 1.00 174.19 ? 1176 LEU A CB  1 
ATOM   8966  C  CG  . LEU A 1 1176 ? 35.991  -6.008  -36.550 1.00 166.68 ? 1176 LEU A CG  1 
ATOM   8967  C  CD1 . LEU A 1 1176 ? 34.977  -5.163  -37.256 1.00 166.56 ? 1176 LEU A CD1 1 
ATOM   8968  C  CD2 . LEU A 1 1176 ? 35.622  -7.472  -36.552 1.00 164.29 ? 1176 LEU A CD2 1 
ATOM   8969  N  N   . GLU A 1 1177 ? 39.797  -4.428  -36.854 1.00 214.97 ? 1177 GLU A N   1 
ATOM   8970  C  CA  . GLU A 1 1177 ? 40.935  -3.691  -37.390 1.00 222.23 ? 1177 GLU A CA  1 
ATOM   8971  C  C   . GLU A 1 1177 ? 42.233  -3.898  -36.624 1.00 223.37 ? 1177 GLU A C   1 
ATOM   8972  O  O   . GLU A 1 1177 ? 43.213  -3.226  -36.912 1.00 229.16 ? 1177 GLU A O   1 
ATOM   8973  C  CB  . GLU A 1 1177 ? 40.623  -2.184  -37.458 1.00 228.26 ? 1177 GLU A CB  1 
ATOM   8974  C  CG  . GLU A 1 1177 ? 39.934  -1.712  -38.749 1.00 235.24 ? 1177 GLU A CG  1 
ATOM   8975  C  CD  . GLU A 1 1177 ? 40.040  -0.203  -38.985 1.00 243.60 ? 1177 GLU A CD  1 
ATOM   8976  O  OE1 . GLU A 1 1177 ? 40.164  0.219   -40.158 1.00 249.32 ? 1177 GLU A OE1 1 
ATOM   8977  O  OE2 . GLU A 1 1177 ? 40.005  0.562   -38.000 1.00 244.32 ? 1177 GLU A OE2 1 
ATOM   8978  N  N   . ASN A 1 1178 ? 42.255  -4.815  -35.663 1.00 194.41 ? 1178 ASN A N   1 
ATOM   8979  C  CA  . ASN A 1 1178 ? 43.467  -5.014  -34.871 1.00 192.83 ? 1178 ASN A CA  1 
ATOM   8980  C  C   . ASN A 1 1178 ? 43.696  -6.431  -34.319 1.00 188.80 ? 1178 ASN A C   1 
ATOM   8981  O  O   . ASN A 1 1178 ? 44.637  -6.636  -33.555 1.00 189.95 ? 1178 ASN A O   1 
ATOM   8982  C  CB  . ASN A 1 1178 ? 43.544  -3.996  -33.715 1.00 190.25 ? 1178 ASN A CB  1 
ATOM   8983  C  CG  . ASN A 1 1178 ? 44.514  -2.834  -33.986 1.00 192.54 ? 1178 ASN A CG  1 
ATOM   8984  O  OD1 . ASN A 1 1178 ? 45.726  -2.947  -33.772 1.00 194.58 ? 1178 ASN A OD1 1 
ATOM   8985  N  ND2 . ASN A 1 1178 ? 43.967  -1.700  -34.414 1.00 192.93 ? 1178 ASN A ND2 1 
ATOM   8986  N  N   . THR A 1 1179 ? 42.867  -7.407  -34.677 1.00 189.69 ? 1179 THR A N   1 
ATOM   8987  C  CA  . THR A 1 1179 ? 43.059  -8.739  -34.099 1.00 186.11 ? 1179 THR A CA  1 
ATOM   8988  C  C   . THR A 1 1179 ? 43.930  -9.669  -34.912 1.00 186.84 ? 1179 THR A C   1 
ATOM   8989  O  O   . THR A 1 1179 ? 44.746  -10.414 -34.373 1.00 186.16 ? 1179 THR A O   1 
ATOM   8990  C  CB  . THR A 1 1179 ? 41.752  -9.517  -33.960 1.00 168.50 ? 1179 THR A CB  1 
ATOM   8991  O  OG1 . THR A 1 1179 ? 40.746  -8.688  -33.389 1.00 166.83 ? 1179 THR A OG1 1 
ATOM   8992  C  CG2 . THR A 1 1179 ? 41.957  -10.750 -33.083 1.00 158.90 ? 1179 THR A CG2 1 
ATOM   8993  N  N   . LEU A 1 1180 ? 43.726  -9.654  -36.218 1.00 265.33 ? 1180 LEU A N   1 
ATOM   8994  C  CA  . LEU A 1 1180 ? 43.990  -10.858 -36.988 1.00 267.32 ? 1180 LEU A CA  1 
ATOM   8995  C  C   . LEU A 1 1180 ? 45.425  -11.311 -37.147 1.00 276.81 ? 1180 LEU A C   1 
ATOM   8996  O  O   . LEU A 1 1180 ? 45.686  -12.507 -37.122 1.00 278.22 ? 1180 LEU A O   1 
ATOM   8997  C  CB  . LEU A 1 1180 ? 43.228  -10.861 -38.306 1.00 264.07 ? 1180 LEU A CB  1 
ATOM   8998  C  CG  . LEU A 1 1180 ? 41.919  -11.603 -38.022 1.00 255.85 ? 1180 LEU A CG  1 
ATOM   8999  C  CD1 . LEU A 1 1180 ? 41.108  -11.844 -39.276 1.00 254.88 ? 1180 LEU A CD1 1 
ATOM   9000  C  CD2 . LEU A 1 1180 ? 42.234  -12.925 -37.327 1.00 253.51 ? 1180 LEU A CD2 1 
ATOM   9001  N  N   . PRO A 1 1181 ? 46.362  -10.376 -37.320 1.00 211.58 ? 1181 PRO A N   1 
ATOM   9002  C  CA  . PRO A 1 1181 ? 47.728  -10.871 -37.157 1.00 213.85 ? 1181 PRO A CA  1 
ATOM   9003  C  C   . PRO A 1 1181 ? 47.851  -11.430 -35.748 1.00 210.91 ? 1181 PRO A C   1 
ATOM   9004  O  O   . PRO A 1 1181 ? 48.476  -10.807 -34.894 1.00 210.54 ? 1181 PRO A O   1 
ATOM   9005  C  CB  . PRO A 1 1181 ? 48.573  -9.608  -37.303 1.00 215.34 ? 1181 PRO A CB  1 
ATOM   9006  C  CG  . PRO A 1 1181 ? 47.760  -8.731  -38.197 1.00 215.16 ? 1181 PRO A CG  1 
ATOM   9007  C  CD  . PRO A 1 1181 ? 46.317  -9.011  -37.869 1.00 211.33 ? 1181 PRO A CD  1 
ATOM   9008  N  N   . ALA A 1 1182 ? 47.251  -12.596 -35.519 1.00 210.33 ? 1182 ALA A N   1 
ATOM   9009  C  CA  . ALA A 1 1182 ? 47.054  -13.139 -34.181 1.00 205.56 ? 1182 ALA A CA  1 
ATOM   9010  C  C   . ALA A 1 1182 ? 48.351  -13.253 -33.390 1.00 210.65 ? 1182 ALA A C   1 
ATOM   9011  O  O   . ALA A 1 1182 ? 49.319  -13.830 -33.878 1.00 215.85 ? 1182 ALA A O   1 
ATOM   9012  C  CB  . ALA A 1 1182 ? 46.360  -14.493 -34.263 1.00 199.20 ? 1182 ALA A CB  1 
ATOM   9013  N  N   . GLN A 1 1183 ? 48.349  -12.695 -32.174 1.00 195.29 ? 1183 GLN A N   1 
ATOM   9014  C  CA  . GLN A 1 1183 ? 49.477  -12.761 -31.241 1.00 194.75 ? 1183 GLN A CA  1 
ATOM   9015  C  C   . GLN A 1 1183 ? 49.394  -13.968 -30.293 1.00 188.71 ? 1183 GLN A C   1 
ATOM   9016  O  O   . GLN A 1 1183 ? 50.411  -14.608 -30.004 1.00 191.91 ? 1183 GLN A O   1 
ATOM   9017  C  CB  . GLN A 1 1183 ? 49.553  -11.478 -30.423 1.00 196.79 ? 1183 GLN A CB  1 
ATOM   9018  C  CG  . GLN A 1 1183 ? 50.847  -11.337 -29.656 1.00 203.60 ? 1183 GLN A CG  1 
ATOM   9019  C  CD  . GLN A 1 1183 ? 52.026  -11.187 -30.587 1.00 210.66 ? 1183 GLN A CD  1 
ATOM   9020  O  OE1 . GLN A 1 1183 ? 51.845  -11.083 -31.796 1.00 211.76 ? 1183 GLN A OE1 1 
ATOM   9021  N  NE2 . GLN A 1 1183 ? 53.239  -11.168 -30.036 1.00 214.88 ? 1183 GLN A NE2 1 
ATOM   9022  N  N   . SER A 1 1184 ? 48.179  -14.269 -29.819 1.00 179.07 ? 1184 SER A N   1 
ATOM   9023  C  CA  . SER A 1 1184 ? 47.909  -15.473 -29.014 1.00 175.94 ? 1184 SER A CA  1 
ATOM   9024  C  C   . SER A 1 1184 ? 46.468  -16.020 -29.093 1.00 170.30 ? 1184 SER A C   1 
ATOM   9025  O  O   . SER A 1 1184 ? 45.514  -15.269 -29.306 1.00 166.80 ? 1184 SER A O   1 
ATOM   9026  C  CB  . SER A 1 1184 ? 48.282  -15.258 -27.550 1.00 177.54 ? 1184 SER A CB  1 
ATOM   9027  O  OG  . SER A 1 1184 ? 47.842  -16.359 -26.772 1.00 175.97 ? 1184 SER A OG  1 
ATOM   9028  N  N   . THR A 1 1185 ? 46.337  -17.335 -28.904 1.00 141.93 ? 1185 THR A N   1 
ATOM   9029  C  CA  . THR A 1 1185 ? 45.058  -18.039 -28.979 1.00 137.14 ? 1185 THR A CA  1 
ATOM   9030  C  C   . THR A 1 1185 ? 44.082  -17.459 -27.979 1.00 133.49 ? 1185 THR A C   1 
ATOM   9031  O  O   . THR A 1 1185 ? 42.890  -17.257 -28.261 1.00 128.15 ? 1185 THR A O   1 
ATOM   9032  C  CB  . THR A 1 1185 ? 45.221  -19.539 -28.611 1.00 136.97 ? 1185 THR A CB  1 
ATOM   9033  O  OG1 . THR A 1 1185 ? 46.021  -20.206 -29.587 1.00 139.25 ? 1185 THR A OG1 1 
ATOM   9034  C  CG2 . THR A 1 1185 ? 43.867  -20.239 -28.512 1.00 132.82 ? 1185 THR A CG2 1 
ATOM   9035  N  N   . PHE A 1 1186 ? 44.608  -17.231 -26.784 1.00 196.36 ? 1186 PHE A N   1 
ATOM   9036  C  CA  . PHE A 1 1186 ? 43.859  -16.604 -25.714 1.00 193.34 ? 1186 PHE A CA  1 
ATOM   9037  C  C   . PHE A 1 1186 ? 43.387  -15.254 -26.244 1.00 194.16 ? 1186 PHE A C   1 
ATOM   9038  O  O   . PHE A 1 1186 ? 42.186  -15.004 -26.274 1.00 192.88 ? 1186 PHE A O   1 
ATOM   9039  C  CB  . PHE A 1 1186 ? 44.756  -16.461 -24.476 1.00 191.89 ? 1186 PHE A CB  1 
ATOM   9040  C  CG  . PHE A 1 1186 ? 44.108  -15.777 -23.309 1.00 187.68 ? 1186 PHE A CG  1 
ATOM   9041  C  CD1 . PHE A 1 1186 ? 43.201  -16.447 -22.509 1.00 185.25 ? 1186 PHE A CD1 1 
ATOM   9042  C  CD2 . PHE A 1 1186 ? 44.436  -14.464 -22.996 1.00 187.53 ? 1186 PHE A CD2 1 
ATOM   9043  C  CE1 . PHE A 1 1186 ? 42.617  -15.810 -21.436 1.00 183.01 ? 1186 PHE A CE1 1 
ATOM   9044  C  CE2 . PHE A 1 1186 ? 43.859  -13.827 -21.921 1.00 185.78 ? 1186 PHE A CE2 1 
ATOM   9045  C  CZ  . PHE A 1 1186 ? 42.947  -14.501 -21.140 1.00 183.60 ? 1186 PHE A CZ  1 
ATOM   9046  N  N   . THR A 1 1187 ? 44.314  -14.420 -26.728 1.00 140.15 ? 1187 THR A N   1 
ATOM   9047  C  CA  . THR A 1 1187 ? 43.963  -13.081 -27.211 1.00 137.29 ? 1187 THR A CA  1 
ATOM   9048  C  C   . THR A 1 1187 ? 42.775  -13.155 -28.145 1.00 133.86 ? 1187 THR A C   1 
ATOM   9049  O  O   . THR A 1 1187 ? 41.731  -12.513 -27.957 1.00 130.98 ? 1187 THR A O   1 
ATOM   9050  C  CB  . THR A 1 1187 ? 45.062  -12.467 -28.079 1.00 139.34 ? 1187 THR A CB  1 
ATOM   9051  O  OG1 . THR A 1 1187 ? 46.352  -12.713 -27.510 1.00 141.23 ? 1187 THR A OG1 1 
ATOM   9052  C  CG2 . THR A 1 1187 ? 44.813  -10.965 -28.248 1.00 138.78 ? 1187 THR A CG2 1 
ATOM   9053  N  N   . LEU A 1 1188 ? 42.990  -13.946 -29.183 1.00 159.31 ? 1188 LEU A N   1 
ATOM   9054  C  CA  . LEU A 1 1188 ? 42.057  -14.121 -30.266 1.00 157.59 ? 1188 LEU A CA  1 
ATOM   9055  C  C   . LEU A 1 1188 ? 40.682  -14.368 -29.716 1.00 153.52 ? 1188 LEU A C   1 
ATOM   9056  O  O   . LEU A 1 1188 ? 39.721  -13.693 -30.067 1.00 151.84 ? 1188 LEU A O   1 
ATOM   9057  C  CB  . LEU A 1 1188 ? 42.492  -15.353 -31.035 1.00 159.33 ? 1188 LEU A CB  1 
ATOM   9058  C  CG  . LEU A 1 1188 ? 42.192  -15.298 -32.513 1.00 155.90 ? 1188 LEU A CG  1 
ATOM   9059  C  CD1 . LEU A 1 1188 ? 42.455  -13.887 -32.997 1.00 155.47 ? 1188 LEU A CD1 1 
ATOM   9060  C  CD2 . LEU A 1 1188 ? 43.073  -16.315 -33.216 1.00 156.81 ? 1188 LEU A CD2 1 
ATOM   9061  N  N   . ALA A 1 1189 ? 40.642  -15.328 -28.802 1.00 141.22 ? 1189 ALA A N   1 
ATOM   9062  C  CA  . ALA A 1 1189 ? 39.430  -16.019 -28.397 1.00 141.35 ? 1189 ALA A CA  1 
ATOM   9063  C  C   . ALA A 1 1189 ? 38.397  -15.114 -27.745 1.00 137.60 ? 1189 ALA A C   1 
ATOM   9064  O  O   . ALA A 1 1189 ? 37.188  -15.322 -27.903 1.00 133.80 ? 1189 ALA A O   1 
ATOM   9065  C  CB  . ALA A 1 1189 ? 39.782  -17.174 -27.475 1.00 141.97 ? 1189 ALA A CB  1 
ATOM   9066  N  N   . ILE A 1 1190 ? 38.861  -14.122 -26.994 1.00 170.33 ? 1190 ILE A N   1 
ATOM   9067  C  CA  . ILE A 1 1190 ? 37.943  -13.160 -26.398 1.00 169.89 ? 1190 ILE A CA  1 
ATOM   9068  C  C   . ILE A 1 1190 ? 37.506  -12.198 -27.497 1.00 169.63 ? 1190 ILE A C   1 
ATOM   9069  O  O   . ILE A 1 1190 ? 36.318  -11.889 -27.621 1.00 167.17 ? 1190 ILE A O   1 
ATOM   9070  C  CB  . ILE A 1 1190 ? 38.549  -12.421 -25.171 1.00 169.45 ? 1190 ILE A CB  1 
ATOM   9071  C  CG1 . ILE A 1 1190 ? 38.862  -13.424 -24.054 1.00 169.76 ? 1190 ILE A CG1 1 
ATOM   9072  C  CG2 . ILE A 1 1190 ? 37.584  -11.379 -24.642 1.00 167.59 ? 1190 ILE A CG2 1 
ATOM   9073  C  CD1 . ILE A 1 1190 ? 39.377  -12.804 -22.774 1.00 171.00 ? 1190 ILE A CD1 1 
ATOM   9074  N  N   . SER A 1 1191 ? 38.460  -11.767 -28.322 1.00 143.03 ? 1191 SER A N   1 
ATOM   9075  C  CA  . SER A 1 1191 ? 38.137  -10.864 -29.413 1.00 141.31 ? 1191 SER A CA  1 
ATOM   9076  C  C   . SER A 1 1191 ? 37.106  -11.523 -30.311 1.00 138.52 ? 1191 SER A C   1 
ATOM   9077  O  O   . SER A 1 1191 ? 36.290  -10.863 -30.955 1.00 136.15 ? 1191 SER A O   1 
ATOM   9078  C  CB  . SER A 1 1191 ? 39.374  -10.521 -30.217 1.00 143.95 ? 1191 SER A CB  1 
ATOM   9079  O  OG  . SER A 1 1191 ? 39.082  -9.420  -31.048 1.00 144.83 ? 1191 SER A OG  1 
ATOM   9080  N  N   . ALA A 1 1192 ? 37.171  -12.848 -30.340 1.00 116.75 ? 1192 ALA A N   1 
ATOM   9081  C  CA  . ALA A 1 1192 ? 36.218  -13.693 -31.054 1.00 114.14 ? 1192 ALA A CA  1 
ATOM   9082  C  C   . ALA A 1 1192 ? 34.873  -13.631 -30.383 1.00 115.63 ? 1192 ALA A C   1 
ATOM   9083  O  O   . ALA A 1 1192 ? 33.890  -13.105 -30.919 1.00 116.86 ? 1192 ALA A O   1 
ATOM   9084  C  CB  . ALA A 1 1192 ? 36.702  -15.147 -31.023 1.00 111.83 ? 1192 ALA A CB  1 
ATOM   9085  N  N   . TYR A 1 1193 ? 34.849  -14.205 -29.194 1.00 135.08 ? 1193 TYR A N   1 
ATOM   9086  C  CA  . TYR A 1 1193 ? 33.620  -14.354 -28.490 1.00 132.60 ? 1193 TYR A CA  1 
ATOM   9087  C  C   . TYR A 1 1193 ? 32.883  -13.008 -28.397 1.00 132.14 ? 1193 TYR A C   1 
ATOM   9088  O  O   . TYR A 1 1193 ? 31.657  -12.983 -28.371 1.00 132.99 ? 1193 TYR A O   1 
ATOM   9089  C  CB  . TYR A 1 1193 ? 33.862  -15.011 -27.129 1.00 132.10 ? 1193 TYR A CB  1 
ATOM   9090  C  CG  . TYR A 1 1193 ? 32.592  -15.068 -26.326 1.00 129.88 ? 1193 TYR A CG  1 
ATOM   9091  C  CD1 . TYR A 1 1193 ? 31.574  -15.937 -26.665 1.00 130.60 ? 1193 TYR A CD1 1 
ATOM   9092  C  CD2 . TYR A 1 1193 ? 32.376  -14.201 -25.260 1.00 127.62 ? 1193 TYR A CD2 1 
ATOM   9093  C  CE1 . TYR A 1 1193 ? 30.381  -15.960 -25.941 1.00 129.46 ? 1193 TYR A CE1 1 
ATOM   9094  C  CE2 . TYR A 1 1193 ? 31.188  -14.215 -24.538 1.00 126.69 ? 1193 TYR A CE2 1 
ATOM   9095  C  CZ  . TYR A 1 1193 ? 30.198  -15.097 -24.881 1.00 126.61 ? 1193 TYR A CZ  1 
ATOM   9096  O  OH  . TYR A 1 1193 ? 29.028  -15.100 -24.156 1.00 123.37 ? 1193 TYR A OH  1 
ATOM   9097  N  N   . ALA A 1 1194 ? 33.620  -11.895 -28.409 1.00 175.09 ? 1194 ALA A N   1 
ATOM   9098  C  CA  . ALA A 1 1194 ? 33.033  -10.550 -28.242 1.00 173.44 ? 1194 ALA A CA  1 
ATOM   9099  C  C   . ALA A 1 1194 ? 32.369  -9.951  -29.494 1.00 171.17 ? 1194 ALA A C   1 
ATOM   9100  O  O   . ALA A 1 1194 ? 31.310  -9.317  -29.412 1.00 169.80 ? 1194 ALA A O   1 
ATOM   9101  C  CB  . ALA A 1 1194 ? 34.080  -9.593  -27.712 1.00 175.55 ? 1194 ALA A CB  1 
ATOM   9102  N  N   . LEU A 1 1195 ? 33.004  -10.131 -30.646 1.00 137.53 ? 1195 LEU A N   1 
ATOM   9103  C  CA  . LEU A 1 1195 ? 32.340  -9.831  -31.893 1.00 136.86 ? 1195 LEU A CA  1 
ATOM   9104  C  C   . LEU A 1 1195 ? 31.125  -10.725 -31.928 1.00 136.96 ? 1195 LEU A C   1 
ATOM   9105  O  O   . LEU A 1 1195 ? 30.049  -10.283 -32.322 1.00 138.12 ? 1195 LEU A O   1 
ATOM   9106  C  CB  . LEU A 1 1195 ? 33.270  -10.142 -33.034 1.00 136.25 ? 1195 LEU A CB  1 
ATOM   9107  C  CG  . LEU A 1 1195 ? 34.547  -9.450  -32.603 1.00 139.11 ? 1195 LEU A CG  1 
ATOM   9108  C  CD1 . LEU A 1 1195 ? 35.740  -9.834  -33.436 1.00 141.51 ? 1195 LEU A CD1 1 
ATOM   9109  C  CD2 . LEU A 1 1195 ? 34.349  -7.941  -32.602 1.00 139.63 ? 1195 LEU A CD2 1 
ATOM   9110  N  N   . SER A 1 1196 ? 31.304  -11.971 -31.470 1.00 80.03  ? 1196 SER A N   1 
ATOM   9111  C  CA  . SER A 1 1196 ? 30.227  -12.978 -31.354 1.00 80.94  ? 1196 SER A CA  1 
ATOM   9112  C  C   . SER A 1 1196 ? 28.937  -12.440 -30.721 1.00 83.03  ? 1196 SER A C   1 
ATOM   9113  O  O   . SER A 1 1196 ? 27.815  -12.867 -31.035 1.00 80.24  ? 1196 SER A O   1 
ATOM   9114  C  CB  . SER A 1 1196 ? 30.718  -14.223 -30.578 1.00 80.34  ? 1196 SER A CB  1 
ATOM   9115  O  OG  . SER A 1 1196 ? 29.784  -15.292 -30.655 1.00 80.41  ? 1196 SER A OG  1 
ATOM   9116  N  N   . LEU A 1 1197 ? 29.096  -11.478 -29.833 1.00 170.15 ? 1197 LEU A N   1 
ATOM   9117  C  CA  . LEU A 1 1197 ? 27.928  -10.924 -29.170 1.00 178.56 ? 1197 LEU A CA  1 
ATOM   9118  C  C   . LEU A 1 1197 ? 27.443  -9.676  -29.896 1.00 184.76 ? 1197 LEU A C   1 
ATOM   9119  O  O   . LEU A 1 1197 ? 26.843  -8.775  -29.305 1.00 184.72 ? 1197 LEU A O   1 
ATOM   9120  C  CB  . LEU A 1 1197 ? 28.216  -10.691 -27.687 1.00 181.31 ? 1197 LEU A CB  1 
ATOM   9121  C  CG  . LEU A 1 1197 ? 28.621  -11.956 -26.905 1.00 184.04 ? 1197 LEU A CG  1 
ATOM   9122  C  CD1 . LEU A 1 1197 ? 29.192  -11.610 -25.535 1.00 186.55 ? 1197 LEU A CD1 1 
ATOM   9123  C  CD2 . LEU A 1 1197 ? 27.476  -12.975 -26.776 1.00 183.64 ? 1197 LEU A CD2 1 
ATOM   9124  N  N   . GLY A 1 1198 ? 27.681  -9.659  -31.200 1.00 200.87 ? 1198 GLY A N   1 
ATOM   9125  C  CA  . GLY A 1 1198 ? 27.285  -8.533  -32.020 1.00 207.50 ? 1198 GLY A CA  1 
ATOM   9126  C  C   . GLY A 1 1198 ? 26.951  -8.928  -33.449 1.00 211.29 ? 1198 GLY A C   1 
ATOM   9127  O  O   . GLY A 1 1198 ? 26.193  -9.882  -33.682 1.00 213.40 ? 1198 GLY A O   1 
ATOM   9128  N  N   . ASP A 1 1199 ? 27.493  -8.166  -34.404 1.00 227.48 ? 1199 ASP A N   1 
ATOM   9129  C  CA  . ASP A 1 1199 ? 27.376  -8.493  -35.821 1.00 225.42 ? 1199 ASP A CA  1 
ATOM   9130  C  C   . ASP A 1 1199 ? 28.260  -9.667  -36.165 1.00 216.99 ? 1199 ASP A C   1 
ATOM   9131  O  O   . ASP A 1 1199 ? 29.450  -9.532  -36.460 1.00 217.47 ? 1199 ASP A O   1 
ATOM   9132  C  CB  . ASP A 1 1199 ? 27.739  -7.326  -36.727 1.00 232.75 ? 1199 ASP A CB  1 
ATOM   9133  C  CG  . ASP A 1 1199 ? 27.644  -7.703  -38.177 1.00 239.69 ? 1199 ASP A CG  1 
ATOM   9134  O  OD1 . ASP A 1 1199 ? 27.184  -8.831  -38.439 1.00 238.91 ? 1199 ASP A OD1 1 
ATOM   9135  O  OD2 . ASP A 1 1199 ? 28.018  -6.894  -39.048 1.00 245.55 ? 1199 ASP A OD2 1 
ATOM   9136  N  N   . LYS A 1 1200 ? 27.641  -10.827 -36.138 1.00 179.48 ? 1200 LYS A N   1 
ATOM   9137  C  CA  . LYS A 1 1200 ? 28.344  -12.063 -36.288 1.00 175.14 ? 1200 LYS A CA  1 
ATOM   9138  C  C   . LYS A 1 1200 ? 28.594  -12.314 -37.749 1.00 180.73 ? 1200 LYS A C   1 
ATOM   9139  O  O   . LYS A 1 1200 ? 28.963  -13.418 -38.119 1.00 185.77 ? 1200 LYS A O   1 
ATOM   9140  C  CB  . LYS A 1 1200 ? 27.466  -13.159 -35.718 1.00 169.04 ? 1200 LYS A CB  1 
ATOM   9141  C  CG  . LYS A 1 1200 ? 26.104  -12.626 -35.302 1.00 169.90 ? 1200 LYS A CG  1 
ATOM   9142  C  CD  . LYS A 1 1200 ? 25.575  -13.412 -34.144 1.00 171.60 ? 1200 LYS A CD  1 
ATOM   9143  C  CE  . LYS A 1 1200 ? 25.460  -14.868 -34.536 1.00 173.79 ? 1200 LYS A CE  1 
ATOM   9144  N  NZ  . LYS A 1 1200 ? 24.901  -15.654 -33.422 1.00 173.05 ? 1200 LYS A NZ  1 
ATOM   9145  N  N   . THR A 1 1201 ? 28.390  -11.300 -38.587 1.00 219.39 ? 1201 THR A N   1 
ATOM   9146  C  CA  . THR A 1 1201 ? 28.470  -11.504 -40.041 1.00 218.72 ? 1201 THR A CA  1 
ATOM   9147  C  C   . THR A 1 1201 ? 29.494  -10.660 -40.794 1.00 222.72 ? 1201 THR A C   1 
ATOM   9148  O  O   . THR A 1 1201 ? 29.623  -10.791 -42.014 1.00 225.32 ? 1201 THR A O   1 
ATOM   9149  C  CB  . THR A 1 1201 ? 27.127  -11.273 -40.733 1.00 216.88 ? 1201 THR A CB  1 
ATOM   9150  O  OG1 . THR A 1 1201 ? 26.580  -10.025 -40.293 1.00 215.73 ? 1201 THR A OG1 1 
ATOM   9151  C  CG2 . THR A 1 1201 ? 26.167  -12.401 -40.426 1.00 213.14 ? 1201 THR A CG2 1 
ATOM   9152  N  N   . HIS A 1 1202 ? 30.207  -9.786  -40.089 1.00 174.63 ? 1202 HIS A N   1 
ATOM   9153  C  CA  . HIS A 1 1202 ? 31.284  -9.046  -40.730 1.00 180.96 ? 1202 HIS A CA  1 
ATOM   9154  C  C   . HIS A 1 1202 ? 32.247  -10.031 -41.351 1.00 185.77 ? 1202 HIS A C   1 
ATOM   9155  O  O   . HIS A 1 1202 ? 32.908  -10.797 -40.656 1.00 184.62 ? 1202 HIS A O   1 
ATOM   9156  C  CB  . HIS A 1 1202 ? 32.048  -8.162  -39.750 1.00 179.21 ? 1202 HIS A CB  1 
ATOM   9157  C  CG  . HIS A 1 1202 ? 32.870  -7.110  -40.425 1.00 184.16 ? 1202 HIS A CG  1 
ATOM   9158  N  ND1 . HIS A 1 1202 ? 32.643  -5.765  -40.246 1.00 186.48 ? 1202 HIS A ND1 1 
ATOM   9159  C  CD2 . HIS A 1 1202 ? 33.885  -7.211  -41.314 1.00 187.12 ? 1202 HIS A CD2 1 
ATOM   9160  C  CE1 . HIS A 1 1202 ? 33.502  -5.077  -40.980 1.00 188.86 ? 1202 HIS A CE1 1 
ATOM   9161  N  NE2 . HIS A 1 1202 ? 34.267  -5.931  -41.634 1.00 190.47 ? 1202 HIS A NE2 1 
ATOM   9162  N  N   . PRO A 1 1203 ? 32.335  -10.004 -42.671 1.00 163.06 ? 1203 PRO A N   1 
ATOM   9163  C  CA  . PRO A 1 1203 ? 33.284  -10.865 -43.354 1.00 165.35 ? 1203 PRO A CA  1 
ATOM   9164  C  C   . PRO A 1 1203 ? 34.457  -11.046 -42.431 1.00 162.73 ? 1203 PRO A C   1 
ATOM   9165  O  O   . PRO A 1 1203 ? 34.793  -12.153 -42.052 1.00 162.69 ? 1203 PRO A O   1 
ATOM   9166  C  CB  . PRO A 1 1203 ? 33.707  -10.005 -44.537 1.00 172.04 ? 1203 PRO A CB  1 
ATOM   9167  C  CG  . PRO A 1 1203 ? 32.464  -9.228  -44.863 1.00 171.72 ? 1203 PRO A CG  1 
ATOM   9168  C  CD  . PRO A 1 1203 ? 31.789  -8.958  -43.548 1.00 165.95 ? 1203 PRO A CD  1 
ATOM   9169  N  N   . GLN A 1 1204 ? 35.042  -9.933  -42.028 1.00 158.17 ? 1204 GLN A N   1 
ATOM   9170  C  CA  . GLN A 1 1204 ? 36.224  -9.983  -41.209 1.00 152.94 ? 1204 GLN A CA  1 
ATOM   9171  C  C   . GLN A 1 1204 ? 36.095  -10.973 -40.045 1.00 143.81 ? 1204 GLN A C   1 
ATOM   9172  O  O   . GLN A 1 1204 ? 36.929  -11.861 -39.905 1.00 141.49 ? 1204 GLN A O   1 
ATOM   9173  C  CB  . GLN A 1 1204 ? 36.574  -8.586  -40.730 1.00 152.87 ? 1204 GLN A CB  1 
ATOM   9174  C  CG  . GLN A 1 1204 ? 37.846  -8.530  -39.964 1.00 151.58 ? 1204 GLN A CG  1 
ATOM   9175  C  CD  . GLN A 1 1204 ? 38.976  -9.145  -40.724 1.00 152.41 ? 1204 GLN A CD  1 
ATOM   9176  O  OE1 . GLN A 1 1204 ? 38.843  -9.473  -41.897 1.00 152.45 ? 1204 GLN A OE1 1 
ATOM   9177  N  NE2 . GLN A 1 1204 ? 40.104  -9.305  -40.063 1.00 153.34 ? 1204 GLN A NE2 1 
ATOM   9178  N  N   . PHE A 1 1205 ? 35.052  -10.838 -39.227 1.00 150.78 ? 1205 PHE A N   1 
ATOM   9179  C  CA  . PHE A 1 1205 ? 34.770  -11.802 -38.153 1.00 146.73 ? 1205 PHE A CA  1 
ATOM   9180  C  C   . PHE A 1 1205 ? 35.024  -13.212 -38.670 1.00 147.45 ? 1205 PHE A C   1 
ATOM   9181  O  O   . PHE A 1 1205 ? 35.626  -14.027 -37.970 1.00 147.51 ? 1205 PHE A O   1 
ATOM   9182  C  CB  . PHE A 1 1205 ? 33.310  -11.621 -37.660 1.00 133.54 ? 1205 PHE A CB  1 
ATOM   9183  C  CG  . PHE A 1 1205 ? 32.747  -12.768 -36.809 1.00 127.93 ? 1205 PHE A CG  1 
ATOM   9184  C  CD1 . PHE A 1 1205 ? 33.031  -12.877 -35.467 1.00 127.09 ? 1205 PHE A CD1 1 
ATOM   9185  C  CD2 . PHE A 1 1205 ? 31.863  -13.683 -37.353 1.00 124.25 ? 1205 PHE A CD2 1 
ATOM   9186  C  CE1 . PHE A 1 1205 ? 32.488  -13.903 -34.719 1.00 124.55 ? 1205 PHE A CE1 1 
ATOM   9187  C  CE2 . PHE A 1 1205 ? 31.321  -14.712 -36.592 1.00 121.24 ? 1205 PHE A CE2 1 
ATOM   9188  C  CZ  . PHE A 1 1205 ? 31.634  -14.820 -35.293 1.00 121.49 ? 1205 PHE A CZ  1 
ATOM   9189  N  N   . ARG A 1 1206 ? 34.609  -13.468 -39.915 1.00 133.20 ? 1206 ARG A N   1 
ATOM   9190  C  CA  . ARG A 1 1206 ? 34.777  -14.776 -40.541 1.00 135.13 ? 1206 ARG A CA  1 
ATOM   9191  C  C   . ARG A 1 1206 ? 36.252  -15.135 -40.568 1.00 136.47 ? 1206 ARG A C   1 
ATOM   9192  O  O   . ARG A 1 1206 ? 36.638  -16.288 -40.350 1.00 134.96 ? 1206 ARG A O   1 
ATOM   9193  C  CB  . ARG A 1 1206 ? 34.233  -14.770 -41.981 1.00 140.99 ? 1206 ARG A CB  1 
ATOM   9194  C  CG  . ARG A 1 1206 ? 32.829  -14.258 -42.135 1.00 144.56 ? 1206 ARG A CG  1 
ATOM   9195  C  CD  . ARG A 1 1206 ? 31.838  -15.399 -42.050 1.00 149.76 ? 1206 ARG A CD  1 
ATOM   9196  N  NE  . ARG A 1 1206 ? 30.441  -14.953 -42.041 1.00 153.57 ? 1206 ARG A NE  1 
ATOM   9197  C  CZ  . ARG A 1 1206 ? 29.950  -13.949 -42.773 1.00 158.41 ? 1206 ARG A CZ  1 
ATOM   9198  N  NH1 . ARG A 1 1206 ? 30.747  -13.255 -43.594 1.00 161.84 ? 1206 ARG A NH1 1 
ATOM   9199  N  NH2 . ARG A 1 1206 ? 28.650  -13.643 -42.688 1.00 157.12 ? 1206 ARG A NH2 1 
ATOM   9200  N  N   . SER A 1 1207 ? 37.072  -14.132 -40.860 1.00 152.74 ? 1207 SER A N   1 
ATOM   9201  C  CA  . SER A 1 1207 ? 38.507  -14.331 -40.964 1.00 153.47 ? 1207 SER A CA  1 
ATOM   9202  C  C   . SER A 1 1207 ? 39.051  -14.602 -39.569 1.00 149.35 ? 1207 SER A C   1 
ATOM   9203  O  O   . SER A 1 1207 ? 39.872  -15.497 -39.376 1.00 151.34 ? 1207 SER A O   1 
ATOM   9204  C  CB  . SER A 1 1207 ? 39.190  -13.112 -41.614 1.00 156.42 ? 1207 SER A CB  1 
ATOM   9205  O  OG  . SER A 1 1207 ? 40.479  -13.436 -42.149 1.00 159.15 ? 1207 SER A OG  1 
ATOM   9206  N  N   . ILE A 1 1208 ? 38.563  -13.848 -38.592 1.00 154.80 ? 1208 ILE A N   1 
ATOM   9207  C  CA  . ILE A 1 1208 ? 39.029  -14.013 -37.226 1.00 146.49 ? 1208 ILE A CA  1 
ATOM   9208  C  C   . ILE A 1 1208 ? 38.610  -15.394 -36.701 1.00 139.07 ? 1208 ILE A C   1 
ATOM   9209  O  O   . ILE A 1 1208 ? 39.449  -16.195 -36.254 1.00 137.02 ? 1208 ILE A O   1 
ATOM   9210  C  CB  . ILE A 1 1208 ? 38.513  -12.857 -36.331 1.00 142.18 ? 1208 ILE A CB  1 
ATOM   9211  C  CG1 . ILE A 1 1208 ? 38.174  -11.630 -37.201 1.00 140.46 ? 1208 ILE A CG1 1 
ATOM   9212  C  CG2 . ILE A 1 1208 ? 39.531  -12.516 -35.244 1.00 143.85 ? 1208 ILE A CG2 1 
ATOM   9213  C  CD1 . ILE A 1 1208 ? 37.900  -10.327 -36.440 1.00 137.70 ? 1208 ILE A CD1 1 
ATOM   9214  N  N   . VAL A 1 1209 ? 37.310  -15.666 -36.799 1.00 97.98  ? 1209 VAL A N   1 
ATOM   9215  C  CA  . VAL A 1 1209 ? 36.723  -16.958 -36.448 1.00 100.27 ? 1209 VAL A CA  1 
ATOM   9216  C  C   . VAL A 1 1209 ? 37.469  -18.089 -37.132 1.00 109.62 ? 1209 VAL A C   1 
ATOM   9217  O  O   . VAL A 1 1209 ? 37.604  -19.196 -36.608 1.00 109.72 ? 1209 VAL A O   1 
ATOM   9218  C  CB  . VAL A 1 1209 ? 35.243  -16.992 -36.899 1.00 98.41  ? 1209 VAL A CB  1 
ATOM   9219  C  CG1 . VAL A 1 1209 ? 34.605  -18.358 -36.645 1.00 96.99  ? 1209 VAL A CG1 1 
ATOM   9220  C  CG2 . VAL A 1 1209 ? 34.451  -15.888 -36.216 1.00 96.88  ? 1209 VAL A CG2 1 
ATOM   9221  N  N   . SER A 1 1210 ? 37.946  -17.789 -38.328 1.00 146.58 ? 1210 SER A N   1 
ATOM   9222  C  CA  . SER A 1 1210 ? 38.757  -18.724 -39.061 1.00 154.98 ? 1210 SER A CA  1 
ATOM   9223  C  C   . SER A 1 1210 ? 40.037  -18.952 -38.292 1.00 160.08 ? 1210 SER A C   1 
ATOM   9224  O  O   . SER A 1 1210 ? 40.371  -20.067 -37.917 1.00 161.95 ? 1210 SER A O   1 
ATOM   9225  C  CB  . SER A 1 1210 ? 39.104  -18.143 -40.427 1.00 160.25 ? 1210 SER A CB  1 
ATOM   9226  O  OG  . SER A 1 1210 ? 40.443  -17.657 -40.467 1.00 165.58 ? 1210 SER A OG  1 
ATOM   9227  N  N   . ALA A 1 1211 ? 40.745  -17.863 -38.054 1.00 182.24 ? 1211 ALA A N   1 
ATOM   9228  C  CA  . ALA A 1 1211 ? 42.039  -17.918 -37.417 1.00 183.77 ? 1211 ALA A CA  1 
ATOM   9229  C  C   . ALA A 1 1211 ? 41.972  -18.777 -36.166 1.00 179.94 ? 1211 ALA A C   1 
ATOM   9230  O  O   . ALA A 1 1211 ? 42.596  -19.837 -36.082 1.00 180.18 ? 1211 ALA A O   1 
ATOM   9231  C  CB  . ALA A 1 1211 ? 42.478  -16.522 -37.078 1.00 184.07 ? 1211 ALA A CB  1 
ATOM   9232  N  N   . LEU A 1 1212 ? 41.205  -18.309 -35.195 1.00 166.41 ? 1212 LEU A N   1 
ATOM   9233  C  CA  . LEU A 1 1212 ? 40.958  -19.086 -34.005 1.00 165.19 ? 1212 LEU A CA  1 
ATOM   9234  C  C   . LEU A 1 1212 ? 40.640  -20.523 -34.425 1.00 164.83 ? 1212 LEU A C   1 
ATOM   9235  O  O   . LEU A 1 1212 ? 41.356  -21.459 -34.052 1.00 166.98 ? 1212 LEU A O   1 
ATOM   9236  C  CB  . LEU A 1 1212 ? 39.791  -18.465 -33.231 1.00 159.66 ? 1212 LEU A CB  1 
ATOM   9237  C  CG  . LEU A 1 1212 ? 39.285  -19.247 -32.021 1.00 155.66 ? 1212 LEU A CG  1 
ATOM   9238  C  CD1 . LEU A 1 1212 ? 40.455  -19.604 -31.160 1.00 157.43 ? 1212 LEU A CD1 1 
ATOM   9239  C  CD2 . LEU A 1 1212 ? 38.246  -18.459 -31.234 1.00 152.15 ? 1212 LEU A CD2 1 
ATOM   9240  N  N   . LYS A 1 1213 ? 39.599  -20.684 -35.244 1.00 119.70 ? 1213 LYS A N   1 
ATOM   9241  C  CA  . LYS A 1 1213 ? 39.124  -22.008 -35.624 1.00 117.35 ? 1213 LYS A CA  1 
ATOM   9242  C  C   . LYS A 1 1213 ? 40.246  -22.799 -36.240 1.00 124.91 ? 1213 LYS A C   1 
ATOM   9243  O  O   . LYS A 1 1213 ? 40.284  -24.028 -36.150 1.00 125.11 ? 1213 LYS A O   1 
ATOM   9244  C  CB  . LYS A 1 1213 ? 37.994  -21.891 -36.619 1.00 110.10 ? 1213 LYS A CB  1 
ATOM   9245  C  CG  . LYS A 1 1213 ? 36.965  -22.908 -36.382 1.00 107.28 ? 1213 LYS A CG  1 
ATOM   9246  C  CD  . LYS A 1 1213 ? 35.657  -22.220 -36.149 1.00 105.49 ? 1213 LYS A CD  1 
ATOM   9247  C  CE  . LYS A 1 1213 ? 34.516  -23.176 -36.453 1.00 105.50 ? 1213 LYS A CE  1 
ATOM   9248  N  NZ  . LYS A 1 1213 ? 33.181  -22.665 -36.035 1.00 102.93 ? 1213 LYS A NZ  1 
ATOM   9249  N  N   . ARG A 1 1214 ? 41.143  -22.060 -36.879 1.00 207.05 ? 1214 ARG A N   1 
ATOM   9250  C  CA  . ARG A 1 1214 ? 42.359  -22.606 -37.432 1.00 220.21 ? 1214 ARG A CA  1 
ATOM   9251  C  C   . ARG A 1 1214 ? 43.171  -23.219 -36.305 1.00 222.24 ? 1214 ARG A C   1 
ATOM   9252  O  O   . ARG A 1 1214 ? 43.593  -24.367 -36.385 1.00 226.51 ? 1214 ARG A O   1 
ATOM   9253  C  CB  . ARG A 1 1214 ? 43.152  -21.500 -38.145 1.00 233.36 ? 1214 ARG A CB  1 
ATOM   9254  C  CG  . ARG A 1 1214 ? 44.661  -21.721 -38.195 1.00 249.46 ? 1214 ARG A CG  1 
ATOM   9255  C  CD  . ARG A 1 1214 ? 45.349  -20.813 -39.213 1.00 262.12 ? 1214 ARG A CD  1 
ATOM   9256  N  NE  . ARG A 1 1214 ? 44.963  -19.410 -39.081 1.00 266.58 ? 1214 ARG A NE  1 
ATOM   9257  C  CZ  . ARG A 1 1214 ? 44.955  -18.548 -40.091 1.00 272.60 ? 1214 ARG A CZ  1 
ATOM   9258  N  NH1 . ARG A 1 1214 ? 45.303  -18.955 -41.299 1.00 278.37 ? 1214 ARG A NH1 1 
ATOM   9259  N  NH2 . ARG A 1 1214 ? 44.593  -17.288 -39.902 1.00 271.58 ? 1214 ARG A NH2 1 
ATOM   9260  N  N   . GLU A 1 1215 ? 43.348  -22.469 -35.231 1.00 151.36 ? 1215 GLU A N   1 
ATOM   9261  C  CA  . GLU A 1 1215 ? 44.366  -22.813 -34.244 1.00 150.86 ? 1215 GLU A CA  1 
ATOM   9262  C  C   . GLU A 1 1215 ? 44.128  -24.047 -33.374 1.00 146.30 ? 1215 GLU A C   1 
ATOM   9263  O  O   . GLU A 1 1215 ? 45.079  -24.571 -32.781 1.00 149.66 ? 1215 GLU A O   1 
ATOM   9264  C  CB  . GLU A 1 1215 ? 44.657  -21.608 -33.362 1.00 148.60 ? 1215 GLU A CB  1 
ATOM   9265  C  CG  . GLU A 1 1215 ? 45.522  -20.574 -34.028 1.00 151.96 ? 1215 GLU A CG  1 
ATOM   9266  C  CD  . GLU A 1 1215 ? 46.989  -20.900 -33.909 1.00 158.58 ? 1215 GLU A CD  1 
ATOM   9267  O  OE1 . GLU A 1 1215 ? 47.317  -22.022 -33.458 1.00 160.77 ? 1215 GLU A OE1 1 
ATOM   9268  O  OE2 . GLU A 1 1215 ? 47.809  -20.026 -34.261 1.00 161.92 ? 1215 GLU A OE2 1 
ATOM   9269  N  N   . ALA A 1 1216 ? 42.881  -24.504 -33.301 1.00 147.97 ? 1216 ALA A N   1 
ATOM   9270  C  CA  . ALA A 1 1216 ? 42.524  -25.624 -32.436 1.00 141.97 ? 1216 ALA A CA  1 
ATOM   9271  C  C   . ALA A 1 1216 ? 43.484  -26.804 -32.589 1.00 143.79 ? 1216 ALA A C   1 
ATOM   9272  O  O   . ALA A 1 1216 ? 44.360  -26.786 -33.450 1.00 148.88 ? 1216 ALA A O   1 
ATOM   9273  C  CB  . ALA A 1 1216 ? 41.104  -26.069 -32.722 1.00 136.47 ? 1216 ALA A CB  1 
ATOM   9274  N  N   . LEU A 1 1217 ? 43.323  -27.815 -31.732 1.00 151.23 ? 1217 LEU A N   1 
ATOM   9275  C  CA  . LEU A 1 1217 ? 44.040  -29.093 -31.826 1.00 152.27 ? 1217 LEU A CA  1 
ATOM   9276  C  C   . LEU A 1 1217 ? 43.122  -30.100 -31.216 1.00 149.88 ? 1217 LEU A C   1 
ATOM   9277  O  O   . LEU A 1 1217 ? 41.997  -29.756 -30.865 1.00 141.80 ? 1217 LEU A O   1 
ATOM   9278  C  CB  . LEU A 1 1217 ? 45.321  -29.079 -31.021 1.00 153.68 ? 1217 LEU A CB  1 
ATOM   9279  C  CG  . LEU A 1 1217 ? 45.800  -27.656 -30.800 1.00 152.89 ? 1217 LEU A CG  1 
ATOM   9280  C  CD1 . LEU A 1 1217 ? 46.083  -27.492 -29.340 1.00 151.09 ? 1217 LEU A CD1 1 
ATOM   9281  C  CD2 . LEU A 1 1217 ? 47.007  -27.345 -31.674 1.00 158.48 ? 1217 LEU A CD2 1 
ATOM   9282  N  N   . VAL A 1 1218 ? 43.579  -31.338 -31.060 1.00 109.46 ? 1218 VAL A N   1 
ATOM   9283  C  CA  . VAL A 1 1218 ? 42.599  -32.385 -30.798 1.00 110.14 ? 1218 VAL A CA  1 
ATOM   9284  C  C   . VAL A 1 1218 ? 43.082  -33.808 -30.558 1.00 111.91 ? 1218 VAL A C   1 
ATOM   9285  O  O   . VAL A 1 1218 ? 44.223  -34.171 -30.878 1.00 112.03 ? 1218 VAL A O   1 
ATOM   9286  C  CB  . VAL A 1 1218 ? 41.721  -32.505 -31.975 1.00 114.82 ? 1218 VAL A CB  1 
ATOM   9287  C  CG1 . VAL A 1 1218 ? 40.475  -31.686 -31.800 1.00 110.56 ? 1218 VAL A CG1 1 
ATOM   9288  C  CG2 . VAL A 1 1218 ? 42.538  -32.061 -33.188 1.00 123.20 ? 1218 VAL A CG2 1 
ATOM   9289  N  N   . LYS A 1 1219 ? 42.136  -34.622 -30.075 1.00 146.09 ? 1219 LYS A N   1 
ATOM   9290  C  CA  . LYS A 1 1219 ? 42.413  -35.912 -29.432 1.00 159.44 ? 1219 LYS A CA  1 
ATOM   9291  C  C   . LYS A 1 1219 ? 41.629  -37.064 -30.055 1.00 166.33 ? 1219 LYS A C   1 
ATOM   9292  O  O   . LYS A 1 1219 ? 40.400  -37.110 -29.965 1.00 164.34 ? 1219 LYS A O   1 
ATOM   9293  C  CB  . LYS A 1 1219 ? 42.088  -35.835 -27.917 1.00 162.30 ? 1219 LYS A CB  1 
ATOM   9294  C  CG  . LYS A 1 1219 ? 43.266  -35.360 -26.965 1.00 227.97 ? 1219 LYS A CG  1 
ATOM   9295  C  CD  . LYS A 1 1219 ? 42.816  -34.996 -25.495 1.00 212.66 ? 1219 LYS A CD  1 
ATOM   9296  C  CE  . LYS A 1 1219 ? 43.981  -34.533 -24.595 1.00 198.78 ? 1219 LYS A CE  1 
ATOM   9297  N  NZ  . LYS A 1 1219 ? 43.524  -33.910 -23.319 1.00 195.79 ? 1219 LYS A NZ  1 
ATOM   9298  N  N   . GLY A 1 1220 ? 42.354  -38.011 -30.645 1.00 240.78 ? 1220 GLY A N   1 
ATOM   9299  C  CA  . GLY A 1 1220 ? 41.742  -39.152 -31.300 1.00 242.17 ? 1220 GLY A CA  1 
ATOM   9300  C  C   . GLY A 1 1220 ? 41.029  -38.761 -32.581 1.00 241.99 ? 1220 GLY A C   1 
ATOM   9301  O  O   . GLY A 1 1220 ? 40.369  -37.722 -32.640 1.00 239.20 ? 1220 GLY A O   1 
ATOM   9302  N  N   . ASN A 1 1221 ? 41.175  -39.591 -33.612 1.00 202.21 ? 1221 ASN A N   1 
ATOM   9303  C  CA  . ASN A 1 1221 ? 40.528  -39.367 -34.902 1.00 201.76 ? 1221 ASN A CA  1 
ATOM   9304  C  C   . ASN A 1 1221 ? 39.400  -40.381 -35.099 1.00 196.58 ? 1221 ASN A C   1 
ATOM   9305  O  O   . ASN A 1 1221 ? 39.505  -41.526 -34.675 1.00 198.74 ? 1221 ASN A O   1 
ATOM   9306  C  CB  . ASN A 1 1221 ? 41.554  -39.438 -36.045 1.00 209.38 ? 1221 ASN A CB  1 
ATOM   9307  C  CG  . ASN A 1 1221 ? 40.950  -39.137 -37.413 1.00 209.64 ? 1221 ASN A CG  1 
ATOM   9308  O  OD1 . ASN A 1 1221 ? 40.804  -40.030 -38.249 1.00 211.70 ? 1221 ASN A OD1 1 
ATOM   9309  N  ND2 . ASN A 1 1221 ? 40.611  -37.874 -37.650 1.00 206.98 ? 1221 ASN A ND2 1 
ATOM   9310  N  N   . PRO A 1 1222 ? 38.285  -39.938 -35.681 1.00 192.88 ? 1222 PRO A N   1 
ATOM   9311  C  CA  . PRO A 1 1222 ? 38.060  -38.515 -35.941 1.00 187.51 ? 1222 PRO A CA  1 
ATOM   9312  C  C   . PRO A 1 1222 ? 38.123  -37.752 -34.614 1.00 184.66 ? 1222 PRO A C   1 
ATOM   9313  O  O   . PRO A 1 1222 ? 38.225  -38.394 -33.572 1.00 186.90 ? 1222 PRO A O   1 
ATOM   9314  C  CB  . PRO A 1 1222 ? 36.633  -38.494 -36.496 1.00 184.30 ? 1222 PRO A CB  1 
ATOM   9315  C  CG  . PRO A 1 1222 ? 36.384  -39.904 -37.003 1.00 186.47 ? 1222 PRO A CG  1 
ATOM   9316  C  CD  . PRO A 1 1222 ? 37.134  -40.775 -36.060 1.00 189.43 ? 1222 PRO A CD  1 
ATOM   9317  N  N   . PRO A 1 1223 ? 38.086  -36.413 -34.642 1.00 209.15 ? 1223 PRO A N   1 
ATOM   9318  C  CA  . PRO A 1 1223 ? 37.997  -35.681 -33.377 1.00 200.34 ? 1223 PRO A CA  1 
ATOM   9319  C  C   . PRO A 1 1223 ? 37.027  -36.288 -32.317 1.00 192.54 ? 1223 PRO A C   1 
ATOM   9320  O  O   . PRO A 1 1223 ? 35.832  -36.457 -32.613 1.00 187.20 ? 1223 PRO A O   1 
ATOM   9321  C  CB  . PRO A 1 1223 ? 37.504  -34.302 -33.843 1.00 196.65 ? 1223 PRO A CB  1 
ATOM   9322  C  CG  . PRO A 1 1223 ? 38.158  -34.120 -35.172 1.00 202.11 ? 1223 PRO A CG  1 
ATOM   9323  C  CD  . PRO A 1 1223 ? 38.330  -35.502 -35.777 1.00 209.55 ? 1223 PRO A CD  1 
ATOM   9324  N  N   . ILE A 1 1224 ? 37.555  -36.622 -31.124 1.00 160.42 ? 1224 ILE A N   1 
ATOM   9325  C  CA  . ILE A 1 1224 ? 36.745  -36.865 -29.909 1.00 155.44 ? 1224 ILE A CA  1 
ATOM   9326  C  C   . ILE A 1 1224 ? 36.887  -35.709 -28.874 1.00 153.26 ? 1224 ILE A C   1 
ATOM   9327  O  O   . ILE A 1 1224 ? 35.921  -35.384 -28.163 1.00 150.44 ? 1224 ILE A O   1 
ATOM   9328  C  CB  . ILE A 1 1224 ? 37.020  -38.241 -29.208 1.00 155.78 ? 1224 ILE A CB  1 
ATOM   9329  C  CG1 . ILE A 1 1224 ? 37.220  -39.370 -30.191 1.00 161.06 ? 1224 ILE A CG1 1 
ATOM   9330  C  CG2 . ILE A 1 1224 ? 35.841  -38.651 -28.357 1.00 149.82 ? 1224 ILE A CG2 1 
ATOM   9331  C  CD1 . ILE A 1 1224 ? 36.926  -40.701 -29.555 1.00 164.35 ? 1224 ILE A CD1 1 
ATOM   9332  N  N   . TYR A 1 1225 ? 38.078  -35.098 -28.801 1.00 134.91 ? 1225 TYR A N   1 
ATOM   9333  C  CA  . TYR A 1 1225 ? 38.272  -33.904 -27.986 1.00 131.92 ? 1225 TYR A CA  1 
ATOM   9334  C  C   . TYR A 1 1225 ? 38.938  -32.785 -28.752 1.00 130.51 ? 1225 TYR A C   1 
ATOM   9335  O  O   . TYR A 1 1225 ? 40.004  -32.955 -29.326 1.00 133.53 ? 1225 TYR A O   1 
ATOM   9336  C  CB  . TYR A 1 1225 ? 39.124  -34.187 -26.760 1.00 136.18 ? 1225 TYR A CB  1 
ATOM   9337  C  CG  . TYR A 1 1225 ? 38.679  -35.348 -25.908 1.00 138.36 ? 1225 TYR A CG  1 
ATOM   9338  C  CD1 . TYR A 1 1225 ? 37.677  -35.205 -24.949 1.00 136.94 ? 1225 TYR A CD1 1 
ATOM   9339  C  CD2 . TYR A 1 1225 ? 39.284  -36.591 -26.042 1.00 143.17 ? 1225 TYR A CD2 1 
ATOM   9340  C  CE1 . TYR A 1 1225 ? 37.286  -36.283 -24.153 1.00 138.72 ? 1225 TYR A CE1 1 
ATOM   9341  C  CE2 . TYR A 1 1225 ? 38.903  -37.668 -25.253 1.00 145.14 ? 1225 TYR A CE2 1 
ATOM   9342  C  CZ  . TYR A 1 1225 ? 37.901  -37.511 -24.316 1.00 142.06 ? 1225 TYR A CZ  1 
ATOM   9343  O  OH  . TYR A 1 1225 ? 37.533  -38.598 -23.549 1.00 142.72 ? 1225 TYR A OH  1 
ATOM   9344  N  N   . ARG A 1 1226 ? 38.304  -31.626 -28.722 1.00 140.79 ? 1226 ARG A N   1 
ATOM   9345  C  CA  . ARG A 1 1226 ? 38.828  -30.436 -29.353 1.00 145.59 ? 1226 ARG A CA  1 
ATOM   9346  C  C   . ARG A 1 1226 ? 39.105  -29.426 -28.291 1.00 146.10 ? 1226 ARG A C   1 
ATOM   9347  O  O   . ARG A 1 1226 ? 38.297  -29.257 -27.402 1.00 144.23 ? 1226 ARG A O   1 
ATOM   9348  C  CB  . ARG A 1 1226 ? 37.781  -29.811 -30.256 1.00 147.27 ? 1226 ARG A CB  1 
ATOM   9349  C  CG  . ARG A 1 1226 ? 38.385  -28.758 -31.179 1.00 149.99 ? 1226 ARG A CG  1 
ATOM   9350  C  CD  . ARG A 1 1226 ? 37.397  -28.210 -32.242 1.00 147.06 ? 1226 ARG A CD  1 
ATOM   9351  N  NE  . ARG A 1 1226 ? 36.418  -29.154 -32.825 1.00 143.93 ? 1226 ARG A NE  1 
ATOM   9352  C  CZ  . ARG A 1 1226 ? 36.618  -29.948 -33.886 1.00 140.30 ? 1226 ARG A CZ  1 
ATOM   9353  N  NH1 . ARG A 1 1226 ? 37.802  -29.976 -34.518 1.00 139.90 ? 1226 ARG A NH1 1 
ATOM   9354  N  NH2 . ARG A 1 1226 ? 35.621  -30.729 -34.311 1.00 137.04 ? 1226 ARG A NH2 1 
ATOM   9355  N  N   . PHE A 1 1227 ? 40.218  -28.722 -28.386 1.00 152.11 ? 1227 PHE A N   1 
ATOM   9356  C  CA  . PHE A 1 1227 ? 40.469  -27.629 -27.460 1.00 148.74 ? 1227 PHE A CA  1 
ATOM   9357  C  C   . PHE A 1 1227 ? 41.641  -26.815 -27.925 1.00 149.49 ? 1227 PHE A C   1 
ATOM   9358  O  O   . PHE A 1 1227 ? 42.423  -27.257 -28.760 1.00 152.08 ? 1227 PHE A O   1 
ATOM   9359  C  CB  . PHE A 1 1227 ? 40.676  -28.119 -26.030 1.00 151.20 ? 1227 PHE A CB  1 
ATOM   9360  C  CG  . PHE A 1 1227 ? 41.832  -29.049 -25.860 1.00 157.82 ? 1227 PHE A CG  1 
ATOM   9361  C  CD1 . PHE A 1 1227 ? 43.119  -28.560 -25.849 1.00 160.54 ? 1227 PHE A CD1 1 
ATOM   9362  C  CD2 . PHE A 1 1227 ? 41.630  -30.412 -25.671 1.00 158.83 ? 1227 PHE A CD2 1 
ATOM   9363  C  CE1 . PHE A 1 1227 ? 44.191  -29.405 -25.674 1.00 163.11 ? 1227 PHE A CE1 1 
ATOM   9364  C  CE2 . PHE A 1 1227 ? 42.701  -31.268 -25.487 1.00 160.72 ? 1227 PHE A CE2 1 
ATOM   9365  C  CZ  . PHE A 1 1227 ? 43.987  -30.762 -25.493 1.00 163.59 ? 1227 PHE A CZ  1 
ATOM   9366  N  N   . TRP A 1 1228 ? 41.753  -25.604 -27.414 1.00 112.38 ? 1228 TRP A N   1 
ATOM   9367  C  CA  . TRP A 1 1228 ? 42.823  -24.755 -27.885 1.00 116.47 ? 1228 TRP A CA  1 
ATOM   9368  C  C   . TRP A 1 1228 ? 43.808  -24.639 -26.754 1.00 137.11 ? 1228 TRP A C   1 
ATOM   9369  O  O   . TRP A 1 1228 ? 43.469  -25.015 -25.640 1.00 135.51 ? 1228 TRP A O   1 
ATOM   9370  C  CB  . TRP A 1 1228 ? 42.303  -23.390 -28.290 1.00 112.47 ? 1228 TRP A CB  1 
ATOM   9371  C  CG  . TRP A 1 1228 ? 41.132  -23.331 -29.334 1.00 111.42 ? 1228 TRP A CG  1 
ATOM   9372  C  CD1 . TRP A 1 1228 ? 41.066  -22.521 -30.445 1.00 112.68 ? 1228 TRP A CD1 1 
ATOM   9373  C  CD2 . TRP A 1 1228 ? 39.888  -24.054 -29.322 1.00 108.75 ? 1228 TRP A CD2 1 
ATOM   9374  N  NE1 . TRP A 1 1228 ? 39.875  -22.689 -31.107 1.00 109.86 ? 1228 TRP A NE1 1 
ATOM   9375  C  CE2 . TRP A 1 1228 ? 39.139  -23.624 -30.435 1.00 107.73 ? 1228 TRP A CE2 1 
ATOM   9376  C  CE3 . TRP A 1 1228 ? 39.331  -25.014 -28.482 1.00 105.68 ? 1228 TRP A CE3 1 
ATOM   9377  C  CZ2 . TRP A 1 1228 ? 37.888  -24.121 -30.713 1.00 103.90 ? 1228 TRP A CZ2 1 
ATOM   9378  C  CZ3 . TRP A 1 1228 ? 38.073  -25.509 -28.785 1.00 102.11 ? 1228 TRP A CZ3 1 
ATOM   9379  C  CH2 . TRP A 1 1228 ? 37.374  -25.059 -29.876 1.00 100.94 ? 1228 TRP A CH2 1 
ATOM   9380  N  N   . LYS A 1 1229 ? 45.017  -24.148 -27.040 1.00 152.15 ? 1229 LYS A N   1 
ATOM   9381  C  CA  . LYS A 1 1229 ? 46.088  -24.012 -26.037 1.00 157.40 ? 1229 LYS A CA  1 
ATOM   9382  C  C   . LYS A 1 1229 ? 46.347  -22.537 -25.730 1.00 164.86 ? 1229 LYS A C   1 
ATOM   9383  O  O   . LYS A 1 1229 ? 45.899  -21.666 -26.474 1.00 164.06 ? 1229 LYS A O   1 
ATOM   9384  C  CB  . LYS A 1 1229 ? 47.384  -24.664 -26.536 1.00 161.07 ? 1229 LYS A CB  1 
ATOM   9385  C  CG  . LYS A 1 1229 ? 48.057  -25.607 -25.556 1.00 166.23 ? 1229 LYS A CG  1 
ATOM   9386  C  CD  . LYS A 1 1229 ? 48.949  -26.594 -26.297 1.00 204.44 ? 1229 LYS A CD  1 
ATOM   9387  C  CE  . LYS A 1 1229 ? 50.060  -25.929 -27.097 1.00 203.35 ? 1229 LYS A CE  1 
ATOM   9388  N  NZ  . LYS A 1 1229 ? 51.227  -25.589 -26.253 1.00 201.64 ? 1229 LYS A NZ  1 
ATOM   9389  N  N   . ASP A 1 1230 ? 47.070  -22.248 -24.650 1.00 203.54 ? 1230 ASP A N   1 
ATOM   9390  C  CA  . ASP A 1 1230 ? 47.371  -20.859 -24.304 1.00 210.42 ? 1230 ASP A CA  1 
ATOM   9391  C  C   . ASP A 1 1230 ? 48.123  -20.178 -25.446 1.00 219.35 ? 1230 ASP A C   1 
ATOM   9392  O  O   . ASP A 1 1230 ? 47.784  -19.069 -25.857 1.00 216.20 ? 1230 ASP A O   1 
ATOM   9393  C  CB  . ASP A 1 1230 ? 48.190  -20.791 -23.005 1.00 216.42 ? 1230 ASP A CB  1 
ATOM   9394  C  CG  . ASP A 1 1230 ? 48.449  -19.357 -22.531 1.00 220.90 ? 1230 ASP A CG  1 
ATOM   9395  O  OD1 . ASP A 1 1230 ? 48.103  -18.404 -23.261 1.00 220.30 ? 1230 ASP A OD1 1 
ATOM   9396  O  OD2 . ASP A 1 1230 ? 49.000  -19.187 -21.419 1.00 224.43 ? 1230 ASP A OD2 1 
ATOM   9397  N  N   . ASN A 1 1231 ? 49.130  -20.867 -25.969 1.00 290.31 ? 1231 ASN A N   1 
ATOM   9398  C  CA  . ASN A 1 1231 ? 49.992  -20.314 -27.009 1.00 301.74 ? 1231 ASN A CA  1 
ATOM   9399  C  C   . ASN A 1 1231 ? 49.254  -19.846 -28.260 1.00 305.93 ? 1231 ASN A C   1 
ATOM   9400  O  O   . ASN A 1 1231 ? 48.086  -19.469 -28.219 1.00 301.45 ? 1231 ASN A O   1 
ATOM   9401  C  CB  . ASN A 1 1231 ? 51.043  -21.345 -27.425 1.00 311.02 ? 1231 ASN A CB  1 
ATOM   9402  C  CG  . ASN A 1 1231 ? 50.464  -22.447 -28.299 1.00 314.34 ? 1231 ASN A CG  1 
ATOM   9403  O  OD1 . ASN A 1 1231 ? 49.683  -23.273 -27.836 1.00 314.29 ? 1231 ASN A OD1 1 
ATOM   9404  N  ND2 . ASN A 1 1231 ? 50.846  -22.460 -29.572 1.00 317.37 ? 1231 ASN A ND2 1 
ATOM   9405  N  N   . LEU A 1 1232 ? 49.970  -19.873 -29.376 1.00 210.00 ? 1232 LEU A N   1 
ATOM   9406  C  CA  . LEU A 1 1232 ? 49.417  -19.543 -30.674 1.00 212.01 ? 1232 LEU A CA  1 
ATOM   9407  C  C   . LEU A 1 1232 ? 50.416  -19.985 -31.735 1.00 225.18 ? 1232 LEU A C   1 
ATOM   9408  O  O   . LEU A 1 1232 ? 51.307  -19.221 -32.097 1.00 232.98 ? 1232 LEU A O   1 
ATOM   9409  C  CB  . LEU A 1 1232 ? 49.185  -18.040 -30.778 1.00 201.33 ? 1232 LEU A CB  1 
ATOM   9410  C  CG  . LEU A 1 1232 ? 49.100  -17.495 -32.200 1.00 192.02 ? 1232 LEU A CG  1 
ATOM   9411  C  CD1 . LEU A 1 1232 ? 47.666  -17.240 -32.616 1.00 184.02 ? 1232 LEU A CD1 1 
ATOM   9412  C  CD2 . LEU A 1 1232 ? 49.919  -16.235 -32.315 1.00 191.08 ? 1232 LEU A CD2 1 
ATOM   9413  N  N   . GLN A 1 1233 ? 50.287  -21.227 -32.200 1.00 294.45 ? 1233 GLN A N   1 
ATOM   9414  C  CA  . GLN A 1 1233 ? 51.106  -21.771 -33.298 1.00 305.56 ? 1233 GLN A CA  1 
ATOM   9415  C  C   . GLN A 1 1233 ? 52.629  -21.792 -33.095 1.00 322.94 ? 1233 GLN A C   1 
ATOM   9416  O  O   . GLN A 1 1233 ? 53.377  -22.053 -34.038 1.00 325.14 ? 1233 GLN A O   1 
ATOM   9417  C  CB  . GLN A 1 1233 ? 50.780  -21.076 -34.623 1.00 314.37 ? 1233 GLN A CB  1 
ATOM   9418  C  CG  . GLN A 1 1233 ? 51.501  -19.756 -34.825 1.00 324.80 ? 1233 GLN A CG  1 
ATOM   9419  C  CD  . GLN A 1 1233 ? 51.122  -19.083 -36.122 1.00 331.91 ? 1233 GLN A CD  1 
ATOM   9420  O  OE1 . GLN A 1 1233 ? 51.438  -19.577 -37.203 1.00 338.29 ? 1233 GLN A OE1 1 
ATOM   9421  N  NE2 . GLN A 1 1233 ? 50.439  -17.948 -36.024 1.00 330.18 ? 1233 GLN A NE2 1 
ATOM   9422  N  N   . HIS A 1 1234 ? 53.090  -21.500 -31.884 1.00 250.60 ? 1234 HIS A N   1 
ATOM   9423  C  CA  . HIS A 1 1234 ? 54.499  -21.690 -31.551 1.00 257.69 ? 1234 HIS A CA  1 
ATOM   9424  C  C   . HIS A 1 1234 ? 54.684  -23.153 -31.170 1.00 263.71 ? 1234 HIS A C   1 
ATOM   9425  O  O   . HIS A 1 1234 ? 55.804  -23.650 -31.057 1.00 268.28 ? 1234 HIS A O   1 
ATOM   9426  C  CB  . HIS A 1 1234 ? 54.934  -20.752 -30.426 1.00 253.50 ? 1234 HIS A CB  1 
ATOM   9427  C  CG  . HIS A 1 1234 ? 54.753  -19.298 -30.751 1.00 248.89 ? 1234 HIS A CG  1 
ATOM   9428  N  ND1 . HIS A 1 1234 ? 55.295  -18.715 -31.874 1.00 251.66 ? 1234 HIS A ND1 1 
ATOM   9429  C  CD2 . HIS A 1 1234 ? 54.096  -18.313 -30.092 1.00 243.66 ? 1234 HIS A CD2 1 
ATOM   9430  C  CE1 . HIS A 1 1234 ? 54.977  -17.431 -31.898 1.00 248.78 ? 1234 HIS A CE1 1 
ATOM   9431  N  NE2 . HIS A 1 1234 ? 54.251  -17.162 -30.829 1.00 243.94 ? 1234 HIS A NE2 1 
ATOM   9432  N  N   . LYS A 1 1235 ? 53.549  -23.814 -30.952 1.00 266.66 ? 1235 LYS A N   1 
ATOM   9433  C  CA  . LYS A 1 1235 ? 53.445  -25.271 -30.896 1.00 274.78 ? 1235 LYS A CA  1 
ATOM   9434  C  C   . LYS A 1 1235 ? 54.586  -25.994 -30.179 1.00 289.84 ? 1235 LYS A C   1 
ATOM   9435  O  O   . LYS A 1 1235 ? 55.149  -26.948 -30.712 1.00 295.81 ? 1235 LYS A O   1 
ATOM   9436  C  CB  . LYS A 1 1235 ? 53.269  -25.840 -32.312 1.00 273.85 ? 1235 LYS A CB  1 
ATOM   9437  C  CG  . LYS A 1 1235 ? 51.984  -25.411 -33.032 1.00 265.88 ? 1235 LYS A CG  1 
ATOM   9438  C  CD  . LYS A 1 1235 ? 50.783  -26.271 -32.630 1.00 258.23 ? 1235 LYS A CD  1 
ATOM   9439  C  CE  . LYS A 1 1235 ? 49.564  -26.027 -33.525 1.00 251.59 ? 1235 LYS A CE  1 
ATOM   9440  N  NZ  . LYS A 1 1235 ? 48.941  -24.685 -33.342 1.00 246.63 ? 1235 LYS A NZ  1 
ATOM   9441  N  N   . ASP A 1 1236 ? 54.930  -25.549 -28.975 1.00 312.66 ? 1236 ASP A N   1 
ATOM   9442  C  CA  . ASP A 1 1236 ? 55.839  -26.330 -28.150 1.00 325.77 ? 1236 ASP A CA  1 
ATOM   9443  C  C   . ASP A 1 1236 ? 55.108  -27.627 -27.847 1.00 329.31 ? 1236 ASP A C   1 
ATOM   9444  O  O   . ASP A 1 1236 ? 55.706  -28.635 -27.466 1.00 333.25 ? 1236 ASP A O   1 
ATOM   9445  C  CB  . ASP A 1 1236 ? 56.183  -25.593 -26.861 1.00 328.96 ? 1236 ASP A CB  1 
ATOM   9446  C  CG  . ASP A 1 1236 ? 57.389  -26.182 -26.167 1.00 337.72 ? 1236 ASP A CG  1 
ATOM   9447  O  OD1 . ASP A 1 1236 ? 57.657  -27.387 -26.363 1.00 339.49 ? 1236 ASP A OD1 1 
ATOM   9448  O  OD2 . ASP A 1 1236 ? 58.073  -25.441 -25.431 1.00 339.28 ? 1236 ASP A OD2 1 
ATOM   9449  N  N   . SER A 1 1237 ? 53.793  -27.565 -28.034 1.00 300.65 ? 1237 SER A N   1 
ATOM   9450  C  CA  . SER A 1 1237 ? 52.892  -28.707 -27.924 1.00 301.27 ? 1237 SER A CA  1 
ATOM   9451  C  C   . SER A 1 1237 ? 52.830  -29.301 -26.521 1.00 302.25 ? 1237 SER A C   1 
ATOM   9452  O  O   . SER A 1 1237 ? 52.197  -30.338 -26.312 1.00 305.15 ? 1237 SER A O   1 
ATOM   9453  C  CB  . SER A 1 1237 ? 53.238  -29.783 -28.952 1.00 304.85 ? 1237 SER A CB  1 
ATOM   9454  O  OG  . SER A 1 1237 ? 52.154  -30.678 -29.115 1.00 301.20 ? 1237 SER A OG  1 
ATOM   9455  N  N   . SER A 1 1238 ? 53.481  -28.638 -25.567 1.00 415.31 ? 1238 SER A N   1 
ATOM   9456  C  CA  . SER A 1 1238 ? 53.450  -29.066 -24.171 1.00 412.36 ? 1238 SER A CA  1 
ATOM   9457  C  C   . SER A 1 1238 ? 52.049  -28.940 -23.564 1.00 406.46 ? 1238 SER A C   1 
ATOM   9458  O  O   . SER A 1 1238 ? 51.732  -27.948 -22.901 1.00 401.71 ? 1238 SER A O   1 
ATOM   9459  C  CB  . SER A 1 1238 ? 54.473  -28.286 -23.334 1.00 417.84 ? 1238 SER A CB  1 
ATOM   9460  O  OG  . SER A 1 1238 ? 54.200  -26.894 -23.343 1.00 419.54 ? 1238 SER A OG  1 
ATOM   9461  N  N   . VAL A 1 1239 ? 51.218  -29.952 -23.807 1.00 251.41 ? 1239 VAL A N   1 
ATOM   9462  C  CA  . VAL A 1 1239 ? 49.911  -30.075 -23.173 1.00 241.93 ? 1239 VAL A CA  1 
ATOM   9463  C  C   . VAL A 1 1239 ? 50.016  -31.155 -22.108 1.00 240.21 ? 1239 VAL A C   1 
ATOM   9464  O  O   . VAL A 1 1239 ? 49.134  -32.007 -22.004 1.00 236.57 ? 1239 VAL A O   1 
ATOM   9465  C  CB  . VAL A 1 1239 ? 48.825  -30.498 -24.187 1.00 239.76 ? 1239 VAL A CB  1 
ATOM   9466  C  CG1 . VAL A 1 1239 ? 48.841  -29.582 -25.379 1.00 240.69 ? 1239 VAL A CG1 1 
ATOM   9467  C  CG2 . VAL A 1 1239 ? 49.040  -31.931 -24.644 1.00 245.57 ? 1239 VAL A CG2 1 
ATOM   9468  N  N   . PRO A 1 1240 ? 51.081  -31.096 -21.290 1.00 298.51 ? 1240 PRO A N   1 
ATOM   9469  C  CA  . PRO A 1 1240 ? 51.583  -32.251 -20.536 1.00 302.07 ? 1240 PRO A CA  1 
ATOM   9470  C  C   . PRO A 1 1240 ? 50.511  -32.965 -19.720 1.00 293.66 ? 1240 PRO A C   1 
ATOM   9471  O  O   . PRO A 1 1240 ? 50.598  -32.991 -18.494 1.00 298.04 ? 1240 PRO A O   1 
ATOM   9472  C  CB  . PRO A 1 1240 ? 52.632  -31.629 -19.607 1.00 309.61 ? 1240 PRO A CB  1 
ATOM   9473  C  CG  . PRO A 1 1240 ? 52.219  -30.212 -19.466 1.00 305.72 ? 1240 PRO A CG  1 
ATOM   9474  C  CD  . PRO A 1 1240 ? 51.675  -29.837 -20.806 1.00 300.81 ? 1240 PRO A CD  1 
ATOM   9475  N  N   . ASN A 1 1241 ? 49.523  -33.543 -20.394 1.00 348.73 ? 1241 ASN A N   1 
ATOM   9476  C  CA  . ASN A 1 1241 ? 48.485  -34.303 -19.717 1.00 335.27 ? 1241 ASN A CA  1 
ATOM   9477  C  C   . ASN A 1 1241 ? 47.788  -33.495 -18.627 1.00 312.13 ? 1241 ASN A C   1 
ATOM   9478  O  O   . ASN A 1 1241 ? 47.299  -34.060 -17.649 1.00 308.28 ? 1241 ASN A O   1 
ATOM   9479  C  CB  . ASN A 1 1241 ? 49.091  -35.562 -19.101 1.00 351.04 ? 1241 ASN A CB  1 
ATOM   9480  C  CG  . ASN A 1 1241 ? 49.861  -36.385 -20.105 1.00 362.72 ? 1241 ASN A CG  1 
ATOM   9481  O  OD1 . ASN A 1 1241 ? 49.484  -36.465 -21.274 1.00 362.24 ? 1241 ASN A OD1 1 
ATOM   9482  N  ND2 . ASN A 1 1241 ? 50.948  -37.007 -19.657 1.00 369.42 ? 1241 ASN A ND2 1 
ATOM   9483  N  N   . THR A 1 1242 ? 47.738  -32.177 -18.786 1.00 213.84 ? 1242 THR A N   1 
ATOM   9484  C  CA  . THR A 1 1242 ? 47.311  -31.330 -17.687 1.00 194.42 ? 1242 THR A CA  1 
ATOM   9485  C  C   . THR A 1 1242 ? 46.706  -30.015 -18.097 1.00 169.00 ? 1242 THR A C   1 
ATOM   9486  O  O   . THR A 1 1242 ? 47.290  -29.250 -18.870 1.00 162.66 ? 1242 THR A O   1 
ATOM   9487  C  CB  . THR A 1 1242 ? 48.497  -30.926 -16.868 1.00 202.72 ? 1242 THR A CB  1 
ATOM   9488  O  OG1 . THR A 1 1242 ? 49.471  -30.360 -17.752 1.00 206.28 ? 1242 THR A OG1 1 
ATOM   9489  C  CG2 . THR A 1 1242 ? 49.079  -32.125 -16.147 1.00 208.42 ? 1242 THR A CG2 1 
ATOM   9490  N  N   . GLY A 1 1243 ? 45.558  -29.737 -17.498 1.00 190.91 ? 1243 GLY A N   1 
ATOM   9491  C  CA  . GLY A 1 1243 ? 44.835  -28.509 -17.734 1.00 177.81 ? 1243 GLY A CA  1 
ATOM   9492  C  C   . GLY A 1 1243 ? 45.486  -27.277 -17.146 1.00 171.14 ? 1243 GLY A C   1 
ATOM   9493  O  O   . GLY A 1 1243 ? 46.489  -27.354 -16.438 1.00 175.93 ? 1243 GLY A O   1 
ATOM   9494  N  N   . THR A 1 1244 ? 44.877  -26.137 -17.446 1.00 157.07 ? 1244 THR A N   1 
ATOM   9495  C  CA  . THR A 1 1244 ? 45.403  -24.841 -17.087 1.00 156.21 ? 1244 THR A CA  1 
ATOM   9496  C  C   . THR A 1 1244 ? 44.239  -23.937 -16.859 1.00 160.43 ? 1244 THR A C   1 
ATOM   9497  O  O   . THR A 1 1244 ? 43.165  -24.124 -17.417 1.00 159.93 ? 1244 THR A O   1 
ATOM   9498  C  CB  . THR A 1 1244 ? 46.207  -24.220 -18.242 1.00 152.72 ? 1244 THR A CB  1 
ATOM   9499  O  OG1 . THR A 1 1244 ? 47.394  -24.989 -18.484 1.00 156.13 ? 1244 THR A OG1 1 
ATOM   9500  C  CG2 . THR A 1 1244 ? 46.574  -22.760 -17.935 1.00 151.10 ? 1244 THR A CG2 1 
ATOM   9501  N  N   . ALA A 1 1245 ? 44.456  -22.945 -16.027 1.00 164.37 ? 1245 ALA A N   1 
ATOM   9502  C  CA  . ALA A 1 1245 ? 43.444  -21.951 -15.820 1.00 163.10 ? 1245 ALA A CA  1 
ATOM   9503  C  C   . ALA A 1 1245 ? 43.192  -21.248 -17.142 1.00 161.41 ? 1245 ALA A C   1 
ATOM   9504  O  O   . ALA A 1 1245 ? 42.049  -20.995 -17.514 1.00 156.10 ? 1245 ALA A O   1 
ATOM   9505  C  CB  . ALA A 1 1245 ? 43.913  -20.969 -14.786 1.00 165.76 ? 1245 ALA A CB  1 
ATOM   9506  N  N   . ARG A 1 1246 ? 44.276  -20.920 -17.838 1.00 171.89 ? 1246 ARG A N   1 
ATOM   9507  C  CA  . ARG A 1 1246 ? 44.187  -20.146 -19.066 1.00 171.21 ? 1246 ARG A CA  1 
ATOM   9508  C  C   . ARG A 1 1246 ? 43.761  -21.025 -20.219 1.00 167.39 ? 1246 ARG A C   1 
ATOM   9509  O  O   . ARG A 1 1246 ? 42.996  -20.594 -21.081 1.00 163.87 ? 1246 ARG A O   1 
ATOM   9510  C  CB  . ARG A 1 1246 ? 45.514  -19.481 -19.393 1.00 174.50 ? 1246 ARG A CB  1 
ATOM   9511  C  CG  . ARG A 1 1246 ? 45.390  -18.440 -20.481 1.00 173.90 ? 1246 ARG A CG  1 
ATOM   9512  C  CD  . ARG A 1 1246 ? 46.717  -17.751 -20.751 1.00 180.93 ? 1246 ARG A CD  1 
ATOM   9513  N  NE  . ARG A 1 1246 ? 47.221  -17.012 -19.596 1.00 189.17 ? 1246 ARG A NE  1 
ATOM   9514  C  CZ  . ARG A 1 1246 ? 47.400  -15.691 -19.561 1.00 195.27 ? 1246 ARG A CZ  1 
ATOM   9515  N  NH1 . ARG A 1 1246 ? 47.127  -14.950 -20.628 1.00 195.48 ? 1246 ARG A NH1 1 
ATOM   9516  N  NH2 . ARG A 1 1246 ? 47.854  -15.104 -18.457 1.00 199.09 ? 1246 ARG A NH2 1 
ATOM   9517  N  N   . MET A 1 1247 ? 44.259  -22.258 -20.240 1.00 206.88 ? 1247 MET A N   1 
ATOM   9518  C  CA  . MET A 1 1247 ? 43.834  -23.229 -21.249 1.00 203.18 ? 1247 MET A CA  1 
ATOM   9519  C  C   . MET A 1 1247 ? 42.308  -23.272 -21.289 1.00 198.26 ? 1247 MET A C   1 
ATOM   9520  O  O   . MET A 1 1247 ? 41.687  -22.693 -22.176 1.00 195.15 ? 1247 MET A O   1 
ATOM   9521  C  CB  . MET A 1 1247 ? 44.401  -24.619 -20.933 1.00 203.61 ? 1247 MET A CB  1 
ATOM   9522  C  CG  . MET A 1 1247 ? 44.560  -25.549 -22.136 1.00 203.16 ? 1247 MET A CG  1 
ATOM   9523  S  SD  . MET A 1 1247 ? 45.934  -26.700 -21.891 1.00 223.03 ? 1247 MET A SD  1 
ATOM   9524  C  CE  . MET A 1 1247 ? 47.261  -25.541 -21.528 1.00 204.80 ? 1247 MET A CE  1 
ATOM   9525  N  N   . VAL A 1 1248 ? 41.706  -23.931 -20.307 1.00 144.54 ? 1248 VAL A N   1 
ATOM   9526  C  CA  . VAL A 1 1248 ? 40.256  -23.990 -20.241 1.00 139.00 ? 1248 VAL A CA  1 
ATOM   9527  C  C   . VAL A 1 1248 ? 39.619  -22.608 -20.376 1.00 132.20 ? 1248 VAL A C   1 
ATOM   9528  O  O   . VAL A 1 1248 ? 38.503  -22.494 -20.868 1.00 126.97 ? 1248 VAL A O   1 
ATOM   9529  C  CB  . VAL A 1 1248 ? 39.748  -24.729 -18.980 1.00 115.57 ? 1248 VAL A CB  1 
ATOM   9530  C  CG1 . VAL A 1 1248 ? 38.231  -24.648 -18.864 1.00 108.67 ? 1248 VAL A CG1 1 
ATOM   9531  C  CG2 . VAL A 1 1248 ? 40.181  -26.178 -19.014 1.00 118.67 ? 1248 VAL A CG2 1 
ATOM   9532  N  N   . GLU A 1 1249 ? 40.304  -21.550 -19.962 1.00 174.57 ? 1249 GLU A N   1 
ATOM   9533  C  CA  . GLU A 1 1249 ? 39.701  -20.229 -20.155 1.00 175.10 ? 1249 GLU A CA  1 
ATOM   9534  C  C   . GLU A 1 1249 ? 39.570  -19.994 -21.647 1.00 175.45 ? 1249 GLU A C   1 
ATOM   9535  O  O   . GLU A 1 1249 ? 38.489  -19.699 -22.159 1.00 174.12 ? 1249 GLU A O   1 
ATOM   9536  C  CB  . GLU A 1 1249 ? 40.464  -19.081 -19.447 1.00 180.61 ? 1249 GLU A CB  1 
ATOM   9537  C  CG  . GLU A 1 1249 ? 39.750  -17.681 -19.541 1.00 183.24 ? 1249 GLU A CG  1 
ATOM   9538  C  CD  . GLU A 1 1249 ? 40.094  -16.683 -18.411 1.00 190.28 ? 1249 GLU A CD  1 
ATOM   9539  O  OE1 . GLU A 1 1249 ? 40.586  -17.116 -17.344 1.00 196.93 ? 1249 GLU A OE1 1 
ATOM   9540  O  OE2 . GLU A 1 1249 ? 39.850  -15.463 -18.592 1.00 189.34 ? 1249 GLU A OE2 1 
ATOM   9541  N  N   . THR A 1 1250 ? 40.662  -20.180 -22.363 1.00 170.32 ? 1250 THR A N   1 
ATOM   9542  C  CA  . THR A 1 1250 ? 40.618  -19.949 -23.795 1.00 166.36 ? 1250 THR A CA  1 
ATOM   9543  C  C   . THR A 1 1250 ? 39.521  -20.783 -24.478 1.00 157.94 ? 1250 THR A C   1 
ATOM   9544  O  O   . THR A 1 1250 ? 38.584  -20.227 -25.058 1.00 151.64 ? 1250 THR A O   1 
ATOM   9545  C  CB  . THR A 1 1250 ? 41.990  -20.196 -24.412 1.00 173.08 ? 1250 THR A CB  1 
ATOM   9546  O  OG1 . THR A 1 1250 ? 42.301  -21.591 -24.331 1.00 177.85 ? 1250 THR A OG1 1 
ATOM   9547  C  CG2 . THR A 1 1250 ? 43.036  -19.398 -23.654 1.00 174.08 ? 1250 THR A CG2 1 
ATOM   9548  N  N   . THR A 1 1251 ? 39.628  -22.108 -24.399 1.00 128.39 ? 1251 THR A N   1 
ATOM   9549  C  CA  . THR A 1 1251 ? 38.656  -23.000 -25.053 1.00 127.76 ? 1251 THR A CA  1 
ATOM   9550  C  C   . THR A 1 1251 ? 37.199  -22.712 -24.679 1.00 125.42 ? 1251 THR A C   1 
ATOM   9551  O  O   . THR A 1 1251 ? 36.268  -23.003 -25.441 1.00 125.67 ? 1251 THR A O   1 
ATOM   9552  C  CB  . THR A 1 1251 ? 38.954  -24.501 -24.785 1.00 129.72 ? 1251 THR A CB  1 
ATOM   9553  O  OG1 . THR A 1 1251 ? 38.121  -24.976 -23.713 1.00 131.23 ? 1251 THR A OG1 1 
ATOM   9554  C  CG2 . THR A 1 1251 ? 40.452  -24.731 -24.504 1.00 130.96 ? 1251 THR A CG2 1 
ATOM   9555  N  N   . ALA A 1 1252 ? 37.003  -22.163 -23.494 1.00 155.27 ? 1252 ALA A N   1 
ATOM   9556  C  CA  . ALA A 1 1252 ? 35.691  -21.679 -23.169 1.00 155.29 ? 1252 ALA A CA  1 
ATOM   9557  C  C   . ALA A 1 1252 ? 35.416  -20.607 -24.209 1.00 155.41 ? 1252 ALA A C   1 
ATOM   9558  O  O   . ALA A 1 1252 ? 34.396  -20.626 -24.883 1.00 152.25 ? 1252 ALA A O   1 
ATOM   9559  C  CB  . ALA A 1 1252 ? 35.660  -21.088 -21.764 1.00 156.74 ? 1252 ALA A CB  1 
ATOM   9560  N  N   . TYR A 1 1253 ? 36.358  -19.689 -24.369 1.00 144.46 ? 1253 TYR A N   1 
ATOM   9561  C  CA  . TYR A 1 1253 ? 36.118  -18.519 -25.191 1.00 146.29 ? 1253 TYR A CA  1 
ATOM   9562  C  C   . TYR A 1 1253 ? 35.800  -18.840 -26.639 1.00 146.22 ? 1253 TYR A C   1 
ATOM   9563  O  O   . TYR A 1 1253 ? 35.125  -18.055 -27.307 1.00 147.52 ? 1253 TYR A O   1 
ATOM   9564  C  CB  . TYR A 1 1253 ? 37.288  -17.554 -25.094 1.00 150.52 ? 1253 TYR A CB  1 
ATOM   9565  C  CG  . TYR A 1 1253 ? 37.270  -16.730 -23.826 1.00 153.15 ? 1253 TYR A CG  1 
ATOM   9566  C  CD1 . TYR A 1 1253 ? 36.190  -15.897 -23.530 1.00 151.56 ? 1253 TYR A CD1 1 
ATOM   9567  C  CD2 . TYR A 1 1253 ? 38.336  -16.765 -22.926 1.00 155.57 ? 1253 TYR A CD2 1 
ATOM   9568  C  CE1 . TYR A 1 1253 ? 36.170  -15.127 -22.367 1.00 150.85 ? 1253 TYR A CE1 1 
ATOM   9569  C  CE2 . TYR A 1 1253 ? 38.325  -15.995 -21.767 1.00 155.51 ? 1253 TYR A CE2 1 
ATOM   9570  C  CZ  . TYR A 1 1253 ? 37.238  -15.184 -21.494 1.00 153.38 ? 1253 TYR A CZ  1 
ATOM   9571  O  OH  . TYR A 1 1253 ? 37.207  -14.428 -20.352 1.00 156.37 ? 1253 TYR A OH  1 
ATOM   9572  N  N   . ALA A 1 1254 ? 36.282  -19.988 -27.116 1.00 179.81 ? 1254 ALA A N   1 
ATOM   9573  C  CA  . ALA A 1 1254 ? 35.990  -20.444 -28.476 1.00 173.71 ? 1254 ALA A CA  1 
ATOM   9574  C  C   . ALA A 1 1254 ? 34.723  -21.264 -28.485 1.00 170.74 ? 1254 ALA A C   1 
ATOM   9575  O  O   . ALA A 1 1254 ? 33.909  -21.149 -29.401 1.00 167.24 ? 1254 ALA A O   1 
ATOM   9576  C  CB  . ALA A 1 1254 ? 37.128  -21.268 -29.029 1.00 172.72 ? 1254 ALA A CB  1 
ATOM   9577  N  N   . LEU A 1 1255 ? 34.567  -22.109 -27.470 1.00 113.03 ? 1255 LEU A N   1 
ATOM   9578  C  CA  . LEU A 1 1255 ? 33.351  -22.899 -27.344 1.00 115.96 ? 1255 LEU A CA  1 
ATOM   9579  C  C   . LEU A 1 1255 ? 32.129  -21.981 -27.227 1.00 112.73 ? 1255 LEU A C   1 
ATOM   9580  O  O   . LEU A 1 1255 ? 31.046  -22.268 -27.745 1.00 108.58 ? 1255 LEU A O   1 
ATOM   9581  C  CB  . LEU A 1 1255 ? 33.439  -23.848 -26.151 1.00 120.44 ? 1255 LEU A CB  1 
ATOM   9582  C  CG  . LEU A 1 1255 ? 32.093  -24.468 -25.746 1.00 119.39 ? 1255 LEU A CG  1 
ATOM   9583  C  CD1 . LEU A 1 1255 ? 31.381  -25.007 -26.949 1.00 118.61 ? 1255 LEU A CD1 1 
ATOM   9584  C  CD2 . LEU A 1 1255 ? 32.258  -25.566 -24.726 1.00 119.20 ? 1255 LEU A CD2 1 
ATOM   9585  N  N   . LEU A 1 1256 ? 32.314  -20.861 -26.550 1.00 150.27 ? 1256 LEU A N   1 
ATOM   9586  C  CA  . LEU A 1 1256 ? 31.267  -19.867 -26.497 1.00 153.88 ? 1256 LEU A CA  1 
ATOM   9587  C  C   . LEU A 1 1256 ? 31.053  -19.247 -27.881 1.00 156.96 ? 1256 LEU A C   1 
ATOM   9588  O  O   . LEU A 1 1256 ? 29.900  -19.129 -28.325 1.00 157.45 ? 1256 LEU A O   1 
ATOM   9589  C  CB  . LEU A 1 1256 ? 31.588  -18.793 -25.450 1.00 156.01 ? 1256 LEU A CB  1 
ATOM   9590  C  CG  . LEU A 1 1256 ? 31.449  -19.155 -23.973 1.00 156.31 ? 1256 LEU A CG  1 
ATOM   9591  C  CD1 . LEU A 1 1256 ? 31.830  -17.952 -23.174 1.00 159.24 ? 1256 LEU A CD1 1 
ATOM   9592  C  CD2 . LEU A 1 1256 ? 30.037  -19.588 -23.659 1.00 151.63 ? 1256 LEU A CD2 1 
ATOM   9593  N  N   . THR A 1 1257 ? 32.133  -18.854 -28.568 1.00 110.35 ? 1257 THR A N   1 
ATOM   9594  C  CA  . THR A 1 1257 ? 31.923  -18.239 -29.867 1.00 108.02 ? 1257 THR A CA  1 
ATOM   9595  C  C   . THR A 1 1257 ? 31.090  -19.224 -30.695 1.00 103.32 ? 1257 THR A C   1 
ATOM   9596  O  O   . THR A 1 1257 ? 29.943  -18.912 -31.033 1.00 99.32  ? 1257 THR A O   1 
ATOM   9597  C  CB  . THR A 1 1257 ? 33.210  -17.814 -30.610 1.00 98.93  ? 1257 THR A CB  1 
ATOM   9598  O  OG1 . THR A 1 1257 ? 34.335  -17.904 -29.740 1.00 101.00 ? 1257 THR A OG1 1 
ATOM   9599  C  CG2 . THR A 1 1257 ? 33.069  -16.372 -31.093 1.00 97.42  ? 1257 THR A CG2 1 
ATOM   9600  N  N   . SER A 1 1258 ? 31.622  -20.426 -30.950 1.00 127.40 ? 1258 SER A N   1 
ATOM   9601  C  CA  . SER A 1 1258 ? 30.893  -21.477 -31.695 1.00 130.72 ? 1258 SER A CA  1 
ATOM   9602  C  C   . SER A 1 1258 ? 29.416  -21.614 -31.334 1.00 129.24 ? 1258 SER A C   1 
ATOM   9603  O  O   . SER A 1 1258 ? 28.568  -21.636 -32.227 1.00 127.49 ? 1258 SER A O   1 
ATOM   9604  C  CB  . SER A 1 1258 ? 31.541  -22.842 -31.498 1.00 132.62 ? 1258 SER A CB  1 
ATOM   9605  O  OG  . SER A 1 1258 ? 32.850  -22.860 -32.022 1.00 135.56 ? 1258 SER A OG  1 
ATOM   9606  N  N   . LEU A 1 1259 ? 29.134  -21.720 -30.029 1.00 111.16 ? 1259 LEU A N   1 
ATOM   9607  C  CA  . LEU A 1 1259 ? 27.777  -21.899 -29.469 1.00 107.29 ? 1259 LEU A CA  1 
ATOM   9608  C  C   . LEU A 1 1259 ? 26.817  -20.699 -29.648 1.00 106.49 ? 1259 LEU A C   1 
ATOM   9609  O  O   . LEU A 1 1259 ? 25.584  -20.829 -29.536 1.00 104.69 ? 1259 LEU A O   1 
ATOM   9610  C  CB  . LEU A 1 1259 ? 27.872  -22.299 -27.996 1.00 102.29 ? 1259 LEU A CB  1 
ATOM   9611  C  CG  . LEU A 1 1259 ? 28.176  -23.779 -27.765 1.00 99.12  ? 1259 LEU A CG  1 
ATOM   9612  C  CD1 . LEU A 1 1259 ? 28.408  -24.035 -26.284 1.00 100.31 ? 1259 LEU A CD1 1 
ATOM   9613  C  CD2 . LEU A 1 1259 ? 27.027  -24.635 -28.254 1.00 95.65  ? 1259 LEU A CD2 1 
ATOM   9614  N  N   . ASN A 1 1260 ? 27.413  -19.539 -29.913 1.00 122.11 ? 1260 ASN A N   1 
ATOM   9615  C  CA  . ASN A 1 1260 ? 26.747  -18.431 -30.575 1.00 123.94 ? 1260 ASN A CA  1 
ATOM   9616  C  C   . ASN A 1 1260 ? 26.397  -18.746 -32.045 1.00 127.82 ? 1260 ASN A C   1 
ATOM   9617  O  O   . ASN A 1 1260 ? 25.250  -18.591 -32.473 1.00 130.49 ? 1260 ASN A O   1 
ATOM   9618  C  CB  . ASN A 1 1260 ? 27.671  -17.231 -30.558 1.00 122.70 ? 1260 ASN A CB  1 
ATOM   9619  C  CG  . ASN A 1 1260 ? 27.224  -16.189 -29.615 1.00 123.43 ? 1260 ASN A CG  1 
ATOM   9620  O  OD1 . ASN A 1 1260 ? 26.081  -15.757 -29.646 1.00 124.76 ? 1260 ASN A OD1 1 
ATOM   9621  N  ND2 . ASN A 1 1260 ? 28.125  -15.748 -28.777 1.00 122.92 ? 1260 ASN A ND2 1 
ATOM   9622  N  N   . LEU A 1 1261 ? 27.380  -19.181 -32.827 1.00 129.79 ? 1261 LEU A N   1 
ATOM   9623  C  CA  . LEU A 1 1261 ? 27.163  -19.395 -34.256 1.00 125.93 ? 1261 LEU A CA  1 
ATOM   9624  C  C   . LEU A 1 1261 ? 26.463  -20.734 -34.558 1.00 125.23 ? 1261 LEU A C   1 
ATOM   9625  O  O   . LEU A 1 1261 ? 26.250  -21.103 -35.718 1.00 125.43 ? 1261 LEU A O   1 
ATOM   9626  C  CB  . LEU A 1 1261 ? 28.497  -19.271 -34.985 1.00 123.90 ? 1261 LEU A CB  1 
ATOM   9627  C  CG  . LEU A 1 1261 ? 29.196  -17.941 -34.661 1.00 121.73 ? 1261 LEU A CG  1 
ATOM   9628  C  CD1 . LEU A 1 1261 ? 30.531  -17.791 -35.407 1.00 124.83 ? 1261 LEU A CD1 1 
ATOM   9629  C  CD2 . LEU A 1 1261 ? 28.243  -16.765 -34.919 1.00 117.36 ? 1261 LEU A CD2 1 
ATOM   9630  N  N   . LYS A 1 1262 ? 26.106  -21.453 -33.500 1.00 99.54  ? 1262 LYS A N   1 
ATOM   9631  C  CA  . LYS A 1 1262 ? 25.269  -22.651 -33.614 1.00 98.08  ? 1262 LYS A CA  1 
ATOM   9632  C  C   . LYS A 1 1262 ? 25.908  -23.787 -34.415 1.00 95.93  ? 1262 LYS A C   1 
ATOM   9633  O  O   . LYS A 1 1262 ? 25.234  -24.633 -34.962 1.00 95.22  ? 1262 LYS A O   1 
ATOM   9634  C  CB  . LYS A 1 1262 ? 23.883  -22.268 -34.134 1.00 101.94 ? 1262 LYS A CB  1 
ATOM   9635  C  CG  . LYS A 1 1262 ? 23.319  -21.040 -33.372 1.00 109.66 ? 1262 LYS A CG  1 
ATOM   9636  C  CD  . LYS A 1 1262 ? 21.919  -21.273 -32.747 1.00 117.10 ? 1262 LYS A CD  1 
ATOM   9637  C  CE  . LYS A 1 1262 ? 21.593  -20.190 -31.733 1.00 121.01 ? 1262 LYS A CE  1 
ATOM   9638  N  NZ  . LYS A 1 1262 ? 22.694  -20.086 -30.707 1.00 122.49 ? 1262 LYS A NZ  1 
ATOM   9639  N  N   . ASP A 1 1263 ? 27.232  -23.798 -34.391 1.00 110.26 ? 1263 ASP A N   1 
ATOM   9640  C  CA  . ASP A 1 1263 ? 28.100  -24.773 -35.031 1.00 113.25 ? 1263 ASP A CA  1 
ATOM   9641  C  C   . ASP A 1 1263 ? 28.004  -26.182 -34.471 1.00 110.51 ? 1263 ASP A C   1 
ATOM   9642  O  O   . ASP A 1 1263 ? 28.965  -26.947 -34.438 1.00 115.99 ? 1263 ASP A O   1 
ATOM   9643  C  CB  . ASP A 1 1263 ? 29.516  -24.277 -34.833 1.00 116.45 ? 1263 ASP A CB  1 
ATOM   9644  C  CG  . ASP A 1 1263 ? 30.398  -24.629 -35.974 1.00 145.81 ? 1263 ASP A CG  1 
ATOM   9645  O  OD1 . ASP A 1 1263 ? 30.445  -25.828 -36.327 1.00 145.82 ? 1263 ASP A OD1 1 
ATOM   9646  O  OD2 . ASP A 1 1263 ? 31.026  -23.698 -36.524 1.00 145.01 ? 1263 ASP A OD2 1 
ATOM   9647  N  N   . ILE A 1 1264 ? 26.816  -26.509 -34.035 1.00 84.64  ? 1264 ILE A N   1 
ATOM   9648  C  CA  . ILE A 1 1264 ? 26.556  -27.738 -33.331 1.00 86.50  ? 1264 ILE A CA  1 
ATOM   9649  C  C   . ILE A 1 1264 ? 27.490  -28.952 -33.486 1.00 91.16  ? 1264 ILE A C   1 
ATOM   9650  O  O   . ILE A 1 1264 ? 27.507  -29.792 -32.621 1.00 91.95  ? 1264 ILE A O   1 
ATOM   9651  C  CB  . ILE A 1 1264 ? 25.079  -28.128 -33.552 1.00 82.95  ? 1264 ILE A CB  1 
ATOM   9652  C  CG1 . ILE A 1 1264 ? 24.182  -26.936 -33.174 1.00 98.93  ? 1264 ILE A CG1 1 
ATOM   9653  C  CG2 . ILE A 1 1264 ? 24.718  -29.474 -32.862 1.00 84.99  ? 1264 ILE A CG2 1 
ATOM   9654  C  CD1 . ILE A 1 1264 ? 22.718  -27.117 -33.460 1.00 97.26  ? 1264 ILE A CD1 1 
ATOM   9655  N  N   . ASN A 1 1265 ? 28.237  -29.133 -34.566 1.00 105.26 ? 1265 ASN A N   1 
ATOM   9656  C  CA  . ASN A 1 1265 ? 28.983  -30.410 -34.577 1.00 113.09 ? 1265 ASN A CA  1 
ATOM   9657  C  C   . ASN A 1 1265 ? 30.434  -30.162 -34.315 1.00 115.20 ? 1265 ASN A C   1 
ATOM   9658  O  O   . ASN A 1 1265 ? 31.184  -31.090 -33.996 1.00 117.47 ? 1265 ASN A O   1 
ATOM   9659  C  CB  . ASN A 1 1265 ? 28.739  -31.165 -35.891 1.00 118.51 ? 1265 ASN A CB  1 
ATOM   9660  C  CG  . ASN A 1 1265 ? 27.774  -32.348 -35.742 1.00 123.20 ? 1265 ASN A CG  1 
ATOM   9661  O  OD1 . ASN A 1 1265 ? 27.696  -32.984 -34.690 1.00 126.02 ? 1265 ASN A OD1 1 
ATOM   9662  N  ND2 . ASN A 1 1265 ? 27.028  -32.642 -36.808 1.00 123.83 ? 1265 ASN A ND2 1 
ATOM   9663  N  N   . TYR A 1 1266 ? 30.824  -28.907 -34.458 1.00 107.12 ? 1266 TYR A N   1 
ATOM   9664  C  CA  . TYR A 1 1266 ? 32.163  -28.514 -34.159 1.00 107.82 ? 1266 TYR A CA  1 
ATOM   9665  C  C   . TYR A 1 1266 ? 32.382  -28.625 -32.659 1.00 109.85 ? 1266 TYR A C   1 
ATOM   9666  O  O   . TYR A 1 1266 ? 33.465  -28.959 -32.162 1.00 115.11 ? 1266 TYR A O   1 
ATOM   9667  C  CB  . TYR A 1 1266 ? 32.436  -27.032 -34.470 1.00 102.40 ? 1266 TYR A CB  1 
ATOM   9668  C  CG  . TYR A 1 1266 ? 33.893  -26.660 -34.427 1.00 100.18 ? 1266 TYR A CG  1 
ATOM   9669  C  CD1 . TYR A 1 1266 ? 34.842  -27.621 -34.754 1.00 102.41 ? 1266 TYR A CD1 1 
ATOM   9670  C  CD2 . TYR A 1 1266 ? 34.312  -25.374 -34.110 1.00 97.65  ? 1266 TYR A CD2 1 
ATOM   9671  C  CE1 . TYR A 1 1266 ? 36.174  -27.288 -34.771 1.00 106.75 ? 1266 TYR A CE1 1 
ATOM   9672  C  CE2 . TYR A 1 1266 ? 35.663  -25.040 -34.155 1.00 99.84  ? 1266 TYR A CE2 1 
ATOM   9673  C  CZ  . TYR A 1 1266 ? 36.590  -25.994 -34.483 1.00 104.82 ? 1266 TYR A CZ  1 
ATOM   9674  O  OH  . TYR A 1 1266 ? 37.940  -25.687 -34.518 1.00 107.30 ? 1266 TYR A OH  1 
ATOM   9675  N  N   . VAL A 1 1267 ? 31.323  -28.308 -31.932 1.00 101.14 ? 1267 VAL A N   1 
ATOM   9676  C  CA  . VAL A 1 1267 ? 31.307  -28.159 -30.497 1.00 94.12  ? 1267 VAL A CA  1 
ATOM   9677  C  C   . VAL A 1 1267 ? 31.290  -29.439 -29.620 1.00 94.58  ? 1267 VAL A C   1 
ATOM   9678  O  O   . VAL A 1 1267 ? 31.876  -29.428 -28.541 1.00 94.69  ? 1267 VAL A O   1 
ATOM   9679  C  CB  . VAL A 1 1267 ? 30.152  -27.184 -30.146 1.00 89.76  ? 1267 VAL A CB  1 
ATOM   9680  C  CG1 . VAL A 1 1267 ? 29.518  -27.536 -28.804 1.00 88.11  ? 1267 VAL A CG1 1 
ATOM   9681  C  CG2 . VAL A 1 1267 ? 30.667  -25.751 -30.120 1.00 87.84  ? 1267 VAL A CG2 1 
ATOM   9682  N  N   . ASN A 1 1268 ? 30.622  -30.520 -30.061 1.00 114.01 ? 1268 ASN A N   1 
ATOM   9683  C  CA  . ASN A 1 1268 ? 30.420  -31.785 -29.293 1.00 122.58 ? 1268 ASN A CA  1 
ATOM   9684  C  C   . ASN A 1 1268 ? 31.645  -32.423 -28.614 1.00 126.35 ? 1268 ASN A C   1 
ATOM   9685  O  O   . ASN A 1 1268 ? 31.497  -33.151 -27.635 1.00 130.61 ? 1268 ASN A O   1 
ATOM   9686  C  CB  . ASN A 1 1268 ? 29.674  -32.742 -30.214 1.00 128.75 ? 1268 ASN A CB  1 
ATOM   9687  C  CG  . ASN A 1 1268 ? 28.378  -32.105 -30.652 1.00 133.11 ? 1268 ASN A CG  1 
ATOM   9688  O  OD1 . ASN A 1 1268 ? 27.802  -31.288 -29.942 1.00 133.16 ? 1268 ASN A OD1 1 
ATOM   9689  N  ND2 . ASN A 1 1268 ? 27.911  -32.484 -31.840 1.00 135.53 ? 1268 ASN A ND2 1 
ATOM   9690  N  N   . PRO A 1 1269 ? 32.805  -32.164 -29.175 1.00 109.67 ? 1269 PRO A N   1 
ATOM   9691  C  CA  . PRO A 1 1269 ? 34.049  -32.669 -28.620 1.00 109.71 ? 1269 PRO A CA  1 
ATOM   9692  C  C   . PRO A 1 1269 ? 34.608  -31.608 -27.664 1.00 106.06 ? 1269 PRO A C   1 
ATOM   9693  O  O   . PRO A 1 1269 ? 35.207  -31.933 -26.646 1.00 106.03 ? 1269 PRO A O   1 
ATOM   9694  C  CB  . PRO A 1 1269 ? 34.951  -32.932 -29.821 1.00 115.72 ? 1269 PRO A CB  1 
ATOM   9695  C  CG  . PRO A 1 1269 ? 34.066  -32.772 -31.007 1.00 115.94 ? 1269 PRO A CG  1 
ATOM   9696  C  CD  . PRO A 1 1269 ? 32.977  -31.838 -30.595 1.00 112.06 ? 1269 PRO A CD  1 
ATOM   9697  N  N   . VAL A 1 1270 ? 34.376  -30.321 -28.003 1.00 109.89 ? 1270 VAL A N   1 
ATOM   9698  C  CA  . VAL A 1 1270 ? 34.846  -29.226 -27.146 1.00 106.21 ? 1270 VAL A CA  1 
ATOM   9699  C  C   . VAL A 1 1270 ? 34.260  -29.390 -25.723 1.00 101.09 ? 1270 VAL A C   1 
ATOM   9700  O  O   . VAL A 1 1270 ? 34.991  -29.340 -24.738 1.00 103.92 ? 1270 VAL A O   1 
ATOM   9701  C  CB  . VAL A 1 1270 ? 34.485  -27.862 -27.755 1.00 103.28 ? 1270 VAL A CB  1 
ATOM   9702  C  CG1 . VAL A 1 1270 ? 34.282  -26.833 -26.661 1.00 99.73  ? 1270 VAL A CG1 1 
ATOM   9703  C  CG2 . VAL A 1 1270 ? 35.555  -27.393 -28.732 1.00 106.09 ? 1270 VAL A CG2 1 
ATOM   9704  N  N   . ILE A 1 1271 ? 32.940  -29.572 -25.603 1.00 95.51  ? 1271 ILE A N   1 
ATOM   9705  C  CA  . ILE A 1 1271 ? 32.371  -29.784 -24.286 1.00 92.94  ? 1271 ILE A CA  1 
ATOM   9706  C  C   . ILE A 1 1271 ? 32.680  -31.211 -23.788 1.00 93.69  ? 1271 ILE A C   1 
ATOM   9707  O  O   . ILE A 1 1271 ? 32.740  -31.415 -22.562 1.00 95.84  ? 1271 ILE A O   1 
ATOM   9708  C  CB  . ILE A 1 1271 ? 30.852  -29.470 -24.209 1.00 92.56  ? 1271 ILE A CB  1 
ATOM   9709  C  CG1 . ILE A 1 1271 ? 30.041  -30.473 -25.010 1.00 91.38  ? 1271 ILE A CG1 1 
ATOM   9710  C  CG2 . ILE A 1 1271 ? 30.582  -28.059 -24.688 1.00 91.63  ? 1271 ILE A CG2 1 
ATOM   9711  C  CD1 . ILE A 1 1271 ? 29.334  -31.503 -24.157 1.00 92.66  ? 1271 ILE A CD1 1 
ATOM   9712  N  N   . LYS A 1 1272 ? 32.876  -32.229 -24.662 1.00 122.80 ? 1272 LYS A N   1 
ATOM   9713  C  CA  . LYS A 1 1272 ? 33.174  -33.567 -24.075 1.00 131.18 ? 1272 LYS A CA  1 
ATOM   9714  C  C   . LYS A 1 1272 ? 34.330  -33.423 -23.088 1.00 136.79 ? 1272 LYS A C   1 
ATOM   9715  O  O   . LYS A 1 1272 ? 34.481  -34.227 -22.166 1.00 140.30 ? 1272 LYS A O   1 
ATOM   9716  C  CB  . LYS A 1 1272 ? 33.559  -34.652 -25.109 1.00 135.86 ? 1272 LYS A CB  1 
ATOM   9717  C  CG  . LYS A 1 1272 ? 34.477  -35.770 -24.582 1.00 137.77 ? 1272 LYS A CG  1 
ATOM   9718  C  CD  . LYS A 1 1272 ? 33.741  -37.055 -24.223 1.00 137.63 ? 1272 LYS A CD  1 
ATOM   9719  C  CE  . LYS A 1 1272 ? 34.645  -38.291 -24.273 1.00 143.86 ? 1272 LYS A CE  1 
ATOM   9720  N  NZ  . LYS A 1 1272 ? 33.915  -39.528 -23.882 1.00 146.14 ? 1272 LYS A NZ  1 
ATOM   9721  N  N   . TRP A 1 1273 ? 35.126  -32.393 -23.349 1.00 129.79 ? 1273 TRP A N   1 
ATOM   9722  C  CA  . TRP A 1 1273 ? 36.383  -32.183 -22.619 1.00 128.63 ? 1273 TRP A CA  1 
ATOM   9723  C  C   . TRP A 1 1273 ? 36.329  -31.090 -21.557 1.00 123.98 ? 1273 TRP A C   1 
ATOM   9724  O  O   . TRP A 1 1273 ? 37.029  -31.142 -20.562 1.00 127.87 ? 1273 TRP A O   1 
ATOM   9725  C  CB  . TRP A 1 1273 ? 37.449  -31.981 -23.659 1.00 129.80 ? 1273 TRP A CB  1 
ATOM   9726  C  CG  . TRP A 1 1273 ? 38.729  -31.337 -23.275 1.00 132.07 ? 1273 TRP A CG  1 
ATOM   9727  C  CD1 . TRP A 1 1273 ? 39.944  -31.963 -23.054 1.00 137.68 ? 1273 TRP A CD1 1 
ATOM   9728  C  CD2 . TRP A 1 1273 ? 38.973  -29.926 -23.089 1.00 131.02 ? 1273 TRP A CD2 1 
ATOM   9729  N  NE1 . TRP A 1 1273 ? 40.909  -31.031 -22.757 1.00 138.88 ? 1273 TRP A NE1 1 
ATOM   9730  C  CE2 . TRP A 1 1273 ? 40.346  -29.781 -22.771 1.00 134.52 ? 1273 TRP A CE2 1 
ATOM   9731  C  CE3 . TRP A 1 1273 ? 38.163  -28.785 -23.172 1.00 129.07 ? 1273 TRP A CE3 1 
ATOM   9732  C  CZ2 . TRP A 1 1273 ? 40.927  -28.519 -22.528 1.00 136.11 ? 1273 TRP A CZ2 1 
ATOM   9733  C  CZ3 . TRP A 1 1273 ? 38.745  -27.545 -22.941 1.00 130.42 ? 1273 TRP A CZ3 1 
ATOM   9734  C  CH2 . TRP A 1 1273 ? 40.114  -27.422 -22.620 1.00 133.70 ? 1273 TRP A CH2 1 
ATOM   9735  N  N   . LEU A 1 1274 ? 35.498  -30.099 -21.781 1.00 103.75 ? 1274 LEU A N   1 
ATOM   9736  C  CA  . LEU A 1 1274 ? 35.156  -29.249 -20.653 1.00 107.62 ? 1274 LEU A CA  1 
ATOM   9737  C  C   . LEU A 1 1274 ? 34.625  -30.222 -19.612 1.00 113.34 ? 1274 LEU A C   1 
ATOM   9738  O  O   . LEU A 1 1274 ? 35.309  -30.535 -18.656 1.00 117.66 ? 1274 LEU A O   1 
ATOM   9739  C  CB  . LEU A 1 1274 ? 34.162  -28.127 -21.003 1.00 109.24 ? 1274 LEU A CB  1 
ATOM   9740  C  CG  . LEU A 1 1274 ? 34.868  -26.922 -21.649 1.00 113.14 ? 1274 LEU A CG  1 
ATOM   9741  C  CD1 . LEU A 1 1274 ? 34.283  -25.615 -21.213 1.00 112.20 ? 1274 LEU A CD1 1 
ATOM   9742  C  CD2 . LEU A 1 1274 ? 36.311  -26.952 -21.308 1.00 116.56 ? 1274 LEU A CD2 1 
ATOM   9743  N  N   . SER A 1 1275 ? 33.458  -30.789 -19.848 1.00 89.29  ? 1275 SER A N   1 
ATOM   9744  C  CA  . SER A 1 1275 ? 32.884  -31.781 -18.927 1.00 94.82  ? 1275 SER A CA  1 
ATOM   9745  C  C   . SER A 1 1275 ? 33.737  -32.992 -18.458 1.00 97.77  ? 1275 SER A C   1 
ATOM   9746  O  O   . SER A 1 1275 ? 33.190  -33.996 -17.980 1.00 97.02  ? 1275 SER A O   1 
ATOM   9747  C  CB  . SER A 1 1275 ? 31.542  -32.290 -19.470 1.00 101.07 ? 1275 SER A CB  1 
ATOM   9748  O  OG  . SER A 1 1275 ? 30.970  -33.249 -18.593 1.00 106.32 ? 1275 SER A OG  1 
ATOM   9749  N  N   . GLU A 1 1276 ? 35.055  -32.903 -18.564 1.00 137.28 ? 1276 GLU A N   1 
ATOM   9750  C  CA  . GLU A 1 1276 ? 35.907  -33.869 -17.883 1.00 145.83 ? 1276 GLU A CA  1 
ATOM   9751  C  C   . GLU A 1 1276 ? 37.127  -33.178 -17.329 1.00 148.70 ? 1276 GLU A C   1 
ATOM   9752  O  O   . GLU A 1 1276 ? 37.948  -33.773 -16.630 1.00 154.11 ? 1276 GLU A O   1 
ATOM   9753  C  CB  . GLU A 1 1276 ? 36.294  -34.995 -18.811 1.00 151.53 ? 1276 GLU A CB  1 
ATOM   9754  C  CG  . GLU A 1 1276 ? 35.106  -35.826 -19.221 1.00 152.04 ? 1276 GLU A CG  1 
ATOM   9755  C  CD  . GLU A 1 1276 ? 35.494  -36.929 -20.176 1.00 152.22 ? 1276 GLU A CD  1 
ATOM   9756  O  OE1 . GLU A 1 1276 ? 36.617  -36.865 -20.716 1.00 152.67 ? 1276 GLU A OE1 1 
ATOM   9757  O  OE2 . GLU A 1 1276 ? 34.687  -37.861 -20.378 1.00 151.78 ? 1276 GLU A OE2 1 
ATOM   9758  N  N   . GLU A 1 1277 ? 37.225  -31.905 -17.675 1.00 194.28 ? 1277 GLU A N   1 
ATOM   9759  C  CA  . GLU A 1 1277 ? 38.130  -30.985 -17.030 1.00 197.04 ? 1277 GLU A CA  1 
ATOM   9760  C  C   . GLU A 1 1277 ? 37.574  -30.607 -15.679 1.00 196.73 ? 1277 GLU A C   1 
ATOM   9761  O  O   . GLU A 1 1277 ? 38.177  -30.919 -14.658 1.00 199.45 ? 1277 GLU A O   1 
ATOM   9762  C  CB  . GLU A 1 1277 ? 38.270  -29.726 -17.871 1.00 195.30 ? 1277 GLU A CB  1 
ATOM   9763  C  CG  . GLU A 1 1277 ? 39.655  -29.174 -17.826 1.00 197.76 ? 1277 GLU A CG  1 
ATOM   9764  C  CD  . GLU A 1 1277 ? 40.697  -30.230 -18.178 1.00 201.91 ? 1277 GLU A CD  1 
ATOM   9765  O  OE1 . GLU A 1 1277 ? 41.907  -29.913 -18.127 1.00 205.88 ? 1277 GLU A OE1 1 
ATOM   9766  O  OE2 . GLU A 1 1277 ? 40.312  -31.378 -18.512 1.00 202.30 ? 1277 GLU A OE2 1 
ATOM   9767  N  N   . GLN A 1 1278 ? 36.401  -29.964 -15.695 1.00 131.91 ? 1278 GLN A N   1 
ATOM   9768  C  CA  . GLN A 1 1278 ? 35.730  -29.450 -14.490 1.00 136.26 ? 1278 GLN A CA  1 
ATOM   9769  C  C   . GLN A 1 1278 ? 35.984  -30.347 -13.266 1.00 143.16 ? 1278 GLN A C   1 
ATOM   9770  O  O   . GLN A 1 1278 ? 35.894  -31.574 -13.366 1.00 143.83 ? 1278 GLN A O   1 
ATOM   9771  C  CB  . GLN A 1 1278 ? 34.211  -29.224 -14.731 1.00 140.37 ? 1278 GLN A CB  1 
ATOM   9772  C  CG  . GLN A 1 1278 ? 33.867  -28.115 -15.740 1.00 169.33 ? 1278 GLN A CG  1 
ATOM   9773  C  CD  . GLN A 1 1278 ? 34.821  -26.905 -15.720 1.00 124.21 ? 1278 GLN A CD  1 
ATOM   9774  O  OE1 . GLN A 1 1278 ? 34.374  -25.761 -15.663 1.00 121.31 ? 1278 GLN A OE1 1 
ATOM   9775  N  NE2 . GLN A 1 1278 ? 36.126  -27.154 -15.816 1.00 125.49 ? 1278 GLN A NE2 1 
ATOM   9776  N  N   . ARG A 1 1279 ? 36.327  -29.742 -12.125 1.00 147.33 ? 1279 ARG A N   1 
ATOM   9777  C  CA  . ARG A 1 1279 ? 36.663  -30.528 -10.945 1.00 150.37 ? 1279 ARG A CA  1 
ATOM   9778  C  C   . ARG A 1 1279 ? 35.513  -30.685 -9.962  1.00 145.95 ? 1279 ARG A C   1 
ATOM   9779  O  O   . ARG A 1 1279 ? 34.851  -29.713 -9.602  1.00 143.40 ? 1279 ARG A O   1 
ATOM   9780  C  CB  . ARG A 1 1279 ? 37.945  -30.022 -10.286 1.00 159.01 ? 1279 ARG A CB  1 
ATOM   9781  C  CG  . ARG A 1 1279 ? 39.180  -30.322 -11.173 1.00 163.32 ? 1279 ARG A CG  1 
ATOM   9782  C  CD  . ARG A 1 1279 ? 40.501  -30.319 -10.430 1.00 173.64 ? 1279 ARG A CD  1 
ATOM   9783  N  NE  . ARG A 1 1279 ? 40.327  -30.639 -9.026  1.00 180.93 ? 1279 ARG A NE  1 
ATOM   9784  C  CZ  . ARG A 1 1279 ? 41.333  -30.852 -8.197  1.00 188.52 ? 1279 ARG A CZ  1 
ATOM   9785  N  NH1 . ARG A 1 1279 ? 42.577  -30.789 -8.651  1.00 189.32 ? 1279 ARG A NH1 1 
ATOM   9786  N  NH2 . ARG A 1 1279 ? 41.087  -31.149 -6.931  1.00 194.34 ? 1279 ARG A NH2 1 
ATOM   9787  N  N   . TYR A 1 1280 ? 35.274  -31.935 -9.563  1.00 178.66 ? 1280 TYR A N   1 
ATOM   9788  C  CA  . TYR A 1 1280 ? 34.146  -32.283 -8.701  1.00 180.27 ? 1280 TYR A CA  1 
ATOM   9789  C  C   . TYR A 1 1280 ? 33.736  -31.056 -7.938  1.00 161.82 ? 1280 TYR A C   1 
ATOM   9790  O  O   . TYR A 1 1280 ? 34.566  -30.412 -7.313  1.00 162.94 ? 1280 TYR A O   1 
ATOM   9791  C  CB  . TYR A 1 1280 ? 34.543  -33.393 -7.730  1.00 185.00 ? 1280 TYR A CB  1 
ATOM   9792  C  CG  . TYR A 1 1280 ? 33.578  -33.598 -6.585  1.00 185.69 ? 1280 TYR A CG  1 
ATOM   9793  C  CD1 . TYR A 1 1280 ? 34.026  -34.106 -5.367  1.00 195.70 ? 1280 TYR A CD1 1 
ATOM   9794  C  CD2 . TYR A 1 1280 ? 32.227  -33.281 -6.714  1.00 179.01 ? 1280 TYR A CD2 1 
ATOM   9795  C  CE1 . TYR A 1 1280 ? 33.163  -34.298 -4.309  1.00 198.92 ? 1280 TYR A CE1 1 
ATOM   9796  C  CE2 . TYR A 1 1280 ? 31.356  -33.470 -5.662  1.00 184.59 ? 1280 TYR A CE2 1 
ATOM   9797  C  CZ  . TYR A 1 1280 ? 31.836  -33.983 -4.456  1.00 194.16 ? 1280 TYR A CZ  1 
ATOM   9798  O  OH  . TYR A 1 1280 ? 30.989  -34.182 -3.391  1.00 199.00 ? 1280 TYR A OH  1 
ATOM   9799  N  N   . GLY A 1 1281 ? 32.465  -30.708 -8.016  1.00 93.88  ? 1281 GLY A N   1 
ATOM   9800  C  CA  . GLY A 1 1281 ? 32.028  -29.457 -7.451  1.00 93.68  ? 1281 GLY A CA  1 
ATOM   9801  C  C   . GLY A 1 1281 ? 31.932  -28.283 -8.421  1.00 91.31  ? 1281 GLY A C   1 
ATOM   9802  O  O   . GLY A 1 1281 ? 30.843  -27.850 -8.743  1.00 90.61  ? 1281 GLY A O   1 
ATOM   9803  N  N   . GLY A 1 1282 ? 33.052  -27.752 -8.887  1.00 126.92 ? 1282 GLY A N   1 
ATOM   9804  C  CA  . GLY A 1 1282 ? 33.024  -26.542 -9.689  1.00 130.33 ? 1282 GLY A CA  1 
ATOM   9805  C  C   . GLY A 1 1282 ? 34.208  -26.538 -10.626 1.00 143.07 ? 1282 GLY A C   1 
ATOM   9806  O  O   . GLY A 1 1282 ? 34.981  -27.495 -10.650 1.00 144.96 ? 1282 GLY A O   1 
ATOM   9807  N  N   . GLY A 1 1283 ? 34.375  -25.465 -11.391 1.00 102.00 ? 1283 GLY A N   1 
ATOM   9808  C  CA  . GLY A 1 1283 ? 35.339  -25.484 -12.492 1.00 110.63 ? 1283 GLY A CA  1 
ATOM   9809  C  C   . GLY A 1 1283 ? 36.843  -25.497 -12.241 1.00 115.10 ? 1283 GLY A C   1 
ATOM   9810  O  O   . GLY A 1 1283 ? 37.573  -24.801 -12.927 1.00 110.90 ? 1283 GLY A O   1 
ATOM   9811  N  N   . PHE A 1 1284 ? 37.311  -26.318 -11.308 1.00 175.85 ? 1284 PHE A N   1 
ATOM   9812  C  CA  . PHE A 1 1284 ? 38.651  -26.175 -10.725 1.00 190.99 ? 1284 PHE A CA  1 
ATOM   9813  C  C   . PHE A 1 1284 ? 39.439  -24.903 -11.042 1.00 181.72 ? 1284 PHE A C   1 
ATOM   9814  O  O   . PHE A 1 1284 ? 39.367  -23.922 -10.302 1.00 186.41 ? 1284 PHE A O   1 
ATOM   9815  C  CB  . PHE A 1 1284 ? 39.537  -27.373 -11.001 1.00 215.49 ? 1284 PHE A CB  1 
ATOM   9816  C  CG  . PHE A 1 1284 ? 40.626  -27.552 -9.980  1.00 249.29 ? 1284 PHE A CG  1 
ATOM   9817  C  CD1 . PHE A 1 1284 ? 40.317  -27.625 -8.631  1.00 267.20 ? 1284 PHE A CD1 1 
ATOM   9818  C  CD2 . PHE A 1 1284 ? 41.950  -27.661 -10.362 1.00 265.32 ? 1284 PHE A CD2 1 
ATOM   9819  C  CE1 . PHE A 1 1284 ? 41.307  -27.793 -7.688  1.00 286.54 ? 1284 PHE A CE1 1 
ATOM   9820  C  CE2 . PHE A 1 1284 ? 42.945  -27.834 -9.426  1.00 282.81 ? 1284 PHE A CE2 1 
ATOM   9821  C  CZ  . PHE A 1 1284 ? 42.624  -27.897 -8.085  1.00 295.96 ? 1284 PHE A CZ  1 
ATOM   9822  N  N   . TYR A 1 1285 ? 40.217  -24.928 -12.118 1.00 170.79 ? 1285 TYR A N   1 
ATOM   9823  C  CA  . TYR A 1 1285 ? 41.178  -23.851 -12.373 1.00 161.25 ? 1285 TYR A CA  1 
ATOM   9824  C  C   . TYR A 1 1285 ? 40.571  -22.456 -12.207 1.00 155.14 ? 1285 TYR A C   1 
ATOM   9825  O  O   . TYR A 1 1285 ? 39.593  -22.130 -12.880 1.00 154.99 ? 1285 TYR A O   1 
ATOM   9826  C  CB  . TYR A 1 1285 ? 41.786  -23.985 -13.775 1.00 155.34 ? 1285 TYR A CB  1 
ATOM   9827  C  CG  . TYR A 1 1285 ? 42.272  -25.369 -14.092 1.00 155.29 ? 1285 TYR A CG  1 
ATOM   9828  C  CD1 . TYR A 1 1285 ? 42.607  -26.250 -13.083 1.00 158.32 ? 1285 TYR A CD1 1 
ATOM   9829  C  CD2 . TYR A 1 1285 ? 42.397  -25.795 -15.395 1.00 152.28 ? 1285 TYR A CD2 1 
ATOM   9830  C  CE1 . TYR A 1 1285 ? 43.048  -27.519 -13.366 1.00 159.11 ? 1285 TYR A CE1 1 
ATOM   9831  C  CE2 . TYR A 1 1285 ? 42.833  -27.058 -15.690 1.00 152.22 ? 1285 TYR A CE2 1 
ATOM   9832  C  CZ  . TYR A 1 1285 ? 43.162  -27.919 -14.675 1.00 156.11 ? 1285 TYR A CZ  1 
ATOM   9833  O  OH  . TYR A 1 1285 ? 43.607  -29.179 -14.969 1.00 159.14 ? 1285 TYR A OH  1 
ATOM   9834  N  N   . SER A 1 1286 ? 41.136  -21.657 -11.301 1.00 149.89 ? 1286 SER A N   1 
ATOM   9835  C  CA  . SER A 1 1286 ? 40.820  -20.224 -11.199 1.00 142.35 ? 1286 SER A CA  1 
ATOM   9836  C  C   . SER A 1 1286 ? 39.358  -19.778 -11.468 1.00 134.80 ? 1286 SER A C   1 
ATOM   9837  O  O   . SER A 1 1286 ? 38.402  -20.559 -11.390 1.00 133.23 ? 1286 SER A O   1 
ATOM   9838  C  CB  . SER A 1 1286 ? 41.822  -19.392 -12.032 1.00 140.63 ? 1286 SER A CB  1 
ATOM   9839  O  OG  . SER A 1 1286 ? 41.559  -17.987 -11.984 1.00 137.60 ? 1286 SER A OG  1 
ATOM   9840  N  N   . THR A 1 1287 ? 39.209  -18.498 -11.787 1.00 170.76 ? 1287 THR A N   1 
ATOM   9841  C  CA  . THR A 1 1287 ? 37.906  -17.868 -11.865 1.00 172.18 ? 1287 THR A CA  1 
ATOM   9842  C  C   . THR A 1 1287 ? 37.473  -17.624 -13.299 1.00 175.71 ? 1287 THR A C   1 
ATOM   9843  O  O   . THR A 1 1287 ? 36.566  -18.289 -13.796 1.00 175.45 ? 1287 THR A O   1 
ATOM   9844  C  CB  . THR A 1 1287 ? 37.928  -16.513 -11.138 1.00 170.46 ? 1287 THR A CB  1 
ATOM   9845  O  OG1 . THR A 1 1287 ? 39.081  -15.764 -11.550 1.00 169.39 ? 1287 THR A OG1 1 
ATOM   9846  C  CG2 . THR A 1 1287 ? 37.988  -16.718 -9.642  1.00 175.17 ? 1287 THR A CG2 1 
ATOM   9847  N  N   . GLN A 1 1288 ? 38.139  -16.671 -13.953 1.00 190.64 ? 1288 GLN A N   1 
ATOM   9848  C  CA  . GLN A 1 1288 ? 37.719  -16.156 -15.258 1.00 189.31 ? 1288 GLN A CA  1 
ATOM   9849  C  C   . GLN A 1 1288 ? 37.333  -17.254 -16.224 1.00 190.81 ? 1288 GLN A C   1 
ATOM   9850  O  O   . GLN A 1 1288 ? 36.413  -17.096 -17.025 1.00 191.87 ? 1288 GLN A O   1 
ATOM   9851  C  CB  . GLN A 1 1288 ? 38.809  -15.276 -15.873 1.00 188.68 ? 1288 GLN A CB  1 
ATOM   9852  C  CG  . GLN A 1 1288 ? 38.846  -13.878 -15.305 1.00 189.93 ? 1288 GLN A CG  1 
ATOM   9853  C  CD  . GLN A 1 1288 ? 37.572  -13.129 -15.583 1.00 187.17 ? 1288 GLN A CD  1 
ATOM   9854  O  OE1 . GLN A 1 1288 ? 37.116  -13.076 -16.718 1.00 186.90 ? 1288 GLN A OE1 1 
ATOM   9855  N  NE2 . GLN A 1 1288 ? 36.986  -12.548 -14.548 1.00 186.35 ? 1288 GLN A NE2 1 
ATOM   9856  N  N   . ASP A 1 1289 ? 38.040  -18.371 -16.150 1.00 153.53 ? 1289 ASP A N   1 
ATOM   9857  C  CA  . ASP A 1 1289 ? 37.659  -19.526 -16.940 1.00 152.60 ? 1289 ASP A CA  1 
ATOM   9858  C  C   . ASP A 1 1289 ? 36.334  -20.120 -16.453 1.00 150.68 ? 1289 ASP A C   1 
ATOM   9859  O  O   . ASP A 1 1289 ? 35.384  -20.223 -17.225 1.00 151.59 ? 1289 ASP A O   1 
ATOM   9860  C  CB  . ASP A 1 1289 ? 38.779  -20.577 -16.960 1.00 155.57 ? 1289 ASP A CB  1 
ATOM   9861  C  CG  . ASP A 1 1289 ? 39.141  -21.057 -15.596 1.00 159.15 ? 1289 ASP A CG  1 
ATOM   9862  O  OD1 . ASP A 1 1289 ? 39.880  -20.338 -14.903 1.00 160.23 ? 1289 ASP A OD1 1 
ATOM   9863  O  OD2 . ASP A 1 1289 ? 38.667  -22.145 -15.215 1.00 161.41 ? 1289 ASP A OD2 1 
ATOM   9864  N  N   . THR A 1 1290 ? 36.267  -20.460 -15.167 1.00 116.45 ? 1290 THR A N   1 
ATOM   9865  C  CA  . THR A 1 1290 ? 35.137  -21.208 -14.611 1.00 109.01 ? 1290 THR A CA  1 
ATOM   9866  C  C   . THR A 1 1290 ? 33.762  -20.467 -14.600 1.00 98.91  ? 1290 THR A C   1 
ATOM   9867  O  O   . THR A 1 1290 ? 32.759  -21.021 -14.129 1.00 95.97  ? 1290 THR A O   1 
ATOM   9868  C  CB  . THR A 1 1290 ? 35.489  -21.828 -13.222 1.00 112.09 ? 1290 THR A CB  1 
ATOM   9869  O  OG1 . THR A 1 1290 ? 36.677  -22.612 -13.343 1.00 114.71 ? 1290 THR A OG1 1 
ATOM   9870  C  CG2 . THR A 1 1290 ? 34.373  -22.734 -12.733 1.00 108.55 ? 1290 THR A CG2 1 
ATOM   9871  N  N   . ILE A 1 1291 ? 33.700  -19.240 -15.128 1.00 142.68 ? 1291 ILE A N   1 
ATOM   9872  C  CA  . ILE A 1 1291 ? 32.411  -18.559 -15.336 1.00 139.03 ? 1291 ILE A CA  1 
ATOM   9873  C  C   . ILE A 1 1291 ? 32.011  -18.675 -16.791 1.00 135.29 ? 1291 ILE A C   1 
ATOM   9874  O  O   . ILE A 1 1291 ? 30.883  -19.035 -17.121 1.00 135.84 ? 1291 ILE A O   1 
ATOM   9875  C  CB  . ILE A 1 1291 ? 32.461  -17.069 -14.954 1.00 128.57 ? 1291 ILE A CB  1 
ATOM   9876  C  CG1 . ILE A 1 1291 ? 31.383  -16.282 -15.719 1.00 121.71 ? 1291 ILE A CG1 1 
ATOM   9877  C  CG2 . ILE A 1 1291 ? 33.845  -16.496 -15.216 1.00 129.32 ? 1291 ILE A CG2 1 
ATOM   9878  C  CD1 . ILE A 1 1291 ? 31.176  -14.884 -15.171 1.00 119.14 ? 1291 ILE A CD1 1 
ATOM   9879  N  N   . ASN A 1 1292 ? 32.967  -18.377 -17.657 1.00 107.54 ? 1292 ASN A N   1 
ATOM   9880  C  CA  . ASN A 1 1292 ? 32.831  -18.704 -19.048 1.00 104.60 ? 1292 ASN A CA  1 
ATOM   9881  C  C   . ASN A 1 1292 ? 32.630  -20.207 -19.160 1.00 106.15 ? 1292 ASN A C   1 
ATOM   9882  O  O   . ASN A 1 1292 ? 31.656  -20.671 -19.748 1.00 107.73 ? 1292 ASN A O   1 
ATOM   9883  C  CB  . ASN A 1 1292 ? 34.076  -18.262 -19.803 1.00 103.85 ? 1292 ASN A CB  1 
ATOM   9884  C  CG  . ASN A 1 1292 ? 34.399  -16.790 -19.584 1.00 104.50 ? 1292 ASN A CG  1 
ATOM   9885  O  OD1 . ASN A 1 1292 ? 33.520  -15.923 -19.582 1.00 103.33 ? 1292 ASN A OD1 1 
ATOM   9886  N  ND2 . ASN A 1 1292 ? 35.674  -16.503 -19.398 1.00 105.48 ? 1292 ASN A ND2 1 
ATOM   9887  N  N   . ALA A 1 1293 ? 33.524  -20.976 -18.558 1.00 89.22  ? 1293 ALA A N   1 
ATOM   9888  C  CA  . ALA A 1 1293 ? 33.409  -22.423 -18.634 1.00 85.94  ? 1293 ALA A CA  1 
ATOM   9889  C  C   . ALA A 1 1293 ? 31.999  -22.867 -18.237 1.00 87.16  ? 1293 ALA A C   1 
ATOM   9890  O  O   . ALA A 1 1293 ? 31.412  -23.742 -18.874 1.00 86.31  ? 1293 ALA A O   1 
ATOM   9891  C  CB  . ALA A 1 1293 ? 34.478  -23.099 -17.759 1.00 90.29  ? 1293 ALA A CB  1 
ATOM   9892  N  N   . ILE A 1 1294 ? 31.437  -22.229 -17.215 1.00 148.60 ? 1294 ILE A N   1 
ATOM   9893  C  CA  . ILE A 1 1294 ? 30.088  -22.582 -16.772 1.00 149.06 ? 1294 ILE A CA  1 
ATOM   9894  C  C   . ILE A 1 1294 ? 29.026  -22.015 -17.714 1.00 148.15 ? 1294 ILE A C   1 
ATOM   9895  O  O   . ILE A 1 1294 ? 27.976  -22.630 -17.903 1.00 149.17 ? 1294 ILE A O   1 
ATOM   9896  C  CB  . ILE A 1 1294 ? 29.772  -22.146 -15.303 1.00 149.13 ? 1294 ILE A CB  1 
ATOM   9897  C  CG1 . ILE A 1 1294 ? 30.752  -22.773 -14.299 1.00 149.86 ? 1294 ILE A CG1 1 
ATOM   9898  C  CG2 . ILE A 1 1294 ? 28.338  -22.517 -14.931 1.00 147.74 ? 1294 ILE A CG2 1 
ATOM   9899  C  CD1 . ILE A 1 1294 ? 30.601  -24.258 -14.064 1.00 148.94 ? 1294 ILE A CD1 1 
ATOM   9900  N  N   . GLU A 1 1295 ? 29.296  -20.849 -18.300 1.00 152.49 ? 1295 GLU A N   1 
ATOM   9901  C  CA  . GLU A 1 1295 ? 28.353  -20.243 -19.239 1.00 149.94 ? 1295 GLU A CA  1 
ATOM   9902  C  C   . GLU A 1 1295 ? 28.150  -21.158 -20.422 1.00 143.63 ? 1295 GLU A C   1 
ATOM   9903  O  O   . GLU A 1 1295 ? 27.017  -21.423 -20.843 1.00 141.92 ? 1295 GLU A O   1 
ATOM   9904  C  CB  . GLU A 1 1295 ? 28.836  -18.875 -19.730 1.00 156.01 ? 1295 GLU A CB  1 
ATOM   9905  C  CG  . GLU A 1 1295 ? 28.121  -18.422 -20.995 1.00 159.77 ? 1295 GLU A CG  1 
ATOM   9906  C  CD  . GLU A 1 1295 ? 28.003  -16.921 -21.097 1.00 163.86 ? 1295 GLU A CD  1 
ATOM   9907  O  OE1 . GLU A 1 1295 ? 28.648  -16.206 -20.293 1.00 163.42 ? 1295 GLU A OE1 1 
ATOM   9908  O  OE2 . GLU A 1 1295 ? 27.251  -16.462 -21.984 1.00 166.24 ? 1295 GLU A OE2 1 
ATOM   9909  N  N   . GLY A 1 1296 ? 29.268  -21.634 -20.959 1.00 114.29 ? 1296 GLY A N   1 
ATOM   9910  C  CA  . GLY A 1 1296 ? 29.226  -22.729 -21.899 1.00 115.08 ? 1296 GLY A CA  1 
ATOM   9911  C  C   . GLY A 1 1296 ? 28.314  -23.819 -21.369 1.00 113.89 ? 1296 GLY A C   1 
ATOM   9912  O  O   . GLY A 1 1296 ? 27.098  -23.790 -21.570 1.00 112.73 ? 1296 GLY A O   1 
ATOM   9913  N  N   . LEU A 1 1297 ? 28.899  -24.761 -20.650 1.00 94.62  ? 1297 LEU A N   1 
ATOM   9914  C  CA  . LEU A 1 1297 ? 28.194  -25.970 -20.250 1.00 95.30  ? 1297 LEU A CA  1 
ATOM   9915  C  C   . LEU A 1 1297 ? 26.698  -25.889 -19.971 1.00 98.75  ? 1297 LEU A C   1 
ATOM   9916  O  O   . LEU A 1 1297 ? 25.996  -26.908 -19.975 1.00 97.91  ? 1297 LEU A O   1 
ATOM   9917  C  CB  . LEU A 1 1297 ? 28.913  -26.586 -19.075 1.00 94.10  ? 1297 LEU A CB  1 
ATOM   9918  C  CG  . LEU A 1 1297 ? 29.904  -27.584 -19.675 1.00 95.85  ? 1297 LEU A CG  1 
ATOM   9919  C  CD1 . LEU A 1 1297 ? 31.345  -27.051 -19.744 1.00 96.14  ? 1297 LEU A CD1 1 
ATOM   9920  C  CD2 . LEU A 1 1297 ? 29.789  -28.908 -18.938 1.00 98.67  ? 1297 LEU A CD2 1 
ATOM   9921  N  N   . THR A 1 1298 ? 26.222  -24.681 -19.709 1.00 164.14 ? 1298 THR A N   1 
ATOM   9922  C  CA  . THR A 1 1298 ? 24.796  -24.452 -19.576 1.00 164.17 ? 1298 THR A CA  1 
ATOM   9923  C  C   . THR A 1 1298 ? 24.263  -24.134 -20.961 1.00 162.27 ? 1298 THR A C   1 
ATOM   9924  O  O   . THR A 1 1298 ? 23.426  -24.871 -21.504 1.00 159.66 ? 1298 THR A O   1 
ATOM   9925  C  CB  . THR A 1 1298 ? 24.461  -23.284 -18.603 1.00 162.04 ? 1298 THR A CB  1 
ATOM   9926  O  OG1 . THR A 1 1298 ? 25.315  -23.323 -17.445 1.00 163.97 ? 1298 THR A OG1 1 
ATOM   9927  C  CG2 . THR A 1 1298 ? 23.002  -23.353 -18.178 1.00 161.28 ? 1298 THR A CG2 1 
ATOM   9928  N  N   . GLU A 1 1299 ? 24.789  -23.052 -21.539 1.00 131.11 ? 1299 GLU A N   1 
ATOM   9929  C  CA  . GLU A 1 1299 ? 24.303  -22.528 -22.813 1.00 132.40 ? 1299 GLU A CA  1 
ATOM   9930  C  C   . GLU A 1 1299 ? 24.104  -23.664 -23.773 1.00 131.96 ? 1299 GLU A C   1 
ATOM   9931  O  O   . GLU A 1 1299 ? 23.070  -23.771 -24.423 1.00 134.68 ? 1299 GLU A O   1 
ATOM   9932  C  CB  . GLU A 1 1299 ? 25.300  -21.535 -23.406 1.00 134.30 ? 1299 GLU A CB  1 
ATOM   9933  C  CG  . GLU A 1 1299 ? 24.627  -20.411 -24.146 1.00 139.62 ? 1299 GLU A CG  1 
ATOM   9934  C  CD  . GLU A 1 1299 ? 23.678  -19.648 -23.245 1.00 144.54 ? 1299 GLU A CD  1 
ATOM   9935  O  OE1 . GLU A 1 1299 ? 24.155  -18.816 -22.440 1.00 147.74 ? 1299 GLU A OE1 1 
ATOM   9936  O  OE2 . GLU A 1 1299 ? 22.457  -19.898 -23.331 1.00 144.78 ? 1299 GLU A OE2 1 
ATOM   9937  N  N   . TYR A 1 1300 ? 25.121  -24.515 -23.821 1.00 98.96  ? 1300 TYR A N   1 
ATOM   9938  C  CA  . TYR A 1 1300 ? 25.126  -25.697 -24.660 1.00 96.01  ? 1300 TYR A CA  1 
ATOM   9939  C  C   . TYR A 1 1300 ? 24.131  -26.789 -24.260 1.00 92.13  ? 1300 TYR A C   1 
ATOM   9940  O  O   . TYR A 1 1300 ? 23.570  -27.432 -25.142 1.00 86.75  ? 1300 TYR A O   1 
ATOM   9941  C  CB  . TYR A 1 1300 ? 26.531  -26.307 -24.762 1.00 100.35 ? 1300 TYR A CB  1 
ATOM   9942  C  CG  . TYR A 1 1300 ? 26.559  -27.708 -25.384 1.00 100.42 ? 1300 TYR A CG  1 
ATOM   9943  C  CD1 . TYR A 1 1300 ? 26.979  -27.909 -26.702 1.00 102.16 ? 1300 TYR A CD1 1 
ATOM   9944  C  CD2 . TYR A 1 1300 ? 26.150  -28.835 -24.657 1.00 98.53  ? 1300 TYR A CD2 1 
ATOM   9945  C  CE1 . TYR A 1 1300 ? 27.001  -29.204 -27.274 1.00 103.13 ? 1300 TYR A CE1 1 
ATOM   9946  C  CE2 . TYR A 1 1300 ? 26.156  -30.118 -25.229 1.00 99.81  ? 1300 TYR A CE2 1 
ATOM   9947  C  CZ  . TYR A 1 1300 ? 26.583  -30.295 -26.526 1.00 103.64 ? 1300 TYR A CZ  1 
ATOM   9948  O  OH  . TYR A 1 1300 ? 26.592  -31.575 -27.039 1.00 107.68 ? 1300 TYR A OH  1 
ATOM   9949  N  N   . SER A 1 1301 ? 23.935  -27.059 -22.971 1.00 96.17  ? 1301 SER A N   1 
ATOM   9950  C  CA  . SER A 1 1301 ? 22.899  -28.039 -22.620 1.00 99.39  ? 1301 SER A CA  1 
ATOM   9951  C  C   . SER A 1 1301 ? 21.520  -27.396 -22.848 1.00 94.75  ? 1301 SER A C   1 
ATOM   9952  O  O   . SER A 1 1301 ? 20.471  -28.051 -22.786 1.00 90.85  ? 1301 SER A O   1 
ATOM   9953  C  CB  . SER A 1 1301 ? 23.070  -28.627 -21.217 1.00 105.80 ? 1301 SER A CB  1 
ATOM   9954  O  OG  . SER A 1 1301 ? 23.010  -30.065 -21.245 1.00 108.96 ? 1301 SER A OG  1 
ATOM   9955  N  N   . LEU A 1 1302 ? 21.557  -26.103 -23.153 1.00 142.69 ? 1302 LEU A N   1 
ATOM   9956  C  CA  . LEU A 1 1302 ? 20.372  -25.319 -23.449 1.00 146.85 ? 1302 LEU A CA  1 
ATOM   9957  C  C   . LEU A 1 1302 ? 19.978  -25.389 -24.911 1.00 149.14 ? 1302 LEU A C   1 
ATOM   9958  O  O   . LEU A 1 1302 ? 18.785  -25.484 -25.249 1.00 155.10 ? 1302 LEU A O   1 
ATOM   9959  C  CB  . LEU A 1 1302 ? 20.671  -23.871 -23.120 1.00 150.95 ? 1302 LEU A CB  1 
ATOM   9960  C  CG  . LEU A 1 1302 ? 19.822  -23.370 -21.969 1.00 154.21 ? 1302 LEU A CG  1 
ATOM   9961  C  CD1 . LEU A 1 1302 ? 20.250  -21.957 -21.644 1.00 154.16 ? 1302 LEU A CD1 1 
ATOM   9962  C  CD2 . LEU A 1 1302 ? 18.321  -23.478 -22.306 1.00 155.44 ? 1302 LEU A CD2 1 
ATOM   9963  N  N   . LEU A 1 1303 ? 21.021  -25.348 -25.748 1.00 137.92 ? 1303 LEU A N   1 
ATOM   9964  C  CA  . LEU A 1 1303 ? 20.985  -25.263 -27.220 1.00 132.48 ? 1303 LEU A CA  1 
ATOM   9965  C  C   . LEU A 1 1303 ? 20.797  -26.605 -27.970 1.00 127.55 ? 1303 LEU A C   1 
ATOM   9966  O  O   . LEU A 1 1303 ? 19.900  -26.708 -28.814 1.00 126.99 ? 1303 LEU A O   1 
ATOM   9967  C  CB  . LEU A 1 1303 ? 22.267  -24.547 -27.673 1.00 132.66 ? 1303 LEU A CB  1 
ATOM   9968  C  CG  . LEU A 1 1303 ? 22.628  -24.336 -29.124 1.00 130.61 ? 1303 LEU A CG  1 
ATOM   9969  C  CD1 . LEU A 1 1303 ? 23.241  -25.609 -29.634 1.00 128.38 ? 1303 LEU A CD1 1 
ATOM   9970  C  CD2 . LEU A 1 1303 ? 21.377  -23.938 -29.887 1.00 132.49 ? 1303 LEU A CD2 1 
ATOM   9971  N  N   . VAL A 1 1304 ? 21.653  -27.595 -27.677 1.00 105.72 ? 1304 VAL A N   1 
ATOM   9972  C  CA  . VAL A 1 1304 ? 21.426  -29.023 -27.981 1.00 109.96 ? 1304 VAL A CA  1 
ATOM   9973  C  C   . VAL A 1 1304 ? 20.104  -29.497 -27.351 1.00 109.76 ? 1304 VAL A C   1 
ATOM   9974  O  O   . VAL A 1 1304 ? 19.355  -28.671 -26.863 1.00 113.40 ? 1304 VAL A O   1 
ATOM   9975  C  CB  . VAL A 1 1304 ? 22.550  -29.847 -27.377 1.00 114.03 ? 1304 VAL A CB  1 
ATOM   9976  C  CG1 . VAL A 1 1304 ? 22.373  -31.320 -27.668 1.00 117.85 ? 1304 VAL A CG1 1 
ATOM   9977  C  CG2 . VAL A 1 1304 ? 23.855  -29.357 -27.898 1.00 113.15 ? 1304 VAL A CG2 1 
ATOM   9978  N  N   . LYS A 1 1305 ? 19.790  -30.793 -27.332 1.00 130.88 ? 1305 LYS A N   1 
ATOM   9979  C  CA  . LYS A 1 1305 ? 18.633  -31.218 -26.533 1.00 134.16 ? 1305 LYS A CA  1 
ATOM   9980  C  C   . LYS A 1 1305 ? 18.965  -32.321 -25.539 1.00 139.84 ? 1305 LYS A C   1 
ATOM   9981  O  O   . LYS A 1 1305 ? 19.800  -33.175 -25.803 1.00 141.55 ? 1305 LYS A O   1 
ATOM   9982  C  CB  . LYS A 1 1305 ? 17.406  -31.577 -27.386 1.00 135.20 ? 1305 LYS A CB  1 
ATOM   9983  C  CG  . LYS A 1 1305 ? 16.049  -31.344 -26.678 1.00 143.43 ? 1305 LYS A CG  1 
ATOM   9984  C  CD  . LYS A 1 1305 ? 14.893  -30.942 -27.662 1.00 154.07 ? 1305 LYS A CD  1 
ATOM   9985  C  CE  . LYS A 1 1305 ? 15.187  -29.616 -28.417 1.00 164.22 ? 1305 LYS A CE  1 
ATOM   9986  N  NZ  . LYS A 1 1305 ? 14.073  -29.053 -29.254 1.00 162.71 ? 1305 LYS A NZ  1 
ATOM   9987  N  N   . GLN A 1 1306 ? 18.306  -32.268 -24.385 1.00 154.89 ? 1306 GLN A N   1 
ATOM   9988  C  CA  . GLN A 1 1306 ? 18.601  -33.160 -23.263 1.00 156.84 ? 1306 GLN A CA  1 
ATOM   9989  C  C   . GLN A 1 1306 ? 18.255  -34.615 -23.575 1.00 159.21 ? 1306 GLN A C   1 
ATOM   9990  O  O   . GLN A 1 1306 ? 17.362  -34.905 -24.376 1.00 160.45 ? 1306 GLN A O   1 
ATOM   9991  C  CB  . GLN A 1 1306 ? 17.882  -32.698 -21.972 1.00 196.87 ? 1306 GLN A CB  1 
ATOM   9992  C  CG  . GLN A 1 1306 ? 18.758  -31.904 -20.936 1.00 248.56 ? 1306 GLN A CG  1 
ATOM   9993  C  CD  . GLN A 1 1306 ? 18.041  -31.568 -19.592 1.00 180.20 ? 1306 GLN A CD  1 
ATOM   9994  O  OE1 . GLN A 1 1306 ? 17.736  -32.447 -18.778 1.00 181.45 ? 1306 GLN A OE1 1 
ATOM   9995  N  NE2 . GLN A 1 1306 ? 17.804  -30.289 -19.365 1.00 180.80 ? 1306 GLN A NE2 1 
ATOM   9996  N  N   . LEU A 1 1307 ? 18.970  -35.525 -22.927 1.00 155.72 ? 1307 LEU A N   1 
ATOM   9997  C  CA  . LEU A 1 1307 ? 18.917  -36.932 -23.287 1.00 156.70 ? 1307 LEU A CA  1 
ATOM   9998  C  C   . LEU A 1 1307 ? 18.404  -37.769 -22.155 1.00 157.87 ? 1307 LEU A C   1 
ATOM   9999  O  O   . LEU A 1 1307 ? 19.186  -38.429 -21.471 1.00 159.27 ? 1307 LEU A O   1 
ATOM   10000 C  CB  . LEU A 1 1307 ? 20.310  -37.413 -23.659 1.00 156.98 ? 1307 LEU A CB  1 
ATOM   10001 C  CG  . LEU A 1 1307 ? 21.092  -36.245 -24.248 1.00 154.54 ? 1307 LEU A CG  1 
ATOM   10002 C  CD1 . LEU A 1 1307 ? 21.920  -35.588 -23.131 1.00 158.13 ? 1307 LEU A CD1 1 
ATOM   10003 C  CD2 . LEU A 1 1307 ? 21.930  -36.689 -25.472 1.00 153.70 ? 1307 LEU A CD2 1 
ATOM   10004 N  N   . ARG A 1 1308 ? 17.089  -37.755 -21.984 1.00 137.63 ? 1308 ARG A N   1 
ATOM   10005 C  CA  . ARG A 1 1308 ? 16.445  -38.508 -20.922 1.00 136.46 ? 1308 ARG A CA  1 
ATOM   10006 C  C   . ARG A 1 1308 ? 17.372  -39.511 -20.273 1.00 133.78 ? 1308 ARG A C   1 
ATOM   10007 O  O   . ARG A 1 1308 ? 17.809  -40.469 -20.905 1.00 131.22 ? 1308 ARG A O   1 
ATOM   10008 C  CB  . ARG A 1 1308 ? 15.223  -39.253 -21.449 1.00 136.32 ? 1308 ARG A CB  1 
ATOM   10009 C  CG  . ARG A 1 1308 ? 14.872  -40.467 -20.610 1.00 139.72 ? 1308 ARG A CG  1 
ATOM   10010 C  CD  . ARG A 1 1308 ? 13.407  -40.790 -20.719 1.00 142.73 ? 1308 ARG A CD  1 
ATOM   10011 N  NE  . ARG A 1 1308 ? 13.031  -41.932 -19.894 1.00 147.94 ? 1308 ARG A NE  1 
ATOM   10012 C  CZ  . ARG A 1 1308 ? 13.530  -43.155 -20.035 1.00 152.22 ? 1308 ARG A CZ  1 
ATOM   10013 N  NH1 . ARG A 1 1308 ? 14.450  -43.403 -20.966 1.00 149.27 ? 1308 ARG A NH1 1 
ATOM   10014 N  NH2 . ARG A 1 1308 ? 13.105  -44.127 -19.236 1.00 157.55 ? 1308 ARG A NH2 1 
ATOM   10015 N  N   . LEU A 1 1309 ? 17.669  -39.290 -19.005 1.00 103.35 ? 1309 LEU A N   1 
ATOM   10016 C  CA  . LEU A 1 1309 ? 18.565  -40.177 -18.289 1.00 105.53 ? 1309 LEU A CA  1 
ATOM   10017 C  C   . LEU A 1 1309 ? 17.916  -41.499 -17.917 1.00 109.16 ? 1309 LEU A C   1 
ATOM   10018 O  O   . LEU A 1 1309 ? 16.726  -41.555 -17.611 1.00 108.74 ? 1309 LEU A O   1 
ATOM   10019 C  CB  . LEU A 1 1309 ? 19.042  -39.494 -17.013 1.00 104.77 ? 1309 LEU A CB  1 
ATOM   10020 C  CG  . LEU A 1 1309 ? 20.311  -38.638 -16.976 1.00 101.38 ? 1309 LEU A CG  1 
ATOM   10021 C  CD1 . LEU A 1 1309 ? 20.391  -37.820 -15.680 1.00 103.14 ? 1309 LEU A CD1 1 
ATOM   10022 C  CD2 . LEU A 1 1309 ? 21.527  -39.534 -17.133 1.00 110.64 ? 1309 LEU A CD2 1 
ATOM   10023 N  N   . SER A 1 1310 ? 18.714  -42.557 -17.908 1.00 114.10 ? 1310 SER A N   1 
ATOM   10024 C  CA  . SER A 1 1310 ? 18.237  -43.832 -17.397 1.00 118.81 ? 1310 SER A CA  1 
ATOM   10025 C  C   . SER A 1 1310 ? 19.321  -44.886 -17.204 1.00 124.51 ? 1310 SER A C   1 
ATOM   10026 O  O   . SER A 1 1310 ? 19.035  -46.083 -17.317 1.00 121.86 ? 1310 SER A O   1 
ATOM   10027 C  CB  . SER A 1 1310 ? 17.121  -44.390 -18.270 1.00 121.46 ? 1310 SER A CB  1 
ATOM   10028 O  OG  . SER A 1 1310 ? 16.705  -45.660 -17.804 1.00 125.89 ? 1310 SER A OG  1 
ATOM   10029 N  N   . MET A 1 1311 ? 20.544  -44.444 -16.901 1.00 106.37 ? 1311 MET A N   1 
ATOM   10030 C  CA  . MET A 1 1311 ? 21.673  -45.346 -16.658 1.00 111.05 ? 1311 MET A CA  1 
ATOM   10031 C  C   . MET A 1 1311 ? 21.367  -46.444 -15.654 1.00 118.84 ? 1311 MET A C   1 
ATOM   10032 O  O   . MET A 1 1311 ? 20.224  -46.847 -15.479 1.00 118.72 ? 1311 MET A O   1 
ATOM   10033 C  CB  . MET A 1 1311 ? 22.883  -44.562 -16.180 1.00 129.52 ? 1311 MET A CB  1 
ATOM   10034 C  CG  . MET A 1 1311 ? 24.047  -44.543 -17.135 1.00 127.27 ? 1311 MET A CG  1 
ATOM   10035 S  SD  . MET A 1 1311 ? 24.590  -42.866 -17.453 1.00 113.59 ? 1311 MET A SD  1 
ATOM   10036 C  CE  . MET A 1 1311 ? 23.107  -42.169 -18.131 1.00 114.15 ? 1311 MET A CE  1 
ATOM   10037 N  N   . ASP A 1 1312 ? 22.401  -46.937 -14.999 1.00 114.64 ? 1312 ASP A N   1 
ATOM   10038 C  CA  . ASP A 1 1312 ? 22.212  -47.972 -14.004 1.00 116.48 ? 1312 ASP A CA  1 
ATOM   10039 C  C   . ASP A 1 1312 ? 23.559  -48.277 -13.399 1.00 119.31 ? 1312 ASP A C   1 
ATOM   10040 O  O   . ASP A 1 1312 ? 24.040  -49.402 -13.480 1.00 121.05 ? 1312 ASP A O   1 
ATOM   10041 C  CB  . ASP A 1 1312 ? 21.623  -49.224 -14.636 1.00 123.12 ? 1312 ASP A CB  1 
ATOM   10042 C  CG  . ASP A 1 1312 ? 20.992  -50.135 -13.624 1.00 121.30 ? 1312 ASP A CG  1 
ATOM   10043 O  OD1 . ASP A 1 1312 ? 21.391  -50.054 -12.451 1.00 119.98 ? 1312 ASP A OD1 1 
ATOM   10044 O  OD2 . ASP A 1 1312 ? 20.100  -50.926 -14.002 1.00 120.44 ? 1312 ASP A OD2 1 
ATOM   10045 N  N   . ILE A 1 1313 ? 24.154  -47.258 -12.780 1.00 121.07 ? 1313 ILE A N   1 
ATOM   10046 C  CA  . ILE A 1 1313 ? 25.560  -47.300 -12.376 1.00 120.65 ? 1313 ILE A CA  1 
ATOM   10047 C  C   . ILE A 1 1313 ? 25.902  -48.383 -11.391 1.00 128.46 ? 1313 ILE A C   1 
ATOM   10048 O  O   . ILE A 1 1313 ? 25.055  -48.927 -10.683 1.00 136.75 ? 1313 ILE A O   1 
ATOM   10049 C  CB  . ILE A 1 1313 ? 26.049  -46.011 -11.703 1.00 121.94 ? 1313 ILE A CB  1 
ATOM   10050 C  CG1 . ILE A 1 1313 ? 25.264  -44.781 -12.194 1.00 119.12 ? 1313 ILE A CG1 1 
ATOM   10051 C  CG2 . ILE A 1 1313 ? 27.562  -45.906 -11.866 1.00 120.88 ? 1313 ILE A CG2 1 
ATOM   10052 C  CD1 . ILE A 1 1313 ? 25.722  -44.200 -13.501 1.00 117.28 ? 1313 ILE A CD1 1 
ATOM   10053 N  N   . ASP A 1 1314 ? 27.185  -48.671 -11.335 1.00 151.57 ? 1314 ASP A N   1 
ATOM   10054 C  CA  . ASP A 1 1314 ? 27.688  -49.524 -10.297 1.00 154.17 ? 1314 ASP A CA  1 
ATOM   10055 C  C   . ASP A 1 1314 ? 29.147  -49.190 -10.102 1.00 152.06 ? 1314 ASP A C   1 
ATOM   10056 O  O   . ASP A 1 1314 ? 29.977  -49.501 -10.963 1.00 151.47 ? 1314 ASP A O   1 
ATOM   10057 C  CB  . ASP A 1 1314 ? 27.496  -50.995 -10.662 1.00 157.80 ? 1314 ASP A CB  1 
ATOM   10058 C  CG  . ASP A 1 1314 ? 28.138  -51.932 -9.661  1.00 164.60 ? 1314 ASP A CG  1 
ATOM   10059 O  OD1 . ASP A 1 1314 ? 29.383  -51.970 -9.591  1.00 163.65 ? 1314 ASP A OD1 1 
ATOM   10060 O  OD2 . ASP A 1 1314 ? 27.397  -52.637 -8.947  1.00 171.44 ? 1314 ASP A OD2 1 
ATOM   10061 N  N   . VAL A 1 1315 ? 29.442  -48.504 -8.996  1.00 125.72 ? 1315 VAL A N   1 
ATOM   10062 C  CA  . VAL A 1 1315 ? 30.807  -48.308 -8.534  1.00 126.03 ? 1315 VAL A CA  1 
ATOM   10063 C  C   . VAL A 1 1315 ? 31.203  -49.569 -7.765  1.00 130.43 ? 1315 VAL A C   1 
ATOM   10064 O  O   . VAL A 1 1315 ? 30.347  -50.207 -7.149  1.00 133.89 ? 1315 VAL A O   1 
ATOM   10065 C  CB  . VAL A 1 1315 ? 30.894  -47.074 -7.633  1.00 125.50 ? 1315 VAL A CB  1 
ATOM   10066 C  CG1 . VAL A 1 1315 ? 30.173  -47.330 -6.315  1.00 127.90 ? 1315 VAL A CG1 1 
ATOM   10067 C  CG2 . VAL A 1 1315 ? 32.334  -46.674 -7.423  1.00 129.05 ? 1315 VAL A CG2 1 
ATOM   10068 N  N   . SER A 1 1316 ? 32.482  -49.947 -7.832  1.00 168.53 ? 1316 SER A N   1 
ATOM   10069 C  CA  . SER A 1 1316 ? 32.954  -51.200 -7.234  1.00 178.36 ? 1316 SER A CA  1 
ATOM   10070 C  C   . SER A 1 1316 ? 34.479  -51.289 -7.106  1.00 184.32 ? 1316 SER A C   1 
ATOM   10071 O  O   . SER A 1 1316 ? 35.213  -50.794 -7.963  1.00 183.15 ? 1316 SER A O   1 
ATOM   10072 C  CB  . SER A 1 1316 ? 32.450  -52.395 -8.047  1.00 179.43 ? 1316 SER A CB  1 
ATOM   10073 O  OG  . SER A 1 1316 ? 31.783  -53.326 -7.220  1.00 184.51 ? 1316 SER A OG  1 
ATOM   10074 N  N   . TYR A 1 1317 ? 34.941  -51.932 -6.033  1.00 216.00 ? 1317 TYR A N   1 
ATOM   10075 C  CA  . TYR A 1 1317 ? 36.366  -52.189 -5.824  1.00 221.91 ? 1317 TYR A CA  1 
ATOM   10076 C  C   . TYR A 1 1317 ? 36.838  -53.345 -6.672  1.00 224.34 ? 1317 TYR A C   1 
ATOM   10077 O  O   . TYR A 1 1317 ? 36.149  -54.357 -6.768  1.00 226.49 ? 1317 TYR A O   1 
ATOM   10078 C  CB  . TYR A 1 1317 ? 36.647  -52.517 -4.365  1.00 230.49 ? 1317 TYR A CB  1 
ATOM   10079 C  CG  . TYR A 1 1317 ? 36.295  -51.379 -3.474  1.00 234.51 ? 1317 TYR A CG  1 
ATOM   10080 C  CD1 . TYR A 1 1317 ? 35.052  -51.313 -2.868  1.00 237.69 ? 1317 TYR A CD1 1 
ATOM   10081 C  CD2 . TYR A 1 1317 ? 37.187  -50.337 -3.273  1.00 236.13 ? 1317 TYR A CD2 1 
ATOM   10082 C  CE1 . TYR A 1 1317 ? 34.715  -50.249 -2.062  1.00 239.79 ? 1317 TYR A CE1 1 
ATOM   10083 C  CE2 . TYR A 1 1317 ? 36.862  -49.267 -2.470  1.00 238.47 ? 1317 TYR A CE2 1 
ATOM   10084 C  CZ  . TYR A 1 1317 ? 35.625  -49.223 -1.863  1.00 240.73 ? 1317 TYR A CZ  1 
ATOM   10085 O  OH  . TYR A 1 1317 ? 35.301  -48.151 -1.054  1.00 241.88 ? 1317 TYR A OH  1 
ATOM   10086 N  N   . LYS A 1 1318 ? 38.027  -53.207 -7.255  1.00 203.96 ? 1318 LYS A N   1 
ATOM   10087 C  CA  . LYS A 1 1318 ? 38.565  -54.215 -8.173  1.00 206.99 ? 1318 LYS A CA  1 
ATOM   10088 C  C   . LYS A 1 1318 ? 38.593  -55.609 -7.559  1.00 216.36 ? 1318 LYS A C   1 
ATOM   10089 O  O   . LYS A 1 1318 ? 38.279  -56.596 -8.220  1.00 216.35 ? 1318 LYS A O   1 
ATOM   10090 C  CB  . LYS A 1 1318 ? 39.970  -53.826 -8.654  1.00 205.66 ? 1318 LYS A CB  1 
ATOM   10091 C  CG  . LYS A 1 1318 ? 40.737  -54.963 -9.336  1.00 210.67 ? 1318 LYS A CG  1 
ATOM   10092 C  CD  . LYS A 1 1318 ? 41.205  -54.627 -10.768 1.00 209.49 ? 1318 LYS A CD  1 
ATOM   10093 C  CE  . LYS A 1 1318 ? 42.431  -53.722 -10.792 1.00 209.42 ? 1318 LYS A CE  1 
ATOM   10094 N  NZ  . LYS A 1 1318 ? 43.073  -53.704 -12.141 1.00 208.07 ? 1318 LYS A NZ  1 
ATOM   10095 N  N   . HIS A 1 1319 ? 38.960  -55.685 -6.288  1.00 202.65 ? 1319 HIS A N   1 
ATOM   10096 C  CA  . HIS A 1 1319 ? 39.091  -56.968 -5.627  1.00 212.64 ? 1319 HIS A CA  1 
ATOM   10097 C  C   . HIS A 1 1319 ? 38.077  -57.128 -4.495  1.00 225.12 ? 1319 HIS A C   1 
ATOM   10098 O  O   . HIS A 1 1319 ? 37.424  -58.166 -4.373  1.00 227.88 ? 1319 HIS A O   1 
ATOM   10099 C  CB  . HIS A 1 1319 ? 40.513  -57.119 -5.109  1.00 210.37 ? 1319 HIS A CB  1 
ATOM   10100 C  CG  . HIS A 1 1319 ? 41.562  -56.984 -6.173  1.00 207.01 ? 1319 HIS A CG  1 
ATOM   10101 N  ND1 . HIS A 1 1319 ? 42.172  -55.786 -6.468  1.00 203.87 ? 1319 HIS A ND1 1 
ATOM   10102 C  CD2 . HIS A 1 1319 ? 42.112  -57.907 -6.997  1.00 208.95 ? 1319 HIS A CD2 1 
ATOM   10103 C  CE1 . HIS A 1 1319 ? 43.060  -55.975 -7.433  1.00 203.48 ? 1319 HIS A CE1 1 
ATOM   10104 N  NE2 . HIS A 1 1319 ? 43.041  -57.250 -7.769  1.00 206.79 ? 1319 HIS A NE2 1 
ATOM   10105 N  N   . LYS A 1 1320 ? 37.943  -56.097 -3.672  1.00 226.96 ? 1320 LYS A N   1 
ATOM   10106 C  CA  . LYS A 1 1320 ? 36.944  -56.104 -2.617  1.00 240.29 ? 1320 LYS A CA  1 
ATOM   10107 C  C   . LYS A 1 1320 ? 35.553  -56.316 -3.200  1.00 245.78 ? 1320 LYS A C   1 
ATOM   10108 O  O   . LYS A 1 1320 ? 35.265  -55.871 -4.310  1.00 244.24 ? 1320 LYS A O   1 
ATOM   10109 C  CB  . LYS A 1 1320 ? 36.984  -54.784 -1.853  1.00 242.98 ? 1320 LYS A CB  1 
ATOM   10110 C  CG  . LYS A 1 1320 ? 35.756  -54.523 -0.994  1.00 248.09 ? 1320 LYS A CG  1 
ATOM   10111 C  CD  . LYS A 1 1320 ? 35.550  -55.617 0.043   1.00 255.84 ? 1320 LYS A CD  1 
ATOM   10112 C  CE  . LYS A 1 1320 ? 34.303  -55.347 0.870   1.00 256.52 ? 1320 LYS A CE  1 
ATOM   10113 N  NZ  . LYS A 1 1320 ? 33.991  -56.464 1.797   1.00 258.81 ? 1320 LYS A NZ  1 
ATOM   10114 N  N   . GLY A 1 1321 ? 34.695  -56.998 -2.448  1.00 232.91 ? 1321 GLY A N   1 
ATOM   10115 C  CA  . GLY A 1 1321 ? 33.300  -57.136 -2.820  1.00 230.37 ? 1321 GLY A CA  1 
ATOM   10116 C  C   . GLY A 1 1321 ? 32.698  -55.810 -3.241  1.00 226.58 ? 1321 GLY A C   1 
ATOM   10117 O  O   . GLY A 1 1321 ? 33.342  -54.763 -3.178  1.00 229.09 ? 1321 GLY A O   1 
ATOM   10118 N  N   . ALA A 1 1322 ? 31.447  -55.848 -3.672  1.00 242.97 ? 1322 ALA A N   1 
ATOM   10119 C  CA  . ALA A 1 1322 ? 30.835  -54.668 -4.260  1.00 234.79 ? 1322 ALA A CA  1 
ATOM   10120 C  C   . ALA A 1 1322 ? 30.405  -53.601 -3.260  1.00 228.42 ? 1322 ALA A C   1 
ATOM   10121 O  O   . ALA A 1 1322 ? 29.818  -53.892 -2.220  1.00 224.96 ? 1322 ALA A O   1 
ATOM   10122 C  CB  . ALA A 1 1322 ? 29.663  -55.060 -5.152  1.00 229.55 ? 1322 ALA A CB  1 
ATOM   10123 N  N   . LEU A 1 1323 ? 30.720  -52.362 -3.615  1.00 238.55 ? 1323 LEU A N   1 
ATOM   10124 C  CA  . LEU A 1 1323 ? 30.172  -51.166 -3.000  1.00 231.72 ? 1323 LEU A CA  1 
ATOM   10125 C  C   . LEU A 1 1323 ? 28.822  -50.862 -3.675  1.00 233.62 ? 1323 LEU A C   1 
ATOM   10126 O  O   . LEU A 1 1323 ? 28.357  -51.653 -4.494  1.00 240.00 ? 1323 LEU A O   1 
ATOM   10127 C  CB  . LEU A 1 1323 ? 31.173  -50.036 -3.201  1.00 207.34 ? 1323 LEU A CB  1 
ATOM   10128 C  CG  . LEU A 1 1323 ? 30.773  -48.592 -2.967  1.00 187.29 ? 1323 LEU A CG  1 
ATOM   10129 C  CD1 . LEU A 1 1323 ? 30.082  -48.458 -1.635  1.00 179.55 ? 1323 LEU A CD1 1 
ATOM   10130 C  CD2 . LEU A 1 1323 ? 32.014  -47.730 -3.028  1.00 174.61 ? 1323 LEU A CD2 1 
ATOM   10131 N  N   . HIS A 1 1324 ? 28.197  -49.731 -3.347  1.00 178.66 ? 1324 HIS A N   1 
ATOM   10132 C  CA  . HIS A 1 1324 ? 26.857  -49.406 -3.859  1.00 175.15 ? 1324 HIS A CA  1 
ATOM   10133 C  C   . HIS A 1 1324 ? 26.700  -49.463 -5.385  1.00 169.71 ? 1324 HIS A C   1 
ATOM   10134 O  O   . HIS A 1 1324 ? 27.691  -49.542 -6.119  1.00 166.97 ? 1324 HIS A O   1 
ATOM   10135 C  CB  . HIS A 1 1324 ? 26.349  -48.055 -3.315  1.00 175.18 ? 1324 HIS A CB  1 
ATOM   10136 C  CG  . HIS A 1 1324 ? 27.027  -46.849 -3.898  1.00 178.32 ? 1324 HIS A CG  1 
ATOM   10137 N  ND1 . HIS A 1 1324 ? 26.377  -45.954 -4.725  1.00 177.49 ? 1324 HIS A ND1 1 
ATOM   10138 C  CD2 . HIS A 1 1324 ? 28.283  -46.365 -3.744  1.00 180.90 ? 1324 HIS A CD2 1 
ATOM   10139 C  CE1 . HIS A 1 1324 ? 27.204  -44.985 -5.063  1.00 177.07 ? 1324 HIS A CE1 1 
ATOM   10140 N  NE2 . HIS A 1 1324 ? 28.371  -45.210 -4.483  1.00 179.53 ? 1324 HIS A NE2 1 
ATOM   10141 N  N   . ASN A 1 1325 ? 25.442  -49.446 -5.837  1.00 184.70 ? 1325 ASN A N   1 
ATOM   10142 C  CA  . ASN A 1 1325 ? 25.093  -49.427 -7.260  1.00 184.41 ? 1325 ASN A CA  1 
ATOM   10143 C  C   . ASN A 1 1325 ? 23.670  -48.966 -7.438  1.00 177.95 ? 1325 ASN A C   1 
ATOM   10144 O  O   . ASN A 1 1325 ? 22.756  -49.537 -6.864  1.00 178.87 ? 1325 ASN A O   1 
ATOM   10145 C  CB  . ASN A 1 1325 ? 25.263  -50.805 -7.900  1.00 193.54 ? 1325 ASN A CB  1 
ATOM   10146 C  CG  . ASN A 1 1325 ? 24.434  -51.874 -7.219  1.00 200.77 ? 1325 ASN A CG  1 
ATOM   10147 O  OD1 . ASN A 1 1325 ? 24.964  -52.723 -6.503  1.00 203.07 ? 1325 ASN A OD1 1 
ATOM   10148 N  ND2 . ASN A 1 1325 ? 23.130  -51.842 -7.444  1.00 200.00 ? 1325 ASN A ND2 1 
ATOM   10149 N  N   . TYR A 1 1326 ? 23.468  -47.939 -8.242  1.00 194.30 ? 1326 TYR A N   1 
ATOM   10150 C  CA  . TYR A 1 1326 ? 22.167  -47.314 -8.226  1.00 193.85 ? 1326 TYR A CA  1 
ATOM   10151 C  C   . TYR A 1 1326 ? 21.620  -46.881 -9.560  1.00 181.01 ? 1326 TYR A C   1 
ATOM   10152 O  O   . TYR A 1 1326 ? 22.267  -46.162 -10.315 1.00 177.34 ? 1326 TYR A O   1 
ATOM   10153 C  CB  . TYR A 1 1326 ? 22.178  -46.118 -7.288  1.00 201.87 ? 1326 TYR A CB  1 
ATOM   10154 C  CG  . TYR A 1 1326 ? 23.220  -45.076 -7.597  1.00 207.12 ? 1326 TYR A CG  1 
ATOM   10155 C  CD1 . TYR A 1 1326 ? 22.854  -43.821 -8.069  1.00 207.45 ? 1326 TYR A CD1 1 
ATOM   10156 C  CD2 . TYR A 1 1326 ? 24.563  -45.332 -7.391  1.00 212.01 ? 1326 TYR A CD2 1 
ATOM   10157 C  CE1 . TYR A 1 1326 ? 23.800  -42.857 -8.330  1.00 207.99 ? 1326 TYR A CE1 1 
ATOM   10158 C  CE2 . TYR A 1 1326 ? 25.515  -44.374 -7.652  1.00 212.61 ? 1326 TYR A CE2 1 
ATOM   10159 C  CZ  . TYR A 1 1326 ? 25.130  -43.140 -8.119  1.00 210.72 ? 1326 TYR A CZ  1 
ATOM   10160 O  OH  . TYR A 1 1326 ? 26.080  -42.185 -8.376  1.00 209.62 ? 1326 TYR A OH  1 
ATOM   10161 N  N   . LYS A 1 1327 ? 20.389  -47.296 -9.819  1.00 176.81 ? 1327 LYS A N   1 
ATOM   10162 C  CA  . LYS A 1 1327 ? 19.689  -46.877 -11.011 1.00 166.77 ? 1327 LYS A CA  1 
ATOM   10163 C  C   . LYS A 1 1327 ? 19.480  -45.362 -10.995 1.00 154.68 ? 1327 LYS A C   1 
ATOM   10164 O  O   . LYS A 1 1327 ? 18.675  -44.843 -10.231 1.00 153.91 ? 1327 LYS A O   1 
ATOM   10165 C  CB  . LYS A 1 1327 ? 18.356  -47.625 -11.118 1.00 171.43 ? 1327 LYS A CB  1 
ATOM   10166 C  CG  . LYS A 1 1327 ? 17.647  -47.438 -12.446 1.00 173.12 ? 1327 LYS A CG  1 
ATOM   10167 C  CD  . LYS A 1 1327 ? 16.914  -48.707 -12.889 1.00 178.20 ? 1327 LYS A CD  1 
ATOM   10168 C  CE  . LYS A 1 1327 ? 16.497  -48.638 -14.366 1.00 173.80 ? 1327 LYS A CE  1 
ATOM   10169 N  NZ  . LYS A 1 1327 ? 17.641  -48.592 -15.338 1.00 169.86 ? 1327 LYS A NZ  1 
ATOM   10170 N  N   . MET A 1 1328 ? 20.238  -44.656 -11.821 1.00 155.42 ? 1328 MET A N   1 
ATOM   10171 C  CA  . MET A 1 1328 ? 20.027  -43.233 -12.030 1.00 143.19 ? 1328 MET A CA  1 
ATOM   10172 C  C   . MET A 1 1328 ? 18.785  -43.019 -12.918 1.00 142.02 ? 1328 MET A C   1 
ATOM   10173 O  O   . MET A 1 1328 ? 18.417  -43.904 -13.673 1.00 141.42 ? 1328 MET A O   1 
ATOM   10174 C  CB  . MET A 1 1328 ? 21.280  -42.647 -12.675 1.00 132.95 ? 1328 MET A CB  1 
ATOM   10175 C  CG  . MET A 1 1328 ? 21.115  -41.264 -13.254 1.00 125.67 ? 1328 MET A CG  1 
ATOM   10176 S  SD  . MET A 1 1328 ? 22.687  -40.371 -13.381 1.00 122.11 ? 1328 MET A SD  1 
ATOM   10177 C  CE  . MET A 1 1328 ? 23.108  -40.197 -11.666 1.00 174.89 ? 1328 MET A CE  1 
ATOM   10178 N  N   . THR A 1 1329 ? 18.128  -41.868 -12.811 1.00 134.43 ? 1329 THR A N   1 
ATOM   10179 C  CA  . THR A 1 1329 ? 17.050  -41.471 -13.718 1.00 132.70 ? 1329 THR A CA  1 
ATOM   10180 C  C   . THR A 1 1329 ? 16.954  -39.967 -13.597 1.00 129.45 ? 1329 THR A C   1 
ATOM   10181 O  O   . THR A 1 1329 ? 17.905  -39.337 -13.175 1.00 129.58 ? 1329 THR A O   1 
ATOM   10182 C  CB  . THR A 1 1329 ? 15.706  -42.082 -13.339 1.00 136.17 ? 1329 THR A CB  1 
ATOM   10183 O  OG1 . THR A 1 1329 ? 15.540  -41.995 -11.929 1.00 138.11 ? 1329 THR A OG1 1 
ATOM   10184 C  CG2 . THR A 1 1329 ? 15.644  -43.538 -13.722 1.00 139.31 ? 1329 THR A CG2 1 
ATOM   10185 N  N   . ASP A 1 1330 ? 15.822  -39.378 -13.953 1.00 155.03 ? 1330 ASP A N   1 
ATOM   10186 C  CA  . ASP A 1 1330 ? 15.640  -37.940 -13.747 1.00 156.14 ? 1330 ASP A CA  1 
ATOM   10187 C  C   . ASP A 1 1330 ? 15.029  -37.662 -12.370 1.00 160.62 ? 1330 ASP A C   1 
ATOM   10188 O  O   . ASP A 1 1330 ? 14.765  -36.509 -12.005 1.00 162.11 ? 1330 ASP A O   1 
ATOM   10189 C  CB  . ASP A 1 1330 ? 14.749  -37.334 -14.833 1.00 155.66 ? 1330 ASP A CB  1 
ATOM   10190 C  CG  . ASP A 1 1330 ? 15.262  -37.587 -16.238 1.00 153.88 ? 1330 ASP A CG  1 
ATOM   10191 O  OD1 . ASP A 1 1330 ? 16.443  -37.281 -16.519 1.00 149.00 ? 1330 ASP A OD1 1 
ATOM   10192 O  OD2 . ASP A 1 1330 ? 14.467  -38.082 -17.070 1.00 156.40 ? 1330 ASP A OD2 1 
ATOM   10193 N  N   . LYS A 1 1331 ? 14.774  -38.745 -11.636 1.00 186.35 ? 1331 LYS A N   1 
ATOM   10194 C  CA  . LYS A 1 1331 ? 14.360  -38.709 -10.230 1.00 189.88 ? 1331 LYS A CA  1 
ATOM   10195 C  C   . LYS A 1 1331 ? 15.516  -38.282 -9.327  1.00 190.50 ? 1331 LYS A C   1 
ATOM   10196 O  O   . LYS A 1 1331 ? 15.504  -37.198 -8.734  1.00 190.08 ? 1331 LYS A O   1 
ATOM   10197 C  CB  . LYS A 1 1331 ? 13.894  -40.098 -9.784  1.00 193.06 ? 1331 LYS A CB  1 
ATOM   10198 C  CG  . LYS A 1 1331 ? 12.753  -40.669 -10.604 1.00 191.04 ? 1331 LYS A CG  1 
ATOM   10199 C  CD  . LYS A 1 1331 ? 11.746  -39.584 -10.893 1.00 189.23 ? 1331 LYS A CD  1 
ATOM   10200 C  CE  . LYS A 1 1331 ? 10.492  -40.138 -11.529 1.00 191.38 ? 1331 LYS A CE  1 
ATOM   10201 N  NZ  . LYS A 1 1331 ? 9.375   -39.164 -11.388 1.00 192.42 ? 1331 LYS A NZ  1 
ATOM   10202 N  N   . ASN A 1 1332 ? 16.503  -39.163 -9.205  1.00 137.58 ? 1332 ASN A N   1 
ATOM   10203 C  CA  . ASN A 1 1332 ? 17.773  -38.804 -8.595  1.00 140.54 ? 1332 ASN A CA  1 
ATOM   10204 C  C   . ASN A 1 1332 ? 18.815  -38.614 -9.665  1.00 140.76 ? 1332 ASN A C   1 
ATOM   10205 O  O   . ASN A 1 1332 ? 19.020  -39.495 -10.489 1.00 141.87 ? 1332 ASN A O   1 
ATOM   10206 C  CB  . ASN A 1 1332 ? 18.276  -39.923 -7.689  1.00 146.21 ? 1332 ASN A CB  1 
ATOM   10207 C  CG  . ASN A 1 1332 ? 19.319  -40.799 -8.369  1.00 147.43 ? 1332 ASN A CG  1 
ATOM   10208 O  OD1 . ASN A 1 1332 ? 18.984  -41.793 -9.011  1.00 145.74 ? 1332 ASN A OD1 1 
ATOM   10209 N  ND2 . ASN A 1 1332 ? 20.590  -40.423 -8.238  1.00 147.30 ? 1332 ASN A ND2 1 
ATOM   10210 N  N   . PHE A 1 1333 ? 19.502  -37.489 -9.668  1.00 158.56 ? 1333 PHE A N   1 
ATOM   10211 C  CA  . PHE A 1 1333 ? 20.706  -37.476 -10.461 1.00 154.19 ? 1333 PHE A CA  1 
ATOM   10212 C  C   . PHE A 1 1333 ? 21.818  -36.729 -9.807  1.00 160.10 ? 1333 PHE A C   1 
ATOM   10213 O  O   . PHE A 1 1333 ? 22.974  -36.990 -10.092 1.00 161.95 ? 1333 PHE A O   1 
ATOM   10214 C  CB  . PHE A 1 1333 ? 20.500  -37.101 -11.943 1.00 142.28 ? 1333 PHE A CB  1 
ATOM   10215 C  CG  . PHE A 1 1333 ? 19.992  -35.700 -12.198 1.00 133.46 ? 1333 PHE A CG  1 
ATOM   10216 C  CD1 . PHE A 1 1333 ? 20.872  -34.630 -12.302 1.00 128.69 ? 1333 PHE A CD1 1 
ATOM   10217 C  CD2 . PHE A 1 1333 ? 18.633  -35.471 -12.434 1.00 132.96 ? 1333 PHE A CD2 1 
ATOM   10218 C  CE1 . PHE A 1 1333 ? 20.396  -33.337 -12.579 1.00 127.93 ? 1333 PHE A CE1 1 
ATOM   10219 C  CE2 . PHE A 1 1333 ? 18.148  -34.189 -12.707 1.00 125.06 ? 1333 PHE A CE2 1 
ATOM   10220 C  CZ  . PHE A 1 1333 ? 19.030  -33.119 -12.775 1.00 123.68 ? 1333 PHE A CZ  1 
ATOM   10221 N  N   . LEU A 1 1334 ? 21.477  -35.838 -8.894  1.00 146.24 ? 1334 LEU A N   1 
ATOM   10222 C  CA  . LEU A 1 1334 ? 22.500  -35.120 -8.147  1.00 142.20 ? 1334 LEU A CA  1 
ATOM   10223 C  C   . LEU A 1 1334 ? 22.885  -35.900 -6.890  1.00 151.86 ? 1334 LEU A C   1 
ATOM   10224 O  O   . LEU A 1 1334 ? 23.299  -35.324 -5.874  1.00 155.04 ? 1334 LEU A O   1 
ATOM   10225 C  CB  . LEU A 1 1334 ? 22.015  -33.729 -7.771  1.00 132.02 ? 1334 LEU A CB  1 
ATOM   10226 C  CG  . LEU A 1 1334 ? 21.207  -32.907 -8.781  1.00 123.11 ? 1334 LEU A CG  1 
ATOM   10227 C  CD1 . LEU A 1 1334 ? 22.063  -32.568 -9.949  1.00 117.29 ? 1334 LEU A CD1 1 
ATOM   10228 C  CD2 . LEU A 1 1334 ? 19.931  -33.618 -9.212  1.00 121.26 ? 1334 LEU A CD2 1 
ATOM   10229 N  N   . GLY A 1 1335 ? 22.733  -37.218 -6.989  1.00 165.65 ? 1335 GLY A N   1 
ATOM   10230 C  CA  . GLY A 1 1335 ? 23.031  -38.144 -5.920  1.00 175.41 ? 1335 GLY A CA  1 
ATOM   10231 C  C   . GLY A 1 1335 ? 24.169  -37.783 -4.989  1.00 181.70 ? 1335 GLY A C   1 
ATOM   10232 O  O   . GLY A 1 1335 ? 25.037  -36.953 -5.279  1.00 181.27 ? 1335 GLY A O   1 
ATOM   10233 N  N   . ARG A 1 1336 ? 24.134  -38.430 -3.836  1.00 207.52 ? 1336 ARG A N   1 
ATOM   10234 C  CA  . ARG A 1 1336 ? 25.156  -38.291 -2.824  1.00 216.45 ? 1336 ARG A CA  1 
ATOM   10235 C  C   . ARG A 1 1336 ? 26.525  -38.438 -3.453  1.00 208.01 ? 1336 ARG A C   1 
ATOM   10236 O  O   . ARG A 1 1336 ? 26.674  -39.162 -4.443  1.00 206.56 ? 1336 ARG A O   1 
ATOM   10237 C  CB  . ARG A 1 1336 ? 24.985  -39.422 -1.831  1.00 233.59 ? 1336 ARG A CB  1 
ATOM   10238 C  CG  . ARG A 1 1336 ? 24.563  -40.685 -2.539  1.00 245.02 ? 1336 ARG A CG  1 
ATOM   10239 C  CD  . ARG A 1 1336 ? 25.164  -41.912 -1.927  1.00 258.52 ? 1336 ARG A CD  1 
ATOM   10240 N  NE  . ARG A 1 1336 ? 24.805  -43.084 -2.711  1.00 266.57 ? 1336 ARG A NE  1 
ATOM   10241 C  CZ  . ARG A 1 1336 ? 24.722  -44.314 -2.221  1.00 275.61 ? 1336 ARG A CZ  1 
ATOM   10242 N  NH1 . ARG A 1 1336 ? 24.970  -44.538 -0.937  1.00 281.12 ? 1336 ARG A NH1 1 
ATOM   10243 N  NH2 . ARG A 1 1336 ? 24.383  -45.319 -3.014  1.00 277.03 ? 1336 ARG A NH2 1 
ATOM   10244 N  N   . PRO A 1 1337 ? 27.520  -37.721 -2.900  1.00 143.86 ? 1337 PRO A N   1 
ATOM   10245 C  CA  . PRO A 1 1337 ? 28.957  -38.010 -3.085  1.00 136.64 ? 1337 PRO A CA  1 
ATOM   10246 C  C   . PRO A 1 1337 ? 29.366  -39.273 -2.319  1.00 136.04 ? 1337 PRO A C   1 
ATOM   10247 O  O   . PRO A 1 1337 ? 28.550  -39.822 -1.583  1.00 135.83 ? 1337 PRO A O   1 
ATOM   10248 C  CB  . PRO A 1 1337 ? 29.647  -36.780 -2.503  1.00 138.25 ? 1337 PRO A CB  1 
ATOM   10249 C  CG  . PRO A 1 1337 ? 28.579  -35.674 -2.594  1.00 140.21 ? 1337 PRO A CG  1 
ATOM   10250 C  CD  . PRO A 1 1337 ? 27.277  -36.371 -2.357  1.00 142.70 ? 1337 PRO A CD  1 
ATOM   10251 N  N   . VAL A 1 1338 ? 30.588  -39.750 -2.504  1.00 134.09 ? 1338 VAL A N   1 
ATOM   10252 C  CA  . VAL A 1 1338 ? 31.046  -40.906 -1.730  1.00 141.99 ? 1338 VAL A CA  1 
ATOM   10253 C  C   . VAL A 1 1338 ? 32.562  -40.983 -1.684  1.00 149.43 ? 1338 VAL A C   1 
ATOM   10254 O  O   . VAL A 1 1338 ? 33.242  -40.856 -2.696  1.00 149.38 ? 1338 VAL A O   1 
ATOM   10255 C  CB  . VAL A 1 1338 ? 30.416  -42.270 -2.183  1.00 181.97 ? 1338 VAL A CB  1 
ATOM   10256 C  CG1 . VAL A 1 1338 ? 31.442  -43.412 -2.097  1.00 183.43 ? 1338 VAL A CG1 1 
ATOM   10257 C  CG2 . VAL A 1 1338 ? 29.190  -42.605 -1.337  1.00 184.07 ? 1338 VAL A CG2 1 
ATOM   10258 N  N   . GLU A 1 1339 ? 33.086  -41.165 -0.482  1.00 196.46 ? 1339 GLU A N   1 
ATOM   10259 C  CA  . GLU A 1 1339 ? 34.519  -41.242 -0.297  1.00 202.73 ? 1339 GLU A CA  1 
ATOM   10260 C  C   . GLU A 1 1339 ? 34.919  -42.703 -0.383  1.00 203.22 ? 1339 GLU A C   1 
ATOM   10261 O  O   . GLU A 1 1339 ? 34.286  -43.585 0.208   1.00 203.56 ? 1339 GLU A O   1 
ATOM   10262 C  CB  . GLU A 1 1339 ? 34.940  -40.553 1.023   1.00 211.85 ? 1339 GLU A CB  1 
ATOM   10263 C  CG  . GLU A 1 1339 ? 34.851  -38.978 0.976   1.00 215.98 ? 1339 GLU A CG  1 
ATOM   10264 C  CD  . GLU A 1 1339 ? 34.748  -38.275 2.353   1.00 223.45 ? 1339 GLU A CD  1 
ATOM   10265 O  OE1 . GLU A 1 1339 ? 35.500  -38.649 3.280   1.00 228.28 ? 1339 GLU A OE1 1 
ATOM   10266 O  OE2 . GLU A 1 1339 ? 33.925  -37.331 2.494   1.00 223.46 ? 1339 GLU A OE2 1 
ATOM   10267 N  N   . VAL A 1 1340 ? 35.937  -42.955 -1.186  1.00 178.30 ? 1340 VAL A N   1 
ATOM   10268 C  CA  . VAL A 1 1340 ? 36.457  -44.294 -1.308  1.00 182.76 ? 1340 VAL A CA  1 
ATOM   10269 C  C   . VAL A 1 1340 ? 37.303  -44.627 -0.109  1.00 188.48 ? 1340 VAL A C   1 
ATOM   10270 O  O   . VAL A 1 1340 ? 38.403  -44.092 0.061   1.00 191.48 ? 1340 VAL A O   1 
ATOM   10271 C  CB  . VAL A 1 1340 ? 37.297  -44.458 -2.554  1.00 182.64 ? 1340 VAL A CB  1 
ATOM   10272 C  CG1 . VAL A 1 1340 ? 38.094  -45.764 -2.504  1.00 186.33 ? 1340 VAL A CG1 1 
ATOM   10273 C  CG2 . VAL A 1 1340 ? 36.386  -44.441 -3.758  1.00 178.97 ? 1340 VAL A CG2 1 
ATOM   10274 N  N   . LEU A 1 1341 ? 36.774  -45.534 0.706   1.00 221.40 ? 1341 LEU A N   1 
ATOM   10275 C  CA  . LEU A 1 1341 ? 37.428  -46.001 1.916   1.00 226.62 ? 1341 LEU A CA  1 
ATOM   10276 C  C   . LEU A 1 1341 ? 38.634  -46.890 1.615   1.00 232.76 ? 1341 LEU A C   1 
ATOM   10277 O  O   . LEU A 1 1341 ? 39.773  -46.416 1.544   1.00 233.11 ? 1341 LEU A O   1 
ATOM   10278 C  CB  . LEU A 1 1341 ? 36.423  -46.780 2.777   1.00 227.93 ? 1341 LEU A CB  1 
ATOM   10279 C  CG  . LEU A 1 1341 ? 35.333  -46.005 3.526   1.00 246.11 ? 1341 LEU A CG  1 
ATOM   10280 C  CD1 . LEU A 1 1341 ? 35.961  -44.907 4.395   1.00 246.18 ? 1341 LEU A CD1 1 
ATOM   10281 C  CD2 . LEU A 1 1341 ? 34.291  -45.444 2.558   1.00 242.45 ? 1341 LEU A CD2 1 
ATOM   10282 N  N   . LEU A 1 1342 ? 38.345  -48.172 1.403   1.00 187.96 ? 1342 LEU A N   1 
ATOM   10283 C  CA  . LEU A 1 1342 ? 39.322  -49.269 1.374   1.00 191.41 ? 1342 LEU A CA  1 
ATOM   10284 C  C   . LEU A 1 1342 ? 40.540  -49.085 0.457   1.00 189.01 ? 1342 LEU A C   1 
ATOM   10285 O  O   . LEU A 1 1342 ? 40.804  -47.996 -0.048  1.00 184.74 ? 1342 LEU A O   1 
ATOM   10286 C  CB  . LEU A 1 1342 ? 38.592  -50.569 1.016   1.00 190.71 ? 1342 LEU A CB  1 
ATOM   10287 C  CG  . LEU A 1 1342 ? 37.086  -50.527 1.323   1.00 186.42 ? 1342 LEU A CG  1 
ATOM   10288 C  CD1 . LEU A 1 1342 ? 36.379  -51.814 0.962   1.00 186.99 ? 1342 LEU A CD1 1 
ATOM   10289 C  CD2 . LEU A 1 1342 ? 36.856  -50.230 2.774   1.00 188.22 ? 1342 LEU A CD2 1 
ATOM   10290 N  N   . ASN A 1 1343 ? 41.301  -50.157 0.266   1.00 221.46 ? 1343 ASN A N   1 
ATOM   10291 C  CA  . ASN A 1 1343 ? 42.467  -50.091 -0.603  1.00 225.66 ? 1343 ASN A CA  1 
ATOM   10292 C  C   . ASN A 1 1343 ? 42.373  -51.014 -1.804  1.00 223.95 ? 1343 ASN A C   1 
ATOM   10293 O  O   . ASN A 1 1343 ? 42.794  -52.168 -1.757  1.00 226.24 ? 1343 ASN A O   1 
ATOM   10294 C  CB  . ASN A 1 1343 ? 43.743  -50.364 0.175   1.00 236.89 ? 1343 ASN A CB  1 
ATOM   10295 C  CG  . ASN A 1 1343 ? 44.121  -49.213 1.063   1.00 245.96 ? 1343 ASN A CG  1 
ATOM   10296 O  OD1 . ASN A 1 1343 ? 45.296  -48.978 1.333   1.00 250.58 ? 1343 ASN A OD1 1 
ATOM   10297 N  ND2 . ASN A 1 1343 ? 43.121  -48.464 1.508   1.00 247.37 ? 1343 ASN A ND2 1 
ATOM   10298 N  N   . ASP A 1 1344 ? 41.834  -50.481 -2.892  1.00 246.57 ? 1344 ASP A N   1 
ATOM   10299 C  CA  . ASP A 1 1344 ? 41.535  -51.276 -4.071  1.00 241.73 ? 1344 ASP A CA  1 
ATOM   10300 C  C   . ASP A 1 1344 ? 41.529  -50.347 -5.271  1.00 236.72 ? 1344 ASP A C   1 
ATOM   10301 O  O   . ASP A 1 1344 ? 41.563  -49.125 -5.118  1.00 236.06 ? 1344 ASP A O   1 
ATOM   10302 C  CB  . ASP A 1 1344 ? 40.159  -51.928 -3.912  1.00 236.75 ? 1344 ASP A CB  1 
ATOM   10303 C  CG  . ASP A 1 1344 ? 40.142  -53.373 -4.344  1.00 231.56 ? 1344 ASP A CG  1 
ATOM   10304 O  OD1 . ASP A 1 1344 ? 41.114  -53.821 -4.989  1.00 230.16 ? 1344 ASP A OD1 1 
ATOM   10305 O  OD2 . ASP A 1 1344 ? 39.148  -54.059 -4.035  1.00 229.26 ? 1344 ASP A OD2 1 
ATOM   10306 N  N   . ASP A 1 1345 ? 41.497  -50.914 -6.469  1.00 234.26 ? 1345 ASP A N   1 
ATOM   10307 C  CA  . ASP A 1 1345 ? 41.315  -50.091 -7.652  1.00 227.99 ? 1345 ASP A CA  1 
ATOM   10308 C  C   . ASP A 1 1345 ? 39.809  -49.949 -7.916  1.00 196.43 ? 1345 ASP A C   1 
ATOM   10309 O  O   . ASP A 1 1345 ? 39.043  -50.894 -7.734  1.00 198.69 ? 1345 ASP A O   1 
ATOM   10310 C  CB  . ASP A 1 1345 ? 42.080  -50.677 -8.841  1.00 228.10 ? 1345 ASP A CB  1 
ATOM   10311 C  CG  . ASP A 1 1345 ? 43.545  -50.952 -8.516  1.00 235.00 ? 1345 ASP A CG  1 
ATOM   10312 O  OD1 . ASP A 1 1345 ? 44.397  -50.812 -9.415  1.00 235.58 ? 1345 ASP A OD1 1 
ATOM   10313 O  OD2 . ASP A 1 1345 ? 43.847  -51.308 -7.359  1.00 239.18 ? 1345 ASP A OD2 1 
ATOM   10314 N  N   . LEU A 1 1346 ? 39.373  -48.763 -8.312  1.00 185.58 ? 1346 LEU A N   1 
ATOM   10315 C  CA  . LEU A 1 1346 ? 37.948  -48.523 -8.412  1.00 180.90 ? 1346 LEU A CA  1 
ATOM   10316 C  C   . LEU A 1 1346 ? 37.412  -48.778 -9.804  1.00 180.20 ? 1346 LEU A C   1 
ATOM   10317 O  O   . LEU A 1 1346 ? 38.175  -48.780 -10.764 1.00 182.21 ? 1346 LEU A O   1 
ATOM   10318 C  CB  . LEU A 1 1346 ? 37.625  -47.101 -8.000  1.00 173.72 ? 1346 LEU A CB  1 
ATOM   10319 C  CG  . LEU A 1 1346 ? 36.120  -46.941 -7.813  1.00 170.34 ? 1346 LEU A CG  1 
ATOM   10320 C  CD1 . LEU A 1 1346 ? 35.558  -48.105 -6.999  1.00 173.45 ? 1346 LEU A CD1 1 
ATOM   10321 C  CD2 . LEU A 1 1346 ? 35.810  -45.618 -7.160  1.00 168.55 ? 1346 LEU A CD2 1 
ATOM   10322 N  N   . ILE A 1 1347 ? 36.097  -48.991 -9.909  1.00 169.99 ? 1347 ILE A N   1 
ATOM   10323 C  CA  . ILE A 1 1347 ? 35.445  -49.189 -11.207 1.00 160.88 ? 1347 ILE A CA  1 
ATOM   10324 C  C   . ILE A 1 1347 ? 33.971  -48.744 -11.301 1.00 152.78 ? 1347 ILE A C   1 
ATOM   10325 O  O   . ILE A 1 1347 ? 33.072  -49.468 -10.878 1.00 153.49 ? 1347 ILE A O   1 
ATOM   10326 C  CB  . ILE A 1 1347 ? 35.543  -50.668 -11.686 1.00 162.50 ? 1347 ILE A CB  1 
ATOM   10327 C  CG1 . ILE A 1 1347 ? 36.358  -51.530 -10.714 1.00 167.20 ? 1347 ILE A CG1 1 
ATOM   10328 C  CG2 . ILE A 1 1347 ? 36.156  -50.735 -13.081 1.00 159.92 ? 1347 ILE A CG2 1 
ATOM   10329 C  CD1 . ILE A 1 1347 ? 36.360  -53.020 -11.072 1.00 172.34 ? 1347 ILE A CD1 1 
ATOM   10330 N  N   . VAL A 1 1348 ? 33.748  -47.557 -11.868 1.00 166.52 ? 1348 VAL A N   1 
ATOM   10331 C  CA  . VAL A 1 1348 ? 32.428  -47.116 -12.330 1.00 163.68 ? 1348 VAL A CA  1 
ATOM   10332 C  C   . VAL A 1 1348 ? 32.133  -47.847 -13.643 1.00 172.60 ? 1348 VAL A C   1 
ATOM   10333 O  O   . VAL A 1 1348 ? 33.044  -48.012 -14.457 1.00 174.68 ? 1348 VAL A O   1 
ATOM   10334 C  CB  . VAL A 1 1348 ? 32.434  -45.595 -12.606 1.00 155.29 ? 1348 VAL A CB  1 
ATOM   10335 C  CG1 . VAL A 1 1348 ? 31.022  -45.066 -12.891 1.00 154.25 ? 1348 VAL A CG1 1 
ATOM   10336 C  CG2 . VAL A 1 1348 ? 33.072  -44.860 -11.446 1.00 155.86 ? 1348 VAL A CG2 1 
ATOM   10337 N  N   . SER A 1 1349 ? 30.880  -48.265 -13.870 1.00 177.73 ? 1349 SER A N   1 
ATOM   10338 C  CA  . SER A 1 1349 ? 30.571  -49.233 -14.947 1.00 178.48 ? 1349 SER A CA  1 
ATOM   10339 C  C   . SER A 1 1349 ? 29.084  -49.483 -15.260 1.00 182.24 ? 1349 SER A C   1 
ATOM   10340 O  O   . SER A 1 1349 ? 28.592  -50.612 -15.148 1.00 183.94 ? 1349 SER A O   1 
ATOM   10341 C  CB  . SER A 1 1349 ? 31.211  -50.578 -14.605 1.00 179.75 ? 1349 SER A CB  1 
ATOM   10342 O  OG  . SER A 1 1349 ? 30.840  -50.974 -13.289 1.00 181.97 ? 1349 SER A OG  1 
ATOM   10343 N  N   . THR A 1 1350 ? 28.386  -48.440 -15.684 1.00 162.39 ? 1350 THR A N   1 
ATOM   10344 C  CA  . THR A 1 1350 ? 26.972  -48.554 -16.013 1.00 163.21 ? 1350 THR A CA  1 
ATOM   10345 C  C   . THR A 1 1350 ? 26.705  -49.757 -16.937 1.00 162.38 ? 1350 THR A C   1 
ATOM   10346 O  O   . THR A 1 1350 ? 27.633  -50.285 -17.550 1.00 160.62 ? 1350 THR A O   1 
ATOM   10347 C  CB  . THR A 1 1350 ? 26.466  -47.243 -16.674 1.00 169.24 ? 1350 THR A CB  1 
ATOM   10348 O  OG1 . THR A 1 1350 ? 25.036  -47.141 -16.561 1.00 171.42 ? 1350 THR A OG1 1 
ATOM   10349 C  CG2 . THR A 1 1350 ? 26.903  -47.158 -18.141 1.00 165.59 ? 1350 THR A CG2 1 
ATOM   10350 N  N   . GLY A 1 1351 ? 25.447  -50.201 -16.992 1.00 158.11 ? 1351 GLY A N   1 
ATOM   10351 C  CA  . GLY A 1 1351 ? 24.990  -51.195 -17.952 1.00 157.41 ? 1351 GLY A CA  1 
ATOM   10352 C  C   . GLY A 1 1351 ? 24.625  -50.501 -19.247 1.00 150.57 ? 1351 GLY A C   1 
ATOM   10353 O  O   . GLY A 1 1351 ? 25.398  -49.679 -19.728 1.00 146.58 ? 1351 GLY A O   1 
ATOM   10354 N  N   . PHE A 1 1352 ? 23.461  -50.792 -19.819 1.00 159.36 ? 1352 PHE A N   1 
ATOM   10355 C  CA  . PHE A 1 1352 ? 23.146  -50.147 -21.091 1.00 154.39 ? 1352 PHE A CA  1 
ATOM   10356 C  C   . PHE A 1 1352 ? 22.751  -48.694 -20.910 1.00 150.57 ? 1352 PHE A C   1 
ATOM   10357 O  O   . PHE A 1 1352 ? 23.599  -47.845 -20.661 1.00 150.28 ? 1352 PHE A O   1 
ATOM   10358 C  CB  . PHE A 1 1352 ? 22.074  -50.876 -21.908 1.00 153.08 ? 1352 PHE A CB  1 
ATOM   10359 C  CG  . PHE A 1 1352 ? 21.806  -50.215 -23.249 1.00 147.49 ? 1352 PHE A CG  1 
ATOM   10360 C  CD1 . PHE A 1 1352 ? 22.867  -49.907 -24.102 1.00 143.22 ? 1352 PHE A CD1 1 
ATOM   10361 C  CD2 . PHE A 1 1352 ? 20.516  -49.863 -23.645 1.00 146.38 ? 1352 PHE A CD2 1 
ATOM   10362 C  CE1 . PHE A 1 1352 ? 22.660  -49.279 -25.326 1.00 137.86 ? 1352 PHE A CE1 1 
ATOM   10363 C  CE2 . PHE A 1 1352 ? 20.300  -49.227 -24.886 1.00 141.14 ? 1352 PHE A CE2 1 
ATOM   10364 C  CZ  . PHE A 1 1352 ? 21.381  -48.941 -25.722 1.00 137.45 ? 1352 PHE A CZ  1 
ATOM   10365 N  N   . GLY A 1 1353 ? 21.460  -48.424 -21.088 1.00 135.34 ? 1353 GLY A N   1 
ATOM   10366 C  CA  . GLY A 1 1353 ? 20.850  -47.168 -20.690 1.00 132.78 ? 1353 GLY A CA  1 
ATOM   10367 C  C   . GLY A 1 1353 ? 20.646  -46.052 -21.694 1.00 128.96 ? 1353 GLY A C   1 
ATOM   10368 O  O   . GLY A 1 1353 ? 20.380  -46.297 -22.864 1.00 126.42 ? 1353 GLY A O   1 
ATOM   10369 N  N   . SER A 1 1354 ? 20.731  -44.818 -21.198 1.00 151.17 ? 1354 SER A N   1 
ATOM   10370 C  CA  . SER A 1 1354 ? 20.615  -43.609 -22.013 1.00 146.50 ? 1354 SER A CA  1 
ATOM   10371 C  C   . SER A 1 1354 ? 21.018  -42.343 -21.242 1.00 143.20 ? 1354 SER A C   1 
ATOM   10372 O  O   . SER A 1 1354 ? 21.101  -42.350 -20.005 1.00 145.23 ? 1354 SER A O   1 
ATOM   10373 C  CB  . SER A 1 1354 ? 19.198  -43.448 -22.574 1.00 147.65 ? 1354 SER A CB  1 
ATOM   10374 O  OG  . SER A 1 1354 ? 18.228  -43.292 -21.554 1.00 148.55 ? 1354 SER A OG  1 
ATOM   10375 N  N   . GLY A 1 1355 ? 21.254  -41.254 -21.974 1.00 132.52 ? 1355 GLY A N   1 
ATOM   10376 C  CA  . GLY A 1 1355 ? 21.682  -40.008 -21.356 1.00 130.78 ? 1355 GLY A CA  1 
ATOM   10377 C  C   . GLY A 1 1355 ? 23.172  -39.951 -21.045 1.00 132.18 ? 1355 GLY A C   1 
ATOM   10378 O  O   . GLY A 1 1355 ? 23.986  -40.613 -21.713 1.00 134.86 ? 1355 GLY A O   1 
ATOM   10379 N  N   . LEU A 1 1356 ? 23.518  -39.208 -19.994 1.00 145.54 ? 1356 LEU A N   1 
ATOM   10380 C  CA  . LEU A 1 1356 ? 24.877  -38.714 -19.794 1.00 146.85 ? 1356 LEU A CA  1 
ATOM   10381 C  C   . LEU A 1 1356 ? 25.271  -38.574 -18.317 1.00 157.29 ? 1356 LEU A C   1 
ATOM   10382 O  O   . LEU A 1 1356 ? 24.671  -37.783 -17.592 1.00 161.67 ? 1356 LEU A O   1 
ATOM   10383 C  CB  . LEU A 1 1356 ? 24.954  -37.339 -20.440 1.00 142.13 ? 1356 LEU A CB  1 
ATOM   10384 C  CG  . LEU A 1 1356 ? 25.607  -37.284 -21.793 1.00 136.22 ? 1356 LEU A CG  1 
ATOM   10385 C  CD1 . LEU A 1 1356 ? 25.324  -35.953 -22.460 1.00 130.52 ? 1356 LEU A CD1 1 
ATOM   10386 C  CD2 . LEU A 1 1356 ? 27.066  -37.480 -21.528 1.00 135.97 ? 1356 LEU A CD2 1 
ATOM   10387 N  N   . ALA A 1 1357 ? 26.290  -39.307 -17.867 1.00 192.21 ? 1357 ALA A N   1 
ATOM   10388 C  CA  . ALA A 1 1357 ? 26.705  -39.229 -16.455 1.00 188.30 ? 1357 ALA A CA  1 
ATOM   10389 C  C   . ALA A 1 1357 ? 28.159  -38.795 -16.267 1.00 185.31 ? 1357 ALA A C   1 
ATOM   10390 O  O   . ALA A 1 1357 ? 29.064  -39.486 -16.733 1.00 183.90 ? 1357 ALA A O   1 
ATOM   10391 C  CB  . ALA A 1 1357 ? 26.463  -40.558 -15.752 1.00 188.11 ? 1357 ALA A CB  1 
ATOM   10392 N  N   . THR A 1 1358 ? 28.376  -37.665 -15.583 1.00 141.63 ? 1358 THR A N   1 
ATOM   10393 C  CA  . THR A 1 1358 ? 29.728  -37.159 -15.330 1.00 140.92 ? 1358 THR A CA  1 
ATOM   10394 C  C   . THR A 1 1358 ? 30.330  -37.695 -14.034 1.00 146.05 ? 1358 THR A C   1 
ATOM   10395 O  O   . THR A 1 1358 ? 30.150  -37.118 -12.966 1.00 147.37 ? 1358 THR A O   1 
ATOM   10396 C  CB  . THR A 1 1358 ? 29.794  -35.623 -15.330 1.00 159.52 ? 1358 THR A CB  1 
ATOM   10397 O  OG1 . THR A 1 1358 ? 28.580  -35.098 -14.800 1.00 159.38 ? 1358 THR A OG1 1 
ATOM   10398 C  CG2 . THR A 1 1358 ? 29.945  -35.116 -16.730 1.00 155.48 ? 1358 THR A CG2 1 
ATOM   10399 N  N   . VAL A 1 1359 ? 31.035  -38.812 -14.152 1.00 127.50 ? 1359 VAL A N   1 
ATOM   10400 C  CA  . VAL A 1 1359 ? 31.774  -39.420 -13.063 1.00 135.39 ? 1359 VAL A CA  1 
ATOM   10401 C  C   . VAL A 1 1359 ? 33.015  -38.558 -12.774 1.00 141.00 ? 1359 VAL A C   1 
ATOM   10402 O  O   . VAL A 1 1359 ? 33.945  -38.529 -13.581 1.00 137.90 ? 1359 VAL A O   1 
ATOM   10403 C  CB  . VAL A 1 1359 ? 32.187  -40.871 -13.470 1.00 132.39 ? 1359 VAL A CB  1 
ATOM   10404 C  CG1 . VAL A 1 1359 ? 33.271  -41.409 -12.594 1.00 135.95 ? 1359 VAL A CG1 1 
ATOM   10405 C  CG2 . VAL A 1 1359 ? 30.998  -41.789 -13.431 1.00 132.99 ? 1359 VAL A CG2 1 
ATOM   10406 N  N   . HIS A 1 1360 ? 33.016  -37.816 -11.664 1.00 131.30 ? 1360 HIS A N   1 
ATOM   10407 C  CA  . HIS A 1 1360 ? 34.255  -37.205 -11.174 1.00 135.37 ? 1360 HIS A CA  1 
ATOM   10408 C  C   . HIS A 1 1360 ? 34.768  -37.945 -9.970  1.00 139.79 ? 1360 HIS A C   1 
ATOM   10409 O  O   . HIS A 1 1360 ? 34.009  -38.542 -9.206  1.00 144.31 ? 1360 HIS A O   1 
ATOM   10410 C  CB  . HIS A 1 1360 ? 34.089  -35.759 -10.747 1.00 138.25 ? 1360 HIS A CB  1 
ATOM   10411 C  CG  . HIS A 1 1360 ? 33.874  -34.801 -11.870 1.00 135.75 ? 1360 HIS A CG  1 
ATOM   10412 N  ND1 . HIS A 1 1360 ? 32.619  -34.403 -12.277 1.00 132.77 ? 1360 HIS A ND1 1 
ATOM   10413 C  CD2 . HIS A 1 1360 ? 34.755  -34.117 -12.634 1.00 134.55 ? 1360 HIS A CD2 1 
ATOM   10414 C  CE1 . HIS A 1 1360 ? 32.733  -33.524 -13.255 1.00 130.49 ? 1360 HIS A CE1 1 
ATOM   10415 N  NE2 . HIS A 1 1360 ? 34.018  -33.335 -13.493 1.00 131.93 ? 1360 HIS A NE2 1 
ATOM   10416 N  N   . VAL A 1 1361 ? 36.068  -37.833 -9.770  1.00 138.54 ? 1361 VAL A N   1 
ATOM   10417 C  CA  . VAL A 1 1361 ? 36.713  -38.500 -8.655  1.00 142.57 ? 1361 VAL A CA  1 
ATOM   10418 C  C   . VAL A 1 1361 ? 37.968  -37.711 -8.238  1.00 145.28 ? 1361 VAL A C   1 
ATOM   10419 O  O   . VAL A 1 1361 ? 39.021  -37.756 -8.912  1.00 144.87 ? 1361 VAL A O   1 
ATOM   10420 C  CB  . VAL A 1 1361 ? 36.943  -40.025 -8.934  1.00 141.46 ? 1361 VAL A CB  1 
ATOM   10421 C  CG1 . VAL A 1 1361 ? 38.382  -40.449 -8.737  1.00 137.55 ? 1361 VAL A CG1 1 
ATOM   10422 C  CG2 . VAL A 1 1361 ? 36.018  -40.854 -8.064  1.00 136.97 ? 1361 VAL A CG2 1 
ATOM   10423 N  N   . THR A 1 1362 ? 37.800  -36.953 -7.139  1.00 118.59 ? 1362 THR A N   1 
ATOM   10424 C  CA  . THR A 1 1362 ? 38.820  -36.051 -6.591  1.00 119.49 ? 1362 THR A CA  1 
ATOM   10425 C  C   . THR A 1 1362 ? 39.522  -36.687 -5.382  1.00 120.78 ? 1362 THR A C   1 
ATOM   10426 O  O   . THR A 1 1362 ? 38.977  -36.751 -4.289  1.00 131.87 ? 1362 THR A O   1 
ATOM   10427 C  CB  . THR A 1 1362 ? 38.234  -34.624 -6.333  1.00 120.81 ? 1362 THR A CB  1 
ATOM   10428 O  OG1 . THR A 1 1362 ? 39.280  -33.711 -5.974  1.00 123.69 ? 1362 THR A OG1 1 
ATOM   10429 C  CG2 . THR A 1 1362 ? 37.148  -34.676 -5.293  1.00 122.76 ? 1362 THR A CG2 1 
ATOM   10430 N  N   . THR A 1 1363 ? 40.725  -37.203 -5.652  1.00 131.27 ? 1363 THR A N   1 
ATOM   10431 C  CA  . THR A 1 1363 ? 41.568  -37.962 -4.717  1.00 141.10 ? 1363 THR A CA  1 
ATOM   10432 C  C   . THR A 1 1363 ? 42.616  -37.064 -4.059  1.00 149.93 ? 1363 THR A C   1 
ATOM   10433 O  O   . THR A 1 1363 ? 43.396  -36.395 -4.743  1.00 150.35 ? 1363 THR A O   1 
ATOM   10434 C  CB  . THR A 1 1363 ? 42.301  -39.163 -5.413  1.00 198.45 ? 1363 THR A CB  1 
ATOM   10435 O  OG1 . THR A 1 1363 ? 43.555  -38.742 -5.970  1.00 198.33 ? 1363 THR A OG1 1 
ATOM   10436 C  CG2 . THR A 1 1363 ? 41.454  -39.760 -6.522  1.00 195.05 ? 1363 THR A CG2 1 
ATOM   10437 N  N   . VAL A 1 1364 ? 42.633  -37.073 -2.725  1.00 119.24 ? 1364 VAL A N   1 
ATOM   10438 C  CA  . VAL A 1 1364 ? 43.490  -36.196 -1.925  1.00 120.23 ? 1364 VAL A CA  1 
ATOM   10439 C  C   . VAL A 1 1364 ? 44.521  -36.908 -1.051  1.00 127.44 ? 1364 VAL A C   1 
ATOM   10440 O  O   . VAL A 1 1364 ? 44.234  -37.878 -0.351  1.00 131.17 ? 1364 VAL A O   1 
ATOM   10441 C  CB  . VAL A 1 1364 ? 42.658  -35.341 -1.010  1.00 122.61 ? 1364 VAL A CB  1 
ATOM   10442 C  CG1 . VAL A 1 1364 ? 43.560  -34.732 0.008   1.00 123.21 ? 1364 VAL A CG1 1 
ATOM   10443 C  CG2 . VAL A 1 1364 ? 41.927  -34.276 -1.816  1.00 118.00 ? 1364 VAL A CG2 1 
ATOM   10444 N  N   . VAL A 1 1365 ? 45.732  -36.397 -1.075  1.00 180.74 ? 1365 VAL A N   1 
ATOM   10445 C  CA  . VAL A 1 1365 ? 46.778  -37.106 -0.406  1.00 186.01 ? 1365 VAL A CA  1 
ATOM   10446 C  C   . VAL A 1 1365 ? 47.771  -36.112 0.194   1.00 195.77 ? 1365 VAL A C   1 
ATOM   10447 O  O   . VAL A 1 1365 ? 47.948  -35.013 -0.330  1.00 197.19 ? 1365 VAL A O   1 
ATOM   10448 C  CB  . VAL A 1 1365 ? 47.424  -38.125 -1.380  1.00 179.81 ? 1365 VAL A CB  1 
ATOM   10449 C  CG1 . VAL A 1 1365 ? 48.542  -37.487 -2.207  1.00 177.85 ? 1365 VAL A CG1 1 
ATOM   10450 C  CG2 . VAL A 1 1365 ? 47.917  -39.342 -0.632  1.00 182.16 ? 1365 VAL A CG2 1 
ATOM   10451 N  N   . HIS A 1 1366 ? 48.372  -36.478 1.326   1.00 183.71 ? 1366 HIS A N   1 
ATOM   10452 C  CA  . HIS A 1 1366 ? 49.349  -35.618 1.990   1.00 186.38 ? 1366 HIS A CA  1 
ATOM   10453 C  C   . HIS A 1 1366 ? 50.770  -36.066 1.702   1.00 184.50 ? 1366 HIS A C   1 
ATOM   10454 O  O   . HIS A 1 1366 ? 51.159  -37.211 1.975   1.00 186.10 ? 1366 HIS A O   1 
ATOM   10455 C  CB  . HIS A 1 1366 ? 49.096  -35.575 3.492   1.00 192.82 ? 1366 HIS A CB  1 
ATOM   10456 C  CG  . HIS A 1 1366 ? 47.698  -35.220 3.849   1.00 193.64 ? 1366 HIS A CG  1 
ATOM   10457 N  ND1 . HIS A 1 1366 ? 46.616  -36.012 3.498   1.00 191.34 ? 1366 HIS A ND1 1 
ATOM   10458 C  CD2 . HIS A 1 1366 ? 47.171  -34.174 4.527   1.00 197.26 ? 1366 HIS A CD2 1 
ATOM   10459 C  CE1 . HIS A 1 1366 ? 45.509  -35.466 3.934   1.00 192.02 ? 1366 HIS A CE1 1 
ATOM   10460 N  NE2 . HIS A 1 1366 ? 45.811  -34.338 4.566   1.00 195.68 ? 1366 HIS A NE2 1 
ATOM   10461 N  N   . LYS A 1 1367 ? 51.542  -35.150 1.135   1.00 187.28 ? 1367 LYS A N   1 
ATOM   10462 C  CA  . LYS A 1 1367 ? 52.936  -35.434 0.869   1.00 191.70 ? 1367 LYS A CA  1 
ATOM   10463 C  C   . LYS A 1 1367 ? 53.889  -34.564 1.670   1.00 194.80 ? 1367 LYS A C   1 
ATOM   10464 O  O   . LYS A 1 1367 ? 53.522  -33.530 2.218   1.00 196.07 ? 1367 LYS A O   1 
ATOM   10465 C  CB  . LYS A 1 1367 ? 53.264  -35.408 -0.634  1.00 192.21 ? 1367 LYS A CB  1 
ATOM   10466 C  CG  . LYS A 1 1367 ? 52.760  -34.212 -1.417  1.00 191.30 ? 1367 LYS A CG  1 
ATOM   10467 C  CD  . LYS A 1 1367 ? 52.942  -34.464 -2.914  1.00 189.09 ? 1367 LYS A CD  1 
ATOM   10468 C  CE  . LYS A 1 1367 ? 52.245  -35.751 -3.360  1.00 187.46 ? 1367 LYS A CE  1 
ATOM   10469 N  NZ  . LYS A 1 1367 ? 52.196  -35.844 -4.848  1.00 184.89 ? 1367 LYS A NZ  1 
ATOM   10470 N  N   . THR A 1 1368 ? 55.130  -35.014 1.704   1.00 202.32 ? 1368 THR A N   1 
ATOM   10471 C  CA  . THR A 1 1368 ? 56.138  -34.482 2.587   1.00 204.05 ? 1368 THR A CA  1 
ATOM   10472 C  C   . THR A 1 1368 ? 57.128  -33.527 1.881   1.00 205.60 ? 1368 THR A C   1 
ATOM   10473 O  O   . THR A 1 1368 ? 57.843  -32.769 2.545   1.00 211.59 ? 1368 THR A O   1 
ATOM   10474 C  CB  . THR A 1 1368 ? 56.931  -35.644 3.157   1.00 209.14 ? 1368 THR A CB  1 
ATOM   10475 O  OG1 . THR A 1 1368 ? 57.769  -36.180 2.127   1.00 212.00 ? 1368 THR A OG1 1 
ATOM   10476 C  CG2 . THR A 1 1368 ? 55.992  -36.735 3.619   1.00 205.68 ? 1368 THR A CG2 1 
ATOM   10477 N  N   . SER A 1 1369 ? 57.184  -33.573 0.546   1.00 155.69 ? 1369 SER A N   1 
ATOM   10478 C  CA  . SER A 1 1369 ? 58.156  -32.777 -0.233  1.00 158.40 ? 1369 SER A CA  1 
ATOM   10479 C  C   . SER A 1 1369 ? 57.577  -32.049 -1.476  1.00 155.12 ? 1369 SER A C   1 
ATOM   10480 O  O   . SER A 1 1369 ? 56.712  -32.575 -2.185  1.00 148.15 ? 1369 SER A O   1 
ATOM   10481 C  CB  . SER A 1 1369 ? 59.359  -33.635 -0.672  1.00 164.26 ? 1369 SER A CB  1 
ATOM   10482 O  OG  . SER A 1 1369 ? 60.126  -34.090 0.425   1.00 170.90 ? 1369 SER A OG  1 
ATOM   10483 N  N   . THR A 1 1370 ? 58.076  -30.836 -1.719  1.00 186.73 ? 1370 THR A N   1 
ATOM   10484 C  CA  . THR A 1 1370 ? 57.790  -30.064 -2.929  1.00 188.94 ? 1370 THR A CA  1 
ATOM   10485 C  C   . THR A 1 1370 ? 58.988  -30.148 -3.866  1.00 202.90 ? 1370 THR A C   1 
ATOM   10486 O  O   . THR A 1 1370 ? 58.971  -29.608 -4.973  1.00 203.22 ? 1370 THR A O   1 
ATOM   10487 C  CB  . THR A 1 1370 ? 57.551  -28.578 -2.609  1.00 183.39 ? 1370 THR A CB  1 
ATOM   10488 O  OG1 . THR A 1 1370 ? 56.394  -28.456 -1.788  1.00 176.27 ? 1370 THR A OG1 1 
ATOM   10489 C  CG2 . THR A 1 1370 ? 57.330  -27.765 -3.872  1.00 180.60 ? 1370 THR A CG2 1 
ATOM   10490 N  N   . SER A 1 1371 ? 60.038  -30.823 -3.414  1.00 231.79 ? 1371 SER A N   1 
ATOM   10491 C  CA  . SER A 1 1371 ? 61.247  -30.969 -4.214  1.00 244.50 ? 1371 SER A CA  1 
ATOM   10492 C  C   . SER A 1 1371 ? 60.909  -31.362 -5.654  1.00 246.78 ? 1371 SER A C   1 
ATOM   10493 O  O   . SER A 1 1371 ? 61.538  -30.893 -6.602  1.00 250.28 ? 1371 SER A O   1 
ATOM   10494 C  CB  . SER A 1 1371 ? 62.170  -32.011 -3.591  1.00 253.20 ? 1371 SER A CB  1 
ATOM   10495 O  OG  . SER A 1 1371 ? 61.543  -33.280 -3.557  1.00 253.38 ? 1371 SER A OG  1 
ATOM   10496 N  N   . GLU A 1 1372 ? 59.910  -32.222 -5.813  1.00 263.30 ? 1372 GLU A N   1 
ATOM   10497 C  CA  . GLU A 1 1372 ? 59.432  -32.597 -7.137  1.00 263.39 ? 1372 GLU A CA  1 
ATOM   10498 C  C   . GLU A 1 1372 ? 58.942  -31.374 -7.915  1.00 251.42 ? 1372 GLU A C   1 
ATOM   10499 O  O   . GLU A 1 1372 ? 59.594  -30.916 -8.856  1.00 252.98 ? 1372 GLU A O   1 
ATOM   10500 C  CB  . GLU A 1 1372 ? 58.283  -33.599 -7.001  1.00 271.02 ? 1372 GLU A CB  1 
ATOM   10501 C  CG  . GLU A 1 1372 ? 57.273  -33.218 -5.910  1.00 278.19 ? 1372 GLU A CG  1 
ATOM   10502 C  CD  . GLU A 1 1372 ? 55.919  -33.902 -6.059  1.00 281.24 ? 1372 GLU A CD  1 
ATOM   10503 O  OE1 . GLU A 1 1372 ? 55.845  -34.933 -6.760  1.00 284.52 ? 1372 GLU A OE1 1 
ATOM   10504 O  OE2 . GLU A 1 1372 ? 54.929  -33.408 -5.468  1.00 279.40 ? 1372 GLU A OE2 1 
ATOM   10505 N  N   . GLU A 1 1373 ? 57.804  -30.846 -7.465  1.00 221.25 ? 1373 GLU A N   1 
ATOM   10506 C  CA  . GLU A 1 1373 ? 56.988  -29.839 -8.150  1.00 208.11 ? 1373 GLU A CA  1 
ATOM   10507 C  C   . GLU A 1 1373 ? 57.716  -28.718 -8.895  1.00 205.47 ? 1373 GLU A C   1 
ATOM   10508 O  O   . GLU A 1 1373 ? 58.931  -28.537 -8.786  1.00 210.21 ? 1373 GLU A O   1 
ATOM   10509 C  CB  . GLU A 1 1373 ? 55.987  -29.222 -7.158  1.00 198.68 ? 1373 GLU A CB  1 
ATOM   10510 C  CG  . GLU A 1 1373 ? 55.056  -30.233 -6.462  1.00 190.33 ? 1373 GLU A CG  1 
ATOM   10511 C  CD  . GLU A 1 1373 ? 54.107  -29.596 -5.438  1.00 181.27 ? 1373 GLU A CD  1 
ATOM   10512 O  OE1 . GLU A 1 1373 ? 54.195  -28.366 -5.209  1.00 178.56 ? 1373 GLU A OE1 1 
ATOM   10513 O  OE2 . GLU A 1 1373 ? 53.268  -30.335 -4.866  1.00 175.84 ? 1373 GLU A OE2 1 
ATOM   10514 N  N   . VAL A 1 1374 ? 56.921  -27.967 -9.648  1.00 193.72 ? 1374 VAL A N   1 
ATOM   10515 C  CA  . VAL A 1 1374 ? 57.390  -26.890 -10.501 1.00 190.64 ? 1374 VAL A CA  1 
ATOM   10516 C  C   . VAL A 1 1374 ? 57.402  -25.574 -9.784  1.00 189.51 ? 1374 VAL A C   1 
ATOM   10517 O  O   . VAL A 1 1374 ? 56.343  -25.049 -9.447  1.00 186.61 ? 1374 VAL A O   1 
ATOM   10518 C  CB  . VAL A 1 1374 ? 56.373  -26.615 -11.596 1.00 184.60 ? 1374 VAL A CB  1 
ATOM   10519 C  CG1 . VAL A 1 1374 ? 57.040  -25.891 -12.753 1.00 186.78 ? 1374 VAL A CG1 1 
ATOM   10520 C  CG2 . VAL A 1 1374 ? 55.680  -27.897 -12.026 1.00 181.48 ? 1374 VAL A CG2 1 
ATOM   10521 N  N   . CYS A 1 1375 ? 58.566  -24.979 -9.599  1.00 237.14 ? 1375 CYS A N   1 
ATOM   10522 C  CA  . CYS A 1 1375 ? 58.536  -23.633 -9.056  1.00 234.49 ? 1375 CYS A CA  1 
ATOM   10523 C  C   . CYS A 1 1375 ? 58.329  -22.558 -10.130 1.00 233.79 ? 1375 CYS A C   1 
ATOM   10524 O  O   . CYS A 1 1375 ? 59.036  -22.506 -11.143 1.00 234.77 ? 1375 CYS A O   1 
ATOM   10525 C  CB  . CYS A 1 1375 ? 59.717  -23.345 -8.119  1.00 237.53 ? 1375 CYS A CB  1 
ATOM   10526 S  SG  . CYS A 1 1375 ? 59.323  -23.700 -6.372  1.00 315.98 ? 1375 CYS A SG  1 
ATOM   10527 N  N   . SER A 1 1376 ? 57.307  -21.740 -9.893  1.00 174.22 ? 1376 SER A N   1 
ATOM   10528 C  CA  . SER A 1 1376 ? 56.974  -20.600 -10.725 1.00 174.02 ? 1376 SER A CA  1 
ATOM   10529 C  C   . SER A 1 1376 ? 57.258  -19.335 -9.932  1.00 179.08 ? 1376 SER A C   1 
ATOM   10530 O  O   . SER A 1 1376 ? 57.242  -18.229 -10.476 1.00 180.48 ? 1376 SER A O   1 
ATOM   10531 C  CB  . SER A 1 1376 ? 55.497  -20.649 -11.081 1.00 166.62 ? 1376 SER A CB  1 
ATOM   10532 O  OG  . SER A 1 1376 ? 55.005  -21.968 -10.935 1.00 162.40 ? 1376 SER A OG  1 
ATOM   10533 N  N   . PHE A 1 1377 ? 57.513  -19.514 -8.637  1.00 194.77 ? 1377 PHE A N   1 
ATOM   10534 C  CA  . PHE A 1 1377 ? 57.857  -18.410 -7.743  1.00 196.54 ? 1377 PHE A CA  1 
ATOM   10535 C  C   . PHE A 1 1377 ? 59.099  -18.654 -6.884  1.00 205.45 ? 1377 PHE A C   1 
ATOM   10536 O  O   . PHE A 1 1377 ? 59.233  -19.685 -6.219  1.00 206.66 ? 1377 PHE A O   1 
ATOM   10537 C  CB  . PHE A 1 1377 ? 56.683  -18.056 -6.842  1.00 191.61 ? 1377 PHE A CB  1 
ATOM   10538 C  CG  . PHE A 1 1377 ? 55.642  -17.242 -7.519  1.00 188.17 ? 1377 PHE A CG  1 
ATOM   10539 C  CD1 . PHE A 1 1377 ? 55.799  -15.872 -7.649  1.00 190.82 ? 1377 PHE A CD1 1 
ATOM   10540 C  CD2 . PHE A 1 1377 ? 54.509  -17.840 -8.037  1.00 183.87 ? 1377 PHE A CD2 1 
ATOM   10541 C  CE1 . PHE A 1 1377 ? 54.844  -15.110 -8.279  1.00 187.26 ? 1377 PHE A CE1 1 
ATOM   10542 C  CE2 . PHE A 1 1377 ? 53.544  -17.084 -8.663  1.00 180.35 ? 1377 PHE A CE2 1 
ATOM   10543 C  CZ  . PHE A 1 1377 ? 53.712  -15.714 -8.786  1.00 182.16 ? 1377 PHE A CZ  1 
ATOM   10544 N  N   . TYR A 1 1378 ? 60.004  -17.684 -6.911  1.00 204.90 ? 1378 TYR A N   1 
ATOM   10545 C  CA  . TYR A 1 1378 ? 61.165  -17.692 -6.050  1.00 208.46 ? 1378 TYR A CA  1 
ATOM   10546 C  C   . TYR A 1 1378 ? 60.731  -17.189 -4.675  1.00 208.34 ? 1378 TYR A C   1 
ATOM   10547 O  O   . TYR A 1 1378 ? 59.987  -16.213 -4.575  1.00 204.51 ? 1378 TYR A O   1 
ATOM   10548 C  CB  . TYR A 1 1378 ? 62.259  -16.784 -6.626  1.00 211.54 ? 1378 TYR A CB  1 
ATOM   10549 C  CG  . TYR A 1 1378 ? 62.982  -17.323 -7.846  1.00 208.56 ? 1378 TYR A CG  1 
ATOM   10550 C  CD1 . TYR A 1 1378 ? 63.521  -18.602 -7.844  1.00 207.47 ? 1378 TYR A CD1 1 
ATOM   10551 C  CD2 . TYR A 1 1378 ? 63.161  -16.536 -8.982  1.00 207.32 ? 1378 TYR A CD2 1 
ATOM   10552 C  CE1 . TYR A 1 1378 ? 64.193  -19.100 -8.945  1.00 207.81 ? 1378 TYR A CE1 1 
ATOM   10553 C  CE2 . TYR A 1 1378 ? 63.833  -17.026 -10.094 1.00 207.20 ? 1378 TYR A CE2 1 
ATOM   10554 C  CZ  . TYR A 1 1378 ? 64.349  -18.315 -10.072 1.00 207.71 ? 1378 TYR A CZ  1 
ATOM   10555 O  OH  . TYR A 1 1378 ? 65.024  -18.840 -11.162 1.00 209.06 ? 1378 TYR A OH  1 
ATOM   10556 N  N   . LEU A 1 1379 ? 61.198  -17.857 -3.622  1.00 190.03 ? 1379 LEU A N   1 
ATOM   10557 C  CA  . LEU A 1 1379 ? 60.830  -17.512 -2.249  1.00 196.96 ? 1379 LEU A CA  1 
ATOM   10558 C  C   . LEU A 1 1379 ? 62.009  -17.534 -1.280  1.00 211.41 ? 1379 LEU A C   1 
ATOM   10559 O  O   . LEU A 1 1379 ? 63.086  -18.062 -1.577  1.00 217.31 ? 1379 LEU A O   1 
ATOM   10560 C  CB  . LEU A 1 1379 ? 59.791  -18.486 -1.707  1.00 190.40 ? 1379 LEU A CB  1 
ATOM   10561 C  CG  . LEU A 1 1379 ? 58.464  -18.576 -2.422  1.00 182.21 ? 1379 LEU A CG  1 
ATOM   10562 C  CD1 . LEU A 1 1379 ? 57.578  -19.544 -1.667  1.00 177.68 ? 1379 LEU A CD1 1 
ATOM   10563 C  CD2 . LEU A 1 1379 ? 57.862  -17.195 -2.488  1.00 181.84 ? 1379 LEU A CD2 1 
ATOM   10564 N  N   . LYS A 1 1380 ? 61.767  -16.952 -0.109  1.00 231.83 ? 1380 LYS A N   1 
ATOM   10565 C  CA  . LYS A 1 1380 ? 62.558  -17.183 1.094   1.00 238.88 ? 1380 LYS A CA  1 
ATOM   10566 C  C   . LYS A 1 1380 ? 61.676  -16.853 2.307   1.00 236.91 ? 1380 LYS A C   1 
ATOM   10567 O  O   . LYS A 1 1380 ? 61.053  -15.788 2.363   1.00 234.51 ? 1380 LYS A O   1 
ATOM   10568 C  CB  . LYS A 1 1380 ? 63.865  -16.376 1.086   1.00 230.64 ? 1380 LYS A CB  1 
ATOM   10569 C  CG  . LYS A 1 1380 ? 63.760  -14.988 0.480   1.00 236.89 ? 1380 LYS A CG  1 
ATOM   10570 C  CD  . LYS A 1 1380 ? 65.138  -14.351 0.306   1.00 241.94 ? 1380 LYS A CD  1 
ATOM   10571 C  CE  . LYS A 1 1380 ? 65.038  -12.891 -0.126  1.00 225.25 ? 1380 LYS A CE  1 
ATOM   10572 N  NZ  . LYS A 1 1380 ? 66.384  -12.254 -0.247  1.00 231.75 ? 1380 LYS A NZ  1 
ATOM   10573 N  N   . ILE A 1 1381 ? 61.585  -17.797 3.243   1.00 168.55 ? 1381 ILE A N   1 
ATOM   10574 C  CA  . ILE A 1 1381 ? 60.863  -17.585 4.498   1.00 166.03 ? 1381 ILE A CA  1 
ATOM   10575 C  C   . ILE A 1 1381 ? 61.703  -18.047 5.694   1.00 178.76 ? 1381 ILE A C   1 
ATOM   10576 O  O   . ILE A 1 1381 ? 62.332  -19.117 5.655   1.00 184.53 ? 1381 ILE A O   1 
ATOM   10577 C  CB  . ILE A 1 1381 ? 59.546  -18.338 4.557   1.00 160.10 ? 1381 ILE A CB  1 
ATOM   10578 C  CG1 . ILE A 1 1381 ? 58.534  -17.526 5.320   1.00 158.48 ? 1381 ILE A CG1 1 
ATOM   10579 C  CG2 . ILE A 1 1381 ? 59.719  -19.629 5.303   1.00 160.23 ? 1381 ILE A CG2 1 
ATOM   10580 C  CD1 . ILE A 1 1381 ? 57.251  -18.218 5.445   1.00 185.90 ? 1381 ILE A CD1 1 
ATOM   10581 N  N   . ASP A 1 1382 ? 61.703  -17.229 6.750   1.00 243.74 ? 1382 ASP A N   1 
ATOM   10582 C  CA  . ASP A 1 1382 ? 62.450  -17.506 7.975   1.00 251.78 ? 1382 ASP A CA  1 
ATOM   10583 C  C   . ASP A 1 1382 ? 61.927  -16.659 9.137   1.00 254.64 ? 1382 ASP A C   1 
ATOM   10584 O  O   . ASP A 1 1382 ? 61.377  -15.573 8.943   1.00 251.03 ? 1382 ASP A O   1 
ATOM   10585 C  CB  . ASP A 1 1382 ? 63.947  -17.267 7.764   1.00 262.19 ? 1382 ASP A CB  1 
ATOM   10586 C  CG  . ASP A 1 1382 ? 64.284  -15.803 7.596   1.00 268.35 ? 1382 ASP A CG  1 
ATOM   10587 O  OD1 . ASP A 1 1382 ? 64.088  -15.257 6.490   1.00 265.19 ? 1382 ASP A OD1 1 
ATOM   10588 O  OD2 . ASP A 1 1382 ? 64.745  -15.197 8.584   1.00 276.41 ? 1382 ASP A OD2 1 
ATOM   10589 N  N   . THR A 1 1383 ? 62.093  -17.173 10.345  1.00 222.65 ? 1383 THR A N   1 
ATOM   10590 C  CA  . THR A 1 1383 ? 61.548  -16.522 11.519  1.00 226.34 ? 1383 THR A CA  1 
ATOM   10591 C  C   . THR A 1 1383 ? 62.654  -15.776 12.295  1.00 234.97 ? 1383 THR A C   1 
ATOM   10592 O  O   . THR A 1 1383 ? 63.630  -16.382 12.754  1.00 238.83 ? 1383 THR A O   1 
ATOM   10593 C  CB  . THR A 1 1383 ? 60.796  -17.550 12.383  1.00 224.80 ? 1383 THR A CB  1 
ATOM   10594 O  OG1 . THR A 1 1383 ? 61.453  -18.822 12.286  1.00 226.15 ? 1383 THR A OG1 1 
ATOM   10595 C  CG2 . THR A 1 1383 ? 59.373  -17.713 11.876  1.00 215.50 ? 1383 THR A CG2 1 
ATOM   10596 N  N   . GLN A 1 1384 ? 62.506  -14.455 12.403  1.00 224.12 ? 1384 GLN A N   1 
ATOM   10597 C  CA  . GLN A 1 1384 ? 63.505  -13.599 13.054  1.00 236.25 ? 1384 GLN A CA  1 
ATOM   10598 C  C   . GLN A 1 1384 ? 63.203  -13.386 14.550  1.00 242.74 ? 1384 GLN A C   1 
ATOM   10599 O  O   . GLN A 1 1384 ? 62.211  -13.904 15.058  1.00 238.52 ? 1384 GLN A O   1 
ATOM   10600 C  CB  . GLN A 1 1384 ? 63.620  -12.255 12.315  1.00 238.66 ? 1384 GLN A CB  1 
ATOM   10601 C  CG  . GLN A 1 1384 ? 64.207  -12.369 10.908  1.00 239.43 ? 1384 GLN A CG  1 
ATOM   10602 C  CD  . GLN A 1 1384 ? 64.430  -11.022 10.252  1.00 243.59 ? 1384 GLN A CD  1 
ATOM   10603 O  OE1 . GLN A 1 1384 ? 63.588  -10.142 10.338  1.00 243.37 ? 1384 GLN A OE1 1 
ATOM   10604 N  NE2 . GLN A 1 1384 ? 65.571  -10.858 9.593   1.00 247.24 ? 1384 GLN A NE2 1 
ATOM   10605 N  N   . ASP A 1 1385 ? 64.053  -12.637 15.255  1.00 294.36 ? 1385 ASP A N   1 
ATOM   10606 C  CA  . ASP A 1 1385 ? 63.808  -12.374 16.678  1.00 300.73 ? 1385 ASP A CA  1 
ATOM   10607 C  C   . ASP A 1 1385 ? 63.771  -10.888 17.070  1.00 304.36 ? 1385 ASP A C   1 
ATOM   10608 O  O   . ASP A 1 1385 ? 63.119  -10.518 18.051  1.00 305.40 ? 1385 ASP A O   1 
ATOM   10609 C  CB  . ASP A 1 1385 ? 64.784  -13.160 17.558  1.00 308.17 ? 1385 ASP A CB  1 
ATOM   10610 C  CG  . ASP A 1 1385 ? 64.474  -14.646 17.581  1.00 305.19 ? 1385 ASP A CG  1 
ATOM   10611 O  OD1 . ASP A 1 1385 ? 63.410  -15.027 18.115  1.00 302.37 ? 1385 ASP A OD1 1 
ATOM   10612 O  OD2 . ASP A 1 1385 ? 65.288  -15.435 17.057  1.00 306.02 ? 1385 ASP A OD2 1 
ATOM   10613 N  N   . ILE A 1 1386 ? 64.453  -10.049 16.293  1.00 276.26 ? 1386 ILE A N   1 
ATOM   10614 C  CA  . ILE A 1 1386 ? 64.489  -8.599  16.520  1.00 278.93 ? 1386 ILE A CA  1 
ATOM   10615 C  C   . ILE A 1 1386 ? 63.094  -7.946  16.457  1.00 270.73 ? 1386 ILE A C   1 
ATOM   10616 O  O   . ILE A 1 1386 ? 62.306  -7.984  17.414  1.00 268.46 ? 1386 ILE A O   1 
ATOM   10617 C  CB  . ILE A 1 1386 ? 65.419  -7.901  15.487  1.00 343.75 ? 1386 ILE A CB  1 
ATOM   10618 C  CG1 . ILE A 1 1386 ? 66.680  -8.734  15.233  1.00 347.07 ? 1386 ILE A CG1 1 
ATOM   10619 C  CG2 . ILE A 1 1386 ? 65.780  -6.488  15.935  1.00 350.08 ? 1386 ILE A CG2 1 
ATOM   10620 C  CD1 . ILE A 1 1386 ? 67.568  -8.183  14.139  1.00 348.69 ? 1386 ILE A CD1 1 
ATOM   10621 N  N   . TYR A 1 1399 ? 60.315  -9.806  19.818  1.00 308.32 ? 1399 TYR A N   1 
ATOM   10622 C  CA  . TYR A 1 1399 ? 60.061  -11.107 20.421  1.00 307.67 ? 1399 TYR A CA  1 
ATOM   10623 C  C   . TYR A 1 1399 ? 60.307  -12.177 19.377  1.00 289.37 ? 1399 TYR A C   1 
ATOM   10624 O  O   . TYR A 1 1399 ? 61.241  -12.974 19.487  1.00 291.98 ? 1399 TYR A O   1 
ATOM   10625 C  CB  . TYR A 1 1399 ? 58.618  -11.175 20.928  1.00 317.46 ? 1399 TYR A CB  1 
ATOM   10626 C  CG  . TYR A 1 1399 ? 58.172  -12.517 21.491  1.00 329.06 ? 1399 TYR A CG  1 
ATOM   10627 C  CD1 . TYR A 1 1399 ? 58.961  -13.224 22.397  1.00 340.72 ? 1399 TYR A CD1 1 
ATOM   10628 C  CD2 . TYR A 1 1399 ? 56.936  -13.059 21.140  1.00 326.27 ? 1399 TYR A CD2 1 
ATOM   10629 C  CE1 . TYR A 1 1399 ? 58.536  -14.446 22.917  1.00 342.77 ? 1399 TYR A CE1 1 
ATOM   10630 C  CE2 . TYR A 1 1399 ? 56.505  -14.273 21.654  1.00 327.98 ? 1399 TYR A CE2 1 
ATOM   10631 C  CZ  . TYR A 1 1399 ? 57.304  -14.962 22.540  1.00 336.02 ? 1399 TYR A CZ  1 
ATOM   10632 O  OH  . TYR A 1 1399 ? 56.868  -16.168 23.047  1.00 335.63 ? 1399 TYR A OH  1 
ATOM   10633 N  N   . LYS A 1 1400 ? 59.459  -12.179 18.355  1.00 261.19 ? 1400 LYS A N   1 
ATOM   10634 C  CA  . LYS A 1 1400 ? 59.622  -13.068 17.208  1.00 241.05 ? 1400 LYS A CA  1 
ATOM   10635 C  C   . LYS A 1 1400 ? 58.643  -12.723 16.072  1.00 219.81 ? 1400 LYS A C   1 
ATOM   10636 O  O   . LYS A 1 1400 ? 57.436  -12.589 16.294  1.00 214.44 ? 1400 LYS A O   1 
ATOM   10637 C  CB  . LYS A 1 1400 ? 59.537  -14.548 17.618  1.00 236.68 ? 1400 LYS A CB  1 
ATOM   10638 C  CG  . LYS A 1 1400 ? 58.357  -14.932 18.496  1.00 233.24 ? 1400 LYS A CG  1 
ATOM   10639 C  CD  . LYS A 1 1400 ? 58.314  -16.441 18.700  1.00 229.36 ? 1400 LYS A CD  1 
ATOM   10640 C  CE  . LYS A 1 1400 ? 59.682  -16.981 19.095  1.00 234.90 ? 1400 LYS A CE  1 
ATOM   10641 N  NZ  . LYS A 1 1400 ? 59.697  -18.463 19.229  1.00 231.54 ? 1400 LYS A NZ  1 
ATOM   10642 N  N   . ARG A 1 1401 ? 59.186  -12.587 14.858  1.00 217.63 ? 1401 ARG A N   1 
ATOM   10643 C  CA  . ARG A 1 1401 ? 58.438  -12.103 13.687  1.00 200.52 ? 1401 ARG A CA  1 
ATOM   10644 C  C   . ARG A 1 1401 ? 58.912  -12.741 12.359  1.00 195.37 ? 1401 ARG A C   1 
ATOM   10645 O  O   . ARG A 1 1401 ? 60.098  -13.050 12.180  1.00 200.12 ? 1401 ARG A O   1 
ATOM   10646 C  CB  . ARG A 1 1401 ? 58.453  -10.558 13.655  1.00 193.77 ? 1401 ARG A CB  1 
ATOM   10647 C  CG  . ARG A 1 1401 ? 58.633  -9.841  12.303  1.00 183.06 ? 1401 ARG A CG  1 
ATOM   10648 C  CD  . ARG A 1 1401 ? 60.114  -9.524  11.938  1.00 184.34 ? 1401 ARG A CD  1 
ATOM   10649 N  NE  . ARG A 1 1401 ? 60.354  -8.075  11.936  1.00 181.92 ? 1401 ARG A NE  1 
ATOM   10650 C  CZ  . ARG A 1 1401 ? 60.959  -7.380  10.967  1.00 182.62 ? 1401 ARG A CZ  1 
ATOM   10651 N  NH1 . ARG A 1 1401 ? 61.411  -7.960  9.866   1.00 184.79 ? 1401 ARG A NH1 1 
ATOM   10652 N  NH2 . ARG A 1 1401 ? 61.110  -6.071  11.101  1.00 181.96 ? 1401 ARG A NH2 1 
ATOM   10653 N  N   . ILE A 1 1402 ? 57.956  -12.953 11.456  1.00 232.12 ? 1402 ILE A N   1 
ATOM   10654 C  CA  . ILE A 1 1402 ? 58.162  -13.650 10.187  1.00 223.51 ? 1402 ILE A CA  1 
ATOM   10655 C  C   . ILE A 1 1402 ? 58.464  -12.692 9.027   1.00 223.09 ? 1402 ILE A C   1 
ATOM   10656 O  O   . ILE A 1 1402 ? 57.701  -11.759 8.776   1.00 220.08 ? 1402 ILE A O   1 
ATOM   10657 C  CB  . ILE A 1 1402 ? 56.884  -14.449 9.810   1.00 211.70 ? 1402 ILE A CB  1 
ATOM   10658 C  CG1 . ILE A 1 1402 ? 56.622  -15.608 10.779  1.00 210.43 ? 1402 ILE A CG1 1 
ATOM   10659 C  CG2 . ILE A 1 1402 ? 56.977  -14.987 8.402   1.00 205.93 ? 1402 ILE A CG2 1 
ATOM   10660 C  CD1 . ILE A 1 1402 ? 55.374  -16.443 10.400  1.00 202.29 ? 1402 ILE A CD1 1 
ATOM   10661 N  N   . VAL A 1 1403 ? 59.568  -12.925 8.318   1.00 166.09 ? 1403 VAL A N   1 
ATOM   10662 C  CA  . VAL A 1 1403 ? 59.845  -12.200 7.073   1.00 166.48 ? 1403 VAL A CA  1 
ATOM   10663 C  C   . VAL A 1 1403 ? 59.993  -13.183 5.920   1.00 165.43 ? 1403 VAL A C   1 
ATOM   10664 O  O   . VAL A 1 1403 ? 61.052  -13.819 5.790   1.00 167.65 ? 1403 VAL A O   1 
ATOM   10665 C  CB  . VAL A 1 1403 ? 61.140  -11.378 7.131   1.00 170.44 ? 1403 VAL A CB  1 
ATOM   10666 C  CG1 . VAL A 1 1403 ? 61.380  -10.657 5.812   1.00 170.73 ? 1403 VAL A CG1 1 
ATOM   10667 C  CG2 . VAL A 1 1403 ? 61.065  -10.380 8.245   1.00 171.71 ? 1403 VAL A CG2 1 
ATOM   10668 N  N   . ALA A 1 1404 ? 58.928  -13.284 5.100   1.00 201.67 ? 1404 ALA A N   1 
ATOM   10669 C  CA  . ALA A 1 1404 ? 58.811  -14.173 3.922   1.00 195.99 ? 1404 ALA A CA  1 
ATOM   10670 C  C   . ALA A 1 1404 ? 58.810  -13.384 2.624   1.00 194.22 ? 1404 ALA A C   1 
ATOM   10671 O  O   . ALA A 1 1404 ? 58.132  -12.358 2.508   1.00 190.79 ? 1404 ALA A O   1 
ATOM   10672 C  CB  . ALA A 1 1404 ? 57.539  -14.992 4.000   1.00 187.08 ? 1404 ALA A CB  1 
ATOM   10673 N  N   . CYS A 1 1405 ? 59.541  -13.890 1.637   1.00 289.67 ? 1405 CYS A N   1 
ATOM   10674 C  CA  . CYS A 1 1405 ? 59.783  -13.145 0.410   1.00 289.96 ? 1405 CYS A CA  1 
ATOM   10675 C  C   . CYS A 1 1405 ? 59.355  -13.911 -0.818  1.00 283.42 ? 1405 CYS A C   1 
ATOM   10676 O  O   . CYS A 1 1405 ? 58.909  -15.055 -0.738  1.00 282.52 ? 1405 CYS A O   1 
ATOM   10677 C  CB  . CYS A 1 1405 ? 61.271  -12.841 0.245   1.00 296.93 ? 1405 CYS A CB  1 
ATOM   10678 S  SG  . CYS A 1 1405 ? 62.160  -12.394 1.734   1.00 322.98 ? 1405 CYS A SG  1 
ATOM   10679 N  N   . ALA A 1 1406 ? 59.547  -13.276 -1.966  1.00 207.69 ? 1406 ALA A N   1 
ATOM   10680 C  CA  . ALA A 1 1406 ? 59.155  -13.863 -3.226  1.00 199.64 ? 1406 ALA A CA  1 
ATOM   10681 C  C   . ALA A 1 1406 ? 59.650  -13.017 -4.384  1.00 202.87 ? 1406 ALA A C   1 
ATOM   10682 O  O   . ALA A 1 1406 ? 59.809  -11.803 -4.256  1.00 204.12 ? 1406 ALA A O   1 
ATOM   10683 C  CB  . ALA A 1 1406 ? 57.647  -13.985 -3.288  1.00 189.99 ? 1406 ALA A CB  1 
ATOM   10684 N  N   . SER A 1 1407 ? 59.907  -13.677 -5.508  1.00 217.05 ? 1407 SER A N   1 
ATOM   10685 C  CA  . SER A 1 1407 ? 60.032  -13.002 -6.789  1.00 217.04 ? 1407 SER A CA  1 
ATOM   10686 C  C   . SER A 1 1407 ? 59.453  -13.885 -7.858  1.00 212.16 ? 1407 SER A C   1 
ATOM   10687 O  O   . SER A 1 1407 ? 59.590  -15.105 -7.814  1.00 212.13 ? 1407 SER A O   1 
ATOM   10688 C  CB  . SER A 1 1407 ? 61.474  -12.706 -7.163  1.00 221.71 ? 1407 SER A CB  1 
ATOM   10689 O  OG  . SER A 1 1407 ? 61.532  -12.383 -8.545  1.00 218.47 ? 1407 SER A OG  1 
ATOM   10690 N  N   . TYR A 1 1408 ? 58.817  -13.260 -8.834  1.00 235.62 ? 1408 TYR A N   1 
ATOM   10691 C  CA  . TYR A 1 1408 ? 58.167  -14.011 -9.883  1.00 228.21 ? 1408 TYR A CA  1 
ATOM   10692 C  C   . TYR A 1 1408 ? 59.176  -14.655 -10.830 1.00 228.61 ? 1408 TYR A C   1 
ATOM   10693 O  O   . TYR A 1 1408 ? 60.202  -14.053 -11.154 1.00 234.62 ? 1408 TYR A O   1 
ATOM   10694 C  CB  . TYR A 1 1408 ? 57.214  -13.115 -10.656 1.00 225.36 ? 1408 TYR A CB  1 
ATOM   10695 C  CG  . TYR A 1 1408 ? 56.625  -13.832 -11.815 1.00 222.68 ? 1408 TYR A CG  1 
ATOM   10696 C  CD1 . TYR A 1 1408 ? 56.209  -15.144 -11.678 1.00 221.07 ? 1408 TYR A CD1 1 
ATOM   10697 C  CD2 . TYR A 1 1408 ? 56.498  -13.219 -13.049 1.00 222.93 ? 1408 TYR A CD2 1 
ATOM   10698 C  CE1 . TYR A 1 1408 ? 55.676  -15.835 -12.733 1.00 220.14 ? 1408 TYR A CE1 1 
ATOM   10699 C  CE2 . TYR A 1 1408 ? 55.957  -13.898 -14.121 1.00 221.61 ? 1408 TYR A CE2 1 
ATOM   10700 C  CZ  . TYR A 1 1408 ? 55.545  -15.213 -13.957 1.00 221.41 ? 1408 TYR A CZ  1 
ATOM   10701 O  OH  . TYR A 1 1408 ? 54.999  -15.912 -15.016 1.00 220.84 ? 1408 TYR A OH  1 
ATOM   10702 N  N   . LYS A 1 1409 ? 58.884  -15.885 -11.254 1.00 218.06 ? 1409 LYS A N   1 
ATOM   10703 C  CA  . LYS A 1 1409 ? 59.705  -16.600 -12.232 1.00 218.48 ? 1409 LYS A CA  1 
ATOM   10704 C  C   . LYS A 1 1409 ? 59.083  -16.454 -13.604 1.00 219.81 ? 1409 LYS A C   1 
ATOM   10705 O  O   . LYS A 1 1409 ? 58.182  -17.213 -13.950 1.00 216.18 ? 1409 LYS A O   1 
ATOM   10706 C  CB  . LYS A 1 1409 ? 59.801  -18.097 -11.896 1.00 214.12 ? 1409 LYS A CB  1 
ATOM   10707 C  CG  . LYS A 1 1409 ? 60.622  -18.425 -10.655 1.00 212.40 ? 1409 LYS A CG  1 
ATOM   10708 C  CD  . LYS A 1 1409 ? 60.778  -19.936 -10.404 1.00 209.63 ? 1409 LYS A CD  1 
ATOM   10709 C  CE  . LYS A 1 1409 ? 62.114  -20.471 -10.946 1.00 214.89 ? 1409 LYS A CE  1 
ATOM   10710 N  NZ  . LYS A 1 1409 ? 62.670  -21.697 -10.267 1.00 217.16 ? 1409 LYS A NZ  1 
ATOM   10711 N  N   . PRO A 1 1410 ? 59.563  -15.485 -14.398 1.00 267.99 ? 1410 PRO A N   1 
ATOM   10712 C  CA  . PRO A 1 1410 ? 58.995  -15.260 -15.732 1.00 269.52 ? 1410 PRO A CA  1 
ATOM   10713 C  C   . PRO A 1 1410 ? 59.172  -16.472 -16.648 1.00 277.68 ? 1410 PRO A C   1 
ATOM   10714 O  O   . PRO A 1 1410 ? 60.304  -16.891 -16.886 1.00 281.25 ? 1410 PRO A O   1 
ATOM   10715 C  CB  . PRO A 1 1410 ? 59.813  -14.075 -16.266 1.00 270.13 ? 1410 PRO A CB  1 
ATOM   10716 C  CG  . PRO A 1 1410 ? 60.374  -13.416 -15.053 1.00 271.37 ? 1410 PRO A CG  1 
ATOM   10717 C  CD  . PRO A 1 1410 ? 60.640  -14.530 -14.089 1.00 273.05 ? 1410 PRO A CD  1 
ATOM   10718 N  N   . SER A 1 1411 ? 58.063  -17.025 -17.140 1.00 282.67 ? 1411 SER A N   1 
ATOM   10719 C  CA  . SER A 1 1411 ? 58.094  -18.090 -18.142 1.00 294.52 ? 1411 SER A CA  1 
ATOM   10720 C  C   . SER A 1 1411 ? 58.655  -17.531 -19.440 1.00 309.53 ? 1411 SER A C   1 
ATOM   10721 O  O   . SER A 1 1411 ? 58.605  -16.325 -19.676 1.00 310.36 ? 1411 SER A O   1 
ATOM   10722 C  CB  . SER A 1 1411 ? 56.686  -18.644 -18.407 1.00 289.68 ? 1411 SER A CB  1 
ATOM   10723 O  OG  . SER A 1 1411 ? 56.077  -19.170 -17.240 1.00 287.33 ? 1411 SER A OG  1 
ATOM   10724 N  N   . ARG A 1 1412 ? 59.174  -18.405 -20.291 1.00 274.07 ? 1412 ARG A N   1 
ATOM   10725 C  CA  . ARG A 1 1412 ? 59.717  -17.954 -21.559 1.00 289.33 ? 1412 ARG A CA  1 
ATOM   10726 C  C   . ARG A 1 1412 ? 58.673  -17.114 -22.286 1.00 285.32 ? 1412 ARG A C   1 
ATOM   10727 O  O   . ARG A 1 1412 ? 57.471  -17.314 -22.114 1.00 281.87 ? 1412 ARG A O   1 
ATOM   10728 C  CB  . ARG A 1 1412 ? 60.136  -19.143 -22.419 1.00 303.43 ? 1412 ARG A CB  1 
ATOM   10729 C  CG  . ARG A 1 1412 ? 59.002  -20.110 -22.702 1.00 310.28 ? 1412 ARG A CG  1 
ATOM   10730 C  CD  . ARG A 1 1412 ? 59.326  -21.051 -23.857 1.00 322.14 ? 1412 ARG A CD  1 
ATOM   10731 N  NE  . ARG A 1 1412 ? 58.104  -21.544 -24.492 1.00 325.25 ? 1412 ARG A NE  1 
ATOM   10732 C  CZ  . ARG A 1 1412 ? 58.072  -22.356 -25.544 1.00 331.36 ? 1412 ARG A CZ  1 
ATOM   10733 N  NH1 . ARG A 1 1412 ? 59.204  -22.782 -26.091 1.00 338.11 ? 1412 ARG A NH1 1 
ATOM   10734 N  NH2 . ARG A 1 1412 ? 56.905  -22.742 -26.047 1.00 328.91 ? 1412 ARG A NH2 1 
ATOM   10735 N  N   . GLU A 1 1413 ? 59.148  -16.169 -23.091 1.00 278.47 ? 1413 GLU A N   1 
ATOM   10736 C  CA  . GLU A 1 1413 ? 58.280  -15.307 -23.888 1.00 273.17 ? 1413 GLU A CA  1 
ATOM   10737 C  C   . GLU A 1 1413 ? 57.633  -14.217 -23.059 1.00 256.55 ? 1413 GLU A C   1 
ATOM   10738 O  O   . GLU A 1 1413 ? 57.047  -13.287 -23.607 1.00 253.06 ? 1413 GLU A O   1 
ATOM   10739 C  CB  . GLU A 1 1413 ? 57.186  -16.123 -24.578 1.00 279.47 ? 1413 GLU A CB  1 
ATOM   10740 C  CG  . GLU A 1 1413 ? 57.711  -17.273 -25.419 1.00 290.70 ? 1413 GLU A CG  1 
ATOM   10741 C  CD  . GLU A 1 1413 ? 58.469  -16.807 -26.653 1.00 301.22 ? 1413 GLU A CD  1 
ATOM   10742 O  OE1 . GLU A 1 1413 ? 58.061  -15.794 -27.260 1.00 303.01 ? 1413 GLU A OE1 1 
ATOM   10743 O  OE2 . GLU A 1 1413 ? 59.469  -17.459 -27.021 1.00 307.11 ? 1413 GLU A OE2 1 
ATOM   10744 N  N   . GLU A 1 1414 ? 57.731  -14.332 -21.741 1.00 238.56 ? 1414 GLU A N   1 
ATOM   10745 C  CA  . GLU A 1 1414 ? 57.042  -13.395 -20.859 1.00 221.32 ? 1414 GLU A CA  1 
ATOM   10746 C  C   . GLU A 1 1414 ? 57.807  -12.118 -20.549 1.00 217.86 ? 1414 GLU A C   1 
ATOM   10747 O  O   . GLU A 1 1414 ? 59.034  -12.100 -20.493 1.00 221.68 ? 1414 GLU A O   1 
ATOM   10748 C  CB  . GLU A 1 1414 ? 56.601  -14.077 -19.566 1.00 210.93 ? 1414 GLU A CB  1 
ATOM   10749 C  CG  . GLU A 1 1414 ? 55.238  -14.728 -19.674 1.00 197.44 ? 1414 GLU A CG  1 
ATOM   10750 C  CD  . GLU A 1 1414 ? 54.978  -15.717 -18.558 1.00 189.94 ? 1414 GLU A CD  1 
ATOM   10751 O  OE1 . GLU A 1 1414 ? 55.842  -15.838 -17.672 1.00 190.71 ? 1414 GLU A OE1 1 
ATOM   10752 O  OE2 . GLU A 1 1414 ? 53.918  -16.379 -18.566 1.00 184.23 ? 1414 GLU A OE2 1 
ATOM   10753 N  N   . SER A 1 1415 ? 57.049  -11.052 -20.331 1.00 246.45 ? 1415 SER A N   1 
ATOM   10754 C  CA  . SER A 1 1415 ? 57.612  -9.736  -20.098 1.00 246.70 ? 1415 SER A CA  1 
ATOM   10755 C  C   . SER A 1 1415 ? 58.374  -9.633  -18.774 1.00 248.60 ? 1415 SER A C   1 
ATOM   10756 O  O   . SER A 1 1415 ? 58.095  -10.358 -17.820 1.00 247.93 ? 1415 SER A O   1 
ATOM   10757 C  CB  . SER A 1 1415 ? 56.496  -8.705  -20.142 1.00 241.73 ? 1415 SER A CB  1 
ATOM   10758 O  OG  . SER A 1 1415 ? 57.003  -7.395  -20.052 1.00 242.82 ? 1415 SER A OG  1 
ATOM   10759 N  N   . SER A 1 1416 ? 59.337  -8.717  -18.729 1.00 198.03 ? 1416 SER A N   1 
ATOM   10760 C  CA  . SER A 1 1416 ? 60.104  -8.451  -17.519 1.00 203.67 ? 1416 SER A CA  1 
ATOM   10761 C  C   . SER A 1 1416 ? 59.229  -7.966  -16.360 1.00 202.48 ? 1416 SER A C   1 
ATOM   10762 O  O   . SER A 1 1416 ? 59.586  -8.132  -15.195 1.00 204.54 ? 1416 SER A O   1 
ATOM   10763 C  CB  . SER A 1 1416 ? 61.211  -7.425  -17.799 1.00 211.15 ? 1416 SER A CB  1 
ATOM   10764 O  OG  . SER A 1 1416 ? 60.685  -6.142  -18.119 1.00 212.20 ? 1416 SER A OG  1 
ATOM   10765 N  N   . SER A 1 1417 ? 58.084  -7.371  -16.671 1.00 235.18 ? 1417 SER A N   1 
ATOM   10766 C  CA  . SER A 1 1417 ? 57.271  -6.753  -15.629 1.00 234.41 ? 1417 SER A CA  1 
ATOM   10767 C  C   . SER A 1 1417 ? 56.937  -7.717  -14.496 1.00 230.57 ? 1417 SER A C   1 
ATOM   10768 O  O   . SER A 1 1417 ? 56.685  -7.292  -13.376 1.00 236.54 ? 1417 SER A O   1 
ATOM   10769 C  CB  . SER A 1 1417 ? 55.991  -6.120  -16.194 1.00 230.80 ? 1417 SER A CB  1 
ATOM   10770 O  OG  . SER A 1 1417 ? 54.905  -7.029  -16.201 1.00 225.10 ? 1417 SER A OG  1 
ATOM   10771 N  N   . GLY A 1 1418 ? 56.952  -9.014  -14.766 1.00 226.18 ? 1418 GLY A N   1 
ATOM   10772 C  CA  . GLY A 1 1418 ? 56.663  -9.977  -13.720 1.00 218.21 ? 1418 GLY A CA  1 
ATOM   10773 C  C   . GLY A 1 1418 ? 55.178  -10.249 -13.591 1.00 209.98 ? 1418 GLY A C   1 
ATOM   10774 O  O   . GLY A 1 1418 ? 54.450  -10.159 -14.570 1.00 203.46 ? 1418 GLY A O   1 
ATOM   10775 N  N   . SER A 1 1419 ? 54.718  -10.562 -12.385 1.00 203.87 ? 1419 SER A N   1 
ATOM   10776 C  CA  . SER A 1 1419 ? 53.404  -11.188 -12.209 1.00 195.63 ? 1419 SER A CA  1 
ATOM   10777 C  C   . SER A 1 1419 ? 52.140  -10.328 -12.447 1.00 186.04 ? 1419 SER A C   1 
ATOM   10778 O  O   . SER A 1 1419 ? 52.200  -9.098  -12.551 1.00 188.39 ? 1419 SER A O   1 
ATOM   10779 C  CB  . SER A 1 1419 ? 53.340  -11.877 -10.843 1.00 196.50 ? 1419 SER A CB  1 
ATOM   10780 O  OG  . SER A 1 1419 ? 52.249  -12.783 -10.781 1.00 189.84 ? 1419 SER A OG  1 
ATOM   10781 N  N   . SER A 1 1420 ? 51.006  -11.018 -12.569 1.00 181.40 ? 1420 SER A N   1 
ATOM   10782 C  CA  . SER A 1 1420 ? 49.685  -10.403 -12.594 1.00 174.42 ? 1420 SER A CA  1 
ATOM   10783 C  C   . SER A 1 1420 ? 49.088  -10.575 -11.209 1.00 175.43 ? 1420 SER A C   1 
ATOM   10784 O  O   . SER A 1 1420 ? 49.718  -11.159 -10.333 1.00 180.94 ? 1420 SER A O   1 
ATOM   10785 C  CB  . SER A 1 1420 ? 48.778  -11.098 -13.609 1.00 165.01 ? 1420 SER A CB  1 
ATOM   10786 O  OG  . SER A 1 1420 ? 48.156  -12.249 -13.050 1.00 159.76 ? 1420 SER A OG  1 
ATOM   10787 N  N   . HIS A 1 1421 ? 47.865  -10.090 -11.017 1.00 183.69 ? 1421 HIS A N   1 
ATOM   10788 C  CA  . HIS A 1 1421 ? 47.183  -10.191 -9.723  1.00 181.03 ? 1421 HIS A CA  1 
ATOM   10789 C  C   . HIS A 1 1421 ? 47.478  -11.527 -9.011  1.00 175.18 ? 1421 HIS A C   1 
ATOM   10790 O  O   . HIS A 1 1421 ? 47.206  -12.605 -9.555  1.00 167.81 ? 1421 HIS A O   1 
ATOM   10791 C  CB  . HIS A 1 1421 ? 45.679  -9.967  -9.914  1.00 179.82 ? 1421 HIS A CB  1 
ATOM   10792 C  CG  . HIS A 1 1421 ? 44.842  -10.431 -8.764  1.00 178.46 ? 1421 HIS A CG  1 
ATOM   10793 N  ND1 . HIS A 1 1421 ? 43.690  -11.164 -8.933  1.00 172.88 ? 1421 HIS A ND1 1 
ATOM   10794 C  CD2 . HIS A 1 1421 ? 44.999  -10.264 -7.430  1.00 181.56 ? 1421 HIS A CD2 1 
ATOM   10795 C  CE1 . HIS A 1 1421 ? 43.164  -11.426 -7.746  1.00 173.74 ? 1421 HIS A CE1 1 
ATOM   10796 N  NE2 . HIS A 1 1421 ? 43.943  -10.900 -6.822  1.00 178.70 ? 1421 HIS A NE2 1 
ATOM   10797 N  N   . ALA A 1 1422 ? 48.024  -11.444 -7.794  1.00 169.01 ? 1422 ALA A N   1 
ATOM   10798 C  CA  . ALA A 1 1422 ? 48.520  -12.626 -7.083  1.00 173.32 ? 1422 ALA A CA  1 
ATOM   10799 C  C   . ALA A 1 1422 ? 48.341  -12.575 -5.563  1.00 179.10 ? 1422 ALA A C   1 
ATOM   10800 O  O   . ALA A 1 1422 ? 48.307  -11.504 -4.957  1.00 180.70 ? 1422 ALA A O   1 
ATOM   10801 C  CB  . ALA A 1 1422 ? 49.984  -12.869 -7.429  1.00 175.47 ? 1422 ALA A CB  1 
ATOM   10802 N  N   . VAL A 1 1423 ? 48.233  -13.758 -4.968  1.00 172.35 ? 1423 VAL A N   1 
ATOM   10803 C  CA  . VAL A 1 1423 ? 48.061  -13.910 -3.533  1.00 177.41 ? 1423 VAL A CA  1 
ATOM   10804 C  C   . VAL A 1 1423 ? 49.353  -14.449 -2.864  1.00 183.94 ? 1423 VAL A C   1 
ATOM   10805 O  O   . VAL A 1 1423 ? 50.210  -15.006 -3.548  1.00 186.71 ? 1423 VAL A O   1 
ATOM   10806 C  CB  . VAL A 1 1423 ? 46.845  -14.841 -3.238  1.00 160.29 ? 1423 VAL A CB  1 
ATOM   10807 C  CG1 . VAL A 1 1423 ? 45.741  -14.569 -4.226  1.00 155.30 ? 1423 VAL A CG1 1 
ATOM   10808 C  CG2 . VAL A 1 1423 ? 47.229  -16.291 -3.298  1.00 159.58 ? 1423 VAL A CG2 1 
ATOM   10809 N  N   . MET A 1 1424 ? 49.514  -14.255 -1.551  1.00 169.19 ? 1424 MET A N   1 
ATOM   10810 C  CA  . MET A 1 1424 ? 50.541  -14.971 -0.789  1.00 168.53 ? 1424 MET A CA  1 
ATOM   10811 C  C   . MET A 1 1424 ? 49.854  -15.751 0.339   1.00 169.69 ? 1424 MET A C   1 
ATOM   10812 O  O   . MET A 1 1424 ? 48.979  -15.212 1.018   1.00 170.66 ? 1424 MET A O   1 
ATOM   10813 C  CB  . MET A 1 1424 ? 51.601  -14.006 -0.247  1.00 167.25 ? 1424 MET A CB  1 
ATOM   10814 C  CG  . MET A 1 1424 ? 52.158  -13.060 -1.303  1.00 165.84 ? 1424 MET A CG  1 
ATOM   10815 S  SD  . MET A 1 1424 ? 53.744  -12.286 -0.869  1.00 178.57 ? 1424 MET A SD  1 
ATOM   10816 C  CE  . MET A 1 1424 ? 54.862  -13.702 -0.857  1.00 174.07 ? 1424 MET A CE  1 
ATOM   10817 N  N   . ASP A 1 1425 ? 50.213  -17.025 0.513   1.00 148.32 ? 1425 ASP A N   1 
ATOM   10818 C  CA  . ASP A 1 1425 ? 49.518  -17.892 1.486   1.00 149.30 ? 1425 ASP A CA  1 
ATOM   10819 C  C   . ASP A 1 1425 ? 50.491  -18.524 2.492   1.00 157.68 ? 1425 ASP A C   1 
ATOM   10820 O  O   . ASP A 1 1425 ? 51.268  -19.425 2.137   1.00 159.85 ? 1425 ASP A O   1 
ATOM   10821 C  CB  . ASP A 1 1425 ? 48.687  -18.969 0.765   1.00 145.11 ? 1425 ASP A CB  1 
ATOM   10822 C  CG  . ASP A 1 1425 ? 47.971  -19.920 1.712   1.00 147.58 ? 1425 ASP A CG  1 
ATOM   10823 O  OD1 . ASP A 1 1425 ? 46.789  -19.658 2.007   1.00 145.25 ? 1425 ASP A OD1 1 
ATOM   10824 O  OD2 . ASP A 1 1425 ? 48.579  -20.946 2.104   1.00 151.58 ? 1425 ASP A OD2 1 
ATOM   10825 N  N   . ILE A 1 1426 ? 50.435  -18.034 3.743   1.00 137.17 ? 1426 ILE A N   1 
ATOM   10826 C  CA  . ILE A 1 1426 ? 51.270  -18.526 4.841   1.00 141.17 ? 1426 ILE A CA  1 
ATOM   10827 C  C   . ILE A 1 1426 ? 50.487  -19.290 5.888   1.00 138.34 ? 1426 ILE A C   1 
ATOM   10828 O  O   . ILE A 1 1426 ? 49.536  -18.785 6.483   1.00 136.28 ? 1426 ILE A O   1 
ATOM   10829 C  CB  . ILE A 1 1426 ? 52.003  -17.414 5.564   1.00 146.08 ? 1426 ILE A CB  1 
ATOM   10830 C  CG1 . ILE A 1 1426 ? 52.594  -16.430 4.561   1.00 144.68 ? 1426 ILE A CG1 1 
ATOM   10831 C  CG2 . ILE A 1 1426 ? 53.079  -18.018 6.414   1.00 145.25 ? 1426 ILE A CG2 1 
ATOM   10832 C  CD1 . ILE A 1 1426 ? 53.818  -15.717 5.060   1.00 152.17 ? 1426 ILE A CD1 1 
ATOM   10833 N  N   . SER A 1 1427 ? 50.903  -20.530 6.082   1.00 208.08 ? 1427 SER A N   1 
ATOM   10834 C  CA  . SER A 1 1427 ? 50.365  -21.393 7.108   1.00 207.06 ? 1427 SER A CA  1 
ATOM   10835 C  C   . SER A 1 1427 ? 51.170  -21.086 8.366   1.00 213.26 ? 1427 SER A C   1 
ATOM   10836 O  O   . SER A 1 1427 ? 52.375  -20.851 8.286   1.00 217.71 ? 1427 SER A O   1 
ATOM   10837 C  CB  . SER A 1 1427 ? 50.548  -22.850 6.674   1.00 196.03 ? 1427 SER A CB  1 
ATOM   10838 O  OG  . SER A 1 1427 ? 49.962  -23.761 7.584   1.00 196.49 ? 1427 SER A OG  1 
ATOM   10839 N  N   . LEU A 1 1428 ? 50.502  -21.048 9.518   1.00 177.61 ? 1428 LEU A N   1 
ATOM   10840 C  CA  . LEU A 1 1428 ? 51.161  -20.749 10.791  1.00 183.77 ? 1428 LEU A CA  1 
ATOM   10841 C  C   . LEU A 1 1428 ? 51.212  -21.963 11.716  1.00 186.60 ? 1428 LEU A C   1 
ATOM   10842 O  O   . LEU A 1 1428 ? 50.169  -22.523 12.066  1.00 182.50 ? 1428 LEU A O   1 
ATOM   10843 C  CB  . LEU A 1 1428 ? 50.446  -19.600 11.488  1.00 181.01 ? 1428 LEU A CB  1 
ATOM   10844 C  CG  . LEU A 1 1428 ? 50.444  -18.328 10.656  1.00 177.87 ? 1428 LEU A CG  1 
ATOM   10845 C  CD1 . LEU A 1 1428 ? 49.590  -17.267 11.309  1.00 177.69 ? 1428 LEU A CD1 1 
ATOM   10846 C  CD2 . LEU A 1 1428 ? 51.870  -17.831 10.405  1.00 180.15 ? 1428 LEU A CD2 1 
ATOM   10847 N  N   . PRO A 1 1429 ? 52.429  -22.333 12.157  1.00 170.73 ? 1429 PRO A N   1 
ATOM   10848 C  CA  . PRO A 1 1429 ? 52.747  -23.538 12.940  1.00 172.25 ? 1429 PRO A CA  1 
ATOM   10849 C  C   . PRO A 1 1429 ? 51.732  -23.708 14.038  1.00 172.34 ? 1429 PRO A C   1 
ATOM   10850 O  O   . PRO A 1 1429 ? 51.385  -22.721 14.664  1.00 171.84 ? 1429 PRO A O   1 
ATOM   10851 C  CB  . PRO A 1 1429 ? 54.070  -23.186 13.599  1.00 178.51 ? 1429 PRO A CB  1 
ATOM   10852 C  CG  . PRO A 1 1429 ? 54.653  -22.156 12.752  1.00 178.73 ? 1429 PRO A CG  1 
ATOM   10853 C  CD  . PRO A 1 1429 ? 53.550  -21.384 12.122  1.00 173.24 ? 1429 PRO A CD  1 
ATOM   10854 N  N   . THR A 1 1430 ? 51.284  -24.923 14.307  1.00 217.98 ? 1430 THR A N   1 
ATOM   10855 C  CA  . THR A 1 1430 ? 50.132  -25.090 15.191  1.00 218.29 ? 1430 THR A CA  1 
ATOM   10856 C  C   . THR A 1 1430 ? 50.183  -24.194 16.474  1.00 228.07 ? 1430 THR A C   1 
ATOM   10857 O  O   . THR A 1 1430 ? 51.078  -24.316 17.312  1.00 237.22 ? 1430 THR A O   1 
ATOM   10858 C  CB  . THR A 1 1430 ? 49.866  -26.587 15.480  1.00 215.98 ? 1430 THR A CB  1 
ATOM   10859 O  OG1 . THR A 1 1430 ? 50.011  -27.335 14.266  1.00 211.65 ? 1430 THR A OG1 1 
ATOM   10860 C  CG2 . THR A 1 1430 ? 48.470  -26.781 16.009  1.00 211.04 ? 1430 THR A CG2 1 
ATOM   10861 N  N   . GLY A 1 1431 ? 49.212  -23.283 16.586  1.00 210.75 ? 1431 GLY A N   1 
ATOM   10862 C  CA  . GLY A 1 1431 ? 49.187  -22.260 17.620  1.00 216.15 ? 1431 GLY A CA  1 
ATOM   10863 C  C   . GLY A 1 1431 ? 50.305  -21.235 17.528  1.00 222.44 ? 1431 GLY A C   1 
ATOM   10864 O  O   . GLY A 1 1431 ? 51.294  -21.359 18.242  1.00 224.85 ? 1431 GLY A O   1 
ATOM   10865 N  N   . ILE A 1 1432 ? 50.148  -20.227 16.662  1.00 168.74 ? 1432 ILE A N   1 
ATOM   10866 C  CA  . ILE A 1 1432 ? 51.149  -19.155 16.481  1.00 176.00 ? 1432 ILE A CA  1 
ATOM   10867 C  C   . ILE A 1 1432 ? 50.551  -17.838 15.930  1.00 174.33 ? 1432 ILE A C   1 
ATOM   10868 O  O   . ILE A 1 1432 ? 51.166  -17.177 15.098  1.00 176.58 ? 1432 ILE A O   1 
ATOM   10869 C  CB  . ILE A 1 1432 ? 52.336  -19.587 15.543  1.00 169.36 ? 1432 ILE A CB  1 
ATOM   10870 C  CG1 . ILE A 1 1432 ? 52.907  -20.949 15.938  1.00 176.32 ? 1432 ILE A CG1 1 
ATOM   10871 C  CG2 . ILE A 1 1432 ? 53.467  -18.553 15.530  1.00 174.14 ? 1432 ILE A CG2 1 
ATOM   10872 C  CD1 . ILE A 1 1432 ? 53.931  -20.897 17.022  1.00 178.15 ? 1432 ILE A CD1 1 
ATOM   10873 N  N   . SER A 1 1433 ? 49.369  -17.447 16.404  1.00 270.09 ? 1433 SER A N   1 
ATOM   10874 C  CA  . SER A 1 1433 ? 48.754  -16.171 16.013  1.00 266.75 ? 1433 SER A CA  1 
ATOM   10875 C  C   . SER A 1 1433 ? 49.755  -15.160 15.473  1.00 268.23 ? 1433 SER A C   1 
ATOM   10876 O  O   . SER A 1 1433 ? 50.875  -15.035 15.965  1.00 273.39 ? 1433 SER A O   1 
ATOM   10877 C  CB  . SER A 1 1433 ? 48.029  -15.526 17.200  1.00 271.43 ? 1433 SER A CB  1 
ATOM   10878 O  OG  . SER A 1 1433 ? 46.805  -16.175 17.495  1.00 269.93 ? 1433 SER A OG  1 
ATOM   10879 N  N   . ALA A 1 1434 ? 49.327  -14.413 14.474  1.00 177.68 ? 1434 ALA A N   1 
ATOM   10880 C  CA  . ALA A 1 1434 ? 50.201  -13.462 13.825  1.00 182.63 ? 1434 ALA A CA  1 
ATOM   10881 C  C   . ALA A 1 1434 ? 49.718  -12.056 14.094  1.00 185.31 ? 1434 ALA A C   1 
ATOM   10882 O  O   . ALA A 1 1434 ? 48.569  -11.851 14.496  1.00 184.67 ? 1434 ALA A O   1 
ATOM   10883 C  CB  . ALA A 1 1434 ? 50.216  -13.724 12.353  1.00 179.16 ? 1434 ALA A CB  1 
ATOM   10884 N  N   . ASN A 1 1435 ? 50.586  -11.085 13.836  1.00 171.18 ? 1435 ASN A N   1 
ATOM   10885 C  CA  . ASN A 1 1435 ? 50.339  -9.713  14.259  1.00 174.86 ? 1435 ASN A CA  1 
ATOM   10886 C  C   . ASN A 1 1435 ? 49.229  -8.994  13.492  1.00 167.80 ? 1435 ASN A C   1 
ATOM   10887 O  O   . ASN A 1 1435 ? 49.507  -8.182  12.619  1.00 165.82 ? 1435 ASN A O   1 
ATOM   10888 C  CB  . ASN A 1 1435 ? 51.647  -8.905  14.216  1.00 181.61 ? 1435 ASN A CB  1 
ATOM   10889 C  CG  . ASN A 1 1435 ? 51.824  -7.960  15.428  1.00 188.91 ? 1435 ASN A CG  1 
ATOM   10890 O  OD1 . ASN A 1 1435 ? 50.869  -7.336  15.908  1.00 187.61 ? 1435 ASN A OD1 1 
ATOM   10891 N  ND2 . ASN A 1 1435 ? 53.057  -7.857  15.917  1.00 197.48 ? 1435 ASN A ND2 1 
ATOM   10892 N  N   . GLU A 1 1436 ? 47.979  -9.272  13.860  1.00 189.25 ? 1436 GLU A N   1 
ATOM   10893 C  CA  . GLU A 1 1436 ? 46.832  -8.633  13.234  1.00 186.42 ? 1436 GLU A CA  1 
ATOM   10894 C  C   . GLU A 1 1436 ? 47.122  -7.204  12.819  1.00 187.73 ? 1436 GLU A C   1 
ATOM   10895 O  O   . GLU A 1 1436 ? 46.778  -6.774  11.725  1.00 184.33 ? 1436 GLU A O   1 
ATOM   10896 C  CB  . GLU A 1 1436 ? 45.646  -8.606  14.188  1.00 189.45 ? 1436 GLU A CB  1 
ATOM   10897 C  CG  . GLU A 1 1436 ? 44.373  -8.031  13.549  1.00 187.54 ? 1436 GLU A CG  1 
ATOM   10898 C  CD  . GLU A 1 1436 ? 43.591  -9.091  12.771  1.00 182.84 ? 1436 GLU A CD  1 
ATOM   10899 O  OE1 . GLU A 1 1436 ? 44.028  -10.265 12.815  1.00 184.36 ? 1436 GLU A OE1 1 
ATOM   10900 O  OE2 . GLU A 1 1436 ? 42.549  -8.772  12.132  1.00 176.34 ? 1436 GLU A OE2 1 
ATOM   10901 N  N   . GLU A 1 1437 ? 47.736  -6.457  13.721  1.00 171.24 ? 1437 GLU A N   1 
ATOM   10902 C  CA  . GLU A 1 1437 ? 48.006  -5.047  13.482  1.00 172.02 ? 1437 GLU A CA  1 
ATOM   10903 C  C   . GLU A 1 1437 ? 49.161  -4.915  12.499  1.00 174.76 ? 1437 GLU A C   1 
ATOM   10904 O  O   . GLU A 1 1437 ? 49.304  -3.910  11.820  1.00 174.74 ? 1437 GLU A O   1 
ATOM   10905 C  CB  . GLU A 1 1437 ? 48.334  -4.320  14.800  1.00 181.19 ? 1437 GLU A CB  1 
ATOM   10906 C  CG  . GLU A 1 1437 ? 47.956  -5.088  16.086  1.00 227.79 ? 1437 GLU A CG  1 
ATOM   10907 C  CD  . GLU A 1 1437 ? 46.553  -4.780  16.617  1.00 220.43 ? 1437 GLU A CD  1 
ATOM   10908 O  OE1 . GLU A 1 1437 ? 45.932  -3.803  16.146  1.00 217.15 ? 1437 GLU A OE1 1 
ATOM   10909 O  OE2 . GLU A 1 1437 ? 46.080  -5.517  17.519  1.00 216.75 ? 1437 GLU A OE2 1 
ATOM   10910 N  N   . ASP A 1 1438 ? 49.994  -5.941  12.424  1.00 217.63 ? 1438 ASP A N   1 
ATOM   10911 C  CA  . ASP A 1 1438 ? 51.154  -5.874  11.558  1.00 219.60 ? 1438 ASP A CA  1 
ATOM   10912 C  C   . ASP A 1 1438 ? 50.742  -5.726  10.111  1.00 211.48 ? 1438 ASP A C   1 
ATOM   10913 O  O   . ASP A 1 1438 ? 51.337  -4.933  9.377   1.00 212.61 ? 1438 ASP A O   1 
ATOM   10914 C  CB  . ASP A 1 1438 ? 52.031  -7.106  11.715  1.00 223.28 ? 1438 ASP A CB  1 
ATOM   10915 C  CG  . ASP A 1 1438 ? 53.248  -6.827  12.541  1.00 231.64 ? 1438 ASP A CG  1 
ATOM   10916 O  OD1 . ASP A 1 1438 ? 53.621  -5.641  12.636  1.00 235.84 ? 1438 ASP A OD1 1 
ATOM   10917 O  OD2 . ASP A 1 1438 ? 53.826  -7.779  13.095  1.00 233.61 ? 1438 ASP A OD2 1 
ATOM   10918 N  N   . LEU A 1 1439 ? 49.722  -6.492  9.711   1.00 171.86 ? 1439 LEU A N   1 
ATOM   10919 C  CA  . LEU A 1 1439 ? 49.288  -6.598  8.304   1.00 161.10 ? 1439 LEU A CA  1 
ATOM   10920 C  C   . LEU A 1 1439 ? 48.537  -5.347  7.850   1.00 157.66 ? 1439 LEU A C   1 
ATOM   10921 O  O   . LEU A 1 1439 ? 48.912  -4.717  6.857   1.00 156.48 ? 1439 LEU A O   1 
ATOM   10922 C  CB  . LEU A 1 1439 ? 48.411  -7.843  8.104   1.00 151.76 ? 1439 LEU A CB  1 
ATOM   10923 C  CG  . LEU A 1 1439 ? 48.990  -9.149  8.666   1.00 151.14 ? 1439 LEU A CG  1 
ATOM   10924 C  CD1 . LEU A 1 1439 ? 47.943  -10.265 8.759   1.00 145.88 ? 1439 LEU A CD1 1 
ATOM   10925 C  CD2 . LEU A 1 1439 ? 50.252  -9.604  7.907   1.00 151.00 ? 1439 LEU A CD2 1 
ATOM   10926 N  N   . LYS A 1 1440 ? 47.488  -4.994  8.597   1.00 163.42 ? 1440 LYS A N   1 
ATOM   10927 C  CA  . LYS A 1 1440 ? 46.738  -3.758  8.391   1.00 164.66 ? 1440 LYS A CA  1 
ATOM   10928 C  C   . LYS A 1 1440 ? 47.688  -2.599  8.061   1.00 166.71 ? 1440 LYS A C   1 
ATOM   10929 O  O   . LYS A 1 1440 ? 47.320  -1.655  7.362   1.00 163.38 ? 1440 LYS A O   1 
ATOM   10930 C  CB  . LYS A 1 1440 ? 45.930  -3.423  9.654   1.00 172.33 ? 1440 LYS A CB  1 
ATOM   10931 C  CG  . LYS A 1 1440 ? 44.798  -4.404  10.031  1.00 174.51 ? 1440 LYS A CG  1 
ATOM   10932 C  CD  . LYS A 1 1440 ? 43.560  -4.248  9.125   1.00 173.88 ? 1440 LYS A CD  1 
ATOM   10933 C  CE  . LYS A 1 1440 ? 42.201  -4.207  9.883   1.00 178.95 ? 1440 LYS A CE  1 
ATOM   10934 N  NZ  . LYS A 1 1440 ? 41.796  -5.434  10.644  1.00 181.26 ? 1440 LYS A NZ  1 
ATOM   10935 N  N   . ALA A 1 1441 ? 48.912  -2.685  8.579   1.00 165.73 ? 1441 ALA A N   1 
ATOM   10936 C  CA  . ALA A 1 1441 ? 49.926  -1.645  8.415   1.00 172.62 ? 1441 ALA A CA  1 
ATOM   10937 C  C   . ALA A 1 1441 ? 50.353  -1.622  6.969   1.00 174.08 ? 1441 ALA A C   1 
ATOM   10938 O  O   . ALA A 1 1441 ? 50.294  -0.598  6.280   1.00 175.99 ? 1441 ALA A O   1 
ATOM   10939 C  CB  . ALA A 1 1441 ? 51.148  -1.935  9.336   1.00 179.18 ? 1441 ALA A CB  1 
ATOM   10940 N  N   . LEU A 1 1442 ? 50.757  -2.801  6.530   1.00 199.39 ? 1442 LEU A N   1 
ATOM   10941 C  CA  . LEU A 1 1442 ? 51.168  -3.046  5.176   1.00 197.79 ? 1442 LEU A CA  1 
ATOM   10942 C  C   . LEU A 1 1442 ? 50.104  -2.562  4.168   1.00 199.40 ? 1442 LEU A C   1 
ATOM   10943 O  O   . LEU A 1 1442 ? 50.414  -1.775  3.271   1.00 203.64 ? 1442 LEU A O   1 
ATOM   10944 C  CB  . LEU A 1 1442 ? 51.484  -4.543  5.040   1.00 191.73 ? 1442 LEU A CB  1 
ATOM   10945 C  CG  . LEU A 1 1442 ? 52.586  -5.096  5.971   1.00 196.08 ? 1442 LEU A CG  1 
ATOM   10946 C  CD1 . LEU A 1 1442 ? 52.333  -6.540  6.395   1.00 194.13 ? 1442 LEU A CD1 1 
ATOM   10947 C  CD2 . LEU A 1 1442 ? 53.971  -4.960  5.340   1.00 199.41 ? 1442 LEU A CD2 1 
ATOM   10948 N  N   . VAL A 1 1443 ? 48.852  -2.991  4.335   1.00 189.95 ? 1443 VAL A N   1 
ATOM   10949 C  CA  . VAL A 1 1443 ? 47.793  -2.669  3.364   1.00 187.21 ? 1443 VAL A CA  1 
ATOM   10950 C  C   . VAL A 1 1443 ? 47.190  -1.275  3.515   1.00 189.08 ? 1443 VAL A C   1 
ATOM   10951 O  O   . VAL A 1 1443 ? 46.974  -0.573  2.534   1.00 187.51 ? 1443 VAL A O   1 
ATOM   10952 C  CB  . VAL A 1 1443 ? 46.630  -3.716  3.389   1.00 181.98 ? 1443 VAL A CB  1 
ATOM   10953 C  CG1 . VAL A 1 1443 ? 47.088  -5.019  4.014   1.00 183.63 ? 1443 VAL A CG1 1 
ATOM   10954 C  CG2 . VAL A 1 1443 ? 45.407  -3.176  4.130   1.00 181.82 ? 1443 VAL A CG2 1 
ATOM   10955 N  N   . GLU A 1 1444 ? 46.927  -0.879  4.751   1.00 222.83 ? 1444 GLU A N   1 
ATOM   10956 C  CA  . GLU A 1 1444 ? 46.063  0.262   5.011   1.00 226.42 ? 1444 GLU A CA  1 
ATOM   10957 C  C   . GLU A 1 1444 ? 46.640  1.609   4.573   1.00 227.47 ? 1444 GLU A C   1 
ATOM   10958 O  O   . GLU A 1 1444 ? 46.161  2.649   5.012   1.00 227.12 ? 1444 GLU A O   1 
ATOM   10959 C  CB  . GLU A 1 1444 ? 45.701  0.300   6.498   1.00 237.57 ? 1444 GLU A CB  1 
ATOM   10960 C  CG  . GLU A 1 1444 ? 44.449  1.084   6.842   1.00 243.75 ? 1444 GLU A CG  1 
ATOM   10961 C  CD  . GLU A 1 1444 ? 43.763  0.542   8.079   1.00 249.19 ? 1444 GLU A CD  1 
ATOM   10962 O  OE1 . GLU A 1 1444 ? 43.642  -0.698  8.172   1.00 247.14 ? 1444 GLU A OE1 1 
ATOM   10963 O  OE2 . GLU A 1 1444 ? 43.343  1.346   8.946   1.00 254.55 ? 1444 GLU A OE2 1 
ATOM   10964 N  N   . GLY A 1 1445 ? 47.645  1.614   3.704   1.00 215.20 ? 1445 GLY A N   1 
ATOM   10965 C  CA  . GLY A 1 1445 ? 48.277  2.872   3.344   1.00 222.10 ? 1445 GLY A CA  1 
ATOM   10966 C  C   . GLY A 1 1445 ? 48.569  3.129   1.876   1.00 221.80 ? 1445 GLY A C   1 
ATOM   10967 O  O   . GLY A 1 1445 ? 48.555  2.212   1.061   1.00 218.50 ? 1445 GLY A O   1 
ATOM   10968 N  N   . VAL A 1 1446 ? 48.824  4.400   1.557   1.00 167.19 ? 1446 VAL A N   1 
ATOM   10969 C  CA  . VAL A 1 1446 ? 49.271  4.852   0.235   1.00 166.50 ? 1446 VAL A CA  1 
ATOM   10970 C  C   . VAL A 1 1446 ? 50.681  4.342   -0.087  1.00 167.44 ? 1446 VAL A C   1 
ATOM   10971 O  O   . VAL A 1 1446 ? 51.177  4.482   -1.201  1.00 165.21 ? 1446 VAL A O   1 
ATOM   10972 C  CB  . VAL A 1 1446 ? 49.231  6.408   0.137   1.00 172.50 ? 1446 VAL A CB  1 
ATOM   10973 C  CG1 . VAL A 1 1446 ? 49.909  6.930   -1.130  1.00 173.37 ? 1446 VAL A CG1 1 
ATOM   10974 C  CG2 . VAL A 1 1446 ? 47.794  6.922   0.255   1.00 169.62 ? 1446 VAL A CG2 1 
ATOM   10975 N  N   . ASP A 1 1447 ? 51.332  3.766   0.910   1.00 252.60 ? 1447 ASP A N   1 
ATOM   10976 C  CA  . ASP A 1 1447 ? 52.523  2.981   0.662   1.00 255.87 ? 1447 ASP A CA  1 
ATOM   10977 C  C   . ASP A 1 1447 ? 52.078  1.528   0.609   1.00 249.08 ? 1447 ASP A C   1 
ATOM   10978 O  O   . ASP A 1 1447 ? 52.809  0.643   1.042   1.00 250.67 ? 1447 ASP A O   1 
ATOM   10979 C  CB  . ASP A 1 1447 ? 53.578  3.193   1.760   1.00 266.08 ? 1447 ASP A CB  1 
ATOM   10980 C  CG  . ASP A 1 1447 ? 53.152  2.628   3.116   1.00 269.09 ? 1447 ASP A CG  1 
ATOM   10981 O  OD1 . ASP A 1 1447 ? 52.036  2.074   3.214   1.00 263.79 ? 1447 ASP A OD1 1 
ATOM   10982 O  OD2 . ASP A 1 1447 ? 53.939  2.739   4.087   1.00 275.98 ? 1447 ASP A OD2 1 
ATOM   10983 N  N   . GLN A 1 1448 ? 50.871  1.284   0.094   1.00 187.50 ? 1448 GLN A N   1 
ATOM   10984 C  CA  . GLN A 1 1448 ? 50.300  -0.065  0.134   1.00 181.15 ? 1448 GLN A CA  1 
ATOM   10985 C  C   . GLN A 1 1448 ? 51.113  -1.091  -0.634  1.00 178.67 ? 1448 GLN A C   1 
ATOM   10986 O  O   . GLN A 1 1448 ? 51.108  -1.135  -1.865  1.00 176.73 ? 1448 GLN A O   1 
ATOM   10987 C  CB  . GLN A 1 1448 ? 48.811  -0.118  -0.255  1.00 175.18 ? 1448 GLN A CB  1 
ATOM   10988 C  CG  . GLN A 1 1448 ? 48.428  0.224   -1.700  1.00 172.80 ? 1448 GLN A CG  1 
ATOM   10989 C  CD  . GLN A 1 1448 ? 46.927  0.010   -1.959  1.00 168.01 ? 1448 GLN A CD  1 
ATOM   10990 O  OE1 . GLN A 1 1448 ? 46.447  -1.127  -2.003  1.00 164.02 ? 1448 GLN A OE1 1 
ATOM   10991 N  NE2 . GLN A 1 1448 ? 46.182  1.108   -2.107  1.00 167.72 ? 1448 GLN A NE2 1 
ATOM   10992 N  N   . LEU A 1 1449 ? 51.822  -1.902  0.142   1.00 208.06 ? 1449 LEU A N   1 
ATOM   10993 C  CA  . LEU A 1 1449 ? 52.691  -2.952  -0.357  1.00 208.82 ? 1449 LEU A CA  1 
ATOM   10994 C  C   . LEU A 1 1449 ? 51.858  -4.155  -0.714  1.00 197.90 ? 1449 LEU A C   1 
ATOM   10995 O  O   . LEU A 1 1449 ? 52.168  -4.888  -1.644  1.00 193.55 ? 1449 LEU A O   1 
ATOM   10996 C  CB  . LEU A 1 1449 ? 53.708  -3.323  0.722   1.00 219.90 ? 1449 LEU A CB  1 
ATOM   10997 C  CG  . LEU A 1 1449 ? 54.386  -4.689  0.639   1.00 224.62 ? 1449 LEU A CG  1 
ATOM   10998 C  CD1 . LEU A 1 1449 ? 54.937  -4.937  -0.759  1.00 224.61 ? 1449 LEU A CD1 1 
ATOM   10999 C  CD2 . LEU A 1 1449 ? 55.472  -4.822  1.719   1.00 232.95 ? 1449 LEU A CD2 1 
ATOM   11000 N  N   . PHE A 1 1450 ? 50.803  -4.356  0.057   1.00 192.23 ? 1450 PHE A N   1 
ATOM   11001 C  CA  . PHE A 1 1450 ? 49.817  -5.366  -0.248  1.00 183.59 ? 1450 PHE A CA  1 
ATOM   11002 C  C   . PHE A 1 1450 ? 48.506  -4.654  -0.328  1.00 180.25 ? 1450 PHE A C   1 
ATOM   11003 O  O   . PHE A 1 1450 ? 48.466  -3.427  -0.224  1.00 183.23 ? 1450 PHE A O   1 
ATOM   11004 C  CB  . PHE A 1 1450 ? 49.776  -6.423  0.835   1.00 182.23 ? 1450 PHE A CB  1 
ATOM   11005 C  CG  . PHE A 1 1450 ? 51.027  -7.196  0.922   1.00 184.62 ? 1450 PHE A CG  1 
ATOM   11006 C  CD1 . PHE A 1 1450 ? 52.096  -6.705  1.634   1.00 192.68 ? 1450 PHE A CD1 1 
ATOM   11007 C  CD2 . PHE A 1 1450 ? 51.163  -8.391  0.251   1.00 180.46 ? 1450 PHE A CD2 1 
ATOM   11008 C  CE1 . PHE A 1 1450 ? 53.273  -7.405  1.708   1.00 195.08 ? 1450 PHE A CE1 1 
ATOM   11009 C  CE2 . PHE A 1 1450 ? 52.340  -9.095  0.313   1.00 183.81 ? 1450 PHE A CE2 1 
ATOM   11010 C  CZ  . PHE A 1 1450 ? 53.398  -8.598  1.045   1.00 190.88 ? 1450 PHE A CZ  1 
ATOM   11011 N  N   . THR A 1 1451 ? 47.425  -5.405  -0.489  1.00 154.33 ? 1451 THR A N   1 
ATOM   11012 C  CA  . THR A 1 1451 ? 46.150  -4.772  -0.776  1.00 147.35 ? 1451 THR A CA  1 
ATOM   11013 C  C   . THR A 1 1451 ? 45.016  -5.549  -0.169  1.00 142.88 ? 1451 THR A C   1 
ATOM   11014 O  O   . THR A 1 1451 ? 43.887  -5.068  -0.091  1.00 139.89 ? 1451 THR A O   1 
ATOM   11015 C  CB  . THR A 1 1451 ? 45.912  -4.792  -2.240  1.00 140.23 ? 1451 THR A CB  1 
ATOM   11016 O  OG1 . THR A 1 1451 ? 45.763  -6.160  -2.629  1.00 134.67 ? 1451 THR A OG1 1 
ATOM   11017 C  CG2 . THR A 1 1451 ? 47.105  -4.199  -2.975  1.00 143.23 ? 1451 THR A CG2 1 
ATOM   11018 N  N   . ASP A 1 1452 ? 45.306  -6.774  0.229   1.00 161.69 ? 1452 ASP A N   1 
ATOM   11019 C  CA  . ASP A 1 1452 ? 44.365  -7.454  1.071   1.00 159.43 ? 1452 ASP A CA  1 
ATOM   11020 C  C   . ASP A 1 1452 ? 45.011  -8.541  1.898   1.00 163.42 ? 1452 ASP A C   1 
ATOM   11021 O  O   . ASP A 1 1452 ? 45.767  -9.374  1.399   1.00 162.51 ? 1452 ASP A O   1 
ATOM   11022 C  CB  . ASP A 1 1452 ? 43.189  -7.989  0.275   1.00 148.41 ? 1452 ASP A CB  1 
ATOM   11023 C  CG  . ASP A 1 1452 ? 41.931  -8.054  1.098   1.00 141.59 ? 1452 ASP A CG  1 
ATOM   11024 O  OD1 . ASP A 1 1452 ? 41.775  -9.025  1.869   1.00 141.65 ? 1452 ASP A OD1 1 
ATOM   11025 O  OD2 . ASP A 1 1452 ? 41.103  -7.128  0.978   1.00 136.78 ? 1452 ASP A OD2 1 
ATOM   11026 N  N   . TYR A 1 1453 ? 44.700  -8.494  3.188   1.00 202.81 ? 1453 TYR A N   1 
ATOM   11027 C  CA  . TYR A 1 1453 ? 45.162  -9.472  4.152   1.00 205.21 ? 1453 TYR A CA  1 
ATOM   11028 C  C   . TYR A 1 1453 ? 43.948  -10.133 4.787   1.00 201.04 ? 1453 TYR A C   1 
ATOM   11029 O  O   . TYR A 1 1453 ? 42.852  -9.578  4.769   1.00 198.64 ? 1453 TYR A O   1 
ATOM   11030 C  CB  . TYR A 1 1453 ? 45.990  -8.779  5.234   1.00 212.17 ? 1453 TYR A CB  1 
ATOM   11031 C  CG  . TYR A 1 1453 ? 45.181  -8.333  6.419   1.00 214.25 ? 1453 TYR A CG  1 
ATOM   11032 C  CD1 . TYR A 1 1453 ? 44.242  -7.319  6.300   1.00 215.53 ? 1453 TYR A CD1 1 
ATOM   11033 C  CD2 . TYR A 1 1453 ? 45.359  -8.930  7.660   1.00 218.18 ? 1453 TYR A CD2 1 
ATOM   11034 C  CE1 . TYR A 1 1453 ? 43.499  -6.920  7.385   1.00 218.38 ? 1453 TYR A CE1 1 
ATOM   11035 C  CE2 . TYR A 1 1453 ? 44.630  -8.538  8.748   1.00 221.39 ? 1453 TYR A CE2 1 
ATOM   11036 C  CZ  . TYR A 1 1453 ? 43.699  -7.533  8.610   1.00 219.83 ? 1453 TYR A CZ  1 
ATOM   11037 O  OH  . TYR A 1 1453 ? 42.961  -7.145  9.702   1.00 218.46 ? 1453 TYR A OH  1 
ATOM   11038 N  N   . GLN A 1 1454 ? 44.141  -11.310 5.364   1.00 190.84 ? 1454 GLN A N   1 
ATOM   11039 C  CA  . GLN A 1 1454 ? 43.053  -11.971 6.056   1.00 187.58 ? 1454 GLN A CA  1 
ATOM   11040 C  C   . GLN A 1 1454 ? 43.509  -13.255 6.679   1.00 189.03 ? 1454 GLN A C   1 
ATOM   11041 O  O   . GLN A 1 1454 ? 43.941  -14.181 5.998   1.00 186.57 ? 1454 GLN A O   1 
ATOM   11042 C  CB  . GLN A 1 1454 ? 41.930  -12.293 5.085   1.00 181.70 ? 1454 GLN A CB  1 
ATOM   11043 C  CG  . GLN A 1 1454 ? 42.427  -12.951 3.802   1.00 180.06 ? 1454 GLN A CG  1 
ATOM   11044 C  CD  . GLN A 1 1454 ? 41.335  -13.663 3.023   1.00 175.61 ? 1454 GLN A CD  1 
ATOM   11045 O  OE1 . GLN A 1 1454 ? 40.842  -14.712 3.441   1.00 174.02 ? 1454 GLN A OE1 1 
ATOM   11046 N  NE2 . GLN A 1 1454 ? 40.969  -13.107 1.873   1.00 173.24 ? 1454 GLN A NE2 1 
ATOM   11047 N  N   . ILE A 1 1455 ? 43.389  -13.321 7.988   1.00 230.70 ? 1455 ILE A N   1 
ATOM   11048 C  CA  . ILE A 1 1455 ? 43.728  -14.541 8.670   1.00 231.13 ? 1455 ILE A CA  1 
ATOM   11049 C  C   . ILE A 1 1455 ? 42.525  -15.462 8.739   1.00 225.28 ? 1455 ILE A C   1 
ATOM   11050 O  O   . ILE A 1 1455 ? 41.596  -15.235 9.514   1.00 224.65 ? 1455 ILE A O   1 
ATOM   11051 C  CB  . ILE A 1 1455 ? 44.229  -14.265 10.078  1.00 244.90 ? 1455 ILE A CB  1 
ATOM   11052 C  CG1 . ILE A 1 1455 ? 45.551  -13.488 10.031  1.00 250.32 ? 1455 ILE A CG1 1 
ATOM   11053 C  CG2 . ILE A 1 1455 ? 44.386  -15.570 10.825  1.00 245.97 ? 1455 ILE A CG2 1 
ATOM   11054 C  CD1 . ILE A 1 1455 ? 45.391  -11.982 9.961   1.00 251.87 ? 1455 ILE A CD1 1 
ATOM   11055 N  N   . LYS A 1 1456 ? 42.537  -16.504 7.924   1.00 185.94 ? 1456 LYS A N   1 
ATOM   11056 C  CA  . LYS A 1 1456 ? 41.501  -17.499 8.046   1.00 181.70 ? 1456 LYS A CA  1 
ATOM   11057 C  C   . LYS A 1 1456 ? 42.099  -18.803 8.514   1.00 179.17 ? 1456 LYS A C   1 
ATOM   11058 O  O   . LYS A 1 1456 ? 43.258  -19.112 8.229   1.00 179.00 ? 1456 LYS A O   1 
ATOM   11059 C  CB  . LYS A 1 1456 ? 40.752  -17.695 6.729   1.00 179.61 ? 1456 LYS A CB  1 
ATOM   11060 C  CG  . LYS A 1 1456 ? 39.395  -18.366 6.891   1.00 181.40 ? 1456 LYS A CG  1 
ATOM   11061 C  CD  . LYS A 1 1456 ? 38.767  -18.689 5.540   1.00 179.79 ? 1456 LYS A CD  1 
ATOM   11062 C  CE  . LYS A 1 1456 ? 37.314  -19.150 5.674   1.00 177.97 ? 1456 LYS A CE  1 
ATOM   11063 N  NZ  . LYS A 1 1456 ? 36.453  -18.100 6.311   1.00 179.29 ? 1456 LYS A NZ  1 
ATOM   11064 N  N   . ASP A 1 1457 ? 41.282  -19.543 9.253   1.00 200.06 ? 1457 ASP A N   1 
ATOM   11065 C  CA  . ASP A 1 1457 ? 41.608  -20.878 9.723   1.00 201.84 ? 1457 ASP A CA  1 
ATOM   11066 C  C   . ASP A 1 1457 ? 43.084  -21.177 9.561   1.00 202.83 ? 1457 ASP A C   1 
ATOM   11067 O  O   . ASP A 1 1457 ? 43.472  -21.981 8.727   1.00 200.36 ? 1457 ASP A O   1 
ATOM   11068 C  CB  . ASP A 1 1457 ? 40.761  -21.922 8.987   1.00 199.43 ? 1457 ASP A CB  1 
ATOM   11069 C  CG  . ASP A 1 1457 ? 39.265  -21.627 9.063   1.00 199.92 ? 1457 ASP A CG  1 
ATOM   11070 O  OD1 . ASP A 1 1457 ? 38.722  -21.483 10.181  1.00 204.96 ? 1457 ASP A OD1 1 
ATOM   11071 O  OD2 . ASP A 1 1457 ? 38.628  -21.543 7.991   1.00 195.49 ? 1457 ASP A OD2 1 
ATOM   11072 N  N   . GLY A 1 1458 ? 43.906  -20.504 10.353  1.00 190.13 ? 1458 GLY A N   1 
ATOM   11073 C  CA  . GLY A 1 1458 ? 45.316  -20.835 10.437  1.00 191.30 ? 1458 GLY A CA  1 
ATOM   11074 C  C   . GLY A 1 1458 ? 46.177  -20.346 9.293   1.00 188.62 ? 1458 GLY A C   1 
ATOM   11075 O  O   . GLY A 1 1458 ? 47.295  -20.818 9.102   1.00 190.68 ? 1458 GLY A O   1 
ATOM   11076 N  N   . HIS A 1 1459 ? 45.681  -19.391 8.529   1.00 210.60 ? 1459 HIS A N   1 
ATOM   11077 C  CA  . HIS A 1 1459 ? 46.461  -18.958 7.402   1.00 209.99 ? 1459 HIS A CA  1 
ATOM   11078 C  C   . HIS A 1 1459 ? 46.414  -17.475 7.218   1.00 208.48 ? 1459 HIS A C   1 
ATOM   11079 O  O   . HIS A 1 1459 ? 45.356  -16.851 7.313   1.00 204.40 ? 1459 HIS A O   1 
ATOM   11080 C  CB  . HIS A 1 1459 ? 45.957  -19.612 6.135   1.00 205.69 ? 1459 HIS A CB  1 
ATOM   11081 C  CG  . HIS A 1 1459 ? 46.043  -21.107 6.140   1.00 208.67 ? 1459 HIS A CG  1 
ATOM   11082 N  ND1 . HIS A 1 1459 ? 47.147  -21.793 5.678   1.00 212.35 ? 1459 HIS A ND1 1 
ATOM   11083 C  CD2 . HIS A 1 1459 ? 45.142  -22.051 6.507   1.00 207.41 ? 1459 HIS A CD2 1 
ATOM   11084 C  CE1 . HIS A 1 1459 ? 46.929  -23.094 5.774   1.00 210.61 ? 1459 HIS A CE1 1 
ATOM   11085 N  NE2 . HIS A 1 1459 ? 45.719  -23.277 6.274   1.00 207.57 ? 1459 HIS A NE2 1 
ATOM   11086 N  N   . VAL A 1 1460 ? 47.588  -16.926 6.943   1.00 177.33 ? 1460 VAL A N   1 
ATOM   11087 C  CA  . VAL A 1 1460 ? 47.735  -15.529 6.571   1.00 180.42 ? 1460 VAL A CA  1 
ATOM   11088 C  C   . VAL A 1 1460 ? 47.669  -15.415 5.065   1.00 180.37 ? 1460 VAL A C   1 
ATOM   11089 O  O   . VAL A 1 1460 ? 48.541  -15.938 4.373   1.00 182.86 ? 1460 VAL A O   1 
ATOM   11090 C  CB  . VAL A 1 1460 ? 49.099  -14.970 7.000   1.00 187.63 ? 1460 VAL A CB  1 
ATOM   11091 C  CG1 . VAL A 1 1460 ? 49.581  -13.922 6.001   1.00 188.04 ? 1460 VAL A CG1 1 
ATOM   11092 C  CG2 . VAL A 1 1460 ? 49.038  -14.393 8.421   1.00 192.99 ? 1460 VAL A CG2 1 
ATOM   11093 N  N   . ILE A 1 1461 ? 46.659  -14.709 4.559   1.00 186.01 ? 1461 ILE A N   1 
ATOM   11094 C  CA  . ILE A 1 1461 ? 46.445  -14.619 3.117   1.00 180.08 ? 1461 ILE A CA  1 
ATOM   11095 C  C   . ILE A 1 1461 ? 46.435  -13.209 2.535   1.00 180.88 ? 1461 ILE A C   1 
ATOM   11096 O  O   . ILE A 1 1461 ? 45.487  -12.443 2.695   1.00 178.58 ? 1461 ILE A O   1 
ATOM   11097 C  CB  . ILE A 1 1461 ? 45.181  -15.338 2.715   1.00 169.29 ? 1461 ILE A CB  1 
ATOM   11098 C  CG1 . ILE A 1 1461 ? 45.427  -16.841 2.781   1.00 167.80 ? 1461 ILE A CG1 1 
ATOM   11099 C  CG2 . ILE A 1 1461 ? 44.811  -14.925 1.331   1.00 162.04 ? 1461 ILE A CG2 1 
ATOM   11100 C  CD1 . ILE A 1 1461 ? 44.173  -17.647 2.906   1.00 163.22 ? 1461 ILE A CD1 1 
ATOM   11101 N  N   . LEU A 1 1462 ? 47.508  -12.888 1.832   1.00 170.63 ? 1462 LEU A N   1 
ATOM   11102 C  CA  . LEU A 1 1462 ? 47.706  -11.546 1.324   1.00 173.33 ? 1462 LEU A CA  1 
ATOM   11103 C  C   . LEU A 1 1462 ? 47.510  -11.464 -0.171  1.00 171.95 ? 1462 LEU A C   1 
ATOM   11104 O  O   . LEU A 1 1462 ? 48.088  -12.258 -0.908  1.00 170.94 ? 1462 LEU A O   1 
ATOM   11105 C  CB  . LEU A 1 1462 ? 49.119  -11.098 1.647   1.00 177.20 ? 1462 LEU A CB  1 
ATOM   11106 C  CG  . LEU A 1 1462 ? 49.266  -10.759 3.108   1.00 167.69 ? 1462 LEU A CG  1 
ATOM   11107 C  CD1 . LEU A 1 1462 ? 50.719  -10.688 3.434   1.00 174.33 ? 1462 LEU A CD1 1 
ATOM   11108 C  CD2 . LEU A 1 1462 ? 48.587  -9.438  3.345   1.00 167.98 ? 1462 LEU A CD2 1 
ATOM   11109 N  N   . GLN A 1 1463 ? 46.720  -10.486 -0.613  1.00 170.92 ? 1463 GLN A N   1 
ATOM   11110 C  CA  . GLN A 1 1463 ? 46.577  -10.184 -2.037  1.00 165.28 ? 1463 GLN A CA  1 
ATOM   11111 C  C   . GLN A 1 1463 ? 47.321  -8.906  -2.426  1.00 165.97 ? 1463 GLN A C   1 
ATOM   11112 O  O   . GLN A 1 1463 ? 47.556  -8.013  -1.605  1.00 167.50 ? 1463 GLN A O   1 
ATOM   11113 C  CB  . GLN A 1 1463 ? 45.096  -10.070 -2.443  1.00 161.45 ? 1463 GLN A CB  1 
ATOM   11114 C  CG  . GLN A 1 1463 ? 44.415  -11.356 -2.921  1.00 158.02 ? 1463 GLN A CG  1 
ATOM   11115 C  CD  . GLN A 1 1463 ? 42.922  -11.179 -3.064  1.00 156.03 ? 1463 GLN A CD  1 
ATOM   11116 O  OE1 . GLN A 1 1463 ? 42.156  -12.140 -2.997  1.00 152.86 ? 1463 GLN A OE1 1 
ATOM   11117 N  NE2 . GLN A 1 1463 ? 42.498  -9.941  -3.251  1.00 157.98 ? 1463 GLN A NE2 1 
ATOM   11118 N  N   . LEU A 1 1464 ? 47.681  -8.840  -3.698  1.00 191.89 ? 1464 LEU A N   1 
ATOM   11119 C  CA  . LEU A 1 1464 ? 48.280  -7.658  -4.275  1.00 194.42 ? 1464 LEU A CA  1 
ATOM   11120 C  C   . LEU A 1 1464 ? 48.378  -7.887  -5.752  1.00 193.12 ? 1464 LEU A C   1 
ATOM   11121 O  O   . LEU A 1 1464 ? 48.116  -8.986  -6.239  1.00 186.98 ? 1464 LEU A O   1 
ATOM   11122 C  CB  . LEU A 1 1464 ? 49.672  -7.425  -3.734  1.00 201.03 ? 1464 LEU A CB  1 
ATOM   11123 C  CG  . LEU A 1 1464 ? 50.501  -8.683  -3.468  1.00 199.87 ? 1464 LEU A CG  1 
ATOM   11124 C  CD1 . LEU A 1 1464 ? 50.402  -9.758  -4.545  1.00 193.95 ? 1464 LEU A CD1 1 
ATOM   11125 C  CD2 . LEU A 1 1464 ? 51.950  -8.281  -3.249  1.00 206.58 ? 1464 LEU A CD2 1 
ATOM   11126 N  N   . ASN A 1 1465 ? 48.791  -6.845  -6.455  1.00 191.12 ? 1465 ASN A N   1 
ATOM   11127 C  CA  . ASN A 1 1465 ? 48.737  -6.812  -7.908  1.00 191.97 ? 1465 ASN A CA  1 
ATOM   11128 C  C   . ASN A 1 1465 ? 49.869  -7.524  -8.634  1.00 194.46 ? 1465 ASN A C   1 
ATOM   11129 O  O   . ASN A 1 1465 ? 49.652  -8.122  -9.684  1.00 190.08 ? 1465 ASN A O   1 
ATOM   11130 C  CB  . ASN A 1 1465 ? 48.692  -5.364  -8.362  1.00 195.53 ? 1465 ASN A CB  1 
ATOM   11131 C  CG  . ASN A 1 1465 ? 47.835  -4.519  -7.469  1.00 196.00 ? 1465 ASN A CG  1 
ATOM   11132 O  OD1 . ASN A 1 1465 ? 46.816  -3.994  -7.903  1.00 190.53 ? 1465 ASN A OD1 1 
ATOM   11133 N  ND2 . ASN A 1 1465 ? 48.231  -4.392  -6.202  1.00 200.28 ? 1465 ASN A ND2 1 
ATOM   11134 N  N   . SER A 1 1466 ? 51.078  -7.452  -8.093  1.00 207.07 ? 1466 SER A N   1 
ATOM   11135 C  CA  . SER A 1 1466 ? 52.231  -8.007  -8.796  1.00 211.86 ? 1466 SER A CA  1 
ATOM   11136 C  C   . SER A 1 1466 ? 53.257  -8.581  -7.839  1.00 215.29 ? 1466 SER A C   1 
ATOM   11137 O  O   . SER A 1 1466 ? 53.214  -8.330  -6.645  1.00 215.89 ? 1466 SER A O   1 
ATOM   11138 C  CB  . SER A 1 1466 ? 52.886  -6.945  -9.689  1.00 217.33 ? 1466 SER A CB  1 
ATOM   11139 O  OG  . SER A 1 1466 ? 54.060  -7.437  -10.316 1.00 222.53 ? 1466 SER A OG  1 
ATOM   11140 N  N   . ILE A 1 1467 ? 54.166  -9.379  -8.375  1.00 195.16 ? 1467 ILE A N   1 
ATOM   11141 C  CA  . ILE A 1 1467 ? 55.287  -9.880  -7.608  1.00 202.31 ? 1467 ILE A CA  1 
ATOM   11142 C  C   . ILE A 1 1467 ? 56.498  -9.732  -8.507  1.00 208.96 ? 1467 ILE A C   1 
ATOM   11143 O  O   . ILE A 1 1467 ? 57.165  -10.720 -8.815  1.00 212.34 ? 1467 ILE A O   1 
ATOM   11144 C  CB  . ILE A 1 1467 ? 55.115  -11.362 -7.243  1.00 195.86 ? 1467 ILE A CB  1 
ATOM   11145 C  CG1 . ILE A 1 1467 ? 53.778  -11.605 -6.550  1.00 186.83 ? 1467 ILE A CG1 1 
ATOM   11146 C  CG2 . ILE A 1 1467 ? 56.246  -11.831 -6.343  1.00 203.12 ? 1467 ILE A CG2 1 
ATOM   11147 C  CD1 . ILE A 1 1467 ? 53.659  -12.993 -5.964  1.00 183.43 ? 1467 ILE A CD1 1 
ATOM   11148 N  N   . PRO A 1 1468 ? 56.778  -8.490  -8.947  1.00 170.72 ? 1468 PRO A N   1 
ATOM   11149 C  CA  . PRO A 1 1468 ? 57.852  -8.168  -9.902  1.00 173.14 ? 1468 PRO A CA  1 
ATOM   11150 C  C   . PRO A 1 1468 ? 59.167  -8.954  -9.739  1.00 178.18 ? 1468 PRO A C   1 
ATOM   11151 O  O   . PRO A 1 1468 ? 59.486  -9.495  -8.681  1.00 177.83 ? 1468 PRO A O   1 
ATOM   11152 C  CB  . PRO A 1 1468 ? 58.041  -6.660  -9.706  1.00 176.90 ? 1468 PRO A CB  1 
ATOM   11153 C  CG  . PRO A 1 1468 ? 56.650  -6.190  -9.420  1.00 172.53 ? 1468 PRO A CG  1 
ATOM   11154 C  CD  . PRO A 1 1468 ? 56.017  -7.283  -8.576  1.00 169.53 ? 1468 PRO A CD  1 
ATOM   11155 N  N   . SER A 1 1469 ? 59.914  -9.027  -10.828 1.00 165.57 ? 1469 SER A N   1 
ATOM   11156 C  CA  . SER A 1 1469 ? 60.989  -9.978  -10.909 1.00 170.57 ? 1469 SER A CA  1 
ATOM   11157 C  C   . SER A 1 1469 ? 62.295  -9.251  -10.959 1.00 179.26 ? 1469 SER A C   1 
ATOM   11158 O  O   . SER A 1 1469 ? 63.321  -9.856  -11.235 1.00 185.08 ? 1469 SER A O   1 
ATOM   11159 C  CB  . SER A 1 1469 ? 60.855  -10.821 -12.170 1.00 166.78 ? 1469 SER A CB  1 
ATOM   11160 O  OG  . SER A 1 1469 ? 59.568  -11.406 -12.271 1.00 160.36 ? 1469 SER A OG  1 
ATOM   11161 N  N   . SER A 1 1470 ? 62.265  -7.947  -10.730 1.00 239.79 ? 1470 SER A N   1 
ATOM   11162 C  CA  . SER A 1 1470 ? 63.499  -7.176  -10.642 1.00 246.49 ? 1470 SER A CA  1 
ATOM   11163 C  C   . SER A 1 1470 ? 64.279  -7.570  -9.382  1.00 248.89 ? 1470 SER A C   1 
ATOM   11164 O  O   . SER A 1 1470 ? 65.505  -7.680  -9.392  1.00 255.24 ? 1470 SER A O   1 
ATOM   11165 C  CB  . SER A 1 1470 ? 63.166  -5.690  -10.627 1.00 249.23 ? 1470 SER A CB  1 
ATOM   11166 O  OG  . SER A 1 1470 ? 61.920  -5.490  -9.987  1.00 247.71 ? 1470 SER A OG  1 
ATOM   11167 N  N   . ASP A 1 1471 ? 63.538  -7.784  -8.303  1.00 198.11 ? 1471 ASP A N   1 
ATOM   11168 C  CA  . ASP A 1 1471 ? 64.068  -8.282  -7.043  1.00 201.45 ? 1471 ASP A CA  1 
ATOM   11169 C  C   . ASP A 1 1471 ? 62.913  -8.998  -6.360  1.00 189.88 ? 1471 ASP A C   1 
ATOM   11170 O  O   . ASP A 1 1471 ? 61.931  -9.340  -7.026  1.00 181.11 ? 1471 ASP A O   1 
ATOM   11171 C  CB  . ASP A 1 1471 ? 64.610  -7.140  -6.173  1.00 214.04 ? 1471 ASP A CB  1 
ATOM   11172 C  CG  . ASP A 1 1471 ? 63.559  -6.082  -5.840  1.00 217.32 ? 1471 ASP A CG  1 
ATOM   11173 O  OD1 . ASP A 1 1471 ? 63.945  -4.931  -5.548  1.00 224.41 ? 1471 ASP A OD1 1 
ATOM   11174 O  OD2 . ASP A 1 1471 ? 62.352  -6.385  -5.859  1.00 211.66 ? 1471 ASP A OD2 1 
ATOM   11175 N  N   . PHE A 1 1472 ? 63.013  -9.237  -5.056  1.00 210.95 ? 1472 PHE A N   1 
ATOM   11176 C  CA  . PHE A 1 1472 ? 61.904  -9.862  -4.343  1.00 201.37 ? 1472 PHE A CA  1 
ATOM   11177 C  C   . PHE A 1 1472 ? 60.830  -8.857  -3.983  1.00 197.37 ? 1472 PHE A C   1 
ATOM   11178 O  O   . PHE A 1 1472 ? 60.867  -7.694  -4.380  1.00 198.27 ? 1472 PHE A O   1 
ATOM   11179 C  CB  . PHE A 1 1472 ? 62.370  -10.556 -3.066  1.00 204.55 ? 1472 PHE A CB  1 
ATOM   11180 C  CG  . PHE A 1 1472 ? 63.059  -11.864 -3.298  1.00 204.30 ? 1472 PHE A CG  1 
ATOM   11181 C  CD1 . PHE A 1 1472 ? 64.254  -11.918 -4.001  1.00 209.15 ? 1472 PHE A CD1 1 
ATOM   11182 C  CD2 . PHE A 1 1472 ? 62.532  -13.038 -2.788  1.00 201.54 ? 1472 PHE A CD2 1 
ATOM   11183 C  CE1 . PHE A 1 1472 ? 64.906  -13.122 -4.208  1.00 210.27 ? 1472 PHE A CE1 1 
ATOM   11184 C  CE2 . PHE A 1 1472 ? 63.179  -14.246 -2.988  1.00 202.58 ? 1472 PHE A CE2 1 
ATOM   11185 C  CZ  . PHE A 1 1472 ? 64.371  -14.288 -3.699  1.00 206.96 ? 1472 PHE A CZ  1 
ATOM   11186 N  N   . LEU A 1 1473 ? 59.866  -9.337  -3.217  1.00 242.79 ? 1473 LEU A N   1 
ATOM   11187 C  CA  . LEU A 1 1473 ? 58.887  -8.487  -2.578  1.00 242.20 ? 1473 LEU A CA  1 
ATOM   11188 C  C   . LEU A 1 1473 ? 58.592  -9.160  -1.248  1.00 245.55 ? 1473 LEU A C   1 
ATOM   11189 O  O   . LEU A 1 1473 ? 58.123  -10.302 -1.224  1.00 241.87 ? 1473 LEU A O   1 
ATOM   11190 C  CB  . LEU A 1 1473 ? 57.623  -8.387  -3.430  1.00 231.60 ? 1473 LEU A CB  1 
ATOM   11191 C  CG  . LEU A 1 1473 ? 56.409  -7.699  -2.797  1.00 229.41 ? 1473 LEU A CG  1 
ATOM   11192 C  CD1 . LEU A 1 1473 ? 55.733  -6.786  -3.798  1.00 226.67 ? 1473 LEU A CD1 1 
ATOM   11193 C  CD2 . LEU A 1 1473 ? 55.422  -8.716  -2.236  1.00 224.69 ? 1473 LEU A CD2 1 
ATOM   11194 N  N   . CYS A 1 1474 ? 58.883  -8.477  -0.142  1.00 215.37 ? 1474 CYS A N   1 
ATOM   11195 C  CA  . CYS A 1 1474 ? 58.750  -9.119  1.162   1.00 214.94 ? 1474 CYS A CA  1 
ATOM   11196 C  C   . CYS A 1 1474 ? 57.779  -8.510  2.156   1.00 215.93 ? 1474 CYS A C   1 
ATOM   11197 O  O   . CYS A 1 1474 ? 57.769  -7.302  2.397   1.00 220.12 ? 1474 CYS A O   1 
ATOM   11198 C  CB  . CYS A 1 1474 ? 60.112  -9.337  1.813   1.00 219.14 ? 1474 CYS A CB  1 
ATOM   11199 S  SG  . CYS A 1 1474 ? 60.830  -10.915 1.304   1.00 229.64 ? 1474 CYS A SG  1 
ATOM   11200 N  N   . VAL A 1 1475 ? 56.975  -9.396  2.733   1.00 188.78 ? 1475 VAL A N   1 
ATOM   11201 C  CA  . VAL A 1 1475 ? 56.056  -9.075  3.807   1.00 190.66 ? 1475 VAL A CA  1 
ATOM   11202 C  C   . VAL A 1 1475 ? 56.780  -9.264  5.154   1.00 200.18 ? 1475 VAL A C   1 
ATOM   11203 O  O   . VAL A 1 1475 ? 57.777  -9.991  5.225   1.00 202.72 ? 1475 VAL A O   1 
ATOM   11204 C  CB  . VAL A 1 1475 ? 54.883  -10.041 3.747   1.00 181.32 ? 1475 VAL A CB  1 
ATOM   11205 C  CG1 . VAL A 1 1475 ? 55.404  -11.484 3.656   1.00 180.41 ? 1475 VAL A CG1 1 
ATOM   11206 C  CG2 . VAL A 1 1475 ? 53.954  -9.838  4.935   1.00 180.63 ? 1475 VAL A CG2 1 
ATOM   11207 N  N   . ARG A 1 1476 ? 56.303  -8.604  6.215   1.00 186.78 ? 1476 ARG A N   1 
ATOM   11208 C  CA  . ARG A 1 1476 ? 56.774  -8.893  7.575   1.00 190.50 ? 1476 ARG A CA  1 
ATOM   11209 C  C   . ARG A 1 1476 ? 55.679  -8.692  8.600   1.00 185.16 ? 1476 ARG A C   1 
ATOM   11210 O  O   . ARG A 1 1476 ? 54.934  -7.712  8.543   1.00 180.88 ? 1476 ARG A O   1 
ATOM   11211 C  CB  . ARG A 1 1476 ? 57.970  -8.037  7.966   1.00 201.30 ? 1476 ARG A CB  1 
ATOM   11212 C  CG  . ARG A 1 1476 ? 57.899  -6.641  7.441   1.00 207.39 ? 1476 ARG A CG  1 
ATOM   11213 C  CD  . ARG A 1 1476 ? 58.883  -6.514  6.300   1.00 213.79 ? 1476 ARG A CD  1 
ATOM   11214 N  NE  . ARG A 1 1476 ? 58.466  -5.502  5.345   1.00 217.50 ? 1476 ARG A NE  1 
ATOM   11215 C  CZ  . ARG A 1 1476 ? 59.139  -5.203  4.240   1.00 222.62 ? 1476 ARG A CZ  1 
ATOM   11216 N  NH1 . ARG A 1 1476 ? 60.275  -5.838  3.941   1.00 226.77 ? 1476 ARG A NH1 1 
ATOM   11217 N  NH2 . ARG A 1 1476 ? 58.669  -4.265  3.433   1.00 220.82 ? 1476 ARG A NH2 1 
ATOM   11218 N  N   . PHE A 1 1477 ? 55.602  -9.637  9.533   1.00 242.89 ? 1477 PHE A N   1 
ATOM   11219 C  CA  . PHE A 1 1477 ? 54.642  -9.597  10.635  1.00 241.36 ? 1477 PHE A CA  1 
ATOM   11220 C  C   . PHE A 1 1477 ? 55.159  -10.416 11.826  1.00 246.16 ? 1477 PHE A C   1 
ATOM   11221 O  O   . PHE A 1 1477 ? 56.003  -11.293 11.671  1.00 248.06 ? 1477 PHE A O   1 
ATOM   11222 C  CB  . PHE A 1 1477 ? 53.247  -10.064 10.178  1.00 231.57 ? 1477 PHE A CB  1 
ATOM   11223 C  CG  . PHE A 1 1477 ? 53.167  -11.527 9.823   1.00 228.10 ? 1477 PHE A CG  1 
ATOM   11224 C  CD1 . PHE A 1 1477 ? 52.405  -12.397 10.580  1.00 226.80 ? 1477 PHE A CD1 1 
ATOM   11225 C  CD2 . PHE A 1 1477 ? 53.844  -12.028 8.733   1.00 226.09 ? 1477 PHE A CD2 1 
ATOM   11226 C  CE1 . PHE A 1 1477 ? 52.327  -13.736 10.255  1.00 223.50 ? 1477 PHE A CE1 1 
ATOM   11227 C  CE2 . PHE A 1 1477 ? 53.769  -13.365 8.415   1.00 223.42 ? 1477 PHE A CE2 1 
ATOM   11228 C  CZ  . PHE A 1 1477 ? 53.008  -14.217 9.177   1.00 221.65 ? 1477 PHE A CZ  1 
ATOM   11229 N  N   . ARG A 1 1478 ? 54.659  -10.121 13.015  1.00 168.24 ? 1478 ARG A N   1 
ATOM   11230 C  CA  . ARG A 1 1478 ? 55.222  -10.690 14.218  1.00 172.90 ? 1478 ARG A CA  1 
ATOM   11231 C  C   . ARG A 1 1478 ? 54.224  -11.685 14.814  1.00 169.37 ? 1478 ARG A C   1 
ATOM   11232 O  O   . ARG A 1 1478 ? 53.037  -11.672 14.466  1.00 158.91 ? 1478 ARG A O   1 
ATOM   11233 C  CB  . ARG A 1 1478 ? 55.578  -9.536  15.149  1.00 179.56 ? 1478 ARG A CB  1 
ATOM   11234 C  CG  . ARG A 1 1478 ? 56.085  -8.317  14.332  1.00 182.11 ? 1478 ARG A CG  1 
ATOM   11235 C  CD  . ARG A 1 1478 ? 56.380  -7.035  15.130  1.00 191.51 ? 1478 ARG A CD  1 
ATOM   11236 N  NE  . ARG A 1 1478 ? 55.199  -6.261  15.520  1.00 189.85 ? 1478 ARG A NE  1 
ATOM   11237 C  CZ  . ARG A 1 1478 ? 55.230  -5.016  16.004  1.00 194.00 ? 1478 ARG A CZ  1 
ATOM   11238 N  NH1 . ARG A 1 1478 ? 56.387  -4.371  16.149  1.00 201.47 ? 1478 ARG A NH1 1 
ATOM   11239 N  NH2 . ARG A 1 1478 ? 54.092  -4.412  16.340  1.00 191.22 ? 1478 ARG A NH2 1 
ATOM   11240 N  N   . ILE A 1 1479 ? 54.700  -12.572 15.682  1.00 210.98 ? 1479 ILE A N   1 
ATOM   11241 C  CA  . ILE A 1 1479 ? 53.848  -13.657 16.174  1.00 214.14 ? 1479 ILE A CA  1 
ATOM   11242 C  C   . ILE A 1 1479 ? 54.096  -14.070 17.639  1.00 225.15 ? 1479 ILE A C   1 
ATOM   11243 O  O   . ILE A 1 1479 ? 55.227  -14.043 18.126  1.00 233.19 ? 1479 ILE A O   1 
ATOM   11244 C  CB  . ILE A 1 1479 ? 53.939  -14.894 15.245  1.00 211.02 ? 1479 ILE A CB  1 
ATOM   11245 C  CG1 . ILE A 1 1479 ? 55.397  -15.247 14.960  1.00 216.85 ? 1479 ILE A CG1 1 
ATOM   11246 C  CG2 . ILE A 1 1479 ? 53.263  -14.610 13.934  1.00 206.11 ? 1479 ILE A CG2 1 
ATOM   11247 C  CD1 . ILE A 1 1479 ? 55.563  -16.434 14.062  1.00 212.34 ? 1479 ILE A CD1 1 
ATOM   11248 N  N   . PHE A 1 1480 ? 53.022  -14.462 18.324  1.00 252.40 ? 1480 PHE A N   1 
ATOM   11249 C  CA  . PHE A 1 1480 ? 53.079  -14.784 19.748  1.00 266.76 ? 1480 PHE A CA  1 
ATOM   11250 C  C   . PHE A 1 1480 ? 52.407  -16.105 20.095  1.00 258.51 ? 1480 PHE A C   1 
ATOM   11251 O  O   . PHE A 1 1480 ? 51.179  -16.200 20.150  1.00 253.14 ? 1480 PHE A O   1 
ATOM   11252 C  CB  . PHE A 1 1480 ? 52.439  -13.665 20.565  1.00 287.95 ? 1480 PHE A CB  1 
ATOM   11253 C  CG  . PHE A 1 1480 ? 51.398  -12.882 19.814  1.00 291.40 ? 1480 PHE A CG  1 
ATOM   11254 C  CD1 . PHE A 1 1480 ? 50.273  -13.509 19.304  1.00 284.57 ? 1480 PHE A CD1 1 
ATOM   11255 C  CD2 . PHE A 1 1480 ? 51.540  -11.512 19.634  1.00 296.32 ? 1480 PHE A CD2 1 
ATOM   11256 C  CE1 . PHE A 1 1480 ? 49.316  -12.787 18.618  1.00 278.40 ? 1480 PHE A CE1 1 
ATOM   11257 C  CE2 . PHE A 1 1480 ? 50.587  -10.783 18.953  1.00 289.60 ? 1480 PHE A CE2 1 
ATOM   11258 C  CZ  . PHE A 1 1480 ? 49.473  -11.421 18.443  1.00 281.04 ? 1480 PHE A CZ  1 
ATOM   11259 N  N   . GLU A 1 1481 ? 53.227  -17.114 20.357  1.00 234.45 ? 1481 GLU A N   1 
ATOM   11260 C  CA  . GLU A 1 1481 ? 52.724  -18.434 20.691  1.00 231.19 ? 1481 GLU A CA  1 
ATOM   11261 C  C   . GLU A 1 1481 ? 51.546  -18.312 21.641  1.00 229.86 ? 1481 GLU A C   1 
ATOM   11262 O  O   . GLU A 1 1481 ? 51.741  -18.039 22.813  1.00 236.86 ? 1481 GLU A O   1 
ATOM   11263 C  CB  . GLU A 1 1481 ? 53.825  -19.277 21.351  1.00 237.86 ? 1481 GLU A CB  1 
ATOM   11264 C  CG  . GLU A 1 1481 ? 55.036  -19.566 20.469  1.00 271.63 ? 1481 GLU A CG  1 
ATOM   11265 C  CD  . GLU A 1 1481 ? 55.959  -20.640 21.044  1.00 276.84 ? 1481 GLU A CD  1 
ATOM   11266 O  OE1 . GLU A 1 1481 ? 55.509  -21.458 21.880  1.00 278.67 ? 1481 GLU A OE1 1 
ATOM   11267 O  OE2 . GLU A 1 1481 ? 57.141  -20.670 20.644  1.00 279.08 ? 1481 GLU A OE2 1 
ATOM   11268 N  N   . LEU A 1 1482 ? 50.332  -18.506 21.139  1.00 175.99 ? 1482 LEU A N   1 
ATOM   11269 C  CA  . LEU A 1 1482 ? 49.143  -18.511 21.988  1.00 172.87 ? 1482 LEU A CA  1 
ATOM   11270 C  C   . LEU A 1 1482 ? 49.113  -19.726 22.923  1.00 172.72 ? 1482 LEU A C   1 
ATOM   11271 O  O   . LEU A 1 1482 ? 48.363  -19.732 23.892  1.00 174.69 ? 1482 LEU A O   1 
ATOM   11272 C  CB  . LEU A 1 1482 ? 47.851  -18.395 21.145  1.00 165.73 ? 1482 LEU A CB  1 
ATOM   11273 C  CG  . LEU A 1 1482 ? 46.393  -18.704 21.592  1.00 164.69 ? 1482 LEU A CG  1 
ATOM   11274 C  CD1 . LEU A 1 1482 ? 45.322  -18.000 20.717  1.00 157.81 ? 1482 LEU A CD1 1 
ATOM   11275 C  CD2 . LEU A 1 1482 ? 46.089  -20.210 21.654  1.00 163.31 ? 1482 LEU A CD2 1 
ATOM   11276 N  N   . PHE A 1 1483 ? 49.920  -20.748 22.642  1.00 209.62 ? 1483 PHE A N   1 
ATOM   11277 C  CA  . PHE A 1 1483 ? 50.194  -21.797 23.640  1.00 212.56 ? 1483 PHE A CA  1 
ATOM   11278 C  C   . PHE A 1 1483 ? 51.352  -22.753 23.330  1.00 217.74 ? 1483 PHE A C   1 
ATOM   11279 O  O   . PHE A 1 1483 ? 52.099  -22.578 22.368  1.00 217.24 ? 1483 PHE A O   1 
ATOM   11280 C  CB  . PHE A 1 1483 ? 48.944  -22.582 24.059  1.00 204.75 ? 1483 PHE A CB  1 
ATOM   11281 C  CG  . PHE A 1 1483 ? 48.202  -23.169 22.922  1.00 193.43 ? 1483 PHE A CG  1 
ATOM   11282 C  CD1 . PHE A 1 1483 ? 48.876  -23.552 21.775  1.00 189.62 ? 1483 PHE A CD1 1 
ATOM   11283 C  CD2 . PHE A 1 1483 ? 46.829  -23.338 22.987  1.00 187.32 ? 1483 PHE A CD2 1 
ATOM   11284 C  CE1 . PHE A 1 1483 ? 48.196  -24.090 20.699  1.00 178.95 ? 1483 PHE A CE1 1 
ATOM   11285 C  CE2 . PHE A 1 1483 ? 46.137  -23.872 21.926  1.00 177.72 ? 1483 PHE A CE2 1 
ATOM   11286 C  CZ  . PHE A 1 1483 ? 46.821  -24.252 20.776  1.00 173.52 ? 1483 PHE A CZ  1 
ATOM   11287 N  N   . GLU A 1 1484 ? 51.490  -23.760 24.184  1.00 276.74 ? 1484 GLU A N   1 
ATOM   11288 C  CA  . GLU A 1 1484 ? 52.690  -24.576 24.230  1.00 284.99 ? 1484 GLU A CA  1 
ATOM   11289 C  C   . GLU A 1 1484 ? 52.532  -25.797 23.351  1.00 279.19 ? 1484 GLU A C   1 
ATOM   11290 O  O   . GLU A 1 1484 ? 51.750  -26.700 23.643  1.00 278.22 ? 1484 GLU A O   1 
ATOM   11291 C  CB  . GLU A 1 1484 ? 53.009  -24.967 25.679  1.00 299.83 ? 1484 GLU A CB  1 
ATOM   11292 C  CG  . GLU A 1 1484 ? 53.309  -23.775 26.630  1.00 313.21 ? 1484 GLU A CG  1 
ATOM   11293 C  CD  . GLU A 1 1484 ? 52.060  -23.150 27.273  1.00 316.69 ? 1484 GLU A CD  1 
ATOM   11294 O  OE1 . GLU A 1 1484 ? 50.930  -23.539 26.902  1.00 311.96 ? 1484 GLU A OE1 1 
ATOM   11295 O  OE2 . GLU A 1 1484 ? 52.213  -22.266 28.152  1.00 323.04 ? 1484 GLU A OE2 1 
ATOM   11296 N  N   . VAL A 1 1485 ? 53.288  -25.806 22.265  1.00 231.63 ? 1485 VAL A N   1 
ATOM   11297 C  CA  . VAL A 1 1485 ? 53.134  -26.816 21.239  1.00 222.70 ? 1485 VAL A CA  1 
ATOM   11298 C  C   . VAL A 1 1485 ? 54.369  -27.696 21.193  1.00 224.77 ? 1485 VAL A C   1 
ATOM   11299 O  O   . VAL A 1 1485 ? 55.483  -27.188 21.124  1.00 227.87 ? 1485 VAL A O   1 
ATOM   11300 C  CB  . VAL A 1 1485 ? 52.921  -26.149 19.878  1.00 234.64 ? 1485 VAL A CB  1 
ATOM   11301 C  CG1 . VAL A 1 1485 ? 51.501  -25.596 19.781  1.00 228.16 ? 1485 VAL A CG1 1 
ATOM   11302 C  CG2 . VAL A 1 1485 ? 53.951  -25.041 19.670  1.00 239.10 ? 1485 VAL A CG2 1 
ATOM   11303 N  N   . GLY A 1 1486 ? 54.166  -29.011 21.226  1.00 233.13 ? 1486 GLY A N   1 
ATOM   11304 C  CA  . GLY A 1 1486 ? 55.258  -29.965 21.336  1.00 236.71 ? 1486 GLY A CA  1 
ATOM   11305 C  C   . GLY A 1 1486 ? 56.244  -29.924 20.191  1.00 233.74 ? 1486 GLY A C   1 
ATOM   11306 O  O   . GLY A 1 1486 ? 56.567  -28.858 19.677  1.00 235.94 ? 1486 GLY A O   1 
ATOM   11307 N  N   . PHE A 1 1487 ? 56.752  -31.084 19.802  1.00 262.88 ? 1487 PHE A N   1 
ATOM   11308 C  CA  . PHE A 1 1487 ? 57.505  -31.157 18.569  1.00 261.23 ? 1487 PHE A CA  1 
ATOM   11309 C  C   . PHE A 1 1487 ? 56.525  -30.721 17.503  1.00 249.57 ? 1487 PHE A C   1 
ATOM   11310 O  O   . PHE A 1 1487 ? 55.535  -31.411 17.278  1.00 243.10 ? 1487 PHE A O   1 
ATOM   11311 C  CB  . PHE A 1 1487 ? 57.947  -32.590 18.277  1.00 265.85 ? 1487 PHE A CB  1 
ATOM   11312 C  CG  . PHE A 1 1487 ? 57.661  -33.562 19.389  1.00 272.51 ? 1487 PHE A CG  1 
ATOM   11313 C  CD1 . PHE A 1 1487 ? 58.662  -34.391 19.879  1.00 280.17 ? 1487 PHE A CD1 1 
ATOM   11314 C  CD2 . PHE A 1 1487 ? 56.391  -33.659 19.937  1.00 270.51 ? 1487 PHE A CD2 1 
ATOM   11315 C  CE1 . PHE A 1 1487 ? 58.406  -35.290 20.899  1.00 284.39 ? 1487 PHE A CE1 1 
ATOM   11316 C  CE2 . PHE A 1 1487 ? 56.131  -34.551 20.957  1.00 274.76 ? 1487 PHE A CE2 1 
ATOM   11317 C  CZ  . PHE A 1 1487 ? 57.141  -35.369 21.439  1.00 281.57 ? 1487 PHE A CZ  1 
ATOM   11318 N  N   . LEU A 1 1488 ? 56.764  -29.582 16.857  1.00 255.49 ? 1488 LEU A N   1 
ATOM   11319 C  CA  . LEU A 1 1488 ? 55.827  -29.124 15.826  1.00 246.30 ? 1488 LEU A CA  1 
ATOM   11320 C  C   . LEU A 1 1488 ? 56.216  -29.508 14.398  1.00 243.37 ? 1488 LEU A C   1 
ATOM   11321 O  O   . LEU A 1 1488 ? 57.394  -29.446 14.044  1.00 248.06 ? 1488 LEU A O   1 
ATOM   11322 C  CB  . LEU A 1 1488 ? 55.553  -27.614 15.926  1.00 244.98 ? 1488 LEU A CB  1 
ATOM   11323 C  CG  . LEU A 1 1488 ? 56.484  -26.518 15.398  1.00 246.95 ? 1488 LEU A CG  1 
ATOM   11324 C  CD1 . LEU A 1 1488 ? 56.916  -26.708 13.953  1.00 243.71 ? 1488 LEU A CD1 1 
ATOM   11325 C  CD2 . LEU A 1 1488 ? 55.770  -25.193 15.546  1.00 244.75 ? 1488 LEU A CD2 1 
ATOM   11326 N  N   . SER A 1 1489 ? 55.227  -29.897 13.587  1.00 187.22 ? 1489 SER A N   1 
ATOM   11327 C  CA  . SER A 1 1489 ? 55.448  -30.165 12.163  1.00 179.53 ? 1489 SER A CA  1 
ATOM   11328 C  C   . SER A 1 1489 ? 55.215  -28.888 11.376  1.00 173.81 ? 1489 SER A C   1 
ATOM   11329 O  O   . SER A 1 1489 ? 54.128  -28.323 11.447  1.00 171.63 ? 1489 SER A O   1 
ATOM   11330 C  CB  . SER A 1 1489 ? 54.521  -31.271 11.668  1.00 169.28 ? 1489 SER A CB  1 
ATOM   11331 O  OG  . SER A 1 1489 ? 53.262  -30.742 11.307  1.00 161.98 ? 1489 SER A OG  1 
ATOM   11332 N  N   . PRO A 1 1490 ? 56.229  -28.446 10.607  1.00 196.18 ? 1490 PRO A N   1 
ATOM   11333 C  CA  . PRO A 1 1490 ? 56.292  -27.089 10.052  1.00 192.60 ? 1490 PRO A CA  1 
ATOM   11334 C  C   . PRO A 1 1490 ? 54.983  -26.697 9.395   1.00 187.23 ? 1490 PRO A C   1 
ATOM   11335 O  O   . PRO A 1 1490 ? 54.134  -27.558 9.164   1.00 180.24 ? 1490 PRO A O   1 
ATOM   11336 C  CB  . PRO A 1 1490 ? 57.378  -27.191 8.978   1.00 193.04 ? 1490 PRO A CB  1 
ATOM   11337 C  CG  . PRO A 1 1490 ? 58.170  -28.371 9.320   1.00 198.14 ? 1490 PRO A CG  1 
ATOM   11338 C  CD  . PRO A 1 1490 ? 57.249  -29.326 10.014  1.00 195.92 ? 1490 PRO A CD  1 
ATOM   11339 N  N   . ALA A 1 1491 ? 54.810  -25.410 9.122   1.00 236.39 ? 1491 ALA A N   1 
ATOM   11340 C  CA  . ALA A 1 1491 ? 53.687  -24.958 8.319   1.00 230.47 ? 1491 ALA A CA  1 
ATOM   11341 C  C   . ALA A 1 1491 ? 54.153  -24.860 6.877   1.00 231.54 ? 1491 ALA A C   1 
ATOM   11342 O  O   . ALA A 1 1491 ? 55.097  -25.539 6.479   1.00 231.81 ? 1491 ALA A O   1 
ATOM   11343 C  CB  . ALA A 1 1491 ? 53.150  -23.625 8.821   1.00 228.73 ? 1491 ALA A CB  1 
ATOM   11344 N  N   . THR A 1 1492 ? 53.510  -24.009 6.093   1.00 175.44 ? 1492 THR A N   1 
ATOM   11345 C  CA  . THR A 1 1492 ? 53.712  -24.065 4.661   1.00 171.40 ? 1492 THR A CA  1 
ATOM   11346 C  C   . THR A 1 1492 ? 53.540  -22.698 4.033   1.00 173.04 ? 1492 THR A C   1 
ATOM   11347 O  O   . THR A 1 1492 ? 52.443  -22.151 4.007   1.00 169.99 ? 1492 THR A O   1 
ATOM   11348 C  CB  . THR A 1 1492 ? 52.732  -25.081 4.046   1.00 160.37 ? 1492 THR A CB  1 
ATOM   11349 O  OG1 . THR A 1 1492 ? 51.385  -24.769 4.438   1.00 152.45 ? 1492 THR A OG1 1 
ATOM   11350 C  CG2 . THR A 1 1492 ? 53.071  -26.480 4.536   1.00 157.73 ? 1492 THR A CG2 1 
ATOM   11351 N  N   . PHE A 1 1493 ? 54.630  -22.122 3.553   1.00 189.83 ? 1493 PHE A N   1 
ATOM   11352 C  CA  . PHE A 1 1493 ? 54.501  -20.858 2.866   1.00 186.28 ? 1493 PHE A CA  1 
ATOM   11353 C  C   . PHE A 1 1493 ? 54.299  -21.156 1.414   1.00 184.79 ? 1493 PHE A C   1 
ATOM   11354 O  O   . PHE A 1 1493 ? 55.207  -21.694 0.777   1.00 186.59 ? 1493 PHE A O   1 
ATOM   11355 C  CB  . PHE A 1 1493 ? 55.743  -20.005 3.021   1.00 186.38 ? 1493 PHE A CB  1 
ATOM   11356 C  CG  . PHE A 1 1493 ? 55.786  -18.820 2.087   1.00 180.07 ? 1493 PHE A CG  1 
ATOM   11357 C  CD1 . PHE A 1 1493 ? 54.651  -18.045 1.862   1.00 173.21 ? 1493 PHE A CD1 1 
ATOM   11358 C  CD2 . PHE A 1 1493 ? 56.970  -18.471 1.444   1.00 182.65 ? 1493 PHE A CD2 1 
ATOM   11359 C  CE1 . PHE A 1 1493 ? 54.698  -16.946 1.004   1.00 172.68 ? 1493 PHE A CE1 1 
ATOM   11360 C  CE2 . PHE A 1 1493 ? 57.030  -17.375 0.594   1.00 180.95 ? 1493 PHE A CE2 1 
ATOM   11361 C  CZ  . PHE A 1 1493 ? 55.893  -16.612 0.371   1.00 176.58 ? 1493 PHE A CZ  1 
ATOM   11362 N  N   . THR A 1 1494 ? 53.114  -20.805 0.899   1.00 154.35 ? 1494 THR A N   1 
ATOM   11363 C  CA  . THR A 1 1494 ? 52.778  -20.968 -0.528  1.00 148.87 ? 1494 THR A CA  1 
ATOM   11364 C  C   . THR A 1 1494 ? 52.502  -19.615 -1.272  1.00 158.19 ? 1494 THR A C   1 
ATOM   11365 O  O   . THR A 1 1494 ? 52.090  -18.616 -0.664  1.00 151.90 ? 1494 THR A O   1 
ATOM   11366 C  CB  . THR A 1 1494 ? 51.691  -22.106 -0.742  1.00 145.28 ? 1494 THR A CB  1 
ATOM   11367 O  OG1 . THR A 1 1494 ? 51.335  -22.224 -2.121  1.00 142.26 ? 1494 THR A OG1 1 
ATOM   11368 C  CG2 . THR A 1 1494 ? 50.451  -21.905 0.120   1.00 144.20 ? 1494 THR A CG2 1 
ATOM   11369 N  N   . VAL A 1 1495 ? 52.808  -19.574 -2.572  1.00 166.86 ? 1495 VAL A N   1 
ATOM   11370 C  CA  . VAL A 1 1495 ? 52.601  -18.368 -3.396  1.00 171.50 ? 1495 VAL A CA  1 
ATOM   11371 C  C   . VAL A 1 1495 ? 52.206  -18.666 -4.869  1.00 170.00 ? 1495 VAL A C   1 
ATOM   11372 O  O   . VAL A 1 1495 ? 53.022  -19.167 -5.673  1.00 175.38 ? 1495 VAL A O   1 
ATOM   11373 C  CB  . VAL A 1 1495 ? 53.834  -17.425 -3.388  1.00 161.94 ? 1495 VAL A CB  1 
ATOM   11374 C  CG1 . VAL A 1 1495 ? 54.976  -18.025 -4.192  1.00 173.41 ? 1495 VAL A CG1 1 
ATOM   11375 C  CG2 . VAL A 1 1495 ? 53.457  -16.046 -3.923  1.00 161.82 ? 1495 VAL A CG2 1 
ATOM   11376 N  N   . TYR A 1 1496 ? 50.956  -18.331 -5.215  1.00 189.85 ? 1496 TYR A N   1 
ATOM   11377 C  CA  . TYR A 1 1496 ? 50.418  -18.546 -6.563  1.00 183.85 ? 1496 TYR A CA  1 
ATOM   11378 C  C   . TYR A 1 1496 ? 49.646  -17.350 -7.128  1.00 181.91 ? 1496 TYR A C   1 
ATOM   11379 O  O   . TYR A 1 1496 ? 49.097  -16.533 -6.383  1.00 181.37 ? 1496 TYR A O   1 
ATOM   11380 C  CB  . TYR A 1 1496 ? 49.556  -19.813 -6.620  1.00 177.27 ? 1496 TYR A CB  1 
ATOM   11381 C  CG  . TYR A 1 1496 ? 48.266  -19.817 -5.804  1.00 175.76 ? 1496 TYR A CG  1 
ATOM   11382 C  CD1 . TYR A 1 1496 ? 47.637  -18.642 -5.428  1.00 174.79 ? 1496 TYR A CD1 1 
ATOM   11383 C  CD2 . TYR A 1 1496 ? 47.659  -21.022 -5.448  1.00 173.08 ? 1496 TYR A CD2 1 
ATOM   11384 C  CE1 . TYR A 1 1496 ? 46.454  -18.671 -4.707  1.00 171.12 ? 1496 TYR A CE1 1 
ATOM   11385 C  CE2 . TYR A 1 1496 ? 46.478  -21.059 -4.731  1.00 169.93 ? 1496 TYR A CE2 1 
ATOM   11386 C  CZ  . TYR A 1 1496 ? 45.883  -19.882 -4.362  1.00 169.31 ? 1496 TYR A CZ  1 
ATOM   11387 O  OH  . TYR A 1 1496 ? 44.714  -19.917 -3.646  1.00 166.65 ? 1496 TYR A OH  1 
ATOM   11388 N  N   . GLU A 1 1497 ? 49.601  -17.276 -8.456  1.00 208.30 ? 1497 GLU A N   1 
ATOM   11389 C  CA  . GLU A 1 1497 ? 48.981  -16.163 -9.188  1.00 204.66 ? 1497 GLU A CA  1 
ATOM   11390 C  C   . GLU A 1 1497 ? 47.466  -16.309 -9.367  1.00 198.00 ? 1497 GLU A C   1 
ATOM   11391 O  O   . GLU A 1 1497 ? 46.996  -17.280 -9.971  1.00 193.54 ? 1497 GLU A O   1 
ATOM   11392 C  CB  . GLU A 1 1497 ? 49.637  -16.048 -10.557 1.00 203.66 ? 1497 GLU A CB  1 
ATOM   11393 C  CG  . GLU A 1 1497 ? 49.472  -14.715 -11.222 1.00 202.20 ? 1497 GLU A CG  1 
ATOM   11394 C  CD  . GLU A 1 1497 ? 50.354  -14.602 -12.444 1.00 203.47 ? 1497 GLU A CD  1 
ATOM   11395 O  OE1 . GLU A 1 1497 ? 51.050  -15.588 -12.776 1.00 202.12 ? 1497 GLU A OE1 1 
ATOM   11396 O  OE2 . GLU A 1 1497 ? 50.353  -13.531 -13.075 1.00 205.61 ? 1497 GLU A OE2 1 
ATOM   11397 N  N   . TYR A 1 1498 ? 46.709  -15.327 -8.878  1.00 200.34 ? 1498 TYR A N   1 
ATOM   11398 C  CA  . TYR A 1 1498 ? 45.264  -15.496 -8.747  1.00 197.50 ? 1498 TYR A CA  1 
ATOM   11399 C  C   . TYR A 1 1498 ? 44.700  -16.103 -10.002 1.00 193.34 ? 1498 TYR A C   1 
ATOM   11400 O  O   . TYR A 1 1498 ? 44.005  -17.114 -9.963  1.00 189.46 ? 1498 TYR A O   1 
ATOM   11401 C  CB  . TYR A 1 1498 ? 44.537  -14.180 -8.439  1.00 199.04 ? 1498 TYR A CB  1 
ATOM   11402 C  CG  . TYR A 1 1498 ? 43.115  -14.392 -7.936  1.00 197.60 ? 1498 TYR A CG  1 
ATOM   11403 C  CD1 . TYR A 1 1498 ? 42.873  -15.160 -6.809  1.00 200.42 ? 1498 TYR A CD1 1 
ATOM   11404 C  CD2 . TYR A 1 1498 ? 42.023  -13.831 -8.581  1.00 194.67 ? 1498 TYR A CD2 1 
ATOM   11405 C  CE1 . TYR A 1 1498 ? 41.599  -15.362 -6.335  1.00 198.24 ? 1498 TYR A CE1 1 
ATOM   11406 C  CE2 . TYR A 1 1498 ? 40.741  -14.028 -8.108  1.00 192.85 ? 1498 TYR A CE2 1 
ATOM   11407 C  CZ  . TYR A 1 1498 ? 40.540  -14.801 -6.986  1.00 194.99 ? 1498 TYR A CZ  1 
ATOM   11408 O  OH  . TYR A 1 1498 ? 39.283  -15.022 -6.491  1.00 194.18 ? 1498 TYR A OH  1 
ATOM   11409 N  N   . HIS A 1 1499 ? 45.013  -15.502 -11.133 1.00 167.25 ? 1499 HIS A N   1 
ATOM   11410 C  CA  . HIS A 1 1499 ? 44.368  -15.964 -12.333 1.00 163.16 ? 1499 HIS A CA  1 
ATOM   11411 C  C   . HIS A 1 1499 ? 44.941  -17.250 -12.899 1.00 167.71 ? 1499 HIS A C   1 
ATOM   11412 O  O   . HIS A 1 1499 ? 44.235  -17.967 -13.581 1.00 168.25 ? 1499 HIS A O   1 
ATOM   11413 C  CB  . HIS A 1 1499 ? 44.205  -14.841 -13.351 1.00 157.87 ? 1499 HIS A CB  1 
ATOM   11414 C  CG  . HIS A 1 1499 ? 43.119  -13.886 -12.976 1.00 151.87 ? 1499 HIS A CG  1 
ATOM   11415 N  ND1 . HIS A 1 1499 ? 43.254  -12.517 -13.069 1.00 153.47 ? 1499 HIS A ND1 1 
ATOM   11416 C  CD2 . HIS A 1 1499 ? 41.888  -14.105 -12.455 1.00 148.92 ? 1499 HIS A CD2 1 
ATOM   11417 C  CE1 . HIS A 1 1499 ? 42.146  -11.936 -12.646 1.00 152.46 ? 1499 HIS A CE1 1 
ATOM   11418 N  NE2 . HIS A 1 1499 ? 41.301  -12.879 -12.266 1.00 149.33 ? 1499 HIS A NE2 1 
ATOM   11419 N  N   . ARG A 1 1500 ? 46.186  -17.583 -12.580 1.00 174.58 ? 1500 ARG A N   1 
ATOM   11420 C  CA  . ARG A 1 1500 ? 46.742  -18.855 -13.057 1.00 174.12 ? 1500 ARG A CA  1 
ATOM   11421 C  C   . ARG A 1 1500 ? 47.385  -19.700 -11.955 1.00 174.32 ? 1500 ARG A C   1 
ATOM   11422 O  O   . ARG A 1 1500 ? 48.604  -19.659 -11.740 1.00 180.03 ? 1500 ARG A O   1 
ATOM   11423 C  CB  . ARG A 1 1500 ? 47.695  -18.640 -14.233 1.00 178.75 ? 1500 ARG A CB  1 
ATOM   11424 C  CG  . ARG A 1 1500 ? 47.884  -17.183 -14.572 1.00 181.64 ? 1500 ARG A CG  1 
ATOM   11425 C  CD  . ARG A 1 1500 ? 49.333  -16.879 -14.732 1.00 189.22 ? 1500 ARG A CD  1 
ATOM   11426 N  NE  . ARG A 1 1500 ? 49.727  -16.959 -16.122 1.00 191.79 ? 1500 ARG A NE  1 
ATOM   11427 C  CZ  . ARG A 1 1500 ? 50.965  -16.777 -16.550 1.00 196.81 ? 1500 ARG A CZ  1 
ATOM   11428 N  NH1 . ARG A 1 1500 ? 51.934  -16.509 -15.687 1.00 199.37 ? 1500 ARG A NH1 1 
ATOM   11429 N  NH2 . ARG A 1 1500 ? 51.226  -16.871 -17.845 1.00 199.09 ? 1500 ARG A NH2 1 
ATOM   11430 N  N   . PRO A 1 1501 ? 46.538  -20.476 -11.262 1.00 161.84 ? 1501 PRO A N   1 
ATOM   11431 C  CA  . PRO A 1 1501 ? 46.801  -21.416 -10.163 1.00 163.52 ? 1501 PRO A CA  1 
ATOM   11432 C  C   . PRO A 1 1501 ? 47.895  -22.418 -10.526 1.00 169.77 ? 1501 PRO A C   1 
ATOM   11433 O  O   . PRO A 1 1501 ? 48.258  -23.316 -9.771  1.00 170.57 ? 1501 PRO A O   1 
ATOM   11434 C  CB  . PRO A 1 1501 ? 45.466  -22.144 -10.009 1.00 158.66 ? 1501 PRO A CB  1 
ATOM   11435 C  CG  . PRO A 1 1501 ? 44.435  -21.189 -10.543 1.00 155.59 ? 1501 PRO A CG  1 
ATOM   11436 C  CD  . PRO A 1 1501 ? 45.104  -20.393 -11.603 1.00 156.76 ? 1501 PRO A CD  1 
ATOM   11437 N  N   . ASP A 1 1502 ? 48.418  -22.241 -11.722 1.00 174.16 ? 1502 ASP A N   1 
ATOM   11438 C  CA  . ASP A 1 1502 ? 49.390  -23.145 -12.277 1.00 180.63 ? 1502 ASP A CA  1 
ATOM   11439 C  C   . ASP A 1 1502 ? 50.754  -22.806 -11.721 1.00 189.93 ? 1502 ASP A C   1 
ATOM   11440 O  O   . ASP A 1 1502 ? 51.704  -23.579 -11.844 1.00 195.03 ? 1502 ASP A O   1 
ATOM   11441 C  CB  . ASP A 1 1502 ? 49.383  -22.983 -13.797 1.00 180.42 ? 1502 ASP A CB  1 
ATOM   11442 C  CG  . ASP A 1 1502 ? 47.976  -22.778 -14.351 1.00 173.40 ? 1502 ASP A CG  1 
ATOM   11443 O  OD1 . ASP A 1 1502 ? 47.033  -23.444 -13.855 1.00 167.05 ? 1502 ASP A OD1 1 
ATOM   11444 O  OD2 . ASP A 1 1502 ? 47.814  -21.957 -15.282 1.00 173.60 ? 1502 ASP A OD2 1 
ATOM   11445 N  N   . LYS A 1 1503 ? 50.846  -21.634 -11.110 1.00 187.85 ? 1503 LYS A N   1 
ATOM   11446 C  CA  . LYS A 1 1503 ? 52.141  -21.069 -10.725 1.00 197.83 ? 1503 LYS A CA  1 
ATOM   11447 C  C   . LYS A 1 1503 ? 52.562  -21.332 -9.253  1.00 185.95 ? 1503 LYS A C   1 
ATOM   11448 O  O   . LYS A 1 1503 ? 53.344  -20.575 -8.656  1.00 184.73 ? 1503 LYS A O   1 
ATOM   11449 C  CB  . LYS A 1 1503 ? 52.148  -19.568 -11.044 1.00 201.86 ? 1503 LYS A CB  1 
ATOM   11450 C  CG  . LYS A 1 1503 ? 52.227  -19.227 -12.534 1.00 205.43 ? 1503 LYS A CG  1 
ATOM   11451 C  CD  . LYS A 1 1503 ? 51.965  -20.435 -13.413 1.00 206.21 ? 1503 LYS A CD  1 
ATOM   11452 C  CE  . LYS A 1 1503 ? 53.048  -20.605 -14.480 1.00 213.57 ? 1503 LYS A CE  1 
ATOM   11453 N  NZ  . LYS A 1 1503 ? 52.874  -21.842 -15.302 1.00 215.26 ? 1503 LYS A NZ  1 
ATOM   11454 N  N   . GLN A 1 1504 ? 52.055  -22.429 -8.696  1.00 192.24 ? 1504 GLN A N   1 
ATOM   11455 C  CA  . GLN A 1 1504 ? 52.218  -22.746 -7.281  1.00 185.84 ? 1504 GLN A CA  1 
ATOM   11456 C  C   . GLN A 1 1504 ? 53.595  -23.192 -6.863  1.00 191.80 ? 1504 GLN A C   1 
ATOM   11457 O  O   . GLN A 1 1504 ? 53.885  -24.386 -6.898  1.00 173.39 ? 1504 GLN A O   1 
ATOM   11458 C  CB  . GLN A 1 1504 ? 51.226  -23.830 -6.863  1.00 181.82 ? 1504 GLN A CB  1 
ATOM   11459 C  CG  . GLN A 1 1504 ? 50.078  -23.288 -6.019  1.00 221.43 ? 1504 GLN A CG  1 
ATOM   11460 C  CD  . GLN A 1 1504 ? 48.904  -24.255 -5.892  1.00 195.77 ? 1504 GLN A CD  1 
ATOM   11461 O  OE1 . GLN A 1 1504 ? 47.814  -23.887 -5.408  1.00 187.05 ? 1504 GLN A OE1 1 
ATOM   11462 N  NE2 . GLN A 1 1504 ? 49.119  -25.499 -6.331  1.00 198.59 ? 1504 GLN A NE2 1 
ATOM   11463 N  N   . CYS A 1 1505 ? 54.425  -22.233 -6.451  1.00 164.66 ? 1505 CYS A N   1 
ATOM   11464 C  CA  . CYS A 1 1505 ? 55.626  -22.538 -5.662  1.00 171.87 ? 1505 CYS A CA  1 
ATOM   11465 C  C   . CYS A 1 1505 ? 55.339  -22.585 -4.161  1.00 174.39 ? 1505 CYS A C   1 
ATOM   11466 O  O   . CYS A 1 1505 ? 55.208  -21.554 -3.499  1.00 170.89 ? 1505 CYS A O   1 
ATOM   11467 C  CB  . CYS A 1 1505 ? 56.772  -21.563 -5.929  1.00 177.25 ? 1505 CYS A CB  1 
ATOM   11468 S  SG  . CYS A 1 1505 ? 58.369  -22.225 -5.355  1.00 235.83 ? 1505 CYS A SG  1 
ATOM   11469 N  N   . THR A 1 1506 ? 55.272  -23.810 -3.653  1.00 169.09 ? 1506 THR A N   1 
ATOM   11470 C  CA  . THR A 1 1506 ? 54.896  -24.104 -2.289  1.00 172.71 ? 1506 THR A CA  1 
ATOM   11471 C  C   . THR A 1 1506 ? 56.160  -24.565 -1.580  1.00 180.30 ? 1506 THR A C   1 
ATOM   11472 O  O   . THR A 1 1506 ? 57.025  -25.201 -2.205  1.00 181.48 ? 1506 THR A O   1 
ATOM   11473 C  CB  . THR A 1 1506 ? 53.835  -25.236 -2.264  1.00 172.09 ? 1506 THR A CB  1 
ATOM   11474 O  OG1 . THR A 1 1506 ? 52.808  -24.959 -3.225  1.00 170.27 ? 1506 THR A OG1 1 
ATOM   11475 C  CG2 . THR A 1 1506 ? 53.208  -25.389 -0.902  1.00 171.93 ? 1506 THR A CG2 1 
ATOM   11476 N  N   . MET A 1 1507 ? 56.258  -24.239 -0.284  1.00 208.85 ? 1507 MET A N   1 
ATOM   11477 C  CA  . MET A 1 1507 ? 57.438  -24.547 0.536   1.00 212.21 ? 1507 MET A CA  1 
ATOM   11478 C  C   . MET A 1 1507 ? 57.220  -24.615 2.053   1.00 211.35 ? 1507 MET A C   1 
ATOM   11479 O  O   . MET A 1 1507 ? 56.630  -23.718 2.659   1.00 206.97 ? 1507 MET A O   1 
ATOM   11480 C  CB  . MET A 1 1507 ? 58.532  -23.534 0.278   1.00 214.97 ? 1507 MET A CB  1 
ATOM   11481 C  CG  . MET A 1 1507 ? 59.701  -23.704 1.201   1.00 222.16 ? 1507 MET A CG  1 
ATOM   11482 S  SD  . MET A 1 1507 ? 60.633  -22.178 1.210   1.00 216.02 ? 1507 MET A SD  1 
ATOM   11483 C  CE  . MET A 1 1507 ? 59.340  -21.036 0.694   1.00 206.59 ? 1507 MET A CE  1 
ATOM   11484 N  N   . PHE A 1 1508 ? 57.736  -25.688 2.647   1.00 222.90 ? 1508 PHE A N   1 
ATOM   11485 C  CA  . PHE A 1 1508 ? 57.707  -25.897 4.090   1.00 229.01 ? 1508 PHE A CA  1 
ATOM   11486 C  C   . PHE A 1 1508 ? 58.585  -24.872 4.818   1.00 245.10 ? 1508 PHE A C   1 
ATOM   11487 O  O   . PHE A 1 1508 ? 59.467  -24.274 4.198   1.00 253.39 ? 1508 PHE A O   1 
ATOM   11488 C  CB  . PHE A 1 1508 ? 58.237  -27.295 4.419   1.00 225.59 ? 1508 PHE A CB  1 
ATOM   11489 C  CG  . PHE A 1 1508 ? 57.229  -28.382 4.260   1.00 213.02 ? 1508 PHE A CG  1 
ATOM   11490 C  CD1 . PHE A 1 1508 ? 56.001  -28.298 4.896   1.00 210.45 ? 1508 PHE A CD1 1 
ATOM   11491 C  CD2 . PHE A 1 1508 ? 57.516  -29.504 3.504   1.00 209.15 ? 1508 PHE A CD2 1 
ATOM   11492 C  CE1 . PHE A 1 1508 ? 55.062  -29.304 4.761   1.00 205.53 ? 1508 PHE A CE1 1 
ATOM   11493 C  CE2 . PHE A 1 1508 ? 56.584  -30.512 3.364   1.00 204.86 ? 1508 PHE A CE2 1 
ATOM   11494 C  CZ  . PHE A 1 1508 ? 55.353  -30.413 3.993   1.00 202.60 ? 1508 PHE A CZ  1 
ATOM   11495 N  N   . TYR A 1 1509 ? 58.358  -24.686 6.126   1.00 194.52 ? 1509 TYR A N   1 
ATOM   11496 C  CA  . TYR A 1 1509 ? 59.283  -23.941 7.005   1.00 199.00 ? 1509 TYR A CA  1 
ATOM   11497 C  C   . TYR A 1 1509 ? 58.847  -24.124 8.458   1.00 204.73 ? 1509 TYR A C   1 
ATOM   11498 O  O   . TYR A 1 1509 ? 57.702  -24.501 8.718   1.00 202.27 ? 1509 TYR A O   1 
ATOM   11499 C  CB  . TYR A 1 1509 ? 59.303  -22.456 6.661   1.00 191.57 ? 1509 TYR A CB  1 
ATOM   11500 C  CG  . TYR A 1 1509 ? 58.109  -21.757 7.219   1.00 184.49 ? 1509 TYR A CG  1 
ATOM   11501 C  CD1 . TYR A 1 1509 ? 58.199  -20.472 7.707   1.00 186.30 ? 1509 TYR A CD1 1 
ATOM   11502 C  CD2 . TYR A 1 1509 ? 56.880  -22.407 7.296   1.00 179.46 ? 1509 TYR A CD2 1 
ATOM   11503 C  CE1 . TYR A 1 1509 ? 57.080  -19.826 8.248   1.00 184.56 ? 1509 TYR A CE1 1 
ATOM   11504 C  CE2 . TYR A 1 1509 ? 55.753  -21.784 7.838   1.00 177.12 ? 1509 TYR A CE2 1 
ATOM   11505 C  CZ  . TYR A 1 1509 ? 55.849  -20.481 8.318   1.00 180.00 ? 1509 TYR A CZ  1 
ATOM   11506 O  OH  . TYR A 1 1509 ? 54.739  -19.828 8.865   1.00 177.48 ? 1509 TYR A OH  1 
ATOM   11507 N  N   . SER A 1 1510 ? 59.748  -23.864 9.404   1.00 248.81 ? 1510 SER A N   1 
ATOM   11508 C  CA  . SER A 1 1510 ? 59.402  -23.995 10.822  1.00 250.87 ? 1510 SER A CA  1 
ATOM   11509 C  C   . SER A 1 1510 ? 59.772  -22.780 11.668  1.00 258.15 ? 1510 SER A C   1 
ATOM   11510 O  O   . SER A 1 1510 ? 60.830  -22.166 11.504  1.00 260.72 ? 1510 SER A O   1 
ATOM   11511 C  CB  . SER A 1 1510 ? 59.985  -25.271 11.434  1.00 254.24 ? 1510 SER A CB  1 
ATOM   11512 O  OG  . SER A 1 1510 ? 59.366  -25.561 12.681  1.00 254.02 ? 1510 SER A OG  1 
ATOM   11513 N  N   . THR A 1 1511 ? 58.877  -22.472 12.596  1.00 193.00 ? 1511 THR A N   1 
ATOM   11514 C  CA  . THR A 1 1511 ? 58.867  -21.210 13.309  1.00 197.72 ? 1511 THR A CA  1 
ATOM   11515 C  C   . THR A 1 1511 ? 59.745  -21.313 14.537  1.00 214.58 ? 1511 THR A C   1 
ATOM   11516 O  O   . THR A 1 1511 ? 59.616  -20.538 15.474  1.00 219.95 ? 1511 THR A O   1 
ATOM   11517 C  CB  . THR A 1 1511 ? 57.425  -20.862 13.723  1.00 188.42 ? 1511 THR A CB  1 
ATOM   11518 O  OG1 . THR A 1 1511 ? 57.252  -19.441 13.802  1.00 189.16 ? 1511 THR A OG1 1 
ATOM   11519 C  CG2 . THR A 1 1511 ? 57.055  -21.542 15.050  1.00 189.23 ? 1511 THR A CG2 1 
ATOM   11520 N  N   . SER A 1 1512 ? 60.649  -22.276 14.531  1.00 248.79 ? 1512 SER A N   1 
ATOM   11521 C  CA  . SER A 1 1512 ? 61.484  -22.484 15.694  1.00 265.75 ? 1512 SER A CA  1 
ATOM   11522 C  C   . SER A 1 1512 ? 62.710  -23.278 15.334  1.00 279.35 ? 1512 SER A C   1 
ATOM   11523 O  O   . SER A 1 1512 ? 62.660  -24.189 14.511  1.00 276.06 ? 1512 SER A O   1 
ATOM   11524 C  CB  . SER A 1 1512 ? 60.713  -23.233 16.773  1.00 265.25 ? 1512 SER A CB  1 
ATOM   11525 O  OG  . SER A 1 1512 ? 60.528  -24.583 16.392  1.00 262.01 ? 1512 SER A OG  1 
ATOM   11526 N  N   . ASN A 1 1513 ? 63.814  -22.930 15.973  1.00 289.63 ? 1513 ASN A N   1 
ATOM   11527 C  CA  . ASN A 1 1513 ? 65.079  -23.581 15.713  1.00 304.35 ? 1513 ASN A CA  1 
ATOM   11528 C  C   . ASN A 1 1513 ? 65.263  -24.779 16.637  1.00 314.58 ? 1513 ASN A C   1 
ATOM   11529 O  O   . ASN A 1 1513 ? 66.231  -25.533 16.506  1.00 320.39 ? 1513 ASN A O   1 
ATOM   11530 C  CB  . ASN A 1 1513 ? 66.198  -22.562 15.892  1.00 314.51 ? 1513 ASN A CB  1 
ATOM   11531 C  CG  . ASN A 1 1513 ? 65.791  -21.176 15.414  1.00 314.66 ? 1513 ASN A CG  1 
ATOM   11532 O  OD1 . ASN A 1 1513 ? 65.127  -21.030 14.386  1.00 307.94 ? 1513 ASN A OD1 1 
ATOM   11533 N  ND2 . ASN A 1 1513 ? 66.180  -20.155 16.163  1.00 321.93 ? 1513 ASN A ND2 1 
ATOM   11534 N  N   . ILE A 1 1514 ? 64.314  -24.955 17.557  1.00 306.26 ? 1514 ILE A N   1 
ATOM   11535 C  CA  . ILE A 1 1514 ? 64.401  -25.999 18.581  1.00 312.26 ? 1514 ILE A CA  1 
ATOM   11536 C  C   . ILE A 1 1514 ? 64.486  -27.408 17.974  1.00 310.53 ? 1514 ILE A C   1 
ATOM   11537 O  O   . ILE A 1 1514 ? 63.597  -27.846 17.239  1.00 303.72 ? 1514 ILE A O   1 
ATOM   11538 C  CB  . ILE A 1 1514 ? 63.226  -25.923 19.605  1.00 324.29 ? 1514 ILE A CB  1 
ATOM   11539 C  CG1 . ILE A 1 1514 ? 62.976  -24.480 20.059  1.00 323.87 ? 1514 ILE A CG1 1 
ATOM   11540 C  CG2 . ILE A 1 1514 ? 63.505  -26.810 20.815  1.00 331.36 ? 1514 ILE A CG2 1 
ATOM   11541 C  CD1 . ILE A 1 1514 ? 61.864  -24.341 21.092  1.00 321.47 ? 1514 ILE A CD1 1 
ATOM   11542 N  N   . SER B 2 1    ? -16.302 -10.706 8.076   1.00 400.36 ? 129  SER X N   1 
ATOM   11543 C  CA  . SER B 2 1    ? -15.783 -10.049 9.270   1.00 399.81 ? 129  SER X CA  1 
ATOM   11544 C  C   . SER B 2 1    ? -15.339 -8.621  8.963   1.00 401.25 ? 129  SER X C   1 
ATOM   11545 O  O   . SER B 2 1    ? -14.200 -8.240  9.234   1.00 400.41 ? 129  SER X O   1 
ATOM   11546 C  CB  . SER B 2 1    ? -14.627 -10.854 9.873   1.00 208.40 ? 129  SER X CB  1 
ATOM   11547 O  OG  . SER B 2 1    ? -13.498 -10.854 9.014   1.00 209.76 ? 129  SER X OG  1 
ATOM   11548 N  N   . SER B 2 2    ? -16.249 -7.842  8.388   1.00 313.15 ? 130  SER X N   1 
ATOM   11549 C  CA  . SER B 2 2    ? -15.992 -6.440  8.078   1.00 315.20 ? 130  SER X CA  1 
ATOM   11550 C  C   . SER B 2 2    ? -15.715 -5.640  9.356   1.00 316.09 ? 130  SER X C   1 
ATOM   11551 O  O   . SER B 2 2    ? -16.308 -5.907  10.402  1.00 314.48 ? 130  SER X O   1 
ATOM   11552 C  CB  . SER B 2 2    ? -17.186 -5.850  7.318   1.00 314.54 ? 130  SER X CB  1 
ATOM   11553 O  OG  . SER B 2 2    ? -16.932 -4.528  6.875   1.00 313.75 ? 130  SER X OG  1 
ATOM   11554 N  N   . GLU B 2 3    ? -14.810 -4.666  9.266   1.00 298.70 ? 131  GLU X N   1 
ATOM   11555 C  CA  . GLU B 2 3    ? -14.446 -3.828  10.411  1.00 297.04 ? 131  GLU X CA  1 
ATOM   11556 C  C   . GLU B 2 3    ? -14.546 -2.337  10.076  1.00 297.52 ? 131  GLU X C   1 
ATOM   11557 O  O   . GLU B 2 3    ? -13.527 -1.682  9.862   1.00 299.58 ? 131  GLU X O   1 
ATOM   11558 C  CB  . GLU B 2 3    ? -13.017 -4.143  10.886  1.00 296.31 ? 131  GLU X CB  1 
ATOM   11559 C  CG  . GLU B 2 3    ? -12.846 -5.465  11.634  1.00 293.86 ? 131  GLU X CG  1 
ATOM   11560 C  CD  . GLU B 2 3    ? -11.457 -5.628  12.252  1.00 292.97 ? 131  GLU X CD  1 
ATOM   11561 O  OE1 . GLU B 2 3    ? -10.546 -4.846  11.904  1.00 293.58 ? 131  GLU X OE1 1 
ATOM   11562 O  OE2 . GLU B 2 3    ? -11.278 -6.540  13.088  1.00 291.65 ? 131  GLU X OE2 1 
ATOM   11563 N  N   . THR B 2 4    ? -15.765 -1.802  10.032  1.00 297.05 ? 132  THR X N   1 
ATOM   11564 C  CA  . THR B 2 4    ? -15.960 -0.387  9.709   1.00 296.76 ? 132  THR X CA  1 
ATOM   11565 C  C   . THR B 2 4    ? -15.745 0.508   10.941  1.00 292.92 ? 132  THR X C   1 
ATOM   11566 O  O   . THR B 2 4    ? -16.151 0.157   12.050  1.00 290.38 ? 132  THR X O   1 
ATOM   11567 C  CB  . THR B 2 4    ? -17.355 -0.122  9.070   1.00 297.91 ? 132  THR X CB  1 
ATOM   11568 O  OG1 . THR B 2 4    ? -17.516 -0.931  7.897   1.00 299.88 ? 132  THR X OG1 1 
ATOM   11569 C  CG2 . THR B 2 4    ? -17.507 1.338   8.681   1.00 298.31 ? 132  THR X CG2 1 
ATOM   11570 N  N   . ASN B 2 5    ? -15.090 1.650   10.738  1.00 309.23 ? 133  ASN X N   1 
ATOM   11571 C  CA  . ASN B 2 5    ? -14.873 2.626   11.807  1.00 304.01 ? 133  ASN X CA  1 
ATOM   11572 C  C   . ASN B 2 5    ? -15.844 3.805   11.720  1.00 300.43 ? 133  ASN X C   1 
ATOM   11573 O  O   . ASN B 2 5    ? -15.504 4.862   11.189  1.00 304.92 ? 133  ASN X O   1 
ATOM   11574 C  CB  . ASN B 2 5    ? -13.422 3.126   11.808  1.00 304.01 ? 133  ASN X CB  1 
ATOM   11575 C  CG  . ASN B 2 5    ? -13.018 3.756   10.486  1.00 302.81 ? 133  ASN X CG  1 
ATOM   11576 O  OD1 . ASN B 2 5    ? -13.376 3.266   9.416   1.00 301.61 ? 133  ASN X OD1 1 
ATOM   11577 N  ND2 . ASN B 2 5    ? -12.261 4.844   10.556  1.00 303.45 ? 133  ASN X ND2 1 
ATOM   11578 N  N   . THR B 2 6    ? -17.052 3.614   12.245  1.00 306.17 ? 134  THR X N   1 
ATOM   11579 C  CA  . THR B 2 6    ? -18.091 4.644   12.200  1.00 300.55 ? 134  THR X CA  1 
ATOM   11580 C  C   . THR B 2 6    ? -17.825 5.807   13.148  1.00 295.82 ? 134  THR X C   1 
ATOM   11581 O  O   . THR B 2 6    ? -17.072 5.676   14.107  1.00 292.22 ? 134  THR X O   1 
ATOM   11582 C  CB  . THR B 2 6    ? -19.472 4.063   12.545  1.00 321.69 ? 134  THR X CB  1 
ATOM   11583 O  OG1 . THR B 2 6    ? -20.372 5.131   12.869  1.00 322.83 ? 134  THR X OG1 1 
ATOM   11584 C  CG2 . THR B 2 6    ? -19.369 3.133   13.736  1.00 318.45 ? 134  THR X CG2 1 
ATOM   11585 N  N   . HIS B 2 7    ? -18.466 6.941   12.881  1.00 421.71 ? 135  HIS X N   1 
ATOM   11586 C  CA  . HIS B 2 7    ? -18.314 8.121   13.722  1.00 421.65 ? 135  HIS X CA  1 
ATOM   11587 C  C   . HIS B 2 7    ? -19.654 8.594   14.279  1.00 419.07 ? 135  HIS X C   1 
ATOM   11588 O  O   . HIS B 2 7    ? -20.574 8.909   13.525  1.00 420.01 ? 135  HIS X O   1 
ATOM   11589 C  CB  . HIS B 2 7    ? -17.651 9.257   12.935  1.00 267.06 ? 135  HIS X CB  1 
ATOM   11590 C  CG  . HIS B 2 7    ? -16.337 8.888   12.325  1.00 267.51 ? 135  HIS X CG  1 
ATOM   11591 N  ND1 . HIS B 2 7    ? -15.151 8.911   13.034  1.00 267.09 ? 135  HIS X ND1 1 
ATOM   11592 C  CD2 . HIS B 2 7    ? -16.009 8.495   11.071  1.00 268.47 ? 135  HIS X CD2 1 
ATOM   11593 C  CE1 . HIS B 2 7    ? -14.158 8.543   12.247  1.00 267.75 ? 135  HIS X CE1 1 
ATOM   11594 N  NE2 . HIS B 2 7    ? -14.655 8.284   11.047  1.00 268.61 ? 135  HIS X NE2 1 
ATOM   11595 N  N   . LEU B 2 8    ? -19.758 8.643   15.604  1.00 206.40 ? 136  LEU X N   1 
ATOM   11596 C  CA  . LEU B 2 8    ? -20.961 9.165   16.254  1.00 202.19 ? 136  LEU X CA  1 
ATOM   11597 C  C   . LEU B 2 8    ? -20.712 10.434  17.070  1.00 202.68 ? 136  LEU X C   1 
ATOM   11598 O  O   . LEU B 2 8    ? -19.649 10.604  17.668  1.00 201.62 ? 136  LEU X O   1 
ATOM   11599 C  CB  . LEU B 2 8    ? -21.678 8.099   17.104  1.00 193.83 ? 136  LEU X CB  1 
ATOM   11600 C  CG  . LEU B 2 8    ? -20.974 7.045   17.955  1.00 185.87 ? 136  LEU X CG  1 
ATOM   11601 C  CD1 . LEU B 2 8    ? -22.010 6.220   18.709  1.00 180.66 ? 136  LEU X CD1 1 
ATOM   11602 C  CD2 . LEU B 2 8    ? -20.128 6.144   17.089  1.00 185.89 ? 136  LEU X CD2 1 
ATOM   11603 N  N   . PHE B 2 9    ? -21.708 11.318  17.076  1.00 281.67 ? 137  PHE X N   1 
ATOM   11604 C  CA  . PHE B 2 9    ? -21.622 12.593  17.783  1.00 283.00 ? 137  PHE X CA  1 
ATOM   11605 C  C   . PHE B 2 9    ? -22.340 12.542  19.138  1.00 277.52 ? 137  PHE X C   1 
ATOM   11606 O  O   . PHE B 2 9    ? -23.483 12.097  19.238  1.00 273.73 ? 137  PHE X O   1 
ATOM   11607 C  CB  . PHE B 2 9    ? -22.199 13.738  16.930  1.00 290.10 ? 137  PHE X CB  1 
ATOM   11608 C  CG  . PHE B 2 9    ? -21.767 13.717  15.477  1.00 297.76 ? 137  PHE X CG  1 
ATOM   11609 C  CD1 . PHE B 2 9    ? -20.543 13.191  15.097  1.00 296.53 ? 137  PHE X CD1 1 
ATOM   11610 C  CD2 . PHE B 2 9    ? -22.592 14.250  14.494  1.00 300.97 ? 137  PHE X CD2 1 
ATOM   11611 C  CE1 . PHE B 2 9    ? -20.161 13.182  13.763  1.00 299.06 ? 137  PHE X CE1 1 
ATOM   11612 C  CE2 . PHE B 2 9    ? -22.212 14.245  13.160  1.00 303.88 ? 137  PHE X CE2 1 
ATOM   11613 C  CZ  . PHE B 2 9    ? -20.998 13.713  12.796  1.00 302.35 ? 137  PHE X CZ  1 
ATOM   11614 N  N   . VAL B 2 10   ? -21.658 13.005  20.177  1.00 239.44 ? 138  VAL X N   1 
ATOM   11615 C  CA  . VAL B 2 10   ? -22.248 13.096  21.500  1.00 232.20 ? 138  VAL X CA  1 
ATOM   11616 C  C   . VAL B 2 10   ? -22.571 14.551  21.815  1.00 236.03 ? 138  VAL X C   1 
ATOM   11617 O  O   . VAL B 2 10   ? -21.773 15.444  21.530  1.00 239.81 ? 138  VAL X O   1 
ATOM   11618 C  CB  . VAL B 2 10   ? -21.305 12.509  22.576  1.00 225.10 ? 138  VAL X CB  1 
ATOM   11619 C  CG1 . VAL B 2 10   ? -21.572 13.128  23.943  1.00 220.81 ? 138  VAL X CG1 1 
ATOM   11620 C  CG2 . VAL B 2 10   ? -21.443 10.995  22.635  1.00 219.21 ? 138  VAL X CG2 1 
ATOM   11621 N  N   . ASN B 2 11   ? -23.749 14.778  22.393  1.00 227.47 ? 139  ASN X N   1 
ATOM   11622 C  CA  . ASN B 2 11   ? -24.164 16.108  22.835  1.00 228.26 ? 139  ASN X CA  1 
ATOM   11623 C  C   . ASN B 2 11   ? -24.926 16.079  24.178  1.00 222.97 ? 139  ASN X C   1 
ATOM   11624 O  O   . ASN B 2 11   ? -26.062 15.606  24.246  1.00 220.65 ? 139  ASN X O   1 
ATOM   11625 C  CB  . ASN B 2 11   ? -25.032 16.769  21.762  1.00 231.90 ? 139  ASN X CB  1 
ATOM   11626 C  CG  . ASN B 2 11   ? -24.542 16.490  20.369  1.00 237.65 ? 139  ASN X CG  1 
ATOM   11627 O  OD1 . ASN B 2 11   ? -23.499 16.985  19.958  1.00 240.53 ? 139  ASN X OD1 1 
ATOM   11628 N  ND2 . ASN B 2 11   ? -25.293 15.691  19.629  1.00 239.42 ? 139  ASN X ND2 1 
ATOM   11629 N  N   . LYS B 2 12   ? -24.307 16.573  25.245  1.00 255.99 ? 140  LYS X N   1 
ATOM   11630 C  CA  . LYS B 2 12   ? -24.995 16.636  26.533  1.00 251.40 ? 140  LYS X CA  1 
ATOM   11631 C  C   . LYS B 2 12   ? -25.849 17.917  26.607  1.00 253.04 ? 140  LYS X C   1 
ATOM   11632 O  O   . LYS B 2 12   ? -25.366 19.001  26.287  1.00 256.25 ? 140  LYS X O   1 
ATOM   11633 C  CB  . LYS B 2 12   ? -23.989 16.544  27.700  1.00 248.99 ? 140  LYS X CB  1 
ATOM   11634 C  CG  . LYS B 2 12   ? -22.984 15.380  27.601  1.00 246.66 ? 140  LYS X CG  1 
ATOM   11635 C  CD  . LYS B 2 12   ? -22.247 15.098  28.921  1.00 241.15 ? 140  LYS X CD  1 
ATOM   11636 C  CE  . LYS B 2 12   ? -22.998 14.096  29.799  1.00 235.04 ? 140  LYS X CE  1 
ATOM   11637 N  NZ  . LYS B 2 12   ? -22.128 13.504  30.852  1.00 231.05 ? 140  LYS X NZ  1 
ATOM   11638 N  N   . VAL B 2 13   ? -27.118 17.800  27.003  1.00 252.02 ? 141  VAL X N   1 
ATOM   11639 C  CA  . VAL B 2 13   ? -27.976 18.988  27.135  1.00 256.75 ? 141  VAL X CA  1 
ATOM   11640 C  C   . VAL B 2 13   ? -28.199 19.434  28.593  1.00 256.20 ? 141  VAL X C   1 
ATOM   11641 O  O   . VAL B 2 13   ? -29.185 19.051  29.230  1.00 249.91 ? 141  VAL X O   1 
ATOM   11642 C  CB  . VAL B 2 13   ? -29.347 18.806  26.434  1.00 259.07 ? 141  VAL X CB  1 
ATOM   11643 C  CG1 . VAL B 2 13   ? -30.059 20.142  26.311  1.00 263.62 ? 141  VAL X CG1 1 
ATOM   11644 C  CG2 . VAL B 2 13   ? -29.166 18.191  25.064  1.00 261.26 ? 141  VAL X CG2 1 
ATOM   11645 N  N   . TYR B 2 14   ? -27.276 20.241  29.112  1.00 444.50 ? 142  TYR X N   1 
ATOM   11646 C  CA  . TYR B 2 14   ? -27.431 20.823  30.442  1.00 442.73 ? 142  TYR X CA  1 
ATOM   11647 C  C   . TYR B 2 14   ? -28.308 22.059  30.352  1.00 446.38 ? 142  TYR X C   1 
ATOM   11648 O  O   . TYR B 2 14   ? -27.985 23.101  30.919  1.00 448.37 ? 142  TYR X O   1 
ATOM   11649 C  CB  . TYR B 2 14   ? -26.075 21.194  31.049  1.00 272.40 ? 142  TYR X CB  1 
ATOM   11650 C  CG  . TYR B 2 14   ? -25.189 20.002  31.354  1.00 270.32 ? 142  TYR X CG  1 
ATOM   11651 C  CD1 . TYR B 2 14   ? -25.279 19.328  32.570  1.00 265.45 ? 142  TYR X CD1 1 
ATOM   11652 C  CD2 . TYR B 2 14   ? -24.263 19.549  30.426  1.00 273.32 ? 142  TYR X CD2 1 
ATOM   11653 C  CE1 . TYR B 2 14   ? -24.465 18.227  32.849  1.00 263.57 ? 142  TYR X CE1 1 
ATOM   11654 C  CE2 . TYR B 2 14   ? -23.449 18.453  30.692  1.00 271.58 ? 142  TYR X CE2 1 
ATOM   11655 C  CZ  . TYR B 2 14   ? -23.553 17.796  31.904  1.00 266.69 ? 142  TYR X CZ  1 
ATOM   11656 O  OH  . TYR B 2 14   ? -22.744 16.708  32.167  1.00 265.04 ? 142  TYR X OH  1 
ATOM   11657 N  N   . GLY B 2 15   ? -29.420 21.935  29.635  1.00 212.42 ? 143  GLY X N   1 
ATOM   11658 C  CA  . GLY B 2 15   ? -30.264 23.077  29.337  1.00 216.28 ? 143  GLY X CA  1 
ATOM   11659 C  C   . GLY B 2 15   ? -29.576 23.973  28.323  1.00 226.74 ? 143  GLY X C   1 
ATOM   11660 O  O   . GLY B 2 15   ? -28.898 23.470  27.427  1.00 232.29 ? 143  GLY X O   1 
ATOM   11661 N  N   . GLY B 2 16   ? -29.757 25.288  28.461  1.00 149.13 ? 144  GLY X N   1 
ATOM   11662 C  CA  . GLY B 2 16   ? -29.030 26.283  27.681  1.00 158.38 ? 144  GLY X CA  1 
ATOM   11663 C  C   . GLY B 2 16   ? -27.520 26.108  27.745  1.00 158.43 ? 144  GLY X C   1 
ATOM   11664 O  O   . GLY B 2 16   ? -26.749 27.078  27.779  1.00 162.20 ? 144  GLY X O   1 
ATOM   11665 N  N   . ASN B 2 17   ? -27.117 24.842  27.798  1.00 398.65 ? 145  ASN X N   1 
ATOM   11666 C  CA  . ASN B 2 17   ? -25.735 24.420  27.699  1.00 395.84 ? 145  ASN X CA  1 
ATOM   11667 C  C   . ASN B 2 17   ? -25.706 23.163  26.862  1.00 389.92 ? 145  ASN X C   1 
ATOM   11668 O  O   . ASN B 2 17   ? -26.622 22.346  26.923  1.00 385.92 ? 145  ASN X O   1 
ATOM   11669 C  CB  . ASN B 2 17   ? -25.172 24.081  29.074  1.00 214.97 ? 145  ASN X CB  1 
ATOM   11670 C  CG  . ASN B 2 17   ? -25.470 25.139  30.093  1.00 213.72 ? 145  ASN X CG  1 
ATOM   11671 O  OD1 . ASN B 2 17   ? -25.370 26.339  29.815  1.00 217.14 ? 145  ASN X OD1 1 
ATOM   11672 N  ND2 . ASN B 2 17   ? -25.850 24.706  31.291  1.00 208.91 ? 145  ASN X ND2 1 
ATOM   11673 N  N   . LEU B 2 18   ? -24.658 23.019  26.068  1.00 183.77 ? 146  LEU X N   1 
ATOM   11674 C  CA  . LEU B 2 18   ? -24.384 21.759  25.420  1.00 178.79 ? 146  LEU X CA  1 
ATOM   11675 C  C   . LEU B 2 18   ? -22.893 21.541  25.245  1.00 177.82 ? 146  LEU X C   1 
ATOM   11676 O  O   . LEU B 2 18   ? -22.213 22.321  24.578  1.00 180.96 ? 146  LEU X O   1 
ATOM   11677 C  CB  . LEU B 2 18   ? -25.060 21.691  24.068  1.00 182.66 ? 146  LEU X CB  1 
ATOM   11678 C  CG  . LEU B 2 18   ? -24.485 20.606  23.149  1.00 181.79 ? 146  LEU X CG  1 
ATOM   11679 C  CD1 . LEU B 2 18   ? -23.310 21.113  22.297  1.00 187.63 ? 146  LEU X CD1 1 
ATOM   11680 C  CD2 . LEU B 2 18   ? -24.122 19.335  23.914  1.00 175.08 ? 146  LEU X CD2 1 
ATOM   11681 N  N   . ASP B 2 19   ? -22.396 20.470  25.855  1.00 196.21 ? 147  ASP X N   1 
ATOM   11682 C  CA  . ASP B 2 19   ? -21.035 20.006  25.627  1.00 195.98 ? 147  ASP X CA  1 
ATOM   11683 C  C   . ASP B 2 19   ? -21.105 18.815  24.657  1.00 200.40 ? 147  ASP X C   1 
ATOM   11684 O  O   . ASP B 2 19   ? -21.624 17.751  25.011  1.00 196.47 ? 147  ASP X O   1 
ATOM   11685 C  CB  . ASP B 2 19   ? -20.363 19.626  26.955  1.00 184.34 ? 147  ASP X CB  1 
ATOM   11686 C  CG  . ASP B 2 19   ? -20.222 20.818  27.920  1.00 178.26 ? 147  ASP X CG  1 
ATOM   11687 O  OD1 . ASP B 2 19   ? -20.190 21.992  27.484  1.00 180.92 ? 147  ASP X OD1 1 
ATOM   11688 O  OD2 . ASP B 2 19   ? -20.133 20.569  29.136  1.00 171.41 ? 147  ASP X OD2 1 
ATOM   11689 N  N   . ALA B 2 20   ? -20.606 19.020  23.432  1.00 183.40 ? 148  ALA X N   1 
ATOM   11690 C  CA  . ALA B 2 20   ? -20.677 18.028  22.344  1.00 186.52 ? 148  ALA X CA  1 
ATOM   11691 C  C   . ALA B 2 20   ? -19.314 17.476  21.908  1.00 190.25 ? 148  ALA X C   1 
ATOM   11692 O  O   . ALA B 2 20   ? -18.408 18.222  21.531  1.00 196.56 ? 148  ALA X O   1 
ATOM   11693 C  CB  . ALA B 2 20   ? -21.417 18.610  21.135  1.00 191.98 ? 148  ALA X CB  1 
ATOM   11694 N  N   . SER B 2 21   ? -19.188 16.157  21.963  1.00 235.20 ? 149  SER X N   1 
ATOM   11695 C  CA  . SER B 2 21   ? -17.958 15.482  21.601  1.00 234.59 ? 149  SER X CA  1 
ATOM   11696 C  C   . SER B 2 21   ? -18.234 14.727  20.317  1.00 230.15 ? 149  SER X C   1 
ATOM   11697 O  O   . SER B 2 21   ? -19.311 14.148  20.180  1.00 225.71 ? 149  SER X O   1 
ATOM   11698 C  CB  . SER B 2 21   ? -17.585 14.471  22.685  1.00 231.75 ? 149  SER X CB  1 
ATOM   11699 O  OG  . SER B 2 21   ? -17.619 15.048  23.980  1.00 230.49 ? 149  SER X OG  1 
ATOM   11700 N  N   . ILE B 2 22   ? -17.284 14.735  19.377  1.00 278.59 ? 150  ILE X N   1 
ATOM   11701 C  CA  . ILE B 2 22   ? -17.360 13.868  18.194  1.00 271.77 ? 150  ILE X CA  1 
ATOM   11702 C  C   . ILE B 2 22   ? -16.412 12.683  18.381  1.00 266.82 ? 150  ILE X C   1 
ATOM   11703 O  O   . ILE B 2 22   ? -15.310 12.843  18.911  1.00 266.80 ? 150  ILE X O   1 
ATOM   11704 C  CB  . ILE B 2 22   ? -17.015 14.612  16.877  1.00 259.96 ? 150  ILE X CB  1 
ATOM   11705 C  CG1 . ILE B 2 22   ? -15.665 14.152  16.332  1.00 255.45 ? 150  ILE X CG1 1 
ATOM   11706 C  CG2 . ILE B 2 22   ? -17.054 16.118  17.068  1.00 268.43 ? 150  ILE X CG2 1 
ATOM   11707 C  CD1 . ILE B 2 22   ? -15.767 12.972  15.396  1.00 242.28 ? 150  ILE X CD1 1 
ATOM   11708 N  N   . ASP B 2 23   ? -16.827 11.500  17.939  1.00 251.57 ? 151  ASP X N   1 
ATOM   11709 C  CA  . ASP B 2 23   ? -16.092 10.286  18.279  1.00 248.10 ? 151  ASP X CA  1 
ATOM   11710 C  C   . ASP B 2 23   ? -16.460 9.109   17.370  1.00 255.06 ? 151  ASP X C   1 
ATOM   11711 O  O   . ASP B 2 23   ? -17.165 9.292   16.374  1.00 255.35 ? 151  ASP X O   1 
ATOM   11712 C  CB  . ASP B 2 23   ? -16.353 9.938   19.741  1.00 236.55 ? 151  ASP X CB  1 
ATOM   11713 C  CG  . ASP B 2 23   ? -15.325 8.997   20.309  1.00 228.35 ? 151  ASP X CG  1 
ATOM   11714 O  OD1 . ASP B 2 23   ? -14.241 8.853   19.699  1.00 230.78 ? 151  ASP X OD1 1 
ATOM   11715 O  OD2 . ASP B 2 23   ? -15.612 8.412   21.375  1.00 220.14 ? 151  ASP X OD2 1 
ATOM   11716 N  N   . SER B 2 24   ? -15.993 7.906   17.720  1.00 220.07 ? 152  SER X N   1 
ATOM   11717 C  CA  . SER B 2 24   ? -16.122 6.732   16.844  1.00 229.84 ? 152  SER X CA  1 
ATOM   11718 C  C   . SER B 2 24   ? -16.628 5.459   17.533  1.00 236.79 ? 152  SER X C   1 
ATOM   11719 O  O   . SER B 2 24   ? -16.508 5.310   18.748  1.00 231.84 ? 152  SER X O   1 
ATOM   11720 C  CB  . SER B 2 24   ? -14.779 6.421   16.173  1.00 231.16 ? 152  SER X CB  1 
ATOM   11721 O  OG  . SER B 2 24   ? -13.854 5.878   17.098  1.00 231.17 ? 152  SER X OG  1 
ATOM   11722 N  N   . PHE B 2 25   ? -17.187 4.547   16.736  1.00 272.75 ? 153  PHE X N   1 
ATOM   11723 C  CA  . PHE B 2 25   ? -17.568 3.209   17.192  1.00 279.79 ? 153  PHE X CA  1 
ATOM   11724 C  C   . PHE B 2 25   ? -16.831 2.197   16.328  1.00 286.94 ? 153  PHE X C   1 
ATOM   11725 O  O   . PHE B 2 25   ? -16.157 2.566   15.363  1.00 288.67 ? 153  PHE X O   1 
ATOM   11726 C  CB  . PHE B 2 25   ? -19.087 2.997   17.082  1.00 285.13 ? 153  PHE X CB  1 
ATOM   11727 C  CG  . PHE B 2 25   ? -19.556 1.609   17.475  1.00 288.64 ? 153  PHE X CG  1 
ATOM   11728 C  CD1 . PHE B 2 25   ? -19.975 1.342   18.765  1.00 285.31 ? 153  PHE X CD1 1 
ATOM   11729 C  CD2 . PHE B 2 25   ? -19.607 0.582   16.545  1.00 294.36 ? 153  PHE X CD2 1 
ATOM   11730 C  CE1 . PHE B 2 25   ? -20.413 0.076   19.120  1.00 284.44 ? 153  PHE X CE1 1 
ATOM   11731 C  CE2 . PHE B 2 25   ? -20.041 -0.686  16.903  1.00 293.26 ? 153  PHE X CE2 1 
ATOM   11732 C  CZ  . PHE B 2 25   ? -20.445 -0.934  18.187  1.00 288.04 ? 153  PHE X CZ  1 
ATOM   11733 N  N   . SER B 2 26   ? -16.952 0.922   16.669  1.00 441.50 ? 154  SER X N   1 
ATOM   11734 C  CA  . SER B 2 26   ? -16.309 -0.113  15.882  1.00 444.11 ? 154  SER X CA  1 
ATOM   11735 C  C   . SER B 2 26   ? -17.225 -1.313  15.676  1.00 445.35 ? 154  SER X C   1 
ATOM   11736 O  O   . SER B 2 26   ? -17.425 -2.127  16.577  1.00 441.80 ? 154  SER X O   1 
ATOM   11737 C  CB  . SER B 2 26   ? -14.990 -0.515  16.532  1.00 245.69 ? 154  SER X CB  1 
ATOM   11738 O  OG  . SER B 2 26   ? -14.139 0.615   16.634  1.00 244.03 ? 154  SER X OG  1 
ATOM   11739 N  N   . ILE B 2 27   ? -17.795 -1.389  14.478  1.00 234.41 ? 155  ILE X N   1 
ATOM   11740 C  CA  . ILE B 2 27   ? -18.658 -2.492  14.087  1.00 237.18 ? 155  ILE X CA  1 
ATOM   11741 C  C   . ILE B 2 27   ? -17.822 -3.626  13.521  1.00 241.32 ? 155  ILE X C   1 
ATOM   11742 O  O   . ILE B 2 27   ? -17.169 -3.475  12.489  1.00 242.73 ? 155  ILE X O   1 
ATOM   11743 C  CB  . ILE B 2 27   ? -19.662 -2.054  13.019  1.00 235.76 ? 155  ILE X CB  1 
ATOM   11744 C  CG1 . ILE B 2 27   ? -20.355 -0.760  13.447  1.00 234.25 ? 155  ILE X CG1 1 
ATOM   11745 C  CG2 . ILE B 2 27   ? -20.662 -3.168  12.756  1.00 236.33 ? 155  ILE X CG2 1 
ATOM   11746 C  CD1 . ILE B 2 27   ? -21.247 -0.161  12.388  1.00 235.33 ? 155  ILE X CD1 1 
ATOM   11747 N  N   . ASN B 2 28   ? -17.860 -4.768  14.195  1.00 485.87 ? 156  ASN X N   1 
ATOM   11748 C  CA  . ASN B 2 28   ? -16.959 -5.868  13.890  1.00 491.26 ? 156  ASN X CA  1 
ATOM   11749 C  C   . ASN B 2 28   ? -17.587 -6.945  13.024  1.00 493.13 ? 156  ASN X C   1 
ATOM   11750 O  O   . ASN B 2 28   ? -17.121 -8.083  13.003  1.00 492.91 ? 156  ASN X O   1 
ATOM   11751 C  CB  . ASN B 2 28   ? -16.459 -6.483  15.190  1.00 269.06 ? 156  ASN X CB  1 
ATOM   11752 C  CG  . ASN B 2 28   ? -16.109 -5.434  16.219  1.00 268.79 ? 156  ASN X CG  1 
ATOM   11753 O  OD1 . ASN B 2 28   ? -15.863 -4.277  15.876  1.00 269.47 ? 156  ASN X OD1 1 
ATOM   11754 N  ND2 . ASN B 2 28   ? -16.091 -5.827  17.489  1.00 265.13 ? 156  ASN X ND2 1 
ATOM   11755 N  N   . LYS B 2 29   ? -18.644 -6.582  12.310  1.00 271.49 ? 157  LYS X N   1 
ATOM   11756 C  CA  . LYS B 2 29   ? -19.376 -7.546  11.495  1.00 276.61 ? 157  LYS X CA  1 
ATOM   11757 C  C   . LYS B 2 29   ? -19.976 -6.881  10.244  1.00 280.98 ? 157  LYS X C   1 
ATOM   11758 O  O   . LYS B 2 29   ? -19.894 -5.660  10.084  1.00 281.39 ? 157  LYS X O   1 
ATOM   11759 C  CB  . LYS B 2 29   ? -20.466 -8.240  12.335  1.00 276.36 ? 157  LYS X CB  1 
ATOM   11760 C  CG  . LYS B 2 29   ? -19.938 -9.103  13.500  1.00 275.83 ? 157  LYS X CG  1 
ATOM   11761 C  CD  . LYS B 2 29   ? -21.055 -9.605  14.433  1.00 274.63 ? 157  LYS X CD  1 
ATOM   11762 C  CE  . LYS B 2 29   ? -21.814 -10.800 13.861  1.00 274.01 ? 157  LYS X CE  1 
ATOM   11763 N  NZ  . LYS B 2 29   ? -22.885 -11.288 14.781  1.00 272.87 ? 157  LYS X NZ  1 
ATOM   11764 N  N   . GLU B 2 30   ? -20.547 -7.696  9.353   1.00 342.31 ? 158  GLU X N   1 
ATOM   11765 C  CA  . GLU B 2 30   ? -21.205 -7.211  8.134   1.00 346.20 ? 158  GLU X CA  1 
ATOM   11766 C  C   . GLU B 2 30   ? -22.685 -6.887  8.370   1.00 344.59 ? 158  GLU X C   1 
ATOM   11767 O  O   . GLU B 2 30   ? -23.270 -6.050  7.676   1.00 345.93 ? 158  GLU X O   1 
ATOM   11768 C  CB  . GLU B 2 30   ? -21.054 -8.228  6.994   1.00 352.54 ? 158  GLU X CB  1 
ATOM   11769 C  CG  . GLU B 2 30   ? -21.349 -9.668  7.396   1.00 357.38 ? 158  GLU X CG  1 
ATOM   11770 C  CD  . GLU B 2 30   ? -21.474 -10.599 6.206   1.00 361.83 ? 158  GLU X CD  1 
ATOM   11771 O  OE1 . GLU B 2 30   ? -21.235 -10.147 5.067   1.00 362.67 ? 158  GLU X OE1 1 
ATOM   11772 O  OE2 . GLU B 2 30   ? -21.814 -11.783 6.409   1.00 364.28 ? 158  GLU X OE2 1 
ATOM   11773 N  N   . GLU B 2 31   ? -23.277 -7.563  9.352   1.00 416.15 ? 159  GLU X N   1 
ATOM   11774 C  CA  . GLU B 2 31   ? -24.644 -7.296  9.787   1.00 412.48 ? 159  GLU X CA  1 
ATOM   11775 C  C   . GLU B 2 31   ? -24.727 -7.520  11.296  1.00 405.98 ? 159  GLU X C   1 
ATOM   11776 O  O   . GLU B 2 31   ? -24.244 -8.531  11.803  1.00 404.83 ? 159  GLU X O   1 
ATOM   11777 C  CB  . GLU B 2 31   ? -25.641 -8.202  9.053   1.00 415.05 ? 159  GLU X CB  1 
ATOM   11778 C  CG  . GLU B 2 31   ? -25.609 -9.678  9.463   1.00 415.82 ? 159  GLU X CG  1 
ATOM   11779 C  CD  . GLU B 2 31   ? -24.641 -10.513 8.638   1.00 419.30 ? 159  GLU X CD  1 
ATOM   11780 O  OE1 . GLU B 2 31   ? -24.187 -10.038 7.577   1.00 421.49 ? 159  GLU X OE1 1 
ATOM   11781 O  OE2 . GLU B 2 31   ? -24.341 -11.654 9.048   1.00 420.23 ? 159  GLU X OE2 1 
ATOM   11782 N  N   . VAL B 2 32   ? -25.322 -6.578  12.019  1.00 435.20 ? 160  VAL X N   1 
ATOM   11783 C  CA  . VAL B 2 32   ? -25.375 -6.695  13.472  1.00 427.97 ? 160  VAL X CA  1 
ATOM   11784 C  C   . VAL B 2 32   ? -26.783 -6.555  14.022  1.00 425.80 ? 160  VAL X C   1 
ATOM   11785 O  O   . VAL B 2 32   ? -27.595 -5.786  13.511  1.00 427.39 ? 160  VAL X O   1 
ATOM   11786 C  CB  . VAL B 2 32   ? -24.464 -5.664  14.170  1.00 204.86 ? 160  VAL X CB  1 
ATOM   11787 C  CG1 . VAL B 2 32   ? -24.547 -5.823  15.684  1.00 200.05 ? 160  VAL X CG1 1 
ATOM   11788 C  CG2 . VAL B 2 32   ? -23.031 -5.821  13.706  1.00 205.32 ? 160  VAL X CG2 1 
ATOM   11789 N  N   . SER B 2 33   ? -27.059 -7.314  15.073  1.00 325.56 ? 161  SER X N   1 
ATOM   11790 C  CA  . SER B 2 33   ? -28.321 -7.208  15.776  1.00 322.31 ? 161  SER X CA  1 
ATOM   11791 C  C   . SER B 2 33   ? -28.420 -5.850  16.450  1.00 319.30 ? 161  SER X C   1 
ATOM   11792 O  O   . SER B 2 33   ? -27.476 -5.393  17.092  1.00 317.22 ? 161  SER X O   1 
ATOM   11793 C  CB  . SER B 2 33   ? -28.445 -8.318  16.819  1.00 317.81 ? 161  SER X CB  1 
ATOM   11794 O  OG  . SER B 2 33   ? -29.648 -8.184  17.553  1.00 312.43 ? 161  SER X OG  1 
ATOM   11795 N  N   . LEU B 2 34   ? -29.574 -5.212  16.299  1.00 268.56 ? 162  LEU X N   1 
ATOM   11796 C  CA  . LEU B 2 34   ? -29.844 -3.929  16.930  1.00 265.76 ? 162  LEU X CA  1 
ATOM   11797 C  C   . LEU B 2 34   ? -29.707 -4.056  18.449  1.00 259.24 ? 162  LEU X C   1 
ATOM   11798 O  O   . LEU B 2 34   ? -29.556 -3.058  19.159  1.00 255.33 ? 162  LEU X O   1 
ATOM   11799 C  CB  . LEU B 2 34   ? -31.246 -3.456  16.542  1.00 267.99 ? 162  LEU X CB  1 
ATOM   11800 C  CG  . LEU B 2 34   ? -31.717 -2.048  16.894  1.00 267.09 ? 162  LEU X CG  1 
ATOM   11801 C  CD1 . LEU B 2 34   ? -30.706 -1.016  16.456  1.00 268.74 ? 162  LEU X CD1 1 
ATOM   11802 C  CD2 . LEU B 2 34   ? -33.063 -1.788  16.242  1.00 270.19 ? 162  LEU X CD2 1 
ATOM   11803 N  N   . LYS B 2 35   ? -29.768 -5.292  18.937  1.00 352.57 ? 163  LYS X N   1 
ATOM   11804 C  CA  . LYS B 2 35   ? -29.502 -5.577  20.339  1.00 346.97 ? 163  LYS X CA  1 
ATOM   11805 C  C   . LYS B 2 35   ? -28.035 -5.302  20.625  1.00 347.00 ? 163  LYS X C   1 
ATOM   11806 O  O   . LYS B 2 35   ? -27.702 -4.473  21.466  1.00 345.82 ? 163  LYS X O   1 
ATOM   11807 C  CB  . LYS B 2 35   ? -29.823 -7.037  20.668  1.00 344.65 ? 163  LYS X CB  1 
ATOM   11808 C  CG  . LYS B 2 35   ? -29.426 -7.458  22.081  1.00 337.61 ? 163  LYS X CG  1 
ATOM   11809 C  CD  . LYS B 2 35   ? -29.432 -8.973  22.236  1.00 336.09 ? 163  LYS X CD  1 
ATOM   11810 C  CE  . LYS B 2 35   ? -29.017 -9.398  23.638  1.00 329.97 ? 163  LYS X CE  1 
ATOM   11811 N  NZ  . LYS B 2 35   ? -30.028 -9.014  24.659  1.00 325.71 ? 163  LYS X NZ  1 
ATOM   11812 N  N   . GLU B 2 36   ? -27.161 -6.004  19.911  1.00 318.83 ? 164  GLU X N   1 
ATOM   11813 C  CA  . GLU B 2 36   ? -25.725 -5.801  20.038  1.00 319.25 ? 164  GLU X CA  1 
ATOM   11814 C  C   . GLU B 2 36   ? -25.380 -4.358  19.682  1.00 313.91 ? 164  GLU X C   1 
ATOM   11815 O  O   . GLU B 2 36   ? -24.460 -3.762  20.251  1.00 309.51 ? 164  GLU X O   1 
ATOM   11816 C  CB  . GLU B 2 36   ? -24.965 -6.767  19.125  1.00 330.73 ? 164  GLU X CB  1 
ATOM   11817 C  CG  . GLU B 2 36   ? -25.179 -8.233  19.464  1.00 336.76 ? 164  GLU X CG  1 
ATOM   11818 C  CD  . GLU B 2 36   ? -24.420 -9.157  18.531  1.00 347.22 ? 164  GLU X CD  1 
ATOM   11819 O  OE1 . GLU B 2 36   ? -23.961 -8.687  17.467  1.00 352.90 ? 164  GLU X OE1 1 
ATOM   11820 O  OE2 . GLU B 2 36   ? -24.285 -10.353 18.858  1.00 349.39 ? 164  GLU X OE2 1 
ATOM   11821 N  N   . LEU B 2 37   ? -26.134 -3.809  18.732  1.00 249.48 ? 165  LEU X N   1 
ATOM   11822 C  CA  . LEU B 2 37   ? -25.990 -2.419  18.316  1.00 246.88 ? 165  LEU X CA  1 
ATOM   11823 C  C   . LEU B 2 37   ? -26.273 -1.511  19.499  1.00 242.95 ? 165  LEU X C   1 
ATOM   11824 O  O   . LEU B 2 37   ? -25.592 -0.510  19.730  1.00 242.40 ? 165  LEU X O   1 
ATOM   11825 C  CB  . LEU B 2 37   ? -26.990 -2.111  17.202  1.00 246.02 ? 165  LEU X CB  1 
ATOM   11826 C  CG  . LEU B 2 37   ? -26.673 -0.874  16.373  1.00 244.43 ? 165  LEU X CG  1 
ATOM   11827 C  CD1 . LEU B 2 37   ? -25.368 -1.107  15.639  1.00 246.32 ? 165  LEU X CD1 1 
ATOM   11828 C  CD2 . LEU B 2 37   ? -27.786 -0.556  15.392  1.00 245.21 ? 165  LEU X CD2 1 
ATOM   11829 N  N   . ASP B 2 38   ? -27.300 -1.887  20.246  1.00 305.38 ? 166  ASP X N   1 
ATOM   11830 C  CA  . ASP B 2 38   ? -27.751 -1.105  21.373  1.00 302.54 ? 166  ASP X CA  1 
ATOM   11831 C  C   . ASP B 2 38   ? -26.927 -1.365  22.628  1.00 299.61 ? 166  ASP X C   1 
ATOM   11832 O  O   . ASP B 2 38   ? -26.703 -0.451  23.420  1.00 296.72 ? 166  ASP X O   1 
ATOM   11833 C  CB  . ASP B 2 38   ? -29.222 -1.388  21.640  1.00 302.51 ? 166  ASP X CB  1 
ATOM   11834 C  CG  . ASP B 2 38   ? -30.012 -0.130  21.847  1.00 303.39 ? 166  ASP X CG  1 
ATOM   11835 O  OD1 . ASP B 2 38   ? -29.394 0.955   21.815  1.00 305.39 ? 166  ASP X OD1 1 
ATOM   11836 O  OD2 . ASP B 2 38   ? -31.242 -0.221  22.036  1.00 303.13 ? 166  ASP X OD2 1 
ATOM   11837 N  N   . PHE B 2 39   ? -26.482 -2.606  22.816  1.00 355.62 ? 167  PHE X N   1 
ATOM   11838 C  CA  . PHE B 2 39   ? -25.674 -2.945  23.988  1.00 355.10 ? 167  PHE X CA  1 
ATOM   11839 C  C   . PHE B 2 39   ? -24.300 -2.298  23.900  1.00 352.63 ? 167  PHE X C   1 
ATOM   11840 O  O   . PHE B 2 39   ? -23.655 -2.046  24.921  1.00 351.24 ? 167  PHE X O   1 
ATOM   11841 C  CB  . PHE B 2 39   ? -25.522 -4.462  24.161  1.00 359.75 ? 167  PHE X CB  1 
ATOM   11842 C  CG  . PHE B 2 39   ? -24.758 -4.861  25.406  1.00 360.26 ? 167  PHE X CG  1 
ATOM   11843 C  CD1 . PHE B 2 39   ? -23.377 -5.005  25.381  1.00 362.44 ? 167  PHE X CD1 1 
ATOM   11844 C  CD2 . PHE B 2 39   ? -25.423 -5.089  26.600  1.00 357.85 ? 167  PHE X CD2 1 
ATOM   11845 C  CE1 . PHE B 2 39   ? -22.678 -5.368  26.521  1.00 360.24 ? 167  PHE X CE1 1 
ATOM   11846 C  CE2 . PHE B 2 39   ? -24.728 -5.452  27.740  1.00 355.72 ? 167  PHE X CE2 1 
ATOM   11847 C  CZ  . PHE B 2 39   ? -23.355 -5.591  27.700  1.00 356.64 ? 167  PHE X CZ  1 
ATOM   11848 N  N   . LYS B 2 40   ? -23.851 -2.037  22.676  1.00 248.82 ? 168  LYS X N   1 
ATOM   11849 C  CA  . LYS B 2 40   ? -22.551 -1.407  22.473  1.00 243.51 ? 168  LYS X CA  1 
ATOM   11850 C  C   . LYS B 2 40   ? -22.610 0.122   22.649  1.00 239.52 ? 168  LYS X C   1 
ATOM   11851 O  O   . LYS B 2 40   ? -21.717 0.723   23.262  1.00 236.78 ? 168  LYS X O   1 
ATOM   11852 C  CB  . LYS B 2 40   ? -21.954 -1.819  21.120  1.00 246.63 ? 168  LYS X CB  1 
ATOM   11853 C  CG  . LYS B 2 40   ? -21.555 -3.296  21.050  1.00 244.58 ? 168  LYS X CG  1 
ATOM   11854 C  CD  . LYS B 2 40   ? -20.424 -3.545  20.057  1.00 247.90 ? 168  LYS X CD  1 
ATOM   11855 C  CE  . LYS B 2 40   ? -19.722 -4.874  20.325  1.00 246.49 ? 168  LYS X CE  1 
ATOM   11856 N  NZ  . LYS B 2 40   ? -18.534 -5.084  19.448  1.00 251.18 ? 168  LYS X NZ  1 
ATOM   11857 N  N   . ILE B 2 41   ? -23.680 0.734   22.140  1.00 236.20 ? 169  ILE X N   1 
ATOM   11858 C  CA  . ILE B 2 41   ? -23.875 2.187   22.229  1.00 232.33 ? 169  ILE X CA  1 
ATOM   11859 C  C   . ILE B 2 41   ? -23.856 2.690   23.684  1.00 228.53 ? 169  ILE X C   1 
ATOM   11860 O  O   . ILE B 2 41   ? -23.038 3.536   24.059  1.00 230.17 ? 169  ILE X O   1 
ATOM   11861 C  CB  . ILE B 2 41   ? -25.193 2.625   21.516  1.00 227.39 ? 169  ILE X CB  1 
ATOM   11862 C  CG1 . ILE B 2 41   ? -25.173 2.235   20.032  1.00 228.43 ? 169  ILE X CG1 1 
ATOM   11863 C  CG2 . ILE B 2 41   ? -25.431 4.124   21.673  1.00 226.48 ? 169  ILE X CG2 1 
ATOM   11864 C  CD1 . ILE B 2 41   ? -24.074 2.896   19.224  1.00 229.22 ? 169  ILE X CD1 1 
ATOM   11865 N  N   . ARG B 2 42   ? -24.754 2.153   24.500  1.00 299.26 ? 170  ARG X N   1 
ATOM   11866 C  CA  . ARG B 2 42   ? -24.796 2.507   25.910  1.00 296.36 ? 170  ARG X CA  1 
ATOM   11867 C  C   . ARG B 2 42   ? -23.541 2.054   26.668  1.00 291.62 ? 170  ARG X C   1 
ATOM   11868 O  O   . ARG B 2 42   ? -23.107 2.732   27.592  1.00 288.85 ? 170  ARG X O   1 
ATOM   11869 C  CB  . ARG B 2 42   ? -26.059 1.952   26.580  1.00 297.86 ? 170  ARG X CB  1 
ATOM   11870 C  CG  . ARG B 2 42   ? -26.198 0.432   26.529  1.00 305.81 ? 170  ARG X CG  1 
ATOM   11871 C  CD  . ARG B 2 42   ? -27.409 -0.042  27.334  1.00 307.72 ? 170  ARG X CD  1 
ATOM   11872 N  NE  . ARG B 2 42   ? -27.780 -1.424  27.029  1.00 314.10 ? 170  ARG X NE  1 
ATOM   11873 C  CZ  . ARG B 2 42   ? -28.822 -2.054  27.565  1.00 314.21 ? 170  ARG X CZ  1 
ATOM   11874 N  NH1 . ARG B 2 42   ? -29.599 -1.432  28.440  1.00 310.81 ? 170  ARG X NH1 1 
ATOM   11875 N  NH2 . ARG B 2 42   ? -29.088 -3.308  27.228  1.00 316.84 ? 170  ARG X NH2 1 
ATOM   11876 N  N   . GLN B 2 43   ? -22.961 0.918   26.280  1.00 238.55 ? 171  GLN X N   1 
ATOM   11877 C  CA  . GLN B 2 43   ? -21.783 0.374   26.970  1.00 236.04 ? 171  GLN X CA  1 
ATOM   11878 C  C   . GLN B 2 43   ? -20.688 1.437   27.075  1.00 236.58 ? 171  GLN X C   1 
ATOM   11879 O  O   . GLN B 2 43   ? -20.056 1.607   28.127  1.00 232.78 ? 171  GLN X O   1 
ATOM   11880 C  CB  . GLN B 2 43   ? -21.248 -0.863  26.230  1.00 237.08 ? 171  GLN X CB  1 
ATOM   11881 C  CG  . GLN B 2 43   ? -20.178 -1.673  26.973  1.00 233.41 ? 171  GLN X CG  1 
ATOM   11882 C  CD  . GLN B 2 43   ? -19.460 -2.667  26.073  1.00 234.42 ? 171  GLN X CD  1 
ATOM   11883 O  OE1 . GLN B 2 43   ? -18.955 -2.305  25.011  1.00 237.84 ? 171  GLN X OE1 1 
ATOM   11884 N  NE2 . GLN B 2 43   ? -19.407 -3.925  26.497  1.00 231.48 ? 171  GLN X NE2 1 
ATOM   11885 N  N   . HIS B 2 44   ? -20.490 2.150   25.968  1.00 419.30 ? 172  HIS X N   1 
ATOM   11886 C  CA  . HIS B 2 44   ? -19.488 3.206   25.853  1.00 420.10 ? 172  HIS X CA  1 
ATOM   11887 C  C   . HIS B 2 44   ? -19.904 4.494   26.540  1.00 421.03 ? 172  HIS X C   1 
ATOM   11888 O  O   . HIS B 2 44   ? -19.171 5.024   27.368  1.00 420.25 ? 172  HIS X O   1 
ATOM   11889 C  CB  . HIS B 2 44   ? -19.191 3.490   24.384  1.00 251.84 ? 172  HIS X CB  1 
ATOM   11890 C  CG  . HIS B 2 44   ? -18.501 2.358   23.680  1.00 253.74 ? 172  HIS X CG  1 
ATOM   11891 N  ND1 . HIS B 2 44   ? -19.054 1.702   22.616  1.00 256.45 ? 172  HIS X ND1 1 
ATOM   11892 C  CD2 . HIS B 2 44   ? -17.302 1.771   23.922  1.00 253.31 ? 172  HIS X CD2 1 
ATOM   11893 C  CE1 . HIS B 2 44   ? -18.217 0.751   22.206  1.00 257.72 ? 172  HIS X CE1 1 
ATOM   11894 N  NE2 . HIS B 2 44   ? -17.158 0.775   22.980  1.00 255.81 ? 172  HIS X NE2 1 
ATOM   11895 N  N   . LEU B 2 45   ? -21.072 5.008   26.177  1.00 232.24 ? 173  LEU X N   1 
ATOM   11896 C  CA  . LEU B 2 45   ? -21.639 6.136   26.898  1.00 231.84 ? 173  LEU X CA  1 
ATOM   11897 C  C   . LEU B 2 45   ? -21.487 5.897   28.407  1.00 228.12 ? 173  LEU X C   1 
ATOM   11898 O  O   . LEU B 2 45   ? -21.164 6.815   29.169  1.00 228.49 ? 173  LEU X O   1 
ATOM   11899 C  CB  . LEU B 2 45   ? -23.114 6.289   26.532  1.00 232.23 ? 173  LEU X CB  1 
ATOM   11900 C  CG  . LEU B 2 45   ? -23.375 6.387   25.034  1.00 237.82 ? 173  LEU X CG  1 
ATOM   11901 C  CD1 . LEU B 2 45   ? -24.849 6.185   24.712  1.00 238.55 ? 173  LEU X CD1 1 
ATOM   11902 C  CD2 . LEU B 2 45   ? -22.873 7.725   24.532  1.00 242.11 ? 173  LEU X CD2 1 
ATOM   11903 N  N   . VAL B 2 46   ? -21.715 4.648   28.816  1.00 252.24 ? 174  VAL X N   1 
ATOM   11904 C  CA  . VAL B 2 46   ? -21.645 4.240   30.218  1.00 246.25 ? 174  VAL X CA  1 
ATOM   11905 C  C   . VAL B 2 46   ? -20.209 4.230   30.701  1.00 246.15 ? 174  VAL X C   1 
ATOM   11906 O  O   . VAL B 2 46   ? -19.924 4.480   31.866  1.00 242.92 ? 174  VAL X O   1 
ATOM   11907 C  CB  . VAL B 2 46   ? -22.272 2.845   30.445  1.00 250.18 ? 174  VAL X CB  1 
ATOM   11908 C  CG1 . VAL B 2 46   ? -21.740 2.214   31.721  1.00 246.88 ? 174  VAL X CG1 1 
ATOM   11909 C  CG2 . VAL B 2 46   ? -23.788 2.951   30.481  1.00 249.20 ? 174  VAL X CG2 1 
ATOM   11910 N  N   . LYS B 2 47   ? -19.282 3.966   29.802  1.00 394.56 ? 175  LYS X N   1 
ATOM   11911 C  CA  . LYS B 2 47   ? -17.899 3.913   30.230  1.00 392.71 ? 175  LYS X CA  1 
ATOM   11912 C  C   . LYS B 2 47   ? -17.129 5.175   29.870  1.00 392.86 ? 175  LYS X C   1 
ATOM   11913 O  O   . LYS B 2 47   ? -15.950 5.292   30.217  1.00 393.17 ? 175  LYS X O   1 
ATOM   11914 C  CB  . LYS B 2 47   ? -17.190 2.723   29.585  1.00 393.46 ? 175  LYS X CB  1 
ATOM   11915 C  CG  . LYS B 2 47   ? -17.572 1.338   30.147  1.00 389.08 ? 175  LYS X CG  1 
ATOM   11916 C  CD  . LYS B 2 47   ? -16.681 0.297   29.626  1.00 167.92 ? 175  LYS X CD  1 
ATOM   11917 C  CE  . LYS B 2 47   ? -16.673 -0.940  30.471  1.00 167.96 ? 175  LYS X CE  1 
ATOM   11918 N  NZ  . LYS B 2 47   ? -16.593 -0.820  31.938  1.00 167.69 ? 175  LYS X NZ  1 
ATOM   11919 N  N   . ASN B 2 48   ? -17.768 6.089   29.134  1.00 275.61 ? 176  ASN X N   1 
ATOM   11920 C  CA  . ASN B 2 48   ? -17.067 7.261   28.592  1.00 276.37 ? 176  ASN X CA  1 
ATOM   11921 C  C   . ASN B 2 48   ? -17.747 8.638   28.707  1.00 272.41 ? 176  ASN X C   1 
ATOM   11922 O  O   . ASN B 2 48   ? -17.080 9.638   28.975  1.00 273.69 ? 176  ASN X O   1 
ATOM   11923 C  CB  . ASN B 2 48   ? -16.688 7.019   27.130  1.00 281.21 ? 176  ASN X CB  1 
ATOM   11924 C  CG  . ASN B 2 48   ? -15.840 5.788   26.950  1.00 280.92 ? 176  ASN X CG  1 
ATOM   11925 O  OD1 . ASN B 2 48   ? -14.639 5.883   26.714  1.00 283.13 ? 176  ASN X OD1 1 
ATOM   11926 N  ND2 . ASN B 2 48   ? -16.458 4.617   27.070  1.00 278.19 ? 176  ASN X ND2 1 
ATOM   11927 N  N   . TYR B 2 49   ? -19.053 8.710   28.475  1.00 206.30 ? 177  TYR X N   1 
ATOM   11928 C  CA  . TYR B 2 49   ? -19.724 10.012  28.450  1.00 206.65 ? 177  TYR X CA  1 
ATOM   11929 C  C   . TYR B 2 49   ? -20.652 10.218  29.628  1.00 206.86 ? 177  TYR X C   1 
ATOM   11930 O  O   . TYR B 2 49   ? -21.613 10.984  29.554  1.00 209.41 ? 177  TYR X O   1 
ATOM   11931 C  CB  . TYR B 2 49   ? -20.459 10.237  27.122  1.00 204.10 ? 177  TYR X CB  1 
ATOM   11932 C  CG  . TYR B 2 49   ? -19.491 10.475  25.990  1.00 204.04 ? 177  TYR X CG  1 
ATOM   11933 C  CD1 . TYR B 2 49   ? -19.073 9.427   25.171  1.00 202.92 ? 177  TYR X CD1 1 
ATOM   11934 C  CD2 . TYR B 2 49   ? -18.948 11.737  25.769  1.00 205.32 ? 177  TYR X CD2 1 
ATOM   11935 C  CE1 . TYR B 2 49   ? -18.157 9.637   24.145  1.00 205.48 ? 177  TYR X CE1 1 
ATOM   11936 C  CE2 . TYR B 2 49   ? -18.034 11.957  24.747  1.00 208.44 ? 177  TYR X CE2 1 
ATOM   11937 C  CZ  . TYR B 2 49   ? -17.643 10.903  23.941  1.00 207.82 ? 177  TYR X CZ  1 
ATOM   11938 O  OH  . TYR B 2 49   ? -16.736 11.117  22.932  1.00 210.63 ? 177  TYR X OH  1 
ATOM   11939 N  N   . GLY B 2 50   ? -20.354 9.531   30.719  1.00 257.60 ? 178  GLY X N   1 
ATOM   11940 C  CA  . GLY B 2 50   ? -21.157 9.646   31.915  1.00 257.65 ? 178  GLY X CA  1 
ATOM   11941 C  C   . GLY B 2 50   ? -22.616 9.388   31.614  1.00 261.68 ? 178  GLY X C   1 
ATOM   11942 O  O   . GLY B 2 50   ? -23.396 10.324  31.420  1.00 261.07 ? 178  GLY X O   1 
ATOM   11943 N  N   . LEU B 2 51   ? -22.975 8.110   31.540  1.00 240.56 ? 179  LEU X N   1 
ATOM   11944 C  CA  . LEU B 2 51   ? -24.378 7.714   31.486  1.00 245.60 ? 179  LEU X CA  1 
ATOM   11945 C  C   . LEU B 2 51   ? -24.689 6.746   32.619  1.00 247.18 ? 179  LEU X C   1 
ATOM   11946 O  O   . LEU B 2 51   ? -23.853 5.920   32.991  1.00 245.49 ? 179  LEU X O   1 
ATOM   11947 C  CB  . LEU B 2 51   ? -24.746 7.082   30.144  1.00 247.56 ? 179  LEU X CB  1 
ATOM   11948 C  CG  . LEU B 2 51   ? -26.124 6.410   30.171  1.00 244.80 ? 179  LEU X CG  1 
ATOM   11949 C  CD1 . LEU B 2 51   ? -27.220 7.418   30.494  1.00 245.18 ? 179  LEU X CD1 1 
ATOM   11950 C  CD2 . LEU B 2 51   ? -26.407 5.711   28.860  1.00 246.48 ? 179  LEU X CD2 1 
ATOM   11951 N  N   . TYR B 2 52   ? -25.900 6.851   33.158  1.00 272.10 ? 180  TYR X N   1 
ATOM   11952 C  CA  . TYR B 2 52   ? -26.308 6.040   34.295  1.00 274.63 ? 180  TYR X CA  1 
ATOM   11953 C  C   . TYR B 2 52   ? -25.491 6.345   35.550  1.00 277.95 ? 180  TYR X C   1 
ATOM   11954 O  O   . TYR B 2 52   ? -25.500 5.564   36.502  1.00 276.39 ? 180  TYR X O   1 
ATOM   11955 C  CB  . TYR B 2 52   ? -26.222 4.554   33.958  1.00 275.03 ? 180  TYR X CB  1 
ATOM   11956 C  CG  . TYR B 2 52   ? -27.323 4.091   33.050  1.00 278.68 ? 180  TYR X CG  1 
ATOM   11957 C  CD1 . TYR B 2 52   ? -28.615 4.560   33.216  1.00 279.88 ? 180  TYR X CD1 1 
ATOM   11958 C  CD2 . TYR B 2 52   ? -27.077 3.179   32.037  1.00 280.58 ? 180  TYR X CD2 1 
ATOM   11959 C  CE1 . TYR B 2 52   ? -29.630 4.141   32.397  1.00 282.00 ? 180  TYR X CE1 1 
ATOM   11960 C  CE2 . TYR B 2 52   ? -28.087 2.750   31.211  1.00 282.69 ? 180  TYR X CE2 1 
ATOM   11961 C  CZ  . TYR B 2 52   ? -29.363 3.234   31.395  1.00 283.05 ? 180  TYR X CZ  1 
ATOM   11962 O  OH  . TYR B 2 52   ? -30.379 2.808   30.573  1.00 284.77 ? 180  TYR X OH  1 
ATOM   11963 N  N   . LYS B 2 53   ? -24.778 7.471   35.538  1.00 267.47 ? 181  LYS X N   1 
ATOM   11964 C  CA  . LYS B 2 53   ? -24.040 7.934   36.712  1.00 269.02 ? 181  LYS X CA  1 
ATOM   11965 C  C   . LYS B 2 53   ? -24.458 9.363   37.078  1.00 269.45 ? 181  LYS X C   1 
ATOM   11966 O  O   . LYS B 2 53   ? -23.807 10.335  36.687  1.00 271.67 ? 181  LYS X O   1 
ATOM   11967 C  CB  . LYS B 2 53   ? -22.519 7.861   36.491  1.00 275.21 ? 181  LYS X CB  1 
ATOM   11968 C  CG  . LYS B 2 53   ? -21.985 6.527   35.953  1.00 276.50 ? 181  LYS X CG  1 
ATOM   11969 C  CD  . LYS B 2 53   ? -22.353 5.329   36.834  1.00 279.11 ? 181  LYS X CD  1 
ATOM   11970 C  CE  . LYS B 2 53   ? -21.677 5.352   38.203  1.00 278.49 ? 181  LYS X CE  1 
ATOM   11971 N  NZ  . LYS B 2 53   ? -22.141 4.215   39.057  1.00 278.78 ? 181  LYS X NZ  1 
ATOM   11972 N  N   . GLY B 2 54   ? -25.547 9.479   37.833  1.00 278.56 ? 182  GLY X N   1 
ATOM   11973 C  CA  . GLY B 2 54   ? -26.064 10.773  38.238  1.00 278.20 ? 182  GLY X CA  1 
ATOM   11974 C  C   . GLY B 2 54   ? -27.321 11.142  37.477  1.00 277.00 ? 182  GLY X C   1 
ATOM   11975 O  O   . GLY B 2 54   ? -28.175 10.289  37.215  1.00 273.36 ? 182  GLY X O   1 
ATOM   11976 N  N   . THR B 2 55   ? -27.433 12.419  37.127  1.00 274.91 ? 183  THR X N   1 
ATOM   11977 C  CA  . THR B 2 55   ? -28.590 12.923  36.395  1.00 275.97 ? 183  THR X CA  1 
ATOM   11978 C  C   . THR B 2 55   ? -28.649 12.371  34.968  1.00 283.14 ? 183  THR X C   1 
ATOM   11979 O  O   . THR B 2 55   ? -29.508 12.720  34.183  1.00 285.95 ? 183  THR X O   1 
ATOM   11980 C  CB  . THR B 2 55   ? -28.590 14.451  36.381  1.00 270.29 ? 183  THR X CB  1 
ATOM   11981 O  OG1 . THR B 2 55   ? -27.254 14.918  36.155  1.00 273.40 ? 183  THR X OG1 1 
ATOM   11982 C  CG2 . THR B 2 55   ? -29.083 14.972  37.703  1.00 265.54 ? 183  THR X CG2 1 
ATOM   11983 N  N   . THR B 2 56   ? -27.722 11.493  34.634  1.00 410.91 ? 184  THR X N   1 
ATOM   11984 C  CA  . THR B 2 56   ? -27.730 10.910  33.302  1.00 415.17 ? 184  THR X CA  1 
ATOM   11985 C  C   . THR B 2 56   ? -28.517 9.609   33.184  1.00 414.60 ? 184  THR X C   1 
ATOM   11986 O  O   . THR B 2 56   ? -28.297 8.641   33.926  1.00 411.21 ? 184  THR X O   1 
ATOM   11987 C  CB  . THR B 2 56   ? -26.313 10.664  32.798  1.00 416.32 ? 184  THR X CB  1 
ATOM   11988 O  OG1 . THR B 2 56   ? -25.372 11.034  33.830  1.00 156.10 ? 184  THR X OG1 1 
ATOM   11989 C  CG2 . THR B 2 56   ? -26.038 11.460  31.420  1.00 155.95 ? 184  THR X CG2 1 
ATOM   11990 N  N   . LYS B 2 57   ? -29.422 9.598   32.212  1.00 262.50 ? 185  LYS X N   1 
ATOM   11991 C  CA  . LYS B 2 57   ? -30.229 8.418   31.921  1.00 261.90 ? 185  LYS X CA  1 
ATOM   11992 C  C   . LYS B 2 57   ? -31.297 8.669   30.846  1.00 261.32 ? 185  LYS X C   1 
ATOM   11993 O  O   . LYS B 2 57   ? -31.713 7.739   30.148  1.00 261.69 ? 185  LYS X O   1 
ATOM   11994 C  CB  . LYS B 2 57   ? -30.867 7.860   33.204  1.00 261.30 ? 185  LYS X CB  1 
ATOM   11995 C  CG  . LYS B 2 57   ? -31.735 8.858   33.943  1.00 262.32 ? 185  LYS X CG  1 
ATOM   11996 C  CD  . LYS B 2 57   ? -32.329 8.296   35.222  1.00 258.02 ? 185  LYS X CD  1 
ATOM   11997 C  CE  . LYS B 2 57   ? -31.354 8.401   36.386  1.00 256.97 ? 185  LYS X CE  1 
ATOM   11998 N  NZ  . LYS B 2 57   ? -32.029 8.230   37.706  1.00 251.69 ? 185  LYS X NZ  1 
ATOM   11999 N  N   . TYR B 2 58   ? -31.741 9.917   30.713  1.00 271.96 ? 186  TYR X N   1 
ATOM   12000 C  CA  . TYR B 2 58   ? -32.810 10.247  29.767  1.00 271.92 ? 186  TYR X CA  1 
ATOM   12001 C  C   . TYR B 2 58   ? -32.320 10.882  28.464  1.00 273.16 ? 186  TYR X C   1 
ATOM   12002 O  O   . TYR B 2 58   ? -31.789 11.994  28.465  1.00 273.83 ? 186  TYR X O   1 
ATOM   12003 C  CB  . TYR B 2 58   ? -33.841 11.163  30.423  1.00 269.38 ? 186  TYR X CB  1 
ATOM   12004 C  CG  . TYR B 2 58   ? -34.972 11.539  29.497  1.00 264.06 ? 186  TYR X CG  1 
ATOM   12005 C  CD1 . TYR B 2 58   ? -36.092 10.729  29.374  1.00 260.07 ? 186  TYR X CD1 1 
ATOM   12006 C  CD2 . TYR B 2 58   ? -34.916 12.699  28.736  1.00 264.25 ? 186  TYR X CD2 1 
ATOM   12007 C  CE1 . TYR B 2 58   ? -37.130 11.067  28.522  1.00 256.01 ? 186  TYR X CE1 1 
ATOM   12008 C  CE2 . TYR B 2 58   ? -35.951 13.047  27.884  1.00 260.22 ? 186  TYR X CE2 1 
ATOM   12009 C  CZ  . TYR B 2 58   ? -37.055 12.227  27.781  1.00 256.16 ? 186  TYR X CZ  1 
ATOM   12010 O  OH  . TYR B 2 58   ? -38.086 12.567  26.933  1.00 252.05 ? 186  TYR X OH  1 
ATOM   12011 N  N   . GLY B 2 59   ? -32.537 10.186  27.352  1.00 262.05 ? 187  GLY X N   1 
ATOM   12012 C  CA  . GLY B 2 59   ? -32.081 10.664  26.057  1.00 263.89 ? 187  GLY X CA  1 
ATOM   12013 C  C   . GLY B 2 59   ? -32.607 9.849   24.887  1.00 263.27 ? 187  GLY X C   1 
ATOM   12014 O  O   . GLY B 2 59   ? -33.457 8.975   25.062  1.00 260.22 ? 187  GLY X O   1 
ATOM   12015 N  N   . LYS B 2 60   ? -32.098 10.136  23.690  1.00 257.04 ? 188  LYS X N   1 
ATOM   12016 C  CA  . LYS B 2 60   ? -32.547 9.460   22.474  1.00 260.73 ? 188  LYS X CA  1 
ATOM   12017 C  C   . LYS B 2 60   ? -31.417 9.320   21.459  1.00 263.07 ? 188  LYS X C   1 
ATOM   12018 O  O   . LYS B 2 60   ? -30.908 10.311  20.938  1.00 268.12 ? 188  LYS X O   1 
ATOM   12019 C  CB  . LYS B 2 60   ? -33.716 10.218  21.840  1.00 264.75 ? 188  LYS X CB  1 
ATOM   12020 C  CG  . LYS B 2 60   ? -35.014 10.170  22.634  1.00 262.58 ? 188  LYS X CG  1 
ATOM   12021 C  CD  . LYS B 2 60   ? -35.661 8.799   22.545  1.00 261.44 ? 188  LYS X CD  1 
ATOM   12022 C  CE  . LYS B 2 60   ? -37.054 8.804   23.151  1.00 259.04 ? 188  LYS X CE  1 
ATOM   12023 N  NZ  . LYS B 2 60   ? -37.028 9.042   24.617  1.00 252.69 ? 188  LYS X NZ  1 
ATOM   12024 N  N   . ILE B 2 61   ? -31.036 8.077   21.187  1.00 387.22 ? 189  ILE X N   1 
ATOM   12025 C  CA  . ILE B 2 61   ? -29.992 7.773   20.215  1.00 388.80 ? 189  ILE X CA  1 
ATOM   12026 C  C   . ILE B 2 61   ? -30.584 7.744   18.804  1.00 393.76 ? 189  ILE X C   1 
ATOM   12027 O  O   . ILE B 2 61   ? -31.537 7.015   18.549  1.00 393.77 ? 189  ILE X O   1 
ATOM   12028 C  CB  . ILE B 2 61   ? -29.342 6.407   20.523  1.00 384.30 ? 189  ILE X CB  1 
ATOM   12029 C  CG1 . ILE B 2 61   ? -29.186 6.211   22.036  1.00 377.83 ? 189  ILE X CG1 1 
ATOM   12030 C  CG2 . ILE B 2 61   ? -28.005 6.272   19.813  1.00 386.97 ? 189  ILE X CG2 1 
ATOM   12031 C  CD1 . ILE B 2 61   ? -28.695 4.832   22.427  1.00 374.56 ? 189  ILE X CD1 1 
ATOM   12032 N  N   . THR B 2 62   ? -30.016 8.522   17.886  1.00 482.62 ? 190  THR X N   1 
ATOM   12033 C  CA  . THR B 2 62   ? -30.577 8.630   16.538  1.00 489.40 ? 190  THR X CA  1 
ATOM   12034 C  C   . THR B 2 62   ? -29.674 8.039   15.453  1.00 494.76 ? 190  THR X C   1 
ATOM   12035 O  O   . THR B 2 62   ? -28.754 8.700   14.973  1.00 497.79 ? 190  THR X O   1 
ATOM   12036 C  CB  . THR B 2 62   ? -30.880 10.094  16.181  1.00 292.03 ? 190  THR X CB  1 
ATOM   12037 O  OG1 . THR B 2 62   ? -29.653 10.794  15.939  1.00 295.34 ? 190  THR X OG1 1 
ATOM   12038 C  CG2 . THR B 2 62   ? -31.624 10.769  17.319  1.00 288.42 ? 190  THR X CG2 1 
ATOM   12039 N  N   . ILE B 2 63   ? -29.952 6.798   15.060  1.00 385.64 ? 191  ILE X N   1 
ATOM   12040 C  CA  . ILE B 2 63   ? -29.158 6.121   14.035  1.00 392.49 ? 191  ILE X CA  1 
ATOM   12041 C  C   . ILE B 2 63   ? -29.468 6.655   12.644  1.00 401.80 ? 191  ILE X C   1 
ATOM   12042 O  O   . ILE B 2 63   ? -30.625 6.677   12.228  1.00 405.01 ? 191  ILE X O   1 
ATOM   12043 C  CB  . ILE B 2 63   ? -29.407 4.590   14.008  1.00 337.32 ? 191  ILE X CB  1 
ATOM   12044 C  CG1 . ILE B 2 63   ? -29.386 3.993   15.414  1.00 326.77 ? 191  ILE X CG1 1 
ATOM   12045 C  CG2 . ILE B 2 63   ? -28.379 3.895   13.120  1.00 341.14 ? 191  ILE X CG2 1 
ATOM   12046 C  CD1 . ILE B 2 63   ? -29.534 2.475   15.435  1.00 321.31 ? 191  ILE X CD1 1 
ATOM   12047 N  N   . ASN B 2 64   ? -28.433 7.081   11.926  1.00 364.61 ? 192  ASN X N   1 
ATOM   12048 C  CA  . ASN B 2 64   ? -28.575 7.416   10.512  1.00 371.43 ? 192  ASN X CA  1 
ATOM   12049 C  C   . ASN B 2 64   ? -28.356 6.179   9.641   1.00 374.96 ? 192  ASN X C   1 
ATOM   12050 O  O   . ASN B 2 64   ? -27.459 5.381   9.910   1.00 372.16 ? 192  ASN X O   1 
ATOM   12051 C  CB  . ASN B 2 64   ? -27.601 8.527   10.107  1.00 373.79 ? 192  ASN X CB  1 
ATOM   12052 C  CG  . ASN B 2 64   ? -27.885 9.841   10.810  1.00 375.56 ? 192  ASN X CG  1 
ATOM   12053 O  OD1 . ASN B 2 64   ? -28.899 9.987   11.492  1.00 376.27 ? 192  ASN X OD1 1 
ATOM   12054 N  ND2 . ASN B 2 64   ? -26.985 10.806  10.645  1.00 376.13 ? 192  ASN X ND2 1 
ATOM   12055 N  N   . LEU B 2 65   ? -29.170 6.026   8.599   1.00 531.37 ? 193  LEU X N   1 
ATOM   12056 C  CA  . LEU B 2 65   ? -29.084 4.861   7.717   1.00 532.51 ? 193  LEU X CA  1 
ATOM   12057 C  C   . LEU B 2 65   ? -29.178 5.239   6.232   1.00 536.58 ? 193  LEU X C   1 
ATOM   12058 O  O   . LEU B 2 65   ? -28.502 4.644   5.391   1.00 536.65 ? 193  LEU X O   1 
ATOM   12059 C  CB  . LEU B 2 65   ? -30.167 3.832   8.079   1.00 529.87 ? 193  LEU X CB  1 
ATOM   12060 C  CG  . LEU B 2 65   ? -30.154 3.234   9.494   1.00 526.00 ? 193  LEU X CG  1 
ATOM   12061 C  CD1 . LEU B 2 65   ? -31.471 2.538   9.816   1.00 524.49 ? 193  LEU X CD1 1 
ATOM   12062 C  CD2 . LEU B 2 65   ? -28.982 2.280   9.684   1.00 524.01 ? 193  LEU X CD2 1 
ATOM   12063 N  N   . LYS B 2 66   ? -30.009 6.232   5.919   1.00 325.20 ? 194  LYS X N   1 
ATOM   12064 C  CA  . LYS B 2 66   ? -30.186 6.701   4.541   1.00 332.38 ? 194  LYS X CA  1 
ATOM   12065 C  C   . LYS B 2 66   ? -30.726 8.136   4.517   1.00 335.04 ? 194  LYS X C   1 
ATOM   12066 O  O   . LYS B 2 66   ? -31.036 8.702   5.565   1.00 331.73 ? 194  LYS X O   1 
ATOM   12067 C  CB  . LYS B 2 66   ? -31.109 5.762   3.760   1.00 337.29 ? 194  LYS X CB  1 
ATOM   12068 C  CG  . LYS B 2 66   ? -31.072 5.983   2.262   1.00 344.75 ? 194  LYS X CG  1 
ATOM   12069 C  CD  . LYS B 2 66   ? -29.648 5.909   1.751   1.00 352.44 ? 194  LYS X CD  1 
ATOM   12070 C  CE  . LYS B 2 66   ? -29.544 6.495   0.365   1.00 359.39 ? 194  LYS X CE  1 
ATOM   12071 N  NZ  . LYS B 2 66   ? -30.016 7.903   0.357   1.00 363.88 ? 194  LYS X NZ  1 
ATOM   12072 N  N   . ASP B 2 67   ? -30.844 8.721   3.325   1.00 234.44 ? 195  ASP X N   1 
ATOM   12073 C  CA  . ASP B 2 67   ? -31.196 10.139  3.192   1.00 237.55 ? 195  ASP X CA  1 
ATOM   12074 C  C   . ASP B 2 67   ? -32.598 10.530  3.682   1.00 244.03 ? 195  ASP X C   1 
ATOM   12075 O  O   . ASP B 2 67   ? -33.104 11.596  3.330   1.00 247.95 ? 195  ASP X O   1 
ATOM   12076 C  CB  . ASP B 2 67   ? -30.979 10.619  1.753   1.00 234.78 ? 195  ASP X CB  1 
ATOM   12077 C  CG  . ASP B 2 67   ? -29.544 11.047  1.489   1.00 226.79 ? 195  ASP X CG  1 
ATOM   12078 O  OD1 . ASP B 2 67   ? -29.130 12.096  2.022   1.00 223.07 ? 195  ASP X OD1 1 
ATOM   12079 O  OD2 . ASP B 2 67   ? -28.832 10.341  0.747   1.00 225.35 ? 195  ASP X OD2 1 
ATOM   12080 N  N   . GLY B 2 68   ? -33.217 9.685   4.501   1.00 386.21 ? 196  GLY X N   1 
ATOM   12081 C  CA  . GLY B 2 68   ? -34.547 9.984   5.002   1.00 391.92 ? 196  GLY X CA  1 
ATOM   12082 C  C   . GLY B 2 68   ? -35.034 9.140   6.166   1.00 382.99 ? 196  GLY X C   1 
ATOM   12083 O  O   . GLY B 2 68   ? -36.220 9.169   6.498   1.00 383.50 ? 196  GLY X O   1 
ATOM   12084 N  N   . GLU B 2 69   ? -34.134 8.393   6.796   1.00 518.22 ? 197  GLU X N   1 
ATOM   12085 C  CA  . GLU B 2 69   ? -34.540 7.523   7.893   1.00 514.91 ? 197  GLU X CA  1 
ATOM   12086 C  C   . GLU B 2 69   ? -33.903 7.897   9.225   1.00 513.66 ? 197  GLU X C   1 
ATOM   12087 O  O   . GLU B 2 69   ? -32.678 7.953   9.343   1.00 514.71 ? 197  GLU X O   1 
ATOM   12088 C  CB  . GLU B 2 69   ? -34.236 6.073   7.543   1.00 304.62 ? 197  GLU X CB  1 
ATOM   12089 C  CG  . GLU B 2 69   ? -35.062 5.079   8.295   1.00 302.58 ? 197  GLU X CG  1 
ATOM   12090 C  CD  . GLU B 2 69   ? -35.108 3.757   7.587   1.00 301.75 ? 197  GLU X CD  1 
ATOM   12091 O  OE1 . GLU B 2 69   ? -34.948 3.755   6.350   1.00 302.84 ? 197  GLU X OE1 1 
ATOM   12092 O  OE2 . GLU B 2 69   ? -35.289 2.724   8.264   1.00 300.15 ? 197  GLU X OE2 1 
ATOM   12093 N  N   . LYS B 2 70   ? -34.751 8.131   10.224  1.00 281.82 ? 198  LYS X N   1 
ATOM   12094 C  CA  . LYS B 2 70   ? -34.307 8.588   11.538  1.00 270.81 ? 198  LYS X CA  1 
ATOM   12095 C  C   . LYS B 2 70   ? -35.097 7.923   12.674  1.00 263.86 ? 198  LYS X C   1 
ATOM   12096 O  O   . LYS B 2 70   ? -36.299 8.159   12.830  1.00 264.82 ? 198  LYS X O   1 
ATOM   12097 C  CB  . LYS B 2 70   ? -34.423 10.117  11.639  1.00 266.64 ? 198  LYS X CB  1 
ATOM   12098 C  CG  . LYS B 2 70   ? -33.649 10.893  10.581  1.00 263.66 ? 198  LYS X CG  1 
ATOM   12099 C  CD  . LYS B 2 70   ? -33.481 12.365  10.958  1.00 258.47 ? 198  LYS X CD  1 
ATOM   12100 C  CE  . LYS B 2 70   ? -34.766 13.161  10.794  1.00 256.29 ? 198  LYS X CE  1 
ATOM   12101 N  NZ  . LYS B 2 70   ? -35.138 13.307  9.368   1.00 253.44 ? 198  LYS X NZ  1 
ATOM   12102 N  N   . GLN B 2 71   ? -34.401 7.108   13.468  1.00 485.11 ? 199  GLN X N   1 
ATOM   12103 C  CA  . GLN B 2 71   ? -35.010 6.333   14.551  1.00 477.60 ? 199  GLN X CA  1 
ATOM   12104 C  C   . GLN B 2 71   ? -34.194 6.436   15.846  1.00 469.63 ? 199  GLN X C   1 
ATOM   12105 O  O   . GLN B 2 71   ? -33.059 6.917   15.828  1.00 468.94 ? 199  GLN X O   1 
ATOM   12106 C  CB  . GLN B 2 71   ? -35.175 4.865   14.127  1.00 269.39 ? 199  GLN X CB  1 
ATOM   12107 C  CG  . GLN B 2 71   ? -34.134 4.383   13.111  1.00 274.43 ? 199  GLN X CG  1 
ATOM   12108 C  CD  . GLN B 2 71   ? -34.161 2.874   12.893  1.00 273.92 ? 199  GLN X CD  1 
ATOM   12109 O  OE1 . GLN B 2 71   ? -33.931 2.098   13.816  1.00 270.50 ? 199  GLN X OE1 1 
ATOM   12110 N  NE2 . GLN B 2 71   ? -34.430 2.458   11.663  1.00 274.86 ? 199  GLN X NE2 1 
ATOM   12111 N  N   . GLU B 2 72   ? -34.768 5.963   16.957  1.00 363.01 ? 200  GLU X N   1 
ATOM   12112 C  CA  . GLU B 2 72   ? -34.172 6.129   18.289  1.00 354.33 ? 200  GLU X CA  1 
ATOM   12113 C  C   . GLU B 2 72   ? -34.437 4.963   19.250  1.00 347.08 ? 200  GLU X C   1 
ATOM   12114 O  O   . GLU B 2 72   ? -35.226 4.067   18.958  1.00 344.96 ? 200  GLU X O   1 
ATOM   12115 C  CB  . GLU B 2 72   ? -34.685 7.418   18.937  1.00 353.85 ? 200  GLU X CB  1 
ATOM   12116 C  CG  . GLU B 2 72   ? -34.666 8.622   18.022  1.00 358.75 ? 200  GLU X CG  1 
ATOM   12117 C  CD  . GLU B 2 72   ? -35.628 9.706   18.469  1.00 359.47 ? 200  GLU X CD  1 
ATOM   12118 O  OE1 . GLU B 2 72   ? -36.055 9.688   19.645  1.00 355.28 ? 200  GLU X OE1 1 
ATOM   12119 O  OE2 . GLU B 2 72   ? -35.955 10.579  17.640  1.00 364.65 ? 200  GLU X OE2 1 
ATOM   12120 N  N   . ILE B 2 73   ? -33.783 5.004   20.409  1.00 322.86 ? 201  ILE X N   1 
ATOM   12121 C  CA  . ILE B 2 73   ? -33.990 4.026   21.477  1.00 316.92 ? 201  ILE X CA  1 
ATOM   12122 C  C   . ILE B 2 73   ? -34.001 4.752   22.809  1.00 316.49 ? 201  ILE X C   1 
ATOM   12123 O  O   . ILE B 2 73   ? -32.949 5.171   23.300  1.00 315.68 ? 201  ILE X O   1 
ATOM   12124 C  CB  . ILE B 2 73   ? -32.858 2.991   21.533  1.00 310.23 ? 201  ILE X CB  1 
ATOM   12125 C  CG1 . ILE B 2 73   ? -32.588 2.426   20.138  1.00 311.75 ? 201  ILE X CG1 1 
ATOM   12126 C  CG2 . ILE B 2 73   ? -33.200 1.893   22.535  1.00 304.37 ? 201  ILE X CG2 1 
ATOM   12127 C  CD1 . ILE B 2 73   ? -31.155 2.003   19.902  1.00 309.39 ? 201  ILE X CD1 1 
ATOM   12128 N  N   . ASP B 2 74   ? -35.182 4.902   23.399  1.00 266.72 ? 202  ASP X N   1 
ATOM   12129 C  CA  . ASP B 2 74   ? -35.289 5.675   24.624  1.00 267.83 ? 202  ASP X CA  1 
ATOM   12130 C  C   . ASP B 2 74   ? -34.278 5.142   25.616  1.00 267.57 ? 202  ASP X C   1 
ATOM   12131 O  O   . ASP B 2 74   ? -34.153 3.930   25.805  1.00 264.58 ? 202  ASP X O   1 
ATOM   12132 C  CB  . ASP B 2 74   ? -36.699 5.613   25.214  1.00 267.62 ? 202  ASP X CB  1 
ATOM   12133 C  CG  . ASP B 2 74   ? -36.865 6.522   26.426  1.00 265.46 ? 202  ASP X CG  1 
ATOM   12134 O  OD1 . ASP B 2 74   ? -37.854 6.349   27.166  1.00 261.28 ? 202  ASP X OD1 1 
ATOM   12135 O  OD2 . ASP B 2 74   ? -36.008 7.407   26.645  1.00 267.30 ? 202  ASP X OD2 1 
ATOM   12136 N  N   . LEU B 2 75   ? -33.532 6.057   26.218  1.00 324.68 ? 203  LEU X N   1 
ATOM   12137 C  CA  . LEU B 2 75   ? -32.567 5.692   27.233  1.00 326.32 ? 203  LEU X CA  1 
ATOM   12138 C  C   . LEU B 2 75   ? -33.244 5.730   28.587  1.00 330.42 ? 203  LEU X C   1 
ATOM   12139 O  O   . LEU B 2 75   ? -32.648 5.380   29.603  1.00 327.23 ? 203  LEU X O   1 
ATOM   12140 C  CB  . LEU B 2 75   ? -31.370 6.632   27.186  1.00 324.25 ? 203  LEU X CB  1 
ATOM   12141 C  CG  . LEU B 2 75   ? -30.676 6.597   25.826  1.00 325.85 ? 203  LEU X CG  1 
ATOM   12142 C  CD1 . LEU B 2 75   ? -29.471 7.518   25.811  1.00 326.42 ? 203  LEU X CD1 1 
ATOM   12143 C  CD2 . LEU B 2 75   ? -30.272 5.172   25.471  1.00 324.41 ? 203  LEU X CD2 1 
ATOM   12144 N  N   . GLY B 2 76   ? -34.500 6.163   28.591  1.00 281.63 ? 204  GLY X N   1 
ATOM   12145 C  CA  . GLY B 2 76   ? -35.311 6.124   29.790  1.00 284.08 ? 204  GLY X CA  1 
ATOM   12146 C  C   . GLY B 2 76   ? -35.718 4.705   30.140  1.00 288.79 ? 204  GLY X C   1 
ATOM   12147 O  O   . GLY B 2 76   ? -36.126 4.431   31.269  1.00 284.65 ? 204  GLY X O   1 
ATOM   12148 N  N   . ASP B 2 77   ? -35.600 3.795   29.176  1.00 286.93 ? 205  ASP X N   1 
ATOM   12149 C  CA  . ASP B 2 77   ? -36.045 2.421   29.385  1.00 291.14 ? 205  ASP X CA  1 
ATOM   12150 C  C   . ASP B 2 77   ? -35.548 1.443   28.317  1.00 294.54 ? 205  ASP X C   1 
ATOM   12151 O  O   . ASP B 2 77   ? -35.620 1.721   27.117  1.00 298.84 ? 205  ASP X O   1 
ATOM   12152 C  CB  . ASP B 2 77   ? -37.573 2.376   29.449  1.00 294.50 ? 205  ASP X CB  1 
ATOM   12153 C  CG  . ASP B 2 77   ? -38.086 1.158   30.177  1.00 296.07 ? 205  ASP X CG  1 
ATOM   12154 O  OD1 . ASP B 2 77   ? -37.280 0.515   30.881  1.00 296.05 ? 205  ASP X OD1 1 
ATOM   12155 O  OD2 . ASP B 2 77   ? -39.292 0.848   30.049  1.00 297.16 ? 205  ASP X OD2 1 
ATOM   12156 N  N   . LYS B 2 78   ? -35.052 0.294   28.772  1.00 274.40 ? 206  LYS X N   1 
ATOM   12157 C  CA  . LYS B 2 78   ? -34.596 -0.778  27.886  1.00 274.95 ? 206  LYS X CA  1 
ATOM   12158 C  C   . LYS B 2 78   ? -35.745 -1.707  27.480  1.00 273.30 ? 206  LYS X C   1 
ATOM   12159 O  O   . LYS B 2 78   ? -35.537 -2.898  27.240  1.00 274.32 ? 206  LYS X O   1 
ATOM   12160 C  CB  . LYS B 2 78   ? -33.465 -1.583  28.550  1.00 273.11 ? 206  LYS X CB  1 
ATOM   12161 C  CG  . LYS B 2 78   ? -33.802 -2.144  29.934  1.00 270.25 ? 206  LYS X CG  1 
ATOM   12162 C  CD  . LYS B 2 78   ? -32.595 -2.814  30.579  1.00 268.16 ? 206  LYS X CD  1 
ATOM   12163 C  CE  . LYS B 2 78   ? -32.907 -3.293  31.989  1.00 265.36 ? 206  LYS X CE  1 
ATOM   12164 N  NZ  . LYS B 2 78   ? -33.954 -4.350  32.003  1.00 262.34 ? 206  LYS X NZ  1 
ATOM   12165 N  N   . LEU B 2 79   ? -36.953 -1.150  27.406  1.00 369.16 ? 207  LEU X N   1 
ATOM   12166 C  CA  . LEU B 2 79   ? -38.172 -1.929  27.164  1.00 365.35 ? 207  LEU X CA  1 
ATOM   12167 C  C   . LEU B 2 79   ? -38.325 -2.407  25.713  1.00 365.87 ? 207  LEU X C   1 
ATOM   12168 O  O   . LEU B 2 79   ? -39.370 -2.949  25.349  1.00 367.60 ? 207  LEU X O   1 
ATOM   12169 C  CB  . LEU B 2 79   ? -39.413 -1.128  27.604  1.00 362.06 ? 207  LEU X CB  1 
ATOM   12170 C  CG  . LEU B 2 79   ? -40.809 -1.767  27.681  1.00 360.52 ? 207  LEU X CG  1 
ATOM   12171 C  CD1 . LEU B 2 79   ? -40.839 -2.947  28.640  1.00 356.83 ? 207  LEU X CD1 1 
ATOM   12172 C  CD2 . LEU B 2 79   ? -41.854 -0.730  28.083  1.00 358.07 ? 207  LEU X CD2 1 
ATOM   12173 N  N   . GLN B 2 80   ? -37.295 -2.207  24.890  1.00 296.09 ? 208  GLN X N   1 
ATOM   12174 C  CA  . GLN B 2 80   ? -37.346 -2.609  23.478  1.00 296.31 ? 208  GLN X CA  1 
ATOM   12175 C  C   . GLN B 2 80   ? -37.035 -4.108  23.276  1.00 294.28 ? 208  GLN X C   1 
ATOM   12176 O  O   . GLN B 2 80   ? -35.925 -4.459  22.878  1.00 294.54 ? 208  GLN X O   1 
ATOM   12177 C  CB  . GLN B 2 80   ? -36.387 -1.749  22.635  1.00 296.55 ? 208  GLN X CB  1 
ATOM   12178 C  CG  . GLN B 2 80   ? -36.708 -0.253  22.596  1.00 299.53 ? 208  GLN X CG  1 
ATOM   12179 C  CD  . GLN B 2 80   ? -36.037 0.548   23.709  1.00 301.01 ? 208  GLN X CD  1 
ATOM   12180 O  OE1 . GLN B 2 80   ? -35.233 0.021   24.471  1.00 302.90 ? 208  GLN X OE1 1 
ATOM   12181 N  NE2 . GLN B 2 80   ? -36.368 1.832   23.799  1.00 300.72 ? 208  GLN X NE2 1 
ATOM   12182 N  N   . PHE B 2 81   ? -38.011 -4.984  23.530  1.00 299.25 ? 209  PHE X N   1 
ATOM   12183 C  CA  . PHE B 2 81   ? -37.770 -6.438  23.490  1.00 299.00 ? 209  PHE X CA  1 
ATOM   12184 C  C   . PHE B 2 81   ? -38.194 -7.183  22.213  1.00 307.60 ? 209  PHE X C   1 
ATOM   12185 O  O   . PHE B 2 81   ? -37.709 -8.288  21.959  1.00 309.59 ? 209  PHE X O   1 
ATOM   12186 C  CB  . PHE B 2 81   ? -38.335 -7.148  24.740  1.00 291.16 ? 209  PHE X CB  1 
ATOM   12187 C  CG  . PHE B 2 81   ? -39.820 -6.974  24.940  1.00 286.56 ? 209  PHE X CG  1 
ATOM   12188 C  CD1 . PHE B 2 81   ? -40.726 -7.685  24.169  1.00 288.45 ? 209  PHE X CD1 1 
ATOM   12189 C  CD2 . PHE B 2 81   ? -40.307 -6.117  25.920  1.00 280.16 ? 209  PHE X CD2 1 
ATOM   12190 C  CE1 . PHE B 2 81   ? -42.086 -7.531  24.359  1.00 286.10 ? 209  PHE X CE1 1 
ATOM   12191 C  CE2 . PHE B 2 81   ? -41.666 -5.960  26.114  1.00 276.69 ? 209  PHE X CE2 1 
ATOM   12192 C  CZ  . PHE B 2 81   ? -42.556 -6.667  25.333  1.00 280.14 ? 209  PHE X CZ  1 
ATOM   12193 N  N   . GLU B 2 82   ? -39.090 -6.592  21.424  1.00 284.02 ? 210  GLU X N   1 
ATOM   12194 C  CA  . GLU B 2 82   ? -39.571 -7.231  20.192  1.00 292.52 ? 210  GLU X CA  1 
ATOM   12195 C  C   . GLU B 2 82   ? -38.749 -6.844  18.964  1.00 295.46 ? 210  GLU X C   1 
ATOM   12196 O  O   . GLU B 2 82   ? -38.561 -7.645  18.044  1.00 300.72 ? 210  GLU X O   1 
ATOM   12197 C  CB  . GLU B 2 82   ? -41.046 -6.896  19.945  1.00 299.34 ? 210  GLU X CB  1 
ATOM   12198 C  CG  . GLU B 2 82   ? -41.289 -5.876  18.833  1.00 308.38 ? 210  GLU X CG  1 
ATOM   12199 C  CD  . GLU B 2 82   ? -40.896 -4.460  19.223  1.00 310.54 ? 210  GLU X CD  1 
ATOM   12200 O  OE1 . GLU B 2 82   ? -40.781 -4.184  20.435  1.00 307.08 ? 210  GLU X OE1 1 
ATOM   12201 O  OE2 . GLU B 2 82   ? -40.704 -3.621  18.316  1.00 315.56 ? 210  GLU X OE2 1 
ATOM   12202 N  N   . ARG B 2 83   ? -38.278 -5.602  18.952  1.00 319.86 ? 211  ARG X N   1 
ATOM   12203 C  CA  . ARG B 2 83   ? -37.480 -5.091  17.848  1.00 318.26 ? 211  ARG X CA  1 
ATOM   12204 C  C   . ARG B 2 83   ? -36.038 -5.583  17.940  1.00 316.85 ? 211  ARG X C   1 
ATOM   12205 O  O   . ARG B 2 83   ? -35.284 -5.476  16.977  1.00 318.42 ? 211  ARG X O   1 
ATOM   12206 C  CB  . ARG B 2 83   ? -37.527 -3.560  17.816  1.00 313.10 ? 211  ARG X CB  1 
ATOM   12207 C  CG  . ARG B 2 83   ? -37.161 -2.898  19.139  1.00 310.29 ? 211  ARG X CG  1 
ATOM   12208 C  CD  . ARG B 2 83   ? -37.213 -1.385  19.033  1.00 306.99 ? 211  ARG X CD  1 
ATOM   12209 N  NE  . ARG B 2 83   ? -38.515 -0.924  18.566  1.00 298.69 ? 211  ARG X NE  1 
ATOM   12210 C  CZ  . ARG B 2 83   ? -39.546 -0.683  19.364  1.00 295.45 ? 211  ARG X CZ  1 
ATOM   12211 N  NH1 . ARG B 2 83   ? -39.422 -0.861  20.671  1.00 298.51 ? 211  ARG X NH1 1 
ATOM   12212 N  NH2 . ARG B 2 83   ? -40.697 -0.267  18.857  1.00 290.57 ? 211  ARG X NH2 1 
ATOM   12213 N  N   . MET B 2 84   ? -35.661 -6.122  19.099  1.00 318.08 ? 212  MET X N   1 
ATOM   12214 C  CA  . MET B 2 84   ? -34.311 -6.656  19.303  1.00 316.32 ? 212  MET X CA  1 
ATOM   12215 C  C   . MET B 2 84   ? -34.003 -7.813  18.349  1.00 317.95 ? 212  MET X C   1 
ATOM   12216 O  O   . MET B 2 84   ? -32.896 -8.350  18.353  1.00 319.93 ? 212  MET X O   1 
ATOM   12217 C  CB  . MET B 2 84   ? -34.089 -7.090  20.761  1.00 310.74 ? 212  MET X CB  1 
ATOM   12218 C  CG  . MET B 2 84   ? -33.627 -5.981  21.712  1.00 306.89 ? 212  MET X CG  1 
ATOM   12219 S  SD  . MET B 2 84   ? -33.302 -6.599  23.381  1.00 279.48 ? 212  MET X SD  1 
ATOM   12220 C  CE  . MET B 2 84   ? -32.847 -5.099  24.258  1.00 178.53 ? 212  MET X CE  1 
ATOM   12221 N  N   . GLY B 2 85   ? -34.992 -8.200  17.546  1.00 279.76 ? 213  GLY X N   1 
ATOM   12222 C  CA  . GLY B 2 85   ? -34.787 -9.172  16.486  1.00 282.05 ? 213  GLY X CA  1 
ATOM   12223 C  C   . GLY B 2 85   ? -34.332 -8.499  15.201  1.00 285.93 ? 213  GLY X C   1 
ATOM   12224 O  O   . GLY B 2 85   ? -33.651 -9.105  14.367  1.00 288.68 ? 213  GLY X O   1 
ATOM   12225 N  N   . ASP B 2 86   ? -34.717 -7.233  15.052  1.00 346.47 ? 214  ASP X N   1 
ATOM   12226 C  CA  . ASP B 2 86   ? -34.341 -6.414  13.903  1.00 348.52 ? 214  ASP X CA  1 
ATOM   12227 C  C   . ASP B 2 86   ? -32.843 -6.563  13.629  1.00 351.08 ? 214  ASP X C   1 
ATOM   12228 O  O   . ASP B 2 86   ? -32.045 -6.679  14.559  1.00 349.96 ? 214  ASP X O   1 
ATOM   12229 C  CB  . ASP B 2 86   ? -34.694 -4.943  14.178  1.00 341.63 ? 214  ASP X CB  1 
ATOM   12230 C  CG  . ASP B 2 86   ? -35.229 -4.218  12.952  1.00 339.79 ? 214  ASP X CG  1 
ATOM   12231 O  OD1 . ASP B 2 86   ? -34.612 -4.323  11.872  1.00 340.75 ? 214  ASP X OD1 1 
ATOM   12232 O  OD2 . ASP B 2 86   ? -36.263 -3.526  13.075  1.00 337.58 ? 214  ASP X OD2 1 
ATOM   12233 N  N   . VAL B 2 87   ? -32.463 -6.571  12.356  1.00 383.39 ? 215  VAL X N   1 
ATOM   12234 C  CA  . VAL B 2 87   ? -31.056 -6.686  11.984  1.00 379.72 ? 215  VAL X CA  1 
ATOM   12235 C  C   . VAL B 2 87   ? -30.661 -5.552  11.035  1.00 377.68 ? 215  VAL X C   1 
ATOM   12236 O  O   . VAL B 2 87   ? -31.481 -5.091  10.241  1.00 378.03 ? 215  VAL X O   1 
ATOM   12237 C  CB  . VAL B 2 87   ? -30.751 -8.057  11.346  1.00 418.38 ? 215  VAL X CB  1 
ATOM   12238 C  CG1 . VAL B 2 87   ? -30.840 -9.159  12.391  1.00 417.09 ? 215  VAL X CG1 1 
ATOM   12239 C  CG2 . VAL B 2 87   ? -31.708 -8.333  10.198  1.00 421.53 ? 215  VAL X CG2 1 
ATOM   12240 N  N   . LEU B 2 88   ? -29.411 -5.100  11.125  1.00 356.77 ? 216  LEU X N   1 
ATOM   12241 C  CA  . LEU B 2 88   ? -28.965 -3.938  10.352  1.00 353.90 ? 216  LEU X CA  1 
ATOM   12242 C  C   . LEU B 2 88   ? -27.750 -4.210  9.461   1.00 351.59 ? 216  LEU X C   1 
ATOM   12243 O  O   . LEU B 2 88   ? -26.938 -5.090  9.747   1.00 349.69 ? 216  LEU X O   1 
ATOM   12244 C  CB  . LEU B 2 88   ? -28.675 -2.748  11.274  1.00 349.42 ? 216  LEU X CB  1 
ATOM   12245 C  CG  . LEU B 2 88   ? -29.837 -2.128  12.056  1.00 345.05 ? 216  LEU X CG  1 
ATOM   12246 C  CD1 . LEU B 2 88   ? -31.031 -1.883  11.147  1.00 346.61 ? 216  LEU X CD1 1 
ATOM   12247 C  CD2 . LEU B 2 88   ? -30.234 -2.998  13.239  1.00 339.65 ? 216  LEU X CD2 1 
ATOM   12248 N  N   . ASN B 2 89   ? -27.635 -3.432  8.386   1.00 369.90 ? 217  ASN X N   1 
ATOM   12249 C  CA  . ASN B 2 89   ? -26.562 -3.588  7.407   1.00 370.05 ? 217  ASN X CA  1 
ATOM   12250 C  C   . ASN B 2 89   ? -25.345 -2.732  7.751   1.00 368.78 ? 217  ASN X C   1 
ATOM   12251 O  O   . ASN B 2 89   ? -25.478 -1.538  8.016   1.00 367.13 ? 217  ASN X O   1 
ATOM   12252 C  CB  . ASN B 2 89   ? -27.074 -3.233  6.009   1.00 373.47 ? 217  ASN X CB  1 
ATOM   12253 C  CG  . ASN B 2 89   ? -28.470 -3.773  5.741   1.00 376.36 ? 217  ASN X CG  1 
ATOM   12254 O  OD1 . ASN B 2 89   ? -28.985 -4.596  6.497   1.00 376.36 ? 217  ASN X OD1 1 
ATOM   12255 N  ND2 . ASN B 2 89   ? -29.091 -3.309  4.661   1.00 378.95 ? 217  ASN X ND2 1 
ATOM   12256 N  N   . SER B 2 90   ? -24.160 -3.339  7.730   1.00 274.33 ? 218  SER X N   1 
ATOM   12257 C  CA  . SER B 2 90   ? -22.947 -2.670  8.206   1.00 276.37 ? 218  SER X CA  1 
ATOM   12258 C  C   . SER B 2 90   ? -22.551 -1.420  7.432   1.00 282.58 ? 218  SER X C   1 
ATOM   12259 O  O   . SER B 2 90   ? -22.356 -0.359  8.019   1.00 280.90 ? 218  SER X O   1 
ATOM   12260 C  CB  . SER B 2 90   ? -21.769 -3.639  8.239   1.00 273.69 ? 218  SER X CB  1 
ATOM   12261 O  OG  . SER B 2 90   ? -21.852 -4.462  9.384   1.00 270.11 ? 218  SER X OG  1 
ATOM   12262 N  N   . LYS B 2 91   ? -22.422 -1.551  6.119   1.00 195.76 ? 219  LYS X N   1 
ATOM   12263 C  CA  . LYS B 2 91   ? -21.905 -0.462  5.294   1.00 204.92 ? 219  LYS X CA  1 
ATOM   12264 C  C   . LYS B 2 91   ? -22.994 0.541   4.877   1.00 199.73 ? 219  LYS X C   1 
ATOM   12265 O  O   . LYS B 2 91   ? -22.737 1.508   4.146   1.00 203.82 ? 219  LYS X O   1 
ATOM   12266 C  CB  . LYS B 2 91   ? -21.155 -1.032  4.086   1.00 223.14 ? 219  LYS X CB  1 
ATOM   12267 C  CG  . LYS B 2 91   ? -20.088 -2.064  4.473   1.00 244.15 ? 219  LYS X CG  1 
ATOM   12268 C  CD  . LYS B 2 91   ? -20.729 -3.377  4.893   1.00 245.28 ? 219  LYS X CD  1 
ATOM   12269 C  CE  . LYS B 2 91   ? -19.736 -4.317  5.530   1.00 252.37 ? 219  LYS X CE  1 
ATOM   12270 N  NZ  . LYS B 2 91   ? -20.377 -5.634  5.738   1.00 255.53 ? 219  LYS X NZ  1 
ATOM   12271 N  N   . ASP B 2 92   ? -24.206 0.295   5.369   1.00 276.34 ? 220  ASP X N   1 
ATOM   12272 C  CA  . ASP B 2 92   ? -25.362 1.151   5.125   1.00 271.60 ? 220  ASP X CA  1 
ATOM   12273 C  C   . ASP B 2 92   ? -25.310 2.415   5.970   1.00 266.62 ? 220  ASP X C   1 
ATOM   12274 O  O   . ASP B 2 92   ? -25.297 3.538   5.456   1.00 269.65 ? 220  ASP X O   1 
ATOM   12275 C  CB  . ASP B 2 92   ? -26.647 0.389   5.464   1.00 269.78 ? 220  ASP X CB  1 
ATOM   12276 C  CG  . ASP B 2 92   ? -27.151 -0.461  4.309   1.00 272.31 ? 220  ASP X CG  1 
ATOM   12277 O  OD1 . ASP B 2 92   ? -26.433 -0.598  3.296   1.00 275.03 ? 220  ASP X OD1 1 
ATOM   12278 O  OD2 . ASP B 2 92   ? -28.279 -0.988  4.411   1.00 272.10 ? 220  ASP X OD2 1 
ATOM   12279 N  N   . ILE B 2 93   ? -25.292 2.209   7.280   1.00 410.18 ? 221  ILE X N   1 
ATOM   12280 C  CA  . ILE B 2 93   ? -25.324 3.295   8.241   1.00 403.38 ? 221  ILE X CA  1 
ATOM   12281 C  C   . ILE B 2 93   ? -24.434 4.437   7.777   1.00 399.53 ? 221  ILE X C   1 
ATOM   12282 O  O   . ILE B 2 93   ? -23.360 4.212   7.223   1.00 401.37 ? 221  ILE X O   1 
ATOM   12283 C  CB  . ILE B 2 93   ? -24.865 2.807   9.626   1.00 359.34 ? 221  ILE X CB  1 
ATOM   12284 C  CG1 . ILE B 2 93   ? -25.589 1.510   9.999   1.00 355.06 ? 221  ILE X CG1 1 
ATOM   12285 C  CG2 . ILE B 2 93   ? -25.086 3.883   10.682  1.00 360.67 ? 221  ILE X CG2 1 
ATOM   12286 C  CD1 . ILE B 2 93   ? -25.309 1.034   11.407  1.00 349.38 ? 221  ILE X CD1 1 
ATOM   12287 N  N   . ASN B 2 94   ? -24.887 5.665   7.990   1.00 372.32 ? 222  ASN X N   1 
ATOM   12288 C  CA  . ASN B 2 94   ? -24.104 6.818   7.583   1.00 371.03 ? 222  ASN X CA  1 
ATOM   12289 C  C   . ASN B 2 94   ? -23.430 7.558   8.746   1.00 367.87 ? 222  ASN X C   1 
ATOM   12290 O  O   . ASN B 2 94   ? -22.228 7.811   8.702   1.00 364.93 ? 222  ASN X O   1 
ATOM   12291 C  CB  . ASN B 2 94   ? -24.950 7.768   6.737   1.00 198.57 ? 222  ASN X CB  1 
ATOM   12292 C  CG  . ASN B 2 94   ? -24.154 8.939   6.212   1.00 200.75 ? 222  ASN X CG  1 
ATOM   12293 O  OD1 . ASN B 2 94   ? -23.880 9.891   6.940   1.00 200.03 ? 222  ASN X OD1 1 
ATOM   12294 N  ND2 . ASN B 2 94   ? -23.773 8.875   4.942   1.00 203.55 ? 222  ASN X ND2 1 
ATOM   12295 N  N   . LYS B 2 95   ? -24.194 7.883   9.788   1.00 387.08 ? 223  LYS X N   1 
ATOM   12296 C  CA  . LYS B 2 95   ? -23.680 8.653   10.928  1.00 382.82 ? 223  LYS X CA  1 
ATOM   12297 C  C   . LYS B 2 95   ? -24.562 8.492   12.176  1.00 372.98 ? 223  LYS X C   1 
ATOM   12298 O  O   . LYS B 2 95   ? -25.730 8.861   12.158  1.00 373.88 ? 223  LYS X O   1 
ATOM   12299 C  CB  . LYS B 2 95   ? -23.590 10.145  10.559  1.00 219.25 ? 223  LYS X CB  1 
ATOM   12300 C  CG  . LYS B 2 95   ? -22.544 10.498  9.504   1.00 220.19 ? 223  LYS X CG  1 
ATOM   12301 C  CD  . LYS B 2 95   ? -22.756 11.895  8.931   1.00 221.85 ? 223  LYS X CD  1 
ATOM   12302 C  CE  . LYS B 2 95   ? -21.678 12.223  7.908   1.00 224.16 ? 223  LYS X CE  1 
ATOM   12303 N  NZ  . LYS B 2 95   ? -21.462 11.112  6.940   1.00 224.43 ? 223  LYS X NZ  1 
ATOM   12304 N  N   . ILE B 2 96   ? -24.013 7.953   13.260  1.00 305.06 ? 224  ILE X N   1 
ATOM   12305 C  CA  . ILE B 2 96   ? -24.771 7.865   14.506  1.00 303.48 ? 224  ILE X CA  1 
ATOM   12306 C  C   . ILE B 2 96   ? -24.741 9.225   15.211  1.00 308.57 ? 224  ILE X C   1 
ATOM   12307 O  O   . ILE B 2 96   ? -23.830 10.017  14.974  1.00 311.50 ? 224  ILE X O   1 
ATOM   12308 C  CB  . ILE B 2 96   ? -24.213 6.767   15.436  1.00 281.81 ? 224  ILE X CB  1 
ATOM   12309 C  CG1 . ILE B 2 96   ? -24.055 5.446   14.684  1.00 281.43 ? 224  ILE X CG1 1 
ATOM   12310 C  CG2 . ILE B 2 96   ? -25.112 6.573   16.651  1.00 276.33 ? 224  ILE X CG2 1 
ATOM   12311 C  CD1 . ILE B 2 96   ? -23.487 4.341   15.544  1.00 275.27 ? 224  ILE X CD1 1 
ATOM   12312 N  N   . GLU B 2 97   ? -25.730 9.496   16.066  1.00 496.81 ? 225  GLU X N   1 
ATOM   12313 C  CA  . GLU B 2 97   ? -25.838 10.792  16.746  1.00 501.00 ? 225  GLU X CA  1 
ATOM   12314 C  C   . GLU B 2 97   ? -26.704 10.742  18.012  1.00 499.93 ? 225  GLU X C   1 
ATOM   12315 O  O   . GLU B 2 97   ? -27.883 10.390  17.953  1.00 500.44 ? 225  GLU X O   1 
ATOM   12316 C  CB  . GLU B 2 97   ? -26.394 11.845  15.783  1.00 336.69 ? 225  GLU X CB  1 
ATOM   12317 C  CG  . GLU B 2 97   ? -25.415 12.265  14.693  1.00 341.80 ? 225  GLU X CG  1 
ATOM   12318 C  CD  . GLU B 2 97   ? -26.104 12.734  13.427  1.00 343.51 ? 225  GLU X CD  1 
ATOM   12319 O  OE1 . GLU B 2 97   ? -27.354 12.780  13.407  1.00 343.80 ? 225  GLU X OE1 1 
ATOM   12320 O  OE2 . GLU B 2 97   ? -25.389 13.052  12.450  1.00 344.66 ? 225  GLU X OE2 1 
ATOM   12321 N  N   . VAL B 2 98   ? -26.118 11.116  19.149  1.00 348.33 ? 226  VAL X N   1 
ATOM   12322 C  CA  . VAL B 2 98   ? -26.816 11.067  20.437  1.00 344.58 ? 226  VAL X CA  1 
ATOM   12323 C  C   . VAL B 2 98   ? -27.049 12.463  21.027  1.00 347.73 ? 226  VAL X C   1 
ATOM   12324 O  O   . VAL B 2 98   ? -26.357 13.418  20.670  1.00 349.39 ? 226  VAL X O   1 
ATOM   12325 C  CB  . VAL B 2 98   ? -26.045 10.202  21.466  1.00 374.77 ? 226  VAL X CB  1 
ATOM   12326 C  CG1 . VAL B 2 98   ? -26.873 9.989   22.725  1.00 369.04 ? 226  VAL X CG1 1 
ATOM   12327 C  CG2 . VAL B 2 98   ? -25.666 8.863   20.859  1.00 374.71 ? 226  VAL X CG2 1 
ATOM   12328 N  N   . THR B 2 99   ? -28.023 12.566  21.931  1.00 298.06 ? 227  THR X N   1 
ATOM   12329 C  CA  . THR B 2 99   ? -28.334 13.816  22.625  1.00 301.24 ? 227  THR X CA  1 
ATOM   12330 C  C   . THR B 2 99   ? -28.768 13.520  24.062  1.00 300.34 ? 227  THR X C   1 
ATOM   12331 O  O   . THR B 2 99   ? -29.665 12.710  24.289  1.00 299.11 ? 227  THR X O   1 
ATOM   12332 C  CB  . THR B 2 99   ? -29.450 14.600  21.909  1.00 301.69 ? 227  THR X CB  1 
ATOM   12333 O  OG1 . THR B 2 99   ? -29.044 14.899  20.569  1.00 306.01 ? 227  THR X OG1 1 
ATOM   12334 C  CG2 . THR B 2 99   ? -29.744 15.897  22.638  1.00 300.90 ? 227  THR X CG2 1 
ATOM   12335 N  N   . LEU B 2 100  ? -28.143 14.189  25.026  1.00 387.66 ? 228  LEU X N   1 
ATOM   12336 C  CA  . LEU B 2 100  ? -28.277 13.808  26.431  1.00 385.40 ? 228  LEU X CA  1 
ATOM   12337 C  C   . LEU B 2 100  ? -29.130 14.747  27.275  1.00 386.76 ? 228  LEU X C   1 
ATOM   12338 O  O   . LEU B 2 100  ? -28.998 15.965  27.188  1.00 389.99 ? 228  LEU X O   1 
ATOM   12339 C  CB  . LEU B 2 100  ? -26.892 13.698  27.064  1.00 189.35 ? 228  LEU X CB  1 
ATOM   12340 C  CG  . LEU B 2 100  ? -25.842 12.929  26.261  1.00 190.54 ? 228  LEU X CG  1 
ATOM   12341 C  CD1 . LEU B 2 100  ? -24.686 12.497  27.156  1.00 187.87 ? 228  LEU X CD1 1 
ATOM   12342 C  CD2 . LEU B 2 100  ? -26.459 11.717  25.579  1.00 189.59 ? 228  LEU X CD2 1 
ATOM   12343 N  N   . LYS B 2 101  ? -29.989 14.172  28.113  1.00 393.01 ? 229  LYS X N   1 
ATOM   12344 C  CA  . LYS B 2 101  ? -30.700 14.960  29.113  1.00 391.97 ? 229  LYS X CA  1 
ATOM   12345 C  C   . LYS B 2 101  ? -30.455 14.483  30.541  1.00 380.03 ? 229  LYS X C   1 
ATOM   12346 O  O   . LYS B 2 101  ? -30.806 13.357  30.898  1.00 374.87 ? 229  LYS X O   1 
ATOM   12347 C  CB  . LYS B 2 101  ? -32.203 14.969  28.868  1.00 191.35 ? 229  LYS X CB  1 
ATOM   12348 C  CG  . LYS B 2 101  ? -32.943 15.486  30.103  1.00 185.54 ? 229  LYS X CG  1 
ATOM   12349 C  CD  . LYS B 2 101  ? -34.421 15.738  29.875  1.00 184.84 ? 229  LYS X CD  1 
ATOM   12350 C  CE  . LYS B 2 101  ? -35.033 16.475  31.064  1.00 179.69 ? 229  LYS X CE  1 
ATOM   12351 N  NZ  . LYS B 2 101  ? -36.470 16.786  30.835  1.00 179.41 ? 229  LYS X NZ  1 
ATOM   12352 N  N   . GLN B 2 102  ? -29.873 15.354  31.358  1.00 318.89 ? 230  GLN X N   1 
ATOM   12353 C  CA  . GLN B 2 102  ? -29.705 15.079  32.781  1.00 308.11 ? 230  GLN X CA  1 
ATOM   12354 C  C   . GLN B 2 102  ? -30.779 15.789  33.602  1.00 303.14 ? 230  GLN X C   1 
ATOM   12355 O  O   . GLN B 2 102  ? -30.507 16.320  34.681  1.00 298.64 ? 230  GLN X O   1 
ATOM   12356 C  CB  . GLN B 2 102  ? -28.310 15.486  33.260  1.00 305.17 ? 230  GLN X CB  1 
ATOM   12357 C  CG  . GLN B 2 102  ? -27.183 14.605  32.737  1.00 301.52 ? 230  GLN X CG  1 
ATOM   12358 C  CD  . GLN B 2 102  ? -25.813 15.082  33.191  1.00 298.22 ? 230  GLN X CD  1 
ATOM   12359 O  OE1 . GLN B 2 102  ? -25.679 15.722  34.232  1.00 296.26 ? 230  GLN X OE1 1 
ATOM   12360 N  NE2 . GLN B 2 102  ? -24.789 14.768  32.407  1.00 298.54 ? 230  GLN X NE2 1 
ATOM   12361 N  N   . THR C 1 22   ? 53.632  80.962  70.137  1.00 251.69 ? 22   THR B N   1 
ATOM   12362 C  CA  . THR C 1 22   ? 53.474  79.855  71.071  1.00 247.36 ? 22   THR B CA  1 
ATOM   12363 C  C   . THR C 1 22   ? 54.526  78.763  70.861  1.00 246.15 ? 22   THR B C   1 
ATOM   12364 O  O   . THR C 1 22   ? 55.260  78.759  69.862  1.00 248.46 ? 22   THR B O   1 
ATOM   12365 C  CB  . THR C 1 22   ? 52.056  79.249  71.020  1.00 243.65 ? 22   THR B CB  1 
ATOM   12366 O  OG1 . THR C 1 22   ? 51.568  79.305  69.677  1.00 243.16 ? 22   THR B OG1 1 
ATOM   12367 C  CG2 . THR C 1 22   ? 51.101  80.017  71.932  1.00 240.32 ? 22   THR B CG2 1 
ATOM   12368 N  N   . TYR C 1 23   ? 54.567  77.835  71.816  1.00 190.28 ? 23   TYR B N   1 
ATOM   12369 C  CA  . TYR C 1 23   ? 55.685  76.900  71.972  1.00 195.98 ? 23   TYR B CA  1 
ATOM   12370 C  C   . TYR C 1 23   ? 55.303  75.409  71.960  1.00 193.93 ? 23   TYR B C   1 
ATOM   12371 O  O   . TYR C 1 23   ? 54.232  75.009  72.435  1.00 188.72 ? 23   TYR B O   1 
ATOM   12372 C  CB  . TYR C 1 23   ? 56.490  77.236  73.247  1.00 201.66 ? 23   TYR B CB  1 
ATOM   12373 C  CG  . TYR C 1 23   ? 55.676  77.297  74.534  1.00 204.77 ? 23   TYR B CG  1 
ATOM   12374 C  CD1 . TYR C 1 23   ? 54.329  76.953  74.548  1.00 202.97 ? 23   TYR B CD1 1 
ATOM   12375 C  CD2 . TYR C 1 23   ? 56.263  77.700  75.729  1.00 208.64 ? 23   TYR B CD2 1 
ATOM   12376 C  CE1 . TYR C 1 23   ? 53.602  77.004  75.693  1.00 202.12 ? 23   TYR B CE1 1 
ATOM   12377 C  CE2 . TYR C 1 23   ? 55.540  77.752  76.884  1.00 206.59 ? 23   TYR B CE2 1 
ATOM   12378 C  CZ  . TYR C 1 23   ? 54.213  77.401  76.855  1.00 204.19 ? 23   TYR B CZ  1 
ATOM   12379 O  OH  . TYR C 1 23   ? 53.505  77.457  78.021  1.00 201.78 ? 23   TYR B OH  1 
ATOM   12380 N  N   . VAL C 1 24   ? 56.201  74.598  71.410  1.00 201.70 ? 24   VAL B N   1 
ATOM   12381 C  CA  . VAL C 1 24   ? 55.981  73.167  71.316  1.00 197.99 ? 24   VAL B CA  1 
ATOM   12382 C  C   . VAL C 1 24   ? 57.158  72.401  71.862  1.00 197.17 ? 24   VAL B C   1 
ATOM   12383 O  O   . VAL C 1 24   ? 58.321  72.661  71.538  1.00 200.51 ? 24   VAL B O   1 
ATOM   12384 C  CB  . VAL C 1 24   ? 55.737  72.702  69.876  1.00 202.02 ? 24   VAL B CB  1 
ATOM   12385 C  CG1 . VAL C 1 24   ? 56.437  71.372  69.636  1.00 203.76 ? 24   VAL B CG1 1 
ATOM   12386 C  CG2 . VAL C 1 24   ? 54.240  72.592  69.594  1.00 198.40 ? 24   VAL B CG2 1 
ATOM   12387 N  N   . ILE C 1 25   ? 56.816  71.435  72.696  1.00 202.55 ? 25   ILE B N   1 
ATOM   12388 C  CA  . ILE C 1 25   ? 57.774  70.601  73.382  1.00 207.85 ? 25   ILE B CA  1 
ATOM   12389 C  C   . ILE C 1 25   ? 57.189  69.212  73.318  1.00 204.89 ? 25   ILE B C   1 
ATOM   12390 O  O   . ILE C 1 25   ? 56.360  68.836  74.135  1.00 201.52 ? 25   ILE B O   1 
ATOM   12391 C  CB  . ILE C 1 25   ? 57.906  71.007  74.868  1.00 211.15 ? 25   ILE B CB  1 
ATOM   12392 C  CG1 . ILE C 1 25   ? 58.317  72.474  74.997  1.00 216.51 ? 25   ILE B CG1 1 
ATOM   12393 C  CG2 . ILE C 1 25   ? 58.914  70.122  75.580  1.00 213.85 ? 25   ILE B CG2 1 
ATOM   12394 C  CD1 . ILE C 1 25   ? 59.786  72.713  74.808  1.00 222.65 ? 25   ILE B CD1 1 
ATOM   12395 N  N   . SER C 1 26   ? 57.592  68.446  72.329  1.00 177.78 ? 26   SER B N   1 
ATOM   12396 C  CA  . SER C 1 26   ? 57.045  67.120  72.233  1.00 174.10 ? 26   SER B CA  1 
ATOM   12397 C  C   . SER C 1 26   ? 57.777  66.187  73.198  1.00 174.35 ? 26   SER B C   1 
ATOM   12398 O  O   . SER C 1 26   ? 58.877  66.503  73.667  1.00 176.14 ? 26   SER B O   1 
ATOM   12399 C  CB  . SER C 1 26   ? 57.164  66.645  70.794  1.00 180.42 ? 26   SER B CB  1 
ATOM   12400 O  OG  . SER C 1 26   ? 57.084  67.757  69.923  1.00 183.16 ? 26   SER B OG  1 
ATOM   12401 N  N   . ALA C 1 27   ? 57.137  65.058  73.506  1.00 175.35 ? 27   ALA B N   1 
ATOM   12402 C  CA  . ALA C 1 27   ? 57.790  63.912  74.144  1.00 172.96 ? 27   ALA B CA  1 
ATOM   12403 C  C   . ALA C 1 27   ? 56.906  62.676  73.996  1.00 185.02 ? 27   ALA B C   1 
ATOM   12404 O  O   . ALA C 1 27   ? 55.720  62.804  73.704  1.00 180.40 ? 27   ALA B O   1 
ATOM   12405 C  CB  . ALA C 1 27   ? 58.056  64.187  75.578  1.00 171.28 ? 27   ALA B CB  1 
ATOM   12406 N  N   . PRO C 1 28   ? 57.476  61.475  74.212  1.00 175.51 ? 28   PRO B N   1 
ATOM   12407 C  CA  . PRO C 1 28   ? 56.711  60.246  73.960  1.00 175.69 ? 28   PRO B CA  1 
ATOM   12408 C  C   . PRO C 1 28   ? 55.338  60.309  74.637  1.00 174.96 ? 28   PRO B C   1 
ATOM   12409 O  O   . PRO C 1 28   ? 54.990  61.339  75.201  1.00 174.94 ? 28   PRO B O   1 
ATOM   12410 C  CB  . PRO C 1 28   ? 57.570  59.154  74.607  1.00 174.75 ? 28   PRO B CB  1 
ATOM   12411 C  CG  . PRO C 1 28   ? 58.947  59.718  74.715  1.00 177.70 ? 28   PRO B CG  1 
ATOM   12412 C  CD  . PRO C 1 28   ? 58.809  61.210  74.789  1.00 176.63 ? 28   PRO B CD  1 
ATOM   12413 N  N   . LYS C 1 29   ? 54.552  59.241  74.555  1.00 249.82 ? 29   LYS B N   1 
ATOM   12414 C  CA  . LYS C 1 29   ? 53.332  59.160  75.355  1.00 246.02 ? 29   LYS B CA  1 
ATOM   12415 C  C   . LYS C 1 29   ? 53.671  58.561  76.713  1.00 245.49 ? 29   LYS B C   1 
ATOM   12416 O  O   . LYS C 1 29   ? 52.895  58.667  77.654  1.00 240.30 ? 29   LYS B O   1 
ATOM   12417 C  CB  . LYS C 1 29   ? 52.228  58.356  74.650  1.00 246.02 ? 29   LYS B CB  1 
ATOM   12418 C  CG  . LYS C 1 29   ? 51.135  57.784  75.570  1.00 244.82 ? 29   LYS B CG  1 
ATOM   12419 C  CD  . LYS C 1 29   ? 50.394  58.854  76.367  1.00 284.39 ? 29   LYS B CD  1 
ATOM   12420 C  CE  . LYS C 1 29   ? 49.647  58.228  77.550  1.00 273.10 ? 29   LYS B CE  1 
ATOM   12421 N  NZ  . LYS C 1 29   ? 49.062  59.231  78.491  1.00 269.13 ? 29   LYS B NZ  1 
ATOM   12422 N  N   . ILE C 1 30   ? 54.846  57.947  76.816  1.00 165.65 ? 30   ILE B N   1 
ATOM   12423 C  CA  . ILE C 1 30   ? 55.311  57.380  78.077  1.00 163.59 ? 30   ILE B CA  1 
ATOM   12424 C  C   . ILE C 1 30   ? 56.812  57.563  78.225  1.00 165.41 ? 30   ILE B C   1 
ATOM   12425 O  O   . ILE C 1 30   ? 57.489  58.087  77.335  1.00 168.62 ? 30   ILE B O   1 
ATOM   12426 C  CB  . ILE C 1 30   ? 55.029  55.866  78.175  1.00 159.90 ? 30   ILE B CB  1 
ATOM   12427 C  CG1 . ILE C 1 30   ? 53.562  55.565  77.864  1.00 157.96 ? 30   ILE B CG1 1 
ATOM   12428 C  CG2 . ILE C 1 30   ? 55.417  55.319  79.538  1.00 158.68 ? 30   ILE B CG2 1 
ATOM   12429 C  CD1 . ILE C 1 30   ? 52.610  56.117  78.851  1.00 156.60 ? 30   ILE B CD1 1 
ATOM   12430 N  N   . PHE C 1 31   ? 57.323  57.133  79.369  1.00 162.29 ? 31   PHE B N   1 
ATOM   12431 C  CA  . PHE C 1 31   ? 58.744  57.082  79.592  1.00 163.01 ? 31   PHE B CA  1 
ATOM   12432 C  C   . PHE C 1 31   ? 59.130  55.671  79.941  1.00 162.62 ? 31   PHE B C   1 
ATOM   12433 O  O   . PHE C 1 31   ? 58.294  54.821  80.260  1.00 160.72 ? 31   PHE B O   1 
ATOM   12434 C  CB  . PHE C 1 31   ? 59.169  58.002  80.741  1.00 160.46 ? 31   PHE B CB  1 
ATOM   12435 C  CG  . PHE C 1 31   ? 58.872  59.472  80.515  1.00 161.17 ? 31   PHE B CG  1 
ATOM   12436 C  CD1 . PHE C 1 31   ? 57.830  60.099  81.190  1.00 157.57 ? 31   PHE B CD1 1 
ATOM   12437 C  CD2 . PHE C 1 31   ? 59.653  60.231  79.653  1.00 164.22 ? 31   PHE B CD2 1 
ATOM   12438 C  CE1 . PHE C 1 31   ? 57.566  61.443  80.988  1.00 156.40 ? 31   PHE B CE1 1 
ATOM   12439 C  CE2 . PHE C 1 31   ? 59.388  61.581  79.456  1.00 163.83 ? 31   PHE B CE2 1 
ATOM   12440 C  CZ  . PHE C 1 31   ? 58.342  62.180  80.124  1.00 159.19 ? 31   PHE B CZ  1 
ATOM   12441 N  N   . ARG C 1 32   ? 60.430  55.450  79.886  1.00 167.56 ? 32   ARG B N   1 
ATOM   12442 C  CA  . ARG C 1 32   ? 61.011  54.193  80.277  1.00 166.95 ? 32   ARG B CA  1 
ATOM   12443 C  C   . ARG C 1 32   ? 62.229  54.493  81.127  1.00 164.61 ? 32   ARG B C   1 
ATOM   12444 O  O   . ARG C 1 32   ? 62.834  55.571  81.037  1.00 164.31 ? 32   ARG B O   1 
ATOM   12445 C  CB  . ARG C 1 32   ? 61.443  53.383  79.039  1.00 175.37 ? 32   ARG B CB  1 
ATOM   12446 C  CG  . ARG C 1 32   ? 60.378  52.417  78.413  1.00 175.97 ? 32   ARG B CG  1 
ATOM   12447 C  CD  . ARG C 1 32   ? 60.829  51.697  77.066  1.00 182.10 ? 32   ARG B CD  1 
ATOM   12448 N  NE  . ARG C 1 32   ? 59.851  50.722  76.543  1.00 179.12 ? 32   ARG B NE  1 
ATOM   12449 C  CZ  . ARG C 1 32   ? 59.206  50.820  75.382  1.00 179.16 ? 32   ARG B CZ  1 
ATOM   12450 N  NH1 . ARG C 1 32   ? 59.423  51.846  74.570  1.00 181.67 ? 32   ARG B NH1 1 
ATOM   12451 N  NH2 . ARG C 1 32   ? 58.339  49.881  75.040  1.00 176.60 ? 32   ARG B NH2 1 
ATOM   12452 N  N   . VAL C 1 33   ? 62.576  53.513  81.945  1.00 170.65 ? 33   VAL B N   1 
ATOM   12453 C  CA  . VAL C 1 33   ? 63.819  53.495  82.686  1.00 173.54 ? 33   VAL B CA  1 
ATOM   12454 C  C   . VAL C 1 33   ? 65.015  53.150  81.810  1.00 180.82 ? 33   VAL B C   1 
ATOM   12455 O  O   . VAL C 1 33   ? 64.972  52.196  81.040  1.00 181.89 ? 33   VAL B O   1 
ATOM   12456 C  CB  . VAL C 1 33   ? 63.712  52.430  83.741  1.00 171.50 ? 33   VAL B CB  1 
ATOM   12457 C  CG1 . VAL C 1 33   ? 64.746  52.654  84.848  1.00 174.33 ? 33   VAL B CG1 1 
ATOM   12458 C  CG2 . VAL C 1 33   ? 62.295  52.439  84.270  1.00 166.00 ? 33   VAL B CG2 1 
ATOM   12459 N  N   . GLY C 1 34   ? 66.091  53.915  81.947  1.00 178.57 ? 34   GLY B N   1 
ATOM   12460 C  CA  . GLY C 1 34   ? 67.299  53.660  81.191  1.00 188.39 ? 34   GLY B CA  1 
ATOM   12461 C  C   . GLY C 1 34   ? 67.073  53.931  79.721  1.00 195.24 ? 34   GLY B C   1 
ATOM   12462 O  O   . GLY C 1 34   ? 67.737  53.353  78.857  1.00 200.87 ? 34   GLY B O   1 
ATOM   12463 N  N   . ALA C 1 35   ? 66.129  54.826  79.444  1.00 167.08 ? 35   ALA B N   1 
ATOM   12464 C  CA  . ALA C 1 35   ? 65.754  55.155  78.076  1.00 170.70 ? 35   ALA B CA  1 
ATOM   12465 C  C   . ALA C 1 35   ? 66.236  56.529  77.659  1.00 176.24 ? 35   ALA B C   1 
ATOM   12466 O  O   . ALA C 1 35   ? 65.867  57.521  78.275  1.00 171.76 ? 35   ALA B O   1 
ATOM   12467 C  CB  . ALA C 1 35   ? 64.263  55.084  77.935  1.00 166.13 ? 35   ALA B CB  1 
ATOM   12468 N  N   . SER C 1 36   ? 67.033  56.579  76.597  1.00 266.97 ? 36   SER B N   1 
ATOM   12469 C  CA  . SER C 1 36   ? 67.477  57.841  76.023  1.00 270.66 ? 36   SER B CA  1 
ATOM   12470 C  C   . SER C 1 36   ? 66.288  58.642  75.484  1.00 268.52 ? 36   SER B C   1 
ATOM   12471 O  O   . SER C 1 36   ? 66.130  58.791  74.271  1.00 271.62 ? 36   SER B O   1 
ATOM   12472 C  CB  . SER C 1 36   ? 68.479  57.576  74.896  1.00 275.79 ? 36   SER B CB  1 
ATOM   12473 O  OG  . SER C 1 36   ? 69.283  56.442  75.184  1.00 276.78 ? 36   SER B OG  1 
ATOM   12474 N  N   . GLU C 1 37   ? 65.462  59.161  76.389  1.00 217.19 ? 37   GLU B N   1 
ATOM   12475 C  CA  . GLU C 1 37   ? 64.251  59.883  76.000  1.00 216.37 ? 37   GLU B CA  1 
ATOM   12476 C  C   . GLU C 1 37   ? 64.536  61.170  75.221  1.00 217.42 ? 37   GLU B C   1 
ATOM   12477 O  O   . GLU C 1 37   ? 65.073  62.148  75.753  1.00 216.90 ? 37   GLU B O   1 
ATOM   12478 C  CB  . GLU C 1 37   ? 63.367  60.179  77.216  1.00 215.62 ? 37   GLU B CB  1 
ATOM   12479 C  CG  . GLU C 1 37   ? 62.949  58.948  78.016  1.00 218.14 ? 37   GLU B CG  1 
ATOM   12480 C  CD  . GLU C 1 37   ? 62.036  58.033  77.241  1.00 222.23 ? 37   GLU B CD  1 
ATOM   12481 O  OE1 . GLU C 1 37   ? 62.116  58.031  75.994  1.00 227.25 ? 37   GLU B OE1 1 
ATOM   12482 O  OE2 . GLU C 1 37   ? 61.241  57.316  77.884  1.00 220.09 ? 37   GLU B OE2 1 
ATOM   12483 N  N   . ASN C 1 38   ? 64.159  61.151  73.949  1.00 203.40 ? 38   ASN B N   1 
ATOM   12484 C  CA  . ASN C 1 38   ? 64.324  62.301  73.074  1.00 203.74 ? 38   ASN B CA  1 
ATOM   12485 C  C   . ASN C 1 38   ? 63.230  63.352  73.321  1.00 197.88 ? 38   ASN B C   1 
ATOM   12486 O  O   . ASN C 1 38   ? 62.039  63.020  73.330  1.00 193.81 ? 38   ASN B O   1 
ATOM   12487 C  CB  . ASN C 1 38   ? 64.343  61.845  71.610  1.00 205.92 ? 38   ASN B CB  1 
ATOM   12488 C  CG  . ASN C 1 38   ? 65.535  60.938  71.289  1.00 209.20 ? 38   ASN B CG  1 
ATOM   12489 O  OD1 . ASN C 1 38   ? 66.197  60.406  72.185  1.00 208.54 ? 38   ASN B OD1 1 
ATOM   12490 N  ND2 . ASN C 1 38   ? 65.804  60.759  70.005  1.00 212.95 ? 38   ASN B ND2 1 
ATOM   12491 N  N   . ILE C 1 39   ? 63.636  64.611  73.532  1.00 167.27 ? 39   ILE B N   1 
ATOM   12492 C  CA  . ILE C 1 39   ? 62.699  65.705  73.822  1.00 161.04 ? 39   ILE B CA  1 
ATOM   12493 C  C   . ILE C 1 39   ? 62.995  67.023  73.106  1.00 161.77 ? 39   ILE B C   1 
ATOM   12494 O  O   . ILE C 1 39   ? 63.756  67.875  73.587  1.00 161.98 ? 39   ILE B O   1 
ATOM   12495 C  CB  . ILE C 1 39   ? 62.644  65.996  75.296  1.00 160.04 ? 39   ILE B CB  1 
ATOM   12496 C  CG1 . ILE C 1 39   ? 62.442  64.687  76.073  1.00 160.18 ? 39   ILE B CG1 1 
ATOM   12497 C  CG2 . ILE C 1 39   ? 61.561  67.022  75.558  1.00 158.68 ? 39   ILE B CG2 1 
ATOM   12498 C  CD1 . ILE C 1 39   ? 61.261  63.838  75.608  1.00 164.39 ? 39   ILE B CD1 1 
ATOM   12499 N  N   . VAL C 1 40   ? 62.350  67.170  71.955  1.00 209.11 ? 40   VAL B N   1 
ATOM   12500 C  CA  . VAL C 1 40   ? 62.519  68.321  71.090  1.00 214.92 ? 40   VAL B CA  1 
ATOM   12501 C  C   . VAL C 1 40   ? 61.755  69.503  71.620  1.00 215.10 ? 40   VAL B C   1 
ATOM   12502 O  O   . VAL C 1 40   ? 60.663  69.368  72.173  1.00 208.86 ? 40   VAL B O   1 
ATOM   12503 C  CB  . VAL C 1 40   ? 61.995  68.059  69.658  1.00 221.87 ? 40   VAL B CB  1 
ATOM   12504 C  CG1 . VAL C 1 40   ? 62.526  66.744  69.113  1.00 224.70 ? 40   VAL B CG1 1 
ATOM   12505 C  CG2 . VAL C 1 40   ? 60.471  68.085  69.636  1.00 216.78 ? 40   VAL B CG2 1 
ATOM   12506 N  N   . ILE C 1 41   ? 62.347  70.668  71.415  1.00 208.33 ? 41   ILE B N   1 
ATOM   12507 C  CA  . ILE C 1 41   ? 61.705  71.927  71.700  1.00 208.16 ? 41   ILE B CA  1 
ATOM   12508 C  C   . ILE C 1 41   ? 61.861  72.794  70.475  1.00 210.06 ? 41   ILE B C   1 
ATOM   12509 O  O   . ILE C 1 41   ? 62.958  72.937  69.951  1.00 212.59 ? 41   ILE B O   1 
ATOM   12510 C  CB  . ILE C 1 41   ? 62.377  72.636  72.869  1.00 213.46 ? 41   ILE B CB  1 
ATOM   12511 C  CG1 . ILE C 1 41   ? 62.110  74.138  72.792  1.00 214.26 ? 41   ILE B CG1 1 
ATOM   12512 C  CG2 . ILE C 1 41   ? 63.869  72.386  72.850  1.00 218.72 ? 41   ILE B CG2 1 
ATOM   12513 C  CD1 . ILE C 1 41   ? 62.902  74.953  73.800  1.00 216.38 ? 41   ILE B CD1 1 
ATOM   12514 N  N   . GLN C 1 42   ? 60.754  73.371  70.032  1.00 262.13 ? 42   GLN B N   1 
ATOM   12515 C  CA  . GLN C 1 42   ? 60.729  74.256  68.876  1.00 270.41 ? 42   GLN B CA  1 
ATOM   12516 C  C   . GLN C 1 42   ? 59.701  75.335  69.192  1.00 271.38 ? 42   GLN B C   1 
ATOM   12517 O  O   . GLN C 1 42   ? 58.803  75.091  69.998  1.00 265.87 ? 42   GLN B O   1 
ATOM   12518 C  CB  . GLN C 1 42   ? 60.315  73.470  67.642  1.00 273.81 ? 42   GLN B CB  1 
ATOM   12519 C  CG  . GLN C 1 42   ? 59.273  74.145  66.802  1.00 274.31 ? 42   GLN B CG  1 
ATOM   12520 C  CD  . GLN C 1 42   ? 58.327  73.152  66.194  1.00 273.94 ? 42   GLN B CD  1 
ATOM   12521 O  OE1 . GLN C 1 42   ? 57.270  73.523  65.694  1.00 274.24 ? 42   GLN B OE1 1 
ATOM   12522 N  NE2 . GLN C 1 42   ? 58.690  71.874  66.247  1.00 273.65 ? 42   GLN B NE2 1 
ATOM   12523 N  N   . VAL C 1 43   ? 59.811  76.523  68.598  1.00 189.61 ? 43   VAL B N   1 
ATOM   12524 C  CA  . VAL C 1 43   ? 58.975  77.612  69.092  1.00 184.35 ? 43   VAL B CA  1 
ATOM   12525 C  C   . VAL C 1 43   ? 58.809  78.794  68.163  1.00 190.61 ? 43   VAL B C   1 
ATOM   12526 O  O   . VAL C 1 43   ? 59.691  79.111  67.376  1.00 196.09 ? 43   VAL B O   1 
ATOM   12527 C  CB  . VAL C 1 43   ? 59.466  78.091  70.491  1.00 176.66 ? 43   VAL B CB  1 
ATOM   12528 C  CG1 . VAL C 1 43   ? 60.816  78.790  70.403  1.00 178.85 ? 43   VAL B CG1 1 
ATOM   12529 C  CG2 . VAL C 1 43   ? 58.438  78.984  71.131  1.00 169.06 ? 43   VAL B CG2 1 
ATOM   12530 N  N   . TYR C 1 44   ? 57.651  79.432  68.271  1.00 280.64 ? 44   TYR B N   1 
ATOM   12531 C  CA  . TYR C 1 44   ? 57.321  80.594  67.468  1.00 287.76 ? 44   TYR B CA  1 
ATOM   12532 C  C   . TYR C 1 44   ? 57.727  81.912  68.142  1.00 305.90 ? 44   TYR B C   1 
ATOM   12533 O  O   . TYR C 1 44   ? 57.138  82.966  67.890  1.00 301.83 ? 44   TYR B O   1 
ATOM   12534 C  CB  . TYR C 1 44   ? 55.826  80.589  67.171  1.00 293.49 ? 44   TYR B CB  1 
ATOM   12535 C  CG  . TYR C 1 44   ? 55.456  81.404  65.961  1.00 307.65 ? 44   TYR B CG  1 
ATOM   12536 C  CD1 . TYR C 1 44   ? 55.609  80.887  64.687  1.00 315.67 ? 44   TYR B CD1 1 
ATOM   12537 C  CD2 . TYR C 1 44   ? 54.961  82.692  66.092  1.00 311.80 ? 44   TYR B CD2 1 
ATOM   12538 C  CE1 . TYR C 1 44   ? 55.282  81.629  63.579  1.00 319.94 ? 44   TYR B CE1 1 
ATOM   12539 C  CE2 . TYR C 1 44   ? 54.626  83.441  64.984  1.00 316.06 ? 44   TYR B CE2 1 
ATOM   12540 C  CZ  . TYR C 1 44   ? 54.786  82.903  63.730  1.00 319.49 ? 44   TYR B CZ  1 
ATOM   12541 O  OH  . TYR C 1 44   ? 54.450  83.648  62.626  1.00 321.19 ? 44   TYR B OH  1 
ATOM   12542 N  N   . GLY C 1 45   ? 58.733  81.855  69.007  1.00 223.38 ? 45   GLY B N   1 
ATOM   12543 C  CA  . GLY C 1 45   ? 59.176  83.042  69.714  1.00 225.16 ? 45   GLY B CA  1 
ATOM   12544 C  C   . GLY C 1 45   ? 59.749  84.044  68.742  1.00 228.92 ? 45   GLY B C   1 
ATOM   12545 O  O   . GLY C 1 45   ? 60.131  83.675  67.631  1.00 230.06 ? 45   GLY B O   1 
ATOM   12546 N  N   . TYR C 1 46   ? 59.806  85.306  69.162  1.00 265.04 ? 46   TYR B N   1 
ATOM   12547 C  CA  . TYR C 1 46   ? 60.338  86.397  68.337  1.00 271.91 ? 46   TYR B CA  1 
ATOM   12548 C  C   . TYR C 1 46   ? 61.860  86.547  68.429  1.00 275.92 ? 46   TYR B C   1 
ATOM   12549 O  O   . TYR C 1 46   ? 62.516  85.834  69.190  1.00 280.64 ? 46   TYR B O   1 
ATOM   12550 C  CB  . TYR C 1 46   ? 59.686  87.710  68.741  1.00 274.04 ? 46   TYR B CB  1 
ATOM   12551 C  CG  . TYR C 1 46   ? 59.654  87.849  70.226  1.00 274.83 ? 46   TYR B CG  1 
ATOM   12552 C  CD1 . TYR C 1 46   ? 60.804  88.164  70.933  1.00 278.77 ? 46   TYR B CD1 1 
ATOM   12553 C  CD2 . TYR C 1 46   ? 58.489  87.613  70.933  1.00 271.58 ? 46   TYR B CD2 1 
ATOM   12554 C  CE1 . TYR C 1 46   ? 60.787  88.272  72.299  1.00 277.69 ? 46   TYR B CE1 1 
ATOM   12555 C  CE2 . TYR C 1 46   ? 58.458  87.720  72.300  1.00 270.40 ? 46   TYR B CE2 1 
ATOM   12556 C  CZ  . TYR C 1 46   ? 59.612  88.050  72.977  1.00 273.80 ? 46   TYR B CZ  1 
ATOM   12557 O  OH  . TYR C 1 46   ? 59.593  88.156  74.343  1.00 272.74 ? 46   TYR B OH  1 
ATOM   12558 N  N   . THR C 1 47   ? 62.393  87.510  67.669  1.00 409.06 ? 47   THR B N   1 
ATOM   12559 C  CA  . THR C 1 47   ? 63.834  87.640  67.398  1.00 409.33 ? 47   THR B CA  1 
ATOM   12560 C  C   . THR C 1 47   ? 64.728  87.384  68.605  1.00 407.34 ? 47   THR B C   1 
ATOM   12561 O  O   . THR C 1 47   ? 65.870  86.945  68.464  1.00 409.58 ? 47   THR B O   1 
ATOM   12562 C  CB  . THR C 1 47   ? 64.196  89.030  66.805  1.00 448.32 ? 47   THR B CB  1 
ATOM   12563 O  OG1 . THR C 1 47   ? 63.371  89.306  65.668  1.00 447.63 ? 47   THR B OG1 1 
ATOM   12564 C  CG2 . THR C 1 47   ? 65.659  89.073  66.376  1.00 452.18 ? 47   THR B CG2 1 
ATOM   12565 N  N   . GLU C 1 48   ? 64.207  87.660  69.792  1.00 338.62 ? 48   GLU B N   1 
ATOM   12566 C  CA  . GLU C 1 48   ? 64.979  87.479  71.006  1.00 337.41 ? 48   GLU B CA  1 
ATOM   12567 C  C   . GLU C 1 48   ? 65.354  86.020  71.224  1.00 333.26 ? 48   GLU B C   1 
ATOM   12568 O  O   . GLU C 1 48   ? 64.509  85.207  71.609  1.00 329.28 ? 48   GLU B O   1 
ATOM   12569 C  CB  . GLU C 1 48   ? 64.192  87.994  72.207  1.00 334.49 ? 48   GLU B CB  1 
ATOM   12570 C  CG  . GLU C 1 48   ? 65.037  88.159  73.445  1.00 335.14 ? 48   GLU B CG  1 
ATOM   12571 C  CD  . GLU C 1 48   ? 66.219  89.073  73.205  1.00 339.21 ? 48   GLU B CD  1 
ATOM   12572 O  OE1 . GLU C 1 48   ? 66.173  89.876  72.247  1.00 340.19 ? 48   GLU B OE1 1 
ATOM   12573 O  OE2 . GLU C 1 48   ? 67.197  88.990  73.974  1.00 340.90 ? 48   GLU B OE2 1 
ATOM   12574 N  N   . ALA C 1 49   ? 66.619  85.691  70.977  1.00 317.75 ? 49   ALA B N   1 
ATOM   12575 C  CA  . ALA C 1 49   ? 67.129  84.364  71.293  1.00 314.41 ? 49   ALA B CA  1 
ATOM   12576 C  C   . ALA C 1 49   ? 66.913  84.130  72.785  1.00 308.91 ? 49   ALA B C   1 
ATOM   12577 O  O   . ALA C 1 49   ? 66.851  85.090  73.555  1.00 308.73 ? 49   ALA B O   1 
ATOM   12578 C  CB  . ALA C 1 49   ? 68.605  84.264  70.939  1.00 319.32 ? 49   ALA B CB  1 
ATOM   12579 N  N   . PHE C 1 50   ? 66.785  82.873  73.203  1.00 331.78 ? 50   PHE B N   1 
ATOM   12580 C  CA  . PHE C 1 50   ? 66.529  82.599  74.620  1.00 328.92 ? 50   PHE B CA  1 
ATOM   12581 C  C   . PHE C 1 50   ? 66.831  81.173  75.090  1.00 323.36 ? 50   PHE B C   1 
ATOM   12582 O  O   . PHE C 1 50   ? 66.688  80.207  74.339  1.00 321.50 ? 50   PHE B O   1 
ATOM   12583 C  CB  . PHE C 1 50   ? 65.104  83.016  75.006  1.00 331.93 ? 50   PHE B CB  1 
ATOM   12584 C  CG  . PHE C 1 50   ? 64.021  82.197  74.360  1.00 337.78 ? 50   PHE B CG  1 
ATOM   12585 C  CD1 . PHE C 1 50   ? 63.227  81.359  75.124  1.00 337.79 ? 50   PHE B CD1 1 
ATOM   12586 C  CD2 . PHE C 1 50   ? 63.782  82.277  72.999  1.00 343.95 ? 50   PHE B CD2 1 
ATOM   12587 C  CE1 . PHE C 1 50   ? 62.225  80.613  74.542  1.00 337.64 ? 50   PHE B CE1 1 
ATOM   12588 C  CE2 . PHE C 1 50   ? 62.779  81.530  72.415  1.00 343.25 ? 50   PHE B CE2 1 
ATOM   12589 C  CZ  . PHE C 1 50   ? 62.002  80.698  73.185  1.00 340.14 ? 50   PHE B CZ  1 
ATOM   12590 N  N   . ASP C 1 51   ? 67.246  81.068  76.350  1.00 239.56 ? 51   ASP B N   1 
ATOM   12591 C  CA  . ASP C 1 51   ? 67.714  79.808  76.935  1.00 237.71 ? 51   ASP B CA  1 
ATOM   12592 C  C   . ASP C 1 51   ? 66.601  78.814  77.285  1.00 232.89 ? 51   ASP B C   1 
ATOM   12593 O  O   . ASP C 1 51   ? 65.453  79.212  77.500  1.00 230.08 ? 51   ASP B O   1 
ATOM   12594 C  CB  . ASP C 1 51   ? 68.560  80.083  78.178  1.00 236.42 ? 51   ASP B CB  1 
ATOM   12595 C  CG  . ASP C 1 51   ? 70.048  79.945  77.920  1.00 239.18 ? 51   ASP B CG  1 
ATOM   12596 O  OD1 . ASP C 1 51   ? 70.503  80.220  76.791  1.00 240.46 ? 51   ASP B OD1 1 
ATOM   12597 O  OD2 . ASP C 1 51   ? 70.767  79.568  78.866  1.00 239.77 ? 51   ASP B OD2 1 
ATOM   12598 N  N   . ALA C 1 52   ? 66.964  77.527  77.356  1.00 281.13 ? 52   ALA B N   1 
ATOM   12599 C  CA  . ALA C 1 52   ? 66.016  76.430  77.620  1.00 273.68 ? 52   ALA B CA  1 
ATOM   12600 C  C   . ALA C 1 52   ? 66.639  75.191  78.283  1.00 272.56 ? 52   ALA B C   1 
ATOM   12601 O  O   . ALA C 1 52   ? 67.345  74.415  77.633  1.00 275.89 ? 52   ALA B O   1 
ATOM   12602 C  CB  . ALA C 1 52   ? 65.309  76.017  76.334  1.00 271.18 ? 52   ALA B CB  1 
ATOM   12603 N  N   . THR C 1 53   ? 66.349  75.004  79.572  1.00 244.88 ? 53   THR B N   1 
ATOM   12604 C  CA  . THR C 1 53   ? 66.762  73.804  80.312  1.00 242.32 ? 53   THR B CA  1 
ATOM   12605 C  C   . THR C 1 53   ? 65.582  72.932  80.733  1.00 235.30 ? 53   THR B C   1 
ATOM   12606 O  O   . THR C 1 53   ? 64.680  73.384  81.438  1.00 230.73 ? 53   THR B O   1 
ATOM   12607 C  CB  . THR C 1 53   ? 67.545  74.143  81.594  1.00 248.33 ? 53   THR B CB  1 
ATOM   12608 O  OG1 . THR C 1 53   ? 68.914  74.398  81.271  1.00 253.55 ? 53   THR B OG1 1 
ATOM   12609 C  CG2 . THR C 1 53   ? 67.491  72.974  82.562  1.00 245.55 ? 53   THR B CG2 1 
ATOM   12610 N  N   . ILE C 1 54   ? 65.614  71.672  80.318  1.00 190.38 ? 54   ILE B N   1 
ATOM   12611 C  CA  . ILE C 1 54   ? 64.582  70.705  80.666  1.00 184.71 ? 54   ILE B CA  1 
ATOM   12612 C  C   . ILE C 1 54   ? 65.142  69.780  81.726  1.00 181.62 ? 54   ILE B C   1 
ATOM   12613 O  O   . ILE C 1 54   ? 66.359  69.714  81.908  1.00 181.57 ? 54   ILE B O   1 
ATOM   12614 C  CB  . ILE C 1 54   ? 64.210  69.834  79.451  1.00 188.03 ? 54   ILE B CB  1 
ATOM   12615 C  CG1 . ILE C 1 54   ? 64.015  70.694  78.199  1.00 190.05 ? 54   ILE B CG1 1 
ATOM   12616 C  CG2 . ILE C 1 54   ? 62.975  68.987  79.732  1.00 182.91 ? 54   ILE B CG2 1 
ATOM   12617 C  CD1 . ILE C 1 54   ? 63.853  69.878  76.911  1.00 190.94 ? 54   ILE B CD1 1 
ATOM   12618 N  N   . SER C 1 55   ? 64.253  69.064  82.412  1.00 176.17 ? 55   SER B N   1 
ATOM   12619 C  CA  . SER C 1 55   ? 64.647  68.030  83.363  1.00 178.13 ? 55   SER B CA  1 
ATOM   12620 C  C   . SER C 1 55   ? 63.464  67.211  83.859  1.00 176.21 ? 55   SER B C   1 
ATOM   12621 O  O   . SER C 1 55   ? 62.299  67.534  83.611  1.00 171.75 ? 55   SER B O   1 
ATOM   12622 C  CB  . SER C 1 55   ? 65.417  68.624  84.549  1.00 180.74 ? 55   SER B CB  1 
ATOM   12623 O  OG  . SER C 1 55   ? 64.647  69.584  85.257  1.00 179.42 ? 55   SER B OG  1 
ATOM   12624 N  N   . ILE C 1 56   ? 63.791  66.154  84.584  1.00 239.34 ? 56   ILE B N   1 
ATOM   12625 C  CA  . ILE C 1 56   ? 62.835  65.130  84.937  1.00 243.00 ? 56   ILE B CA  1 
ATOM   12626 C  C   . ILE C 1 56   ? 62.675  65.073  86.447  1.00 245.10 ? 56   ILE B C   1 
ATOM   12627 O  O   . ILE C 1 56   ? 63.603  64.701  87.157  1.00 245.30 ? 56   ILE B O   1 
ATOM   12628 C  CB  . ILE C 1 56   ? 63.344  63.796  84.406  1.00 249.00 ? 56   ILE B CB  1 
ATOM   12629 C  CG1 . ILE C 1 56   ? 64.835  63.645  84.724  1.00 255.92 ? 56   ILE B CG1 1 
ATOM   12630 C  CG2 . ILE C 1 56   ? 63.177  63.745  82.891  1.00 258.42 ? 56   ILE B CG2 1 
ATOM   12631 C  CD1 . ILE C 1 56   ? 65.534  62.574  83.892  1.00 261.25 ? 56   ILE B CD1 1 
ATOM   12632 N  N   . LYS C 1 57   ? 61.500  65.451  86.937  1.00 262.90 ? 57   LYS B N   1 
ATOM   12633 C  CA  . LYS C 1 57   ? 61.285  65.555  88.379  1.00 264.38 ? 57   LYS B CA  1 
ATOM   12634 C  C   . LYS C 1 57   ? 60.118  64.706  88.871  1.00 261.71 ? 57   LYS B C   1 
ATOM   12635 O  O   . LYS C 1 57   ? 59.160  64.461  88.136  1.00 261.23 ? 57   LYS B O   1 
ATOM   12636 C  CB  . LYS C 1 57   ? 61.141  67.018  88.815  1.00 263.58 ? 57   LYS B CB  1 
ATOM   12637 C  CG  . LYS C 1 57   ? 62.448  67.795  88.709  1.00 266.86 ? 57   LYS B CG  1 
ATOM   12638 C  CD  . LYS C 1 57   ? 62.267  69.285  88.923  1.00 266.02 ? 57   LYS B CD  1 
ATOM   12639 C  CE  . LYS C 1 57   ? 63.565  70.024  88.640  1.00 270.34 ? 57   LYS B CE  1 
ATOM   12640 N  NZ  . LYS C 1 57   ? 63.392  71.493  88.721  1.00 271.12 ? 57   LYS B NZ  1 
ATOM   12641 N  N   . SER C 1 58   ? 60.223  64.274  90.127  1.00 294.02 ? 58   SER B N   1 
ATOM   12642 C  CA  . SER C 1 58   ? 59.380  63.223  90.704  1.00 291.56 ? 58   SER B CA  1 
ATOM   12643 C  C   . SER C 1 58   ? 58.036  63.710  91.236  1.00 285.70 ? 58   SER B C   1 
ATOM   12644 O  O   . SER C 1 58   ? 57.957  64.780  91.833  1.00 285.81 ? 58   SER B O   1 
ATOM   12645 C  CB  . SER C 1 58   ? 60.141  62.520  91.829  1.00 293.72 ? 58   SER B CB  1 
ATOM   12646 O  OG  . SER C 1 58   ? 60.641  63.462  92.767  1.00 296.09 ? 58   SER B OG  1 
ATOM   12647 N  N   . TYR C 1 59   ? 57.008  62.876  91.065  1.00 232.99 ? 59   TYR B N   1 
ATOM   12648 C  CA  . TYR C 1 59   ? 55.595  63.236  91.277  1.00 228.30 ? 59   TYR B CA  1 
ATOM   12649 C  C   . TYR C 1 59   ? 55.255  64.671  91.805  1.00 256.92 ? 59   TYR B C   1 
ATOM   12650 O  O   . TYR C 1 59   ? 55.534  65.638  91.086  1.00 261.02 ? 59   TYR B O   1 
ATOM   12651 C  CB  . TYR C 1 59   ? 54.815  62.106  91.963  1.00 222.88 ? 59   TYR B CB  1 
ATOM   12652 C  CG  . TYR C 1 59   ? 53.348  62.171  91.623  1.00 217.51 ? 59   TYR B CG  1 
ATOM   12653 C  CD1 . TYR C 1 59   ? 52.942  62.648  90.387  1.00 217.68 ? 59   TYR B CD1 1 
ATOM   12654 C  CD2 . TYR C 1 59   ? 52.372  61.780  92.528  1.00 212.04 ? 59   TYR B CD2 1 
ATOM   12655 C  CE1 . TYR C 1 59   ? 51.612  62.735  90.050  1.00 213.53 ? 59   TYR B CE1 1 
ATOM   12656 C  CE2 . TYR C 1 59   ? 51.027  61.862  92.199  1.00 207.93 ? 59   TYR B CE2 1 
ATOM   12657 C  CZ  . TYR C 1 59   ? 50.655  62.341  90.952  1.00 208.72 ? 59   TYR B CZ  1 
ATOM   12658 O  OH  . TYR C 1 59   ? 49.332  62.436  90.584  1.00 204.95 ? 59   TYR B OH  1 
ATOM   12659 N  N   . PRO C 1 60   ? 54.638  64.829  93.020  1.00 225.48 ? 60   PRO B N   1 
ATOM   12660 C  CA  . PRO C 1 60   ? 54.207  66.201  93.385  1.00 221.85 ? 60   PRO B CA  1 
ATOM   12661 C  C   . PRO C 1 60   ? 55.294  67.192  93.882  1.00 220.38 ? 60   PRO B C   1 
ATOM   12662 O  O   . PRO C 1 60   ? 55.178  68.405  93.647  1.00 220.17 ? 60   PRO B O   1 
ATOM   12663 C  CB  . PRO C 1 60   ? 53.140  65.956  94.469  1.00 218.90 ? 60   PRO B CB  1 
ATOM   12664 C  CG  . PRO C 1 60   ? 52.763  64.503  94.326  1.00 216.99 ? 60   PRO B CG  1 
ATOM   12665 C  CD  . PRO C 1 60   ? 54.066  63.858  93.969  1.00 220.91 ? 60   PRO B CD  1 
ATOM   12666 N  N   . ASP C 1 61   ? 56.324  66.684  94.555  1.00 224.91 ? 61   ASP B N   1 
ATOM   12667 C  CA  . ASP C 1 61   ? 57.442  67.510  95.008  1.00 225.69 ? 61   ASP B CA  1 
ATOM   12668 C  C   . ASP C 1 61   ? 58.507  67.636  93.933  1.00 228.02 ? 61   ASP B C   1 
ATOM   12669 O  O   . ASP C 1 61   ? 59.288  66.711  93.713  1.00 228.90 ? 61   ASP B O   1 
ATOM   12670 C  CB  . ASP C 1 61   ? 58.087  66.885  96.241  1.00 226.46 ? 61   ASP B CB  1 
ATOM   12671 C  CG  . ASP C 1 61   ? 58.754  65.552  95.934  1.00 229.02 ? 61   ASP B CG  1 
ATOM   12672 O  OD1 . ASP C 1 61   ? 59.976  65.533  95.658  1.00 233.61 ? 61   ASP B OD1 1 
ATOM   12673 O  OD2 . ASP C 1 61   ? 58.046  64.525  95.956  1.00 225.53 ? 61   ASP B OD2 1 
ATOM   12674 N  N   . LYS C 1 62   ? 58.558  68.774  93.261  1.00 272.46 ? 62   LYS B N   1 
ATOM   12675 C  CA  . LYS C 1 62   ? 59.590  68.956  92.252  1.00 275.89 ? 62   LYS B CA  1 
ATOM   12676 C  C   . LYS C 1 62   ? 60.980  68.998  92.897  1.00 279.49 ? 62   LYS B C   1 
ATOM   12677 O  O   . LYS C 1 62   ? 61.785  69.876  92.594  1.00 285.08 ? 62   LYS B O   1 
ATOM   12678 C  CB  . LYS C 1 62   ? 59.317  70.202  91.404  1.00 273.85 ? 62   LYS B CB  1 
ATOM   12679 C  CG  . LYS C 1 62   ? 58.325  69.966  90.270  1.00 267.50 ? 62   LYS B CG  1 
ATOM   12680 C  CD  . LYS C 1 62   ? 57.719  71.264  89.785  1.00 262.06 ? 62   LYS B CD  1 
ATOM   12681 C  CE  . LYS C 1 62   ? 56.577  70.995  88.835  1.00 255.16 ? 62   LYS B CE  1 
ATOM   12682 N  NZ  . LYS C 1 62   ? 55.809  72.234  88.563  1.00 251.55 ? 62   LYS B NZ  1 
ATOM   12683 N  N   . LYS C 1 63   ? 61.254  68.041  93.784  1.00 297.10 ? 63   LYS B N   1 
ATOM   12684 C  CA  . LYS C 1 63   ? 62.529  67.983  94.501  1.00 299.02 ? 63   LYS B CA  1 
ATOM   12685 C  C   . LYS C 1 63   ? 63.638  67.221  93.770  1.00 300.16 ? 63   LYS B C   1 
ATOM   12686 O  O   . LYS C 1 63   ? 64.647  67.816  93.394  1.00 304.27 ? 63   LYS B O   1 
ATOM   12687 C  CB  . LYS C 1 63   ? 62.338  67.432  95.916  1.00 297.50 ? 63   LYS B CB  1 
ATOM   12688 C  CG  . LYS C 1 63   ? 61.555  68.367  96.826  1.00 297.91 ? 63   LYS B CG  1 
ATOM   12689 C  CD  . LYS C 1 63   ? 62.139  69.774  96.807  1.00 303.94 ? 63   LYS B CD  1 
ATOM   12690 C  CE  . LYS C 1 63   ? 63.578  69.778  97.296  1.00 308.63 ? 63   LYS B CE  1 
ATOM   12691 N  NZ  . LYS C 1 63   ? 64.205  71.119  97.162  1.00 312.80 ? 63   LYS B NZ  1 
ATOM   12692 N  N   . PHE C 1 64   ? 63.469  65.915  93.577  1.00 228.59 ? 64   PHE B N   1 
ATOM   12693 C  CA  . PHE C 1 64   ? 64.467  65.147  92.832  1.00 228.37 ? 64   PHE B CA  1 
ATOM   12694 C  C   . PHE C 1 64   ? 64.488  65.587  91.364  1.00 230.79 ? 64   PHE B C   1 
ATOM   12695 O  O   . PHE C 1 64   ? 63.442  65.848  90.766  1.00 228.68 ? 64   PHE B O   1 
ATOM   12696 C  CB  . PHE C 1 64   ? 64.202  63.639  92.931  1.00 223.47 ? 64   PHE B CB  1 
ATOM   12697 C  CG  . PHE C 1 64   ? 65.293  62.857  93.635  1.00 222.05 ? 64   PHE B CG  1 
ATOM   12698 C  CD1 . PHE C 1 64   ? 65.037  62.235  94.854  1.00 217.43 ? 64   PHE B CD1 1 
ATOM   12699 C  CD2 . PHE C 1 64   ? 66.558  62.723  93.073  1.00 224.55 ? 64   PHE B CD2 1 
ATOM   12700 C  CE1 . PHE C 1 64   ? 66.021  61.503  95.506  1.00 217.31 ? 64   PHE B CE1 1 
ATOM   12701 C  CE2 . PHE C 1 64   ? 67.548  61.992  93.721  1.00 224.52 ? 64   PHE B CE2 1 
ATOM   12702 C  CZ  . PHE C 1 64   ? 67.277  61.381  94.940  1.00 220.99 ? 64   PHE B CZ  1 
ATOM   12703 N  N   . SER C 1 65   ? 65.688  65.676  90.799  1.00 284.37 ? 65   SER B N   1 
ATOM   12704 C  CA  . SER C 1 65   ? 65.858  65.959  89.379  1.00 288.20 ? 65   SER B CA  1 
ATOM   12705 C  C   . SER C 1 65   ? 66.974  65.063  88.859  1.00 291.48 ? 65   SER B C   1 
ATOM   12706 O  O   . SER C 1 65   ? 68.155  65.284  89.135  1.00 296.00 ? 65   SER B O   1 
ATOM   12707 C  CB  . SER C 1 65   ? 66.175  67.436  89.130  1.00 292.94 ? 65   SER B CB  1 
ATOM   12708 O  OG  . SER C 1 65   ? 67.541  67.727  89.371  1.00 298.51 ? 65   SER B OG  1 
ATOM   12709 N  N   . TYR C 1 66   ? 66.575  64.039  88.116  1.00 262.52 ? 66   TYR B N   1 
ATOM   12710 C  CA  . TYR C 1 66   ? 67.481  62.989  87.688  1.00 260.21 ? 66   TYR B CA  1 
ATOM   12711 C  C   . TYR C 1 66   ? 68.531  63.516  86.701  1.00 265.81 ? 66   TYR B C   1 
ATOM   12712 O  O   . TYR C 1 66   ? 69.728  63.263  86.864  1.00 268.49 ? 66   TYR B O   1 
ATOM   12713 C  CB  . TYR C 1 66   ? 66.656  61.836  87.123  1.00 250.57 ? 66   TYR B CB  1 
ATOM   12714 C  CG  . TYR C 1 66   ? 65.443  61.531  87.986  1.00 238.19 ? 66   TYR B CG  1 
ATOM   12715 C  CD1 . TYR C 1 66   ? 65.553  60.712  89.096  1.00 233.09 ? 66   TYR B CD1 1 
ATOM   12716 C  CD2 . TYR C 1 66   ? 64.195  62.082  87.705  1.00 232.19 ? 66   TYR B CD2 1 
ATOM   12717 C  CE1 . TYR C 1 66   ? 64.462  60.432  89.901  1.00 225.02 ? 66   TYR B CE1 1 
ATOM   12718 C  CE2 . TYR C 1 66   ? 63.089  61.804  88.508  1.00 224.53 ? 66   TYR B CE2 1 
ATOM   12719 C  CZ  . TYR C 1 66   ? 63.235  60.972  89.610  1.00 220.02 ? 66   TYR B CZ  1 
ATOM   12720 O  OH  . TYR C 1 66   ? 62.167  60.670  90.432  1.00 211.06 ? 66   TYR B OH  1 
ATOM   12721 N  N   . SER C 1 67   ? 68.081  64.273  85.700  1.00 208.27 ? 67   SER B N   1 
ATOM   12722 C  CA  . SER C 1 67   ? 68.985  64.930  84.750  1.00 211.31 ? 67   SER B CA  1 
ATOM   12723 C  C   . SER C 1 67   ? 68.286  66.052  83.983  1.00 208.29 ? 67   SER B C   1 
ATOM   12724 O  O   . SER C 1 67   ? 67.076  66.251  84.109  1.00 203.14 ? 67   SER B O   1 
ATOM   12725 C  CB  . SER C 1 67   ? 69.613  63.924  83.775  1.00 213.97 ? 67   SER B CB  1 
ATOM   12726 O  OG  . SER C 1 67   ? 68.655  63.421  82.858  1.00 210.89 ? 67   SER B OG  1 
ATOM   12727 N  N   . SER C 1 68   ? 69.060  66.776  83.184  1.00 238.87 ? 68   SER B N   1 
ATOM   12728 C  CA  . SER C 1 68   ? 68.577  67.987  82.550  1.00 241.26 ? 68   SER B CA  1 
ATOM   12729 C  C   . SER C 1 68   ? 69.395  68.268  81.314  1.00 247.81 ? 68   SER B C   1 
ATOM   12730 O  O   . SER C 1 68   ? 70.188  67.431  80.891  1.00 248.06 ? 68   SER B O   1 
ATOM   12731 C  CB  . SER C 1 68   ? 68.790  69.157  83.480  1.00 242.68 ? 68   SER B CB  1 
ATOM   12732 O  OG  . SER C 1 68   ? 70.174  69.433  83.542  1.00 247.95 ? 68   SER B OG  1 
ATOM   12733 N  N   . GLY C 1 69   ? 69.227  69.463  80.756  1.00 233.41 ? 69   GLY B N   1 
ATOM   12734 C  CA  . GLY C 1 69   ? 69.928  69.821  79.540  1.00 242.26 ? 69   GLY B CA  1 
ATOM   12735 C  C   . GLY C 1 69   ? 69.775  71.277  79.174  1.00 245.45 ? 69   GLY B C   1 
ATOM   12736 O  O   . GLY C 1 69   ? 68.672  71.770  78.944  1.00 242.38 ? 69   GLY B O   1 
ATOM   12737 N  N   . HIS C 1 70   ? 70.905  71.964  79.115  1.00 331.40 ? 70   HIS B N   1 
ATOM   12738 C  CA  . HIS C 1 70   ? 70.915  73.382  78.827  1.00 335.18 ? 70   HIS B CA  1 
ATOM   12739 C  C   . HIS C 1 70   ? 70.939  73.585  77.323  1.00 334.64 ? 70   HIS B C   1 
ATOM   12740 O  O   . HIS C 1 70   ? 71.995  73.789  76.729  1.00 337.25 ? 70   HIS B O   1 
ATOM   12741 C  CB  . HIS C 1 70   ? 72.138  74.023  79.473  1.00 344.70 ? 70   HIS B CB  1 
ATOM   12742 C  CG  . HIS C 1 70   ? 71.951  75.466  79.821  1.00 351.57 ? 70   HIS B CG  1 
ATOM   12743 N  ND1 . HIS C 1 70   ? 71.464  75.879  81.043  1.00 351.23 ? 70   HIS B ND1 1 
ATOM   12744 C  CD2 . HIS C 1 70   ? 72.187  76.592  79.108  1.00 358.36 ? 70   HIS B CD2 1 
ATOM   12745 C  CE1 . HIS C 1 70   ? 71.407  77.198  81.067  1.00 353.91 ? 70   HIS B CE1 1 
ATOM   12746 N  NE2 . HIS C 1 70   ? 71.842  77.655  79.908  1.00 358.28 ? 70   HIS B NE2 1 
ATOM   12747 N  N   . VAL C 1 71   ? 69.771  73.524  76.703  1.00 251.14 ? 71   VAL B N   1 
ATOM   12748 C  CA  . VAL C 1 71   ? 69.711  73.579  75.255  1.00 252.76 ? 71   VAL B CA  1 
ATOM   12749 C  C   . VAL C 1 71   ? 69.193  74.924  74.734  1.00 253.01 ? 71   VAL B C   1 
ATOM   12750 O  O   . VAL C 1 71   ? 67.984  75.144  74.617  1.00 248.51 ? 71   VAL B O   1 
ATOM   12751 C  CB  . VAL C 1 71   ? 68.900  72.397  74.718  1.00 248.11 ? 71   VAL B CB  1 
ATOM   12752 C  CG1 . VAL C 1 71   ? 69.723  71.116  74.846  1.00 248.90 ? 71   VAL B CG1 1 
ATOM   12753 C  CG2 . VAL C 1 71   ? 67.593  72.271  75.482  1.00 241.59 ? 71   VAL B CG2 1 
ATOM   12754 N  N   . HIS C 1 72   ? 70.131  75.816  74.418  1.00 250.24 ? 72   HIS B N   1 
ATOM   12755 C  CA  . HIS C 1 72   ? 69.803  77.183  74.025  1.00 254.34 ? 72   HIS B CA  1 
ATOM   12756 C  C   . HIS C 1 72   ? 69.370  77.312  72.584  1.00 255.66 ? 72   HIS B C   1 
ATOM   12757 O  O   . HIS C 1 72   ? 70.106  76.951  71.671  1.00 259.58 ? 72   HIS B O   1 
ATOM   12758 C  CB  . HIS C 1 72   ? 70.978  78.133  74.271  1.00 264.16 ? 72   HIS B CB  1 
ATOM   12759 C  CG  . HIS C 1 72   ? 70.786  79.488  73.663  1.00 271.14 ? 72   HIS B CG  1 
ATOM   12760 N  ND1 . HIS C 1 72   ? 70.198  80.538  74.343  1.00 271.12 ? 72   HIS B ND1 1 
ATOM   12761 C  CD2 . HIS C 1 72   ? 71.087  79.966  72.433  1.00 277.33 ? 72   HIS B CD2 1 
ATOM   12762 C  CE1 . HIS C 1 72   ? 70.154  81.599  73.561  1.00 274.46 ? 72   HIS B CE1 1 
ATOM   12763 N  NE2 . HIS C 1 72   ? 70.688  81.279  72.393  1.00 278.18 ? 72   HIS B NE2 1 
ATOM   12764 N  N   . LEU C 1 73   ? 68.183  77.869  72.395  1.00 252.71 ? 73   LEU B N   1 
ATOM   12765 C  CA  . LEU C 1 73   ? 67.638  78.112  71.068  1.00 255.95 ? 73   LEU B CA  1 
ATOM   12766 C  C   . LEU C 1 73   ? 67.842  79.553  70.595  1.00 262.63 ? 73   LEU B C   1 
ATOM   12767 O  O   . LEU C 1 73   ? 68.132  80.446  71.387  1.00 262.12 ? 73   LEU B O   1 
ATOM   12768 C  CB  . LEU C 1 73   ? 66.148  77.768  71.052  1.00 247.65 ? 73   LEU B CB  1 
ATOM   12769 C  CG  . LEU C 1 73   ? 65.393  78.032  72.361  1.00 240.73 ? 73   LEU B CG  1 
ATOM   12770 C  CD1 . LEU C 1 73   ? 63.914  78.230  72.096  1.00 235.44 ? 73   LEU B CD1 1 
ATOM   12771 C  CD2 . LEU C 1 73   ? 65.627  76.901  73.339  1.00 238.06 ? 73   LEU B CD2 1 
ATOM   12772 N  N   . SER C 1 74   ? 67.683  79.767  69.294  1.00 309.67 ? 74   SER B N   1 
ATOM   12773 C  CA  . SER C 1 74   ? 67.839  81.089  68.705  1.00 316.01 ? 74   SER B CA  1 
ATOM   12774 C  C   . SER C 1 74   ? 67.323  81.062  67.277  1.00 321.02 ? 74   SER B C   1 
ATOM   12775 O  O   . SER C 1 74   ? 67.008  79.999  66.744  1.00 323.39 ? 74   SER B O   1 
ATOM   12776 C  CB  . SER C 1 74   ? 69.307  81.520  68.707  1.00 319.84 ? 74   SER B CB  1 
ATOM   12777 O  OG  . SER C 1 74   ? 70.029  80.880  67.666  1.00 322.30 ? 74   SER B OG  1 
ATOM   12778 N  N   . SER C 1 75   ? 67.234  82.234  66.659  1.00 272.85 ? 75   SER B N   1 
ATOM   12779 C  CA  . SER C 1 75   ? 66.831  82.319  65.264  1.00 278.01 ? 75   SER B CA  1 
ATOM   12780 C  C   . SER C 1 75   ? 67.830  81.572  64.380  1.00 283.34 ? 75   SER B C   1 
ATOM   12781 O  O   . SER C 1 75   ? 67.524  81.236  63.234  1.00 283.45 ? 75   SER B O   1 
ATOM   12782 C  CB  . SER C 1 75   ? 66.691  83.779  64.821  1.00 283.65 ? 75   SER B CB  1 
ATOM   12783 O  OG  . SER C 1 75   ? 65.474  84.342  65.280  1.00 281.51 ? 75   SER B OG  1 
ATOM   12784 N  N   . GLU C 1 76   ? 69.023  81.320  64.920  1.00 339.89 ? 76   GLU B N   1 
ATOM   12785 C  CA  . GLU C 1 76   ? 70.034  80.512  64.236  1.00 341.98 ? 76   GLU B CA  1 
ATOM   12786 C  C   . GLU C 1 76   ? 69.638  79.051  64.286  1.00 334.00 ? 76   GLU B C   1 
ATOM   12787 O  O   . GLU C 1 76   ? 69.921  78.276  63.370  1.00 337.23 ? 76   GLU B O   1 
ATOM   12788 C  CB  . GLU C 1 76   ? 71.401  80.666  64.897  1.00 347.42 ? 76   GLU B CB  1 
ATOM   12789 C  CG  . GLU C 1 76   ? 72.445  79.720  64.325  1.00 351.95 ? 76   GLU B CG  1 
ATOM   12790 C  CD  . GLU C 1 76   ? 73.737  79.747  65.101  1.00 354.47 ? 76   GLU B CD  1 
ATOM   12791 O  OE1 . GLU C 1 76   ? 73.800  80.475  66.113  1.00 352.15 ? 76   GLU B OE1 1 
ATOM   12792 O  OE2 . GLU C 1 76   ? 74.686  79.041  64.699  1.00 358.43 ? 76   GLU B OE2 1 
ATOM   12793 N  N   . ASN C 1 77   ? 69.001  78.683  65.390  1.00 292.11 ? 77   ASN B N   1 
ATOM   12794 C  CA  . ASN C 1 77   ? 68.467  77.347  65.559  1.00 281.66 ? 77   ASN B CA  1 
ATOM   12795 C  C   . ASN C 1 77   ? 66.965  77.341  65.313  1.00 264.28 ? 77   ASN B C   1 
ATOM   12796 O  O   . ASN C 1 77   ? 66.258  76.449  65.774  1.00 256.20 ? 77   ASN B O   1 
ATOM   12797 C  CB  . ASN C 1 77   ? 68.775  76.830  66.959  1.00 284.24 ? 77   ASN B CB  1 
ATOM   12798 C  CG  . ASN C 1 77   ? 68.962  75.338  66.988  1.00 291.67 ? 77   ASN B CG  1 
ATOM   12799 O  OD1 . ASN C 1 77   ? 68.729  74.654  65.993  1.00 295.86 ? 77   ASN B OD1 1 
ATOM   12800 N  ND2 . ASN C 1 77   ? 69.391  74.821  68.123  1.00 292.53 ? 77   ASN B ND2 1 
ATOM   12801 N  N   . LYS C 1 78   ? 66.490  78.354  64.594  1.00 244.65 ? 78   LYS B N   1 
ATOM   12802 C  CA  . LYS C 1 78   ? 65.069  78.529  64.314  1.00 232.32 ? 78   LYS B CA  1 
ATOM   12803 C  C   . LYS C 1 78   ? 64.233  78.185  65.524  1.00 220.51 ? 78   LYS B C   1 
ATOM   12804 O  O   . LYS C 1 78   ? 63.099  77.730  65.396  1.00 215.64 ? 78   LYS B O   1 
ATOM   12805 C  CB  . LYS C 1 78   ? 64.631  77.665  63.141  1.00 225.17 ? 78   LYS B CB  1 
ATOM   12806 C  CG  . LYS C 1 78   ? 65.384  77.947  61.855  1.00 220.14 ? 78   LYS B CG  1 
ATOM   12807 C  CD  . LYS C 1 78   ? 65.325  79.418  61.473  1.00 209.54 ? 78   LYS B CD  1 
ATOM   12808 C  CE  . LYS C 1 78   ? 65.953  79.665  60.109  1.00 205.67 ? 78   LYS B CE  1 
ATOM   12809 N  NZ  . LYS C 1 78   ? 66.107  81.126  59.879  1.00 204.78 ? 78   LYS B NZ  1 
ATOM   12810 N  N   . PHE C 1 79   ? 64.816  78.388  66.699  1.00 226.39 ? 79   PHE B N   1 
ATOM   12811 C  CA  . PHE C 1 79   ? 64.149  78.098  67.957  1.00 220.51 ? 79   PHE B CA  1 
ATOM   12812 C  C   . PHE C 1 79   ? 63.702  76.661  68.042  1.00 220.20 ? 79   PHE B C   1 
ATOM   12813 O  O   . PHE C 1 79   ? 62.511  76.369  68.047  1.00 217.53 ? 79   PHE B O   1 
ATOM   12814 C  CB  . PHE C 1 79   ? 62.968  79.035  68.167  1.00 215.51 ? 79   PHE B CB  1 
ATOM   12815 C  CG  . PHE C 1 79   ? 63.377  80.437  68.435  1.00 219.29 ? 79   PHE B CG  1 
ATOM   12816 C  CD1 . PHE C 1 79   ? 63.292  81.393  67.442  1.00 220.49 ? 79   PHE B CD1 1 
ATOM   12817 C  CD2 . PHE C 1 79   ? 63.898  80.787  69.669  1.00 219.30 ? 79   PHE B CD2 1 
ATOM   12818 C  CE1 . PHE C 1 79   ? 63.690  82.678  67.683  1.00 221.48 ? 79   PHE B CE1 1 
ATOM   12819 C  CE2 . PHE C 1 79   ? 64.301  82.068  69.919  1.00 220.59 ? 79   PHE B CE2 1 
ATOM   12820 C  CZ  . PHE C 1 79   ? 64.195  83.019  68.930  1.00 221.47 ? 79   PHE B CZ  1 
ATOM   12821 N  N   . GLN C 1 80   ? 64.677  75.768  68.104  1.00 274.14 ? 80   GLN B N   1 
ATOM   12822 C  CA  . GLN C 1 80   ? 64.413  74.353  68.263  1.00 274.69 ? 80   GLN B CA  1 
ATOM   12823 C  C   . GLN C 1 80   ? 65.642  73.724  68.887  1.00 276.00 ? 80   GLN B C   1 
ATOM   12824 O  O   . GLN C 1 80   ? 66.751  74.237  68.724  1.00 280.21 ? 80   GLN B O   1 
ATOM   12825 C  CB  . GLN C 1 80   ? 64.115  73.685  66.914  1.00 278.84 ? 80   GLN B CB  1 
ATOM   12826 C  CG  . GLN C 1 80   ? 62.934  74.263  66.136  1.00 278.69 ? 80   GLN B CG  1 
ATOM   12827 C  CD  . GLN C 1 80   ? 62.373  73.296  65.101  1.00 279.58 ? 80   GLN B CD  1 
ATOM   12828 O  OE1 . GLN C 1 80   ? 63.082  72.427  64.593  1.00 283.00 ? 80   GLN B OE1 1 
ATOM   12829 N  NE2 . GLN C 1 80   ? 61.093  73.446  64.783  1.00 276.18 ? 80   GLN B NE2 1 
ATOM   12830 N  N   . ASN C 1 81   ? 65.448  72.623  69.605  1.00 205.81 ? 81   ASN B N   1 
ATOM   12831 C  CA  . ASN C 1 81   ? 66.575  71.890  70.173  1.00 202.80 ? 81   ASN B CA  1 
ATOM   12832 C  C   . ASN C 1 81   ? 66.191  70.619  70.946  1.00 202.69 ? 81   ASN B C   1 
ATOM   12833 O  O   . ASN C 1 81   ? 65.075  70.492  71.459  1.00 195.46 ? 81   ASN B O   1 
ATOM   12834 C  CB  . ASN C 1 81   ? 67.429  72.810  71.045  1.00 208.10 ? 81   ASN B CB  1 
ATOM   12835 C  CG  . ASN C 1 81   ? 68.912  72.645  70.786  1.00 216.84 ? 81   ASN B CG  1 
ATOM   12836 O  OD1 . ASN C 1 81   ? 69.468  71.557  70.954  1.00 218.03 ? 81   ASN B OD1 1 
ATOM   12837 N  ND2 . ASN C 1 81   ? 69.563  73.729  70.385  1.00 222.06 ? 81   ASN B ND2 1 
ATOM   12838 N  N   . SER C 1 82   ? 67.140  69.687  71.033  1.00 204.72 ? 82   SER B N   1 
ATOM   12839 C  CA  . SER C 1 82   ? 66.900  68.361  71.604  1.00 203.13 ? 82   SER B CA  1 
ATOM   12840 C  C   . SER C 1 82   ? 67.585  68.119  72.950  1.00 204.95 ? 82   SER B C   1 
ATOM   12841 O  O   . SER C 1 82   ? 68.596  68.747  73.280  1.00 209.13 ? 82   SER B O   1 
ATOM   12842 C  CB  . SER C 1 82   ? 67.352  67.270  70.617  1.00 207.14 ? 82   SER B CB  1 
ATOM   12843 O  OG  . SER C 1 82   ? 66.530  67.219  69.461  1.00 207.00 ? 82   SER B OG  1 
ATOM   12844 N  N   . ALA C 1 83   ? 67.041  67.167  73.702  1.00 172.47 ? 83   ALA B N   1 
ATOM   12845 C  CA  . ALA C 1 83   ? 67.617  66.789  74.982  1.00 171.15 ? 83   ALA B CA  1 
ATOM   12846 C  C   . ALA C 1 83   ? 67.477  65.302  75.323  1.00 171.67 ? 83   ALA B C   1 
ATOM   12847 O  O   . ALA C 1 83   ? 66.379  64.740  75.272  1.00 170.13 ? 83   ALA B O   1 
ATOM   12848 C  CB  . ALA C 1 83   ? 67.002  67.626  76.080  1.00 166.95 ? 83   ALA B CB  1 
ATOM   12849 N  N   . ILE C 1 84   ? 68.602  64.679  75.679  1.00 216.66 ? 84   ILE B N   1 
ATOM   12850 C  CA  . ILE C 1 84   ? 68.599  63.340  76.273  1.00 213.02 ? 84   ILE B CA  1 
ATOM   12851 C  C   . ILE C 1 84   ? 68.530  63.390  77.811  1.00 208.30 ? 84   ILE B C   1 
ATOM   12852 O  O   . ILE C 1 84   ? 69.550  63.336  78.512  1.00 209.09 ? 84   ILE B O   1 
ATOM   12853 C  CB  . ILE C 1 84   ? 69.796  62.470  75.812  1.00 276.69 ? 84   ILE B CB  1 
ATOM   12854 C  CG1 . ILE C 1 84   ? 71.129  63.169  76.088  1.00 280.51 ? 84   ILE B CG1 1 
ATOM   12855 C  CG2 . ILE C 1 84   ? 69.661  62.120  74.343  1.00 279.02 ? 84   ILE B CG2 1 
ATOM   12856 C  CD1 . ILE C 1 84   ? 72.335  62.257  75.942  1.00 283.81 ? 84   ILE B CD1 1 
ATOM   12857 N  N   . LEU C 1 85   ? 67.306  63.514  78.316  1.00 243.44 ? 85   LEU B N   1 
ATOM   12858 C  CA  . LEU C 1 85   ? 67.015  63.317  79.729  1.00 236.69 ? 85   LEU B CA  1 
ATOM   12859 C  C   . LEU C 1 85   ? 67.277  61.851  79.994  1.00 231.14 ? 85   LEU B C   1 
ATOM   12860 O  O   . LEU C 1 85   ? 67.882  61.183  79.159  1.00 234.43 ? 85   LEU B O   1 
ATOM   12861 C  CB  . LEU C 1 85   ? 65.550  63.643  80.018  1.00 231.35 ? 85   LEU B CB  1 
ATOM   12862 C  CG  . LEU C 1 85   ? 65.100  65.060  79.643  1.00 231.74 ? 85   LEU B CG  1 
ATOM   12863 C  CD1 . LEU C 1 85   ? 66.075  66.080  80.207  1.00 235.18 ? 85   LEU B CD1 1 
ATOM   12864 C  CD2 . LEU C 1 85   ? 64.967  65.236  78.136  1.00 233.45 ? 85   LEU B CD2 1 
ATOM   12865 N  N   . THR C 1 86   ? 66.831  61.347  81.142  1.00 255.52 ? 86   THR B N   1 
ATOM   12866 C  CA  . THR C 1 86   ? 66.930  59.916  81.428  1.00 251.45 ? 86   THR B CA  1 
ATOM   12867 C  C   . THR C 1 86   ? 66.632  59.546  82.885  1.00 247.14 ? 86   THR B C   1 
ATOM   12868 O  O   . THR C 1 86   ? 67.460  59.775  83.765  1.00 246.15 ? 86   THR B O   1 
ATOM   12869 C  CB  . THR C 1 86   ? 68.327  59.348  81.043  1.00 242.05 ? 86   THR B CB  1 
ATOM   12870 O  OG1 . THR C 1 86   ? 68.333  57.926  81.213  1.00 242.02 ? 86   THR B OG1 1 
ATOM   12871 C  CG2 . THR C 1 86   ? 69.439  59.968  81.890  1.00 243.42 ? 86   THR B CG2 1 
ATOM   12872 N  N   . ILE C 1 87   ? 65.459  58.965  83.142  1.00 190.53 ? 87   ILE B N   1 
ATOM   12873 C  CA  . ILE C 1 87   ? 65.165  58.406  84.469  1.00 188.06 ? 87   ILE B CA  1 
ATOM   12874 C  C   . ILE C 1 87   ? 65.955  57.123  84.695  1.00 205.51 ? 87   ILE B C   1 
ATOM   12875 O  O   . ILE C 1 87   ? 65.637  56.093  84.106  1.00 209.48 ? 87   ILE B O   1 
ATOM   12876 C  CB  . ILE C 1 87   ? 63.679  57.998  84.644  1.00 170.27 ? 87   ILE B CB  1 
ATOM   12877 C  CG1 . ILE C 1 87   ? 62.749  59.198  84.689  1.00 163.41 ? 87   ILE B CG1 1 
ATOM   12878 C  CG2 . ILE C 1 87   ? 63.492  57.212  85.924  1.00 161.52 ? 87   ILE B CG2 1 
ATOM   12879 C  CD1 . ILE C 1 87   ? 61.332  58.798  85.044  1.00 158.97 ? 87   ILE B CD1 1 
ATOM   12880 N  N   . GLN C 1 88   ? 66.971  57.161  85.547  1.00 223.16 ? 88   GLN B N   1 
ATOM   12881 C  CA  . GLN C 1 88   ? 67.657  55.930  85.915  1.00 231.74 ? 88   GLN B CA  1 
ATOM   12882 C  C   . GLN C 1 88   ? 66.900  55.322  87.102  1.00 237.11 ? 88   GLN B C   1 
ATOM   12883 O  O   . GLN C 1 88   ? 65.809  55.786  87.418  1.00 233.70 ? 88   GLN B O   1 
ATOM   12884 C  CB  . GLN C 1 88   ? 69.132  56.210  86.199  1.00 237.14 ? 88   GLN B CB  1 
ATOM   12885 C  CG  . GLN C 1 88   ? 69.804  56.964  85.064  1.00 242.49 ? 88   GLN B CG  1 
ATOM   12886 C  CD  . GLN C 1 88   ? 71.195  56.457  84.760  1.00 248.00 ? 88   GLN B CD  1 
ATOM   12887 O  OE1 . GLN C 1 88   ? 72.019  57.178  84.196  1.00 252.67 ? 88   GLN B OE1 1 
ATOM   12888 N  NE2 . GLN C 1 88   ? 71.466  55.210  85.130  1.00 246.51 ? 88   GLN B NE2 1 
ATOM   12889 N  N   . PRO C 1 89   ? 67.437  54.255  87.720  1.00 229.70 ? 89   PRO B N   1 
ATOM   12890 C  CA  . PRO C 1 89   ? 66.853  53.594  88.910  1.00 229.32 ? 89   PRO B CA  1 
ATOM   12891 C  C   . PRO C 1 89   ? 67.003  54.267  90.312  1.00 223.56 ? 89   PRO B C   1 
ATOM   12892 O  O   . PRO C 1 89   ? 67.878  53.860  91.095  1.00 219.91 ? 89   PRO B O   1 
ATOM   12893 C  CB  . PRO C 1 89   ? 67.551  52.229  88.916  1.00 231.85 ? 89   PRO B CB  1 
ATOM   12894 C  CG  . PRO C 1 89   ? 68.002  52.027  87.501  1.00 234.89 ? 89   PRO B CG  1 
ATOM   12895 C  CD  . PRO C 1 89   ? 68.384  53.372  87.017  1.00 235.88 ? 89   PRO B CD  1 
ATOM   12896 N  N   . LYS C 1 90   ? 66.150  55.254  90.617  1.00 162.79 ? 90   LYS B N   1 
ATOM   12897 C  CA  . LYS C 1 90   ? 66.009  55.791  91.969  1.00 162.06 ? 90   LYS B CA  1 
ATOM   12898 C  C   . LYS C 1 90   ? 65.262  54.753  92.783  1.00 161.89 ? 90   LYS B C   1 
ATOM   12899 O  O   . LYS C 1 90   ? 65.849  53.754  93.209  1.00 162.78 ? 90   LYS B O   1 
ATOM   12900 C  CB  . LYS C 1 90   ? 65.203  57.092  91.988  1.00 160.77 ? 90   LYS B CB  1 
ATOM   12901 C  CG  . LYS C 1 90   ? 65.686  58.127  91.028  1.00 194.41 ? 90   LYS B CG  1 
ATOM   12902 C  CD  . LYS C 1 90   ? 67.141  58.494  91.242  1.00 190.31 ? 90   LYS B CD  1 
ATOM   12903 C  CE  . LYS C 1 90   ? 67.751  58.975  89.929  1.00 191.90 ? 90   LYS B CE  1 
ATOM   12904 N  NZ  . LYS C 1 90   ? 68.946  59.854  90.063  1.00 195.63 ? 90   LYS B NZ  1 
ATOM   12905 N  N   . GLN C 1 91   ? 63.957  54.983  92.946  1.00 308.60 ? 91   GLN B N   1 
ATOM   12906 C  CA  . GLN C 1 91   ? 63.067  54.154  93.768  1.00 321.00 ? 91   GLN B CA  1 
ATOM   12907 C  C   . GLN C 1 91   ? 63.172  52.650  93.514  1.00 336.94 ? 91   GLN B C   1 
ATOM   12908 O  O   . GLN C 1 91   ? 62.777  52.166  92.454  1.00 338.39 ? 91   GLN B O   1 
ATOM   12909 C  CB  . GLN C 1 91   ? 61.610  54.594  93.570  1.00 319.61 ? 91   GLN B CB  1 
ATOM   12910 C  CG  . GLN C 1 91   ? 61.325  55.997  94.051  1.00 322.58 ? 91   GLN B CG  1 
ATOM   12911 C  CD  . GLN C 1 91   ? 61.740  56.183  95.486  1.00 325.32 ? 91   GLN B CD  1 
ATOM   12912 O  OE1 . GLN C 1 91   ? 62.661  56.943  95.784  1.00 329.44 ? 91   GLN B OE1 1 
ATOM   12913 N  NE2 . GLN C 1 91   ? 61.076  55.471  96.389  1.00 322.74 ? 91   GLN B NE2 1 
ATOM   12914 N  N   . LEU C 1 92   ? 63.680  51.917  94.505  1.00 249.54 ? 92   LEU B N   1 
ATOM   12915 C  CA  . LEU C 1 92   ? 63.817  50.460  94.411  1.00 264.14 ? 92   LEU B CA  1 
ATOM   12916 C  C   . LEU C 1 92   ? 63.014  49.647  95.466  1.00 270.29 ? 92   LEU B C   1 
ATOM   12917 O  O   . LEU C 1 92   ? 63.154  48.420  95.527  1.00 269.96 ? 92   LEU B O   1 
ATOM   12918 C  CB  . LEU C 1 92   ? 65.308  50.041  94.434  1.00 272.36 ? 92   LEU B CB  1 
ATOM   12919 C  CG  . LEU C 1 92   ? 66.325  50.586  93.410  1.00 280.61 ? 92   LEU B CG  1 
ATOM   12920 C  CD1 . LEU C 1 92   ? 67.763  50.282  93.821  1.00 285.08 ? 92   LEU B CD1 1 
ATOM   12921 C  CD2 . LEU C 1 92   ? 66.059  50.053  92.020  1.00 282.49 ? 92   LEU B CD2 1 
ATOM   12922 N  N   . PRO C 1 93   ? 62.166  50.311  96.287  1.00 313.27 ? 93   PRO B N   1 
ATOM   12923 C  CA  . PRO C 1 93   ? 61.443  49.540  97.308  1.00 314.92 ? 93   PRO B CA  1 
ATOM   12924 C  C   . PRO C 1 93   ? 60.367  48.632  96.713  1.00 317.62 ? 93   PRO B C   1 
ATOM   12925 O  O   . PRO C 1 93   ? 59.274  49.111  96.408  1.00 316.97 ? 93   PRO B O   1 
ATOM   12926 C  CB  . PRO C 1 93   ? 60.769  50.627  98.160  1.00 311.25 ? 93   PRO B CB  1 
ATOM   12927 C  CG  . PRO C 1 93   ? 61.408  51.914  97.760  1.00 314.11 ? 93   PRO B CG  1 
ATOM   12928 C  CD  . PRO C 1 93   ? 61.793  51.734  96.335  1.00 316.06 ? 93   PRO B CD  1 
ATOM   12929 N  N   . GLY C 1 94   ? 60.666  47.344  96.563  1.00 321.53 ? 94   GLY B N   1 
ATOM   12930 C  CA  . GLY C 1 94   ? 59.693  46.390  96.059  1.00 321.74 ? 94   GLY B CA  1 
ATOM   12931 C  C   . GLY C 1 94   ? 58.443  46.396  96.916  1.00 319.15 ? 94   GLY B C   1 
ATOM   12932 O  O   . GLY C 1 94   ? 58.523  46.535  98.133  1.00 318.44 ? 94   GLY B O   1 
ATOM   12933 N  N   . GLY C 1 95   ? 57.286  46.243  96.285  1.00 317.66 ? 95   GLY B N   1 
ATOM   12934 C  CA  . GLY C 1 95   ? 56.028  46.330  97.003  1.00 313.06 ? 95   GLY B CA  1 
ATOM   12935 C  C   . GLY C 1 95   ? 55.411  47.711  96.892  1.00 313.23 ? 95   GLY B C   1 
ATOM   12936 O  O   . GLY C 1 95   ? 54.298  47.852  96.387  1.00 311.02 ? 95   GLY B O   1 
ATOM   12937 N  N   . GLN C 1 96   ? 56.124  48.733  97.363  1.00 317.01 ? 96   GLN B N   1 
ATOM   12938 C  CA  . GLN C 1 96   ? 55.696  50.108  97.141  1.00 315.60 ? 96   GLN B CA  1 
ATOM   12939 C  C   . GLN C 1 96   ? 55.399  50.205  95.655  1.00 319.36 ? 96   GLN B C   1 
ATOM   12940 O  O   . GLN C 1 96   ? 56.075  49.561  94.858  1.00 324.45 ? 96   GLN B O   1 
ATOM   12941 C  CB  . GLN C 1 96   ? 56.808  51.090  97.533  1.00 314.95 ? 96   GLN B CB  1 
ATOM   12942 C  CG  . GLN C 1 96   ? 56.530  52.546  97.168  1.00 313.25 ? 96   GLN B CG  1 
ATOM   12943 C  CD  . GLN C 1 96   ? 57.697  53.467  97.481  1.00 315.81 ? 96   GLN B CD  1 
ATOM   12944 O  OE1 . GLN C 1 96   ? 58.647  53.073  98.156  1.00 317.01 ? 96   GLN B OE1 1 
ATOM   12945 N  NE2 . GLN C 1 96   ? 57.629  54.701  96.990  1.00 317.15 ? 96   GLN B NE2 1 
ATOM   12946 N  N   . ASN C 1 97   ? 54.368  50.957  95.282  1.00 335.41 ? 97   ASN B N   1 
ATOM   12947 C  CA  . ASN C 1 97   ? 54.066  51.189  93.873  1.00 335.00 ? 97   ASN B CA  1 
ATOM   12948 C  C   . ASN C 1 97   ? 54.884  52.359  93.358  1.00 332.62 ? 97   ASN B C   1 
ATOM   12949 O  O   . ASN C 1 97   ? 54.332  53.415  93.051  1.00 332.85 ? 97   ASN B O   1 
ATOM   12950 C  CB  . ASN C 1 97   ? 52.582  51.490  93.677  1.00 335.60 ? 97   ASN B CB  1 
ATOM   12951 C  CG  . ASN C 1 97   ? 51.691  50.405  94.229  1.00 333.93 ? 97   ASN B CG  1 
ATOM   12952 O  OD1 . ASN C 1 97   ? 52.136  49.284  94.466  1.00 335.08 ? 97   ASN B OD1 1 
ATOM   12953 N  ND2 . ASN C 1 97   ? 50.423  50.731  94.438  1.00 330.95 ? 97   ASN B ND2 1 
ATOM   12954 N  N   . PRO C 1 98   ? 56.206  52.174  93.246  1.00 374.92 ? 98   PRO B N   1 
ATOM   12955 C  CA  . PRO C 1 98   ? 57.064  53.332  93.029  1.00 369.96 ? 98   PRO B CA  1 
ATOM   12956 C  C   . PRO C 1 98   ? 56.979  53.714  91.572  1.00 357.97 ? 98   PRO B C   1 
ATOM   12957 O  O   . PRO C 1 98   ? 56.406  52.965  90.782  1.00 358.19 ? 98   PRO B O   1 
ATOM   12958 C  CB  . PRO C 1 98   ? 58.468  52.777  93.314  1.00 377.46 ? 98   PRO B CB  1 
ATOM   12959 C  CG  . PRO C 1 98   ? 58.299  51.255  93.459  1.00 378.10 ? 98   PRO B CG  1 
ATOM   12960 C  CD  . PRO C 1 98   ? 56.932  50.935  92.945  1.00 376.22 ? 98   PRO B CD  1 
ATOM   12961 N  N   . VAL C 1 99   ? 57.527  54.866  91.218  1.00 350.01 ? 99   VAL B N   1 
ATOM   12962 C  CA  . VAL C 1 99   ? 57.790  55.144  89.819  1.00 337.68 ? 99   VAL B CA  1 
ATOM   12963 C  C   . VAL C 1 99   ? 56.531  55.356  88.963  1.00 317.07 ? 99   VAL B C   1 
ATOM   12964 O  O   . VAL C 1 99   ? 56.617  55.888  87.859  1.00 319.54 ? 99   VAL B O   1 
ATOM   12965 C  CB  . VAL C 1 99   ? 58.626  54.000  89.215  1.00 344.11 ? 99   VAL B CB  1 
ATOM   12966 C  CG1 . VAL C 1 99   ? 58.938  54.268  87.755  1.00 349.62 ? 99   VAL B CG1 1 
ATOM   12967 C  CG2 . VAL C 1 99   ? 59.903  53.791  90.025  1.00 347.29 ? 99   VAL B CG2 1 
ATOM   12968 N  N   . SER C 1 100  ? 55.365  54.946  89.456  1.00 201.46 ? 100  SER B N   1 
ATOM   12969 C  CA  . SER C 1 100  ? 54.128  55.111  88.687  1.00 180.95 ? 100  SER B CA  1 
ATOM   12970 C  C   . SER C 1 100  ? 53.712  56.588  88.564  1.00 166.03 ? 100  SER B C   1 
ATOM   12971 O  O   . SER C 1 100  ? 53.012  57.070  89.440  1.00 165.74 ? 100  SER B O   1 
ATOM   12972 C  CB  . SER C 1 100  ? 52.988  54.320  89.342  1.00 171.83 ? 100  SER B CB  1 
ATOM   12973 O  OG  . SER C 1 100  ? 53.487  53.231  90.093  1.00 169.49 ? 100  SER B OG  1 
ATOM   12974 N  N   . TYR C 1 101  ? 54.122  57.289  87.493  1.00 220.09 ? 101  TYR B N   1 
ATOM   12975 C  CA  . TYR C 1 101  ? 53.816  58.734  87.239  1.00 206.61 ? 101  TYR B CA  1 
ATOM   12976 C  C   . TYR C 1 101  ? 54.984  59.705  87.434  1.00 202.18 ? 101  TYR B C   1 
ATOM   12977 O  O   . TYR C 1 101  ? 55.596  59.748  88.503  1.00 201.66 ? 101  TYR B O   1 
ATOM   12978 C  CB  . TYR C 1 101  ? 52.660  59.271  88.086  1.00 197.63 ? 101  TYR B CB  1 
ATOM   12979 C  CG  . TYR C 1 101  ? 51.285  58.810  87.695  1.00 191.84 ? 101  TYR B CG  1 
ATOM   12980 C  CD1 . TYR C 1 101  ? 50.364  59.694  87.168  1.00 192.05 ? 101  TYR B CD1 1 
ATOM   12981 C  CD2 . TYR C 1 101  ? 50.896  57.489  87.883  1.00 188.19 ? 101  TYR B CD2 1 
ATOM   12982 C  CE1 . TYR C 1 101  ? 49.100  59.274  86.830  1.00 189.38 ? 101  TYR B CE1 1 
ATOM   12983 C  CE2 . TYR C 1 101  ? 49.636  57.058  87.550  1.00 185.70 ? 101  TYR B CE2 1 
ATOM   12984 C  CZ  . TYR C 1 101  ? 48.739  57.955  87.023  1.00 186.75 ? 101  TYR B CZ  1 
ATOM   12985 O  OH  . TYR C 1 101  ? 47.477  57.524  86.689  1.00 184.22 ? 101  TYR B OH  1 
ATOM   12986 N  N   . VAL C 1 102  ? 55.259  60.530  86.428  1.00 218.01 ? 102  VAL B N   1 
ATOM   12987 C  CA  . VAL C 1 102  ? 56.313  61.523  86.592  1.00 217.54 ? 102  VAL B CA  1 
ATOM   12988 C  C   . VAL C 1 102  ? 55.985  62.909  86.085  1.00 219.90 ? 102  VAL B C   1 
ATOM   12989 O  O   . VAL C 1 102  ? 54.973  63.145  85.416  1.00 217.48 ? 102  VAL B O   1 
ATOM   12990 C  CB  . VAL C 1 102  ? 57.649  61.100  85.954  1.00 218.19 ? 102  VAL B CB  1 
ATOM   12991 C  CG1 . VAL C 1 102  ? 58.037  59.704  86.401  1.00 215.03 ? 102  VAL B CG1 1 
ATOM   12992 C  CG2 . VAL C 1 102  ? 57.561  61.179  84.445  1.00 219.99 ? 102  VAL B CG2 1 
ATOM   12993 N  N   . TYR C 1 103  ? 56.885  63.817  86.442  1.00 241.33 ? 103  TYR B N   1 
ATOM   12994 C  CA  . TYR C 1 103  ? 56.806  65.208  86.067  1.00 243.61 ? 103  TYR B CA  1 
ATOM   12995 C  C   . TYR C 1 103  ? 58.000  65.553  85.210  1.00 246.81 ? 103  TYR B C   1 
ATOM   12996 O  O   . TYR C 1 103  ? 59.161  65.498  85.626  1.00 243.97 ? 103  TYR B O   1 
ATOM   12997 C  CB  . TYR C 1 103  ? 56.743  66.110  87.306  1.00 253.43 ? 103  TYR B CB  1 
ATOM   12998 C  CG  . TYR C 1 103  ? 55.345  66.271  87.869  1.00 256.01 ? 103  TYR B CG  1 
ATOM   12999 C  CD1 . TYR C 1 103  ? 54.625  65.171  88.316  1.00 258.12 ? 103  TYR B CD1 1 
ATOM   13000 C  CD2 . TYR C 1 103  ? 54.748  67.524  87.961  1.00 259.89 ? 103  TYR B CD2 1 
ATOM   13001 C  CE1 . TYR C 1 103  ? 53.346  65.313  88.832  1.00 257.15 ? 103  TYR B CE1 1 
ATOM   13002 C  CE2 . TYR C 1 103  ? 53.467  67.675  88.480  1.00 258.87 ? 103  TYR B CE2 1 
ATOM   13003 C  CZ  . TYR C 1 103  ? 52.772  66.566  88.912  1.00 257.94 ? 103  TYR B CZ  1 
ATOM   13004 O  OH  . TYR C 1 103  ? 51.502  66.709  89.423  1.00 255.57 ? 103  TYR B OH  1 
ATOM   13005 N  N   . LEU C 1 104  ? 57.678  65.872  83.978  1.00 161.45 ? 104  LEU B N   1 
ATOM   13006 C  CA  . LEU C 1 104  ? 58.637  66.320  83.011  1.00 167.11 ? 104  LEU B CA  1 
ATOM   13007 C  C   . LEU C 1 104  ? 58.648  67.815  83.189  1.00 168.18 ? 104  LEU B C   1 
ATOM   13008 O  O   . LEU C 1 104  ? 57.593  68.402  83.391  1.00 162.06 ? 104  LEU B O   1 
ATOM   13009 C  CB  . LEU C 1 104  ? 58.066  65.981  81.639  1.00 167.11 ? 104  LEU B CB  1 
ATOM   13010 C  CG  . LEU C 1 104  ? 58.900  65.735  80.383  1.00 169.35 ? 104  LEU B CG  1 
ATOM   13011 C  CD1 . LEU C 1 104  ? 60.051  64.755  80.637  1.00 171.36 ? 104  LEU B CD1 1 
ATOM   13012 C  CD2 . LEU C 1 104  ? 57.958  65.215  79.319  1.00 167.39 ? 104  LEU B CD2 1 
ATOM   13013 N  N   . GLU C 1 105  ? 59.812  68.446  83.098  1.00 213.70 ? 105  GLU B N   1 
ATOM   13014 C  CA  . GLU C 1 105  ? 59.874  69.883  83.333  1.00 218.36 ? 105  GLU B CA  1 
ATOM   13015 C  C   . GLU C 1 105  ? 60.740  70.605  82.319  1.00 223.67 ? 105  GLU B C   1 
ATOM   13016 O  O   . GLU C 1 105  ? 61.754  70.087  81.868  1.00 226.87 ? 105  GLU B O   1 
ATOM   13017 C  CB  . GLU C 1 105  ? 60.376  70.174  84.759  1.00 220.40 ? 105  GLU B CB  1 
ATOM   13018 C  CG  . GLU C 1 105  ? 60.069  71.592  85.308  1.00 222.06 ? 105  GLU B CG  1 
ATOM   13019 C  CD  . GLU C 1 105  ? 60.129  71.679  86.847  1.00 222.31 ? 105  GLU B CD  1 
ATOM   13020 O  OE1 . GLU C 1 105  ? 61.230  71.553  87.424  1.00 225.48 ? 105  GLU B OE1 1 
ATOM   13021 O  OE2 . GLU C 1 105  ? 59.071  71.887  87.484  1.00 219.23 ? 105  GLU B OE2 1 
ATOM   13022 N  N   . VAL C 1 106  ? 60.331  71.814  81.969  1.00 253.33 ? 106  VAL B N   1 
ATOM   13023 C  CA  . VAL C 1 106  ? 61.135  72.640  81.097  1.00 258.16 ? 106  VAL B CA  1 
ATOM   13024 C  C   . VAL C 1 106  ? 61.242  74.031  81.683  1.00 259.18 ? 106  VAL B C   1 
ATOM   13025 O  O   . VAL C 1 106  ? 60.474  74.394  82.568  1.00 256.03 ? 106  VAL B O   1 
ATOM   13026 C  CB  . VAL C 1 106  ? 60.526  72.713  79.710  1.00 258.63 ? 106  VAL B CB  1 
ATOM   13027 C  CG1 . VAL C 1 106  ? 61.442  73.492  78.776  1.00 264.16 ? 106  VAL B CG1 1 
ATOM   13028 C  CG2 . VAL C 1 106  ? 60.299  71.311  79.192  1.00 258.61 ? 106  VAL B CG2 1 
ATOM   13029 N  N   . VAL C 1 107  ? 62.203  74.806  81.198  1.00 204.96 ? 107  VAL B N   1 
ATOM   13030 C  CA  . VAL C 1 107  ? 62.439  76.132  81.741  1.00 205.81 ? 107  VAL B CA  1 
ATOM   13031 C  C   . VAL C 1 107  ? 62.788  77.101  80.620  1.00 208.10 ? 107  VAL B C   1 
ATOM   13032 O  O   . VAL C 1 107  ? 63.176  76.685  79.524  1.00 210.56 ? 107  VAL B O   1 
ATOM   13033 C  CB  . VAL C 1 107  ? 63.577  76.107  82.791  1.00 213.69 ? 107  VAL B CB  1 
ATOM   13034 C  CG1 . VAL C 1 107  ? 63.677  77.442  83.506  1.00 214.08 ? 107  VAL B CG1 1 
ATOM   13035 C  CG2 . VAL C 1 107  ? 63.352  74.988  83.790  1.00 210.30 ? 107  VAL B CG2 1 
ATOM   13036 N  N   . SER C 1 108  ? 62.631  78.391  80.900  1.00 197.16 ? 108  SER B N   1 
ATOM   13037 C  CA  . SER C 1 108  ? 63.037  79.434  79.970  1.00 203.16 ? 108  SER B CA  1 
ATOM   13038 C  C   . SER C 1 108  ? 62.766  80.808  80.565  1.00 209.16 ? 108  SER B C   1 
ATOM   13039 O  O   . SER C 1 108  ? 62.207  80.919  81.651  1.00 207.63 ? 108  SER B O   1 
ATOM   13040 C  CB  . SER C 1 108  ? 62.347  79.268  78.607  1.00 203.02 ? 108  SER B CB  1 
ATOM   13041 O  OG  . SER C 1 108  ? 61.010  78.806  78.736  1.00 198.75 ? 108  SER B OG  1 
ATOM   13042 N  N   . LYS C 1 109  ? 63.178  81.848  79.848  1.00 292.43 ? 109  LYS B N   1 
ATOM   13043 C  CA  . LYS C 1 109  ? 62.997  83.221  80.300  1.00 297.44 ? 109  LYS B CA  1 
ATOM   13044 C  C   . LYS C 1 109  ? 61.537  83.637  80.269  1.00 298.04 ? 109  LYS B C   1 
ATOM   13045 O  O   . LYS C 1 109  ? 61.092  84.422  81.094  1.00 296.79 ? 109  LYS B O   1 
ATOM   13046 C  CB  . LYS C 1 109  ? 63.833  84.191  79.450  1.00 302.30 ? 109  LYS B CB  1 
ATOM   13047 C  CG  . LYS C 1 109  ? 63.694  84.032  77.919  1.00 306.46 ? 109  LYS B CG  1 
ATOM   13048 C  CD  . LYS C 1 109  ? 62.413  84.660  77.356  1.00 301.67 ? 109  LYS B CD  1 
ATOM   13049 C  CE  . LYS C 1 109  ? 62.297  84.522  75.829  1.00 302.34 ? 109  LYS B CE  1 
ATOM   13050 N  NZ  . LYS C 1 109  ? 62.951  85.633  75.069  1.00 305.55 ? 109  LYS B NZ  1 
ATOM   13051 N  N   . HIS C 1 110  ? 60.792  83.096  79.315  1.00 308.82 ? 110  HIS B N   1 
ATOM   13052 C  CA  . HIS C 1 110  ? 59.460  83.599  79.008  1.00 308.77 ? 110  HIS B CA  1 
ATOM   13053 C  C   . HIS C 1 110  ? 58.351  82.927  79.819  1.00 300.29 ? 110  HIS B C   1 
ATOM   13054 O  O   . HIS C 1 110  ? 57.224  83.425  79.873  1.00 297.91 ? 110  HIS B O   1 
ATOM   13055 C  CB  . HIS C 1 110  ? 59.208  83.466  77.501  1.00 316.67 ? 110  HIS B CB  1 
ATOM   13056 C  CG  . HIS C 1 110  ? 57.860  83.942  77.060  1.00 321.67 ? 110  HIS B CG  1 
ATOM   13057 N  ND1 . HIS C 1 110  ? 57.217  83.424  75.955  1.00 324.46 ? 110  HIS B ND1 1 
ATOM   13058 C  CD2 . HIS C 1 110  ? 57.033  84.885  77.570  1.00 322.62 ? 110  HIS B CD2 1 
ATOM   13059 C  CE1 . HIS C 1 110  ? 56.052  84.027  75.805  1.00 323.63 ? 110  HIS B CE1 1 
ATOM   13060 N  NE2 . HIS C 1 110  ? 55.914  84.917  76.774  1.00 322.44 ? 110  HIS B NE2 1 
ATOM   13061 N  N   . PHE C 1 111  ? 58.680  81.810  80.463  1.00 265.49 ? 111  PHE B N   1 
ATOM   13062 C  CA  . PHE C 1 111  ? 57.677  80.970  81.120  1.00 255.96 ? 111  PHE B CA  1 
ATOM   13063 C  C   . PHE C 1 111  ? 58.329  79.692  81.653  1.00 246.95 ? 111  PHE B C   1 
ATOM   13064 O  O   . PHE C 1 111  ? 59.556  79.559  81.657  1.00 246.39 ? 111  PHE B O   1 
ATOM   13065 C  CB  . PHE C 1 111  ? 56.565  80.602  80.122  1.00 256.50 ? 111  PHE B CB  1 
ATOM   13066 C  CG  . PHE C 1 111  ? 55.224  80.301  80.761  1.00 253.64 ? 111  PHE B CG  1 
ATOM   13067 C  CD1 . PHE C 1 111  ? 54.340  81.329  81.059  1.00 253.02 ? 111  PHE B CD1 1 
ATOM   13068 C  CD2 . PHE C 1 111  ? 54.839  78.989  81.033  1.00 251.55 ? 111  PHE B CD2 1 
ATOM   13069 C  CE1 . PHE C 1 111  ? 53.108  81.059  81.634  1.00 249.32 ? 111  PHE B CE1 1 
ATOM   13070 C  CE2 . PHE C 1 111  ? 53.608  78.710  81.609  1.00 247.38 ? 111  PHE B CE2 1 
ATOM   13071 C  CZ  . PHE C 1 111  ? 52.740  79.745  81.907  1.00 246.30 ? 111  PHE B CZ  1 
ATOM   13072 N  N   . SER C 1 112  ? 57.492  78.758  82.101  1.00 210.28 ? 112  SER B N   1 
ATOM   13073 C  CA  . SER C 1 112  ? 57.939  77.425  82.497  1.00 205.17 ? 112  SER B CA  1 
ATOM   13074 C  C   . SER C 1 112  ? 56.740  76.467  82.656  1.00 200.39 ? 112  SER B C   1 
ATOM   13075 O  O   . SER C 1 112  ? 55.677  76.856  83.164  1.00 197.49 ? 112  SER B O   1 
ATOM   13076 C  CB  . SER C 1 112  ? 58.783  77.489  83.775  1.00 201.73 ? 112  SER B CB  1 
ATOM   13077 O  OG  . SER C 1 112  ? 59.833  76.533  83.754  1.00 201.32 ? 112  SER B OG  1 
ATOM   13078 N  N   . LYS C 1 113  ? 56.909  75.219  82.212  1.00 199.97 ? 113  LYS B N   1 
ATOM   13079 C  CA  . LYS C 1 113  ? 55.802  74.267  82.236  1.00 192.61 ? 113  LYS B CA  1 
ATOM   13080 C  C   . LYS C 1 113  ? 56.179  72.797  82.060  1.00 188.45 ? 113  LYS B C   1 
ATOM   13081 O  O   . LYS C 1 113  ? 57.211  72.442  81.480  1.00 190.38 ? 113  LYS B O   1 
ATOM   13082 C  CB  . LYS C 1 113  ? 54.723  74.674  81.233  1.00 192.90 ? 113  LYS B CB  1 
ATOM   13083 C  CG  . LYS C 1 113  ? 53.495  73.784  81.225  1.00 191.81 ? 113  LYS B CG  1 
ATOM   13084 C  CD  . LYS C 1 113  ? 52.505  74.131  82.322  1.00 190.86 ? 113  LYS B CD  1 
ATOM   13085 C  CE  . LYS C 1 113  ? 51.188  73.384  82.108  1.00 188.16 ? 113  LYS B CE  1 
ATOM   13086 N  NZ  . LYS C 1 113  ? 50.271  74.113  81.169  1.00 186.30 ? 113  LYS B NZ  1 
ATOM   13087 N  N   . SER C 1 114  ? 55.269  71.961  82.546  1.00 214.00 ? 114  SER B N   1 
ATOM   13088 C  CA  . SER C 1 114  ? 55.543  70.579  82.890  1.00 217.94 ? 114  SER B CA  1 
ATOM   13089 C  C   . SER C 1 114  ? 54.242  69.777  83.001  1.00 215.27 ? 114  SER B C   1 
ATOM   13090 O  O   . SER C 1 114  ? 53.153  70.312  82.759  1.00 211.72 ? 114  SER B O   1 
ATOM   13091 C  CB  . SER C 1 114  ? 56.281  70.553  84.223  1.00 220.54 ? 114  SER B CB  1 
ATOM   13092 O  OG  . SER C 1 114  ? 55.977  71.712  84.993  1.00 220.69 ? 114  SER B OG  1 
ATOM   13093 N  N   . LYS C 1 115  ? 54.340  68.507  83.396  1.00 216.33 ? 115  LYS B N   1 
ATOM   13094 C  CA  . LYS C 1 115  ? 53.203  67.609  83.229  1.00 213.06 ? 115  LYS B CA  1 
ATOM   13095 C  C   . LYS C 1 115  ? 53.310  66.248  83.948  1.00 211.37 ? 115  LYS B C   1 
ATOM   13096 O  O   . LYS C 1 115  ? 54.394  65.848  84.361  1.00 211.74 ? 115  LYS B O   1 
ATOM   13097 C  CB  . LYS C 1 115  ? 53.000  67.410  81.729  1.00 214.89 ? 115  LYS B CB  1 
ATOM   13098 C  CG  . LYS C 1 115  ? 52.208  66.209  81.372  1.00 210.24 ? 115  LYS B CG  1 
ATOM   13099 C  CD  . LYS C 1 115  ? 51.159  66.525  80.345  1.00 205.96 ? 115  LYS B CD  1 
ATOM   13100 C  CE  . LYS C 1 115  ? 50.589  65.229  79.803  1.00 202.51 ? 115  LYS B CE  1 
ATOM   13101 N  NZ  . LYS C 1 115  ? 49.391  65.433  78.956  1.00 199.42 ? 115  LYS B NZ  1 
ATOM   13102 N  N   . ARG C 1 116  ? 52.175  65.560  84.111  1.00 232.35 ? 116  ARG B N   1 
ATOM   13103 C  CA  . ARG C 1 116  ? 52.142  64.188  84.643  1.00 234.74 ? 116  ARG B CA  1 
ATOM   13104 C  C   . ARG C 1 116  ? 51.680  63.180  83.594  1.00 235.64 ? 116  ARG B C   1 
ATOM   13105 O  O   . ARG C 1 116  ? 50.658  63.397  82.942  1.00 235.90 ? 116  ARG B O   1 
ATOM   13106 C  CB  . ARG C 1 116  ? 51.199  64.093  85.835  1.00 233.88 ? 116  ARG B CB  1 
ATOM   13107 C  CG  . ARG C 1 116  ? 50.649  62.687  86.081  1.00 235.49 ? 116  ARG B CG  1 
ATOM   13108 C  CD  . ARG C 1 116  ? 49.395  62.390  85.247  1.00 238.03 ? 116  ARG B CD  1 
ATOM   13109 N  NE  . ARG C 1 116  ? 48.331  61.798  86.056  1.00 237.98 ? 116  ARG B NE  1 
ATOM   13110 C  CZ  . ARG C 1 116  ? 47.181  61.327  85.579  1.00 238.18 ? 116  ARG B CZ  1 
ATOM   13111 N  NH1 . ARG C 1 116  ? 46.929  61.368  84.280  1.00 240.16 ? 116  ARG B NH1 1 
ATOM   13112 N  NH2 . ARG C 1 116  ? 46.282  60.810  86.408  1.00 235.12 ? 116  ARG B NH2 1 
ATOM   13113 N  N   . MET C 1 117  ? 52.395  62.059  83.476  1.00 227.46 ? 117  MET B N   1 
ATOM   13114 C  CA  . MET C 1 117  ? 52.208  61.101  82.373  1.00 226.69 ? 117  MET B CA  1 
ATOM   13115 C  C   . MET C 1 117  ? 52.841  59.745  82.709  1.00 224.02 ? 117  MET B C   1 
ATOM   13116 O  O   . MET C 1 117  ? 54.033  59.679  83.016  1.00 224.43 ? 117  MET B O   1 
ATOM   13117 C  CB  . MET C 1 117  ? 52.854  61.657  81.103  1.00 231.88 ? 117  MET B CB  1 
ATOM   13118 C  CG  . MET C 1 117  ? 54.287  62.115  81.340  1.00 236.23 ? 117  MET B CG  1 
ATOM   13119 S  SD  . MET C 1 117  ? 55.029  63.167  80.075  1.00 242.40 ? 117  MET B SD  1 
ATOM   13120 C  CE  . MET C 1 117  ? 53.640  64.168  79.582  1.00 201.51 ? 117  MET B CE  1 
ATOM   13121 N  N   . PRO C 1 118  ? 52.056  58.653  82.622  1.00 198.15 ? 118  PRO B N   1 
ATOM   13122 C  CA  . PRO C 1 118  ? 52.479  57.329  83.123  1.00 195.90 ? 118  PRO B CA  1 
ATOM   13123 C  C   . PRO C 1 118  ? 53.875  56.914  82.648  1.00 198.84 ? 118  PRO B C   1 
ATOM   13124 O  O   . PRO C 1 118  ? 54.320  57.429  81.632  1.00 200.42 ? 118  PRO B O   1 
ATOM   13125 C  CB  . PRO C 1 118  ? 51.416  56.384  82.555  1.00 193.07 ? 118  PRO B CB  1 
ATOM   13126 C  CG  . PRO C 1 118  ? 50.204  57.247  82.359  1.00 191.41 ? 118  PRO B CG  1 
ATOM   13127 C  CD  . PRO C 1 118  ? 50.704  58.626  82.033  1.00 195.51 ? 118  PRO B CD  1 
ATOM   13128 N  N   . ILE C 1 119  ? 54.562  56.028  83.368  1.00 198.07 ? 119  ILE B N   1 
ATOM   13129 C  CA  . ILE C 1 119  ? 55.857  55.524  82.898  1.00 200.64 ? 119  ILE B CA  1 
ATOM   13130 C  C   . ILE C 1 119  ? 56.026  54.064  83.258  1.00 199.01 ? 119  ILE B C   1 
ATOM   13131 O  O   . ILE C 1 119  ? 55.320  53.574  84.139  1.00 192.93 ? 119  ILE B O   1 
ATOM   13132 C  CB  . ILE C 1 119  ? 57.053  56.318  83.467  1.00 201.18 ? 119  ILE B CB  1 
ATOM   13133 C  CG1 . ILE C 1 119  ? 57.864  55.451  84.437  1.00 198.05 ? 119  ILE B CG1 1 
ATOM   13134 C  CG2 . ILE C 1 119  ? 56.586  57.625  84.093  1.00 199.64 ? 119  ILE B CG2 1 
ATOM   13135 C  CD1 . ILE C 1 119  ? 59.316  55.884  84.598  1.00 201.58 ? 119  ILE B CD1 1 
ATOM   13136 N  N   . THR C 1 120  ? 56.948  53.370  82.582  1.00 159.70 ? 120  THR B N   1 
ATOM   13137 C  CA  . THR C 1 120  ? 57.184  51.961  82.894  1.00 160.60 ? 120  THR B CA  1 
ATOM   13138 C  C   . THR C 1 120  ? 58.647  51.541  82.887  1.00 162.26 ? 120  THR B C   1 
ATOM   13139 O  O   . THR C 1 120  ? 59.566  52.343  82.635  1.00 165.69 ? 120  THR B O   1 
ATOM   13140 C  CB  . THR C 1 120  ? 56.329  50.967  82.014  1.00 160.95 ? 120  THR B CB  1 
ATOM   13141 O  OG1 . THR C 1 120  ? 54.948  51.329  82.090  1.00 159.70 ? 120  THR B OG1 1 
ATOM   13142 C  CG2 . THR C 1 120  ? 56.475  49.494  82.483  1.00 161.81 ? 120  THR B CG2 1 
ATOM   13143 N  N   . TYR C 1 121  ? 58.795  50.251  83.184  1.00 207.75 ? 121  TYR B N   1 
ATOM   13144 C  CA  . TYR C 1 121  ? 60.030  49.569  83.476  1.00 208.97 ? 121  TYR B CA  1 
ATOM   13145 C  C   . TYR C 1 121  ? 60.344  48.629  82.338  1.00 201.06 ? 121  TYR B C   1 
ATOM   13146 O  O   . TYR C 1 121  ? 60.904  47.569  82.567  1.00 202.13 ? 121  TYR B O   1 
ATOM   13147 C  CB  . TYR C 1 121  ? 59.835  48.696  84.716  1.00 212.26 ? 121  TYR B CB  1 
ATOM   13148 C  CG  . TYR C 1 121  ? 59.381  49.404  85.994  1.00 216.82 ? 121  TYR B CG  1 
ATOM   13149 C  CD1 . TYR C 1 121  ? 60.306  49.970  86.869  1.00 222.98 ? 121  TYR B CD1 1 
ATOM   13150 C  CD2 . TYR C 1 121  ? 58.033  49.466  86.348  1.00 214.50 ? 121  TYR B CD2 1 
ATOM   13151 C  CE1 . TYR C 1 121  ? 59.905  50.597  88.034  1.00 225.78 ? 121  TYR B CE1 1 
ATOM   13152 C  CE2 . TYR C 1 121  ? 57.629  50.093  87.520  1.00 216.67 ? 121  TYR B CE2 1 
ATOM   13153 C  CZ  . TYR C 1 121  ? 58.571  50.654  88.349  1.00 223.75 ? 121  TYR B CZ  1 
ATOM   13154 O  OH  . TYR C 1 121  ? 58.181  51.275  89.503  1.00 228.78 ? 121  TYR B OH  1 
ATOM   13155 N  N   . ASP C 1 122  ? 59.979  49.010  81.117  1.00 222.61 ? 122  ASP B N   1 
ATOM   13156 C  CA  . ASP C 1 122  ? 60.117  48.128  79.953  1.00 215.44 ? 122  ASP B CA  1 
ATOM   13157 C  C   . ASP C 1 122  ? 61.249  48.480  78.980  1.00 214.10 ? 122  ASP B C   1 
ATOM   13158 O  O   . ASP C 1 122  ? 60.995  48.774  77.815  1.00 216.85 ? 122  ASP B O   1 
ATOM   13159 C  CB  . ASP C 1 122  ? 58.802  48.091  79.181  1.00 213.32 ? 122  ASP B CB  1 
ATOM   13160 C  CG  . ASP C 1 122  ? 58.402  46.694  78.800  1.00 211.21 ? 122  ASP B CG  1 
ATOM   13161 O  OD1 . ASP C 1 122  ? 57.210  46.491  78.485  1.00 208.61 ? 122  ASP B OD1 1 
ATOM   13162 O  OD2 . ASP C 1 122  ? 59.276  45.799  78.829  1.00 211.88 ? 122  ASP B OD2 1 
ATOM   13163 N  N   . ASN C 1 123  ? 62.491  48.413  79.444  1.00 208.14 ? 123  ASN B N   1 
ATOM   13164 C  CA  . ASN C 1 123  ? 63.639  48.800  78.630  1.00 209.62 ? 123  ASN B CA  1 
ATOM   13165 C  C   . ASN C 1 123  ? 64.222  47.639  77.829  1.00 209.79 ? 123  ASN B C   1 
ATOM   13166 O  O   . ASN C 1 123  ? 64.746  46.690  78.408  1.00 210.26 ? 123  ASN B O   1 
ATOM   13167 C  CB  . ASN C 1 123  ? 64.719  49.407  79.530  1.00 214.12 ? 123  ASN B CB  1 
ATOM   13168 C  CG  . ASN C 1 123  ? 65.854  50.048  78.747  1.00 217.35 ? 123  ASN B CG  1 
ATOM   13169 O  OD1 . ASN C 1 123  ? 66.497  50.982  79.229  1.00 221.85 ? 123  ASN B OD1 1 
ATOM   13170 N  ND2 . ASN C 1 123  ? 66.111  49.548  77.542  1.00 216.99 ? 123  ASN B ND2 1 
ATOM   13171 N  N   . GLY C 1 124  ? 64.148  47.732  76.502  1.00 171.09 ? 124  GLY B N   1 
ATOM   13172 C  CA  . GLY C 1 124  ? 64.767  46.750  75.623  1.00 173.42 ? 124  GLY B CA  1 
ATOM   13173 C  C   . GLY C 1 124  ? 63.986  45.475  75.359  1.00 165.56 ? 124  GLY B C   1 
ATOM   13174 O  O   . GLY C 1 124  ? 62.766  45.441  75.458  1.00 162.02 ? 124  GLY B O   1 
ATOM   13175 N  N   . PHE C 1 125  ? 64.680  44.406  75.004  1.00 184.79 ? 125  PHE B N   1 
ATOM   13176 C  CA  . PHE C 1 125  ? 63.962  43.193  74.701  1.00 179.84 ? 125  PHE B CA  1 
ATOM   13177 C  C   . PHE C 1 125  ? 64.839  42.022  74.859  1.00 180.08 ? 125  PHE B C   1 
ATOM   13178 O  O   . PHE C 1 125  ? 66.068  42.124  74.795  1.00 183.61 ? 125  PHE B O   1 
ATOM   13179 C  CB  . PHE C 1 125  ? 63.518  43.222  73.279  1.00 179.21 ? 125  PHE B CB  1 
ATOM   13180 C  CG  . PHE C 1 125  ? 63.173  44.571  72.824  1.00 180.40 ? 125  PHE B CG  1 
ATOM   13181 C  CD1 . PHE C 1 125  ? 64.159  45.438  72.376  1.00 185.52 ? 125  PHE B CD1 1 
ATOM   13182 C  CD2 . PHE C 1 125  ? 61.867  45.006  72.884  1.00 176.98 ? 125  PHE B CD2 1 
ATOM   13183 C  CE1 . PHE C 1 125  ? 63.839  46.719  71.960  1.00 187.18 ? 125  PHE B CE1 1 
ATOM   13184 C  CE2 . PHE C 1 125  ? 61.531  46.283  72.470  1.00 179.79 ? 125  PHE B CE2 1 
ATOM   13185 C  CZ  . PHE C 1 125  ? 62.519  47.144  72.007  1.00 184.59 ? 125  PHE B CZ  1 
ATOM   13186 N  N   . LEU C 1 126  ? 64.188  40.889  75.050  1.00 145.48 ? 126  LEU B N   1 
ATOM   13187 C  CA  . LEU C 1 126  ? 64.915  39.659  75.235  1.00 144.35 ? 126  LEU B CA  1 
ATOM   13188 C  C   . LEU C 1 126  ? 64.590  38.665  74.115  1.00 144.36 ? 126  LEU B C   1 
ATOM   13189 O  O   . LEU C 1 126  ? 63.429  38.330  73.868  1.00 143.76 ? 126  LEU B O   1 
ATOM   13190 C  CB  . LEU C 1 126  ? 64.655  39.073  76.635  1.00 142.21 ? 126  LEU B CB  1 
ATOM   13191 C  CG  . LEU C 1 126  ? 65.449  39.552  77.872  1.00 141.93 ? 126  LEU B CG  1 
ATOM   13192 C  CD1 . LEU C 1 126  ? 66.828  40.142  77.554  1.00 143.61 ? 126  LEU B CD1 1 
ATOM   13193 C  CD2 . LEU C 1 126  ? 64.631  40.520  78.688  1.00 141.72 ? 126  LEU B CD2 1 
ATOM   13194 N  N   . PHE C 1 127  ? 65.639  38.218  73.436  1.00 161.79 ? 127  PHE B N   1 
ATOM   13195 C  CA  . PHE C 1 127  ? 65.517  37.254  72.366  1.00 161.71 ? 127  PHE B CA  1 
ATOM   13196 C  C   . PHE C 1 127  ? 66.150  35.970  72.824  1.00 163.74 ? 127  PHE B C   1 
ATOM   13197 O  O   . PHE C 1 127  ? 67.288  35.962  73.279  1.00 163.86 ? 127  PHE B O   1 
ATOM   13198 C  CB  . PHE C 1 127  ? 66.232  37.757  71.118  1.00 167.70 ? 127  PHE B CB  1 
ATOM   13199 C  CG  . PHE C 1 127  ? 65.534  38.911  70.437  1.00 164.91 ? 127  PHE B CG  1 
ATOM   13200 C  CD1 . PHE C 1 127  ? 64.151  38.974  70.377  1.00 165.59 ? 127  PHE B CD1 1 
ATOM   13201 C  CD2 . PHE C 1 127  ? 66.263  39.925  69.838  1.00 171.84 ? 127  PHE B CD2 1 
ATOM   13202 C  CE1 . PHE C 1 127  ? 63.512  40.036  69.744  1.00 166.99 ? 127  PHE B CE1 1 
ATOM   13203 C  CE2 . PHE C 1 127  ? 65.627  40.989  69.205  1.00 172.87 ? 127  PHE B CE2 1 
ATOM   13204 C  CZ  . PHE C 1 127  ? 64.252  41.045  69.161  1.00 170.42 ? 127  PHE B CZ  1 
ATOM   13205 N  N   . ILE C 1 128  ? 65.410  34.880  72.709  1.00 144.87 ? 128  ILE B N   1 
ATOM   13206 C  CA  . ILE C 1 128  ? 65.886  33.609  73.223  1.00 145.06 ? 128  ILE B CA  1 
ATOM   13207 C  C   . ILE C 1 128  ? 66.051  32.546  72.162  1.00 145.89 ? 128  ILE B C   1 
ATOM   13208 O  O   . ILE C 1 128  ? 65.204  31.672  71.987  1.00 140.69 ? 128  ILE B O   1 
ATOM   13209 C  CB  . ILE C 1 128  ? 64.933  33.059  74.227  1.00 139.99 ? 128  ILE B CB  1 
ATOM   13210 C  CG1 . ILE C 1 128  ? 63.975  34.155  74.679  1.00 139.83 ? 128  ILE B CG1 1 
ATOM   13211 C  CG2 . ILE C 1 128  ? 65.711  32.466  75.377  1.00 141.52 ? 128  ILE B CG2 1 
ATOM   13212 C  CD1 . ILE C 1 128  ? 63.259  33.818  75.955  1.00 137.52 ? 128  ILE B CD1 1 
ATOM   13213 N  N   . HIS C 1 129  ? 67.177  32.620  71.480  1.00 181.57 ? 129  HIS B N   1 
ATOM   13214 C  CA  . HIS C 1 129  ? 67.466  31.751  70.363  1.00 184.25 ? 129  HIS B CA  1 
ATOM   13215 C  C   . HIS C 1 129  ? 67.773  30.323  70.814  1.00 185.91 ? 129  HIS B C   1 
ATOM   13216 O  O   . HIS C 1 129  ? 68.931  29.951  70.999  1.00 191.41 ? 129  HIS B O   1 
ATOM   13217 C  CB  . HIS C 1 129  ? 68.595  32.381  69.529  1.00 186.66 ? 129  HIS B CB  1 
ATOM   13218 C  CG  . HIS C 1 129  ? 69.340  31.423  68.655  1.00 185.43 ? 129  HIS B CG  1 
ATOM   13219 N  ND1 . HIS C 1 129  ? 70.652  31.638  68.279  1.00 188.89 ? 129  HIS B ND1 1 
ATOM   13220 C  CD2 . HIS C 1 129  ? 68.977  30.257  68.070  1.00 182.58 ? 129  HIS B CD2 1 
ATOM   13221 C  CE1 . HIS C 1 129  ? 71.061  30.652  67.511  1.00 190.50 ? 129  HIS B CE1 1 
ATOM   13222 N  NE2 . HIS C 1 129  ? 70.062  29.795  67.367  1.00 187.17 ? 129  HIS B NE2 1 
ATOM   13223 N  N   . THR C 1 130  ? 66.717  29.537  71.019  1.00 145.90 ? 130  THR B N   1 
ATOM   13224 C  CA  . THR C 1 130  ? 66.868  28.094  71.205  1.00 145.55 ? 130  THR B CA  1 
ATOM   13225 C  C   . THR C 1 130  ? 67.449  27.522  69.915  1.00 148.21 ? 130  THR B C   1 
ATOM   13226 O  O   . THR C 1 130  ? 66.981  27.868  68.847  1.00 150.01 ? 130  THR B O   1 
ATOM   13227 C  CB  . THR C 1 130  ? 65.513  27.420  71.543  1.00 139.89 ? 130  THR B CB  1 
ATOM   13228 O  OG1 . THR C 1 130  ? 65.588  26.018  71.280  1.00 138.38 ? 130  THR B OG1 1 
ATOM   13229 C  CG2 . THR C 1 130  ? 64.376  28.018  70.729  1.00 139.05 ? 130  THR B CG2 1 
ATOM   13230 N  N   . ASP C 1 131  ? 68.459  26.659  70.002  1.00 203.59 ? 131  ASP B N   1 
ATOM   13231 C  CA  . ASP C 1 131  ? 69.128  26.167  68.795  1.00 206.00 ? 131  ASP B CA  1 
ATOM   13232 C  C   . ASP C 1 131  ? 68.129  25.593  67.794  1.00 206.47 ? 131  ASP B C   1 
ATOM   13233 O  O   . ASP C 1 131  ? 68.032  26.070  66.665  1.00 209.51 ? 131  ASP B O   1 
ATOM   13234 C  CB  . ASP C 1 131  ? 70.182  25.114  69.125  1.00 206.91 ? 131  ASP B CB  1 
ATOM   13235 C  CG  . ASP C 1 131  ? 69.657  23.703  68.964  1.00 204.45 ? 131  ASP B CG  1 
ATOM   13236 O  OD1 . ASP C 1 131  ? 68.671  23.371  69.640  1.00 200.56 ? 131  ASP B OD1 1 
ATOM   13237 O  OD2 . ASP C 1 131  ? 70.207  22.925  68.160  1.00 206.89 ? 131  ASP B OD2 1 
ATOM   13238 N  N   . LYS C 1 132  ? 67.403  24.558  68.206  1.00 145.54 ? 132  LYS B N   1 
ATOM   13239 C  CA  . LYS C 1 132  ? 66.287  24.024  67.429  1.00 144.41 ? 132  LYS B CA  1 
ATOM   13240 C  C   . LYS C 1 132  ? 65.042  24.093  68.296  1.00 143.31 ? 132  LYS B C   1 
ATOM   13241 O  O   . LYS C 1 132  ? 65.142  24.508  69.444  1.00 138.61 ? 132  LYS B O   1 
ATOM   13242 C  CB  . LYS C 1 132  ? 66.564  22.612  66.900  1.00 141.04 ? 132  LYS B CB  1 
ATOM   13243 C  CG  . LYS C 1 132  ? 66.832  21.541  67.935  1.00 139.42 ? 132  LYS B CG  1 
ATOM   13244 C  CD  . LYS C 1 132  ? 67.954  20.609  67.466  1.00 146.50 ? 132  LYS B CD  1 
ATOM   13245 C  CE  . LYS C 1 132  ? 67.975  19.270  68.212  1.00 143.11 ? 132  LYS B CE  1 
ATOM   13246 N  NZ  . LYS C 1 132  ? 69.254  18.518  67.984  1.00 149.46 ? 132  LYS B NZ  1 
ATOM   13247 N  N   . PRO C 1 133  ? 63.863  23.741  67.752  1.00 146.98 ? 133  PRO B N   1 
ATOM   13248 C  CA  . PRO C 1 133  ? 62.649  23.998  68.503  1.00 138.54 ? 133  PRO B CA  1 
ATOM   13249 C  C   . PRO C 1 133  ? 61.903  22.717  68.581  1.00 137.60 ? 133  PRO B C   1 
ATOM   13250 O  O   . PRO C 1 133  ? 60.684  22.730  68.492  1.00 137.41 ? 133  PRO B O   1 
ATOM   13251 C  CB  . PRO C 1 133  ? 61.864  24.889  67.566  1.00 139.91 ? 133  PRO B CB  1 
ATOM   13252 C  CG  . PRO C 1 133  ? 62.295  24.384  66.182  1.00 144.96 ? 133  PRO B CG  1 
ATOM   13253 C  CD  . PRO C 1 133  ? 63.487  23.430  66.379  1.00 146.84 ? 133  PRO B CD  1 
ATOM   13254 N  N   . VAL C 1 134  ? 62.646  21.628  68.679  1.00 164.02 ? 134  VAL B N   1 
ATOM   13255 C  CA  . VAL C 1 134  ? 62.097  20.379  69.166  1.00 158.85 ? 134  VAL B CA  1 
ATOM   13256 C  C   . VAL C 1 134  ? 63.178  19.358  69.543  1.00 164.59 ? 134  VAL B C   1 
ATOM   13257 O  O   . VAL C 1 134  ? 64.226  19.252  68.892  1.00 171.65 ? 134  VAL B O   1 
ATOM   13258 C  CB  . VAL C 1 134  ? 61.052  19.781  68.209  1.00 154.66 ? 134  VAL B CB  1 
ATOM   13259 C  CG1 . VAL C 1 134  ? 60.863  18.314  68.504  1.00 153.68 ? 134  VAL B CG1 1 
ATOM   13260 C  CG2 . VAL C 1 134  ? 59.727  20.495  68.366  1.00 151.56 ? 134  VAL B CG2 1 
ATOM   13261 N  N   . TYR C 1 135  ? 62.907  18.621  70.616  1.00 135.66 ? 135  TYR B N   1 
ATOM   13262 C  CA  . TYR C 1 135  ? 63.896  17.757  71.202  1.00 139.31 ? 135  TYR B CA  1 
ATOM   13263 C  C   . TYR C 1 135  ? 63.267  16.477  71.682  1.00 136.97 ? 135  TYR B C   1 
ATOM   13264 O  O   . TYR C 1 135  ? 62.109  16.432  72.087  1.00 134.33 ? 135  TYR B O   1 
ATOM   13265 C  CB  . TYR C 1 135  ? 64.526  18.441  72.400  1.00 136.58 ? 135  TYR B CB  1 
ATOM   13266 C  CG  . TYR C 1 135  ? 65.267  19.729  72.136  1.00 138.93 ? 135  TYR B CG  1 
ATOM   13267 C  CD1 . TYR C 1 135  ? 66.651  19.742  71.983  1.00 142.83 ? 135  TYR B CD1 1 
ATOM   13268 C  CD2 . TYR C 1 135  ? 64.594  20.931  72.096  1.00 142.32 ? 135  TYR B CD2 1 
ATOM   13269 C  CE1 . TYR C 1 135  ? 67.337  20.913  71.771  1.00 145.17 ? 135  TYR B CE1 1 
ATOM   13270 C  CE2 . TYR C 1 135  ? 65.266  22.107  71.881  1.00 139.69 ? 135  TYR B CE2 1 
ATOM   13271 C  CZ  . TYR C 1 135  ? 66.638  22.096  71.717  1.00 143.57 ? 135  TYR B CZ  1 
ATOM   13272 O  OH  . TYR C 1 135  ? 67.296  23.285  71.498  1.00 146.03 ? 135  TYR B OH  1 
ATOM   13273 N  N   . THR C 1 136  ? 64.079  15.441  71.660  1.00 153.69 ? 136  THR B N   1 
ATOM   13274 C  CA  . THR C 1 136  ? 63.665  14.124  72.050  1.00 153.23 ? 136  THR B CA  1 
ATOM   13275 C  C   . THR C 1 136  ? 64.509  13.755  73.251  1.00 156.80 ? 136  THR B C   1 
ATOM   13276 O  O   . THR C 1 136  ? 65.557  14.371  73.478  1.00 157.20 ? 136  THR B O   1 
ATOM   13277 C  CB  . THR C 1 136  ? 63.996  13.160  70.937  1.00 157.41 ? 136  THR B CB  1 
ATOM   13278 O  OG1 . THR C 1 136  ? 65.343  13.407  70.517  1.00 161.72 ? 136  THR B OG1 1 
ATOM   13279 C  CG2 . THR C 1 136  ? 63.058  13.371  69.741  1.00 155.32 ? 136  THR B CG2 1 
ATOM   13280 N  N   . PRO C 1 137  ? 64.080  12.730  74.004  1.00 153.53 ? 137  PRO B N   1 
ATOM   13281 C  CA  . PRO C 1 137  ? 64.743  12.382  75.258  1.00 151.79 ? 137  PRO B CA  1 
ATOM   13282 C  C   . PRO C 1 137  ? 66.258  12.547  75.197  1.00 156.20 ? 137  PRO B C   1 
ATOM   13283 O  O   . PRO C 1 137  ? 66.912  12.062  74.274  1.00 158.00 ? 137  PRO B O   1 
ATOM   13284 C  CB  . PRO C 1 137  ? 64.386  10.908  75.425  1.00 153.29 ? 137  PRO B CB  1 
ATOM   13285 C  CG  . PRO C 1 137  ? 63.051  10.793  74.802  1.00 147.70 ? 137  PRO B CG  1 
ATOM   13286 C  CD  . PRO C 1 137  ? 63.025  11.761  73.660  1.00 149.76 ? 137  PRO B CD  1 
ATOM   13287 N  N   . ASP C 1 138  ? 66.802  13.253  76.176  1.00 176.17 ? 138  ASP B N   1 
ATOM   13288 C  CA  . ASP C 1 138  ? 68.231  13.200  76.453  1.00 180.74 ? 138  ASP B CA  1 
ATOM   13289 C  C   . ASP C 1 138  ? 69.092  14.152  75.632  1.00 187.15 ? 138  ASP B C   1 
ATOM   13290 O  O   . ASP C 1 138  ? 70.311  14.192  75.785  1.00 190.49 ? 138  ASP B O   1 
ATOM   13291 C  CB  . ASP C 1 138  ? 68.744  11.753  76.360  1.00 193.20 ? 138  ASP B CB  1 
ATOM   13292 C  CG  . ASP C 1 138  ? 68.389  10.926  77.597  1.00 196.73 ? 138  ASP B CG  1 
ATOM   13293 O  OD1 . ASP C 1 138  ? 68.869  11.285  78.695  1.00 199.12 ? 138  ASP B OD1 1 
ATOM   13294 O  OD2 . ASP C 1 138  ? 67.634  9.930   77.473  1.00 195.11 ? 138  ASP B OD2 1 
ATOM   13295 N  N   . GLN C 1 139  ? 68.482  14.943  74.776  1.00 156.48 ? 139  GLN B N   1 
ATOM   13296 C  CA  . GLN C 1 139  ? 69.302  15.893  74.061  1.00 159.74 ? 139  GLN B CA  1 
ATOM   13297 C  C   . GLN C 1 139  ? 69.753  17.019  75.004  1.00 163.19 ? 139  GLN B C   1 
ATOM   13298 O  O   . GLN C 1 139  ? 69.205  17.171  76.090  1.00 161.45 ? 139  GLN B O   1 
ATOM   13299 C  CB  . GLN C 1 139  ? 68.570  16.410  72.810  1.00 160.05 ? 139  GLN B CB  1 
ATOM   13300 C  CG  . GLN C 1 139  ? 68.263  15.318  71.749  1.00 159.50 ? 139  GLN B CG  1 
ATOM   13301 C  CD  . GLN C 1 139  ? 67.873  15.887  70.383  1.00 159.93 ? 139  GLN B CD  1 
ATOM   13302 O  OE1 . GLN C 1 139  ? 66.687  16.018  70.066  1.00 154.74 ? 139  GLN B OE1 1 
ATOM   13303 N  NE2 . GLN C 1 139  ? 68.875  16.220  69.569  1.00 164.79 ? 139  GLN B NE2 1 
ATOM   13304 N  N   . SER C 1 140  ? 70.792  17.753  74.611  1.00 147.90 ? 140  SER B N   1 
ATOM   13305 C  CA  . SER C 1 140  ? 71.164  18.994  75.288  1.00 150.03 ? 140  SER B CA  1 
ATOM   13306 C  C   . SER C 1 140  ? 70.648  20.201  74.487  1.00 146.64 ? 140  SER B C   1 
ATOM   13307 O  O   . SER C 1 140  ? 71.109  20.469  73.374  1.00 147.87 ? 140  SER B O   1 
ATOM   13308 C  CB  . SER C 1 140  ? 72.687  19.081  75.487  1.00 155.69 ? 140  SER B CB  1 
ATOM   13309 O  OG  . SER C 1 140  ? 73.031  19.830  76.643  1.00 156.74 ? 140  SER B OG  1 
ATOM   13310 N  N   . VAL C 1 141  ? 69.688  20.921  75.063  1.00 149.39 ? 141  VAL B N   1 
ATOM   13311 C  CA  . VAL C 1 141  ? 69.173  22.161  74.480  1.00 151.89 ? 141  VAL B CA  1 
ATOM   13312 C  C   . VAL C 1 141  ? 70.226  23.271  74.446  1.00 151.05 ? 141  VAL B C   1 
ATOM   13313 O  O   . VAL C 1 141  ? 70.396  24.002  75.419  1.00 151.80 ? 141  VAL B O   1 
ATOM   13314 C  CB  . VAL C 1 141  ? 67.931  22.678  75.256  1.00 145.67 ? 141  VAL B CB  1 
ATOM   13315 C  CG1 . VAL C 1 141  ? 67.537  24.083  74.798  1.00 144.26 ? 141  VAL B CG1 1 
ATOM   13316 C  CG2 . VAL C 1 141  ? 66.773  21.714  75.115  1.00 141.01 ? 141  VAL B CG2 1 
ATOM   13317 N  N   . LYS C 1 142  ? 70.942  23.390  73.332  1.00 154.99 ? 142  LYS B N   1 
ATOM   13318 C  CA  . LYS C 1 142  ? 71.756  24.579  73.108  1.00 162.55 ? 142  LYS B CA  1 
ATOM   13319 C  C   . LYS C 1 142  ? 70.845  25.808  73.118  1.00 163.63 ? 142  LYS B C   1 
ATOM   13320 O  O   . LYS C 1 142  ? 69.743  25.788  72.575  1.00 162.55 ? 142  LYS B O   1 
ATOM   13321 C  CB  . LYS C 1 142  ? 72.530  24.488  71.789  1.00 164.50 ? 142  LYS B CB  1 
ATOM   13322 C  CG  . LYS C 1 142  ? 73.949  23.937  71.931  1.00 169.58 ? 142  LYS B CG  1 
ATOM   13323 C  CD  . LYS C 1 142  ? 74.884  24.482  70.849  1.00 174.70 ? 142  LYS B CD  1 
ATOM   13324 C  CE  . LYS C 1 142  ? 76.322  24.037  71.070  1.00 180.15 ? 142  LYS B CE  1 
ATOM   13325 N  NZ  . LYS C 1 142  ? 76.395  22.566  71.265  1.00 178.46 ? 142  LYS B NZ  1 
ATOM   13326 N  N   . VAL C 1 143  ? 71.288  26.881  73.750  1.00 162.67 ? 143  VAL B N   1 
ATOM   13327 C  CA  . VAL C 1 143  ? 70.460  28.067  73.802  1.00 159.74 ? 143  VAL B CA  1 
ATOM   13328 C  C   . VAL C 1 143  ? 71.294  29.236  74.225  1.00 161.26 ? 143  VAL B C   1 
ATOM   13329 O  O   . VAL C 1 143  ? 72.270  29.076  74.950  1.00 165.41 ? 143  VAL B O   1 
ATOM   13330 C  CB  . VAL C 1 143  ? 69.331  27.900  74.807  1.00 155.20 ? 143  VAL B CB  1 
ATOM   13331 C  CG1 . VAL C 1 143  ? 69.900  27.371  76.084  1.00 155.82 ? 143  VAL B CG1 1 
ATOM   13332 C  CG2 . VAL C 1 143  ? 68.629  29.224  75.041  1.00 156.21 ? 143  VAL B CG2 1 
ATOM   13333 N  N   . ARG C 1 144  ? 70.909  30.409  73.747  1.00 156.03 ? 144  ARG B N   1 
ATOM   13334 C  CA  . ARG C 1 144  ? 71.498  31.643  74.205  1.00 159.11 ? 144  ARG B CA  1 
ATOM   13335 C  C   . ARG C 1 144  ? 70.452  32.746  74.203  1.00 155.61 ? 144  ARG B C   1 
ATOM   13336 O  O   . ARG C 1 144  ? 69.254  32.474  74.122  1.00 148.64 ? 144  ARG B O   1 
ATOM   13337 C  CB  . ARG C 1 144  ? 72.716  32.014  73.365  1.00 157.23 ? 144  ARG B CB  1 
ATOM   13338 C  CG  . ARG C 1 144  ? 72.656  31.604  71.909  1.00 158.70 ? 144  ARG B CG  1 
ATOM   13339 C  CD  . ARG C 1 144  ? 73.667  32.437  71.109  1.00 165.26 ? 144  ARG B CD  1 
ATOM   13340 N  NE  . ARG C 1 144  ? 73.714  32.128  69.681  1.00 166.73 ? 144  ARG B NE  1 
ATOM   13341 C  CZ  . ARG C 1 144  ? 74.740  31.537  69.079  1.00 171.42 ? 144  ARG B CZ  1 
ATOM   13342 N  NH1 . ARG C 1 144  ? 75.812  31.189  69.774  1.00 174.14 ? 144  ARG B NH1 1 
ATOM   13343 N  NH2 . ARG C 1 144  ? 74.696  31.297  67.780  1.00 172.61 ? 144  ARG B NH2 1 
ATOM   13344 N  N   . VAL C 1 145  ? 70.915  33.988  74.304  1.00 172.09 ? 145  VAL B N   1 
ATOM   13345 C  CA  . VAL C 1 145  ? 70.022  35.137  74.323  1.00 163.94 ? 145  VAL B CA  1 
ATOM   13346 C  C   . VAL C 1 145  ? 70.655  36.430  73.843  1.00 172.22 ? 145  VAL B C   1 
ATOM   13347 O  O   . VAL C 1 145  ? 71.765  36.810  74.239  1.00 172.10 ? 145  VAL B O   1 
ATOM   13348 C  CB  . VAL C 1 145  ? 69.422  35.390  75.694  1.00 163.63 ? 145  VAL B CB  1 
ATOM   13349 C  CG1 . VAL C 1 145  ? 69.037  36.853  75.831  1.00 164.07 ? 145  VAL B CG1 1 
ATOM   13350 C  CG2 . VAL C 1 145  ? 68.217  34.524  75.873  1.00 159.54 ? 145  VAL B CG2 1 
ATOM   13351 N  N   . TYR C 1 146  ? 69.914  37.097  72.970  1.00 168.93 ? 146  TYR B N   1 
ATOM   13352 C  CA  . TYR C 1 146  ? 70.298  38.390  72.459  1.00 172.60 ? 146  TYR B CA  1 
ATOM   13353 C  C   . TYR C 1 146  ? 69.428  39.399  73.170  1.00 174.33 ? 146  TYR B C   1 
ATOM   13354 O  O   . TYR C 1 146  ? 68.210  39.223  73.252  1.00 171.52 ? 146  TYR B O   1 
ATOM   13355 C  CB  . TYR C 1 146  ? 70.047  38.421  70.963  1.00 166.11 ? 146  TYR B CB  1 
ATOM   13356 C  CG  . TYR C 1 146  ? 70.552  37.174  70.294  1.00 175.00 ? 146  TYR B CG  1 
ATOM   13357 C  CD1 . TYR C 1 146  ? 71.893  36.831  70.367  1.00 181.37 ? 146  TYR B CD1 1 
ATOM   13358 C  CD2 . TYR C 1 146  ? 69.694  36.329  69.607  1.00 173.45 ? 146  TYR B CD2 1 
ATOM   13359 C  CE1 . TYR C 1 146  ? 72.372  35.686  69.763  1.00 181.80 ? 146  TYR B CE1 1 
ATOM   13360 C  CE2 . TYR C 1 146  ? 70.167  35.181  68.993  1.00 172.96 ? 146  TYR B CE2 1 
ATOM   13361 C  CZ  . TYR C 1 146  ? 71.510  34.863  69.077  1.00 176.61 ? 146  TYR B CZ  1 
ATOM   13362 O  OH  . TYR C 1 146  ? 72.000  33.726  68.475  1.00 175.17 ? 146  TYR B OH  1 
ATOM   13363 N  N   . SER C 1 147  ? 70.057  40.443  73.707  1.00 158.93 ? 147  SER B N   1 
ATOM   13364 C  CA  . SER C 1 147  ? 69.346  41.443  74.509  1.00 160.79 ? 147  SER B CA  1 
ATOM   13365 C  C   . SER C 1 147  ? 69.724  42.871  74.141  1.00 166.09 ? 147  SER B C   1 
ATOM   13366 O  O   . SER C 1 147  ? 70.903  43.228  74.061  1.00 171.33 ? 147  SER B O   1 
ATOM   13367 C  CB  . SER C 1 147  ? 69.572  41.217  76.005  1.00 163.24 ? 147  SER B CB  1 
ATOM   13368 O  OG  . SER C 1 147  ? 70.891  41.560  76.386  1.00 170.02 ? 147  SER B OG  1 
ATOM   13369 N  N   . LEU C 1 148  ? 68.699  43.684  73.932  1.00 226.88 ? 148  LEU B N   1 
ATOM   13370 C  CA  . LEU C 1 148  ? 68.892  45.051  73.507  1.00 230.21 ? 148  LEU B CA  1 
ATOM   13371 C  C   . LEU C 1 148  ? 68.139  45.985  74.413  1.00 235.31 ? 148  LEU B C   1 
ATOM   13372 O  O   . LEU C 1 148  ? 67.170  45.588  75.048  1.00 235.28 ? 148  LEU B O   1 
ATOM   13373 C  CB  . LEU C 1 148  ? 68.396  45.233  72.086  1.00 227.61 ? 148  LEU B CB  1 
ATOM   13374 C  CG  . LEU C 1 148  ? 69.549  45.474  71.128  1.00 230.41 ? 148  LEU B CG  1 
ATOM   13375 C  CD1 . LEU C 1 148  ? 70.678  44.508  71.433  1.00 231.18 ? 148  LEU B CD1 1 
ATOM   13376 C  CD2 . LEU C 1 148  ? 69.080  45.330  69.698  1.00 229.52 ? 148  LEU B CD2 1 
ATOM   13377 N  N   . ASN C 1 149  ? 68.612  47.226  74.471  1.00 241.63 ? 149  ASN B N   1 
ATOM   13378 C  CA  . ASN C 1 149  ? 67.946  48.299  75.187  1.00 240.45 ? 149  ASN B CA  1 
ATOM   13379 C  C   . ASN C 1 149  ? 67.065  49.087  74.232  1.00 237.68 ? 149  ASN B C   1 
ATOM   13380 O  O   . ASN C 1 149  ? 67.239  49.007  73.023  1.00 236.30 ? 149  ASN B O   1 
ATOM   13381 C  CB  . ASN C 1 149  ? 68.985  49.225  75.809  1.00 249.34 ? 149  ASN B CB  1 
ATOM   13382 C  CG  . ASN C 1 149  ? 69.943  49.784  74.784  1.00 257.60 ? 149  ASN B CG  1 
ATOM   13383 O  OD1 . ASN C 1 149  ? 70.098  49.237  73.691  1.00 257.74 ? 149  ASN B OD1 1 
ATOM   13384 N  ND2 . ASN C 1 149  ? 70.595  50.880  75.130  1.00 264.16 ? 149  ASN B ND2 1 
ATOM   13385 N  N   . ASP C 1 150  ? 66.118  49.832  74.783  1.00 197.99 ? 150  ASP B N   1 
ATOM   13386 C  CA  . ASP C 1 150  ? 65.307  50.760  74.021  1.00 200.40 ? 150  ASP B CA  1 
ATOM   13387 C  C   . ASP C 1 150  ? 66.063  51.334  72.847  1.00 201.37 ? 150  ASP B C   1 
ATOM   13388 O  O   . ASP C 1 150  ? 65.474  51.574  71.809  1.00 200.70 ? 150  ASP B O   1 
ATOM   13389 C  CB  . ASP C 1 150  ? 64.976  51.932  74.908  1.00 203.75 ? 150  ASP B CB  1 
ATOM   13390 C  CG  . ASP C 1 150  ? 66.224  52.512  75.565  1.00 223.31 ? 150  ASP B CG  1 
ATOM   13391 O  OD1 . ASP C 1 150  ? 66.391  53.755  75.577  1.00 225.78 ? 150  ASP B OD1 1 
ATOM   13392 O  OD2 . ASP C 1 150  ? 67.059  51.707  76.048  1.00 225.19 ? 150  ASP B OD2 1 
ATOM   13393 N  N   . ASP C 1 151  ? 67.358  51.595  73.029  1.00 227.19 ? 151  ASP B N   1 
ATOM   13394 C  CA  . ASP C 1 151  ? 68.197  52.231  72.002  1.00 235.31 ? 151  ASP B CA  1 
ATOM   13395 C  C   . ASP C 1 151  ? 68.870  51.175  71.110  1.00 234.60 ? 151  ASP B C   1 
ATOM   13396 O  O   . ASP C 1 151  ? 69.890  51.437  70.475  1.00 240.18 ? 151  ASP B O   1 
ATOM   13397 C  CB  . ASP C 1 151  ? 69.262  53.143  72.652  1.00 244.43 ? 151  ASP B CB  1 
ATOM   13398 C  CG  . ASP C 1 151  ? 69.287  54.578  72.076  1.00 250.78 ? 151  ASP B CG  1 
ATOM   13399 O  OD1 . ASP C 1 151  ? 70.054  55.416  72.613  1.00 256.47 ? 151  ASP B OD1 1 
ATOM   13400 O  OD2 . ASP C 1 151  ? 68.559  54.876  71.102  1.00 249.46 ? 151  ASP B OD2 1 
ATOM   13401 N  N   . LEU C 1 152  ? 68.298  49.975  71.086  1.00 194.42 ? 152  LEU B N   1 
ATOM   13402 C  CA  . LEU C 1 152  ? 68.754  48.900  70.206  1.00 196.76 ? 152  LEU B CA  1 
ATOM   13403 C  C   . LEU C 1 152  ? 70.287  48.837  70.063  1.00 204.29 ? 152  LEU B C   1 
ATOM   13404 O  O   . LEU C 1 152  ? 70.822  48.719  68.954  1.00 205.85 ? 152  LEU B O   1 
ATOM   13405 C  CB  . LEU C 1 152  ? 68.053  48.980  68.837  1.00 196.44 ? 152  LEU B CB  1 
ATOM   13406 C  CG  . LEU C 1 152  ? 66.524  48.809  68.755  1.00 192.85 ? 152  LEU B CG  1 
ATOM   13407 C  CD1 . LEU C 1 152  ? 66.050  47.733  69.697  1.00 187.94 ? 152  LEU B CD1 1 
ATOM   13408 C  CD2 . LEU C 1 152  ? 65.769  50.100  69.015  1.00 195.31 ? 152  LEU B CD2 1 
ATOM   13409 N  N   . LYS C 1 153  ? 70.982  48.933  71.196  1.00 229.66 ? 153  LYS B N   1 
ATOM   13410 C  CA  . LYS C 1 153  ? 72.425  48.706  71.246  1.00 233.79 ? 153  LYS B CA  1 
ATOM   13411 C  C   . LYS C 1 153  ? 72.715  47.566  72.232  1.00 232.93 ? 153  LYS B C   1 
ATOM   13412 O  O   . LYS C 1 153  ? 71.801  47.117  72.922  1.00 226.94 ? 153  LYS B O   1 
ATOM   13413 C  CB  . LYS C 1 153  ? 73.171  49.998  71.592  1.00 241.12 ? 153  LYS B CB  1 
ATOM   13414 C  CG  . LYS C 1 153  ? 73.655  50.762  70.358  1.00 245.05 ? 153  LYS B CG  1 
ATOM   13415 C  CD  . LYS C 1 153  ? 74.335  52.085  70.722  1.00 252.18 ? 153  LYS B CD  1 
ATOM   13416 C  CE  . LYS C 1 153  ? 74.975  52.776  69.505  1.00 257.36 ? 153  LYS B CE  1 
ATOM   13417 N  NZ  . LYS C 1 153  ? 74.005  53.238  68.460  1.00 256.48 ? 153  LYS B NZ  1 
ATOM   13418 N  N   . PRO C 1 154  ? 73.976  47.088  72.296  1.00 199.02 ? 154  PRO B N   1 
ATOM   13419 C  CA  . PRO C 1 154  ? 74.311  45.822  72.968  1.00 201.69 ? 154  PRO B CA  1 
ATOM   13420 C  C   . PRO C 1 154  ? 73.472  45.549  74.212  1.00 201.38 ? 154  PRO B C   1 
ATOM   13421 O  O   . PRO C 1 154  ? 73.003  44.425  74.404  1.00 200.10 ? 154  PRO B O   1 
ATOM   13422 C  CB  . PRO C 1 154  ? 75.773  46.019  73.369  1.00 204.89 ? 154  PRO B CB  1 
ATOM   13423 C  CG  . PRO C 1 154  ? 76.317  46.923  72.340  1.00 208.13 ? 154  PRO B CG  1 
ATOM   13424 C  CD  . PRO C 1 154  ? 75.189  47.817  71.887  1.00 205.46 ? 154  PRO B CD  1 
ATOM   13425 N  N   . ALA C 1 155  ? 73.306  46.580  75.039  1.00 256.35 ? 155  ALA B N   1 
ATOM   13426 C  CA  . ALA C 1 155  ? 72.476  46.536  76.240  1.00 256.17 ? 155  ALA B CA  1 
ATOM   13427 C  C   . ALA C 1 155  ? 73.086  45.692  77.355  1.00 260.19 ? 155  ALA B C   1 
ATOM   13428 O  O   . ALA C 1 155  ? 72.360  45.119  78.169  1.00 257.69 ? 155  ALA B O   1 
ATOM   13429 C  CB  . ALA C 1 155  ? 71.079  46.045  75.906  1.00 249.14 ? 155  ALA B CB  1 
ATOM   13430 N  N   . LYS C 1 156  ? 74.415  45.629  77.391  1.00 210.81 ? 156  LYS B N   1 
ATOM   13431 C  CA  . LYS C 1 156  ? 75.127  44.845  78.389  1.00 211.17 ? 156  LYS B CA  1 
ATOM   13432 C  C   . LYS C 1 156  ? 74.323  44.880  79.681  1.00 206.87 ? 156  LYS B C   1 
ATOM   13433 O  O   . LYS C 1 156  ? 73.785  45.923  80.045  1.00 207.86 ? 156  LYS B O   1 
ATOM   13434 C  CB  . LYS C 1 156  ? 76.541  45.409  78.594  1.00 218.81 ? 156  LYS B CB  1 
ATOM   13435 C  CG  . LYS C 1 156  ? 77.439  45.323  77.353  1.00 222.03 ? 156  LYS B CG  1 
ATOM   13436 C  CD  . LYS C 1 156  ? 78.506  46.430  77.284  1.00 229.80 ? 156  LYS B CD  1 
ATOM   13437 C  CE  . LYS C 1 156  ? 79.230  46.420  75.927  1.00 233.32 ? 156  LYS B CE  1 
ATOM   13438 N  NZ  . LYS C 1 156  ? 80.180  47.554  75.722  1.00 240.71 ? 156  LYS B NZ  1 
ATOM   13439 N  N   . ARG C 1 157  ? 74.211  43.733  80.345  1.00 218.50 ? 157  ARG B N   1 
ATOM   13440 C  CA  . ARG C 1 157  ? 73.488  43.624  81.607  1.00 214.79 ? 157  ARG B CA  1 
ATOM   13441 C  C   . ARG C 1 157  ? 73.612  42.217  82.158  1.00 214.99 ? 157  ARG B C   1 
ATOM   13442 O  O   . ARG C 1 157  ? 74.243  41.358  81.549  1.00 215.41 ? 157  ARG B O   1 
ATOM   13443 C  CB  . ARG C 1 157  ? 72.002  43.940  81.424  1.00 205.82 ? 157  ARG B CB  1 
ATOM   13444 C  CG  . ARG C 1 157  ? 71.657  45.402  81.198  1.00 202.25 ? 157  ARG B CG  1 
ATOM   13445 C  CD  . ARG C 1 157  ? 70.170  45.578  81.022  1.00 192.43 ? 157  ARG B CD  1 
ATOM   13446 N  NE  . ARG C 1 157  ? 69.829  46.793  80.297  1.00 192.43 ? 157  ARG B NE  1 
ATOM   13447 C  CZ  . ARG C 1 157  ? 68.589  47.123  79.951  1.00 188.24 ? 157  ARG B CZ  1 
ATOM   13448 N  NH1 . ARG C 1 157  ? 67.573  46.331  80.269  1.00 181.98 ? 157  ARG B NH1 1 
ATOM   13449 N  NH2 . ARG C 1 157  ? 68.365  48.250  79.289  1.00 190.19 ? 157  ARG B NH2 1 
ATOM   13450 N  N   . GLU C 1 158  ? 73.004  41.990  83.317  1.00 247.32 ? 158  GLU B N   1 
ATOM   13451 C  CA  . GLU C 1 158  ? 72.870  40.641  83.858  1.00 246.75 ? 158  GLU B CA  1 
ATOM   13452 C  C   . GLU C 1 158  ? 71.437  40.141  83.729  1.00 239.71 ? 158  GLU B C   1 
ATOM   13453 O  O   . GLU C 1 158  ? 70.490  40.817  84.134  1.00 239.48 ? 158  GLU B O   1 
ATOM   13454 C  CB  . GLU C 1 158  ? 73.326  40.570  85.317  1.00 254.20 ? 158  GLU B CB  1 
ATOM   13455 C  CG  . GLU C 1 158  ? 74.833  40.535  85.480  1.00 263.02 ? 158  GLU B CG  1 
ATOM   13456 C  CD  . GLU C 1 158  ? 75.271  39.706  86.668  1.00 269.09 ? 158  GLU B CD  1 
ATOM   13457 O  OE1 . GLU C 1 158  ? 74.844  38.536  86.765  1.00 268.00 ? 158  GLU B OE1 1 
ATOM   13458 O  OE2 . GLU C 1 158  ? 76.040  40.222  87.506  1.00 274.83 ? 158  GLU B OE2 1 
ATOM   13459 N  N   . THR C 1 159  ? 71.288  38.948  83.163  1.00 190.48 ? 159  THR B N   1 
ATOM   13460 C  CA  . THR C 1 159  ? 69.976  38.386  82.914  1.00 178.18 ? 159  THR B CA  1 
ATOM   13461 C  C   . THR C 1 159  ? 69.902  36.984  83.449  1.00 167.12 ? 159  THR B C   1 
ATOM   13462 O  O   . THR C 1 159  ? 70.920  36.298  83.591  1.00 168.39 ? 159  THR B O   1 
ATOM   13463 C  CB  . THR C 1 159  ? 69.686  38.295  81.413  1.00 179.16 ? 159  THR B CB  1 
ATOM   13464 O  OG1 . THR C 1 159  ? 69.861  39.582  80.801  1.00 182.84 ? 159  THR B OG1 1 
ATOM   13465 C  CG2 . THR C 1 159  ? 68.269  37.795  81.174  1.00 174.06 ? 159  THR B CG2 1 
ATOM   13466 N  N   . VAL C 1 160  ? 68.671  36.577  83.738  1.00 160.04 ? 160  VAL B N   1 
ATOM   13467 C  CA  . VAL C 1 160  ? 68.344  35.207  84.112  1.00 153.49 ? 160  VAL B CA  1 
ATOM   13468 C  C   . VAL C 1 160  ? 67.147  34.725  83.321  1.00 147.85 ? 160  VAL B C   1 
ATOM   13469 O  O   . VAL C 1 160  ? 66.173  35.476  83.101  1.00 144.95 ? 160  VAL B O   1 
ATOM   13470 C  CB  . VAL C 1 160  ? 67.880  35.067  85.565  1.00 153.36 ? 160  VAL B CB  1 
ATOM   13471 C  CG1 . VAL C 1 160  ? 66.650  34.169  85.640  1.00 148.30 ? 160  VAL B CG1 1 
ATOM   13472 C  CG2 . VAL C 1 160  ? 68.952  34.481  86.407  1.00 157.96 ? 160  VAL B CG2 1 
ATOM   13473 N  N   . LEU C 1 161  ? 67.224  33.453  82.931  1.00 176.36 ? 161  LEU B N   1 
ATOM   13474 C  CA  . LEU C 1 161  ? 66.070  32.692  82.483  1.00 171.25 ? 161  LEU B CA  1 
ATOM   13475 C  C   . LEU C 1 161  ? 65.618  31.643  83.509  1.00 170.13 ? 161  LEU B C   1 
ATOM   13476 O  O   . LEU C 1 161  ? 66.220  31.464  84.579  1.00 173.28 ? 161  LEU B O   1 
ATOM   13477 C  CB  . LEU C 1 161  ? 66.338  32.051  81.120  1.00 169.75 ? 161  LEU B CB  1 
ATOM   13478 C  CG  . LEU C 1 161  ? 67.797  31.789  80.765  1.00 172.72 ? 161  LEU B CG  1 
ATOM   13479 C  CD1 . LEU C 1 161  ? 68.271  30.391  81.179  1.00 173.31 ? 161  LEU B CD1 1 
ATOM   13480 C  CD2 . LEU C 1 161  ? 67.955  31.989  79.294  1.00 171.23 ? 161  LEU B CD2 1 
ATOM   13481 N  N   . THR C 1 162  ? 64.551  30.946  83.147  1.00 185.80 ? 162  THR B N   1 
ATOM   13482 C  CA  . THR C 1 162  ? 63.833  30.113  84.081  1.00 181.99 ? 162  THR B CA  1 
ATOM   13483 C  C   . THR C 1 162  ? 62.937  29.107  83.344  1.00 177.48 ? 162  THR B C   1 
ATOM   13484 O  O   . THR C 1 162  ? 61.734  29.337  83.201  1.00 174.62 ? 162  THR B O   1 
ATOM   13485 C  CB  . THR C 1 162  ? 63.017  31.014  85.041  1.00 204.01 ? 162  THR B CB  1 
ATOM   13486 O  OG1 . THR C 1 162  ? 61.682  30.521  85.191  1.00 199.95 ? 162  THR B OG1 1 
ATOM   13487 C  CG2 . THR C 1 162  ? 62.942  32.439  84.507  1.00 203.08 ? 162  THR B CG2 1 
ATOM   13488 N  N   . PHE C 1 163  ? 63.529  27.994  82.882  1.00 171.02 ? 163  PHE B N   1 
ATOM   13489 C  CA  . PHE C 1 163  ? 62.812  26.957  82.105  1.00 166.80 ? 163  PHE B CA  1 
ATOM   13490 C  C   . PHE C 1 163  ? 61.604  26.490  82.867  1.00 164.05 ? 163  PHE B C   1 
ATOM   13491 O  O   . PHE C 1 163  ? 61.573  26.575  84.086  1.00 165.85 ? 163  PHE B O   1 
ATOM   13492 C  CB  . PHE C 1 163  ? 63.679  25.728  81.827  1.00 167.91 ? 163  PHE B CB  1 
ATOM   13493 C  CG  . PHE C 1 163  ? 65.029  26.048  81.295  1.00 170.92 ? 163  PHE B CG  1 
ATOM   13494 C  CD1 . PHE C 1 163  ? 65.778  27.068  81.840  1.00 175.07 ? 163  PHE B CD1 1 
ATOM   13495 C  CD2 . PHE C 1 163  ? 65.573  25.313  80.281  1.00 169.35 ? 163  PHE B CD2 1 
ATOM   13496 C  CE1 . PHE C 1 163  ? 67.033  27.362  81.366  1.00 180.18 ? 163  PHE B CE1 1 
ATOM   13497 C  CE2 . PHE C 1 163  ? 66.832  25.607  79.810  1.00 173.41 ? 163  PHE B CE2 1 
ATOM   13498 C  CZ  . PHE C 1 163  ? 67.560  26.631  80.356  1.00 179.43 ? 163  PHE B CZ  1 
ATOM   13499 N  N   . ILE C 1 164  ? 60.621  25.964  82.158  1.00 151.58 ? 164  ILE B N   1 
ATOM   13500 C  CA  . ILE C 1 164  ? 59.350  25.654  82.785  1.00 151.88 ? 164  ILE B CA  1 
ATOM   13501 C  C   . ILE C 1 164  ? 58.682  24.436  82.155  1.00 151.58 ? 164  ILE B C   1 
ATOM   13502 O  O   . ILE C 1 164  ? 58.105  24.503  81.062  1.00 149.45 ? 164  ILE B O   1 
ATOM   13503 C  CB  . ILE C 1 164  ? 58.400  26.863  82.745  1.00 154.34 ? 164  ILE B CB  1 
ATOM   13504 C  CG1 . ILE C 1 164  ? 59.025  28.055  83.462  1.00 159.26 ? 164  ILE B CG1 1 
ATOM   13505 C  CG2 . ILE C 1 164  ? 57.073  26.535  83.385  1.00 152.56 ? 164  ILE B CG2 1 
ATOM   13506 C  CD1 . ILE C 1 164  ? 58.091  29.244  83.568  1.00 158.60 ? 164  ILE B CD1 1 
ATOM   13507 N  N   . ASP C 1 165  ? 58.747  23.320  82.872  1.00 197.92 ? 165  ASP B N   1 
ATOM   13508 C  CA  . ASP C 1 165  ? 58.242  22.061  82.361  1.00 199.70 ? 165  ASP B CA  1 
ATOM   13509 C  C   . ASP C 1 165  ? 56.849  22.218  81.810  1.00 191.10 ? 165  ASP B C   1 
ATOM   13510 O  O   . ASP C 1 165  ? 56.134  23.152  82.140  1.00 187.06 ? 165  ASP B O   1 
ATOM   13511 C  CB  . ASP C 1 165  ? 58.298  20.958  83.425  1.00 208.93 ? 165  ASP B CB  1 
ATOM   13512 C  CG  . ASP C 1 165  ? 57.054  20.892  84.288  1.00 216.30 ? 165  ASP B CG  1 
ATOM   13513 O  OD1 . ASP C 1 165  ? 56.148  21.746  84.156  1.00 218.19 ? 165  ASP B OD1 1 
ATOM   13514 O  OD2 . ASP C 1 165  ? 57.000  19.961  85.117  1.00 218.98 ? 165  ASP B OD2 1 
ATOM   13515 N  N   . PRO C 1 166  ? 56.479  21.301  80.938  1.00 158.34 ? 166  PRO B N   1 
ATOM   13516 C  CA  . PRO C 1 166  ? 55.209  21.259  80.212  1.00 155.11 ? 166  PRO B CA  1 
ATOM   13517 C  C   . PRO C 1 166  ? 53.930  21.286  81.084  1.00 151.16 ? 166  PRO B C   1 
ATOM   13518 O  O   . PRO C 1 166  ? 52.837  21.068  80.563  1.00 147.67 ? 166  PRO B O   1 
ATOM   13519 C  CB  . PRO C 1 166  ? 55.327  19.959  79.403  1.00 157.00 ? 166  PRO B CB  1 
ATOM   13520 C  CG  . PRO C 1 166  ? 56.831  19.795  79.181  1.00 161.37 ? 166  PRO B CG  1 
ATOM   13521 C  CD  . PRO C 1 166  ? 57.481  20.362  80.400  1.00 162.06 ? 166  PRO B CD  1 
ATOM   13522 N  N   . GLU C 1 167  ? 54.045  21.555  82.379  1.00 195.95 ? 167  GLU B N   1 
ATOM   13523 C  CA  . GLU C 1 167  ? 52.848  21.654  83.218  1.00 195.95 ? 167  GLU B CA  1 
ATOM   13524 C  C   . GLU C 1 167  ? 52.829  22.969  83.971  1.00 197.26 ? 167  GLU B C   1 
ATOM   13525 O  O   . GLU C 1 167  ? 51.856  23.313  84.642  1.00 198.04 ? 167  GLU B O   1 
ATOM   13526 C  CB  . GLU C 1 167  ? 52.747  20.479  84.191  1.00 199.29 ? 167  GLU B CB  1 
ATOM   13527 C  CG  . GLU C 1 167  ? 52.353  19.144  83.546  1.00 200.95 ? 167  GLU B CG  1 
ATOM   13528 C  CD  . GLU C 1 167  ? 52.192  17.996  84.558  1.00 205.48 ? 167  GLU B CD  1 
ATOM   13529 O  OE1 . GLU C 1 167  ? 51.152  17.942  85.254  1.00 205.61 ? 167  GLU B OE1 1 
ATOM   13530 O  OE2 . GLU C 1 167  ? 53.095  17.131  84.644  1.00 208.07 ? 167  GLU B OE2 1 
ATOM   13531 N  N   . GLY C 1 168  ? 53.925  23.702  83.852  1.00 190.10 ? 168  GLY B N   1 
ATOM   13532 C  CA  . GLY C 1 168  ? 53.946  25.075  84.295  1.00 192.22 ? 168  GLY B CA  1 
ATOM   13533 C  C   . GLY C 1 168  ? 54.594  25.171  85.639  1.00 197.97 ? 168  GLY B C   1 
ATOM   13534 O  O   . GLY C 1 168  ? 54.231  26.007  86.454  1.00 199.07 ? 168  GLY B O   1 
ATOM   13535 N  N   . SER C 1 169  ? 55.560  24.300  85.874  1.00 141.31 ? 169  SER B N   1 
ATOM   13536 C  CA  . SER C 1 169  ? 56.299  24.334  87.127  1.00 148.32 ? 169  SER B CA  1 
ATOM   13537 C  C   . SER C 1 169  ? 57.786  24.579  86.884  1.00 149.08 ? 169  SER B C   1 
ATOM   13538 O  O   . SER C 1 169  ? 58.437  23.803  86.189  1.00 147.53 ? 169  SER B O   1 
ATOM   13539 C  CB  . SER C 1 169  ? 56.087  23.023  87.882  1.00 152.48 ? 169  SER B CB  1 
ATOM   13540 O  OG  . SER C 1 169  ? 57.214  22.704  88.676  1.00 158.51 ? 169  SER B OG  1 
ATOM   13541 N  N   . GLU C 1 170  ? 58.327  25.649  87.458  1.00 161.06 ? 170  GLU B N   1 
ATOM   13542 C  CA  . GLU C 1 170  ? 59.732  25.959  87.240  1.00 164.53 ? 170  GLU B CA  1 
ATOM   13543 C  C   . GLU C 1 170  ? 60.520  24.660  87.239  1.00 160.87 ? 170  GLU B C   1 
ATOM   13544 O  O   . GLU C 1 170  ? 60.033  23.657  87.733  1.00 156.98 ? 170  GLU B O   1 
ATOM   13545 C  CB  . GLU C 1 170  ? 60.261  26.867  88.348  1.00 174.61 ? 170  GLU B CB  1 
ATOM   13546 C  CG  . GLU C 1 170  ? 59.652  28.260  88.399  1.00 179.70 ? 170  GLU B CG  1 
ATOM   13547 C  CD  . GLU C 1 170  ? 60.487  29.230  89.233  1.00 190.37 ? 170  GLU B CD  1 
ATOM   13548 O  OE1 . GLU C 1 170  ? 61.262  28.762  90.098  1.00 195.94 ? 170  GLU B OE1 1 
ATOM   13549 O  OE2 . GLU C 1 170  ? 60.373  30.459  89.017  1.00 192.97 ? 170  GLU B OE2 1 
ATOM   13550 N  N   . VAL C 1 171  ? 61.732  24.661  86.700  1.00 152.59 ? 171  VAL B N   1 
ATOM   13551 C  CA  . VAL C 1 171  ? 62.544  23.452  86.758  1.00 154.32 ? 171  VAL B CA  1 
ATOM   13552 C  C   . VAL C 1 171  ? 64.043  23.754  86.813  1.00 155.49 ? 171  VAL B C   1 
ATOM   13553 O  O   . VAL C 1 171  ? 64.866  22.860  86.967  1.00 157.77 ? 171  VAL B O   1 
ATOM   13554 C  CB  . VAL C 1 171  ? 62.162  22.427  85.631  1.00 156.13 ? 171  VAL B CB  1 
ATOM   13555 C  CG1 . VAL C 1 171  ? 63.116  21.231  85.601  1.00 159.21 ? 171  VAL B CG1 1 
ATOM   13556 C  CG2 . VAL C 1 171  ? 60.752  21.922  85.819  1.00 152.32 ? 171  VAL B CG2 1 
ATOM   13557 N  N   . ASP C 1 172  ? 64.399  25.022  86.741  1.00 146.55 ? 172  ASP B N   1 
ATOM   13558 C  CA  . ASP C 1 172  ? 65.803  25.371  86.779  1.00 152.52 ? 172  ASP B CA  1 
ATOM   13559 C  C   . ASP C 1 172  ? 65.861  26.865  86.882  1.00 154.50 ? 172  ASP B C   1 
ATOM   13560 O  O   . ASP C 1 172  ? 64.893  27.488  87.303  1.00 151.55 ? 172  ASP B O   1 
ATOM   13561 C  CB  . ASP C 1 172  ? 66.479  24.904  85.492  1.00 154.67 ? 172  ASP B CB  1 
ATOM   13562 C  CG  . ASP C 1 172  ? 67.996  24.776  85.612  1.00 163.15 ? 172  ASP B CG  1 
ATOM   13563 O  OD1 . ASP C 1 172  ? 68.494  23.659  85.348  1.00 163.64 ? 172  ASP B OD1 1 
ATOM   13564 O  OD2 . ASP C 1 172  ? 68.689  25.772  85.932  1.00 168.18 ? 172  ASP B OD2 1 
ATOM   13565 N  N   . MET C 1 173  ? 66.986  27.435  86.473  1.00 163.92 ? 173  MET B N   1 
ATOM   13566 C  CA  . MET C 1 173  ? 67.196  28.865  86.527  1.00 165.40 ? 173  MET B CA  1 
ATOM   13567 C  C   . MET C 1 173  ? 68.664  29.075  86.286  1.00 167.89 ? 173  MET B C   1 
ATOM   13568 O  O   . MET C 1 173  ? 69.432  28.116  86.264  1.00 171.17 ? 173  MET B O   1 
ATOM   13569 C  CB  . MET C 1 173  ? 66.842  29.385  87.915  1.00 168.88 ? 173  MET B CB  1 
ATOM   13570 C  CG  . MET C 1 173  ? 65.938  30.592  87.925  1.00 169.66 ? 173  MET B CG  1 
ATOM   13571 S  SD  . MET C 1 173  ? 65.118  30.798  89.519  1.00 184.80 ? 173  MET B SD  1 
ATOM   13572 C  CE  . MET C 1 173  ? 64.287  29.218  89.686  1.00 173.39 ? 173  MET B CE  1 
ATOM   13573 N  N   . VAL C 1 174  ? 69.050  30.327  86.102  1.00 173.68 ? 174  VAL B N   1 
ATOM   13574 C  CA  . VAL C 1 174  ? 70.457  30.686  86.033  1.00 180.42 ? 174  VAL B CA  1 
ATOM   13575 C  C   . VAL C 1 174  ? 70.577  32.069  85.417  1.00 181.64 ? 174  VAL B C   1 
ATOM   13576 O  O   . VAL C 1 174  ? 69.671  32.519  84.720  1.00 179.95 ? 174  VAL B O   1 
ATOM   13577 C  CB  . VAL C 1 174  ? 71.284  29.641  85.245  1.00 183.99 ? 174  VAL B CB  1 
ATOM   13578 C  CG1 . VAL C 1 174  ? 70.579  29.277  83.955  1.00 180.05 ? 174  VAL B CG1 1 
ATOM   13579 C  CG2 . VAL C 1 174  ? 72.699  30.134  84.982  1.00 189.74 ? 174  VAL B CG2 1 
ATOM   13580 N  N   . GLU C 1 175  ? 71.683  32.745  85.700  1.00 197.28 ? 175  GLU B N   1 
ATOM   13581 C  CA  . GLU C 1 175  ? 71.924  34.089  85.203  1.00 199.73 ? 175  GLU B CA  1 
ATOM   13582 C  C   . GLU C 1 175  ? 73.181  34.052  84.346  1.00 202.10 ? 175  GLU B C   1 
ATOM   13583 O  O   . GLU C 1 175  ? 73.671  32.973  84.032  1.00 200.95 ? 175  GLU B O   1 
ATOM   13584 C  CB  . GLU C 1 175  ? 72.108  35.041  86.395  1.00 207.54 ? 175  GLU B CB  1 
ATOM   13585 C  CG  . GLU C 1 175  ? 72.113  34.343  87.785  1.00 212.14 ? 175  GLU B CG  1 
ATOM   13586 C  CD  . GLU C 1 175  ? 71.601  35.243  88.919  1.00 213.95 ? 175  GLU B CD  1 
ATOM   13587 O  OE1 . GLU C 1 175  ? 72.104  36.379  89.068  1.00 215.65 ? 175  GLU B OE1 1 
ATOM   13588 O  OE2 . GLU C 1 175  ? 70.698  34.810  89.669  1.00 211.16 ? 175  GLU B OE2 1 
ATOM   13589 N  N   . GLU C 1 176  ? 73.696  35.214  83.955  1.00 165.53 ? 176  GLU B N   1 
ATOM   13590 C  CA  . GLU C 1 176  ? 75.088  35.291  83.508  1.00 170.32 ? 176  GLU B CA  1 
ATOM   13591 C  C   . GLU C 1 176  ? 75.496  36.730  83.260  1.00 177.57 ? 176  GLU B C   1 
ATOM   13592 O  O   . GLU C 1 176  ? 74.735  37.643  83.562  1.00 176.19 ? 176  GLU B O   1 
ATOM   13593 C  CB  . GLU C 1 176  ? 75.354  34.403  82.284  1.00 167.07 ? 176  GLU B CB  1 
ATOM   13594 C  CG  . GLU C 1 176  ? 76.780  33.802  82.212  1.00 186.61 ? 176  GLU B CG  1 
ATOM   13595 C  CD  . GLU C 1 176  ? 76.834  32.281  82.476  1.00 199.56 ? 176  GLU B CD  1 
ATOM   13596 O  OE1 . GLU C 1 176  ? 76.022  31.773  83.279  1.00 199.34 ? 176  GLU B OE1 1 
ATOM   13597 O  OE2 . GLU C 1 176  ? 77.701  31.588  81.892  1.00 198.90 ? 176  GLU B OE2 1 
ATOM   13598 N  N   . ILE C 1 177  ? 76.702  36.925  82.732  1.00 215.15 ? 177  ILE B N   1 
ATOM   13599 C  CA  . ILE C 1 177  ? 77.239  38.265  82.474  1.00 222.05 ? 177  ILE B CA  1 
ATOM   13600 C  C   . ILE C 1 177  ? 77.146  38.682  81.004  1.00 224.48 ? 177  ILE B C   1 
ATOM   13601 O  O   . ILE C 1 177  ? 77.481  37.913  80.100  1.00 221.85 ? 177  ILE B O   1 
ATOM   13602 C  CB  . ILE C 1 177  ? 78.714  38.378  82.929  1.00 228.29 ? 177  ILE B CB  1 
ATOM   13603 C  CG1 . ILE C 1 177  ? 79.684  38.004  81.794  1.00 229.74 ? 177  ILE B CG1 1 
ATOM   13604 C  CG2 . ILE C 1 177  ? 78.948  37.517  84.164  1.00 229.39 ? 177  ILE B CG2 1 
ATOM   13605 C  CD1 . ILE C 1 177  ? 80.189  39.185  80.961  1.00 230.57 ? 177  ILE B CD1 1 
ATOM   13606 N  N   . ASP C 1 178  ? 76.711  39.913  80.763  1.00 248.65 ? 178  ASP B N   1 
ATOM   13607 C  CA  . ASP C 1 178  ? 76.645  40.408  79.400  1.00 252.13 ? 178  ASP B CA  1 
ATOM   13608 C  C   . ASP C 1 178  ? 77.891  41.196  79.024  1.00 259.92 ? 178  ASP B C   1 
ATOM   13609 O  O   . ASP C 1 178  ? 77.981  42.395  79.277  1.00 263.68 ? 178  ASP B O   1 
ATOM   13610 C  CB  . ASP C 1 178  ? 75.402  41.258  79.189  1.00 247.87 ? 178  ASP B CB  1 
ATOM   13611 C  CG  . ASP C 1 178  ? 75.110  41.481  77.736  1.00 241.83 ? 178  ASP B CG  1 
ATOM   13612 O  OD1 . ASP C 1 178  ? 74.024  42.003  77.416  1.00 238.63 ? 178  ASP B OD1 1 
ATOM   13613 O  OD2 . ASP C 1 178  ? 75.973  41.121  76.911  1.00 241.04 ? 178  ASP B OD2 1 
ATOM   13614 N  N   . HIS C 1 179  ? 78.847  40.509  78.411  1.00 259.92 ? 179  HIS B N   1 
ATOM   13615 C  CA  . HIS C 1 179  ? 80.073  41.143  77.944  1.00 266.26 ? 179  HIS B CA  1 
ATOM   13616 C  C   . HIS C 1 179  ? 79.841  41.906  76.624  1.00 264.01 ? 179  HIS B C   1 
ATOM   13617 O  O   . HIS C 1 179  ? 80.350  43.019  76.459  1.00 266.73 ? 179  HIS B O   1 
ATOM   13618 C  CB  . HIS C 1 179  ? 81.177  40.089  77.786  1.00 273.70 ? 179  HIS B CB  1 
ATOM   13619 C  CG  . HIS C 1 179  ? 82.574  40.634  77.883  1.00 286.08 ? 179  HIS B CG  1 
ATOM   13620 N  ND1 . HIS C 1 179  ? 83.398  40.371  78.954  1.00 291.31 ? 179  HIS B ND1 1 
ATOM   13621 C  CD2 . HIS C 1 179  ? 83.295  41.402  77.031  1.00 292.32 ? 179  HIS B CD2 1 
ATOM   13622 C  CE1 . HIS C 1 179  ? 84.567  40.961  78.762  1.00 298.41 ? 179  HIS B CE1 1 
ATOM   13623 N  NE2 . HIS C 1 179  ? 84.530  41.593  77.605  1.00 299.05 ? 179  HIS B NE2 1 
ATOM   13624 N  N   . ILE C 1 180  ? 79.074  41.318  75.694  1.00 257.12 ? 180  ILE B N   1 
ATOM   13625 C  CA  . ILE C 1 180  ? 78.789  41.951  74.387  1.00 254.87 ? 180  ILE B CA  1 
ATOM   13626 C  C   . ILE C 1 180  ? 77.301  42.189  74.096  1.00 245.92 ? 180  ILE B C   1 
ATOM   13627 O  O   . ILE C 1 180  ? 76.914  43.267  73.643  1.00 242.17 ? 180  ILE B O   1 
ATOM   13628 C  CB  . ILE C 1 180  ? 79.420  41.177  73.189  1.00 239.23 ? 180  ILE B CB  1 
ATOM   13629 C  CG1 . ILE C 1 180  ? 79.174  39.677  73.305  1.00 234.04 ? 180  ILE B CG1 1 
ATOM   13630 C  CG2 . ILE C 1 180  ? 80.906  41.412  73.119  1.00 245.22 ? 180  ILE B CG2 1 
ATOM   13631 C  CD1 . ILE C 1 180  ? 80.187  38.864  72.537  1.00 233.53 ? 180  ILE B CD1 1 
ATOM   13632 N  N   . GLY C 1 181  ? 76.478  41.176  74.341  1.00 155.30 ? 181  GLY B N   1 
ATOM   13633 C  CA  . GLY C 1 181  ? 75.044  41.279  74.141  1.00 155.14 ? 181  GLY B CA  1 
ATOM   13634 C  C   . GLY C 1 181  ? 74.524  39.907  73.782  1.00 152.69 ? 181  GLY B C   1 
ATOM   13635 O  O   . GLY C 1 181  ? 73.326  39.639  73.781  1.00 152.65 ? 181  GLY B O   1 
ATOM   13636 N  N   . ILE C 1 182  ? 75.459  39.032  73.452  1.00 241.00 ? 182  ILE B N   1 
ATOM   13637 C  CA  . ILE C 1 182  ? 75.136  37.650  73.189  1.00 237.06 ? 182  ILE B CA  1 
ATOM   13638 C  C   . ILE C 1 182  ? 75.369  36.869  74.469  1.00 234.70 ? 182  ILE B C   1 
ATOM   13639 O  O   . ILE C 1 182  ? 76.452  36.324  74.685  1.00 236.58 ? 182  ILE B O   1 
ATOM   13640 C  CB  . ILE C 1 182  ? 76.042  37.089  72.100  1.00 237.40 ? 182  ILE B CB  1 
ATOM   13641 C  CG1 . ILE C 1 182  ? 76.325  38.167  71.046  1.00 239.88 ? 182  ILE B CG1 1 
ATOM   13642 C  CG2 . ILE C 1 182  ? 75.437  35.826  71.494  1.00 233.99 ? 182  ILE B CG2 1 
ATOM   13643 C  CD1 . ILE C 1 182  ? 77.337  37.750  69.987  1.00 242.94 ? 182  ILE B CD1 1 
ATOM   13644 N  N   . ILE C 1 183  ? 74.352  36.826  75.322  1.00 208.77 ? 183  ILE B N   1 
ATOM   13645 C  CA  . ILE C 1 183  ? 74.463  36.154  76.615  1.00 206.17 ? 183  ILE B CA  1 
ATOM   13646 C  C   . ILE C 1 183  ? 74.553  34.642  76.458  1.00 203.69 ? 183  ILE B C   1 
ATOM   13647 O  O   . ILE C 1 183  ? 73.592  34.001  76.050  1.00 200.95 ? 183  ILE B O   1 
ATOM   13648 C  CB  . ILE C 1 183  ? 73.275  36.494  77.529  1.00 202.62 ? 183  ILE B CB  1 
ATOM   13649 C  CG1 . ILE C 1 183  ? 73.245  38.002  77.814  1.00 204.16 ? 183  ILE B CG1 1 
ATOM   13650 C  CG2 . ILE C 1 183  ? 73.381  35.703  78.807  1.00 202.90 ? 183  ILE B CG2 1 
ATOM   13651 C  CD1 . ILE C 1 183  ? 71.952  38.515  78.433  1.00 201.52 ? 183  ILE B CD1 1 
ATOM   13652 N  N   . SER C 1 184  ? 75.704  34.076  76.804  1.00 229.36 ? 184  SER B N   1 
ATOM   13653 C  CA  . SER C 1 184  ? 75.985  32.668  76.542  1.00 226.73 ? 184  SER B CA  1 
ATOM   13654 C  C   . SER C 1 184  ? 75.637  31.781  77.725  1.00 232.80 ? 184  SER B C   1 
ATOM   13655 O  O   . SER C 1 184  ? 76.493  31.496  78.560  1.00 235.54 ? 184  SER B O   1 
ATOM   13656 C  CB  . SER C 1 184  ? 77.468  32.495  76.212  1.00 230.28 ? 184  SER B CB  1 
ATOM   13657 O  OG  . SER C 1 184  ? 77.999  33.675  75.637  1.00 231.00 ? 184  SER B OG  1 
ATOM   13658 N  N   . PHE C 1 185  ? 74.388  31.337  77.789  1.00 192.82 ? 185  PHE B N   1 
ATOM   13659 C  CA  . PHE C 1 185  ? 73.952  30.407  78.821  1.00 190.73 ? 185  PHE B CA  1 
ATOM   13660 C  C   . PHE C 1 185  ? 74.587  29.030  78.635  1.00 189.01 ? 185  PHE B C   1 
ATOM   13661 O  O   . PHE C 1 185  ? 75.374  28.843  77.710  1.00 188.16 ? 185  PHE B O   1 
ATOM   13662 C  CB  . PHE C 1 185  ? 72.436  30.294  78.802  1.00 185.26 ? 185  PHE B CB  1 
ATOM   13663 C  CG  . PHE C 1 185  ? 71.745  31.518  79.276  1.00 184.58 ? 185  PHE B CG  1 
ATOM   13664 C  CD1 . PHE C 1 185  ? 71.141  31.547  80.512  1.00 184.90 ? 185  PHE B CD1 1 
ATOM   13665 C  CD2 . PHE C 1 185  ? 71.712  32.651  78.490  1.00 185.11 ? 185  PHE B CD2 1 
ATOM   13666 C  CE1 . PHE C 1 185  ? 70.509  32.686  80.952  1.00 185.58 ? 185  PHE B CE1 1 
ATOM   13667 C  CE2 . PHE C 1 185  ? 71.066  33.784  78.921  1.00 185.67 ? 185  PHE B CE2 1 
ATOM   13668 C  CZ  . PHE C 1 185  ? 70.464  33.804  80.152  1.00 186.58 ? 185  PHE B CZ  1 
ATOM   13669 N  N   . PRO C 1 186  ? 74.252  28.071  79.519  1.00 137.10 ? 186  PRO B N   1 
ATOM   13670 C  CA  . PRO C 1 186  ? 74.838  26.732  79.570  1.00 136.72 ? 186  PRO B CA  1 
ATOM   13671 C  C   . PRO C 1 186  ? 73.822  25.642  79.272  1.00 135.52 ? 186  PRO B C   1 
ATOM   13672 O  O   . PRO C 1 186  ? 72.745  25.624  79.877  1.00 134.35 ? 186  PRO B O   1 
ATOM   13673 C  CB  . PRO C 1 186  ? 75.261  26.622  81.026  1.00 136.09 ? 186  PRO B CB  1 
ATOM   13674 C  CG  . PRO C 1 186  ? 74.480  27.756  81.764  1.00 135.69 ? 186  PRO B CG  1 
ATOM   13675 C  CD  . PRO C 1 186  ? 73.550  28.356  80.771  1.00 135.92 ? 186  PRO B CD  1 
ATOM   13676 N  N   . ASP C 1 187  ? 74.200  24.727  78.376  1.00 192.90 ? 187  ASP B N   1 
ATOM   13677 C  CA  . ASP C 1 187  ? 73.312  23.679  77.866  1.00 187.74 ? 187  ASP B CA  1 
ATOM   13678 C  C   . ASP C 1 187  ? 72.344  23.190  78.942  1.00 182.50 ? 187  ASP B C   1 
ATOM   13679 O  O   . ASP C 1 187  ? 72.703  23.094  80.109  1.00 181.81 ? 187  ASP B O   1 
ATOM   13680 C  CB  . ASP C 1 187  ? 74.119  22.488  77.304  1.00 191.89 ? 187  ASP B CB  1 
ATOM   13681 C  CG  . ASP C 1 187  ? 74.787  22.788  75.952  1.00 197.29 ? 187  ASP B CG  1 
ATOM   13682 O  OD1 . ASP C 1 187  ? 74.909  23.977  75.579  1.00 199.31 ? 187  ASP B OD1 1 
ATOM   13683 O  OD2 . ASP C 1 187  ? 75.199  21.818  75.266  1.00 198.90 ? 187  ASP B OD2 1 
ATOM   13684 N  N   . PHE C 1 188  ? 71.112  22.902  78.547  1.00 164.90 ? 188  PHE B N   1 
ATOM   13685 C  CA  . PHE C 1 188  ? 70.137  22.315  79.444  1.00 158.01 ? 188  PHE B CA  1 
ATOM   13686 C  C   . PHE C 1 188  ? 69.833  20.945  78.885  1.00 156.40 ? 188  PHE B C   1 
ATOM   13687 O  O   . PHE C 1 188  ? 69.350  20.838  77.770  1.00 154.15 ? 188  PHE B O   1 
ATOM   13688 C  CB  . PHE C 1 188  ? 68.881  23.177  79.469  1.00 152.02 ? 188  PHE B CB  1 
ATOM   13689 C  CG  . PHE C 1 188  ? 67.684  22.519  80.111  1.00 145.69 ? 188  PHE B CG  1 
ATOM   13690 C  CD1 . PHE C 1 188  ? 67.091  21.396  79.550  1.00 143.19 ? 188  PHE B CD1 1 
ATOM   13691 C  CD2 . PHE C 1 188  ? 67.123  23.053  81.251  1.00 147.11 ? 188  PHE B CD2 1 
ATOM   13692 C  CE1 . PHE C 1 188  ? 65.981  20.806  80.132  1.00 139.69 ? 188  PHE B CE1 1 
ATOM   13693 C  CE2 . PHE C 1 188  ? 66.008  22.472  81.825  1.00 144.24 ? 188  PHE B CE2 1 
ATOM   13694 C  CZ  . PHE C 1 188  ? 65.440  21.347  81.265  1.00 140.54 ? 188  PHE B CZ  1 
ATOM   13695 N  N   . LYS C 1 189  ? 70.134  19.900  79.649  1.00 188.81 ? 189  LYS B N   1 
ATOM   13696 C  CA  . LYS C 1 189  ? 69.936  18.534  79.186  1.00 185.17 ? 189  LYS B CA  1 
ATOM   13697 C  C   . LYS C 1 189  ? 68.531  18.043  79.451  1.00 180.88 ? 189  LYS B C   1 
ATOM   13698 O  O   . LYS C 1 189  ? 67.927  18.340  80.481  1.00 179.23 ? 189  LYS B O   1 
ATOM   13699 C  CB  . LYS C 1 189  ? 70.946  17.578  79.825  1.00 191.60 ? 189  LYS B CB  1 
ATOM   13700 C  CG  . LYS C 1 189  ? 70.394  16.180  80.152  1.00 192.46 ? 189  LYS B CG  1 
ATOM   13701 C  CD  . LYS C 1 189  ? 71.120  15.075  79.369  1.00 195.97 ? 189  LYS B CD  1 
ATOM   13702 C  CE  . LYS C 1 189  ? 71.361  13.797  80.203  1.00 198.25 ? 189  LYS B CE  1 
ATOM   13703 N  NZ  . LYS C 1 189  ? 70.133  13.233  80.848  1.00 195.51 ? 189  LYS B NZ  1 
ATOM   13704 N  N   . ILE C 1 190  ? 68.020  17.288  78.494  1.00 188.25 ? 190  ILE B N   1 
ATOM   13705 C  CA  . ILE C 1 190  ? 66.720  16.663  78.614  1.00 185.26 ? 190  ILE B CA  1 
ATOM   13706 C  C   . ILE C 1 190  ? 66.852  15.457  79.535  1.00 189.46 ? 190  ILE B C   1 
ATOM   13707 O  O   . ILE C 1 190  ? 67.864  14.762  79.506  1.00 198.42 ? 190  ILE B O   1 
ATOM   13708 C  CB  . ILE C 1 190  ? 66.218  16.215  77.235  1.00 180.17 ? 190  ILE B CB  1 
ATOM   13709 C  CG1 . ILE C 1 190  ? 66.415  17.344  76.236  1.00 173.20 ? 190  ILE B CG1 1 
ATOM   13710 C  CG2 . ILE C 1 190  ? 64.765  15.800  77.298  1.00 169.34 ? 190  ILE B CG2 1 
ATOM   13711 C  CD1 . ILE C 1 190  ? 65.982  18.691  76.774  1.00 170.92 ? 190  ILE B CD1 1 
ATOM   13712 N  N   . PRO C 1 191  ? 65.835  15.212  80.369  1.00 194.78 ? 191  PRO B N   1 
ATOM   13713 C  CA  . PRO C 1 191  ? 65.832  14.044  81.254  1.00 193.99 ? 191  PRO B CA  1 
ATOM   13714 C  C   . PRO C 1 191  ? 65.936  12.741  80.480  1.00 198.62 ? 191  PRO B C   1 
ATOM   13715 O  O   . PRO C 1 191  ? 65.441  12.639  79.353  1.00 194.93 ? 191  PRO B O   1 
ATOM   13716 C  CB  . PRO C 1 191  ? 64.459  14.111  81.922  1.00 189.45 ? 191  PRO B CB  1 
ATOM   13717 C  CG  . PRO C 1 191  ? 64.087  15.535  81.872  1.00 188.08 ? 191  PRO B CG  1 
ATOM   13718 C  CD  . PRO C 1 191  ? 64.687  16.096  80.616  1.00 189.35 ? 191  PRO B CD  1 
ATOM   13719 N  N   . SER C 1 192  ? 66.571  11.749  81.090  1.00 178.97 ? 192  SER B N   1 
ATOM   13720 C  CA  . SER C 1 192  ? 66.666  10.422  80.498  1.00 178.14 ? 192  SER B CA  1 
ATOM   13721 C  C   . SER C 1 192  ? 65.260  9.983   80.123  1.00 167.67 ? 192  SER B C   1 
ATOM   13722 O  O   . SER C 1 192  ? 65.053  9.192   79.211  1.00 163.54 ? 192  SER B O   1 
ATOM   13723 C  CB  . SER C 1 192  ? 67.264  9.440   81.512  1.00 182.97 ? 192  SER B CB  1 
ATOM   13724 O  OG  . SER C 1 192  ? 68.255  10.060  82.333  1.00 187.72 ? 192  SER B OG  1 
ATOM   13725 N  N   . ASN C 1 193  ? 64.304  10.538  80.855  1.00 147.84 ? 193  ASN B N   1 
ATOM   13726 C  CA  . ASN C 1 193  ? 62.885  10.331  80.649  1.00 146.15 ? 193  ASN B CA  1 
ATOM   13727 C  C   . ASN C 1 193  ? 62.158  11.527  81.294  1.00 144.86 ? 193  ASN B C   1 
ATOM   13728 O  O   . ASN C 1 193  ? 62.005  11.562  82.516  1.00 146.28 ? 193  ASN B O   1 
ATOM   13729 C  CB  . ASN C 1 193  ? 62.465  8.994   81.264  1.00 147.20 ? 193  ASN B CB  1 
ATOM   13730 C  CG  . ASN C 1 193  ? 60.964  8.829   81.334  1.00 145.07 ? 193  ASN B CG  1 
ATOM   13731 O  OD1 . ASN C 1 193  ? 60.216  9.671   80.844  1.00 142.34 ? 193  ASN B OD1 1 
ATOM   13732 N  ND2 . ASN C 1 193  ? 60.514  7.743   81.950  1.00 145.84 ? 193  ASN B ND2 1 
ATOM   13733 N  N   . PRO C 1 194  ? 61.771  12.538  80.471  1.00 168.91 ? 194  PRO B N   1 
ATOM   13734 C  CA  . PRO C 1 194  ? 61.084  13.789  80.865  1.00 165.55 ? 194  PRO B CA  1 
ATOM   13735 C  C   . PRO C 1 194  ? 59.552  13.831  80.692  1.00 159.69 ? 194  PRO B C   1 
ATOM   13736 O  O   . PRO C 1 194  ? 58.962  12.897  80.162  1.00 156.84 ? 194  PRO B O   1 
ATOM   13737 C  CB  . PRO C 1 194  ? 61.685  14.833  79.915  1.00 167.82 ? 194  PRO B CB  1 
ATOM   13738 C  CG  . PRO C 1 194  ? 62.612  14.088  78.975  1.00 171.96 ? 194  PRO B CG  1 
ATOM   13739 C  CD  . PRO C 1 194  ? 62.287  12.633  79.093  1.00 170.62 ? 194  PRO B CD  1 
ATOM   13740 N  N   . ARG C 1 195  ? 58.929  14.928  81.121  1.00 186.48 ? 195  ARG B N   1 
ATOM   13741 C  CA  . ARG C 1 195  ? 57.502  15.150  80.884  1.00 185.74 ? 195  ARG B CA  1 
ATOM   13742 C  C   . ARG C 1 195  ? 57.236  15.609  79.453  1.00 185.14 ? 195  ARG B C   1 
ATOM   13743 O  O   . ARG C 1 195  ? 57.792  16.612  78.997  1.00 186.58 ? 195  ARG B O   1 
ATOM   13744 C  CB  . ARG C 1 195  ? 56.933  16.177  81.864  1.00 188.61 ? 195  ARG B CB  1 
ATOM   13745 C  CG  . ARG C 1 195  ? 56.608  15.630  83.253  1.00 190.18 ? 195  ARG B CG  1 
ATOM   13746 C  CD  . ARG C 1 195  ? 57.475  16.276  84.346  1.00 197.16 ? 195  ARG B CD  1 
ATOM   13747 N  NE  . ARG C 1 195  ? 56.711  17.118  85.265  1.00 200.56 ? 195  ARG B NE  1 
ATOM   13748 C  CZ  . ARG C 1 195  ? 55.693  16.689  86.007  1.00 200.94 ? 195  ARG B CZ  1 
ATOM   13749 N  NH1 . ARG C 1 195  ? 55.302  15.423  85.944  1.00 198.90 ? 195  ARG B NH1 1 
ATOM   13750 N  NH2 . ARG C 1 195  ? 55.055  17.527  86.812  1.00 202.66 ? 195  ARG B NH2 1 
ATOM   13751 N  N   . TYR C 1 196  ? 56.370  14.884  78.751  1.00 186.15 ? 196  TYR B N   1 
ATOM   13752 C  CA  . TYR C 1 196  ? 56.192  15.101  77.313  1.00 182.23 ? 196  TYR B CA  1 
ATOM   13753 C  C   . TYR C 1 196  ? 55.243  16.232  76.906  1.00 177.20 ? 196  TYR B C   1 
ATOM   13754 O  O   . TYR C 1 196  ? 54.064  16.240  77.245  1.00 173.84 ? 196  TYR B O   1 
ATOM   13755 C  CB  . TYR C 1 196  ? 55.867  13.772  76.597  1.00 184.56 ? 196  TYR B CB  1 
ATOM   13756 C  CG  . TYR C 1 196  ? 57.070  12.834  76.557  1.00 187.89 ? 196  TYR B CG  1 
ATOM   13757 C  CD1 . TYR C 1 196  ? 58.247  13.225  75.920  1.00 189.33 ? 196  TYR B CD1 1 
ATOM   13758 C  CD2 . TYR C 1 196  ? 57.045  11.579  77.168  1.00 187.87 ? 196  TYR B CD2 1 
ATOM   13759 C  CE1 . TYR C 1 196  ? 59.367  12.402  75.883  1.00 192.20 ? 196  TYR B CE1 1 
ATOM   13760 C  CE2 . TYR C 1 196  ? 58.170  10.740  77.133  1.00 189.84 ? 196  TYR B CE2 1 
ATOM   13761 C  CZ  . TYR C 1 196  ? 59.327  11.169  76.486  1.00 191.63 ? 196  TYR B CZ  1 
ATOM   13762 O  OH  . TYR C 1 196  ? 60.462  10.393  76.416  1.00 193.35 ? 196  TYR B OH  1 
ATOM   13763 N  N   . GLY C 1 197  ? 55.773  17.193  76.171  1.00 192.28 ? 197  GLY B N   1 
ATOM   13764 C  CA  . GLY C 1 197  ? 54.921  18.229  75.655  1.00 192.35 ? 197  GLY B CA  1 
ATOM   13765 C  C   . GLY C 1 197  ? 55.653  19.500  75.325  1.00 193.51 ? 197  GLY B C   1 
ATOM   13766 O  O   . GLY C 1 197  ? 56.712  19.488  74.700  1.00 197.41 ? 197  GLY B O   1 
ATOM   13767 N  N   . MET C 1 198  ? 55.073  20.608  75.765  1.00 143.08 ? 198  MET B N   1 
ATOM   13768 C  CA  . MET C 1 198  ? 55.514  21.926  75.358  1.00 144.86 ? 198  MET B CA  1 
ATOM   13769 C  C   . MET C 1 198  ? 56.273  22.699  76.454  1.00 142.37 ? 198  MET B C   1 
ATOM   13770 O  O   . MET C 1 198  ? 55.685  23.169  77.427  1.00 144.61 ? 198  MET B O   1 
ATOM   13771 C  CB  . MET C 1 198  ? 54.297  22.712  74.886  1.00 147.55 ? 198  MET B CB  1 
ATOM   13772 C  CG  . MET C 1 198  ? 54.660  24.041  74.313  1.00 173.74 ? 198  MET B CG  1 
ATOM   13773 S  SD  . MET C 1 198  ? 56.167  23.844  73.357  1.00 189.68 ? 198  MET B SD  1 
ATOM   13774 C  CE  . MET C 1 198  ? 55.527  23.005  71.915  1.00 149.99 ? 198  MET B CE  1 
ATOM   13775 N  N   . TRP C 1 199  ? 57.578  22.856  76.276  1.00 162.22 ? 199  TRP B N   1 
ATOM   13776 C  CA  . TRP C 1 199  ? 58.406  23.559  77.253  1.00 165.16 ? 199  TRP B CA  1 
ATOM   13777 C  C   . TRP C 1 199  ? 58.414  25.075  77.080  1.00 167.22 ? 199  TRP B C   1 
ATOM   13778 O  O   . TRP C 1 199  ? 58.245  25.562  75.977  1.00 169.62 ? 199  TRP B O   1 
ATOM   13779 C  CB  . TRP C 1 199  ? 59.819  23.033  77.151  1.00 170.33 ? 199  TRP B CB  1 
ATOM   13780 C  CG  . TRP C 1 199  ? 59.985  21.734  77.852  1.00 173.72 ? 199  TRP B CG  1 
ATOM   13781 C  CD1 . TRP C 1 199  ? 59.483  20.517  77.490  1.00 173.74 ? 199  TRP B CD1 1 
ATOM   13782 C  CD2 . TRP C 1 199  ? 60.711  21.526  79.059  1.00 176.68 ? 199  TRP B CD2 1 
ATOM   13783 N  NE1 . TRP C 1 199  ? 59.863  19.560  78.405  1.00 176.51 ? 199  TRP B NE1 1 
ATOM   13784 C  CE2 . TRP C 1 199  ? 60.621  20.162  79.374  1.00 177.26 ? 199  TRP B CE2 1 
ATOM   13785 C  CE3 . TRP C 1 199  ? 61.440  22.372  79.907  1.00 179.20 ? 199  TRP B CE3 1 
ATOM   13786 C  CZ2 . TRP C 1 199  ? 61.228  19.627  80.497  1.00 177.04 ? 199  TRP B CZ2 1 
ATOM   13787 C  CZ3 . TRP C 1 199  ? 62.045  21.839  81.018  1.00 180.01 ? 199  TRP B CZ3 1 
ATOM   13788 C  CH2 . TRP C 1 199  ? 61.935  20.480  81.306  1.00 179.67 ? 199  TRP B CH2 1 
ATOM   13789 N  N   . THR C 1 200  ? 58.631  25.823  78.155  1.00 135.93 ? 200  THR B N   1 
ATOM   13790 C  CA  . THR C 1 200  ? 58.633  27.275  78.058  1.00 132.85 ? 200  THR B CA  1 
ATOM   13791 C  C   . THR C 1 200  ? 59.898  27.902  78.655  1.00 137.35 ? 200  THR B C   1 
ATOM   13792 O  O   . THR C 1 200  ? 60.090  27.840  79.847  1.00 140.04 ? 200  THR B O   1 
ATOM   13793 C  CB  . THR C 1 200  ? 57.397  27.865  78.788  1.00 130.81 ? 200  THR B CB  1 
ATOM   13794 O  OG1 . THR C 1 200  ? 56.258  27.018  78.592  1.00 134.19 ? 200  THR B OG1 1 
ATOM   13795 C  CG2 . THR C 1 200  ? 57.084  29.240  78.275  1.00 131.77 ? 200  THR B CG2 1 
ATOM   13796 N  N   . ILE C 1 201  ? 60.767  28.503  77.854  1.00 149.40 ? 201  ILE B N   1 
ATOM   13797 C  CA  . ILE C 1 201  ? 61.854  29.295  78.429  1.00 148.27 ? 201  ILE B CA  1 
ATOM   13798 C  C   . ILE C 1 201  ? 61.462  30.773  78.477  1.00 151.61 ? 201  ILE B C   1 
ATOM   13799 O  O   . ILE C 1 201  ? 61.149  31.358  77.432  1.00 157.26 ? 201  ILE B O   1 
ATOM   13800 C  CB  . ILE C 1 201  ? 63.177  29.173  77.637  1.00 156.82 ? 201  ILE B CB  1 
ATOM   13801 C  CG1 . ILE C 1 201  ? 63.579  27.726  77.472  1.00 156.41 ? 201  ILE B CG1 1 
ATOM   13802 C  CG2 . ILE C 1 201  ? 64.322  29.896  78.348  1.00 158.03 ? 201  ILE B CG2 1 
ATOM   13803 C  CD1 . ILE C 1 201  ? 64.998  27.598  76.989  1.00 154.82 ? 201  ILE B CD1 1 
ATOM   13804 N  N   . LYS C 1 202  ? 61.461  31.358  79.685  1.00 168.45 ? 202  LYS B N   1 
ATOM   13805 C  CA  . LYS C 1 202  ? 61.301  32.807  79.913  1.00 168.84 ? 202  LYS B CA  1 
ATOM   13806 C  C   . LYS C 1 202  ? 62.592  33.462  80.398  1.00 172.44 ? 202  LYS B C   1 
ATOM   13807 O  O   . LYS C 1 202  ? 63.454  32.803  80.962  1.00 173.62 ? 202  LYS B O   1 
ATOM   13808 C  CB  . LYS C 1 202  ? 60.202  33.076  80.932  1.00 172.88 ? 202  LYS B CB  1 
ATOM   13809 C  CG  . LYS C 1 202  ? 58.889  32.521  80.526  1.00 172.91 ? 202  LYS B CG  1 
ATOM   13810 C  CD  . LYS C 1 202  ? 57.825  32.971  81.460  1.00 176.36 ? 202  LYS B CD  1 
ATOM   13811 C  CE  . LYS C 1 202  ? 56.570  32.191  81.207  1.00 175.26 ? 202  LYS B CE  1 
ATOM   13812 N  NZ  . LYS C 1 202  ? 55.551  32.515  82.227  1.00 176.43 ? 202  LYS B NZ  1 
ATOM   13813 N  N   . ALA C 1 203  ? 62.719  34.767  80.206  1.00 141.70 ? 203  ALA B N   1 
ATOM   13814 C  CA  . ALA C 1 203  ? 63.951  35.435  80.582  1.00 143.69 ? 203  ALA B CA  1 
ATOM   13815 C  C   . ALA C 1 203  ? 63.663  36.836  81.055  1.00 147.79 ? 203  ALA B C   1 
ATOM   13816 O  O   . ALA C 1 203  ? 62.834  37.537  80.456  1.00 145.31 ? 203  ALA B O   1 
ATOM   13817 C  CB  . ALA C 1 203  ? 64.915  35.464  79.423  1.00 146.17 ? 203  ALA B CB  1 
ATOM   13818 N  N   . LYS C 1 204  ? 64.384  37.234  82.113  1.00 173.62 ? 204  LYS B N   1 
ATOM   13819 C  CA  . LYS C 1 204  ? 64.281  38.560  82.747  1.00 179.18 ? 204  LYS B CA  1 
ATOM   13820 C  C   . LYS C 1 204  ? 65.626  39.140  83.177  1.00 182.60 ? 204  LYS B C   1 
ATOM   13821 O  O   . LYS C 1 204  ? 66.546  38.410  83.534  1.00 182.36 ? 204  LYS B O   1 
ATOM   13822 C  CB  . LYS C 1 204  ? 63.398  38.489  83.985  1.00 181.63 ? 204  LYS B CB  1 
ATOM   13823 C  CG  . LYS C 1 204  ? 63.828  37.416  84.955  1.00 188.14 ? 204  LYS B CG  1 
ATOM   13824 C  CD  . LYS C 1 204  ? 62.717  37.130  85.938  1.00 190.42 ? 204  LYS B CD  1 
ATOM   13825 C  CE  . LYS C 1 204  ? 62.858  35.761  86.569  1.00 192.25 ? 204  LYS B CE  1 
ATOM   13826 N  NZ  . LYS C 1 204  ? 61.918  35.632  87.706  1.00 193.51 ? 204  LYS B NZ  1 
ATOM   13827 N  N   . TYR C 1 205  ? 65.725  40.461  83.153  1.00 198.57 ? 205  TYR B N   1 
ATOM   13828 C  CA  . TYR C 1 205  ? 66.915  41.117  83.655  1.00 210.01 ? 205  TYR B CA  1 
ATOM   13829 C  C   . TYR C 1 205  ? 67.030  40.908  85.151  1.00 219.32 ? 205  TYR B C   1 
ATOM   13830 O  O   . TYR C 1 205  ? 66.040  41.044  85.873  1.00 221.17 ? 205  TYR B O   1 
ATOM   13831 C  CB  . TYR C 1 205  ? 66.883  42.605  83.338  1.00 211.90 ? 205  TYR B CB  1 
ATOM   13832 C  CG  . TYR C 1 205  ? 67.306  42.861  81.937  1.00 212.99 ? 205  TYR B CG  1 
ATOM   13833 C  CD1 . TYR C 1 205  ? 66.425  43.387  81.007  1.00 210.19 ? 205  TYR B CD1 1 
ATOM   13834 C  CD2 . TYR C 1 205  ? 68.581  42.525  81.526  1.00 217.40 ? 205  TYR B CD2 1 
ATOM   13835 C  CE1 . TYR C 1 205  ? 66.816  43.597  79.705  1.00 210.79 ? 205  TYR B CE1 1 
ATOM   13836 C  CE2 . TYR C 1 205  ? 68.983  42.726  80.231  1.00 217.73 ? 205  TYR B CE2 1 
ATOM   13837 C  CZ  . TYR C 1 205  ? 68.100  43.263  79.320  1.00 214.49 ? 205  TYR B CZ  1 
ATOM   13838 O  OH  . TYR C 1 205  ? 68.516  43.459  78.020  1.00 214.54 ? 205  TYR B OH  1 
ATOM   13839 N  N   . LYS C 1 206  ? 68.234  40.581  85.618  1.00 198.72 ? 206  LYS B N   1 
ATOM   13840 C  CA  . LYS C 1 206  ? 68.457  40.370  87.046  1.00 202.56 ? 206  LYS B CA  1 
ATOM   13841 C  C   . LYS C 1 206  ? 67.971  41.610  87.761  1.00 206.01 ? 206  LYS B C   1 
ATOM   13842 O  O   . LYS C 1 206  ? 66.940  41.596  88.439  1.00 203.47 ? 206  LYS B O   1 
ATOM   13843 C  CB  . LYS C 1 206  ? 69.943  40.147  87.341  1.00 209.08 ? 206  LYS B CB  1 
ATOM   13844 C  CG  . LYS C 1 206  ? 70.217  39.551  88.710  1.00 212.90 ? 206  LYS B CG  1 
ATOM   13845 C  CD  . LYS C 1 206  ? 71.662  39.107  88.830  1.00 217.67 ? 206  LYS B CD  1 
ATOM   13846 C  CE  . LYS C 1 206  ? 72.623  40.271  88.668  1.00 223.33 ? 206  LYS B CE  1 
ATOM   13847 N  NZ  . LYS C 1 206  ? 73.957  39.971  89.269  1.00 227.53 ? 206  LYS B NZ  1 
ATOM   13848 N  N   . GLU C 1 207  ? 68.713  42.690  87.544  1.00 200.46 ? 207  GLU B N   1 
ATOM   13849 C  CA  . GLU C 1 207  ? 68.448  43.988  88.142  1.00 204.03 ? 207  GLU B CA  1 
ATOM   13850 C  C   . GLU C 1 207  ? 67.052  44.520  87.842  1.00 197.21 ? 207  GLU B C   1 
ATOM   13851 O  O   . GLU C 1 207  ? 66.120  43.759  87.586  1.00 190.57 ? 207  GLU B O   1 
ATOM   13852 C  CB  . GLU C 1 207  ? 69.508  44.999  87.690  1.00 212.99 ? 207  GLU B CB  1 
ATOM   13853 C  CG  . GLU C 1 207  ? 70.941  44.638  88.102  1.00 219.41 ? 207  GLU B CG  1 
ATOM   13854 C  CD  . GLU C 1 207  ? 71.164  44.672  89.611  1.00 223.42 ? 207  GLU B CD  1 
ATOM   13855 O  OE1 . GLU C 1 207  ? 70.197  44.936  90.359  1.00 222.37 ? 207  GLU B OE1 1 
ATOM   13856 O  OE2 . GLU C 1 207  ? 72.312  44.436  90.049  1.00 227.89 ? 207  GLU B OE2 1 
ATOM   13857 N  N   . ASP C 1 208  ? 66.913  45.837  87.911  1.00 222.03 ? 208  ASP B N   1 
ATOM   13858 C  CA  . ASP C 1 208  ? 65.640  46.484  87.658  1.00 213.80 ? 208  ASP B CA  1 
ATOM   13859 C  C   . ASP C 1 208  ? 65.364  46.458  86.174  1.00 207.47 ? 208  ASP B C   1 
ATOM   13860 O  O   . ASP C 1 208  ? 66.280  46.244  85.381  1.00 209.78 ? 208  ASP B O   1 
ATOM   13861 C  CB  . ASP C 1 208  ? 65.704  47.921  88.122  1.00 214.57 ? 208  ASP B CB  1 
ATOM   13862 C  CG  . ASP C 1 208  ? 66.909  48.635  87.575  1.00 217.08 ? 208  ASP B CG  1 
ATOM   13863 O  OD1 . ASP C 1 208  ? 67.143  48.548  86.350  1.00 213.45 ? 208  ASP B OD1 1 
ATOM   13864 O  OD2 . ASP C 1 208  ? 67.630  49.263  88.376  1.00 222.80 ? 208  ASP B OD2 1 
ATOM   13865 N  N   . PHE C 1 209  ? 64.107  46.726  85.824  1.00 196.43 ? 209  PHE B N   1 
ATOM   13866 C  CA  . PHE C 1 209  ? 63.558  46.540  84.482  1.00 189.89 ? 209  PHE B CA  1 
ATOM   13867 C  C   . PHE C 1 209  ? 62.550  45.376  84.448  1.00 184.25 ? 209  PHE B C   1 
ATOM   13868 O  O   . PHE C 1 209  ? 62.887  44.228  84.763  1.00 184.31 ? 209  PHE B O   1 
ATOM   13869 C  CB  . PHE C 1 209  ? 64.654  46.288  83.447  1.00 187.98 ? 209  PHE B CB  1 
ATOM   13870 C  CG  . PHE C 1 209  ? 65.470  47.496  83.106  1.00 189.91 ? 209  PHE B CG  1 
ATOM   13871 C  CD1 . PHE C 1 209  ? 66.815  47.365  82.801  1.00 192.49 ? 209  PHE B CD1 1 
ATOM   13872 C  CD2 . PHE C 1 209  ? 64.898  48.755  83.078  1.00 187.67 ? 209  PHE B CD2 1 
ATOM   13873 C  CE1 . PHE C 1 209  ? 67.575  48.464  82.475  1.00 194.71 ? 209  PHE B CE1 1 
ATOM   13874 C  CE2 . PHE C 1 209  ? 65.653  49.865  82.751  1.00 192.28 ? 209  PHE B CE2 1 
ATOM   13875 C  CZ  . PHE C 1 209  ? 66.995  49.720  82.447  1.00 195.17 ? 209  PHE B CZ  1 
ATOM   13876 N  N   . SER C 1 210  ? 61.318  45.683  84.048  1.00 207.77 ? 210  SER B N   1 
ATOM   13877 C  CA  . SER C 1 210  ? 60.245  44.690  83.937  1.00 202.22 ? 210  SER B CA  1 
ATOM   13878 C  C   . SER C 1 210  ? 60.421  43.709  82.761  1.00 198.28 ? 210  SER B C   1 
ATOM   13879 O  O   . SER C 1 210  ? 59.750  42.676  82.712  1.00 192.12 ? 210  SER B O   1 
ATOM   13880 C  CB  . SER C 1 210  ? 58.896  45.408  83.793  1.00 200.40 ? 210  SER B CB  1 
ATOM   13881 O  OG  . SER C 1 210  ? 57.827  44.483  83.744  1.00 196.06 ? 210  SER B OG  1 
ATOM   13882 N  N   . THR C 1 211  ? 61.333  44.033  81.837  1.00 172.70 ? 211  THR B N   1 
ATOM   13883 C  CA  . THR C 1 211  ? 61.360  43.455  80.480  1.00 170.79 ? 211  THR B CA  1 
ATOM   13884 C  C   . THR C 1 211  ? 61.293  41.930  80.361  1.00 167.10 ? 211  THR B C   1 
ATOM   13885 O  O   . THR C 1 211  ? 62.083  41.208  80.946  1.00 167.53 ? 211  THR B O   1 
ATOM   13886 C  CB  . THR C 1 211  ? 62.529  44.014  79.614  1.00 175.59 ? 211  THR B CB  1 
ATOM   13887 O  OG1 . THR C 1 211  ? 63.747  44.042  80.370  1.00 180.98 ? 211  THR B OG1 1 
ATOM   13888 C  CG2 . THR C 1 211  ? 62.205  45.422  79.124  1.00 175.88 ? 211  THR B CG2 1 
ATOM   13889 N  N   . THR C 1 212  ? 60.347  41.469  79.556  1.00 149.53 ? 212  THR B N   1 
ATOM   13890 C  CA  . THR C 1 212  ? 60.032  40.058  79.391  1.00 147.01 ? 212  THR B CA  1 
ATOM   13891 C  C   . THR C 1 212  ? 60.694  39.380  78.172  1.00 148.79 ? 212  THR B C   1 
ATOM   13892 O  O   . THR C 1 212  ? 60.452  39.751  77.011  1.00 151.68 ? 212  THR B O   1 
ATOM   13893 C  CB  . THR C 1 212  ? 58.504  39.919  79.218  1.00 142.64 ? 212  THR B CB  1 
ATOM   13894 O  OG1 . THR C 1 212  ? 57.848  40.977  79.929  1.00 144.08 ? 212  THR B OG1 1 
ATOM   13895 C  CG2 . THR C 1 212  ? 58.008  38.566  79.699  1.00 139.26 ? 212  THR B CG2 1 
ATOM   13896 N  N   . GLY C 1 213  ? 61.504  38.363  78.424  1.00 242.81 ? 213  GLY B N   1 
ATOM   13897 C  CA  . GLY C 1 213  ? 61.881  37.460  77.356  1.00 241.64 ? 213  GLY B CA  1 
ATOM   13898 C  C   . GLY C 1 213  ? 61.035  36.194  77.399  1.00 237.05 ? 213  GLY B C   1 
ATOM   13899 O  O   . GLY C 1 213  ? 60.954  35.561  78.450  1.00 237.12 ? 213  GLY B O   1 
ATOM   13900 N  N   . THR C 1 214  ? 60.387  35.824  76.291  1.00 179.13 ? 214  THR B N   1 
ATOM   13901 C  CA  . THR C 1 214  ? 59.742  34.504  76.211  1.00 173.86 ? 214  THR B CA  1 
ATOM   13902 C  C   . THR C 1 214  ? 60.301  33.721  75.038  1.00 169.19 ? 214  THR B C   1 
ATOM   13903 O  O   . THR C 1 214  ? 60.924  34.295  74.151  1.00 170.38 ? 214  THR B O   1 
ATOM   13904 C  CB  . THR C 1 214  ? 58.202  34.564  76.084  1.00 172.97 ? 214  THR B CB  1 
ATOM   13905 O  OG1 . THR C 1 214  ? 57.651  35.246  77.213  1.00 173.68 ? 214  THR B OG1 1 
ATOM   13906 C  CG2 . THR C 1 214  ? 57.608  33.156  76.036  1.00 167.81 ? 214  THR B CG2 1 
ATOM   13907 N  N   . ALA C 1 215  ? 60.089  32.409  75.054  1.00 167.35 ? 215  ALA B N   1 
ATOM   13908 C  CA  . ALA C 1 215  ? 60.497  31.524  73.971  1.00 164.68 ? 215  ALA B CA  1 
ATOM   13909 C  C   . ALA C 1 215  ? 59.844  30.190  74.251  1.00 161.28 ? 215  ALA B C   1 
ATOM   13910 O  O   . ALA C 1 215  ? 59.248  30.035  75.317  1.00 158.33 ? 215  ALA B O   1 
ATOM   13911 C  CB  . ALA C 1 215  ? 61.995  31.384  73.939  1.00 166.36 ? 215  ALA B CB  1 
ATOM   13912 N  N   . TYR C 1 216  ? 59.938  29.240  73.312  1.00 172.38 ? 216  TYR B N   1 
ATOM   13913 C  CA  . TYR C 1 216  ? 59.437  27.878  73.537  1.00 167.44 ? 216  TYR B CA  1 
ATOM   13914 C  C   . TYR C 1 216  ? 60.281  26.806  72.915  1.00 168.58 ? 216  TYR B C   1 
ATOM   13915 O  O   . TYR C 1 216  ? 61.215  27.068  72.155  1.00 174.99 ? 216  TYR B O   1 
ATOM   13916 C  CB  . TYR C 1 216  ? 58.023  27.679  73.006  1.00 168.59 ? 216  TYR B CB  1 
ATOM   13917 C  CG  . TYR C 1 216  ? 57.043  28.642  73.562  1.00 172.17 ? 216  TYR B CG  1 
ATOM   13918 C  CD1 . TYR C 1 216  ? 55.979  28.217  74.330  1.00 172.94 ? 216  TYR B CD1 1 
ATOM   13919 C  CD2 . TYR C 1 216  ? 57.182  29.994  73.316  1.00 178.97 ? 216  TYR B CD2 1 
ATOM   13920 C  CE1 . TYR C 1 216  ? 55.078  29.123  74.844  1.00 174.71 ? 216  TYR B CE1 1 
ATOM   13921 C  CE2 . TYR C 1 216  ? 56.302  30.908  73.823  1.00 180.96 ? 216  TYR B CE2 1 
ATOM   13922 C  CZ  . TYR C 1 216  ? 55.247  30.475  74.589  1.00 179.00 ? 216  TYR B CZ  1 
ATOM   13923 O  OH  . TYR C 1 216  ? 54.367  31.409  75.089  1.00 180.30 ? 216  TYR B OH  1 
ATOM   13924 N  N   . PHE C 1 217  ? 59.908  25.583  73.260  1.00 158.02 ? 217  PHE B N   1 
ATOM   13925 C  CA  . PHE C 1 217  ? 60.497  24.390  72.688  1.00 156.22 ? 217  PHE B CA  1 
ATOM   13926 C  C   . PHE C 1 217  ? 59.815  23.102  73.168  1.00 155.79 ? 217  PHE B C   1 
ATOM   13927 O  O   . PHE C 1 217  ? 59.558  22.931  74.353  1.00 155.71 ? 217  PHE B O   1 
ATOM   13928 C  CB  . PHE C 1 217  ? 62.009  24.370  72.913  1.00 158.10 ? 217  PHE B CB  1 
ATOM   13929 C  CG  . PHE C 1 217  ? 62.436  23.743  74.209  1.00 158.86 ? 217  PHE B CG  1 
ATOM   13930 C  CD1 . PHE C 1 217  ? 62.715  22.389  74.270  1.00 157.53 ? 217  PHE B CD1 1 
ATOM   13931 C  CD2 . PHE C 1 217  ? 62.605  24.504  75.349  1.00 160.53 ? 217  PHE B CD2 1 
ATOM   13932 C  CE1 . PHE C 1 217  ? 63.132  21.797  75.441  1.00 163.44 ? 217  PHE B CE1 1 
ATOM   13933 C  CE2 . PHE C 1 217  ? 63.017  23.915  76.512  1.00 155.93 ? 217  PHE B CE2 1 
ATOM   13934 C  CZ  . PHE C 1 217  ? 63.282  22.556  76.558  1.00 157.04 ? 217  PHE B CZ  1 
ATOM   13935 N  N   . GLU C 1 218  ? 59.531  22.212  72.224  1.00 196.68 ? 218  GLU B N   1 
ATOM   13936 C  CA  . GLU C 1 218  ? 58.726  21.028  72.458  1.00 198.31 ? 218  GLU B CA  1 
ATOM   13937 C  C   . GLU C 1 218  ? 59.625  19.827  72.678  1.00 197.92 ? 218  GLU B C   1 
ATOM   13938 O  O   . GLU C 1 218  ? 60.658  19.680  72.022  1.00 199.12 ? 218  GLU B O   1 
ATOM   13939 C  CB  . GLU C 1 218  ? 57.855  20.788  71.223  1.00 204.76 ? 218  GLU B CB  1 
ATOM   13940 C  CG  . GLU C 1 218  ? 56.588  19.958  71.425  1.00 209.49 ? 218  GLU B CG  1 
ATOM   13941 C  CD  . GLU C 1 218  ? 55.643  20.034  70.216  1.00 214.68 ? 218  GLU B CD  1 
ATOM   13942 O  OE1 . GLU C 1 218  ? 54.710  19.205  70.112  1.00 215.35 ? 218  GLU B OE1 1 
ATOM   13943 O  OE2 . GLU C 1 218  ? 55.834  20.924  69.362  1.00 218.19 ? 218  GLU B OE2 1 
ATOM   13944 N  N   . VAL C 1 219  ? 59.236  18.969  73.608  1.00 148.58 ? 219  VAL B N   1 
ATOM   13945 C  CA  . VAL C 1 219  ? 59.922  17.708  73.786  1.00 148.54 ? 219  VAL B CA  1 
ATOM   13946 C  C   . VAL C 1 219  ? 58.996  16.608  73.386  1.00 146.38 ? 219  VAL B C   1 
ATOM   13947 O  O   . VAL C 1 219  ? 57.848  16.557  73.831  1.00 145.16 ? 219  VAL B O   1 
ATOM   13948 C  CB  . VAL C 1 219  ? 60.245  17.431  75.229  1.00 146.40 ? 219  VAL B CB  1 
ATOM   13949 C  CG1 . VAL C 1 219  ? 60.700  15.992  75.356  1.00 151.09 ? 219  VAL B CG1 1 
ATOM   13950 C  CG2 . VAL C 1 219  ? 61.310  18.390  75.729  1.00 148.55 ? 219  VAL B CG2 1 
ATOM   13951 N  N   . LYS C 1 220  ? 59.510  15.712  72.560  1.00 158.22 ? 220  LYS B N   1 
ATOM   13952 C  CA  . LYS C 1 220  ? 58.707  14.621  72.049  1.00 156.02 ? 220  LYS B CA  1 
ATOM   13953 C  C   . LYS C 1 220  ? 59.435  13.305  72.286  1.00 155.15 ? 220  LYS B C   1 
ATOM   13954 O  O   . LYS C 1 220  ? 60.668  13.256  72.374  1.00 165.43 ? 220  LYS B O   1 
ATOM   13955 C  CB  . LYS C 1 220  ? 58.405  14.812  70.543  1.00 155.63 ? 220  LYS B CB  1 
ATOM   13956 C  CG  . LYS C 1 220  ? 57.453  15.981  70.162  1.00 155.23 ? 220  LYS B CG  1 
ATOM   13957 C  CD  . LYS C 1 220  ? 57.467  16.235  68.638  1.00 162.23 ? 220  LYS B CD  1 
ATOM   13958 C  CE  . LYS C 1 220  ? 56.477  17.315  68.171  1.00 160.60 ? 220  LYS B CE  1 
ATOM   13959 N  NZ  . LYS C 1 220  ? 55.086  16.803  68.027  1.00 158.01 ? 220  LYS B NZ  1 
ATOM   13960 N  N   . GLU C 1 221  ? 58.650  12.243  72.398  1.00 191.47 ? 221  GLU B N   1 
ATOM   13961 C  CA  . GLU C 1 221  ? 59.191  10.923  72.638  1.00 202.10 ? 221  GLU B CA  1 
ATOM   13962 C  C   . GLU C 1 221  ? 59.559  10.192  71.347  1.00 201.68 ? 221  GLU B C   1 
ATOM   13963 O  O   . GLU C 1 221  ? 58.684  9.781   70.585  1.00 198.90 ? 221  GLU B O   1 
ATOM   13964 C  CB  . GLU C 1 221  ? 58.190  10.086  73.422  1.00 210.30 ? 221  GLU B CB  1 
ATOM   13965 C  CG  . GLU C 1 221  ? 58.597  8.634   73.482  1.00 221.60 ? 221  GLU B CG  1 
ATOM   13966 C  CD  . GLU C 1 221  ? 57.623  7.763   74.240  1.00 226.57 ? 221  GLU B CD  1 
ATOM   13967 O  OE1 . GLU C 1 221  ? 56.673  8.315   74.841  1.00 225.45 ? 221  GLU B OE1 1 
ATOM   13968 O  OE2 . GLU C 1 221  ? 57.820  6.523   74.232  1.00 230.38 ? 221  GLU B OE2 1 
ATOM   13969 N  N   . TYR C 1 222  ? 60.855  10.005  71.116  1.00 181.65 ? 222  TYR B N   1 
ATOM   13970 C  CA  . TYR C 1 222  ? 61.311  9.295   69.925  1.00 182.81 ? 222  TYR B CA  1 
ATOM   13971 C  C   . TYR C 1 222  ? 60.864  7.841   69.903  1.00 183.27 ? 222  TYR B C   1 
ATOM   13972 O  O   . TYR C 1 222  ? 61.076  7.085   70.848  1.00 183.71 ? 222  TYR B O   1 
ATOM   13973 C  CB  . TYR C 1 222  ? 62.833  9.355   69.779  1.00 184.31 ? 222  TYR B CB  1 
ATOM   13974 C  CG  . TYR C 1 222  ? 63.333  8.547   68.610  1.00 185.40 ? 222  TYR B CG  1 
ATOM   13975 C  CD1 . TYR C 1 222  ? 63.303  9.068   67.324  1.00 185.66 ? 222  TYR B CD1 1 
ATOM   13976 C  CD2 . TYR C 1 222  ? 63.813  7.258   68.788  1.00 187.80 ? 222  TYR B CD2 1 
ATOM   13977 C  CE1 . TYR C 1 222  ? 63.749  8.332   66.247  1.00 188.91 ? 222  TYR B CE1 1 
ATOM   13978 C  CE2 . TYR C 1 222  ? 64.260  6.513   67.718  1.00 190.75 ? 222  TYR B CE2 1 
ATOM   13979 C  CZ  . TYR C 1 222  ? 64.225  7.053   66.451  1.00 191.22 ? 222  TYR B CZ  1 
ATOM   13980 O  OH  . TYR C 1 222  ? 64.677  6.311   65.389  1.00 193.54 ? 222  TYR B OH  1 
ATOM   13981 N  N   . VAL C 1 223  ? 60.238  7.450   68.810  1.00 163.62 ? 223  VAL B N   1 
ATOM   13982 C  CA  . VAL C 1 223  ? 59.967  6.046   68.591  1.00 161.05 ? 223  VAL B CA  1 
ATOM   13983 C  C   . VAL C 1 223  ? 60.784  5.578   67.391  1.00 164.98 ? 223  VAL B C   1 
ATOM   13984 O  O   . VAL C 1 223  ? 61.274  6.398   66.615  1.00 164.90 ? 223  VAL B O   1 
ATOM   13985 C  CB  . VAL C 1 223  ? 58.458  5.787   68.387  1.00 156.25 ? 223  VAL B CB  1 
ATOM   13986 C  CG1 . VAL C 1 223  ? 58.178  4.282   68.245  1.00 155.02 ? 223  VAL B CG1 1 
ATOM   13987 C  CG2 . VAL C 1 223  ? 57.659  6.401   69.544  1.00 152.98 ? 223  VAL B CG2 1 
ATOM   13988 N  N   . LEU C 1 224  ? 60.965  4.269   67.256  1.00 210.92 ? 224  LEU B N   1 
ATOM   13989 C  CA  . LEU C 1 224  ? 61.676  3.750   66.103  1.00 216.40 ? 224  LEU B CA  1 
ATOM   13990 C  C   . LEU C 1 224  ? 60.674  3.427   65.016  1.00 217.19 ? 224  LEU B C   1 
ATOM   13991 O  O   . LEU C 1 224  ? 59.689  2.722   65.261  1.00 215.95 ? 224  LEU B O   1 
ATOM   13992 C  CB  . LEU C 1 224  ? 62.514  2.519   66.454  1.00 216.64 ? 224  LEU B CB  1 
ATOM   13993 C  CG  . LEU C 1 224  ? 63.773  2.290   65.601  1.00 221.61 ? 224  LEU B CG  1 
ATOM   13994 C  CD1 . LEU C 1 224  ? 63.416  1.870   64.181  1.00 223.91 ? 224  LEU B CD1 1 
ATOM   13995 C  CD2 . LEU C 1 224  ? 64.680  3.522   65.596  1.00 221.93 ? 224  LEU B CD2 1 
ATOM   13996 N  N   . PRO C 1 225  ? 60.911  3.978   63.813  1.00 242.53 ? 225  PRO B N   1 
ATOM   13997 C  CA  . PRO C 1 225  ? 60.095  3.698   62.637  1.00 235.01 ? 225  PRO B CA  1 
ATOM   13998 C  C   . PRO C 1 225  ? 60.406  2.313   62.118  1.00 236.45 ? 225  PRO B C   1 
ATOM   13999 O  O   . PRO C 1 225  ? 61.570  1.997   61.860  1.00 238.72 ? 225  PRO B O   1 
ATOM   14000 C  CB  . PRO C 1 225  ? 60.592  4.721   61.603  1.00 230.83 ? 225  PRO B CB  1 
ATOM   14001 C  CG  . PRO C 1 225  ? 61.462  5.668   62.334  1.00 232.28 ? 225  PRO B CG  1 
ATOM   14002 C  CD  . PRO C 1 225  ? 62.000  4.916   63.499  1.00 240.02 ? 225  PRO B CD  1 
ATOM   14003 N  N   . HIS C 1 226  ? 59.370  1.500   61.969  1.00 221.19 ? 226  HIS B N   1 
ATOM   14004 C  CA  . HIS C 1 226  ? 59.482  0.238   61.259  1.00 225.64 ? 226  HIS B CA  1 
ATOM   14005 C  C   . HIS C 1 226  ? 59.332  0.454   59.729  1.00 216.85 ? 226  HIS B C   1 
ATOM   14006 O  O   . HIS C 1 226  ? 60.105  -0.090  58.934  1.00 216.08 ? 226  HIS B O   1 
ATOM   14007 C  CB  . HIS C 1 226  ? 58.437  -0.757  61.782  1.00 230.10 ? 226  HIS B CB  1 
ATOM   14008 C  CG  . HIS C 1 226  ? 58.576  -1.089  63.234  1.00 243.32 ? 226  HIS B CG  1 
ATOM   14009 N  ND1 . HIS C 1 226  ? 57.627  -0.734  64.178  1.00 246.05 ? 226  HIS B ND1 1 
ATOM   14010 C  CD2 . HIS C 1 226  ? 59.535  -1.759  63.913  1.00 252.68 ? 226  HIS B CD2 1 
ATOM   14011 C  CE1 . HIS C 1 226  ? 58.003  -1.166  65.362  1.00 254.62 ? 226  HIS B CE1 1 
ATOM   14012 N  NE2 . HIS C 1 226  ? 59.161  -1.795  65.231  1.00 258.79 ? 226  HIS B NE2 1 
ATOM   14013 N  N   . PHE C 1 227  ? 58.343  1.251   59.322  1.00 224.12 ? 227  PHE B N   1 
ATOM   14014 C  CA  . PHE C 1 227  ? 58.138  1.573   57.907  1.00 216.65 ? 227  PHE B CA  1 
ATOM   14015 C  C   . PHE C 1 227  ? 57.588  2.979   57.739  1.00 213.00 ? 227  PHE B C   1 
ATOM   14016 O  O   . PHE C 1 227  ? 56.750  3.430   58.511  1.00 214.98 ? 227  PHE B O   1 
ATOM   14017 C  CB  . PHE C 1 227  ? 57.185  0.581   57.252  1.00 207.79 ? 227  PHE B CB  1 
ATOM   14018 C  CG  . PHE C 1 227  ? 55.872  0.459   57.954  1.00 199.16 ? 227  PHE B CG  1 
ATOM   14019 C  CD1 . PHE C 1 227  ? 54.886  1.408   57.784  1.00 190.73 ? 227  PHE B CD1 1 
ATOM   14020 C  CD2 . PHE C 1 227  ? 55.620  -0.609  58.786  1.00 201.40 ? 227  PHE B CD2 1 
ATOM   14021 C  CE1 . PHE C 1 227  ? 53.679  1.287   58.434  1.00 188.30 ? 227  PHE B CE1 1 
ATOM   14022 C  CE2 . PHE C 1 227  ? 54.417  -0.728  59.435  1.00 198.14 ? 227  PHE B CE2 1 
ATOM   14023 C  CZ  . PHE C 1 227  ? 53.449  0.218   59.260  1.00 192.18 ? 227  PHE B CZ  1 
ATOM   14024 N  N   . SER C 1 228  ? 58.059  3.669   56.715  1.00 237.23 ? 228  SER B N   1 
ATOM   14025 C  CA  . SER C 1 228  ? 57.702  5.060   56.531  1.00 235.51 ? 228  SER B CA  1 
ATOM   14026 C  C   . SER C 1 228  ? 56.271  5.227   56.015  1.00 224.22 ? 228  SER B C   1 
ATOM   14027 O  O   . SER C 1 228  ? 55.989  4.907   54.860  1.00 219.17 ? 228  SER B O   1 
ATOM   14028 C  CB  . SER C 1 228  ? 58.698  5.703   55.570  1.00 239.98 ? 228  SER B CB  1 
ATOM   14029 O  OG  . SER C 1 228  ? 58.206  6.927   55.071  1.00 237.82 ? 228  SER B OG  1 
ATOM   14030 N  N   . VAL C 1 229  ? 55.364  5.707   56.867  1.00 176.54 ? 229  VAL B N   1 
ATOM   14031 C  CA  . VAL C 1 229  ? 54.037  6.115   56.392  1.00 158.61 ? 229  VAL B CA  1 
ATOM   14032 C  C   . VAL C 1 229  ? 53.966  7.628   56.224  1.00 160.67 ? 229  VAL B C   1 
ATOM   14033 O  O   . VAL C 1 229  ? 54.282  8.380   57.147  1.00 161.43 ? 229  VAL B O   1 
ATOM   14034 C  CB  . VAL C 1 229  ? 52.872  5.622   57.293  1.00 153.34 ? 229  VAL B CB  1 
ATOM   14035 C  CG1 . VAL C 1 229  ? 51.716  6.601   57.274  1.00 144.86 ? 229  VAL B CG1 1 
ATOM   14036 C  CG2 . VAL C 1 229  ? 52.387  4.270   56.830  1.00 149.96 ? 229  VAL B CG2 1 
ATOM   14037 N  N   . SER C 1 230  ? 53.586  8.059   55.023  1.00 208.00 ? 230  SER B N   1 
ATOM   14038 C  CA  . SER C 1 230  ? 53.352  9.466   54.721  1.00 203.20 ? 230  SER B CA  1 
ATOM   14039 C  C   . SER C 1 230  ? 51.866  9.723   54.779  1.00 197.26 ? 230  SER B C   1 
ATOM   14040 O  O   . SER C 1 230  ? 51.086  8.844   55.135  1.00 196.52 ? 230  SER B O   1 
ATOM   14041 C  CB  . SER C 1 230  ? 53.872  9.818   53.315  1.00 200.13 ? 230  SER B CB  1 
ATOM   14042 O  OG  . SER C 1 230  ? 53.183  9.107   52.285  1.00 195.48 ? 230  SER B OG  1 
ATOM   14043 N  N   . ILE C 1 231  ? 51.480  10.935  54.423  1.00 139.55 ? 231  ILE B N   1 
ATOM   14044 C  CA  . ILE C 1 231  ? 50.084  11.231  54.172  1.00 135.14 ? 231  ILE B CA  1 
ATOM   14045 C  C   . ILE C 1 231  ? 49.992  12.605  53.497  1.00 130.22 ? 231  ILE B C   1 
ATOM   14046 O  O   . ILE C 1 231  ? 50.461  13.609  54.043  1.00 134.40 ? 231  ILE B O   1 
ATOM   14047 C  CB  . ILE C 1 231  ? 49.252  11.121  55.466  1.00 132.52 ? 231  ILE B CB  1 
ATOM   14048 C  CG1 . ILE C 1 231  ? 48.012  12.008  55.408  1.00 128.15 ? 231  ILE B CG1 1 
ATOM   14049 C  CG2 . ILE C 1 231  ? 50.113  11.470  56.637  1.00 137.64 ? 231  ILE B CG2 1 
ATOM   14050 C  CD1 . ILE C 1 231  ? 47.207  12.019  56.676  1.00 130.24 ? 231  ILE B CD1 1 
ATOM   14051 N  N   . GLU C 1 232  ? 49.444  12.607  52.276  1.00 165.62 ? 232  GLU B N   1 
ATOM   14052 C  CA  . GLU C 1 232  ? 49.261  13.799  51.452  1.00 167.20 ? 232  GLU B CA  1 
ATOM   14053 C  C   . GLU C 1 232  ? 47.774  14.028  51.235  1.00 161.79 ? 232  GLU B C   1 
ATOM   14054 O  O   . GLU C 1 232  ? 47.020  13.131  50.842  1.00 158.15 ? 232  GLU B O   1 
ATOM   14055 C  CB  . GLU C 1 232  ? 49.960  13.653  50.096  1.00 172.93 ? 232  GLU B CB  1 
ATOM   14056 C  CG  . GLU C 1 232  ? 51.283  12.885  50.123  1.00 185.46 ? 232  GLU B CG  1 
ATOM   14057 C  CD  . GLU C 1 232  ? 51.377  11.767  49.069  1.00 190.96 ? 232  GLU B CD  1 
ATOM   14058 O  OE1 . GLU C 1 232  ? 50.559  11.730  48.114  1.00 189.41 ? 232  GLU B OE1 1 
ATOM   14059 O  OE2 . GLU C 1 232  ? 52.289  10.922  49.208  1.00 196.27 ? 232  GLU B OE2 1 
ATOM   14060 N  N   . PRO C 1 233  ? 47.359  15.255  51.478  1.00 156.43 ? 233  PRO B N   1 
ATOM   14061 C  CA  . PRO C 1 233  ? 45.990  15.745  51.450  1.00 155.00 ? 233  PRO B CA  1 
ATOM   14062 C  C   . PRO C 1 233  ? 45.643  16.133  50.027  1.00 150.49 ? 233  PRO B C   1 
ATOM   14063 O  O   . PRO C 1 233  ? 46.569  16.411  49.258  1.00 152.88 ? 233  PRO B O   1 
ATOM   14064 C  CB  . PRO C 1 233  ? 46.081  17.011  52.308  1.00 157.26 ? 233  PRO B CB  1 
ATOM   14065 C  CG  . PRO C 1 233  ? 47.569  17.191  52.635  1.00 158.52 ? 233  PRO B CG  1 
ATOM   14066 C  CD  . PRO C 1 233  ? 48.313  16.346  51.687  1.00 158.43 ? 233  PRO B CD  1 
ATOM   14067 N  N   . GLU C 1 234  ? 44.358  16.179  49.686  1.00 192.89 ? 234  GLU B N   1 
ATOM   14068 C  CA  . GLU C 1 234  ? 43.973  16.599  48.352  1.00 186.20 ? 234  GLU B CA  1 
ATOM   14069 C  C   . GLU C 1 234  ? 44.634  17.935  47.991  1.00 182.91 ? 234  GLU B C   1 
ATOM   14070 O  O   . GLU C 1 234  ? 45.370  18.019  47.016  1.00 183.97 ? 234  GLU B O   1 
ATOM   14071 C  CB  . GLU C 1 234  ? 42.448  16.646  48.201  1.00 184.37 ? 234  GLU B CB  1 
ATOM   14072 C  CG  . GLU C 1 234  ? 41.960  16.142  46.826  1.00 197.03 ? 234  GLU B CG  1 
ATOM   14073 C  CD  . GLU C 1 234  ? 40.462  16.367  46.585  1.00 196.06 ? 234  GLU B CD  1 
ATOM   14074 O  OE1 . GLU C 1 234  ? 39.746  16.672  47.569  1.00 197.73 ? 234  GLU B OE1 1 
ATOM   14075 O  OE2 . GLU C 1 234  ? 39.996  16.245  45.420  1.00 193.52 ? 234  GLU B OE2 1 
ATOM   14076 N  N   . TYR C 1 235  ? 44.390  18.972  48.781  1.00 162.07 ? 235  TYR B N   1 
ATOM   14077 C  CA  . TYR C 1 235  ? 45.073  20.246  48.583  1.00 159.01 ? 235  TYR B CA  1 
ATOM   14078 C  C   . TYR C 1 235  ? 45.535  20.680  49.960  1.00 159.59 ? 235  TYR B C   1 
ATOM   14079 O  O   . TYR C 1 235  ? 45.532  19.872  50.877  1.00 161.19 ? 235  TYR B O   1 
ATOM   14080 C  CB  . TYR C 1 235  ? 44.155  21.316  47.981  1.00 157.18 ? 235  TYR B CB  1 
ATOM   14081 C  CG  . TYR C 1 235  ? 43.317  20.901  46.779  1.00 156.97 ? 235  TYR B CG  1 
ATOM   14082 C  CD1 . TYR C 1 235  ? 43.071  21.792  45.729  1.00 158.44 ? 235  TYR B CD1 1 
ATOM   14083 C  CD2 . TYR C 1 235  ? 42.745  19.631  46.694  1.00 157.77 ? 235  TYR B CD2 1 
ATOM   14084 C  CE1 . TYR C 1 235  ? 42.275  21.411  44.608  1.00 159.11 ? 235  TYR B CE1 1 
ATOM   14085 C  CE2 . TYR C 1 235  ? 41.960  19.246  45.587  1.00 158.18 ? 235  TYR B CE2 1 
ATOM   14086 C  CZ  . TYR C 1 235  ? 41.725  20.136  44.552  1.00 159.38 ? 235  TYR B CZ  1 
ATOM   14087 O  OH  . TYR C 1 235  ? 40.944  19.739  43.484  1.00 159.06 ? 235  TYR B OH  1 
ATOM   14088 N  N   . ASN C 1 236  ? 45.901  21.949  50.122  1.00 202.93 ? 236  ASN B N   1 
ATOM   14089 C  CA  . ASN C 1 236  ? 46.442  22.418  51.400  1.00 205.87 ? 236  ASN B CA  1 
ATOM   14090 C  C   . ASN C 1 236  ? 45.481  23.130  52.333  1.00 202.22 ? 236  ASN B C   1 
ATOM   14091 O  O   . ASN C 1 236  ? 45.769  23.296  53.516  1.00 210.06 ? 236  ASN B O   1 
ATOM   14092 C  CB  . ASN C 1 236  ? 47.661  23.300  51.189  1.00 211.41 ? 236  ASN B CB  1 
ATOM   14093 C  CG  . ASN C 1 236  ? 48.947  22.526  51.307  1.00 219.21 ? 236  ASN B CG  1 
ATOM   14094 O  OD1 . ASN C 1 236  ? 49.020  21.364  50.905  1.00 221.95 ? 236  ASN B OD1 1 
ATOM   14095 N  ND2 . ASN C 1 236  ? 49.971  23.157  51.867  1.00 222.23 ? 236  ASN B ND2 1 
ATOM   14096 N  N   . PHE C 1 237  ? 44.363  23.582  51.793  1.00 145.04 ? 237  PHE B N   1 
ATOM   14097 C  CA  . PHE C 1 237  ? 43.343  24.210  52.597  1.00 143.79 ? 237  PHE B CA  1 
ATOM   14098 C  C   . PHE C 1 237  ? 42.087  23.515  52.237  1.00 138.26 ? 237  PHE B C   1 
ATOM   14099 O  O   . PHE C 1 237  ? 42.123  22.444  51.679  1.00 133.56 ? 237  PHE B O   1 
ATOM   14100 C  CB  . PHE C 1 237  ? 43.218  25.673  52.256  1.00 137.04 ? 237  PHE B CB  1 
ATOM   14101 C  CG  . PHE C 1 237  ? 44.455  26.463  52.552  1.00 140.44 ? 237  PHE B CG  1 
ATOM   14102 C  CD1 . PHE C 1 237  ? 44.427  27.494  53.489  1.00 141.86 ? 237  PHE B CD1 1 
ATOM   14103 C  CD2 . PHE C 1 237  ? 45.649  26.179  51.907  1.00 139.56 ? 237  PHE B CD2 1 
ATOM   14104 C  CE1 . PHE C 1 237  ? 45.563  28.243  53.779  1.00 142.25 ? 237  PHE B CE1 1 
ATOM   14105 C  CE2 . PHE C 1 237  ? 46.789  26.916  52.186  1.00 144.37 ? 237  PHE B CE2 1 
ATOM   14106 C  CZ  . PHE C 1 237  ? 46.748  27.955  53.129  1.00 139.99 ? 237  PHE B CZ  1 
ATOM   14107 N  N   . ILE C 1 238  ? 40.964  24.120  52.529  1.00 111.97 ? 238  ILE B N   1 
ATOM   14108 C  CA  . ILE C 1 238  ? 39.735  23.512  52.126  1.00 110.74 ? 238  ILE B CA  1 
ATOM   14109 C  C   . ILE C 1 238  ? 38.868  24.668  51.834  1.00 114.98 ? 238  ILE B C   1 
ATOM   14110 O  O   . ILE C 1 238  ? 38.256  25.210  52.746  1.00 117.12 ? 238  ILE B O   1 
ATOM   14111 C  CB  . ILE C 1 238  ? 39.115  22.704  53.244  1.00 110.98 ? 238  ILE B CB  1 
ATOM   14112 C  CG1 . ILE C 1 238  ? 39.921  21.437  53.461  1.00 111.02 ? 238  ILE B CG1 1 
ATOM   14113 C  CG2 . ILE C 1 238  ? 37.705  22.320  52.896  1.00 111.18 ? 238  ILE B CG2 1 
ATOM   14114 C  CD1 . ILE C 1 238  ? 39.111  20.288  54.005  1.00 112.18 ? 238  ILE B CD1 1 
ATOM   14115 N  N   . GLY C 1 239  ? 38.876  25.075  50.563  1.00 190.15 ? 239  GLY B N   1 
ATOM   14116 C  CA  . GLY C 1 239  ? 38.048  26.149  50.046  1.00 190.40 ? 239  GLY B CA  1 
ATOM   14117 C  C   . GLY C 1 239  ? 36.737  25.583  49.553  1.00 191.42 ? 239  GLY B C   1 
ATOM   14118 O  O   . GLY C 1 239  ? 36.648  24.411  49.182  1.00 190.71 ? 239  GLY B O   1 
ATOM   14119 N  N   . TYR C 1 240  ? 35.720  26.428  49.533  1.00 169.14 ? 240  TYR B N   1 
ATOM   14120 C  CA  . TYR C 1 240  ? 34.354  25.958  49.418  1.00 171.78 ? 240  TYR B CA  1 
ATOM   14121 C  C   . TYR C 1 240  ? 34.102  25.038  48.237  1.00 172.45 ? 240  TYR B C   1 
ATOM   14122 O  O   . TYR C 1 240  ? 32.971  24.609  48.027  1.00 170.03 ? 240  TYR B O   1 
ATOM   14123 C  CB  . TYR C 1 240  ? 33.437  27.138  49.236  1.00 171.22 ? 240  TYR B CB  1 
ATOM   14124 C  CG  . TYR C 1 240  ? 33.458  27.524  47.807  1.00 164.79 ? 240  TYR B CG  1 
ATOM   14125 C  CD1 . TYR C 1 240  ? 32.522  27.025  46.917  1.00 158.91 ? 240  TYR B CD1 1 
ATOM   14126 C  CD2 . TYR C 1 240  ? 34.467  28.332  47.322  1.00 164.38 ? 240  TYR B CD2 1 
ATOM   14127 C  CE1 . TYR C 1 240  ? 32.579  27.354  45.579  1.00 155.49 ? 240  TYR B CE1 1 
ATOM   14128 C  CE2 . TYR C 1 240  ? 34.529  28.683  45.991  1.00 161.52 ? 240  TYR B CE2 1 
ATOM   14129 C  CZ  . TYR C 1 240  ? 33.593  28.195  45.113  1.00 158.26 ? 240  TYR B CZ  1 
ATOM   14130 O  OH  . TYR C 1 240  ? 33.685  28.573  43.779  1.00 159.60 ? 240  TYR B OH  1 
ATOM   14131 N  N   . LYS C 1 241  ? 35.116  24.771  47.430  1.00 197.58 ? 241  LYS B N   1 
ATOM   14132 C  CA  . LYS C 1 241  ? 34.925  23.871  46.302  1.00 200.39 ? 241  LYS B CA  1 
ATOM   14133 C  C   . LYS C 1 241  ? 34.559  22.458  46.748  1.00 205.03 ? 241  LYS B C   1 
ATOM   14134 O  O   . LYS C 1 241  ? 33.540  21.912  46.314  1.00 205.37 ? 241  LYS B O   1 
ATOM   14135 C  CB  . LYS C 1 241  ? 36.144  23.886  45.396  1.00 183.40 ? 241  LYS B CB  1 
ATOM   14136 C  CG  . LYS C 1 241  ? 36.293  25.225  44.708  1.00 164.58 ? 241  LYS B CG  1 
ATOM   14137 C  CD  . LYS C 1 241  ? 37.516  25.291  43.824  1.00 178.37 ? 241  LYS B CD  1 
ATOM   14138 C  CE  . LYS C 1 241  ? 37.401  26.446  42.830  1.00 208.62 ? 241  LYS B CE  1 
ATOM   14139 N  NZ  . LYS C 1 241  ? 37.371  27.804  43.451  1.00 207.94 ? 241  LYS B NZ  1 
ATOM   14140 N  N   . ASN C 1 242  ? 35.381  21.870  47.614  1.00 148.66 ? 242  ASN B N   1 
ATOM   14141 C  CA  . ASN C 1 242  ? 34.999  20.630  48.293  1.00 150.24 ? 242  ASN B CA  1 
ATOM   14142 C  C   . ASN C 1 242  ? 34.579  20.990  49.683  1.00 155.47 ? 242  ASN B C   1 
ATOM   14143 O  O   . ASN C 1 242  ? 35.221  21.812  50.330  1.00 155.04 ? 242  ASN B O   1 
ATOM   14144 C  CB  . ASN C 1 242  ? 36.159  19.661  48.399  1.00 145.74 ? 242  ASN B CB  1 
ATOM   14145 C  CG  . ASN C 1 242  ? 37.254  19.948  47.408  1.00 139.31 ? 242  ASN B CG  1 
ATOM   14146 O  OD1 . ASN C 1 242  ? 37.723  19.041  46.719  1.00 137.05 ? 242  ASN B OD1 1 
ATOM   14147 N  ND2 . ASN C 1 242  ? 37.679  21.212  47.327  1.00 143.07 ? 242  ASN B ND2 1 
ATOM   14148 N  N   . PHE C 1 243  ? 33.507  20.388  50.156  1.00 188.83 ? 243  PHE B N   1 
ATOM   14149 C  CA  . PHE C 1 243  ? 33.077  20.678  51.508  1.00 198.54 ? 243  PHE B CA  1 
ATOM   14150 C  C   . PHE C 1 243  ? 32.255  19.482  51.911  1.00 204.57 ? 243  PHE B C   1 
ATOM   14151 O  O   . PHE C 1 243  ? 31.990  19.239  53.093  1.00 207.19 ? 243  PHE B O   1 
ATOM   14152 C  CB  . PHE C 1 243  ? 32.276  21.986  51.558  1.00 199.45 ? 243  PHE B CB  1 
ATOM   14153 C  CG  . PHE C 1 243  ? 31.972  22.463  52.948  1.00 204.74 ? 243  PHE B CG  1 
ATOM   14154 C  CD1 . PHE C 1 243  ? 32.988  22.675  53.861  1.00 207.21 ? 243  PHE B CD1 1 
ATOM   14155 C  CD2 . PHE C 1 243  ? 30.669  22.715  53.332  1.00 207.01 ? 243  PHE B CD2 1 
ATOM   14156 C  CE1 . PHE C 1 243  ? 32.707  23.109  55.136  1.00 210.60 ? 243  PHE B CE1 1 
ATOM   14157 C  CE2 . PHE C 1 243  ? 30.384  23.147  54.603  1.00 210.53 ? 243  PHE B CE2 1 
ATOM   14158 C  CZ  . PHE C 1 243  ? 31.404  23.341  55.505  1.00 212.40 ? 243  PHE B CZ  1 
ATOM   14159 N  N   . LYS C 1 244  ? 31.875  18.727  50.887  1.00 276.87 ? 244  LYS B N   1 
ATOM   14160 C  CA  . LYS C 1 244  ? 31.312  17.406  51.054  1.00 285.31 ? 244  LYS B CA  1 
ATOM   14161 C  C   . LYS C 1 244  ? 32.348  16.408  50.598  1.00 286.20 ? 244  LYS B C   1 
ATOM   14162 O  O   . LYS C 1 244  ? 32.086  15.202  50.571  1.00 292.42 ? 244  LYS B O   1 
ATOM   14163 C  CB  . LYS C 1 244  ? 30.038  17.246  50.242  1.00 288.33 ? 244  LYS B CB  1 
ATOM   14164 C  CG  . LYS C 1 244  ? 28.907  18.091  50.749  1.00 292.51 ? 244  LYS B CG  1 
ATOM   14165 C  CD  . LYS C 1 244  ? 27.579  17.499  50.352  1.00 295.12 ? 244  LYS B CD  1 
ATOM   14166 C  CE  . LYS C 1 244  ? 26.448  18.420  50.740  1.00 297.01 ? 244  LYS B CE  1 
ATOM   14167 N  NZ  . LYS C 1 244  ? 26.585  19.748  50.092  1.00 293.60 ? 244  LYS B NZ  1 
ATOM   14168 N  N   . ASN C 1 245  ? 33.528  16.911  50.235  1.00 187.55 ? 245  ASN B N   1 
ATOM   14169 C  CA  . ASN C 1 245  ? 34.634  15.995  49.963  1.00 185.85 ? 245  ASN B CA  1 
ATOM   14170 C  C   . ASN C 1 245  ? 36.059  16.555  49.946  1.00 180.33 ? 245  ASN B C   1 
ATOM   14171 O  O   . ASN C 1 245  ? 36.301  17.681  49.547  1.00 179.65 ? 245  ASN B O   1 
ATOM   14172 C  CB  . ASN C 1 245  ? 34.394  15.284  48.648  1.00 185.45 ? 245  ASN B CB  1 
ATOM   14173 C  CG  . ASN C 1 245  ? 34.672  16.159  47.511  1.00 185.87 ? 245  ASN B CG  1 
ATOM   14174 O  OD1 . ASN C 1 245  ? 34.577  17.382  47.639  1.00 186.29 ? 245  ASN B OD1 1 
ATOM   14175 N  ND2 . ASN C 1 245  ? 35.047  15.568  46.385  1.00 187.91 ? 245  ASN B ND2 1 
ATOM   14176 N  N   . PHE C 1 246  ? 36.997  15.703  50.356  1.00 124.52 ? 246  PHE B N   1 
ATOM   14177 C  CA  . PHE C 1 246  ? 38.432  15.987  50.333  1.00 115.55 ? 246  PHE B CA  1 
ATOM   14178 C  C   . PHE C 1 246  ? 39.147  14.652  50.061  1.00 125.50 ? 246  PHE B C   1 
ATOM   14179 O  O   . PHE C 1 246  ? 38.736  13.623  50.586  1.00 125.24 ? 246  PHE B O   1 
ATOM   14180 C  CB  . PHE C 1 246  ? 38.843  16.522  51.698  1.00 123.19 ? 246  PHE B CB  1 
ATOM   14181 C  CG  . PHE C 1 246  ? 40.090  17.340  51.688  1.00 122.76 ? 246  PHE B CG  1 
ATOM   14182 C  CD1 . PHE C 1 246  ? 40.050  18.672  51.372  1.00 114.93 ? 246  PHE B CD1 1 
ATOM   14183 C  CD2 . PHE C 1 246  ? 41.295  16.781  52.037  1.00 122.48 ? 246  PHE B CD2 1 
ATOM   14184 C  CE1 . PHE C 1 246  ? 41.188  19.415  51.375  1.00 117.91 ? 246  PHE B CE1 1 
ATOM   14185 C  CE2 . PHE C 1 246  ? 42.429  17.531  52.042  1.00 120.17 ? 246  PHE B CE2 1 
ATOM   14186 C  CZ  . PHE C 1 246  ? 42.373  18.846  51.707  1.00 121.10 ? 246  PHE B CZ  1 
ATOM   14187 N  N   . GLU C 1 247  ? 40.199  14.649  49.248  1.00 216.42 ? 247  GLU B N   1 
ATOM   14188 C  CA  . GLU C 1 247  ? 40.855  13.386  48.934  1.00 217.84 ? 247  GLU B CA  1 
ATOM   14189 C  C   . GLU C 1 247  ? 42.272  13.268  49.462  1.00 225.28 ? 247  GLU B C   1 
ATOM   14190 O  O   . GLU C 1 247  ? 43.227  13.860  48.941  1.00 226.40 ? 247  GLU B O   1 
ATOM   14191 C  CB  . GLU C 1 247  ? 40.827  13.068  47.448  1.00 260.46 ? 247  GLU B CB  1 
ATOM   14192 C  CG  . GLU C 1 247  ? 41.223  11.605  47.138  1.00 242.29 ? 247  GLU B CG  1 
ATOM   14193 C  CD  . GLU C 1 247  ? 41.295  11.313  45.630  1.00 189.11 ? 247  GLU B CD  1 
ATOM   14194 O  OE1 . GLU C 1 247  ? 40.946  12.217  44.878  1.00 182.76 ? 247  GLU B OE1 1 
ATOM   14195 O  OE2 . GLU C 1 247  ? 41.691  10.201  45.237  1.00 183.72 ? 247  GLU B OE2 1 
ATOM   14196 N  N   . ILE C 1 248  ? 42.386  12.426  50.472  1.00 155.48 ? 248  ILE B N   1 
ATOM   14197 C  CA  . ILE C 1 248  ? 43.628  12.202  51.144  1.00 153.37 ? 248  ILE B CA  1 
ATOM   14198 C  C   . ILE C 1 248  ? 44.151  10.842  50.775  1.00 152.10 ? 248  ILE B C   1 
ATOM   14199 O  O   . ILE C 1 248  ? 43.466  9.836   50.930  1.00 153.23 ? 248  ILE B O   1 
ATOM   14200 C  CB  . ILE C 1 248  ? 43.412  12.191  52.641  1.00 154.64 ? 248  ILE B CB  1 
ATOM   14201 C  CG1 . ILE C 1 248  ? 42.436  13.305  53.054  1.00 152.26 ? 248  ILE B CG1 1 
ATOM   14202 C  CG2 . ILE C 1 248  ? 44.756  12.323  53.346  1.00 158.62 ? 248  ILE B CG2 1 
ATOM   14203 C  CD1 . ILE C 1 248  ? 41.948  13.209  54.524  1.00 154.44 ? 248  ILE B CD1 1 
ATOM   14204 N  N   . THR C 1 249  ? 45.395  10.820  50.332  1.00 162.93 ? 249  THR B N   1 
ATOM   14205 C  CA  . THR C 1 249  ? 46.076  9.587   50.008  1.00 165.53 ? 249  THR B CA  1 
ATOM   14206 C  C   . THR C 1 249  ? 47.062  9.300   51.128  1.00 172.65 ? 249  THR B C   1 
ATOM   14207 O  O   . THR C 1 249  ? 47.652  10.233  51.663  1.00 173.83 ? 249  THR B O   1 
ATOM   14208 C  CB  . THR C 1 249  ? 46.867  9.792   48.733  1.00 171.38 ? 249  THR B CB  1 
ATOM   14209 O  OG1 . THR C 1 249  ? 46.545  11.086  48.205  1.00 168.00 ? 249  THR B OG1 1 
ATOM   14210 C  CG2 . THR C 1 249  ? 46.540  8.702   47.727  1.00 170.05 ? 249  THR B CG2 1 
ATOM   14211 N  N   . ILE C 1 250  ? 47.237  8.030   51.494  1.00 135.10 ? 250  ILE B N   1 
ATOM   14212 C  CA  . ILE C 1 250  ? 48.209  7.647   52.519  1.00 141.74 ? 250  ILE B CA  1 
ATOM   14213 C  C   . ILE C 1 250  ? 49.053  6.495   52.012  1.00 147.55 ? 250  ILE B C   1 
ATOM   14214 O  O   . ILE C 1 250  ? 48.524  5.445   51.671  1.00 146.01 ? 250  ILE B O   1 
ATOM   14215 C  CB  . ILE C 1 250  ? 47.509  7.181   53.793  1.00 142.44 ? 250  ILE B CB  1 
ATOM   14216 C  CG1 . ILE C 1 250  ? 46.418  6.161   53.430  1.00 143.01 ? 250  ILE B CG1 1 
ATOM   14217 C  CG2 . ILE C 1 250  ? 46.979  8.390   54.583  1.00 139.17 ? 250  ILE B CG2 1 
ATOM   14218 C  CD1 . ILE C 1 250  ? 45.720  5.512   54.626  1.00 146.24 ? 250  ILE B CD1 1 
ATOM   14219 N  N   . LYS C 1 251  ? 50.367  6.687   51.991  1.00 212.21 ? 251  LYS B N   1 
ATOM   14220 C  CA  . LYS C 1 251  ? 51.256  5.805   51.241  1.00 221.36 ? 251  LYS B CA  1 
ATOM   14221 C  C   . LYS C 1 251  ? 52.358  5.169   52.085  1.00 234.38 ? 251  LYS B C   1 
ATOM   14222 O  O   . LYS C 1 251  ? 53.360  5.818   52.394  1.00 237.88 ? 251  LYS B O   1 
ATOM   14223 C  CB  . LYS C 1 251  ? 51.895  6.583   50.090  1.00 221.42 ? 251  LYS B CB  1 
ATOM   14224 C  CG  . LYS C 1 251  ? 50.933  7.503   49.358  1.00 217.35 ? 251  LYS B CG  1 
ATOM   14225 C  CD  . LYS C 1 251  ? 51.446  7.899   47.979  1.00 217.41 ? 251  LYS B CD  1 
ATOM   14226 C  CE  . LYS C 1 251  ? 52.766  8.646   48.042  1.00 220.56 ? 251  LYS B CE  1 
ATOM   14227 N  NZ  . LYS C 1 251  ? 52.932  9.526   46.846  1.00 217.77 ? 251  LYS B NZ  1 
ATOM   14228 N  N   . ALA C 1 252  ? 52.187  3.889   52.416  1.00 206.81 ? 252  ALA B N   1 
ATOM   14229 C  CA  . ALA C 1 252  ? 53.127  3.174   53.285  1.00 215.15 ? 252  ALA B CA  1 
ATOM   14230 C  C   . ALA C 1 252  ? 54.177  2.384   52.513  1.00 218.36 ? 252  ALA B C   1 
ATOM   14231 O  O   . ALA C 1 252  ? 53.939  1.948   51.399  1.00 216.69 ? 252  ALA B O   1 
ATOM   14232 C  CB  . ALA C 1 252  ? 52.374  2.250   54.232  1.00 216.87 ? 252  ALA B CB  1 
ATOM   14233 N  N   . ARG C 1 253  ? 55.331  2.167   53.129  1.00 261.99 ? 253  ARG B N   1 
ATOM   14234 C  CA  . ARG C 1 253  ? 56.412  1.465   52.459  1.00 266.95 ? 253  ARG B CA  1 
ATOM   14235 C  C   . ARG C 1 253  ? 57.576  1.203   53.408  1.00 268.45 ? 253  ARG B C   1 
ATOM   14236 O  O   . ARG C 1 253  ? 57.977  2.085   54.172  1.00 271.29 ? 253  ARG B O   1 
ATOM   14237 C  CB  . ARG C 1 253  ? 56.899  2.286   51.273  1.00 271.43 ? 253  ARG B CB  1 
ATOM   14238 C  CG  . ARG C 1 253  ? 57.443  3.659   51.648  1.00 280.19 ? 253  ARG B CG  1 
ATOM   14239 C  CD  . ARG C 1 253  ? 58.389  4.168   50.576  1.00 289.22 ? 253  ARG B CD  1 
ATOM   14240 N  NE  . ARG C 1 253  ? 59.300  3.115   50.122  1.00 300.36 ? 253  ARG B NE  1 
ATOM   14241 C  CZ  . ARG C 1 253  ? 59.039  2.271   49.125  1.00 303.00 ? 253  ARG B CZ  1 
ATOM   14242 N  NH1 . ARG C 1 253  ? 57.893  2.346   48.468  1.00 298.32 ? 253  ARG B NH1 1 
ATOM   14243 N  NH2 . ARG C 1 253  ? 59.920  1.348   48.782  1.00 308.83 ? 253  ARG B NH2 1 
ATOM   14244 N  N   . TYR C 1 254  ? 58.117  -0.012  53.359  1.00 214.19 ? 254  TYR B N   1 
ATOM   14245 C  CA  . TYR C 1 254  ? 59.253  -0.370  54.202  1.00 214.26 ? 254  TYR B CA  1 
ATOM   14246 C  C   . TYR C 1 254  ? 60.520  0.308   53.672  1.00 212.25 ? 254  TYR B C   1 
ATOM   14247 O  O   . TYR C 1 254  ? 60.534  0.840   52.560  1.00 206.75 ? 254  TYR B O   1 
ATOM   14248 C  CB  . TYR C 1 254  ? 59.421  -1.897  54.295  1.00 217.31 ? 254  TYR B CB  1 
ATOM   14249 C  CG  . TYR C 1 254  ? 58.146  -2.653  54.653  1.00 214.51 ? 254  TYR B CG  1 
ATOM   14250 C  CD1 . TYR C 1 254  ? 57.768  -3.798  53.955  1.00 214.34 ? 254  TYR B CD1 1 
ATOM   14251 C  CD2 . TYR C 1 254  ? 57.316  -2.215  55.682  1.00 213.70 ? 254  TYR B CD2 1 
ATOM   14252 C  CE1 . TYR C 1 254  ? 56.605  -4.486  54.278  1.00 212.04 ? 254  TYR B CE1 1 
ATOM   14253 C  CE2 . TYR C 1 254  ? 56.151  -2.894  56.009  1.00 211.53 ? 254  TYR B CE2 1 
ATOM   14254 C  CZ  . TYR C 1 254  ? 55.799  -4.027  55.306  1.00 210.47 ? 254  TYR B CZ  1 
ATOM   14255 O  OH  . TYR C 1 254  ? 54.641  -4.697  55.634  1.00 208.91 ? 254  TYR B OH  1 
ATOM   14256 N  N   . PHE C 1 255  ? 61.577  0.304   54.475  1.00 236.95 ? 255  PHE B N   1 
ATOM   14257 C  CA  . PHE C 1 255  ? 62.822  0.956   54.086  1.00 242.72 ? 255  PHE B CA  1 
ATOM   14258 C  C   . PHE C 1 255  ? 63.545  0.244   52.948  1.00 251.56 ? 255  PHE B C   1 
ATOM   14259 O  O   . PHE C 1 255  ? 64.276  0.881   52.190  1.00 251.28 ? 255  PHE B O   1 
ATOM   14260 C  CB  . PHE C 1 255  ? 63.734  1.146   55.300  1.00 248.77 ? 255  PHE B CB  1 
ATOM   14261 C  CG  . PHE C 1 255  ? 63.298  2.264   56.195  1.00 245.63 ? 255  PHE B CG  1 
ATOM   14262 C  CD1 . PHE C 1 255  ? 64.148  3.322   56.480  1.00 244.22 ? 255  PHE B CD1 1 
ATOM   14263 C  CD2 . PHE C 1 255  ? 62.015  2.281   56.714  1.00 240.57 ? 255  PHE B CD2 1 
ATOM   14264 C  CE1 . PHE C 1 255  ? 63.736  4.360   57.293  1.00 240.87 ? 255  PHE B CE1 1 
ATOM   14265 C  CE2 . PHE C 1 255  ? 61.596  3.316   57.521  1.00 238.85 ? 255  PHE B CE2 1 
ATOM   14266 C  CZ  . PHE C 1 255  ? 62.460  4.358   57.814  1.00 239.62 ? 255  PHE B CZ  1 
ATOM   14267 N  N   . TYR C 1 256  ? 63.322  -1.064  52.816  1.00 285.64 ? 256  TYR B N   1 
ATOM   14268 C  CA  . TYR C 1 256  ? 63.956  -1.846  51.746  1.00 297.38 ? 256  TYR B CA  1 
ATOM   14269 C  C   . TYR C 1 256  ? 63.245  -1.763  50.386  1.00 305.53 ? 256  TYR B C   1 
ATOM   14270 O  O   . TYR C 1 256  ? 63.069  -2.773  49.696  1.00 310.54 ? 256  TYR B O   1 
ATOM   14271 C  CB  . TYR C 1 256  ? 64.186  -3.304  52.166  1.00 298.24 ? 256  TYR B CB  1 
ATOM   14272 C  CG  . TYR C 1 256  ? 63.023  -3.970  52.866  1.00 290.65 ? 256  TYR B CG  1 
ATOM   14273 C  CD1 . TYR C 1 256  ? 62.075  -4.692  52.152  1.00 285.37 ? 256  TYR B CD1 1 
ATOM   14274 C  CD2 . TYR C 1 256  ? 62.885  -3.891  54.245  1.00 290.82 ? 256  TYR B CD2 1 
ATOM   14275 C  CE1 . TYR C 1 256  ? 61.014  -5.304  52.791  1.00 281.06 ? 256  TYR B CE1 1 
ATOM   14276 C  CE2 . TYR C 1 256  ? 61.830  -4.500  54.894  1.00 286.59 ? 256  TYR B CE2 1 
ATOM   14277 C  CZ  . TYR C 1 256  ? 60.898  -5.205  54.163  1.00 281.27 ? 256  TYR B CZ  1 
ATOM   14278 O  OH  . TYR C 1 256  ? 59.847  -5.812  54.809  1.00 277.56 ? 256  TYR B OH  1 
ATOM   14279 N  N   . ASN C 1 257  ? 62.862  -0.541  50.015  1.00 386.12 ? 257  ASN B N   1 
ATOM   14280 C  CA  . ASN C 1 257  ? 62.224  -0.232  48.730  1.00 386.61 ? 257  ASN B CA  1 
ATOM   14281 C  C   . ASN C 1 257  ? 61.148  -1.214  48.265  1.00 378.99 ? 257  ASN B C   1 
ATOM   14282 O  O   . ASN C 1 257  ? 61.141  -1.644  47.113  1.00 376.35 ? 257  ASN B O   1 
ATOM   14283 C  CB  . ASN C 1 257  ? 63.260  0.013   47.629  1.00 400.36 ? 257  ASN B CB  1 
ATOM   14284 C  CG  . ASN C 1 257  ? 63.700  -1.259  46.958  1.00 417.66 ? 257  ASN B CG  1 
ATOM   14285 O  OD1 . ASN C 1 257  ? 63.537  -1.421  45.750  1.00 426.99 ? 257  ASN B OD1 1 
ATOM   14286 N  ND2 . ASN C 1 257  ? 64.262  -2.177  47.735  1.00 419.90 ? 257  ASN B ND2 1 
ATOM   14287 N  N   . LYS C 1 258  ? 60.239  -1.551  49.174  1.00 247.47 ? 258  LYS B N   1 
ATOM   14288 C  CA  . LYS C 1 258  ? 59.059  -2.344  48.847  1.00 243.78 ? 258  LYS B CA  1 
ATOM   14289 C  C   . LYS C 1 258  ? 57.875  -1.848  49.673  1.00 232.20 ? 258  LYS B C   1 
ATOM   14290 O  O   . LYS C 1 258  ? 57.897  -1.877  50.900  1.00 235.31 ? 258  LYS B O   1 
ATOM   14291 C  CB  . LYS C 1 258  ? 59.304  -3.845  49.084  1.00 252.48 ? 258  LYS B CB  1 
ATOM   14292 C  CG  . LYS C 1 258  ? 59.646  -4.659  47.821  1.00 257.94 ? 258  LYS B CG  1 
ATOM   14293 C  CD  . LYS C 1 258  ? 58.403  -5.033  47.005  1.00 254.99 ? 258  LYS B CD  1 
ATOM   14294 C  CE  . LYS C 1 258  ? 58.759  -5.927  45.819  1.00 259.19 ? 258  LYS B CE  1 
ATOM   14295 N  NZ  . LYS C 1 258  ? 57.573  -6.243  44.976  1.00 255.22 ? 258  LYS B NZ  1 
ATOM   14296 N  N   . VAL C 1 259  ? 56.848  -1.377  48.983  1.00 240.47 ? 259  VAL B N   1 
ATOM   14297 C  CA  . VAL C 1 259  ? 55.642  -0.901  49.630  1.00 230.12 ? 259  VAL B CA  1 
ATOM   14298 C  C   . VAL C 1 259  ? 54.967  -2.011  50.403  1.00 227.64 ? 259  VAL B C   1 
ATOM   14299 O  O   . VAL C 1 259  ? 55.161  -3.187  50.121  1.00 229.05 ? 259  VAL B O   1 
ATOM   14300 C  CB  . VAL C 1 259  ? 54.616  -0.431  48.594  1.00 218.33 ? 259  VAL B CB  1 
ATOM   14301 C  CG1 . VAL C 1 259  ? 55.285  0.408   47.510  1.00 217.54 ? 259  VAL B CG1 1 
ATOM   14302 C  CG2 . VAL C 1 259  ? 53.897  -1.631  47.976  1.00 217.63 ? 259  VAL B CG2 1 
ATOM   14303 N  N   . VAL C 1 260  ? 54.148  -1.628  51.371  1.00 226.03 ? 260  VAL B N   1 
ATOM   14304 C  CA  . VAL C 1 260  ? 53.312  -2.590  52.068  1.00 227.00 ? 260  VAL B CA  1 
ATOM   14305 C  C   . VAL C 1 260  ? 52.229  -3.095  51.134  1.00 226.44 ? 260  VAL B C   1 
ATOM   14306 O  O   . VAL C 1 260  ? 51.888  -2.437  50.159  1.00 222.02 ? 260  VAL B O   1 
ATOM   14307 C  CB  . VAL C 1 260  ? 52.622  -1.956  53.291  1.00 223.60 ? 260  VAL B CB  1 
ATOM   14308 C  CG1 . VAL C 1 260  ? 51.745  -2.980  54.008  1.00 223.95 ? 260  VAL B CG1 1 
ATOM   14309 C  CG2 . VAL C 1 260  ? 53.657  -1.375  54.245  1.00 226.82 ? 260  VAL B CG2 1 
ATOM   14310 N  N   . THR C 1 261  ? 51.704  -4.277  51.425  1.00 160.26 ? 261  THR B N   1 
ATOM   14311 C  CA  . THR C 1 261  ? 50.445  -4.702  50.838  1.00 160.94 ? 261  THR B CA  1 
ATOM   14312 C  C   . THR C 1 261  ? 49.391  -4.635  51.941  1.00 161.16 ? 261  THR B C   1 
ATOM   14313 O  O   . THR C 1 261  ? 49.058  -3.541  52.387  1.00 159.62 ? 261  THR B O   1 
ATOM   14314 C  CB  . THR C 1 261  ? 50.548  -6.088  50.177  1.00 165.74 ? 261  THR B CB  1 
ATOM   14315 O  OG1 . THR C 1 261  ? 51.767  -6.156  49.428  1.00 169.33 ? 261  THR B OG1 1 
ATOM   14316 C  CG2 . THR C 1 261  ? 49.357  -6.342  49.234  1.00 163.76 ? 261  THR B CG2 1 
ATOM   14317 N  N   . GLU C 1 262  ? 48.878  -5.766  52.416  1.00 305.79 ? 262  GLU B N   1 
ATOM   14318 C  CA  . GLU C 1 262  ? 47.828  -5.675  53.431  1.00 309.18 ? 262  GLU B CA  1 
ATOM   14319 C  C   . GLU C 1 262  ? 48.293  -4.941  54.688  1.00 309.69 ? 262  GLU B C   1 
ATOM   14320 O  O   . GLU C 1 262  ? 49.398  -5.167  55.189  1.00 311.93 ? 262  GLU B O   1 
ATOM   14321 C  CB  . GLU C 1 262  ? 47.235  -7.034  53.812  1.00 319.48 ? 262  GLU B CB  1 
ATOM   14322 C  CG  . GLU C 1 262  ? 46.097  -6.892  54.835  1.00 326.44 ? 262  GLU B CG  1 
ATOM   14323 C  CD  . GLU C 1 262  ? 45.592  -8.216  55.379  1.00 337.20 ? 262  GLU B CD  1 
ATOM   14324 O  OE1 . GLU C 1 262  ? 45.247  -8.280  56.582  1.00 341.98 ? 262  GLU B OE1 1 
ATOM   14325 O  OE2 . GLU C 1 262  ? 45.527  -9.189  54.603  1.00 340.55 ? 262  GLU B OE2 1 
ATOM   14326 N  N   . ALA C 1 263  ? 47.426  -4.058  55.173  1.00 245.21 ? 263  ALA B N   1 
ATOM   14327 C  CA  . ALA C 1 263  ? 47.645  -3.327  56.405  1.00 247.38 ? 263  ALA B CA  1 
ATOM   14328 C  C   . ALA C 1 263  ? 46.332  -2.720  56.838  1.00 242.26 ? 263  ALA B C   1 
ATOM   14329 O  O   . ALA C 1 263  ? 45.563  -2.223  56.030  1.00 239.53 ? 263  ALA B O   1 
ATOM   14330 C  CB  . ALA C 1 263  ? 48.680  -2.236  56.211  1.00 248.55 ? 263  ALA B CB  1 
ATOM   14331 N  N   . ASP C 1 264  ? 46.057  -2.755  58.129  1.00 319.70 ? 264  ASP B N   1 
ATOM   14332 C  CA  . ASP C 1 264  ? 44.869  -2.088  58.649  1.00 317.43 ? 264  ASP B CA  1 
ATOM   14333 C  C   . ASP C 1 264  ? 45.160  -0.594  58.686  1.00 314.44 ? 264  ASP B C   1 
ATOM   14334 O  O   . ASP C 1 264  ? 46.265  -0.169  59.046  1.00 314.30 ? 264  ASP B O   1 
ATOM   14335 C  CB  . ASP C 1 264  ? 44.453  -2.643  60.033  1.00 327.24 ? 264  ASP B CB  1 
ATOM   14336 C  CG  . ASP C 1 264  ? 43.003  -3.009  60.074  1.00 333.43 ? 264  ASP B CG  1 
ATOM   14337 O  OD1 . ASP C 1 264  ? 42.208  -2.369  59.374  1.00 330.58 ? 264  ASP B OD1 1 
ATOM   14338 O  OD2 . ASP C 1 264  ? 42.631  -3.930  60.839  1.00 341.28 ? 264  ASP B OD2 1 
ATOM   14339 N  N   . VAL C 1 265  ? 44.140  0.194   58.382  1.00 194.46 ? 265  VAL B N   1 
ATOM   14340 C  CA  . VAL C 1 265  ? 44.269  1.639   58.324  1.00 189.10 ? 265  VAL B CA  1 
ATOM   14341 C  C   . VAL C 1 265  ? 43.377  2.308   59.394  1.00 191.13 ? 265  VAL B C   1 
ATOM   14342 O  O   . VAL C 1 265  ? 42.181  2.055   59.456  1.00 192.08 ? 265  VAL B O   1 
ATOM   14343 C  CB  . VAL C 1 265  ? 43.938  2.125   56.894  1.00 175.24 ? 265  VAL B CB  1 
ATOM   14344 C  CG1 . VAL C 1 265  ? 43.897  3.623   56.817  1.00 170.15 ? 265  VAL B CG1 1 
ATOM   14345 C  CG2 . VAL C 1 265  ? 44.970  1.596   55.940  1.00 173.47 ? 265  VAL B CG2 1 
ATOM   14346 N  N   . TYR C 1 266  ? 43.950  3.137   60.258  1.00 279.59 ? 266  TYR B N   1 
ATOM   14347 C  CA  . TYR C 1 266  ? 43.119  3.863   61.213  1.00 282.58 ? 266  TYR B CA  1 
ATOM   14348 C  C   . TYR C 1 266  ? 43.362  5.357   61.105  1.00 276.24 ? 266  TYR B C   1 
ATOM   14349 O  O   . TYR C 1 266  ? 44.479  5.823   61.315  1.00 278.14 ? 266  TYR B O   1 
ATOM   14350 C  CB  . TYR C 1 266  ? 43.350  3.385   62.650  1.00 296.48 ? 266  TYR B CB  1 
ATOM   14351 C  CG  . TYR C 1 266  ? 42.686  2.065   62.982  1.00 308.13 ? 266  TYR B CG  1 
ATOM   14352 C  CD1 . TYR C 1 266  ? 43.092  0.893   62.361  1.00 313.80 ? 266  TYR B CD1 1 
ATOM   14353 C  CD2 . TYR C 1 266  ? 41.663  1.985   63.926  1.00 316.06 ? 266  TYR B CD2 1 
ATOM   14354 C  CE1 . TYR C 1 266  ? 42.496  -0.326  62.659  1.00 319.73 ? 266  TYR B CE1 1 
ATOM   14355 C  CE2 . TYR C 1 266  ? 41.057  0.765   64.231  1.00 322.25 ? 266  TYR B CE2 1 
ATOM   14356 C  CZ  . TYR C 1 266  ? 41.479  -0.387  63.593  1.00 324.14 ? 266  TYR B CZ  1 
ATOM   14357 O  OH  . TYR C 1 266  ? 40.886  -1.596  63.890  1.00 327.97 ? 266  TYR B OH  1 
ATOM   14358 N  N   . ILE C 1 267  ? 42.319  6.112   60.777  1.00 161.24 ? 267  ILE B N   1 
ATOM   14359 C  CA  . ILE C 1 267  ? 42.495  7.541   60.570  1.00 153.49 ? 267  ILE B CA  1 
ATOM   14360 C  C   . ILE C 1 267  ? 41.571  8.433   61.385  1.00 153.33 ? 267  ILE B C   1 
ATOM   14361 O  O   . ILE C 1 267  ? 40.362  8.492   61.149  1.00 153.87 ? 267  ILE B O   1 
ATOM   14362 C  CB  . ILE C 1 267  ? 42.300  7.906   59.112  1.00 150.09 ? 267  ILE B CB  1 
ATOM   14363 C  CG1 . ILE C 1 267  ? 43.193  7.048   58.231  1.00 146.94 ? 267  ILE B CG1 1 
ATOM   14364 C  CG2 . ILE C 1 267  ? 42.653  9.344   58.921  1.00 149.09 ? 267  ILE B CG2 1 
ATOM   14365 C  CD1 . ILE C 1 267  ? 43.009  7.333   56.789  1.00 144.13 ? 267  ILE B CD1 1 
ATOM   14366 N  N   . THR C 1 268  ? 42.139  9.153   62.335  1.00 214.32 ? 268  THR B N   1 
ATOM   14367 C  CA  . THR C 1 268  ? 41.326  10.116  63.050  1.00 214.13 ? 268  THR B CA  1 
ATOM   14368 C  C   . THR C 1 268  ? 41.390  11.477  62.356  1.00 211.93 ? 268  THR B C   1 
ATOM   14369 O  O   . THR C 1 268  ? 42.221  11.689  61.480  1.00 211.26 ? 268  THR B O   1 
ATOM   14370 C  CB  . THR C 1 268  ? 41.690  10.191  64.567  1.00 223.05 ? 268  THR B CB  1 
ATOM   14371 O  OG1 . THR C 1 268  ? 43.076  10.518  64.738  1.00 226.41 ? 268  THR B OG1 1 
ATOM   14372 C  CG2 . THR C 1 268  ? 41.406  8.859   65.246  1.00 226.64 ? 268  THR B CG2 1 
ATOM   14373 N  N   . PHE C 1 269  ? 40.494  12.383  62.731  1.00 241.59 ? 269  PHE B N   1 
ATOM   14374 C  CA  . PHE C 1 269  ? 40.568  13.757  62.263  1.00 235.08 ? 269  PHE B CA  1 
ATOM   14375 C  C   . PHE C 1 269  ? 40.333  14.677  63.409  1.00 231.43 ? 269  PHE B C   1 
ATOM   14376 O  O   . PHE C 1 269  ? 39.962  14.238  64.490  1.00 236.70 ? 269  PHE B O   1 
ATOM   14377 C  CB  . PHE C 1 269  ? 39.495  14.029  61.256  1.00 231.13 ? 269  PHE B CB  1 
ATOM   14378 C  CG  . PHE C 1 269  ? 39.474  13.066  60.162  1.00 228.02 ? 269  PHE B CG  1 
ATOM   14379 C  CD1 . PHE C 1 269  ? 38.643  11.980  60.223  1.00 227.74 ? 269  PHE B CD1 1 
ATOM   14380 C  CD2 . PHE C 1 269  ? 40.297  13.237  59.064  1.00 224.93 ? 269  PHE B CD2 1 
ATOM   14381 C  CE1 . PHE C 1 269  ? 38.619  11.081  59.204  1.00 225.43 ? 269  PHE B CE1 1 
ATOM   14382 C  CE2 . PHE C 1 269  ? 40.281  12.344  58.034  1.00 222.39 ? 269  PHE B CE2 1 
ATOM   14383 C  CZ  . PHE C 1 269  ? 39.440  11.259  58.099  1.00 222.86 ? 269  PHE B CZ  1 
ATOM   14384 N  N   . GLY C 1 270  ? 40.507  15.966  63.177  1.00 226.96 ? 270  GLY B N   1 
ATOM   14385 C  CA  . GLY C 1 270  ? 40.346  16.892  64.271  1.00 228.34 ? 270  GLY B CA  1 
ATOM   14386 C  C   . GLY C 1 270  ? 40.029  18.310  63.883  1.00 221.70 ? 270  GLY B C   1 
ATOM   14387 O  O   . GLY C 1 270  ? 40.211  18.705  62.734  1.00 220.44 ? 270  GLY B O   1 
ATOM   14388 N  N   . ILE C 1 271  ? 39.511  19.057  64.855  1.00 178.11 ? 271  ILE B N   1 
ATOM   14389 C  CA  . ILE C 1 271  ? 39.481  20.499  64.788  1.00 169.61 ? 271  ILE B CA  1 
ATOM   14390 C  C   . ILE C 1 271  ? 40.625  21.000  65.691  1.00 176.38 ? 271  ILE B C   1 
ATOM   14391 O  O   . ILE C 1 271  ? 41.438  20.206  66.150  1.00 180.79 ? 271  ILE B O   1 
ATOM   14392 C  CB  . ILE C 1 271  ? 38.096  21.059  65.149  1.00 163.50 ? 271  ILE B CB  1 
ATOM   14393 C  CG1 . ILE C 1 271  ? 36.992  20.117  64.661  1.00 158.08 ? 271  ILE B CG1 1 
ATOM   14394 C  CG2 . ILE C 1 271  ? 37.903  22.378  64.462  1.00 160.69 ? 271  ILE B CG2 1 
ATOM   14395 C  CD1 . ILE C 1 271  ? 36.800  20.118  63.170  1.00 149.12 ? 271  ILE B CD1 1 
ATOM   14396 N  N   . ARG C 1 272  ? 40.719  22.301  65.919  1.00 197.58 ? 272  ARG B N   1 
ATOM   14397 C  CA  . ARG C 1 272  ? 41.911  22.860  66.538  1.00 209.66 ? 272  ARG B CA  1 
ATOM   14398 C  C   . ARG C 1 272  ? 41.699  24.334  66.641  1.00 217.75 ? 272  ARG B C   1 
ATOM   14399 O  O   . ARG C 1 272  ? 40.591  24.808  66.446  1.00 214.23 ? 272  ARG B O   1 
ATOM   14400 C  CB  . ARG C 1 272  ? 43.118  22.609  65.653  1.00 205.85 ? 272  ARG B CB  1 
ATOM   14401 C  CG  . ARG C 1 272  ? 44.449  22.926  66.282  1.00 208.65 ? 272  ARG B CG  1 
ATOM   14402 C  CD  . ARG C 1 272  ? 45.448  21.962  65.700  1.00 206.19 ? 272  ARG B CD  1 
ATOM   14403 N  NE  . ARG C 1 272  ? 46.797  22.121  66.222  1.00 206.62 ? 272  ARG B NE  1 
ATOM   14404 C  CZ  . ARG C 1 272  ? 47.798  21.286  65.945  1.00 208.55 ? 272  ARG B CZ  1 
ATOM   14405 N  NH1 . ARG C 1 272  ? 47.586  20.234  65.157  1.00 209.69 ? 272  ARG B NH1 1 
ATOM   14406 N  NH2 . ARG C 1 272  ? 49.009  21.498  66.456  1.00 209.04 ? 272  ARG B NH2 1 
ATOM   14407 N  N   . GLU C 1 273  ? 42.754  25.069  66.941  1.00 207.96 ? 273  GLU B N   1 
ATOM   14408 C  CA  . GLU C 1 273  ? 42.639  26.503  66.894  1.00 212.31 ? 273  GLU B CA  1 
ATOM   14409 C  C   . GLU C 1 273  ? 43.789  27.044  66.101  1.00 207.65 ? 273  GLU B C   1 
ATOM   14410 O  O   . GLU C 1 273  ? 43.594  27.799  65.155  1.00 203.54 ? 273  GLU B O   1 
ATOM   14411 C  CB  . GLU C 1 273  ? 42.583  27.123  68.293  1.00 224.79 ? 273  GLU B CB  1 
ATOM   14412 C  CG  . GLU C 1 273  ? 41.159  27.329  68.810  1.00 233.92 ? 273  GLU B CG  1 
ATOM   14413 C  CD  . GLU C 1 273  ? 40.128  27.352  67.683  1.00 232.65 ? 273  GLU B CD  1 
ATOM   14414 O  OE1 . GLU C 1 273  ? 40.137  28.316  66.883  1.00 229.22 ? 273  GLU B OE1 1 
ATOM   14415 O  OE2 . GLU C 1 273  ? 39.315  26.400  67.597  1.00 231.73 ? 273  GLU B OE2 1 
ATOM   14416 N  N   . ASP C 1 274  ? 44.989  26.633  66.471  1.00 281.68 ? 274  ASP B N   1 
ATOM   14417 C  CA  . ASP C 1 274  ? 46.179  27.100  65.788  1.00 277.19 ? 274  ASP B CA  1 
ATOM   14418 C  C   . ASP C 1 274  ? 47.203  25.990  65.754  1.00 279.81 ? 274  ASP B C   1 
ATOM   14419 O  O   . ASP C 1 274  ? 46.881  24.836  66.037  1.00 281.20 ? 274  ASP B O   1 
ATOM   14420 C  CB  . ASP C 1 274  ? 46.757  28.360  66.456  1.00 279.29 ? 274  ASP B CB  1 
ATOM   14421 C  CG  . ASP C 1 274  ? 46.957  28.204  67.962  1.00 317.27 ? 274  ASP B CG  1 
ATOM   14422 O  OD1 . ASP C 1 274  ? 47.928  28.786  68.490  1.00 318.74 ? 274  ASP B OD1 1 
ATOM   14423 O  OD2 . ASP C 1 274  ? 46.144  27.521  68.622  1.00 321.81 ? 274  ASP B OD2 1 
ATOM   14424 N  N   . LEU C 1 275  ? 48.429  26.342  65.379  1.00 191.79 ? 275  LEU B N   1 
ATOM   14425 C  CA  . LEU C 1 275  ? 49.538  25.386  65.396  1.00 196.63 ? 275  LEU B CA  1 
ATOM   14426 C  C   . LEU C 1 275  ? 50.372  25.439  66.723  1.00 209.52 ? 275  LEU B C   1 
ATOM   14427 O  O   . LEU C 1 275  ? 51.269  24.614  66.944  1.00 211.82 ? 275  LEU B O   1 
ATOM   14428 C  CB  . LEU C 1 275  ? 50.407  25.502  64.110  1.00 186.67 ? 275  LEU B CB  1 
ATOM   14429 C  CG  . LEU C 1 275  ? 49.861  25.160  62.701  1.00 178.44 ? 275  LEU B CG  1 
ATOM   14430 C  CD1 . LEU C 1 275  ? 50.994  24.699  61.795  1.00 173.80 ? 275  LEU B CD1 1 
ATOM   14431 C  CD2 . LEU C 1 275  ? 48.751  24.114  62.711  1.00 180.03 ? 275  LEU B CD2 1 
ATOM   14432 N  N   . LYS C 1 276  ? 50.053  26.393  67.601  1.00 217.16 ? 276  LYS B N   1 
ATOM   14433 C  CA  . LYS C 1 276  ? 50.726  26.539  68.898  1.00 228.07 ? 276  LYS B CA  1 
ATOM   14434 C  C   . LYS C 1 276  ? 49.889  25.878  70.003  1.00 243.22 ? 276  LYS B C   1 
ATOM   14435 O  O   . LYS C 1 276  ? 50.194  25.994  71.192  1.00 252.43 ? 276  LYS B O   1 
ATOM   14436 C  CB  . LYS C 1 276  ? 50.959  28.028  69.207  1.00 222.17 ? 276  LYS B CB  1 
ATOM   14437 C  CG  . LYS C 1 276  ? 52.166  28.347  70.094  1.00 221.59 ? 276  LYS B CG  1 
ATOM   14438 C  CD  . LYS C 1 276  ? 52.366  29.866  70.273  1.00 215.32 ? 276  LYS B CD  1 
ATOM   14439 C  CE  . LYS C 1 276  ? 51.340  30.489  71.229  1.00 212.10 ? 276  LYS B CE  1 
ATOM   14440 N  NZ  . LYS C 1 276  ? 51.454  29.973  72.639  1.00 217.62 ? 276  LYS B NZ  1 
ATOM   14441 N  N   . ASP C 1 277  ? 48.820  25.199  69.588  1.00 241.14 ? 277  ASP B N   1 
ATOM   14442 C  CA  . ASP C 1 277  ? 47.905  24.511  70.500  1.00 255.29 ? 277  ASP B CA  1 
ATOM   14443 C  C   . ASP C 1 277  ? 48.202  23.010  70.516  1.00 260.57 ? 277  ASP B C   1 
ATOM   14444 O  O   . ASP C 1 277  ? 47.967  22.311  69.530  1.00 258.41 ? 277  ASP B O   1 
ATOM   14445 C  CB  . ASP C 1 277  ? 46.446  24.766  70.078  1.00 259.84 ? 277  ASP B CB  1 
ATOM   14446 C  CG  . ASP C 1 277  ? 45.434  24.279  71.108  1.00 273.49 ? 277  ASP B CG  1 
ATOM   14447 O  OD1 . ASP C 1 277  ? 45.852  23.900  72.212  1.00 282.51 ? 277  ASP B OD1 1 
ATOM   14448 O  OD2 . ASP C 1 277  ? 44.218  24.281  70.820  1.00 274.71 ? 277  ASP B OD2 1 
ATOM   14449 N  N   . ASP C 1 278  ? 48.725  22.522  71.639  1.00 350.32 ? 278  ASP B N   1 
ATOM   14450 C  CA  . ASP C 1 278  ? 49.027  21.100  71.804  1.00 352.37 ? 278  ASP B CA  1 
ATOM   14451 C  C   . ASP C 1 278  ? 47.766  20.242  71.950  1.00 351.07 ? 278  ASP B C   1 
ATOM   14452 O  O   . ASP C 1 278  ? 47.847  19.013  72.039  1.00 352.98 ? 278  ASP B O   1 
ATOM   14453 C  CB  . ASP C 1 278  ? 50.007  20.862  72.973  1.00 390.79 ? 278  ASP B CB  1 
ATOM   14454 C  CG  . ASP C 1 278  ? 49.665  21.675  74.225  1.00 393.99 ? 278  ASP B CG  1 
ATOM   14455 O  OD1 . ASP C 1 278  ? 48.566  22.263  74.292  1.00 391.84 ? 278  ASP B OD1 1 
ATOM   14456 O  OD2 . ASP C 1 278  ? 50.507  21.722  75.151  1.00 398.37 ? 278  ASP B OD2 1 
ATOM   14457 N  N   . GLN C 1 279  ? 46.604  20.897  71.957  1.00 225.02 ? 279  GLN B N   1 
ATOM   14458 C  CA  . GLN C 1 279  ? 45.324  20.213  72.144  1.00 223.03 ? 279  GLN B CA  1 
ATOM   14459 C  C   . GLN C 1 279  ? 44.227  20.652  71.181  1.00 209.15 ? 279  GLN B C   1 
ATOM   14460 O  O   . GLN C 1 279  ? 43.874  21.833  71.073  1.00 202.23 ? 279  GLN B O   1 
ATOM   14461 C  CB  . GLN C 1 279  ? 44.816  20.347  73.578  1.00 235.44 ? 279  GLN B CB  1 
ATOM   14462 C  CG  . GLN C 1 279  ? 43.450  19.710  73.795  1.00 240.70 ? 279  GLN B CG  1 
ATOM   14463 C  CD  . GLN C 1 279  ? 43.462  18.220  73.526  1.00 242.30 ? 279  GLN B CD  1 
ATOM   14464 O  OE1 . GLN C 1 279  ? 42.573  17.692  72.859  1.00 236.58 ? 279  GLN B OE1 1 
ATOM   14465 N  NE2 . GLN C 1 279  ? 44.479  17.532  74.036  1.00 250.15 ? 279  GLN B NE2 1 
ATOM   14466 N  N   . LYS C 1 280  ? 43.666  19.645  70.528  1.00 244.92 ? 280  LYS B N   1 
ATOM   14467 C  CA  . LYS C 1 280  ? 42.719  19.811  69.445  1.00 231.87 ? 280  LYS B CA  1 
ATOM   14468 C  C   . LYS C 1 280  ? 41.547  18.857  69.651  1.00 230.31 ? 280  LYS B C   1 
ATOM   14469 O  O   . LYS C 1 280  ? 41.732  17.658  69.846  1.00 233.97 ? 280  LYS B O   1 
ATOM   14470 C  CB  . LYS C 1 280  ? 43.414  19.518  68.112  1.00 221.33 ? 280  LYS B CB  1 
ATOM   14471 C  CG  . LYS C 1 280  ? 44.155  18.166  68.048  1.00 217.30 ? 280  LYS B CG  1 
ATOM   14472 C  CD  . LYS C 1 280  ? 45.565  18.232  68.670  1.00 220.19 ? 280  LYS B CD  1 
ATOM   14473 C  CE  . LYS C 1 280  ? 46.353  16.925  68.506  1.00 219.39 ? 280  LYS B CE  1 
ATOM   14474 N  NZ  . LYS C 1 280  ? 47.751  17.042  69.024  1.00 223.21 ? 280  LYS B NZ  1 
ATOM   14475 N  N   . GLU C 1 281  ? 40.339  19.395  69.592  1.00 200.82 ? 281  GLU B N   1 
ATOM   14476 C  CA  . GLU C 1 281  ? 39.154  18.639  69.964  1.00 201.71 ? 281  GLU B CA  1 
ATOM   14477 C  C   . GLU C 1 281  ? 38.624  17.764  68.841  1.00 188.99 ? 281  GLU B C   1 
ATOM   14478 O  O   . GLU C 1 281  ? 37.761  18.173  68.067  1.00 180.72 ? 281  GLU B O   1 
ATOM   14479 C  CB  . GLU C 1 281  ? 38.078  19.600  70.451  1.00 210.47 ? 281  GLU B CB  1 
ATOM   14480 C  CG  . GLU C 1 281  ? 38.663  20.799  71.187  1.00 226.85 ? 281  GLU B CG  1 
ATOM   14481 C  CD  . GLU C 1 281  ? 39.570  20.400  72.337  1.00 245.95 ? 281  GLU B CD  1 
ATOM   14482 O  OE1 . GLU C 1 281  ? 39.401  19.290  72.886  1.00 251.86 ? 281  GLU B OE1 1 
ATOM   14483 O  OE2 . GLU C 1 281  ? 40.455  21.202  72.691  1.00 254.19 ? 281  GLU B OE2 1 
ATOM   14484 N  N   . MET C 1 282  ? 39.140  16.545  68.789  1.00 178.14 ? 282  MET B N   1 
ATOM   14485 C  CA  . MET C 1 282  ? 38.725  15.568  67.809  1.00 173.38 ? 282  MET B CA  1 
ATOM   14486 C  C   . MET C 1 282  ? 37.248  15.532  67.517  1.00 172.00 ? 282  MET B C   1 
ATOM   14487 O  O   . MET C 1 282  ? 36.425  16.291  68.040  1.00 173.93 ? 282  MET B O   1 
ATOM   14488 C  CB  . MET C 1 282  ? 39.096  14.156  68.251  1.00 176.84 ? 282  MET B CB  1 
ATOM   14489 C  CG  . MET C 1 282  ? 40.567  13.862  68.350  1.00 179.65 ? 282  MET B CG  1 
ATOM   14490 S  SD  . MET C 1 282  ? 41.393  13.408  66.832  1.00 180.18 ? 282  MET B SD  1 
ATOM   14491 C  CE  . MET C 1 282  ? 42.513  14.805  66.755  1.00 159.45 ? 282  MET B CE  1 
ATOM   14492 N  N   . MET C 1 283  ? 36.956  14.557  66.672  1.00 204.46 ? 283  MET B N   1 
ATOM   14493 C  CA  . MET C 1 283  ? 35.672  14.348  66.055  1.00 207.64 ? 283  MET B CA  1 
ATOM   14494 C  C   . MET C 1 283  ? 35.443  12.866  66.216  1.00 219.49 ? 283  MET B C   1 
ATOM   14495 O  O   . MET C 1 283  ? 36.398  12.091  66.283  1.00 220.35 ? 283  MET B O   1 
ATOM   14496 C  CB  . MET C 1 283  ? 35.728  14.736  64.552  1.00 199.68 ? 283  MET B CB  1 
ATOM   14497 C  CG  . MET C 1 283  ? 35.916  16.274  64.308  1.00 211.85 ? 283  MET B CG  1 
ATOM   14498 S  SD  . MET C 1 283  ? 36.267  16.973  62.649  1.00 143.06 ? 283  MET B SD  1 
ATOM   14499 C  CE  . MET C 1 283  ? 37.765  16.104  62.250  1.00 138.52 ? 283  MET B CE  1 
ATOM   14500 N  N   . GLN C 1 284  ? 34.179  12.486  66.331  1.00 277.34 ? 284  GLN B N   1 
ATOM   14501 C  CA  . GLN C 1 284  ? 33.785  11.096  66.267  1.00 285.47 ? 284  GLN B CA  1 
ATOM   14502 C  C   . GLN C 1 284  ? 33.408  10.778  64.816  1.00 283.89 ? 284  GLN B C   1 
ATOM   14503 O  O   . GLN C 1 284  ? 33.382  11.667  63.964  1.00 280.46 ? 284  GLN B O   1 
ATOM   14504 C  CB  . GLN C 1 284  ? 32.630  10.825  67.237  1.00 290.77 ? 284  GLN B CB  1 
ATOM   14505 C  CG  . GLN C 1 284  ? 31.421  11.756  67.080  1.00 287.65 ? 284  GLN B CG  1 
ATOM   14506 C  CD  . GLN C 1 284  ? 31.595  13.125  67.745  1.00 288.22 ? 284  GLN B CD  1 
ATOM   14507 O  OE1 . GLN C 1 284  ? 32.704  13.651  67.857  1.00 286.28 ? 284  GLN B OE1 1 
ATOM   14508 N  NE2 . GLN C 1 284  ? 30.482  13.708  68.182  1.00 291.45 ? 284  GLN B NE2 1 
ATOM   14509 N  N   . THR C 1 285  ? 33.149  9.509   64.526  1.00 282.36 ? 285  THR B N   1 
ATOM   14510 C  CA  . THR C 1 285  ? 32.807  9.095   63.167  1.00 279.44 ? 285  THR B CA  1 
ATOM   14511 C  C   . THR C 1 285  ? 33.910  9.427   62.163  1.00 273.74 ? 285  THR B C   1 
ATOM   14512 O  O   . THR C 1 285  ? 33.629  9.790   61.021  1.00 267.80 ? 285  THR B O   1 
ATOM   14513 C  CB  . THR C 1 285  ? 31.506  9.744   62.690  1.00 280.23 ? 285  THR B CB  1 
ATOM   14514 O  OG1 . THR C 1 285  ? 30.590  9.827   63.785  1.00 285.97 ? 285  THR B OG1 1 
ATOM   14515 C  CG2 . THR C 1 285  ? 30.890  8.925   61.566  1.00 279.26 ? 285  THR B CG2 1 
ATOM   14516 N  N   . ALA C 1 286  ? 35.159  9.318   62.611  1.00 313.98 ? 286  ALA B N   1 
ATOM   14517 C  CA  . ALA C 1 286  ? 36.328  9.425   61.741  1.00 308.29 ? 286  ALA B CA  1 
ATOM   14518 C  C   . ALA C 1 286  ? 36.742  8.027   61.276  1.00 305.51 ? 286  ALA B C   1 
ATOM   14519 O  O   . ALA C 1 286  ? 37.209  7.212   62.069  1.00 306.83 ? 286  ALA B O   1 
ATOM   14520 C  CB  . ALA C 1 286  ? 37.469  10.115  62.466  1.00 311.17 ? 286  ALA B CB  1 
ATOM   14521 N  N   . MET C 1 287  ? 36.590  7.776   59.979  1.00 249.72 ? 287  MET B N   1 
ATOM   14522 C  CA  . MET C 1 287  ? 36.620  6.427   59.410  1.00 247.16 ? 287  MET B CA  1 
ATOM   14523 C  C   . MET C 1 287  ? 37.823  5.536   59.691  1.00 251.08 ? 287  MET B C   1 
ATOM   14524 O  O   . MET C 1 287  ? 38.963  5.840   59.326  1.00 250.53 ? 287  MET B O   1 
ATOM   14525 C  CB  . MET C 1 287  ? 36.372  6.483   57.908  1.00 239.13 ? 287  MET B CB  1 
ATOM   14526 C  CG  . MET C 1 287  ? 34.992  6.979   57.570  1.00 234.49 ? 287  MET B CG  1 
ATOM   14527 S  SD  . MET C 1 287  ? 34.902  7.704   55.918  1.00 269.32 ? 287  MET B SD  1 
ATOM   14528 C  CE  . MET C 1 287  ? 36.065  9.065   56.041  1.00 231.03 ? 287  MET B CE  1 
ATOM   14529 N  N   . GLN C 1 288  ? 37.515  4.410   60.327  1.00 462.42 ? 288  GLN B N   1 
ATOM   14530 C  CA  . GLN C 1 288  ? 38.450  3.317   60.525  1.00 467.39 ? 288  GLN B CA  1 
ATOM   14531 C  C   . GLN C 1 288  ? 38.525  2.471   59.255  1.00 467.04 ? 288  GLN B C   1 
ATOM   14532 O  O   . GLN C 1 288  ? 37.660  2.562   58.383  1.00 465.10 ? 288  GLN B O   1 
ATOM   14533 C  CB  . GLN C 1 288  ? 38.013  2.451   61.723  1.00 473.99 ? 288  GLN B CB  1 
ATOM   14534 C  CG  . GLN C 1 288  ? 36.524  2.058   61.727  1.00 478.17 ? 288  GLN B CG  1 
ATOM   14535 C  CD  . GLN C 1 288  ? 36.132  1.146   62.891  1.00 485.19 ? 288  GLN B CD  1 
ATOM   14536 O  OE1 . GLN C 1 288  ? 36.982  0.508   63.515  1.00 488.70 ? 288  GLN B OE1 1 
ATOM   14537 N  NE2 . GLN C 1 288  ? 34.835  1.075   63.176  1.00 487.43 ? 288  GLN B NE2 1 
ATOM   14538 N  N   . ASN C 1 289  ? 39.588  1.681   59.151  1.00 281.72 ? 289  ASN B N   1 
ATOM   14539 C  CA  . ASN C 1 289  ? 39.728  0.625   58.143  1.00 283.43 ? 289  ASN B CA  1 
ATOM   14540 C  C   . ASN C 1 289  ? 39.223  0.894   56.712  1.00 273.37 ? 289  ASN B C   1 
ATOM   14541 O  O   . ASN C 1 289  ? 38.020  0.998   56.458  1.00 268.52 ? 289  ASN B O   1 
ATOM   14542 C  CB  . ASN C 1 289  ? 39.149  -0.705  58.675  1.00 294.68 ? 289  ASN B CB  1 
ATOM   14543 C  CG  . ASN C 1 289  ? 39.616  -1.032  60.094  1.00 305.20 ? 289  ASN B CG  1 
ATOM   14544 O  OD1 . ASN C 1 289  ? 40.480  -0.356  60.647  1.00 308.64 ? 289  ASN B OD1 1 
ATOM   14545 N  ND2 . ASN C 1 289  ? 39.035  -2.069  60.685  1.00 309.88 ? 289  ASN B ND2 1 
ATOM   14546 N  N   . THR C 1 290  ? 40.171  1.002   55.788  1.00 172.29 ? 290  THR B N   1 
ATOM   14547 C  CA  . THR C 1 290  ? 39.907  0.735   54.370  1.00 167.07 ? 290  THR B CA  1 
ATOM   14548 C  C   . THR C 1 290  ? 41.082  -0.099  53.829  1.00 165.06 ? 290  THR B C   1 
ATOM   14549 O  O   . THR C 1 290  ? 41.275  -0.271  52.615  1.00 164.58 ? 290  THR B O   1 
ATOM   14550 C  CB  . THR C 1 290  ? 39.568  2.018   53.538  1.00 146.70 ? 290  THR B CB  1 
ATOM   14551 O  OG1 . THR C 1 290  ? 38.147  2.193   53.513  1.00 145.04 ? 290  THR B OG1 1 
ATOM   14552 C  CG2 . THR C 1 290  ? 40.058  1.929   52.088  1.00 148.88 ? 290  THR B CG2 1 
ATOM   14553 N  N   . MET C 1 291  ? 41.855  -0.624  54.777  1.00 280.92 ? 291  MET B N   1 
ATOM   14554 C  CA  . MET C 1 291  ? 42.963  -1.525  54.490  1.00 279.77 ? 291  MET B CA  1 
ATOM   14555 C  C   . MET C 1 291  ? 43.894  -0.955  53.437  1.00 271.95 ? 291  MET B C   1 
ATOM   14556 O  O   . MET C 1 291  ? 43.560  -0.889  52.253  1.00 269.03 ? 291  MET B O   1 
ATOM   14557 C  CB  . MET C 1 291  ? 42.461  -2.912  54.081  1.00 283.86 ? 291  MET B CB  1 
ATOM   14558 C  CG  . MET C 1 291  ? 41.713  -3.637  55.183  1.00 288.65 ? 291  MET B CG  1 
ATOM   14559 S  SD  . MET C 1 291  ? 41.360  -5.337  54.724  1.00 315.25 ? 291  MET B SD  1 
ATOM   14560 C  CE  . MET C 1 291  ? 40.856  -5.099  53.028  1.00 307.58 ? 291  MET B CE  1 
ATOM   14561 N  N   . LEU C 1 292  ? 45.060  -0.517  53.892  1.00 284.20 ? 292  LEU B N   1 
ATOM   14562 C  CA  . LEU C 1 292  ? 46.091  -0.073  52.985  1.00 277.76 ? 292  LEU B CA  1 
ATOM   14563 C  C   . LEU C 1 292  ? 46.168  -1.173  51.969  1.00 272.93 ? 292  LEU B C   1 
ATOM   14564 O  O   . LEU C 1 292  ? 46.262  -2.346  52.329  1.00 276.31 ? 292  LEU B O   1 
ATOM   14565 C  CB  . LEU C 1 292  ? 47.428  0.043   53.710  1.00 281.56 ? 292  LEU B CB  1 
ATOM   14566 C  CG  . LEU C 1 292  ? 48.585  0.654   52.914  1.00 280.37 ? 292  LEU B CG  1 
ATOM   14567 C  CD1 . LEU C 1 292  ? 48.985  -0.211  51.732  1.00 280.20 ? 292  LEU B CD1 1 
ATOM   14568 C  CD2 . LEU C 1 292  ? 48.223  2.050   52.454  1.00 274.65 ? 292  LEU B CD2 1 
ATOM   14569 N  N   . ILE C 1 293  ? 46.109  -0.810  50.699  1.00 217.97 ? 293  ILE B N   1 
ATOM   14570 C  CA  . ILE C 1 293  ? 46.155  -1.825  49.661  1.00 213.26 ? 293  ILE B CA  1 
ATOM   14571 C  C   . ILE C 1 293  ? 47.179  -1.540  48.556  1.00 210.11 ? 293  ILE B C   1 
ATOM   14572 O  O   . ILE C 1 293  ? 46.966  -0.731  47.658  1.00 206.34 ? 293  ILE B O   1 
ATOM   14573 C  CB  . ILE C 1 293  ? 44.744  -2.156  49.130  1.00 208.92 ? 293  ILE B CB  1 
ATOM   14574 C  CG1 . ILE C 1 293  ? 43.921  -2.802  50.259  1.00 208.53 ? 293  ILE B CG1 1 
ATOM   14575 C  CG2 . ILE C 1 293  ? 44.844  -3.073  47.923  1.00 209.57 ? 293  ILE B CG2 1 
ATOM   14576 C  CD1 . ILE C 1 293  ? 42.407  -2.786  50.073  1.00 205.21 ? 293  ILE B CD1 1 
ATOM   14577 N  N   . ASN C 1 294  ? 48.289  -2.260  48.655  1.00 161.30 ? 294  ASN B N   1 
ATOM   14578 C  CA  . ASN C 1 294  ? 49.497  -2.036  47.871  1.00 162.33 ? 294  ASN B CA  1 
ATOM   14579 C  C   . ASN C 1 294  ? 50.097  -0.637  47.927  1.00 154.86 ? 294  ASN B C   1 
ATOM   14580 O  O   . ASN C 1 294  ? 50.151  0.084   46.931  1.00 151.42 ? 294  ASN B O   1 
ATOM   14581 C  CB  . ASN C 1 294  ? 49.352  -2.478  46.429  1.00 167.19 ? 294  ASN B CB  1 
ATOM   14582 C  CG  . ASN C 1 294  ? 50.684  -2.498  45.720  1.00 175.39 ? 294  ASN B CG  1 
ATOM   14583 O  OD1 . ASN C 1 294  ? 51.116  -1.497  45.143  1.00 175.40 ? 294  ASN B OD1 1 
ATOM   14584 N  ND2 . ASN C 1 294  ? 51.372  -3.629  45.804  1.00 181.70 ? 294  ASN B ND2 1 
ATOM   14585 N  N   . GLY C 1 295  ? 50.584  -0.281  49.104  1.00 248.82 ? 295  GLY B N   1 
ATOM   14586 C  CA  . GLY C 1 295  ? 51.299  0.964   49.271  1.00 245.98 ? 295  GLY B CA  1 
ATOM   14587 C  C   . GLY C 1 295  ? 50.389  2.156   49.143  1.00 238.92 ? 295  GLY B C   1 
ATOM   14588 O  O   . GLY C 1 295  ? 50.858  3.290   49.074  1.00 236.44 ? 295  GLY B O   1 
ATOM   14589 N  N   . ILE C 1 296  ? 49.087  1.896   49.093  1.00 185.51 ? 296  ILE B N   1 
ATOM   14590 C  CA  . ILE C 1 296  ? 48.104  2.973   49.177  1.00 177.67 ? 296  ILE B CA  1 
ATOM   14591 C  C   . ILE C 1 296  ? 46.721  2.510   49.714  1.00 179.68 ? 296  ILE B C   1 
ATOM   14592 O  O   . ILE C 1 296  ? 46.529  1.361   50.137  1.00 183.04 ? 296  ILE B O   1 
ATOM   14593 C  CB  . ILE C 1 296  ? 47.934  3.747   47.805  1.00 164.37 ? 296  ILE B CB  1 
ATOM   14594 C  CG1 . ILE C 1 296  ? 49.179  3.602   46.906  1.00 163.63 ? 296  ILE B CG1 1 
ATOM   14595 C  CG2 . ILE C 1 296  ? 47.579  5.216   48.041  1.00 155.79 ? 296  ILE B CG2 1 
ATOM   14596 C  CD1 . ILE C 1 296  ? 50.127  4.781   46.917  1.00 162.26 ? 296  ILE B CD1 1 
ATOM   14597 N  N   . ALA C 1 297  ? 45.806  3.473   49.771  1.00 172.90 ? 297  ALA B N   1 
ATOM   14598 C  CA  . ALA C 1 297  ? 44.362  3.280   49.838  1.00 169.80 ? 297  ALA B CA  1 
ATOM   14599 C  C   . ALA C 1 297  ? 43.876  4.716   49.795  1.00 168.60 ? 297  ALA B C   1 
ATOM   14600 O  O   . ALA C 1 297  ? 44.670  5.628   49.522  1.00 169.40 ? 297  ALA B O   1 
ATOM   14601 C  CB  . ALA C 1 297  ? 43.913  2.575   51.107  1.00 171.10 ? 297  ALA B CB  1 
ATOM   14602 N  N   . GLN C 1 298  ? 42.597  4.939   50.068  1.00 201.98 ? 298  GLN B N   1 
ATOM   14603 C  CA  . GLN C 1 298  ? 42.084  6.303   50.027  1.00 199.31 ? 298  GLN B CA  1 
ATOM   14604 C  C   . GLN C 1 298  ? 40.697  6.505   50.586  1.00 195.62 ? 298  GLN B C   1 
ATOM   14605 O  O   . GLN C 1 298  ? 39.983  5.540   50.887  1.00 197.05 ? 298  GLN B O   1 
ATOM   14606 C  CB  . GLN C 1 298  ? 42.049  6.794   48.599  1.00 200.01 ? 298  GLN B CB  1 
ATOM   14607 C  CG  . GLN C 1 298  ? 43.309  7.402   48.103  1.00 205.96 ? 298  GLN B CG  1 
ATOM   14608 C  CD  . GLN C 1 298  ? 43.144  7.854   46.679  1.00 209.06 ? 298  GLN B CD  1 
ATOM   14609 O  OE1 . GLN C 1 298  ? 42.027  7.908   46.159  1.00 209.84 ? 298  GLN B OE1 1 
ATOM   14610 N  NE2 . GLN C 1 298  ? 44.250  8.175   46.030  1.00 210.51 ? 298  GLN B NE2 1 
ATOM   14611 N  N   . VAL C 1 299  ? 40.329  7.784   50.672  1.00 129.04 ? 299  VAL B N   1 
ATOM   14612 C  CA  . VAL C 1 299  ? 38.999  8.210   51.093  1.00 126.23 ? 299  VAL B CA  1 
ATOM   14613 C  C   . VAL C 1 299  ? 38.712  9.671   50.755  1.00 125.03 ? 299  VAL B C   1 
ATOM   14614 O  O   . VAL C 1 299  ? 39.568  10.373  50.203  1.00 129.13 ? 299  VAL B O   1 
ATOM   14615 C  CB  . VAL C 1 299  ? 38.745  7.987   52.589  1.00 129.02 ? 299  VAL B CB  1 
ATOM   14616 C  CG1 . VAL C 1 299  ? 38.130  6.603   52.838  1.00 129.20 ? 299  VAL B CG1 1 
ATOM   14617 C  CG2 . VAL C 1 299  ? 40.026  8.192   53.378  1.00 131.94 ? 299  VAL B CG2 1 
ATOM   14618 N  N   . THR C 1 300  ? 37.488  10.102  51.074  1.00 201.72 ? 300  THR B N   1 
ATOM   14619 C  CA  . THR C 1 300  ? 37.014  11.459  50.801  1.00 198.52 ? 300  THR B CA  1 
ATOM   14620 C  C   . THR C 1 300  ? 36.035  11.889  51.879  1.00 203.78 ? 300  THR B C   1 
ATOM   14621 O  O   . THR C 1 300  ? 35.077  11.186  52.205  1.00 202.78 ? 300  THR B O   1 
ATOM   14622 C  CB  . THR C 1 300  ? 36.345  11.561  49.428  1.00 233.47 ? 300  THR B CB  1 
ATOM   14623 O  OG1 . THR C 1 300  ? 35.448  10.456  49.259  1.00 235.04 ? 300  THR B OG1 1 
ATOM   14624 C  CG2 . THR C 1 300  ? 37.392  11.545  48.314  1.00 231.83 ? 300  THR B CG2 1 
ATOM   14625 N  N   . PHE C 1 301  ? 36.278  13.060  52.429  1.00 150.07 ? 301  PHE B N   1 
ATOM   14626 C  CA  . PHE C 1 301  ? 35.766  13.332  53.749  1.00 160.40 ? 301  PHE B CA  1 
ATOM   14627 C  C   . PHE C 1 301  ? 34.817  14.535  53.735  1.00 167.52 ? 301  PHE B C   1 
ATOM   14628 O  O   . PHE C 1 301  ? 35.224  15.678  53.938  1.00 170.87 ? 301  PHE B O   1 
ATOM   14629 C  CB  . PHE C 1 301  ? 36.983  13.405  54.697  1.00 159.95 ? 301  PHE B CB  1 
ATOM   14630 C  CG  . PHE C 1 301  ? 36.805  14.249  55.912  1.00 157.87 ? 301  PHE B CG  1 
ATOM   14631 C  CD1 . PHE C 1 301  ? 36.256  13.726  57.052  1.00 158.90 ? 301  PHE B CD1 1 
ATOM   14632 C  CD2 . PHE C 1 301  ? 37.270  15.567  55.931  1.00 156.13 ? 301  PHE B CD2 1 
ATOM   14633 C  CE1 . PHE C 1 301  ? 36.130  14.521  58.162  1.00 160.85 ? 301  PHE B CE1 1 
ATOM   14634 C  CE2 . PHE C 1 301  ? 37.152  16.369  57.043  1.00 156.96 ? 301  PHE B CE2 1 
ATOM   14635 C  CZ  . PHE C 1 301  ? 36.584  15.850  58.154  1.00 160.27 ? 301  PHE B CZ  1 
ATOM   14636 N  N   . ASP C 1 302  ? 33.545  14.247  53.445  1.00 179.64 ? 302  ASP B N   1 
ATOM   14637 C  CA  . ASP C 1 302  ? 32.473  15.246  53.475  1.00 180.66 ? 302  ASP B CA  1 
ATOM   14638 C  C   . ASP C 1 302  ? 32.518  16.011  54.786  1.00 180.98 ? 302  ASP B C   1 
ATOM   14639 O  O   . ASP C 1 302  ? 31.985  15.556  55.792  1.00 181.95 ? 302  ASP B O   1 
ATOM   14640 C  CB  . ASP C 1 302  ? 31.092  14.585  53.276  1.00 186.86 ? 302  ASP B CB  1 
ATOM   14641 C  CG  . ASP C 1 302  ? 29.919  15.516  53.625  1.00 194.00 ? 302  ASP B CG  1 
ATOM   14642 O  OD1 . ASP C 1 302  ? 28.759  15.051  53.633  1.00 198.06 ? 302  ASP B OD1 1 
ATOM   14643 O  OD2 . ASP C 1 302  ? 30.147  16.710  53.898  1.00 195.54 ? 302  ASP B OD2 1 
ATOM   14644 N  N   . SER C 1 303  ? 33.150  17.180  54.755  1.00 218.99 ? 303  SER B N   1 
ATOM   14645 C  CA  . SER C 1 303  ? 33.443  17.957  55.956  1.00 220.68 ? 303  SER B CA  1 
ATOM   14646 C  C   . SER C 1 303  ? 32.185  18.404  56.724  1.00 223.28 ? 303  SER B C   1 
ATOM   14647 O  O   . SER C 1 303  ? 32.213  18.642  57.948  1.00 227.81 ? 303  SER B O   1 
ATOM   14648 C  CB  . SER C 1 303  ? 34.315  19.152  55.576  1.00 216.47 ? 303  SER B CB  1 
ATOM   14649 O  OG  . SER C 1 303  ? 35.521  18.715  54.974  1.00 211.47 ? 303  SER B OG  1 
ATOM   14650 N  N   . GLU C 1 304  ? 31.088  18.504  55.983  1.00 220.44 ? 304  GLU B N   1 
ATOM   14651 C  CA  . GLU C 1 304  ? 29.770  18.841  56.515  1.00 218.18 ? 304  GLU B CA  1 
ATOM   14652 C  C   . GLU C 1 304  ? 29.394  18.046  57.751  1.00 218.51 ? 304  GLU B C   1 
ATOM   14653 O  O   . GLU C 1 304  ? 29.502  18.513  58.900  1.00 218.14 ? 304  GLU B O   1 
ATOM   14654 C  CB  . GLU C 1 304  ? 28.741  18.503  55.449  1.00 217.51 ? 304  GLU B CB  1 
ATOM   14655 C  CG  . GLU C 1 304  ? 27.956  19.667  54.945  1.00 219.20 ? 304  GLU B CG  1 
ATOM   14656 C  CD  . GLU C 1 304  ? 27.118  19.274  53.776  1.00 220.16 ? 304  GLU B CD  1 
ATOM   14657 O  OE1 . GLU C 1 304  ? 27.097  18.059  53.470  1.00 221.47 ? 304  GLU B OE1 1 
ATOM   14658 O  OE2 . GLU C 1 304  ? 26.496  20.174  53.171  1.00 219.61 ? 304  GLU B OE2 1 
ATOM   14659 N  N   . THR C 1 305  ? 28.887  16.853  57.461  1.00 170.62 ? 305  THR B N   1 
ATOM   14660 C  CA  . THR C 1 305  ? 28.724  15.814  58.440  1.00 176.99 ? 305  THR B CA  1 
ATOM   14661 C  C   . THR C 1 305  ? 29.718  16.089  59.543  1.00 180.62 ? 305  THR B C   1 
ATOM   14662 O  O   . THR C 1 305  ? 29.421  16.815  60.480  1.00 181.07 ? 305  THR B O   1 
ATOM   14663 C  CB  . THR C 1 305  ? 29.071  14.439  57.817  1.00 174.31 ? 305  THR B CB  1 
ATOM   14664 O  OG1 . THR C 1 305  ? 28.518  14.348  56.494  1.00 172.24 ? 305  THR B OG1 1 
ATOM   14665 C  CG2 . THR C 1 305  ? 28.562  13.290  58.687  1.00 178.77 ? 305  THR B CG2 1 
ATOM   14666 N  N   . ALA C 1 306  ? 30.924  15.561  59.376  1.00 198.34 ? 306  ALA B N   1 
ATOM   14667 C  CA  . ALA C 1 306  ? 31.862  15.371  60.479  1.00 210.89 ? 306  ALA B CA  1 
ATOM   14668 C  C   . ALA C 1 306  ? 32.377  16.608  61.232  1.00 220.47 ? 306  ALA B C   1 
ATOM   14669 O  O   . ALA C 1 306  ? 33.585  16.791  61.365  1.00 223.02 ? 306  ALA B O   1 
ATOM   14670 C  CB  . ALA C 1 306  ? 33.025  14.501  60.028  1.00 207.27 ? 306  ALA B CB  1 
ATOM   14671 N  N   . VAL C 1 307  ? 31.453  17.427  61.735  1.00 413.42 ? 307  VAL B N   1 
ATOM   14672 C  CA  . VAL C 1 307  ? 31.743  18.446  62.749  1.00 430.05 ? 307  VAL B CA  1 
ATOM   14673 C  C   . VAL C 1 307  ? 30.453  18.961  63.391  1.00 445.70 ? 307  VAL B C   1 
ATOM   14674 O  O   . VAL C 1 307  ? 30.425  19.270  64.583  1.00 446.09 ? 307  VAL B O   1 
ATOM   14675 C  CB  . VAL C 1 307  ? 32.520  19.669  62.200  1.00 366.99 ? 307  VAL B CB  1 
ATOM   14676 C  CG1 . VAL C 1 307  ? 32.611  20.740  63.269  1.00 370.74 ? 307  VAL B CG1 1 
ATOM   14677 C  CG2 . VAL C 1 307  ? 33.914  19.291  61.753  1.00 365.34 ? 307  VAL B CG2 1 
ATOM   14678 N  N   . LYS C 1 308  ? 29.387  19.047  62.599  1.00 251.68 ? 308  LYS B N   1 
ATOM   14679 C  CA  . LYS C 1 308  ? 28.139  19.640  63.062  1.00 273.02 ? 308  LYS B CA  1 
ATOM   14680 C  C   . LYS C 1 308  ? 27.779  19.131  64.447  1.00 296.87 ? 308  LYS B C   1 
ATOM   14681 O  O   . LYS C 1 308  ? 28.024  19.809  65.438  1.00 302.51 ? 308  LYS B O   1 
ATOM   14682 C  CB  . LYS C 1 308  ? 27.009  19.384  62.063  1.00 271.02 ? 308  LYS B CB  1 
ATOM   14683 C  CG  . LYS C 1 308  ? 27.189  20.101  60.724  1.00 262.62 ? 308  LYS B CG  1 
ATOM   14684 C  CD  . LYS C 1 308  ? 25.980  19.887  59.841  1.00 262.52 ? 308  LYS B CD  1 
ATOM   14685 C  CE  . LYS C 1 308  ? 25.768  18.405  59.586  1.00 262.60 ? 308  LYS B CE  1 
ATOM   14686 N  NZ  . LYS C 1 308  ? 24.419  18.125  59.033  1.00 266.92 ? 308  LYS B NZ  1 
ATOM   14687 N  N   . GLU C 1 309  ? 27.219  17.934  64.525  1.00 368.70 ? 309  GLU B N   1 
ATOM   14688 C  CA  . GLU C 1 309  ? 26.939  17.358  65.829  1.00 387.20 ? 309  GLU B CA  1 
ATOM   14689 C  C   . GLU C 1 309  ? 28.243  17.000  66.547  1.00 377.63 ? 309  GLU B C   1 
ATOM   14690 O  O   . GLU C 1 309  ? 28.229  16.672  67.733  1.00 395.98 ? 309  GLU B O   1 
ATOM   14691 C  CB  . GLU C 1 309  ? 26.018  16.136  65.709  1.00 412.64 ? 309  GLU B CB  1 
ATOM   14692 C  CG  . GLU C 1 309  ? 25.704  15.421  67.031  1.00 435.18 ? 309  GLU B CG  1 
ATOM   14693 C  CD  . GLU C 1 309  ? 24.754  16.191  67.937  1.00 447.12 ? 309  GLU B CD  1 
ATOM   14694 O  OE1 . GLU C 1 309  ? 24.088  17.129  67.454  1.00 449.96 ? 309  GLU B OE1 1 
ATOM   14695 O  OE2 . GLU C 1 309  ? 24.666  15.850  69.137  1.00 452.92 ? 309  GLU B OE2 1 
ATOM   14696 N  N   . LEU C 1 310  ? 29.372  17.078  65.845  1.00 327.61 ? 310  LEU B N   1 
ATOM   14697 C  CA  . LEU C 1 310  ? 30.634  16.593  66.416  1.00 318.46 ? 310  LEU B CA  1 
ATOM   14698 C  C   . LEU C 1 310  ? 31.495  17.667  67.112  1.00 304.17 ? 310  LEU B C   1 
ATOM   14699 O  O   . LEU C 1 310  ? 32.562  17.364  67.657  1.00 303.72 ? 310  LEU B O   1 
ATOM   14700 C  CB  . LEU C 1 310  ? 31.440  15.798  65.376  1.00 317.37 ? 310  LEU B CB  1 
ATOM   14701 C  CG  . LEU C 1 310  ? 30.680  14.763  64.525  1.00 314.82 ? 310  LEU B CG  1 
ATOM   14702 C  CD1 . LEU C 1 310  ? 31.622  13.708  63.962  1.00 312.14 ? 310  LEU B CD1 1 
ATOM   14703 C  CD2 . LEU C 1 310  ? 29.562  14.089  65.299  1.00 319.83 ? 310  LEU B CD2 1 
ATOM   14704 N  N   . SER C 1 311  ? 31.010  18.907  67.085  1.00 300.01 ? 311  SER B N   1 
ATOM   14705 C  CA  . SER C 1 311  ? 31.574  20.027  67.846  1.00 290.12 ? 311  SER B CA  1 
ATOM   14706 C  C   . SER C 1 311  ? 30.740  21.303  67.594  1.00 283.21 ? 311  SER B C   1 
ATOM   14707 O  O   . SER C 1 311  ? 29.811  21.272  66.782  1.00 278.26 ? 311  SER B O   1 
ATOM   14708 C  CB  . SER C 1 311  ? 33.059  20.244  67.522  1.00 281.89 ? 311  SER B CB  1 
ATOM   14709 O  OG  . SER C 1 311  ? 33.884  19.289  68.174  1.00 280.99 ? 311  SER B OG  1 
ATOM   14710 N  N   . TYR C 1 312  ? 31.098  22.431  68.263  1.00 255.60 ? 312  TYR B N   1 
ATOM   14711 C  CA  . TYR C 1 312  ? 30.360  23.711  68.206  1.00 254.66 ? 312  TYR B CA  1 
ATOM   14712 C  C   . TYR C 1 312  ? 30.243  24.337  66.778  1.00 205.15 ? 312  TYR B C   1 
ATOM   14713 O  O   . TYR C 1 312  ? 29.744  25.443  66.635  1.00 203.24 ? 312  TYR B O   1 
ATOM   14714 C  CB  . TYR C 1 312  ? 31.003  24.753  69.168  1.00 260.69 ? 312  TYR B CB  1 
ATOM   14715 C  CG  . TYR C 1 312  ? 30.345  24.970  70.541  1.00 270.34 ? 312  TYR B CG  1 
ATOM   14716 C  CD1 . TYR C 1 312  ? 31.104  25.345  71.651  1.00 277.71 ? 312  TYR B CD1 1 
ATOM   14717 C  CD2 . TYR C 1 312  ? 28.974  24.831  70.720  1.00 272.64 ? 312  TYR B CD2 1 
ATOM   14718 C  CE1 . TYR C 1 312  ? 30.514  25.556  72.898  1.00 285.89 ? 312  TYR B CE1 1 
ATOM   14719 C  CE2 . TYR C 1 312  ? 28.381  25.038  71.967  1.00 280.46 ? 312  TYR B CE2 1 
ATOM   14720 C  CZ  . TYR C 1 312  ? 29.153  25.400  73.046  1.00 286.67 ? 312  TYR B CZ  1 
ATOM   14721 O  OH  . TYR C 1 312  ? 28.552  25.606  74.266  1.00 294.49 ? 312  TYR B OH  1 
ATOM   14722 N  N   . TYR C 1 313  ? 30.715  23.606  65.749  1.00 270.06 ? 313  TYR B N   1 
ATOM   14723 C  CA  . TYR C 1 313  ? 30.684  24.039  64.331  1.00 259.48 ? 313  TYR B CA  1 
ATOM   14724 C  C   . TYR C 1 313  ? 29.673  23.255  63.474  1.00 259.45 ? 313  TYR B C   1 
ATOM   14725 O  O   . TYR C 1 313  ? 29.891  22.085  63.170  1.00 259.20 ? 313  TYR B O   1 
ATOM   14726 C  CB  . TYR C 1 313  ? 32.070  23.904  63.662  1.00 247.56 ? 313  TYR B CB  1 
ATOM   14727 C  CG  . TYR C 1 313  ? 33.262  24.100  64.572  1.00 243.93 ? 313  TYR B CG  1 
ATOM   14728 C  CD1 . TYR C 1 313  ? 34.046  23.018  64.970  1.00 244.15 ? 313  TYR B CD1 1 
ATOM   14729 C  CD2 . TYR C 1 313  ? 33.606  25.367  65.038  1.00 243.50 ? 313  TYR B CD2 1 
ATOM   14730 C  CE1 . TYR C 1 313  ? 35.143  23.191  65.822  1.00 248.12 ? 313  TYR B CE1 1 
ATOM   14731 C  CE2 . TYR C 1 313  ? 34.701  25.555  65.892  1.00 247.18 ? 313  TYR B CE2 1 
ATOM   14732 C  CZ  . TYR C 1 313  ? 35.471  24.462  66.283  1.00 249.01 ? 313  TYR B CZ  1 
ATOM   14733 O  OH  . TYR C 1 313  ? 36.560  24.636  67.127  1.00 252.93 ? 313  TYR B OH  1 
ATOM   14734 N  N   . SER C 1 314  ? 28.583  23.904  63.068  1.00 280.94 ? 314  SER B N   1 
ATOM   14735 C  CA  . SER C 1 314  ? 27.596  23.282  62.182  1.00 277.12 ? 314  SER B CA  1 
ATOM   14736 C  C   . SER C 1 314  ? 27.598  23.994  60.832  1.00 265.13 ? 314  SER B C   1 
ATOM   14737 O  O   . SER C 1 314  ? 27.092  23.476  59.829  1.00 259.71 ? 314  SER B O   1 
ATOM   14738 C  CB  . SER C 1 314  ? 26.200  23.347  62.809  1.00 287.64 ? 314  SER B CB  1 
ATOM   14739 O  OG  . SER C 1 314  ? 25.855  24.679  63.150  1.00 292.92 ? 314  SER B OG  1 
ATOM   14740 N  N   . LEU C 1 315  ? 28.181  25.192  60.806  1.00 240.48 ? 315  LEU B N   1 
ATOM   14741 C  CA  . LEU C 1 315  ? 28.215  26.046  59.616  1.00 234.01 ? 315  LEU B CA  1 
ATOM   14742 C  C   . LEU C 1 315  ? 29.506  26.043  58.803  1.00 223.17 ? 315  LEU B C   1 
ATOM   14743 O  O   . LEU C 1 315  ? 30.581  25.851  59.354  1.00 223.85 ? 315  LEU B O   1 
ATOM   14744 C  CB  . LEU C 1 315  ? 27.941  27.483  60.050  1.00 242.34 ? 315  LEU B CB  1 
ATOM   14745 C  CG  . LEU C 1 315  ? 26.533  28.040  59.886  1.00 248.70 ? 315  LEU B CG  1 
ATOM   14746 C  CD1 . LEU C 1 315  ? 26.337  29.287  60.731  1.00 252.37 ? 315  LEU B CD1 1 
ATOM   14747 C  CD2 . LEU C 1 315  ? 26.235  28.349  58.433  1.00 242.94 ? 315  LEU B CD2 1 
ATOM   14748 N  N   . GLU C 1 316  ? 29.368  26.249  57.476  1.00 155.57 ? 316  GLU B N   1 
ATOM   14749 C  CA  . GLU C 1 316  ? 30.521  26.287  56.600  1.00 147.80 ? 316  GLU B CA  1 
ATOM   14750 C  C   . GLU C 1 316  ? 31.382  27.486  56.882  1.00 144.46 ? 316  GLU B C   1 
ATOM   14751 O  O   . GLU C 1 316  ? 32.604  27.431  56.938  1.00 144.40 ? 316  GLU B O   1 
ATOM   14752 C  CB  . GLU C 1 316  ? 30.115  26.308  55.120  1.00 145.68 ? 316  GLU B CB  1 
ATOM   14753 C  CG  . GLU C 1 316  ? 31.185  25.843  54.162  1.00 148.08 ? 316  GLU B CG  1 
ATOM   14754 C  CD  . GLU C 1 316  ? 32.243  26.884  53.872  1.00 152.54 ? 316  GLU B CD  1 
ATOM   14755 O  OE1 . GLU C 1 316  ? 31.925  28.095  53.886  1.00 154.12 ? 316  GLU B OE1 1 
ATOM   14756 O  OE2 . GLU C 1 316  ? 33.410  26.503  53.615  1.00 153.60 ? 316  GLU B OE2 1 
ATOM   14757 N  N   . ASP C 1 317  ? 30.664  28.580  57.035  1.00 150.62 ? 317  ASP B N   1 
ATOM   14758 C  CA  . ASP C 1 317  ? 31.087  29.947  57.285  1.00 154.56 ? 317  ASP B CA  1 
ATOM   14759 C  C   . ASP C 1 317  ? 31.500  30.162  58.718  1.00 161.36 ? 317  ASP B C   1 
ATOM   14760 O  O   . ASP C 1 317  ? 32.160  31.152  59.066  1.00 160.30 ? 317  ASP B O   1 
ATOM   14761 C  CB  . ASP C 1 317  ? 29.918  30.838  56.780  1.00 157.23 ? 317  ASP B CB  1 
ATOM   14762 C  CG  . ASP C 1 317  ? 29.721  32.240  57.341  1.00 172.32 ? 317  ASP B CG  1 
ATOM   14763 O  OD1 . ASP C 1 317  ? 30.254  32.538  58.440  1.00 175.32 ? 317  ASP B OD1 1 
ATOM   14764 O  OD2 . ASP C 1 317  ? 29.033  33.050  56.688  1.00 171.57 ? 317  ASP B OD2 1 
ATOM   14765 N  N   . LEU C 1 318  ? 31.105  29.214  59.564  1.00 257.35 ? 318  LEU B N   1 
ATOM   14766 C  CA  . LEU C 1 318  ? 31.441  29.272  60.974  1.00 264.86 ? 318  LEU B CA  1 
ATOM   14767 C  C   . LEU C 1 318  ? 32.840  28.759  61.273  1.00 262.90 ? 318  LEU B C   1 
ATOM   14768 O  O   . LEU C 1 318  ? 33.266  28.779  62.435  1.00 264.18 ? 318  LEU B O   1 
ATOM   14769 C  CB  . LEU C 1 318  ? 30.393  28.544  61.814  1.00 270.96 ? 318  LEU B CB  1 
ATOM   14770 C  CG  . LEU C 1 318  ? 29.726  29.354  62.944  1.00 280.29 ? 318  LEU B CG  1 
ATOM   14771 C  CD1 . LEU C 1 318  ? 28.458  28.649  63.412  1.00 284.11 ? 318  LEU B CD1 1 
ATOM   14772 C  CD2 . LEU C 1 318  ? 30.690  29.545  64.116  1.00 288.61 ? 318  LEU B CD2 1 
ATOM   14773 N  N   . ASN C 1 319  ? 33.521  28.329  60.296  1.00 129.11 ? 319  ASN B N   1 
ATOM   14774 C  CA  . ASN C 1 319  ? 34.826  27.792  60.490  1.00 125.09 ? 319  ASN B CA  1 
ATOM   14775 C  C   . ASN C 1 319  ? 35.824  28.652  59.740  1.00 123.31 ? 319  ASN B C   1 
ATOM   14776 O  O   . ASN C 1 319  ? 35.505  29.146  58.661  1.00 121.37 ? 319  ASN B O   1 
ATOM   14777 C  CB  . ASN C 1 319  ? 34.739  26.352  59.968  1.00 123.81 ? 319  ASN B CB  1 
ATOM   14778 C  CG  . ASN C 1 319  ? 35.973  25.500  60.110  1.00 125.78 ? 319  ASN B CG  1 
ATOM   14779 O  OD1 . ASN C 1 319  ? 36.658  25.544  61.124  1.00 131.99 ? 319  ASN B OD1 1 
ATOM   14780 N  ND2 . ASN C 1 319  ? 36.251  24.710  59.072  1.00 125.46 ? 319  ASN B ND2 1 
ATOM   14781 N  N   . ASN C 1 320  ? 37.036  28.833  60.251  1.00 159.24 ? 320  ASN B N   1 
ATOM   14782 C  CA  . ASN C 1 320  ? 38.110  29.561  59.579  1.00 157.49 ? 320  ASN B CA  1 
ATOM   14783 C  C   . ASN C 1 320  ? 39.356  29.214  60.338  1.00 163.12 ? 320  ASN B C   1 
ATOM   14784 O  O   . ASN C 1 320  ? 40.414  29.809  60.213  1.00 164.70 ? 320  ASN B O   1 
ATOM   14785 C  CB  . ASN C 1 320  ? 37.854  31.055  59.517  1.00 158.54 ? 320  ASN B CB  1 
ATOM   14786 C  CG  . ASN C 1 320  ? 36.926  31.404  58.351  1.00 156.90 ? 320  ASN B CG  1 
ATOM   14787 O  OD1 . ASN C 1 320  ? 37.354  31.837  57.283  1.00 154.05 ? 320  ASN B OD1 1 
ATOM   14788 N  ND2 . ASN C 1 320  ? 35.627  31.201  58.575  1.00 158.12 ? 320  ASN B ND2 1 
ATOM   14789 N  N   . LYS C 1 321  ? 39.118  28.169  61.143  1.00 242.24 ? 321  LYS B N   1 
ATOM   14790 C  CA  . LYS C 1 321  ? 40.137  27.534  61.941  1.00 247.80 ? 321  LYS B CA  1 
ATOM   14791 C  C   . LYS C 1 321  ? 40.668  26.336  61.181  1.00 241.41 ? 321  LYS B C   1 
ATOM   14792 O  O   . LYS C 1 321  ? 40.561  26.302  59.959  1.00 235.34 ? 321  LYS B O   1 
ATOM   14793 C  CB  . LYS C 1 321  ? 39.643  27.154  63.333  1.00 259.81 ? 321  LYS B CB  1 
ATOM   14794 C  CG  . LYS C 1 321  ? 38.278  26.497  63.336  1.00 263.18 ? 321  LYS B CG  1 
ATOM   14795 C  CD  . LYS C 1 321  ? 37.757  26.269  64.739  1.00 275.27 ? 321  LYS B CD  1 
ATOM   14796 C  CE  . LYS C 1 321  ? 37.439  27.584  65.423  1.00 279.74 ? 321  LYS B CE  1 
ATOM   14797 N  NZ  . LYS C 1 321  ? 36.958  27.381  66.811  1.00 287.02 ? 321  LYS B NZ  1 
ATOM   14798 N  N   . TYR C 1 322  ? 41.220  25.360  61.895  1.00 173.58 ? 322  TYR B N   1 
ATOM   14799 C  CA  . TYR C 1 322  ? 41.879  24.291  61.168  1.00 170.59 ? 322  TYR B CA  1 
ATOM   14800 C  C   . TYR C 1 322  ? 41.187  22.936  61.026  1.00 171.14 ? 322  TYR B C   1 
ATOM   14801 O  O   . TYR C 1 322  ? 40.046  22.730  61.464  1.00 173.73 ? 322  TYR B O   1 
ATOM   14802 C  CB  . TYR C 1 322  ? 43.275  24.123  61.780  1.00 173.75 ? 322  TYR B CB  1 
ATOM   14803 C  CG  . TYR C 1 322  ? 44.144  25.320  61.530  1.00 172.27 ? 322  TYR B CG  1 
ATOM   14804 C  CD1 . TYR C 1 322  ? 45.514  25.195  61.363  1.00 168.66 ? 322  TYR B CD1 1 
ATOM   14805 C  CD2 . TYR C 1 322  ? 43.576  26.583  61.425  1.00 174.97 ? 322  TYR B CD2 1 
ATOM   14806 C  CE1 . TYR C 1 322  ? 46.296  26.312  61.109  1.00 169.09 ? 322  TYR B CE1 1 
ATOM   14807 C  CE2 . TYR C 1 322  ? 44.333  27.691  61.175  1.00 174.30 ? 322  TYR B CE2 1 
ATOM   14808 C  CZ  . TYR C 1 322  ? 45.691  27.561  61.011  1.00 172.77 ? 322  TYR B CZ  1 
ATOM   14809 O  OH  . TYR C 1 322  ? 46.460  28.665  60.752  1.00 172.26 ? 322  TYR B OH  1 
ATOM   14810 N  N   . LEU C 1 323  ? 41.915  22.004  60.392  1.00 126.29 ? 323  LEU B N   1 
ATOM   14811 C  CA  . LEU C 1 323  ? 41.518  20.593  60.187  1.00 122.73 ? 323  LEU B CA  1 
ATOM   14812 C  C   . LEU C 1 323  ? 42.737  19.645  60.384  1.00 124.66 ? 323  LEU B C   1 
ATOM   14813 O  O   . LEU C 1 323  ? 43.583  19.552  59.498  1.00 124.02 ? 323  LEU B O   1 
ATOM   14814 C  CB  . LEU C 1 323  ? 40.906  20.413  58.784  1.00 121.53 ? 323  LEU B CB  1 
ATOM   14815 C  CG  . LEU C 1 323  ? 40.117  19.200  58.258  1.00 119.45 ? 323  LEU B CG  1 
ATOM   14816 C  CD1 . LEU C 1 323  ? 41.020  18.090  57.797  1.00 118.73 ? 323  LEU B CD1 1 
ATOM   14817 C  CD2 . LEU C 1 323  ? 39.116  18.685  59.237  1.00 120.15 ? 323  LEU B CD2 1 
ATOM   14818 N  N   . TYR C 1 324  ? 42.813  18.956  61.538  1.00 179.60 ? 324  TYR B N   1 
ATOM   14819 C  CA  . TYR C 1 324  ? 43.951  18.086  61.926  1.00 187.59 ? 324  TYR B CA  1 
ATOM   14820 C  C   . TYR C 1 324  ? 43.713  16.636  61.560  1.00 186.48 ? 324  TYR B C   1 
ATOM   14821 O  O   . TYR C 1 324  ? 42.634  16.086  61.825  1.00 184.88 ? 324  TYR B O   1 
ATOM   14822 C  CB  . TYR C 1 324  ? 44.233  18.178  63.434  1.00 199.24 ? 324  TYR B CB  1 
ATOM   14823 C  CG  . TYR C 1 324  ? 44.989  16.992  64.061  1.00 208.55 ? 324  TYR B CG  1 
ATOM   14824 C  CD1 . TYR C 1 324  ? 46.289  17.138  64.544  1.00 216.56 ? 324  TYR B CD1 1 
ATOM   14825 C  CD2 . TYR C 1 324  ? 44.387  15.736  64.210  1.00 210.17 ? 324  TYR B CD2 1 
ATOM   14826 C  CE1 . TYR C 1 324  ? 46.979  16.057  65.145  1.00 222.25 ? 324  TYR B CE1 1 
ATOM   14827 C  CE2 . TYR C 1 324  ? 45.070  14.648  64.807  1.00 215.71 ? 324  TYR B CE2 1 
ATOM   14828 C  CZ  . TYR C 1 324  ? 46.361  14.816  65.273  1.00 220.94 ? 324  TYR B CZ  1 
ATOM   14829 O  OH  . TYR C 1 324  ? 47.020  13.748  65.855  1.00 224.79 ? 324  TYR B OH  1 
ATOM   14830 N  N   . ILE C 1 325  ? 44.741  16.021  60.978  1.00 169.29 ? 325  ILE B N   1 
ATOM   14831 C  CA  . ILE C 1 325  ? 44.664  14.638  60.526  1.00 165.38 ? 325  ILE B CA  1 
ATOM   14832 C  C   . ILE C 1 325  ? 45.781  13.772  61.120  1.00 168.72 ? 325  ILE B C   1 
ATOM   14833 O  O   . ILE C 1 325  ? 46.902  14.232  61.338  1.00 171.49 ? 325  ILE B O   1 
ATOM   14834 C  CB  . ILE C 1 325  ? 44.744  14.526  58.967  1.00 157.34 ? 325  ILE B CB  1 
ATOM   14835 C  CG1 . ILE C 1 325  ? 43.894  15.578  58.278  1.00 154.23 ? 325  ILE B CG1 1 
ATOM   14836 C  CG2 . ILE C 1 325  ? 44.215  13.203  58.487  1.00 154.38 ? 325  ILE B CG2 1 
ATOM   14837 C  CD1 . ILE C 1 325  ? 43.698  15.280  56.825  1.00 148.48 ? 325  ILE B CD1 1 
ATOM   14838 N  N   . ALA C 1 326  ? 45.459  12.503  61.354  1.00 154.01 ? 326  ALA B N   1 
ATOM   14839 C  CA  . ALA C 1 326  ? 46.440  11.514  61.772  1.00 158.23 ? 326  ALA B CA  1 
ATOM   14840 C  C   . ALA C 1 326  ? 45.969  10.102  61.426  1.00 156.90 ? 326  ALA B C   1 
ATOM   14841 O  O   . ALA C 1 326  ? 44.808  9.734   61.647  1.00 154.35 ? 326  ALA B O   1 
ATOM   14842 C  CB  . ALA C 1 326  ? 46.705  11.635  63.242  1.00 163.25 ? 326  ALA B CB  1 
ATOM   14843 N  N   . VAL C 1 327  ? 46.887  9.332   60.854  1.00 179.54 ? 327  VAL B N   1 
ATOM   14844 C  CA  . VAL C 1 327  ? 46.641  7.945   60.498  1.00 180.56 ? 327  VAL B CA  1 
ATOM   14845 C  C   . VAL C 1 327  ? 47.456  7.067   61.446  1.00 188.25 ? 327  VAL B C   1 
ATOM   14846 O  O   . VAL C 1 327  ? 48.367  7.549   62.131  1.00 194.57 ? 327  VAL B O   1 
ATOM   14847 C  CB  . VAL C 1 327  ? 47.089  7.623   59.027  1.00 172.68 ? 327  VAL B CB  1 
ATOM   14848 C  CG1 . VAL C 1 327  ? 46.606  6.254   58.607  1.00 171.91 ? 327  VAL B CG1 1 
ATOM   14849 C  CG2 . VAL C 1 327  ? 46.593  8.660   58.043  1.00 165.31 ? 327  VAL B CG2 1 
ATOM   14850 N  N   . THR C 1 328  ? 47.105  5.784   61.502  1.00 199.07 ? 328  THR B N   1 
ATOM   14851 C  CA  . THR C 1 328  ? 47.997  4.742   62.006  1.00 205.96 ? 328  THR B CA  1 
ATOM   14852 C  C   . THR C 1 328  ? 47.794  3.559   61.053  1.00 204.52 ? 328  THR B C   1 
ATOM   14853 O  O   . THR C 1 328  ? 46.657  3.177   60.744  1.00 198.13 ? 328  THR B O   1 
ATOM   14854 C  CB  . THR C 1 328  ? 47.733  4.361   63.500  1.00 213.56 ? 328  THR B CB  1 
ATOM   14855 O  OG1 . THR C 1 328  ? 47.924  5.507   64.342  1.00 217.97 ? 328  THR B OG1 1 
ATOM   14856 C  CG2 . THR C 1 328  ? 48.685  3.260   63.966  1.00 218.64 ? 328  THR B CG2 1 
ATOM   14857 N  N   . VAL C 1 329  ? 48.903  3.028   60.547  1.00 228.86 ? 329  VAL B N   1 
ATOM   14858 C  CA  . VAL C 1 329  ? 48.885  1.918   59.599  1.00 230.46 ? 329  VAL B CA  1 
ATOM   14859 C  C   . VAL C 1 329  ? 49.731  0.764   60.137  1.00 244.71 ? 329  VAL B C   1 
ATOM   14860 O  O   . VAL C 1 329  ? 50.928  0.677   59.861  1.00 252.38 ? 329  VAL B O   1 
ATOM   14861 C  CB  . VAL C 1 329  ? 49.444  2.342   58.226  1.00 221.77 ? 329  VAL B CB  1 
ATOM   14862 C  CG1 . VAL C 1 329  ? 49.259  1.228   57.210  1.00 217.42 ? 329  VAL B CG1 1 
ATOM   14863 C  CG2 . VAL C 1 329  ? 48.776  3.620   57.756  1.00 215.37 ? 329  VAL B CG2 1 
ATOM   14864 N  N   . ILE C 1 330  ? 49.109  -0.108  60.924  1.00 240.35 ? 330  ILE B N   1 
ATOM   14865 C  CA  . ILE C 1 330  ? 49.792  -1.290  61.435  1.00 251.29 ? 330  ILE B CA  1 
ATOM   14866 C  C   . ILE C 1 330  ? 49.847  -2.355  60.327  1.00 257.32 ? 330  ILE B C   1 
ATOM   14867 O  O   . ILE C 1 330  ? 48.824  -2.695  59.727  1.00 251.30 ? 330  ILE B O   1 
ATOM   14868 C  CB  . ILE C 1 330  ? 49.126  -1.821  62.740  1.00 265.94 ? 330  ILE B CB  1 
ATOM   14869 C  CG1 . ILE C 1 330  ? 47.662  -2.182  62.514  1.00 262.08 ? 330  ILE B CG1 1 
ATOM   14870 C  CG2 . ILE C 1 330  ? 49.155  -0.777  63.827  1.00 267.62 ? 330  ILE B CG2 1 
ATOM   14871 C  CD1 . ILE C 1 330  ? 46.880  -2.312  63.813  1.00 265.42 ? 330  ILE B CD1 1 
ATOM   14872 N  N   . GLU C 1 331  ? 51.049  -2.854  60.042  1.00 302.12 ? 331  GLU B N   1 
ATOM   14873 C  CA  . GLU C 1 331  ? 51.269  -3.804  58.949  1.00 310.95 ? 331  GLU B CA  1 
ATOM   14874 C  C   . GLU C 1 331  ? 50.620  -5.159  59.216  1.00 321.54 ? 331  GLU B C   1 
ATOM   14875 O  O   . GLU C 1 331  ? 50.708  -5.687  60.321  1.00 327.53 ? 331  GLU B O   1 
ATOM   14876 C  CB  . GLU C 1 331  ? 52.769  -3.990  58.706  1.00 315.87 ? 331  GLU B CB  1 
ATOM   14877 C  CG  . GLU C 1 331  ? 53.129  -5.307  58.033  1.00 318.51 ? 331  GLU B CG  1 
ATOM   14878 C  CD  . GLU C 1 331  ? 54.543  -5.765  58.357  1.00 325.82 ? 331  GLU B CD  1 
ATOM   14879 O  OE1 . GLU C 1 331  ? 55.253  -5.042  59.086  1.00 328.61 ? 331  GLU B OE1 1 
ATOM   14880 O  OE2 . GLU C 1 331  ? 54.945  -6.851  57.887  1.00 329.01 ? 331  GLU B OE2 1 
ATOM   14881 N  N   . SER C 1 332  ? 49.986  -5.731  58.197  1.00 238.11 ? 332  SER B N   1 
ATOM   14882 C  CA  . SER C 1 332  ? 49.249  -6.983  58.373  1.00 247.61 ? 332  SER B CA  1 
ATOM   14883 C  C   . SER C 1 332  ? 50.132  -8.210  58.559  1.00 259.99 ? 332  SER B C   1 
ATOM   14884 O  O   . SER C 1 332  ? 49.796  -9.118  59.324  1.00 263.81 ? 332  SER B O   1 
ATOM   14885 C  CB  . SER C 1 332  ? 48.310  -7.233  57.197  1.00 244.75 ? 332  SER B CB  1 
ATOM   14886 O  OG  . SER C 1 332  ? 47.758  -8.537  57.285  1.00 248.55 ? 332  SER B OG  1 
ATOM   14887 N  N   . THR C 1 333  ? 51.245  -8.248  57.838  1.00 258.89 ? 333  THR B N   1 
ATOM   14888 C  CA  . THR C 1 333  ? 52.144  -9.390  57.905  1.00 269.27 ? 333  THR B CA  1 
ATOM   14889 C  C   . THR C 1 333  ? 52.875  -9.467  59.244  1.00 276.97 ? 333  THR B C   1 
ATOM   14890 O  O   . THR C 1 333  ? 52.694  -10.421 59.994  1.00 282.03 ? 333  THR B O   1 
ATOM   14891 C  CB  . THR C 1 333  ? 53.154  -9.380  56.741  1.00 270.73 ? 333  THR B CB  1 
ATOM   14892 O  OG1 . THR C 1 333  ? 54.487  -9.460  57.256  1.00 277.00 ? 333  THR B OG1 1 
ATOM   14893 C  CG2 . THR C 1 333  ? 53.005  -8.107  55.925  1.00 264.74 ? 333  THR B CG2 1 
ATOM   14894 N  N   . GLY C 1 334  ? 53.685  -8.457  59.548  1.00 278.64 ? 334  GLY B N   1 
ATOM   14895 C  CA  . GLY C 1 334  ? 54.527  -8.478  60.733  1.00 283.83 ? 334  GLY B CA  1 
ATOM   14896 C  C   . GLY C 1 334  ? 53.813  -8.271  62.055  1.00 282.16 ? 334  GLY B C   1 
ATOM   14897 O  O   . GLY C 1 334  ? 54.246  -8.782  63.087  1.00 291.41 ? 334  GLY B O   1 
ATOM   14898 N  N   . GLY C 1 335  ? 52.712  -7.529  62.031  1.00 280.01 ? 335  GLY B N   1 
ATOM   14899 C  CA  . GLY C 1 335  ? 52.011  -7.187  63.254  1.00 272.29 ? 335  GLY B CA  1 
ATOM   14900 C  C   . GLY C 1 335  ? 52.582  -5.919  63.858  1.00 264.24 ? 335  GLY B C   1 
ATOM   14901 O  O   . GLY C 1 335  ? 52.292  -5.578  65.007  1.00 265.91 ? 335  GLY B O   1 
ATOM   14902 N  N   . PHE C 1 336  ? 53.410  -5.232  63.075  1.00 231.14 ? 336  PHE B N   1 
ATOM   14903 C  CA  . PHE C 1 336  ? 53.989  -3.951  63.474  1.00 222.03 ? 336  PHE B CA  1 
ATOM   14904 C  C   . PHE C 1 336  ? 52.919  -2.872  63.582  1.00 209.70 ? 336  PHE B C   1 
ATOM   14905 O  O   . PHE C 1 336  ? 51.742  -3.110  63.313  1.00 205.40 ? 336  PHE B O   1 
ATOM   14906 C  CB  . PHE C 1 336  ? 55.011  -3.472  62.440  1.00 215.83 ? 336  PHE B CB  1 
ATOM   14907 C  CG  . PHE C 1 336  ? 56.374  -4.092  62.567  1.00 216.08 ? 336  PHE B CG  1 
ATOM   14908 C  CD1 . PHE C 1 336  ? 56.903  -4.829  61.518  1.00 211.83 ? 336  PHE B CD1 1 
ATOM   14909 C  CD2 . PHE C 1 336  ? 57.141  -3.902  63.704  1.00 220.95 ? 336  PHE B CD2 1 
ATOM   14910 C  CE1 . PHE C 1 336  ? 58.153  -5.379  61.602  1.00 216.83 ? 336  PHE B CE1 1 
ATOM   14911 C  CE2 . PHE C 1 336  ? 58.396  -4.456  63.798  1.00 226.66 ? 336  PHE B CE2 1 
ATOM   14912 C  CZ  . PHE C 1 336  ? 58.904  -5.194  62.743  1.00 225.04 ? 336  PHE B CZ  1 
ATOM   14913 N  N   . SER C 1 337  ? 53.350  -1.671  63.952  1.00 245.08 ? 337  SER B N   1 
ATOM   14914 C  CA  . SER C 1 337  ? 52.475  -0.509  63.958  1.00 233.80 ? 337  SER B CA  1 
ATOM   14915 C  C   . SER C 1 337  ? 53.276  0.738   63.633  1.00 232.87 ? 337  SER B C   1 
ATOM   14916 O  O   . SER C 1 337  ? 54.400  0.912   64.115  1.00 238.46 ? 337  SER B O   1 
ATOM   14917 C  CB  . SER C 1 337  ? 51.799  -0.343  65.317  1.00 232.75 ? 337  SER B CB  1 
ATOM   14918 O  OG  . SER C 1 337  ? 50.897  0.752   65.301  1.00 223.49 ? 337  SER B OG  1 
ATOM   14919 N  N   . GLU C 1 338  ? 52.692  1.599   62.805  1.00 228.19 ? 338  GLU B N   1 
ATOM   14920 C  CA  . GLU C 1 338  ? 53.298  2.885   62.485  1.00 227.30 ? 338  GLU B CA  1 
ATOM   14921 C  C   . GLU C 1 338  ? 52.246  3.985   62.515  1.00 219.40 ? 338  GLU B C   1 
ATOM   14922 O  O   . GLU C 1 338  ? 51.088  3.761   62.180  1.00 212.92 ? 338  GLU B O   1 
ATOM   14923 C  CB  . GLU C 1 338  ? 53.989  2.845   61.125  1.00 228.15 ? 338  GLU B CB  1 
ATOM   14924 C  CG  . GLU C 1 338  ? 55.198  3.753   61.045  1.00 235.09 ? 338  GLU B CG  1 
ATOM   14925 C  CD  . GLU C 1 338  ? 56.241  3.415   62.101  1.00 247.79 ? 338  GLU B CD  1 
ATOM   14926 O  OE1 . GLU C 1 338  ? 56.409  2.216   62.412  1.00 252.55 ? 338  GLU B OE1 1 
ATOM   14927 O  OE2 . GLU C 1 338  ? 56.894  4.344   62.623  1.00 253.08 ? 338  GLU B OE2 1 
ATOM   14928 N  N   . GLU C 1 339  ? 52.649  5.174   62.933  1.00 257.57 ? 339  GLU B N   1 
ATOM   14929 C  CA  . GLU C 1 339  ? 51.709  6.271   63.056  1.00 254.17 ? 339  GLU B CA  1 
ATOM   14930 C  C   . GLU C 1 339  ? 52.194  7.450   62.235  1.00 244.28 ? 339  GLU B C   1 
ATOM   14931 O  O   . GLU C 1 339  ? 53.381  7.556   61.931  1.00 243.08 ? 339  GLU B O   1 
ATOM   14932 C  CB  . GLU C 1 339  ? 51.526  6.645   64.524  1.00 267.28 ? 339  GLU B CB  1 
ATOM   14933 C  CG  . GLU C 1 339  ? 50.806  5.567   65.312  1.00 278.20 ? 339  GLU B CG  1 
ATOM   14934 C  CD  . GLU C 1 339  ? 51.011  5.690   66.804  1.00 295.20 ? 339  GLU B CD  1 
ATOM   14935 O  OE1 . GLU C 1 339  ? 51.550  6.727   67.245  1.00 301.77 ? 339  GLU B OE1 1 
ATOM   14936 O  OE2 . GLU C 1 339  ? 50.637  4.746   67.533  1.00 301.18 ? 339  GLU B OE2 1 
ATOM   14937 N  N   . ALA C 1 340  ? 51.264  8.325   61.864  1.00 184.74 ? 340  ALA B N   1 
ATOM   14938 C  CA  . ALA C 1 340  ? 51.571  9.473   61.014  1.00 180.79 ? 340  ALA B CA  1 
ATOM   14939 C  C   . ALA C 1 340  ? 50.465  10.528  61.097  1.00 174.56 ? 340  ALA B C   1 
ATOM   14940 O  O   . ALA C 1 340  ? 49.278  10.206  61.115  1.00 170.88 ? 340  ALA B O   1 
ATOM   14941 C  CB  . ALA C 1 340  ? 51.792  9.021   59.573  1.00 178.78 ? 340  ALA B CB  1 
ATOM   14942 N  N   . GLU C 1 341  ? 50.853  11.794  61.155  1.00 194.09 ? 341  GLU B N   1 
ATOM   14943 C  CA  . GLU C 1 341  ? 49.868  12.834  61.399  1.00 193.01 ? 341  GLU B CA  1 
ATOM   14944 C  C   . GLU C 1 341  ? 50.117  14.052  60.558  1.00 164.56 ? 341  GLU B C   1 
ATOM   14945 O  O   . GLU C 1 341  ? 51.244  14.298  60.124  1.00 165.42 ? 341  GLU B O   1 
ATOM   14946 C  CB  . GLU C 1 341  ? 49.891  13.265  62.866  1.00 200.68 ? 341  GLU B CB  1 
ATOM   14947 C  CG  . GLU C 1 341  ? 51.167  14.019  63.289  1.00 208.51 ? 341  GLU B CG  1 
ATOM   14948 C  CD  . GLU C 1 341  ? 51.134  14.469  64.754  1.00 213.41 ? 341  GLU B CD  1 
ATOM   14949 O  OE1 . GLU C 1 341  ? 50.118  14.217  65.440  1.00 214.80 ? 341  GLU B OE1 1 
ATOM   14950 O  OE2 . GLU C 1 341  ? 52.121  15.078  65.222  1.00 214.92 ? 341  GLU B OE2 1 
ATOM   14951 N  N   . ILE C 1 342  ? 49.049  14.815  60.347  1.00 174.54 ? 342  ILE B N   1 
ATOM   14952 C  CA  . ILE C 1 342  ? 49.140  16.131  59.737  1.00 169.78 ? 342  ILE B CA  1 
ATOM   14953 C  C   . ILE C 1 342  ? 48.621  17.188  60.694  1.00 173.43 ? 342  ILE B C   1 
ATOM   14954 O  O   . ILE C 1 342  ? 47.523  17.058  61.232  1.00 173.32 ? 342  ILE B O   1 
ATOM   14955 C  CB  . ILE C 1 342  ? 48.370  16.211  58.414  1.00 157.70 ? 342  ILE B CB  1 
ATOM   14956 C  CG1 . ILE C 1 342  ? 48.862  15.120  57.458  1.00 157.25 ? 342  ILE B CG1 1 
ATOM   14957 C  CG2 . ILE C 1 342  ? 48.517  17.601  57.797  1.00 150.93 ? 342  ILE B CG2 1 
ATOM   14958 C  CD1 . ILE C 1 342  ? 48.186  15.121  56.101  1.00 151.02 ? 342  ILE B CD1 1 
ATOM   14959 N  N   . PRO C 1 343  ? 49.402  18.260  60.879  1.00 189.90 ? 343  PRO B N   1 
ATOM   14960 C  CA  . PRO C 1 343  ? 49.143  19.173  61.992  1.00 191.23 ? 343  PRO B CA  1 
ATOM   14961 C  C   . PRO C 1 343  ? 47.725  19.632  61.892  1.00 187.82 ? 343  PRO B C   1 
ATOM   14962 O  O   . PRO C 1 343  ? 46.835  19.283  62.671  1.00 193.18 ? 343  PRO B O   1 
ATOM   14963 C  CB  . PRO C 1 343  ? 50.023  20.386  61.670  1.00 187.36 ? 343  PRO B CB  1 
ATOM   14964 C  CG  . PRO C 1 343  ? 50.954  19.962  60.599  1.00 185.62 ? 343  PRO B CG  1 
ATOM   14965 C  CD  . PRO C 1 343  ? 50.311  18.843  59.875  1.00 185.52 ? 343  PRO B CD  1 
ATOM   14966 N  N   . GLY C 1 344  ? 47.540  20.445  60.868  1.00 217.94 ? 344  GLY B N   1 
ATOM   14967 C  CA  . GLY C 1 344  ? 46.259  21.022  60.567  1.00 212.99 ? 344  GLY B CA  1 
ATOM   14968 C  C   . GLY C 1 344  ? 46.123  21.292  59.084  1.00 203.41 ? 344  GLY B C   1 
ATOM   14969 O  O   . GLY C 1 344  ? 47.045  21.076  58.291  1.00 204.24 ? 344  GLY B O   1 
ATOM   14970 N  N   . ILE C 1 345  ? 44.949  21.789  58.725  1.00 123.33 ? 345  ILE B N   1 
ATOM   14971 C  CA  . ILE C 1 345  ? 44.560  22.004  57.347  1.00 118.15 ? 345  ILE B CA  1 
ATOM   14972 C  C   . ILE C 1 345  ? 43.560  23.147  57.416  1.00 116.18 ? 345  ILE B C   1 
ATOM   14973 O  O   . ILE C 1 345  ? 42.368  22.939  57.629  1.00 116.49 ? 345  ILE B O   1 
ATOM   14974 C  CB  . ILE C 1 345  ? 43.953  20.708  56.762  1.00 114.70 ? 345  ILE B CB  1 
ATOM   14975 C  CG1 . ILE C 1 345  ? 45.061  19.765  56.319  1.00 122.47 ? 345  ILE B CG1 1 
ATOM   14976 C  CG2 . ILE C 1 345  ? 43.069  20.972  55.585  1.00 113.10 ? 345  ILE B CG2 1 
ATOM   14977 C  CD1 . ILE C 1 345  ? 44.549  18.588  55.569  1.00 119.07 ? 345  ILE B CD1 1 
ATOM   14978 N  N   . LYS C 1 346  ? 44.072  24.366  57.294  1.00 166.06 ? 346  LYS B N   1 
ATOM   14979 C  CA  . LYS C 1 346  ? 43.273  25.567  57.485  1.00 154.89 ? 346  LYS B CA  1 
ATOM   14980 C  C   . LYS C 1 346  ? 42.082  25.562  56.529  1.00 149.19 ? 346  LYS B C   1 
ATOM   14981 O  O   . LYS C 1 346  ? 42.285  25.601  55.325  1.00 151.19 ? 346  LYS B O   1 
ATOM   14982 C  CB  . LYS C 1 346  ? 44.162  26.787  57.218  1.00 154.17 ? 346  LYS B CB  1 
ATOM   14983 C  CG  . LYS C 1 346  ? 43.569  28.136  57.621  1.00 157.38 ? 346  LYS B CG  1 
ATOM   14984 C  CD  . LYS C 1 346  ? 44.311  29.351  56.992  1.00 155.74 ? 346  LYS B CD  1 
ATOM   14985 C  CE  . LYS C 1 346  ? 45.329  30.033  57.940  1.00 158.21 ? 346  LYS B CE  1 
ATOM   14986 N  NZ  . LYS C 1 346  ? 45.610  31.482  57.611  1.00 156.14 ? 346  LYS B NZ  1 
ATOM   14987 N  N   . TYR C 1 347  ? 40.852  25.472  57.038  1.00 136.41 ? 347  TYR B N   1 
ATOM   14988 C  CA  . TYR C 1 347  ? 39.665  25.659  56.191  1.00 132.62 ? 347  TYR B CA  1 
ATOM   14989 C  C   . TYR C 1 347  ? 39.632  27.078  55.741  1.00 131.28 ? 347  TYR B C   1 
ATOM   14990 O  O   . TYR C 1 347  ? 40.161  27.927  56.437  1.00 131.07 ? 347  TYR B O   1 
ATOM   14991 C  CB  . TYR C 1 347  ? 38.399  25.528  56.994  1.00 132.10 ? 347  TYR B CB  1 
ATOM   14992 C  CG  . TYR C 1 347  ? 37.829  24.167  57.010  1.00 132.04 ? 347  TYR B CG  1 
ATOM   14993 C  CD1 . TYR C 1 347  ? 36.471  23.966  56.848  1.00 130.17 ? 347  TYR B CD1 1 
ATOM   14994 C  CD2 . TYR C 1 347  ? 38.646  23.077  57.198  1.00 136.23 ? 347  TYR B CD2 1 
ATOM   14995 C  CE1 . TYR C 1 347  ? 35.942  22.712  56.887  1.00 131.74 ? 347  TYR B CE1 1 
ATOM   14996 C  CE2 . TYR C 1 347  ? 38.138  21.826  57.230  1.00 137.50 ? 347  TYR B CE2 1 
ATOM   14997 C  CZ  . TYR C 1 347  ? 36.787  21.642  57.070  1.00 136.21 ? 347  TYR B CZ  1 
ATOM   14998 O  OH  . TYR C 1 347  ? 36.298  20.365  57.095  1.00 137.76 ? 347  TYR B OH  1 
ATOM   14999 N  N   . VAL C 1 348  ? 38.966  27.373  54.630  1.00 127.08 ? 348  VAL B N   1 
ATOM   15000 C  CA  . VAL C 1 348  ? 38.734  28.776  54.290  1.00 130.32 ? 348  VAL B CA  1 
ATOM   15001 C  C   . VAL C 1 348  ? 37.335  29.004  53.797  1.00 129.03 ? 348  VAL B C   1 
ATOM   15002 O  O   . VAL C 1 348  ? 36.644  28.118  53.302  1.00 128.16 ? 348  VAL B O   1 
ATOM   15003 C  CB  . VAL C 1 348  ? 39.736  29.371  53.260  1.00 117.14 ? 348  VAL B CB  1 
ATOM   15004 C  CG1 . VAL C 1 348  ? 39.321  30.761  52.843  1.00 117.05 ? 348  VAL B CG1 1 
ATOM   15005 C  CG2 . VAL C 1 348  ? 41.130  29.444  53.830  1.00 117.48 ? 348  VAL B CG2 1 
ATOM   15006 N  N   . LEU C 1 349  ? 36.912  30.230  53.948  1.00 131.54 ? 349  LEU B N   1 
ATOM   15007 C  CA  . LEU C 1 349  ? 35.625  30.590  53.472  1.00 129.82 ? 349  LEU B CA  1 
ATOM   15008 C  C   . LEU C 1 349  ? 35.745  31.056  52.032  1.00 122.63 ? 349  LEU B C   1 
ATOM   15009 O  O   . LEU C 1 349  ? 35.099  30.501  51.150  1.00 117.27 ? 349  LEU B O   1 
ATOM   15010 C  CB  . LEU C 1 349  ? 35.133  31.701  54.356  1.00 137.06 ? 349  LEU B CB  1 
ATOM   15011 C  CG  . LEU C 1 349  ? 33.721  32.150  54.095  1.00 137.62 ? 349  LEU B CG  1 
ATOM   15012 C  CD1 . LEU C 1 349  ? 33.754  33.622  53.681  1.00 137.34 ? 349  LEU B CD1 1 
ATOM   15013 C  CD2 . LEU C 1 349  ? 33.058  31.225  53.056  1.00 134.51 ? 349  LEU B CD2 1 
ATOM   15014 N  N   . SER C 1 350  ? 36.596  32.067  51.821  1.00 135.50 ? 350  SER B N   1 
ATOM   15015 C  CA  . SER C 1 350  ? 36.844  32.729  50.527  1.00 131.67 ? 350  SER B CA  1 
ATOM   15016 C  C   . SER C 1 350  ? 38.349  33.016  50.325  1.00 133.24 ? 350  SER B C   1 
ATOM   15017 O  O   . SER C 1 350  ? 38.950  33.768  51.081  1.00 139.21 ? 350  SER B O   1 
ATOM   15018 C  CB  . SER C 1 350  ? 36.072  34.037  50.485  1.00 131.22 ? 350  SER B CB  1 
ATOM   15019 O  OG  . SER C 1 350  ? 36.367  34.769  49.317  1.00 129.75 ? 350  SER B OG  1 
ATOM   15020 N  N   . PRO C 1 351  ? 38.947  32.444  49.271  1.00 125.17 ? 351  PRO B N   1 
ATOM   15021 C  CA  . PRO C 1 351  ? 40.394  32.269  49.047  1.00 128.75 ? 351  PRO B CA  1 
ATOM   15022 C  C   . PRO C 1 351  ? 41.174  33.578  49.039  1.00 133.51 ? 351  PRO B C   1 
ATOM   15023 O  O   . PRO C 1 351  ? 42.399  33.590  48.901  1.00 139.19 ? 351  PRO B O   1 
ATOM   15024 C  CB  . PRO C 1 351  ? 40.455  31.609  47.669  1.00 123.97 ? 351  PRO B CB  1 
ATOM   15025 C  CG  . PRO C 1 351  ? 39.062  31.070  47.448  1.00 120.25 ? 351  PRO B CG  1 
ATOM   15026 C  CD  . PRO C 1 351  ? 38.171  32.065  48.086  1.00 120.31 ? 351  PRO B CD  1 
ATOM   15027 N  N   . TYR C 1 352  ? 40.444  34.672  49.206  1.00 135.40 ? 352  TYR B N   1 
ATOM   15028 C  CA  . TYR C 1 352  ? 41.019  36.011  49.218  1.00 138.96 ? 352  TYR B CA  1 
ATOM   15029 C  C   . TYR C 1 352  ? 40.736  36.723  50.554  1.00 141.01 ? 352  TYR B C   1 
ATOM   15030 O  O   . TYR C 1 352  ? 39.764  36.418  51.239  1.00 137.41 ? 352  TYR B O   1 
ATOM   15031 C  CB  . TYR C 1 352  ? 40.385  36.883  48.127  1.00 138.13 ? 352  TYR B CB  1 
ATOM   15032 C  CG  . TYR C 1 352  ? 40.477  36.477  46.650  1.00 136.88 ? 352  TYR B CG  1 
ATOM   15033 C  CD1 . TYR C 1 352  ? 41.450  37.037  45.828  1.00 140.04 ? 352  TYR B CD1 1 
ATOM   15034 C  CD2 . TYR C 1 352  ? 39.526  35.643  46.066  1.00 133.83 ? 352  TYR B CD2 1 
ATOM   15035 C  CE1 . TYR C 1 352  ? 41.530  36.738  44.509  1.00 138.23 ? 352  TYR B CE1 1 
ATOM   15036 C  CE2 . TYR C 1 352  ? 39.596  35.337  44.738  1.00 133.28 ? 352  TYR B CE2 1 
ATOM   15037 C  CZ  . TYR C 1 352  ? 40.611  35.889  43.963  1.00 135.36 ? 352  TYR B CZ  1 
ATOM   15038 O  OH  . TYR C 1 352  ? 40.733  35.605  42.620  1.00 133.84 ? 352  TYR B OH  1 
ATOM   15039 N  N   . LYS C 1 353  ? 41.528  37.738  50.862  1.00 120.08 ? 353  LYS B N   1 
ATOM   15040 C  CA  . LYS C 1 353  ? 41.379  38.446  52.109  1.00 125.07 ? 353  LYS B CA  1 
ATOM   15041 C  C   . LYS C 1 353  ? 41.848  39.860  51.918  1.00 126.27 ? 353  LYS B C   1 
ATOM   15042 O  O   . LYS C 1 353  ? 43.030  40.111  51.747  1.00 123.53 ? 353  LYS B O   1 
ATOM   15043 C  CB  . LYS C 1 353  ? 42.222  37.770  53.196  1.00 127.76 ? 353  LYS B CB  1 
ATOM   15044 C  CG  . LYS C 1 353  ? 43.602  37.333  52.746  1.00 136.79 ? 353  LYS B CG  1 
ATOM   15045 C  CD  . LYS C 1 353  ? 43.959  35.979  53.349  1.00 144.26 ? 353  LYS B CD  1 
ATOM   15046 C  CE  . LYS C 1 353  ? 44.919  36.097  54.519  1.00 153.16 ? 353  LYS B CE  1 
ATOM   15047 N  NZ  . LYS C 1 353  ? 45.278  34.738  55.034  1.00 156.04 ? 353  LYS B NZ  1 
ATOM   15048 N  N   . LEU C 1 354  ? 40.918  40.793  51.955  1.00 129.30 ? 354  LEU B N   1 
ATOM   15049 C  CA  . LEU C 1 354  ? 41.263  42.177  51.740  1.00 131.39 ? 354  LEU B CA  1 
ATOM   15050 C  C   . LEU C 1 354  ? 42.003  42.648  52.965  1.00 135.43 ? 354  LEU B C   1 
ATOM   15051 O  O   . LEU C 1 354  ? 41.928  42.022  54.001  1.00 137.85 ? 354  LEU B O   1 
ATOM   15052 C  CB  . LEU C 1 354  ? 39.998  43.009  51.619  1.00 130.30 ? 354  LEU B CB  1 
ATOM   15053 C  CG  . LEU C 1 354  ? 38.744  42.490  50.900  1.00 123.88 ? 354  LEU B CG  1 
ATOM   15054 C  CD1 . LEU C 1 354  ? 38.594  43.101  49.491  1.00 123.09 ? 354  LEU B CD1 1 
ATOM   15055 C  CD2 . LEU C 1 354  ? 38.629  40.945  50.884  1.00 121.09 ? 354  LEU B CD2 1 
ATOM   15056 N  N   . ASN C 1 355  ? 42.706  43.759  52.858  1.00 131.93 ? 355  ASN B N   1 
ATOM   15057 C  CA  . ASN C 1 355  ? 43.084  44.503  54.042  1.00 138.77 ? 355  ASN B CA  1 
ATOM   15058 C  C   . ASN C 1 355  ? 43.540  45.876  53.663  1.00 139.70 ? 355  ASN B C   1 
ATOM   15059 O  O   . ASN C 1 355  ? 44.490  46.015  52.910  1.00 136.40 ? 355  ASN B O   1 
ATOM   15060 C  CB  . ASN C 1 355  ? 44.152  43.788  54.867  1.00 152.25 ? 355  ASN B CB  1 
ATOM   15061 C  CG  . ASN C 1 355  ? 45.450  43.619  54.132  1.00 159.37 ? 355  ASN B CG  1 
ATOM   15062 O  OD1 . ASN C 1 355  ? 45.694  42.574  53.534  1.00 159.40 ? 355  ASN B OD1 1 
ATOM   15063 N  ND2 . ASN C 1 355  ? 46.307  44.635  54.190  1.00 165.87 ? 355  ASN B ND2 1 
ATOM   15064 N  N   . LEU C 1 356  ? 42.849  46.887  54.177  1.00 115.45 ? 356  LEU B N   1 
ATOM   15065 C  CA  . LEU C 1 356  ? 43.183  48.265  53.871  1.00 115.62 ? 356  LEU B CA  1 
ATOM   15066 C  C   . LEU C 1 356  ? 44.686  48.453  53.845  1.00 122.11 ? 356  LEU B C   1 
ATOM   15067 O  O   . LEU C 1 356  ? 45.411  47.686  54.477  1.00 127.82 ? 356  LEU B O   1 
ATOM   15068 C  CB  . LEU C 1 356  ? 42.605  49.167  54.936  1.00 120.46 ? 356  LEU B CB  1 
ATOM   15069 C  CG  . LEU C 1 356  ? 41.102  49.295  54.875  1.00 114.77 ? 356  LEU B CG  1 
ATOM   15070 C  CD1 . LEU C 1 356  ? 40.656  50.239  55.953  1.00 117.43 ? 356  LEU B CD1 1 
ATOM   15071 C  CD2 . LEU C 1 356  ? 40.799  49.835  53.513  1.00 112.24 ? 356  LEU B CD2 1 
ATOM   15072 N  N   . VAL C 1 357  ? 45.174  49.464  53.131  1.00 113.53 ? 357  VAL B N   1 
ATOM   15073 C  CA  . VAL C 1 357  ? 46.621  49.662  53.081  1.00 120.31 ? 357  VAL B CA  1 
ATOM   15074 C  C   . VAL C 1 357  ? 47.088  51.108  53.084  1.00 130.09 ? 357  VAL B C   1 
ATOM   15075 O  O   . VAL C 1 357  ? 46.718  51.870  52.209  1.00 122.46 ? 357  VAL B O   1 
ATOM   15076 C  CB  . VAL C 1 357  ? 47.234  49.007  51.859  1.00 120.57 ? 357  VAL B CB  1 
ATOM   15077 C  CG1 . VAL C 1 357  ? 48.740  49.161  51.938  1.00 120.12 ? 357  VAL B CG1 1 
ATOM   15078 C  CG2 . VAL C 1 357  ? 46.839  47.551  51.782  1.00 116.93 ? 357  VAL B CG2 1 
ATOM   15079 N  N   . ALA C 1 358  ? 47.922  51.480  54.048  1.00 155.84 ? 358  ALA B N   1 
ATOM   15080 C  CA  . ALA C 1 358  ? 48.322  52.872  54.183  1.00 163.10 ? 358  ALA B CA  1 
ATOM   15081 C  C   . ALA C 1 358  ? 47.158  53.842  53.875  1.00 159.88 ? 358  ALA B C   1 
ATOM   15082 O  O   . ALA C 1 358  ? 47.311  54.760  53.065  1.00 156.08 ? 358  ALA B O   1 
ATOM   15083 C  CB  . ALA C 1 358  ? 49.520  53.153  53.297  1.00 169.24 ? 358  ALA B CB  1 
ATOM   15084 N  N   . THR C 1 359  ? 46.013  53.632  54.539  1.00 137.31 ? 359  THR B N   1 
ATOM   15085 C  CA  . THR C 1 359  ? 44.783  54.426  54.340  1.00 135.35 ? 359  THR B CA  1 
ATOM   15086 C  C   . THR C 1 359  ? 44.025  54.853  55.624  1.00 133.53 ? 359  THR B C   1 
ATOM   15087 O  O   . THR C 1 359  ? 42.985  54.277  55.945  1.00 126.17 ? 359  THR B O   1 
ATOM   15088 C  CB  . THR C 1 359  ? 43.783  53.690  53.408  1.00 131.62 ? 359  THR B CB  1 
ATOM   15089 O  OG1 . THR C 1 359  ? 43.687  52.308  53.774  1.00 130.83 ? 359  THR B OG1 1 
ATOM   15090 C  CG2 . THR C 1 359  ? 44.250  53.763  51.978  1.00 129.03 ? 359  THR B CG2 1 
ATOM   15091 N  N   . PRO C 1 360  ? 44.522  55.893  56.331  1.00 169.29 ? 360  PRO B N   1 
ATOM   15092 C  CA  . PRO C 1 360  ? 43.975  56.396  57.605  1.00 170.59 ? 360  PRO B CA  1 
ATOM   15093 C  C   . PRO C 1 360  ? 42.441  56.425  57.635  1.00 166.23 ? 360  PRO B C   1 
ATOM   15094 O  O   . PRO C 1 360  ? 41.852  56.670  56.577  1.00 155.59 ? 360  PRO B O   1 
ATOM   15095 C  CB  . PRO C 1 360  ? 44.499  57.832  57.653  1.00 176.01 ? 360  PRO B CB  1 
ATOM   15096 C  CG  . PRO C 1 360  ? 45.787  57.791  56.905  1.00 178.80 ? 360  PRO B CG  1 
ATOM   15097 C  CD  . PRO C 1 360  ? 45.653  56.714  55.859  1.00 173.24 ? 360  PRO B CD  1 
ATOM   15098 N  N   . LEU C 1 361  ? 41.816  56.209  58.801  1.00 137.93 ? 361  LEU B N   1 
ATOM   15099 C  CA  . LEU C 1 361  ? 40.342  56.198  58.905  1.00 120.61 ? 361  LEU B CA  1 
ATOM   15100 C  C   . LEU C 1 361  ? 39.699  57.453  59.534  1.00 131.40 ? 361  LEU B C   1 
ATOM   15101 O  O   . LEU C 1 361  ? 38.766  57.375  60.324  1.00 129.88 ? 361  LEU B O   1 
ATOM   15102 C  CB  . LEU C 1 361  ? 39.849  54.923  59.585  1.00 132.17 ? 361  LEU B CB  1 
ATOM   15103 C  CG  . LEU C 1 361  ? 40.099  53.602  58.844  1.00 126.38 ? 361  LEU B CG  1 
ATOM   15104 C  CD1 . LEU C 1 361  ? 41.593  53.309  58.582  1.00 125.94 ? 361  LEU B CD1 1 
ATOM   15105 C  CD2 . LEU C 1 361  ? 39.434  52.472  59.623  1.00 126.62 ? 361  LEU B CD2 1 
ATOM   15106 N  N   . PHE C 1 362  ? 40.234  58.605  59.149  1.00 205.32 ? 362  PHE B N   1 
ATOM   15107 C  CA  . PHE C 1 362  ? 39.603  59.896  59.375  1.00 213.09 ? 362  PHE B CA  1 
ATOM   15108 C  C   . PHE C 1 362  ? 39.678  60.714  58.094  1.00 203.76 ? 362  PHE B C   1 
ATOM   15109 O  O   . PHE C 1 362  ? 40.755  60.982  57.538  1.00 202.34 ? 362  PHE B O   1 
ATOM   15110 C  CB  . PHE C 1 362  ? 40.264  60.637  60.519  1.00 232.70 ? 362  PHE B CB  1 
ATOM   15111 C  CG  . PHE C 1 362  ? 40.631  59.751  61.622  1.00 246.18 ? 362  PHE B CG  1 
ATOM   15112 C  CD1 . PHE C 1 362  ? 41.922  59.308  61.757  1.00 253.15 ? 362  PHE B CD1 1 
ATOM   15113 C  CD2 . PHE C 1 362  ? 39.673  59.301  62.486  1.00 249.38 ? 362  PHE B CD2 1 
ATOM   15114 C  CE1 . PHE C 1 362  ? 42.259  58.462  62.760  1.00 259.49 ? 362  PHE B CE1 1 
ATOM   15115 C  CE2 . PHE C 1 362  ? 40.000  58.456  63.494  1.00 255.01 ? 362  PHE B CE2 1 
ATOM   15116 C  CZ  . PHE C 1 362  ? 41.297  58.031  63.636  1.00 259.74 ? 362  PHE B CZ  1 
ATOM   15117 N  N   . LEU C 1 363  ? 38.511  61.098  57.620  1.00 138.80 ? 363  LEU B N   1 
ATOM   15118 C  CA  . LEU C 1 363  ? 38.422  61.906  56.449  1.00 133.66 ? 363  LEU B CA  1 
ATOM   15119 C  C   . LEU C 1 363  ? 38.331  63.347  56.901  1.00 134.08 ? 363  LEU B C   1 
ATOM   15120 O  O   . LEU C 1 363  ? 37.354  63.741  57.514  1.00 132.94 ? 363  LEU B O   1 
ATOM   15121 C  CB  . LEU C 1 363  ? 37.165  61.475  55.701  1.00 124.60 ? 363  LEU B CB  1 
ATOM   15122 C  CG  . LEU C 1 363  ? 36.046  61.051  56.660  1.00 125.23 ? 363  LEU B CG  1 
ATOM   15123 C  CD1 . LEU C 1 363  ? 35.121  62.241  56.886  1.00 127.85 ? 363  LEU B CD1 1 
ATOM   15124 C  CD2 . LEU C 1 363  ? 35.286  59.839  56.139  1.00 118.37 ? 363  LEU B CD2 1 
ATOM   15125 N  N   . LYS C 1 364  ? 39.376  64.119  56.649  1.00 146.60 ? 364  LYS B N   1 
ATOM   15126 C  CA  . LYS C 1 364  ? 39.263  65.563  56.744  1.00 145.65 ? 364  LYS B CA  1 
ATOM   15127 C  C   . LYS C 1 364  ? 38.136  65.964  55.753  1.00 144.74 ? 364  LYS B C   1 
ATOM   15128 O  O   . LYS C 1 364  ? 37.867  65.219  54.811  1.00 138.18 ? 364  LYS B O   1 
ATOM   15129 C  CB  . LYS C 1 364  ? 40.608  66.232  56.422  1.00 152.46 ? 364  LYS B CB  1 
ATOM   15130 C  CG  . LYS C 1 364  ? 41.787  65.660  57.198  1.00 160.72 ? 364  LYS B CG  1 
ATOM   15131 C  CD  . LYS C 1 364  ? 41.958  64.170  56.960  1.00 158.87 ? 364  LYS B CD  1 
ATOM   15132 C  CE  . LYS C 1 364  ? 43.311  63.744  57.409  1.00 165.19 ? 364  LYS B CE  1 
ATOM   15133 N  NZ  . LYS C 1 364  ? 43.715  64.652  58.498  1.00 173.51 ? 364  LYS B NZ  1 
ATOM   15134 N  N   . PRO C 1 365  ? 37.423  67.096  55.999  1.00 196.41 ? 365  PRO B N   1 
ATOM   15135 C  CA  . PRO C 1 365  ? 36.312  67.484  55.108  1.00 193.88 ? 365  PRO B CA  1 
ATOM   15136 C  C   . PRO C 1 365  ? 36.756  68.209  53.846  1.00 197.90 ? 365  PRO B C   1 
ATOM   15137 O  O   . PRO C 1 365  ? 37.859  68.756  53.793  1.00 204.97 ? 365  PRO B O   1 
ATOM   15138 C  CB  . PRO C 1 365  ? 35.472  68.441  55.975  1.00 195.42 ? 365  PRO B CB  1 
ATOM   15139 C  CG  . PRO C 1 365  ? 35.939  68.264  57.362  1.00 199.06 ? 365  PRO B CG  1 
ATOM   15140 C  CD  . PRO C 1 365  ? 37.396  67.884  57.246  1.00 201.78 ? 365  PRO B CD  1 
ATOM   15141 N  N   . GLY C 1 366  ? 35.889  68.229  52.841  1.00 184.60 ? 366  GLY B N   1 
ATOM   15142 C  CA  . GLY C 1 366  ? 36.236  68.853  51.580  1.00 192.72 ? 366  GLY B CA  1 
ATOM   15143 C  C   . GLY C 1 366  ? 37.242  68.025  50.805  1.00 185.63 ? 366  GLY B C   1 
ATOM   15144 O  O   . GLY C 1 366  ? 37.099  67.852  49.598  1.00 183.21 ? 366  GLY B O   1 
ATOM   15145 N  N   . ILE C 1 367  ? 38.260  67.507  51.486  1.00 182.12 ? 367  ILE B N   1 
ATOM   15146 C  CA  . ILE C 1 367  ? 39.214  66.623  50.823  1.00 177.43 ? 367  ILE B CA  1 
ATOM   15147 C  C   . ILE C 1 367  ? 38.527  65.326  50.365  1.00 169.03 ? 367  ILE B C   1 
ATOM   15148 O  O   . ILE C 1 367  ? 37.479  64.944  50.897  1.00 166.63 ? 367  ILE B O   1 
ATOM   15149 C  CB  . ILE C 1 367  ? 40.466  66.365  51.709  1.00 183.06 ? 367  ILE B CB  1 
ATOM   15150 C  CG1 . ILE C 1 367  ? 41.380  67.586  51.654  1.00 188.47 ? 367  ILE B CG1 1 
ATOM   15151 C  CG2 . ILE C 1 367  ? 41.223  65.121  51.269  1.00 180.36 ? 367  ILE B CG2 1 
ATOM   15152 C  CD1 . ILE C 1 367  ? 42.681  67.418  52.378  1.00 193.94 ? 367  ILE B CD1 1 
ATOM   15153 N  N   . PRO C 1 368  ? 39.075  64.688  49.320  1.00 135.09 ? 368  PRO B N   1 
ATOM   15154 C  CA  . PRO C 1 368  ? 38.628  63.358  48.914  1.00 128.00 ? 368  PRO B CA  1 
ATOM   15155 C  C   . PRO C 1 368  ? 39.347  62.298  49.719  1.00 125.14 ? 368  PRO B C   1 
ATOM   15156 O  O   . PRO C 1 368  ? 40.557  62.369  49.981  1.00 131.13 ? 368  PRO B O   1 
ATOM   15157 C  CB  . PRO C 1 368  ? 39.062  63.250  47.442  1.00 122.39 ? 368  PRO B CB  1 
ATOM   15158 C  CG  . PRO C 1 368  ? 39.622  64.550  47.081  1.00 127.85 ? 368  PRO B CG  1 
ATOM   15159 C  CD  . PRO C 1 368  ? 40.016  65.251  48.349  1.00 135.70 ? 368  PRO B CD  1 
ATOM   15160 N  N   . TYR C 1 369  ? 38.573  61.298  50.096  1.00 132.28 ? 369  TYR B N   1 
ATOM   15161 C  CA  . TYR C 1 369  ? 39.072  60.209  50.889  1.00 131.83 ? 369  TYR B CA  1 
ATOM   15162 C  C   . TYR C 1 369  ? 39.679  59.101  49.987  1.00 126.62 ? 369  TYR B C   1 
ATOM   15163 O  O   . TYR C 1 369  ? 39.035  58.609  49.050  1.00 127.47 ? 369  TYR B O   1 
ATOM   15164 C  CB  . TYR C 1 369  ? 37.938  59.729  51.790  1.00 127.93 ? 369  TYR B CB  1 
ATOM   15165 C  CG  . TYR C 1 369  ? 38.372  58.765  52.848  1.00 133.28 ? 369  TYR B CG  1 
ATOM   15166 C  CD1 . TYR C 1 369  ? 39.518  59.009  53.604  1.00 143.16 ? 369  TYR B CD1 1 
ATOM   15167 C  CD2 . TYR C 1 369  ? 37.631  57.613  53.102  1.00 132.68 ? 369  TYR B CD2 1 
ATOM   15168 C  CE1 . TYR C 1 369  ? 39.925  58.125  54.564  1.00 144.82 ? 369  TYR B CE1 1 
ATOM   15169 C  CE2 . TYR C 1 369  ? 38.028  56.722  54.049  1.00 135.94 ? 369  TYR B CE2 1 
ATOM   15170 C  CZ  . TYR C 1 369  ? 39.174  56.978  54.776  1.00 143.35 ? 369  TYR B CZ  1 
ATOM   15171 O  OH  . TYR C 1 369  ? 39.582  56.081  55.720  1.00 147.94 ? 369  TYR B OH  1 
ATOM   15172 N  N   . PRO C 1 370  ? 40.956  58.754  50.245  1.00 126.69 ? 370  PRO B N   1 
ATOM   15173 C  CA  . PRO C 1 370  ? 41.767  57.754  49.526  1.00 124.52 ? 370  PRO B CA  1 
ATOM   15174 C  C   . PRO C 1 370  ? 41.585  56.329  50.038  1.00 117.81 ? 370  PRO B C   1 
ATOM   15175 O  O   . PRO C 1 370  ? 42.226  56.004  51.026  1.00 121.24 ? 370  PRO B O   1 
ATOM   15176 C  CB  . PRO C 1 370  ? 43.218  58.183  49.838  1.00 130.86 ? 370  PRO B CB  1 
ATOM   15177 C  CG  . PRO C 1 370  ? 43.124  59.518  50.518  1.00 125.13 ? 370  PRO B CG  1 
ATOM   15178 C  CD  . PRO C 1 370  ? 41.777  59.571  51.157  1.00 133.82 ? 370  PRO B CD  1 
ATOM   15179 N  N   . ILE C 1 371  ? 40.798  55.477  49.387  1.00 139.70 ? 371  ILE B N   1 
ATOM   15180 C  CA  . ILE C 1 371  ? 40.634  54.104  49.895  1.00 137.45 ? 371  ILE B CA  1 
ATOM   15181 C  C   . ILE C 1 371  ? 41.388  52.984  49.138  1.00 138.46 ? 371  ILE B C   1 
ATOM   15182 O  O   . ILE C 1 371  ? 40.898  52.480  48.124  1.00 132.78 ? 371  ILE B O   1 
ATOM   15183 C  CB  . ILE C 1 371  ? 39.153  53.690  49.961  1.00 134.35 ? 371  ILE B CB  1 
ATOM   15184 C  CG1 . ILE C 1 371  ? 38.255  54.882  50.282  1.00 133.66 ? 371  ILE B CG1 1 
ATOM   15185 C  CG2 . ILE C 1 371  ? 38.981  52.582  50.979  1.00 131.50 ? 371  ILE B CG2 1 
ATOM   15186 C  CD1 . ILE C 1 371  ? 36.803  54.496  50.424  1.00 129.28 ? 371  ILE B CD1 1 
ATOM   15187 N  N   . LYS C 1 372  ? 42.544  52.559  49.653  1.00 116.87 ? 372  LYS B N   1 
ATOM   15188 C  CA  . LYS C 1 372  ? 43.365  51.540  48.983  1.00 114.06 ? 372  LYS B CA  1 
ATOM   15189 C  C   . LYS C 1 372  ? 43.267  50.145  49.605  1.00 112.51 ? 372  LYS B C   1 
ATOM   15190 O  O   . LYS C 1 372  ? 44.123  49.779  50.409  1.00 122.10 ? 372  LYS B O   1 
ATOM   15191 C  CB  . LYS C 1 372  ? 44.840  51.955  48.987  1.00 119.64 ? 372  LYS B CB  1 
ATOM   15192 C  CG  . LYS C 1 372  ? 45.081  53.427  48.744  1.00 129.07 ? 372  LYS B CG  1 
ATOM   15193 C  CD  . LYS C 1 372  ? 46.520  53.837  48.982  1.00 137.69 ? 372  LYS B CD  1 
ATOM   15194 C  CE  . LYS C 1 372  ? 46.589  55.297  49.465  1.00 140.62 ? 372  LYS B CE  1 
ATOM   15195 N  NZ  . LYS C 1 372  ? 47.439  56.170  48.583  1.00 142.46 ? 372  LYS B NZ  1 
ATOM   15196 N  N   . VAL C 1 373  ? 42.246  49.371  49.238  1.00 115.58 ? 373  VAL B N   1 
ATOM   15197 C  CA  . VAL C 1 373  ? 42.143  47.974  49.679  1.00 126.26 ? 373  VAL B CA  1 
ATOM   15198 C  C   . VAL C 1 373  ? 43.201  47.121  48.987  1.00 122.48 ? 373  VAL B C   1 
ATOM   15199 O  O   . VAL C 1 373  ? 43.873  47.626  48.097  1.00 123.78 ? 373  VAL B O   1 
ATOM   15200 C  CB  . VAL C 1 373  ? 40.723  47.421  49.468  1.00 108.33 ? 373  VAL B CB  1 
ATOM   15201 C  CG1 . VAL C 1 373  ? 39.877  48.439  48.729  1.00 106.04 ? 373  VAL B CG1 1 
ATOM   15202 C  CG2 . VAL C 1 373  ? 40.734  46.064  48.763  1.00 104.74 ? 373  VAL B CG2 1 
ATOM   15203 N  N   . GLN C 1 374  ? 43.354  45.852  49.379  1.00 117.45 ? 374  GLN B N   1 
ATOM   15204 C  CA  . GLN C 1 374  ? 44.476  45.031  48.898  1.00 120.29 ? 374  GLN B CA  1 
ATOM   15205 C  C   . GLN C 1 374  ? 44.216  43.525  48.983  1.00 125.05 ? 374  GLN B C   1 
ATOM   15206 O  O   . GLN C 1 374  ? 44.458  42.903  50.015  1.00 132.84 ? 374  GLN B O   1 
ATOM   15207 C  CB  . GLN C 1 374  ? 45.764  45.401  49.659  1.00 125.07 ? 374  GLN B CB  1 
ATOM   15208 C  CG  . GLN C 1 374  ? 46.884  44.385  49.611  1.00 131.23 ? 374  GLN B CG  1 
ATOM   15209 C  CD  . GLN C 1 374  ? 48.130  44.904  50.280  1.00 143.45 ? 374  GLN B CD  1 
ATOM   15210 O  OE1 . GLN C 1 374  ? 48.294  44.777  51.487  1.00 147.79 ? 374  GLN B OE1 1 
ATOM   15211 N  NE2 . GLN C 1 374  ? 49.004  45.528  49.502  1.00 147.33 ? 374  GLN B NE2 1 
ATOM   15212 N  N   . VAL C 1 375  ? 43.735  42.947  47.887  1.00 103.00 ? 375  VAL B N   1 
ATOM   15213 C  CA  . VAL C 1 375  ? 43.364  41.542  47.872  1.00 103.99 ? 375  VAL B CA  1 
ATOM   15214 C  C   . VAL C 1 375  ? 44.569  40.677  48.105  1.00 104.36 ? 375  VAL B C   1 
ATOM   15215 O  O   . VAL C 1 375  ? 45.684  41.064  47.761  1.00 107.89 ? 375  VAL B O   1 
ATOM   15216 C  CB  . VAL C 1 375  ? 42.695  41.133  46.543  1.00 105.44 ? 375  VAL B CB  1 
ATOM   15217 C  CG1 . VAL C 1 375  ? 42.851  39.661  46.288  1.00 101.72 ? 375  VAL B CG1 1 
ATOM   15218 C  CG2 . VAL C 1 375  ? 41.235  41.480  46.570  1.00 99.47  ? 375  VAL B CG2 1 
ATOM   15219 N  N   . LYS C 1 376  ? 44.336  39.522  48.718  1.00 114.37 ? 376  LYS B N   1 
ATOM   15220 C  CA  . LYS C 1 376  ? 45.364  38.521  48.890  1.00 115.28 ? 376  LYS B CA  1 
ATOM   15221 C  C   . LYS C 1 376  ? 44.710  37.165  48.863  1.00 108.52 ? 376  LYS B C   1 
ATOM   15222 O  O   . LYS C 1 376  ? 43.496  37.031  48.846  1.00 109.87 ? 376  LYS B O   1 
ATOM   15223 C  CB  . LYS C 1 376  ? 46.097  38.681  50.224  1.00 122.42 ? 376  LYS B CB  1 
ATOM   15224 C  CG  . LYS C 1 376  ? 47.000  39.916  50.367  1.00 120.66 ? 376  LYS B CG  1 
ATOM   15225 C  CD  . LYS C 1 376  ? 47.443  40.132  51.831  1.00 126.57 ? 376  LYS B CD  1 
ATOM   15226 C  CE  . LYS C 1 376  ? 48.573  41.160  51.970  1.00 132.65 ? 376  LYS B CE  1 
ATOM   15227 N  NZ  . LYS C 1 376  ? 48.489  41.862  53.288  1.00 138.21 ? 376  LYS B NZ  1 
ATOM   15228 N  N   . ASP C 1 377  ? 45.548  36.156  48.899  1.00 117.78 ? 377  ASP B N   1 
ATOM   15229 C  CA  . ASP C 1 377  ? 45.094  34.801  48.804  1.00 118.89 ? 377  ASP B CA  1 
ATOM   15230 C  C   . ASP C 1 377  ? 45.373  34.052  50.090  1.00 127.00 ? 377  ASP B C   1 
ATOM   15231 O  O   . ASP C 1 377  ? 46.139  34.500  50.945  1.00 132.87 ? 377  ASP B O   1 
ATOM   15232 C  CB  . ASP C 1 377  ? 45.926  34.125  47.758  1.00 119.26 ? 377  ASP B CB  1 
ATOM   15233 C  CG  . ASP C 1 377  ? 47.385  34.145  48.115  1.00 127.79 ? 377  ASP B CG  1 
ATOM   15234 O  OD1 . ASP C 1 377  ? 47.867  35.225  48.538  1.00 132.47 ? 377  ASP B OD1 1 
ATOM   15235 O  OD2 . ASP C 1 377  ? 48.023  33.071  48.005  1.00 131.62 ? 377  ASP B OD2 1 
ATOM   15236 N  N   . SER C 1 378  ? 44.791  32.867  50.180  1.00 141.68 ? 378  SER B N   1 
ATOM   15237 C  CA  . SER C 1 378  ? 44.964  31.968  51.309  1.00 146.14 ? 378  SER B CA  1 
ATOM   15238 C  C   . SER C 1 378  ? 46.409  31.786  51.769  1.00 128.00 ? 378  SER B C   1 
ATOM   15239 O  O   . SER C 1 378  ? 46.658  31.141  52.778  1.00 131.04 ? 378  SER B O   1 
ATOM   15240 C  CB  . SER C 1 378  ? 44.401  30.610  50.900  1.00 145.44 ? 378  SER B CB  1 
ATOM   15241 O  OG  . SER C 1 378  ? 44.196  30.574  49.477  1.00 141.59 ? 378  SER B OG  1 
ATOM   15242 N  N   . LEU C 1 379  ? 47.350  32.354  51.024  1.00 128.73 ? 379  LEU B N   1 
ATOM   15243 C  CA  . LEU C 1 379  ? 48.777  32.146  51.247  1.00 138.05 ? 379  LEU B CA  1 
ATOM   15244 C  C   . LEU C 1 379  ? 49.557  33.445  51.436  1.00 149.40 ? 379  LEU B C   1 
ATOM   15245 O  O   . LEU C 1 379  ? 50.791  33.450  51.528  1.00 157.04 ? 379  LEU B O   1 
ATOM   15246 C  CB  . LEU C 1 379  ? 49.353  31.382  50.073  1.00 136.04 ? 379  LEU B CB  1 
ATOM   15247 C  CG  . LEU C 1 379  ? 49.646  29.938  50.438  1.00 137.45 ? 379  LEU B CG  1 
ATOM   15248 C  CD1 . LEU C 1 379  ? 49.654  29.003  49.215  1.00 134.82 ? 379  LEU B CD1 1 
ATOM   15249 C  CD2 . LEU C 1 379  ? 50.965  29.894  51.228  1.00 142.43 ? 379  LEU B CD2 1 
ATOM   15250 N  N   . ASP C 1 380  ? 48.815  34.546  51.451  1.00 184.04 ? 380  ASP B N   1 
ATOM   15251 C  CA  . ASP C 1 380  ? 49.342  35.859  51.796  1.00 192.49 ? 380  ASP B CA  1 
ATOM   15252 C  C   . ASP C 1 380  ? 50.365  36.418  50.825  1.00 196.78 ? 380  ASP B C   1 
ATOM   15253 O  O   . ASP C 1 380  ? 51.345  37.029  51.241  1.00 201.95 ? 380  ASP B O   1 
ATOM   15254 C  CB  . ASP C 1 380  ? 49.907  35.868  53.218  1.00 204.03 ? 380  ASP B CB  1 
ATOM   15255 C  CG  . ASP C 1 380  ? 48.827  36.033  54.276  1.00 209.69 ? 380  ASP B CG  1 
ATOM   15256 O  OD1 . ASP C 1 380  ? 48.088  37.040  54.225  1.00 208.59 ? 380  ASP B OD1 1 
ATOM   15257 O  OD2 . ASP C 1 380  ? 48.722  35.154  55.162  1.00 215.87 ? 380  ASP B OD2 1 
ATOM   15258 N  N   . GLN C 1 381  ? 50.142  36.188  49.537  1.00 184.33 ? 381  GLN B N   1 
ATOM   15259 C  CA  . GLN C 1 381  ? 50.808  36.965  48.503  1.00 186.69 ? 381  GLN B CA  1 
ATOM   15260 C  C   . GLN C 1 381  ? 49.782  37.920  47.953  1.00 179.60 ? 381  GLN B C   1 
ATOM   15261 O  O   . GLN C 1 381  ? 48.582  37.691  48.101  1.00 173.78 ? 381  GLN B O   1 
ATOM   15262 C  CB  . GLN C 1 381  ? 51.294  36.091  47.358  1.00 189.88 ? 381  GLN B CB  1 
ATOM   15263 C  CG  . GLN C 1 381  ? 52.359  35.089  47.724  1.00 199.12 ? 381  GLN B CG  1 
ATOM   15264 C  CD  . GLN C 1 381  ? 52.031  33.712  47.187  1.00 201.22 ? 381  GLN B CD  1 
ATOM   15265 O  OE1 . GLN C 1 381  ? 52.555  33.284  46.148  1.00 203.72 ? 381  GLN B OE1 1 
ATOM   15266 N  NE2 . GLN C 1 381  ? 51.139  33.011  47.887  1.00 198.96 ? 381  GLN B NE2 1 
ATOM   15267 N  N   . LEU C 1 382  ? 50.243  38.982  47.305  1.00 150.37 ? 382  LEU B N   1 
ATOM   15268 C  CA  . LEU C 1 382  ? 49.328  39.898  46.647  1.00 143.15 ? 382  LEU B CA  1 
ATOM   15269 C  C   . LEU C 1 382  ? 48.747  39.183  45.456  1.00 139.39 ? 382  LEU B C   1 
ATOM   15270 O  O   . LEU C 1 382  ? 49.403  38.321  44.891  1.00 143.83 ? 382  LEU B O   1 
ATOM   15271 C  CB  . LEU C 1 382  ? 50.082  41.121  46.169  1.00 145.37 ? 382  LEU B CB  1 
ATOM   15272 C  CG  . LEU C 1 382  ? 50.465  42.032  47.328  1.00 149.97 ? 382  LEU B CG  1 
ATOM   15273 C  CD1 . LEU C 1 382  ? 51.276  43.215  46.845  1.00 154.75 ? 382  LEU B CD1 1 
ATOM   15274 C  CD2 . LEU C 1 382  ? 49.195  42.490  48.012  1.00 145.27 ? 382  LEU B CD2 1 
ATOM   15275 N  N   . VAL C 1 383  ? 47.520  39.508  45.071  1.00 129.46 ? 383  VAL B N   1 
ATOM   15276 C  CA  . VAL C 1 383  ? 46.950  38.916  43.859  1.00 121.83 ? 383  VAL B CA  1 
ATOM   15277 C  C   . VAL C 1 383  ? 46.214  39.964  43.080  1.00 119.96 ? 383  VAL B C   1 
ATOM   15278 O  O   . VAL C 1 383  ? 45.262  40.571  43.572  1.00 118.87 ? 383  VAL B O   1 
ATOM   15279 C  CB  . VAL C 1 383  ? 46.027  37.703  44.145  1.00 113.39 ? 383  VAL B CB  1 
ATOM   15280 C  CG1 . VAL C 1 383  ? 45.710  37.630  45.605  1.00 116.44 ? 383  VAL B CG1 1 
ATOM   15281 C  CG2 . VAL C 1 383  ? 44.746  37.776  43.316  1.00 115.64 ? 383  VAL B CG2 1 
ATOM   15282 N  N   . GLY C 1 384  ? 46.679  40.184  41.856  1.00 129.28 ? 384  GLY B N   1 
ATOM   15283 C  CA  . GLY C 1 384  ? 46.221  41.314  41.077  1.00 128.23 ? 384  GLY B CA  1 
ATOM   15284 C  C   . GLY C 1 384  ? 45.029  40.979  40.219  1.00 125.18 ? 384  GLY B C   1 
ATOM   15285 O  O   . GLY C 1 384  ? 44.688  39.805  40.065  1.00 124.83 ? 384  GLY B O   1 
ATOM   15286 N  N   . GLY C 1 385  ? 44.395  42.014  39.674  1.00 119.27 ? 385  GLY B N   1 
ATOM   15287 C  CA  . GLY C 1 385  ? 43.408  41.848  38.626  1.00 114.18 ? 385  GLY B CA  1 
ATOM   15288 C  C   . GLY C 1 385  ? 42.100  41.262  39.103  1.00 109.46 ? 385  GLY B C   1 
ATOM   15289 O  O   . GLY C 1 385  ? 41.600  40.274  38.553  1.00 106.85 ? 385  GLY B O   1 
ATOM   15290 N  N   . VAL C 1 386  ? 41.526  41.879  40.121  1.00 109.20 ? 386  VAL B N   1 
ATOM   15291 C  CA  . VAL C 1 386  ? 40.354  41.304  40.722  1.00 104.04 ? 386  VAL B CA  1 
ATOM   15292 C  C   . VAL C 1 386  ? 39.407  42.407  41.086  1.00 97.42  ? 386  VAL B C   1 
ATOM   15293 O  O   . VAL C 1 386  ? 39.849  43.449  41.533  1.00 100.09 ? 386  VAL B O   1 
ATOM   15294 C  CB  . VAL C 1 386  ? 40.743  40.484  41.988  1.00 96.15  ? 386  VAL B CB  1 
ATOM   15295 C  CG1 . VAL C 1 386  ? 39.890  39.210  42.113  1.00 91.32  ? 386  VAL B CG1 1 
ATOM   15296 C  CG2 . VAL C 1 386  ? 42.227  40.106  41.980  1.00 100.28 ? 386  VAL B CG2 1 
ATOM   15297 N  N   . PRO C 1 387  ? 38.102  42.156  40.915  1.00 108.22 ? 387  PRO B N   1 
ATOM   15298 C  CA  . PRO C 1 387  ? 36.957  43.024  41.220  1.00 111.37 ? 387  PRO B CA  1 
ATOM   15299 C  C   . PRO C 1 387  ? 36.850  43.405  42.733  1.00 115.59 ? 387  PRO B C   1 
ATOM   15300 O  O   . PRO C 1 387  ? 37.250  42.622  43.587  1.00 118.29 ? 387  PRO B O   1 
ATOM   15301 C  CB  . PRO C 1 387  ? 35.740  42.187  40.781  1.00 110.50 ? 387  PRO B CB  1 
ATOM   15302 C  CG  . PRO C 1 387  ? 36.263  40.881  40.319  1.00 102.55 ? 387  PRO B CG  1 
ATOM   15303 C  CD  . PRO C 1 387  ? 37.689  40.773  40.659  1.00 104.14 ? 387  PRO B CD  1 
ATOM   15304 N  N   . VAL C 1 388  ? 36.282  44.573  43.053  1.00 114.73 ? 388  VAL B N   1 
ATOM   15305 C  CA  . VAL C 1 388  ? 36.387  45.159  44.382  1.00 116.92 ? 388  VAL B CA  1 
ATOM   15306 C  C   . VAL C 1 388  ? 35.259  46.149  44.712  1.00 118.74 ? 388  VAL B C   1 
ATOM   15307 O  O   . VAL C 1 388  ? 35.523  47.298  45.009  1.00 121.87 ? 388  VAL B O   1 
ATOM   15308 C  CB  . VAL C 1 388  ? 37.728  45.916  44.493  1.00 121.32 ? 388  VAL B CB  1 
ATOM   15309 C  CG1 . VAL C 1 388  ? 37.848  46.627  45.805  1.00 125.84 ? 388  VAL B CG1 1 
ATOM   15310 C  CG2 . VAL C 1 388  ? 38.891  44.968  44.327  1.00 121.39 ? 388  VAL B CG2 1 
ATOM   15311 N  N   . THR C 1 389  ? 34.006  45.704  44.682  1.00 142.68 ? 389  THR B N   1 
ATOM   15312 C  CA  . THR C 1 389  ? 32.858  46.594  44.926  1.00 144.26 ? 389  THR B CA  1 
ATOM   15313 C  C   . THR C 1 389  ? 32.898  47.356  46.268  1.00 148.15 ? 389  THR B C   1 
ATOM   15314 O  O   . THR C 1 389  ? 32.902  46.736  47.337  1.00 153.31 ? 389  THR B O   1 
ATOM   15315 C  CB  . THR C 1 389  ? 31.516  45.839  44.840  1.00 155.88 ? 389  THR B CB  1 
ATOM   15316 O  OG1 . THR C 1 389  ? 31.728  44.525  44.329  1.00 154.64 ? 389  THR B OG1 1 
ATOM   15317 C  CG2 . THR C 1 389  ? 30.544  46.561  43.937  1.00 155.31 ? 389  THR B CG2 1 
ATOM   15318 N  N   . LEU C 1 390  ? 32.888  48.693  46.212  1.00 113.61 ? 390  LEU B N   1 
ATOM   15319 C  CA  . LEU C 1 390  ? 32.899  49.519  47.426  1.00 113.75 ? 390  LEU B CA  1 
ATOM   15320 C  C   . LEU C 1 390  ? 31.567  50.217  47.674  1.00 119.21 ? 390  LEU B C   1 
ATOM   15321 O  O   . LEU C 1 390  ? 31.332  51.279  47.129  1.00 124.47 ? 390  LEU B O   1 
ATOM   15322 C  CB  . LEU C 1 390  ? 34.017  50.575  47.373  1.00 113.14 ? 390  LEU B CB  1 
ATOM   15323 C  CG  . LEU C 1 390  ? 34.058  51.515  48.581  1.00 118.52 ? 390  LEU B CG  1 
ATOM   15324 C  CD1 . LEU C 1 390  ? 34.147  50.658  49.803  1.00 124.78 ? 390  LEU B CD1 1 
ATOM   15325 C  CD2 . LEU C 1 390  ? 35.216  52.492  48.547  1.00 119.50 ? 390  LEU B CD2 1 
ATOM   15326 N  N   . ASN C 1 391  ? 30.705  49.633  48.499  1.00 144.56 ? 391  ASN B N   1 
ATOM   15327 C  CA  . ASN C 1 391  ? 29.507  50.333  48.950  1.00 149.39 ? 391  ASN B CA  1 
ATOM   15328 C  C   . ASN C 1 391  ? 29.775  51.191  50.166  1.00 155.66 ? 391  ASN B C   1 
ATOM   15329 O  O   . ASN C 1 391  ? 30.467  50.778  51.089  1.00 159.43 ? 391  ASN B O   1 
ATOM   15330 C  CB  . ASN C 1 391  ? 28.412  49.357  49.285  1.00 152.41 ? 391  ASN B CB  1 
ATOM   15331 C  CG  . ASN C 1 391  ? 27.882  48.682  48.076  1.00 153.82 ? 391  ASN B CG  1 
ATOM   15332 O  OD1 . ASN C 1 391  ? 28.631  48.082  47.301  1.00 151.19 ? 391  ASN B OD1 1 
ATOM   15333 N  ND2 . ASN C 1 391  ? 26.579  48.781  47.885  1.00 157.33 ? 391  ASN B ND2 1 
ATOM   15334 N  N   . ALA C 1 392  ? 29.198  52.378  50.194  1.00 144.45 ? 392  ALA B N   1 
ATOM   15335 C  CA  . ALA C 1 392  ? 29.467  53.281  51.291  1.00 147.08 ? 392  ALA B CA  1 
ATOM   15336 C  C   . ALA C 1 392  ? 28.161  53.760  51.927  1.00 147.14 ? 392  ALA B C   1 
ATOM   15337 O  O   . ALA C 1 392  ? 27.081  53.580  51.352  1.00 146.42 ? 392  ALA B O   1 
ATOM   15338 C  CB  . ALA C 1 392  ? 30.308  54.451  50.808  1.00 148.00 ? 392  ALA B CB  1 
ATOM   15339 N  N   . GLN C 1 393  ? 28.281  54.329  53.135  1.00 153.33 ? 393  GLN B N   1 
ATOM   15340 C  CA  . GLN C 1 393  ? 27.192  54.980  53.883  1.00 160.81 ? 393  GLN B CA  1 
ATOM   15341 C  C   . GLN C 1 393  ? 27.781  56.088  54.754  1.00 165.26 ? 393  GLN B C   1 
ATOM   15342 O  O   . GLN C 1 393  ? 28.933  56.033  55.192  1.00 163.92 ? 393  GLN B O   1 
ATOM   15343 C  CB  . GLN C 1 393  ? 26.435  53.985  54.768  1.00 162.67 ? 393  GLN B CB  1 
ATOM   15344 C  CG  . GLN C 1 393  ? 25.102  54.493  55.344  1.00 165.28 ? 393  GLN B CG  1 
ATOM   15345 C  CD  . GLN C 1 393  ? 25.177  54.927  56.820  1.00 169.48 ? 393  GLN B CD  1 
ATOM   15346 O  OE1 . GLN C 1 393  ? 24.502  55.874  57.233  1.00 172.56 ? 393  GLN B OE1 1 
ATOM   15347 N  NE2 . GLN C 1 393  ? 25.986  54.227  57.613  1.00 169.49 ? 393  GLN B NE2 1 
ATOM   15348 N  N   . THR C 1 394  ? 26.987  57.108  55.002  1.00 196.35 ? 394  THR B N   1 
ATOM   15349 C  CA  . THR C 1 394  ? 27.503  58.249  55.713  1.00 202.83 ? 394  THR B CA  1 
ATOM   15350 C  C   . THR C 1 394  ? 26.327  59.033  56.230  1.00 215.13 ? 394  THR B C   1 
ATOM   15351 O  O   . THR C 1 394  ? 25.187  58.728  55.880  1.00 217.98 ? 394  THR B O   1 
ATOM   15352 C  CB  . THR C 1 394  ? 28.379  59.116  54.792  1.00 196.36 ? 394  THR B CB  1 
ATOM   15353 O  OG1 . THR C 1 394  ? 29.713  59.154  55.313  1.00 195.02 ? 394  THR B OG1 1 
ATOM   15354 C  CG2 . THR C 1 394  ? 27.827  60.542  54.661  1.00 198.88 ? 394  THR B CG2 1 
ATOM   15355 N  N   . ILE C 1 395  ? 26.598  60.007  57.096  1.00 182.84 ? 395  ILE B N   1 
ATOM   15356 C  CA  . ILE C 1 395  ? 25.566  60.921  57.551  1.00 189.28 ? 395  ILE B CA  1 
ATOM   15357 C  C   . ILE C 1 395  ? 26.103  62.335  57.636  1.00 197.19 ? 395  ILE B C   1 
ATOM   15358 O  O   . ILE C 1 395  ? 27.309  62.567  57.651  1.00 198.45 ? 395  ILE B O   1 
ATOM   15359 C  CB  . ILE C 1 395  ? 25.014  60.515  58.902  1.00 191.44 ? 395  ILE B CB  1 
ATOM   15360 C  CG1 . ILE C 1 395  ? 25.970  60.960  60.005  1.00 193.25 ? 395  ILE B CG1 1 
ATOM   15361 C  CG2 . ILE C 1 395  ? 24.774  59.017  58.933  1.00 189.18 ? 395  ILE B CG2 1 
ATOM   15362 C  CD1 . ILE C 1 395  ? 25.250  61.420  61.271  1.00 198.49 ? 395  ILE B CD1 1 
ATOM   15363 N  N   . ASP C 1 396  ? 25.179  63.278  57.667  1.00 163.60 ? 396  ASP B N   1 
ATOM   15364 C  CA  . ASP C 1 396  ? 25.515  64.674  57.675  1.00 168.05 ? 396  ASP B CA  1 
ATOM   15365 C  C   . ASP C 1 396  ? 25.879  64.977  59.097  1.00 172.34 ? 396  ASP B C   1 
ATOM   15366 O  O   . ASP C 1 396  ? 25.633  64.162  59.969  1.00 173.74 ? 396  ASP B O   1 
ATOM   15367 C  CB  . ASP C 1 396  ? 24.272  65.467  57.301  1.00 173.10 ? 396  ASP B CB  1 
ATOM   15368 C  CG  . ASP C 1 396  ? 24.575  66.666  56.419  1.00 179.69 ? 396  ASP B CG  1 
ATOM   15369 O  OD1 . ASP C 1 396  ? 23.624  67.424  56.132  1.00 184.40 ? 396  ASP B OD1 1 
ATOM   15370 O  OD2 . ASP C 1 396  ? 25.744  66.856  56.002  1.00 179.68 ? 396  ASP B OD2 1 
ATOM   15371 N  N   . VAL C 1 397  ? 26.474  66.142  59.330  1.00 212.92 ? 397  VAL B N   1 
ATOM   15372 C  CA  . VAL C 1 397  ? 26.477  66.744  60.657  1.00 220.15 ? 397  VAL B CA  1 
ATOM   15373 C  C   . VAL C 1 397  ? 25.011  67.065  60.937  1.00 224.50 ? 397  VAL B C   1 
ATOM   15374 O  O   . VAL C 1 397  ? 24.560  67.089  62.085  1.00 227.69 ? 397  VAL B O   1 
ATOM   15375 C  CB  . VAL C 1 397  ? 27.338  68.035  60.701  1.00 224.13 ? 397  VAL B CB  1 
ATOM   15376 C  CG1 . VAL C 1 397  ? 26.547  69.248  60.207  1.00 226.31 ? 397  VAL B CG1 1 
ATOM   15377 C  CG2 . VAL C 1 397  ? 27.878  68.278  62.103  1.00 230.75 ? 397  VAL B CG2 1 
ATOM   15378 N  N   . ASN C 1 398  ? 24.271  67.283  59.853  1.00 247.13 ? 398  ASN B N   1 
ATOM   15379 C  CA  . ASN C 1 398  ? 22.834  67.523  59.889  1.00 250.12 ? 398  ASN B CA  1 
ATOM   15380 C  C   . ASN C 1 398  ? 22.058  66.295  60.342  1.00 247.55 ? 398  ASN B C   1 
ATOM   15381 O  O   . ASN C 1 398  ? 20.843  66.227  60.154  1.00 245.70 ? 398  ASN B O   1 
ATOM   15382 C  CB  . ASN C 1 398  ? 22.349  67.900  58.488  1.00 250.44 ? 398  ASN B CB  1 
ATOM   15383 C  CG  . ASN C 1 398  ? 21.569  69.193  58.462  1.00 257.43 ? 398  ASN B CG  1 
ATOM   15384 O  OD1 . ASN C 1 398  ? 21.496  69.900  59.461  1.00 264.31 ? 398  ASN B OD1 1 
ATOM   15385 N  ND2 . ASN C 1 398  ? 20.981  69.513  57.311  1.00 256.32 ? 398  ASN B ND2 1 
ATOM   15386 N  N   . GLN C 1 399  ? 22.759  65.328  60.932  1.00 217.42 ? 399  GLN B N   1 
ATOM   15387 C  CA  . GLN C 1 399  ? 22.191  64.005  61.196  1.00 217.44 ? 399  GLN B CA  1 
ATOM   15388 C  C   . GLN C 1 399  ? 21.251  63.605  60.058  1.00 214.38 ? 399  GLN B C   1 
ATOM   15389 O  O   . GLN C 1 399  ? 20.089  63.249  60.295  1.00 214.54 ? 399  GLN B O   1 
ATOM   15390 C  CB  . GLN C 1 399  ? 21.484  63.928  62.559  1.00 223.39 ? 399  GLN B CB  1 
ATOM   15391 C  CG  . GLN C 1 399  ? 22.416  63.992  63.772  1.00 227.78 ? 399  GLN B CG  1 
ATOM   15392 C  CD  . GLN C 1 399  ? 23.353  62.802  63.872  1.00 225.20 ? 399  GLN B CD  1 
ATOM   15393 O  OE1 . GLN C 1 399  ? 22.911  61.661  63.978  1.00 224.04 ? 399  GLN B OE1 1 
ATOM   15394 N  NE2 . GLN C 1 399  ? 24.657  63.066  63.848  1.00 223.93 ? 399  GLN B NE2 1 
ATOM   15395 N  N   . GLU C 1 400  ? 21.772  63.696  58.828  1.00 232.66 ? 400  GLU B N   1 
ATOM   15396 C  CA  . GLU C 1 400  ? 21.079  63.263  57.610  1.00 229.91 ? 400  GLU B CA  1 
ATOM   15397 C  C   . GLU C 1 400  ? 21.908  62.174  56.919  1.00 220.29 ? 400  GLU B C   1 
ATOM   15398 O  O   . GLU C 1 400  ? 23.080  62.385  56.635  1.00 217.41 ? 400  GLU B O   1 
ATOM   15399 C  CB  . GLU C 1 400  ? 20.875  64.452  56.667  1.00 233.23 ? 400  GLU B CB  1 
ATOM   15400 C  CG  . GLU C 1 400  ? 19.677  64.312  55.742  1.00 238.06 ? 400  GLU B CG  1 
ATOM   15401 C  CD  . GLU C 1 400  ? 19.211  65.651  55.184  1.00 245.56 ? 400  GLU B CD  1 
ATOM   15402 O  OE1 . GLU C 1 400  ? 18.063  66.056  55.456  1.00 250.09 ? 400  GLU B OE1 1 
ATOM   15403 O  OE2 . GLU C 1 400  ? 19.995  66.310  54.474  1.00 246.54 ? 400  GLU B OE2 1 
ATOM   15404 N  N   . THR C 1 401  ? 21.311  61.009  56.672  1.00 227.51 ? 401  THR B N   1 
ATOM   15405 C  CA  . THR C 1 401  ? 22.056  59.892  56.094  1.00 218.23 ? 401  THR B CA  1 
ATOM   15406 C  C   . THR C 1 401  ? 22.236  60.061  54.611  1.00 211.40 ? 401  THR B C   1 
ATOM   15407 O  O   . THR C 1 401  ? 21.635  60.946  53.997  1.00 215.05 ? 401  THR B O   1 
ATOM   15408 C  CB  . THR C 1 401  ? 21.349  58.534  56.248  1.00 217.01 ? 401  THR B CB  1 
ATOM   15409 O  OG1 . THR C 1 401  ? 20.193  58.493  55.398  1.00 217.20 ? 401  THR B OG1 1 
ATOM   15410 C  CG2 . THR C 1 401  ? 20.964  58.284  57.673  1.00 221.33 ? 401  THR B CG2 1 
ATOM   15411 N  N   . SER C 1 402  ? 23.048  59.171  54.048  1.00 197.64 ? 402  SER B N   1 
ATOM   15412 C  CA  . SER C 1 402  ? 23.221  59.061  52.615  1.00 189.22 ? 402  SER B CA  1 
ATOM   15413 C  C   . SER C 1 402  ? 23.642  57.638  52.283  1.00 180.01 ? 402  SER B C   1 
ATOM   15414 O  O   . SER C 1 402  ? 24.607  57.119  52.853  1.00 174.82 ? 402  SER B O   1 
ATOM   15415 C  CB  . SER C 1 402  ? 24.247  60.084  52.094  1.00 189.44 ? 402  SER B CB  1 
ATOM   15416 O  OG  . SER C 1 402  ? 25.365  60.215  52.957  1.00 189.71 ? 402  SER B OG  1 
ATOM   15417 N  N   . ASP C 1 403  ? 22.880  56.995  51.401  1.00 199.75 ? 403  ASP B N   1 
ATOM   15418 C  CA  . ASP C 1 403  ? 23.329  55.756  50.781  1.00 195.30 ? 403  ASP B CA  1 
ATOM   15419 C  C   . ASP C 1 403  ? 24.051  56.063  49.489  1.00 189.86 ? 403  ASP B C   1 
ATOM   15420 O  O   . ASP C 1 403  ? 23.463  56.500  48.505  1.00 190.85 ? 403  ASP B O   1 
ATOM   15421 C  CB  . ASP C 1 403  ? 22.177  54.799  50.510  1.00 199.47 ? 403  ASP B CB  1 
ATOM   15422 C  CG  . ASP C 1 403  ? 22.302  53.510  51.287  1.00 203.18 ? 403  ASP B CG  1 
ATOM   15423 O  OD1 . ASP C 1 403  ? 23.405  52.916  51.335  1.00 199.41 ? 403  ASP B OD1 1 
ATOM   15424 O  OD2 . ASP C 1 403  ? 21.277  53.095  51.856  1.00 208.73 ? 403  ASP B OD2 1 
ATOM   15425 N  N   . LEU C 1 404  ? 25.346  55.832  49.508  1.00 139.69 ? 404  LEU B N   1 
ATOM   15426 C  CA  . LEU C 1 404  ? 26.147  56.091  48.353  1.00 134.06 ? 404  LEU B CA  1 
ATOM   15427 C  C   . LEU C 1 404  ? 25.907  55.118  47.199  1.00 132.61 ? 404  LEU B C   1 
ATOM   15428 O  O   . LEU C 1 404  ? 25.054  54.209  47.249  1.00 134.36 ? 404  LEU B O   1 
ATOM   15429 C  CB  . LEU C 1 404  ? 27.617  56.081  48.734  1.00 127.14 ? 404  LEU B CB  1 
ATOM   15430 C  CG  . LEU C 1 404  ? 28.174  57.422  49.166  1.00 126.73 ? 404  LEU B CG  1 
ATOM   15431 C  CD1 . LEU C 1 404  ? 29.649  57.253  49.374  1.00 122.40 ? 404  LEU B CD1 1 
ATOM   15432 C  CD2 . LEU C 1 404  ? 27.898  58.440  48.095  1.00 122.95 ? 404  LEU B CD2 1 
ATOM   15433 N  N   . ASP C 1 405  ? 26.706  55.339  46.161  1.00 140.98 ? 405  ASP B N   1 
ATOM   15434 C  CA  . ASP C 1 405  ? 26.580  54.632  44.921  1.00 136.75 ? 405  ASP B CA  1 
ATOM   15435 C  C   . ASP C 1 405  ? 27.809  53.852  44.680  1.00 129.32 ? 405  ASP B C   1 
ATOM   15436 O  O   . ASP C 1 405  ? 28.924  54.374  44.741  1.00 127.59 ? 405  ASP B O   1 
ATOM   15437 C  CB  . ASP C 1 405  ? 26.358  55.605  43.790  1.00 141.45 ? 405  ASP B CB  1 
ATOM   15438 C  CG  . ASP C 1 405  ? 24.924  56.010  43.694  1.00 159.69 ? 405  ASP B CG  1 
ATOM   15439 O  OD1 . ASP C 1 405  ? 24.082  55.079  43.866  1.00 161.89 ? 405  ASP B OD1 1 
ATOM   15440 O  OD2 . ASP C 1 405  ? 24.644  57.222  43.476  1.00 159.46 ? 405  ASP B OD2 1 
ATOM   15441 N  N   . PRO C 1 406  ? 27.587  52.591  44.352  1.00 123.04 ? 406  PRO B N   1 
ATOM   15442 C  CA  . PRO C 1 406  ? 28.549  51.492  44.272  1.00 119.74 ? 406  PRO B CA  1 
ATOM   15443 C  C   . PRO C 1 406  ? 29.708  51.875  43.385  1.00 122.51 ? 406  PRO B C   1 
ATOM   15444 O  O   . PRO C 1 406  ? 29.489  52.101  42.205  1.00 126.51 ? 406  PRO B O   1 
ATOM   15445 C  CB  . PRO C 1 406  ? 27.749  50.376  43.595  1.00 118.67 ? 406  PRO B CB  1 
ATOM   15446 C  CG  . PRO C 1 406  ? 26.299  50.759  43.787  1.00 122.24 ? 406  PRO B CG  1 
ATOM   15447 C  CD  . PRO C 1 406  ? 26.254  52.233  43.839  1.00 123.18 ? 406  PRO B CD  1 
ATOM   15448 N  N   . SER C 1 407  ? 30.910  51.975  43.928  1.00 127.79 ? 407  SER B N   1 
ATOM   15449 C  CA  . SER C 1 407  ? 32.063  52.083  43.062  1.00 130.93 ? 407  SER B CA  1 
ATOM   15450 C  C   . SER C 1 407  ? 32.708  50.727  43.004  1.00 130.36 ? 407  SER B C   1 
ATOM   15451 O  O   . SER C 1 407  ? 32.582  49.960  43.958  1.00 131.77 ? 407  SER B O   1 
ATOM   15452 C  CB  . SER C 1 407  ? 33.044  53.120  43.560  1.00 135.60 ? 407  SER B CB  1 
ATOM   15453 O  OG  . SER C 1 407  ? 32.417  54.381  43.595  1.00 139.89 ? 407  SER B OG  1 
ATOM   15454 N  N   . LYS C 1 408  ? 33.374  50.430  41.885  1.00 145.62 ? 408  LYS B N   1 
ATOM   15455 C  CA  . LYS C 1 408  ? 34.062  49.156  41.682  1.00 140.40 ? 408  LYS B CA  1 
ATOM   15456 C  C   . LYS C 1 408  ? 35.307  49.418  40.919  1.00 136.11 ? 408  LYS B C   1 
ATOM   15457 O  O   . LYS C 1 408  ? 35.229  49.908  39.814  1.00 136.68 ? 408  LYS B O   1 
ATOM   15458 C  CB  . LYS C 1 408  ? 33.233  48.198  40.832  1.00 138.75 ? 408  LYS B CB  1 
ATOM   15459 C  CG  . LYS C 1 408  ? 34.045  47.039  40.291  1.00 141.15 ? 408  LYS B CG  1 
ATOM   15460 C  CD  . LYS C 1 408  ? 33.221  46.159  39.358  1.00 143.99 ? 408  LYS B CD  1 
ATOM   15461 C  CE  . LYS C 1 408  ? 31.830  45.832  39.906  1.00 146.63 ? 408  LYS B CE  1 
ATOM   15462 N  NZ  . LYS C 1 408  ? 31.174  44.666  39.219  1.00 147.34 ? 408  LYS B NZ  1 
ATOM   15463 N  N   . SER C 1 409  ? 36.454  49.114  41.504  1.00 114.70 ? 409  SER B N   1 
ATOM   15464 C  CA  . SER C 1 409  ? 37.695  49.104  40.751  1.00 119.26 ? 409  SER B CA  1 
ATOM   15465 C  C   . SER C 1 409  ? 38.079  47.672  40.585  1.00 115.33 ? 409  SER B C   1 
ATOM   15466 O  O   . SER C 1 409  ? 37.290  46.778  40.893  1.00 108.73 ? 409  SER B O   1 
ATOM   15467 C  CB  . SER C 1 409  ? 38.828  49.855  41.461  1.00 128.70 ? 409  SER B CB  1 
ATOM   15468 O  OG  . SER C 1 409  ? 40.029  49.824  40.676  1.00 121.09 ? 409  SER B OG  1 
ATOM   15469 N  N   . VAL C 1 410  ? 39.294  47.473  40.088  1.00 106.08 ? 410  VAL B N   1 
ATOM   15470 C  CA  . VAL C 1 410  ? 39.914  46.169  40.082  1.00 109.58 ? 410  VAL B CA  1 
ATOM   15471 C  C   . VAL C 1 410  ? 41.394  46.328  40.420  1.00 119.21 ? 410  VAL B C   1 
ATOM   15472 O  O   . VAL C 1 410  ? 42.028  47.340  40.091  1.00 123.60 ? 410  VAL B O   1 
ATOM   15473 C  CB  . VAL C 1 410  ? 39.718  45.476  38.749  1.00 106.72 ? 410  VAL B CB  1 
ATOM   15474 C  CG1 . VAL C 1 410  ? 40.542  44.185  38.707  1.00 109.75 ? 410  VAL B CG1 1 
ATOM   15475 C  CG2 . VAL C 1 410  ? 38.219  45.203  38.540  1.00 100.74 ? 410  VAL B CG2 1 
ATOM   15476 N  N   . THR C 1 411  ? 41.912  45.323  41.110  1.00 99.10  ? 411  THR B N   1 
ATOM   15477 C  CA  . THR C 1 411  ? 43.195  45.401  41.761  1.00 102.65 ? 411  THR B CA  1 
ATOM   15478 C  C   . THR C 1 411  ? 44.331  45.407  40.775  1.00 103.32 ? 411  THR B C   1 
ATOM   15479 O  O   . THR C 1 411  ? 44.339  44.602  39.857  1.00 97.30  ? 411  THR B O   1 
ATOM   15480 C  CB  . THR C 1 411  ? 43.345  44.192  42.665  1.00 104.63 ? 411  THR B CB  1 
ATOM   15481 O  OG1 . THR C 1 411  ? 44.731  43.887  42.831  1.00 112.37 ? 411  THR B OG1 1 
ATOM   15482 C  CG2 . THR C 1 411  ? 42.688  43.053  42.026  1.00 98.37  ? 411  THR B CG2 1 
ATOM   15483 N  N   . ARG C 1 412  ? 45.313  46.276  41.008  1.00 127.81 ? 412  ARG B N   1 
ATOM   15484 C  CA  . ARG C 1 412  ? 46.488  46.385  40.142  1.00 140.04 ? 412  ARG B CA  1 
ATOM   15485 C  C   . ARG C 1 412  ? 47.236  45.048  40.010  1.00 141.93 ? 412  ARG B C   1 
ATOM   15486 O  O   . ARG C 1 412  ? 47.001  44.133  40.791  1.00 142.45 ? 412  ARG B O   1 
ATOM   15487 C  CB  . ARG C 1 412  ? 47.427  47.493  40.643  1.00 155.26 ? 412  ARG B CB  1 
ATOM   15488 C  CG  . ARG C 1 412  ? 48.501  47.915  39.645  1.00 168.54 ? 412  ARG B CG  1 
ATOM   15489 C  CD  . ARG C 1 412  ? 49.418  49.002  40.203  1.00 183.42 ? 412  ARG B CD  1 
ATOM   15490 N  NE  . ARG C 1 412  ? 49.157  50.316  39.623  1.00 190.69 ? 412  ARG B NE  1 
ATOM   15491 C  CZ  . ARG C 1 412  ? 49.721  51.447  40.039  1.00 200.93 ? 412  ARG B CZ  1 
ATOM   15492 N  NH1 . ARG C 1 412  ? 50.582  51.432  41.048  1.00 207.53 ? 412  ARG B NH1 1 
ATOM   15493 N  NH2 . ARG C 1 412  ? 49.419  52.597  39.447  1.00 202.95 ? 412  ARG B NH2 1 
ATOM   15494 N  N   . VAL C 1 413  ? 48.125  44.949  39.017  1.00 122.40 ? 413  VAL B N   1 
ATOM   15495 C  CA  . VAL C 1 413  ? 48.872  43.723  38.695  1.00 124.22 ? 413  VAL B CA  1 
ATOM   15496 C  C   . VAL C 1 413  ? 50.167  43.621  39.479  1.00 130.80 ? 413  VAL B C   1 
ATOM   15497 O  O   . VAL C 1 413  ? 50.572  42.542  39.918  1.00 131.36 ? 413  VAL B O   1 
ATOM   15498 C  CB  . VAL C 1 413  ? 49.316  43.708  37.216  1.00 126.35 ? 413  VAL B CB  1 
ATOM   15499 C  CG1 . VAL C 1 413  ? 49.982  42.377  36.875  1.00 126.60 ? 413  VAL B CG1 1 
ATOM   15500 C  CG2 . VAL C 1 413  ? 48.149  44.004  36.262  1.00 121.14 ? 413  VAL B CG2 1 
ATOM   15501 N  N   . ASP C 1 414  ? 50.833  44.762  39.591  1.00 188.70 ? 414  ASP B N   1 
ATOM   15502 C  CA  . ASP C 1 414  ? 52.075  44.896  40.335  1.00 195.99 ? 414  ASP B CA  1 
ATOM   15503 C  C   . ASP C 1 414  ? 51.811  45.242  41.798  1.00 194.37 ? 414  ASP B C   1 
ATOM   15504 O  O   . ASP C 1 414  ? 52.606  44.928  42.681  1.00 198.80 ? 414  ASP B O   1 
ATOM   15505 C  CB  . ASP C 1 414  ? 52.905  46.020  39.718  1.00 204.46 ? 414  ASP B CB  1 
ATOM   15506 C  CG  . ASP C 1 414  ? 52.146  47.337  39.658  1.00 207.19 ? 414  ASP B CG  1 
ATOM   15507 O  OD1 . ASP C 1 414  ? 51.253  47.458  38.792  1.00 203.82 ? 414  ASP B OD1 1 
ATOM   15508 O  OD2 . ASP C 1 414  ? 52.438  48.242  40.471  1.00 211.89 ? 414  ASP B OD2 1 
ATOM   15509 N  N   . ASP C 1 415  ? 50.684  45.902  42.036  1.00 170.79 ? 415  ASP B N   1 
ATOM   15510 C  CA  . ASP C 1 415  ? 50.390  46.543  43.310  1.00 171.62 ? 415  ASP B CA  1 
ATOM   15511 C  C   . ASP C 1 415  ? 49.597  45.649  44.242  1.00 160.92 ? 415  ASP B C   1 
ATOM   15512 O  O   . ASP C 1 415  ? 49.816  45.637  45.450  1.00 160.84 ? 415  ASP B O   1 
ATOM   15513 C  CB  . ASP C 1 415  ? 49.582  47.810  43.045  1.00 177.45 ? 415  ASP B CB  1 
ATOM   15514 C  CG  . ASP C 1 415  ? 49.455  48.685  44.261  1.00 187.14 ? 415  ASP B CG  1 
ATOM   15515 O  OD1 . ASP C 1 415  ? 49.833  48.216  45.353  1.00 193.39 ? 415  ASP B OD1 1 
ATOM   15516 O  OD2 . ASP C 1 415  ? 48.974  49.838  44.127  1.00 187.73 ? 415  ASP B OD2 1 
ATOM   15517 N  N   . GLY C 1 416  ? 48.665  44.904  43.665  1.00 126.11 ? 416  GLY B N   1 
ATOM   15518 C  CA  . GLY C 1 416  ? 47.728  44.122  44.438  1.00 122.18 ? 416  GLY B CA  1 
ATOM   15519 C  C   . GLY C 1 416  ? 46.700  45.067  45.009  1.00 123.87 ? 416  GLY B C   1 
ATOM   15520 O  O   . GLY C 1 416  ? 45.804  44.678  45.756  1.00 124.50 ? 416  GLY B O   1 
ATOM   15521 N  N   . VAL C 1 417  ? 46.836  46.331  44.649  1.00 136.88 ? 417  VAL B N   1 
ATOM   15522 C  CA  . VAL C 1 417  ? 45.975  47.350  45.202  1.00 136.08 ? 417  VAL B CA  1 
ATOM   15523 C  C   . VAL C 1 417  ? 44.868  47.799  44.277  1.00 129.73 ? 417  VAL B C   1 
ATOM   15524 O  O   . VAL C 1 417  ? 45.102  48.185  43.130  1.00 128.59 ? 417  VAL B O   1 
ATOM   15525 C  CB  . VAL C 1 417  ? 46.773  48.572  45.576  1.00 145.45 ? 417  VAL B CB  1 
ATOM   15526 C  CG1 . VAL C 1 417  ? 45.839  49.767  45.776  1.00 144.89 ? 417  VAL B CG1 1 
ATOM   15527 C  CG2 . VAL C 1 417  ? 47.593  48.282  46.809  1.00 152.31 ? 417  VAL B CG2 1 
ATOM   15528 N  N   . ALA C 1 418  ? 43.657  47.783  44.811  1.00 141.39 ? 418  ALA B N   1 
ATOM   15529 C  CA  . ALA C 1 418  ? 42.491  48.272  44.097  1.00 139.75 ? 418  ALA B CA  1 
ATOM   15530 C  C   . ALA C 1 418  ? 42.134  49.662  44.614  1.00 142.25 ? 418  ALA B C   1 
ATOM   15531 O  O   . ALA C 1 418  ? 41.292  49.806  45.494  1.00 141.91 ? 418  ALA B O   1 
ATOM   15532 C  CB  . ALA C 1 418  ? 41.331  47.321  44.297  1.00 135.71 ? 418  ALA B CB  1 
ATOM   15533 N  N   . SER C 1 419  ? 42.744  50.690  44.043  1.00 125.93 ? 419  SER B N   1 
ATOM   15534 C  CA  . SER C 1 419  ? 42.623  52.035  44.588  1.00 130.85 ? 419  SER B CA  1 
ATOM   15535 C  C   . SER C 1 419  ? 41.270  52.693  44.323  1.00 124.22 ? 419  SER B C   1 
ATOM   15536 O  O   . SER C 1 419  ? 40.715  52.522  43.253  1.00 121.18 ? 419  SER B O   1 
ATOM   15537 C  CB  . SER C 1 419  ? 43.750  52.868  44.027  1.00 138.87 ? 419  SER B CB  1 
ATOM   15538 O  OG  . SER C 1 419  ? 44.923  52.094  44.069  1.00 142.57 ? 419  SER B OG  1 
ATOM   15539 N  N   . PHE C 1 420  ? 40.748  53.444  45.292  1.00 123.91 ? 420  PHE B N   1 
ATOM   15540 C  CA  . PHE C 1 420  ? 39.488  54.165  45.122  1.00 127.10 ? 420  PHE B CA  1 
ATOM   15541 C  C   . PHE C 1 420  ? 39.637  55.611  45.535  1.00 136.15 ? 420  PHE B C   1 
ATOM   15542 O  O   . PHE C 1 420  ? 40.675  55.996  46.046  1.00 147.24 ? 420  PHE B O   1 
ATOM   15543 C  CB  . PHE C 1 420  ? 38.450  53.638  46.068  1.00 123.94 ? 420  PHE B CB  1 
ATOM   15544 C  CG  . PHE C 1 420  ? 37.977  52.290  45.765  1.00 114.21 ? 420  PHE B CG  1 
ATOM   15545 C  CD1 . PHE C 1 420  ? 36.740  52.113  45.185  1.00 109.40 ? 420  PHE B CD1 1 
ATOM   15546 C  CD2 . PHE C 1 420  ? 38.730  51.188  46.112  1.00 114.84 ? 420  PHE B CD2 1 
ATOM   15547 C  CE1 . PHE C 1 420  ? 36.269  50.857  44.933  1.00 108.41 ? 420  PHE B CE1 1 
ATOM   15548 C  CE2 . PHE C 1 420  ? 38.270  49.920  45.858  1.00 116.39 ? 420  PHE B CE2 1 
ATOM   15549 C  CZ  . PHE C 1 420  ? 37.041  49.748  45.267  1.00 110.95 ? 420  PHE B CZ  1 
ATOM   15550 N  N   . VAL C 1 421  ? 38.577  56.395  45.333  1.00 165.82 ? 421  VAL B N   1 
ATOM   15551 C  CA  . VAL C 1 421  ? 38.401  57.690  45.996  1.00 164.46 ? 421  VAL B CA  1 
ATOM   15552 C  C   . VAL C 1 421  ? 36.942  58.107  45.945  1.00 161.26 ? 421  VAL B C   1 
ATOM   15553 O  O   . VAL C 1 421  ? 36.327  58.096  44.880  1.00 159.03 ? 421  VAL B O   1 
ATOM   15554 C  CB  . VAL C 1 421  ? 39.265  58.833  45.384  1.00 164.43 ? 421  VAL B CB  1 
ATOM   15555 C  CG1 . VAL C 1 421  ? 38.460  60.127  45.269  1.00 163.96 ? 421  VAL B CG1 1 
ATOM   15556 C  CG2 . VAL C 1 421  ? 40.508  59.071  46.216  1.00 168.17 ? 421  VAL B CG2 1 
ATOM   15557 N  N   . LEU C 1 422  ? 36.381  58.435  47.103  1.00 118.28 ? 422  LEU B N   1 
ATOM   15558 C  CA  . LEU C 1 422  ? 35.087  59.105  47.152  1.00 116.85 ? 422  LEU B CA  1 
ATOM   15559 C  C   . LEU C 1 422  ? 35.282  60.530  47.689  1.00 126.25 ? 422  LEU B C   1 
ATOM   15560 O  O   . LEU C 1 422  ? 35.937  60.743  48.717  1.00 130.74 ? 422  LEU B O   1 
ATOM   15561 C  CB  . LEU C 1 422  ? 34.014  58.306  47.938  1.00 113.24 ? 422  LEU B CB  1 
ATOM   15562 C  CG  . LEU C 1 422  ? 34.368  57.078  48.796  1.00 105.84 ? 422  LEU B CG  1 
ATOM   15563 C  CD1 . LEU C 1 422  ? 35.374  57.485  49.846  1.00 111.91 ? 422  LEU B CD1 1 
ATOM   15564 C  CD2 . LEU C 1 422  ? 33.159  56.337  49.428  1.00 102.54 ? 422  LEU B CD2 1 
ATOM   15565 N  N   . ASN C 1 423  ? 34.752  61.506  46.953  1.00 177.43 ? 423  ASN B N   1 
ATOM   15566 C  CA  . ASN C 1 423  ? 34.883  62.915  47.306  1.00 182.33 ? 423  ASN B CA  1 
ATOM   15567 C  C   . ASN C 1 423  ? 33.743  63.238  48.243  1.00 181.36 ? 423  ASN B C   1 
ATOM   15568 O  O   . ASN C 1 423  ? 32.593  62.972  47.898  1.00 175.14 ? 423  ASN B O   1 
ATOM   15569 C  CB  . ASN C 1 423  ? 34.792  63.765  46.040  1.00 180.85 ? 423  ASN B CB  1 
ATOM   15570 C  CG  . ASN C 1 423  ? 35.131  62.971  44.782  1.00 177.06 ? 423  ASN B CG  1 
ATOM   15571 O  OD1 . ASN C 1 423  ? 36.257  63.014  44.286  1.00 181.19 ? 423  ASN B OD1 1 
ATOM   15572 N  ND2 . ASN C 1 423  ? 34.155  62.230  44.271  1.00 169.87 ? 423  ASN B ND2 1 
ATOM   15573 N  N   . LEU C 1 424  ? 34.028  63.792  49.421  1.00 125.46 ? 424  LEU B N   1 
ATOM   15574 C  CA  . LEU C 1 424  ? 32.989  63.835  50.467  1.00 126.85 ? 424  LEU B CA  1 
ATOM   15575 C  C   . LEU C 1 424  ? 32.432  65.185  50.946  1.00 132.04 ? 424  LEU B C   1 
ATOM   15576 O  O   . LEU C 1 424  ? 33.189  66.076  51.338  1.00 136.91 ? 424  LEU B O   1 
ATOM   15577 C  CB  . LEU C 1 424  ? 33.408  62.970  51.655  1.00 127.80 ? 424  LEU B CB  1 
ATOM   15578 C  CG  . LEU C 1 424  ? 33.263  61.479  51.298  1.00 122.94 ? 424  LEU B CG  1 
ATOM   15579 C  CD1 . LEU C 1 424  ? 33.727  60.504  52.400  1.00 126.12 ? 424  LEU B CD1 1 
ATOM   15580 C  CD2 . LEU C 1 424  ? 31.822  61.176  50.883  1.00 117.53 ? 424  LEU B CD2 1 
ATOM   15581 N  N   . PRO C 1 425  ? 31.090  65.306  50.948  1.00 171.07 ? 425  PRO B N   1 
ATOM   15582 C  CA  . PRO C 1 425  ? 30.358  66.535  51.272  1.00 177.14 ? 425  PRO B CA  1 
ATOM   15583 C  C   . PRO C 1 425  ? 30.739  67.101  52.637  1.00 188.41 ? 425  PRO B C   1 
ATOM   15584 O  O   . PRO C 1 425  ? 29.999  66.862  53.587  1.00 193.18 ? 425  PRO B O   1 
ATOM   15585 C  CB  . PRO C 1 425  ? 28.895  66.073  51.300  1.00 173.65 ? 425  PRO B CB  1 
ATOM   15586 C  CG  . PRO C 1 425  ? 28.852  64.863  50.446  1.00 166.61 ? 425  PRO B CG  1 
ATOM   15587 C  CD  . PRO C 1 425  ? 30.179  64.193  50.626  1.00 163.39 ? 425  PRO B CD  1 
ATOM   15588 N  N   . SER C 1 426  ? 31.844  67.848  52.711  1.00 187.37 ? 426  SER B N   1 
ATOM   15589 C  CA  . SER C 1 426  ? 32.414  68.388  53.962  1.00 197.15 ? 426  SER B CA  1 
ATOM   15590 C  C   . SER C 1 426  ? 31.654  68.147  55.288  1.00 205.83 ? 426  SER B C   1 
ATOM   15591 O  O   . SER C 1 426  ? 32.268  67.793  56.305  1.00 206.97 ? 426  SER B O   1 
ATOM   15592 C  CB  . SER C 1 426  ? 32.759  69.878  53.796  1.00 205.21 ? 426  SER B CB  1 
ATOM   15593 O  OG  . SER C 1 426  ? 31.673  70.616  53.260  1.00 203.80 ? 426  SER B OG  1 
ATOM   15594 N  N   . GLY C 1 427  ? 30.336  68.346  55.274  1.00 167.85 ? 427  GLY B N   1 
ATOM   15595 C  CA  . GLY C 1 427  ? 29.494  68.077  56.428  1.00 169.51 ? 427  GLY B CA  1 
ATOM   15596 C  C   . GLY C 1 427  ? 29.409  66.612  56.822  1.00 164.15 ? 427  GLY B C   1 
ATOM   15597 O  O   . GLY C 1 427  ? 28.599  66.210  57.663  1.00 163.46 ? 427  GLY B O   1 
ATOM   15598 N  N   . VAL C 1 428  ? 30.245  65.794  56.210  1.00 154.44 ? 428  VAL B N   1 
ATOM   15599 C  CA  . VAL C 1 428  ? 30.245  64.389  56.556  1.00 148.02 ? 428  VAL B CA  1 
ATOM   15600 C  C   . VAL C 1 428  ? 30.878  64.234  57.934  1.00 150.44 ? 428  VAL B C   1 
ATOM   15601 O  O   . VAL C 1 428  ? 31.348  65.219  58.503  1.00 155.85 ? 428  VAL B O   1 
ATOM   15602 C  CB  . VAL C 1 428  ? 30.993  63.562  55.522  1.00 143.73 ? 428  VAL B CB  1 
ATOM   15603 C  CG1 . VAL C 1 428  ? 32.502  63.740  55.707  1.00 148.56 ? 428  VAL B CG1 1 
ATOM   15604 C  CG2 . VAL C 1 428  ? 30.550  62.101  55.590  1.00 138.85 ? 428  VAL B CG2 1 
ATOM   15605 N  N   . THR C 1 429  ? 30.939  62.992  58.427  1.00 117.49 ? 429  THR B N   1 
ATOM   15606 C  CA  . THR C 1 429  ? 30.942  62.685  59.860  1.00 119.70 ? 429  THR B CA  1 
ATOM   15607 C  C   . THR C 1 429  ? 31.704  61.412  60.189  1.00 119.05 ? 429  THR B C   1 
ATOM   15608 O  O   . THR C 1 429  ? 32.845  61.397  60.668  1.00 120.63 ? 429  THR B O   1 
ATOM   15609 C  CB  . THR C 1 429  ? 29.471  62.435  60.282  1.00 120.65 ? 429  THR B CB  1 
ATOM   15610 O  OG1 . THR C 1 429  ? 29.024  61.152  59.801  1.00 116.83 ? 429  THR B OG1 1 
ATOM   15611 C  CG2 . THR C 1 429  ? 28.567  63.535  59.707  1.00 119.14 ? 429  THR B CG2 1 
ATOM   15612 N  N   . VAL C 1 430  ? 31.002  60.334  59.928  1.00 191.94 ? 430  VAL B N   1 
ATOM   15613 C  CA  . VAL C 1 430  ? 31.540  59.022  60.000  1.00 186.52 ? 430  VAL B CA  1 
ATOM   15614 C  C   . VAL C 1 430  ? 31.200  58.432  58.679  1.00 182.87 ? 430  VAL B C   1 
ATOM   15615 O  O   . VAL C 1 430  ? 30.080  58.582  58.194  1.00 179.84 ? 430  VAL B O   1 
ATOM   15616 C  CB  . VAL C 1 430  ? 30.793  58.222  61.000  1.00 181.33 ? 430  VAL B CB  1 
ATOM   15617 C  CG1 . VAL C 1 430  ? 31.299  56.785  61.024  1.00 177.26 ? 430  VAL B CG1 1 
ATOM   15618 C  CG2 . VAL C 1 430  ? 30.968  58.851  62.302  1.00 187.14 ? 430  VAL B CG2 1 
ATOM   15619 N  N   . LEU C 1 431  ? 32.162  57.748  58.095  1.00 158.67 ? 431  LEU B N   1 
ATOM   15620 C  CA  . LEU C 1 431  ? 31.927  57.116  56.844  1.00 148.48 ? 431  LEU B CA  1 
ATOM   15621 C  C   . LEU C 1 431  ? 32.045  55.648  57.146  1.00 146.71 ? 431  LEU B C   1 
ATOM   15622 O  O   . LEU C 1 431  ? 33.099  55.177  57.564  1.00 139.15 ? 431  LEU B O   1 
ATOM   15623 C  CB  . LEU C 1 431  ? 33.002  57.566  55.881  1.00 143.50 ? 431  LEU B CB  1 
ATOM   15624 C  CG  . LEU C 1 431  ? 32.711  57.267  54.428  1.00 136.15 ? 431  LEU B CG  1 
ATOM   15625 C  CD1 . LEU C 1 431  ? 34.003  56.965  53.649  1.00 133.71 ? 431  LEU B CD1 1 
ATOM   15626 C  CD2 . LEU C 1 431  ? 31.744  56.098  54.370  1.00 131.06 ? 431  LEU B CD2 1 
ATOM   15627 N  N   . GLU C 1 432  ? 30.951  54.923  56.984  1.00 177.75 ? 432  GLU B N   1 
ATOM   15628 C  CA  . GLU C 1 432  ? 31.032  53.475  57.066  1.00 176.01 ? 432  GLU B CA  1 
ATOM   15629 C  C   . GLU C 1 432  ? 31.009  52.926  55.639  1.00 172.42 ? 432  GLU B C   1 
ATOM   15630 O  O   . GLU C 1 432  ? 30.236  53.409  54.811  1.00 173.10 ? 432  GLU B O   1 
ATOM   15631 C  CB  . GLU C 1 432  ? 29.859  52.903  57.860  1.00 175.46 ? 432  GLU B CB  1 
ATOM   15632 C  CG  . GLU C 1 432  ? 29.545  53.622  59.149  1.00 184.86 ? 432  GLU B CG  1 
ATOM   15633 C  CD  . GLU C 1 432  ? 30.078  52.899  60.366  1.00 191.22 ? 432  GLU B CD  1 
ATOM   15634 O  OE1 . GLU C 1 432  ? 30.853  51.927  60.206  1.00 186.57 ? 432  GLU B OE1 1 
ATOM   15635 O  OE2 . GLU C 1 432  ? 29.715  53.313  61.484  1.00 198.42 ? 432  GLU B OE2 1 
ATOM   15636 N  N   . PHE C 1 433  ? 31.838  51.922  55.346  1.00 124.48 ? 433  PHE B N   1 
ATOM   15637 C  CA  . PHE C 1 433  ? 31.864  51.337  54.009  1.00 117.76 ? 433  PHE B CA  1 
ATOM   15638 C  C   . PHE C 1 433  ? 32.240  49.838  53.951  1.00 120.35 ? 433  PHE B C   1 
ATOM   15639 O  O   . PHE C 1 433  ? 33.034  49.353  54.760  1.00 125.07 ? 433  PHE B O   1 
ATOM   15640 C  CB  . PHE C 1 433  ? 32.719  52.207  53.063  1.00 115.26 ? 433  PHE B CB  1 
ATOM   15641 C  CG  . PHE C 1 433  ? 34.162  52.445  53.517  1.00 119.65 ? 433  PHE B CG  1 
ATOM   15642 C  CD1 . PHE C 1 433  ? 34.728  53.721  53.451  1.00 122.52 ? 433  PHE B CD1 1 
ATOM   15643 C  CD2 . PHE C 1 433  ? 34.967  51.397  53.943  1.00 122.68 ? 433  PHE B CD2 1 
ATOM   15644 C  CE1 . PHE C 1 433  ? 36.050  53.946  53.819  1.00 126.09 ? 433  PHE B CE1 1 
ATOM   15645 C  CE2 . PHE C 1 433  ? 36.287  51.622  54.315  1.00 127.36 ? 433  PHE B CE2 1 
ATOM   15646 C  CZ  . PHE C 1 433  ? 36.824  52.895  54.249  1.00 132.57 ? 433  PHE B CZ  1 
ATOM   15647 N  N   . ASN C 1 434  ? 31.642  49.115  53.003  1.00 140.30 ? 434  ASN B N   1 
ATOM   15648 C  CA  . ASN C 1 434  ? 31.987  47.710  52.755  1.00 136.57 ? 434  ASN B CA  1 
ATOM   15649 C  C   . ASN C 1 434  ? 32.751  47.427  51.432  1.00 137.73 ? 434  ASN B C   1 
ATOM   15650 O  O   . ASN C 1 434  ? 32.314  47.774  50.328  1.00 138.70 ? 434  ASN B O   1 
ATOM   15651 C  CB  . ASN C 1 434  ? 30.750  46.820  52.872  1.00 133.40 ? 434  ASN B CB  1 
ATOM   15652 C  CG  . ASN C 1 434  ? 29.966  47.095  54.136  1.00 133.00 ? 434  ASN B CG  1 
ATOM   15653 O  OD1 . ASN C 1 434  ? 30.122  46.399  55.137  1.00 132.08 ? 434  ASN B OD1 1 
ATOM   15654 N  ND2 . ASN C 1 434  ? 29.141  48.134  54.107  1.00 134.75 ? 434  ASN B ND2 1 
ATOM   15655 N  N   . VAL C 1 435  ? 33.899  46.781  51.562  1.00 88.60  ? 435  VAL B N   1 
ATOM   15656 C  CA  . VAL C 1 435  ? 34.657  46.310  50.421  1.00 86.72  ? 435  VAL B CA  1 
ATOM   15657 C  C   . VAL C 1 435  ? 34.398  44.837  50.255  1.00 105.33 ? 435  VAL B C   1 
ATOM   15658 O  O   . VAL C 1 435  ? 34.061  44.161  51.205  1.00 105.96 ? 435  VAL B O   1 
ATOM   15659 C  CB  . VAL C 1 435  ? 36.109  46.493  50.690  1.00 92.36  ? 435  VAL B CB  1 
ATOM   15660 C  CG1 . VAL C 1 435  ? 36.932  45.544  49.892  1.00 91.05  ? 435  VAL B CG1 1 
ATOM   15661 C  CG2 . VAL C 1 435  ? 36.453  47.921  50.384  1.00 94.55  ? 435  VAL B CG2 1 
ATOM   15662 N  N   . LYS C 1 436  ? 34.555  44.330  49.050  1.00 152.57 ? 436  LYS B N   1 
ATOM   15663 C  CA  . LYS C 1 436  ? 34.342  42.919  48.794  1.00 148.83 ? 436  LYS B CA  1 
ATOM   15664 C  C   . LYS C 1 436  ? 34.787  42.604  47.366  1.00 150.54 ? 436  LYS B C   1 
ATOM   15665 O  O   . LYS C 1 436  ? 34.612  43.423  46.464  1.00 149.39 ? 436  LYS B O   1 
ATOM   15666 C  CB  . LYS C 1 436  ? 32.882  42.533  49.033  1.00 144.60 ? 436  LYS B CB  1 
ATOM   15667 C  CG  . LYS C 1 436  ? 31.879  42.951  47.979  1.00 139.16 ? 436  LYS B CG  1 
ATOM   15668 C  CD  . LYS C 1 436  ? 31.436  41.727  47.184  1.00 155.99 ? 436  LYS B CD  1 
ATOM   15669 C  CE  . LYS C 1 436  ? 30.058  41.918  46.595  1.00 161.05 ? 436  LYS B CE  1 
ATOM   15670 N  NZ  . LYS C 1 436  ? 29.062  42.051  47.673  1.00 161.70 ? 436  LYS B NZ  1 
ATOM   15671 N  N   . THR C 1 437  ? 35.392  41.441  47.153  1.00 113.80 ? 437  THR B N   1 
ATOM   15672 C  CA  . THR C 1 437  ? 35.741  41.047  45.802  1.00 118.78 ? 437  THR B CA  1 
ATOM   15673 C  C   . THR C 1 437  ? 34.469  40.602  45.119  1.00 112.68 ? 437  THR B C   1 
ATOM   15674 O  O   . THR C 1 437  ? 33.549  40.079  45.769  1.00 106.97 ? 437  THR B O   1 
ATOM   15675 C  CB  . THR C 1 437  ? 36.711  39.892  45.796  1.00 112.80 ? 437  THR B CB  1 
ATOM   15676 O  OG1 . THR C 1 437  ? 36.214  38.875  46.672  1.00 113.51 ? 437  THR B OG1 1 
ATOM   15677 C  CG2 . THR C 1 437  ? 38.071  40.368  46.271  1.00 117.24 ? 437  THR B CG2 1 
ATOM   15678 N  N   . ASP C 1 438  ? 34.404  40.825  43.814  1.00 131.48 ? 438  ASP B N   1 
ATOM   15679 C  CA  . ASP C 1 438  ? 33.289  40.327  43.047  1.00 138.50 ? 438  ASP B CA  1 
ATOM   15680 C  C   . ASP C 1 438  ? 33.849  39.411  42.012  1.00 137.62 ? 438  ASP B C   1 
ATOM   15681 O  O   . ASP C 1 438  ? 33.384  39.363  40.875  1.00 135.93 ? 438  ASP B O   1 
ATOM   15682 C  CB  . ASP C 1 438  ? 32.490  41.453  42.421  1.00 145.69 ? 438  ASP B CB  1 
ATOM   15683 C  CG  . ASP C 1 438  ? 30.994  41.212  42.522  1.00 153.89 ? 438  ASP B CG  1 
ATOM   15684 O  OD1 . ASP C 1 438  ? 30.600  40.022  42.594  1.00 155.83 ? 438  ASP B OD1 1 
ATOM   15685 O  OD2 . ASP C 1 438  ? 30.221  42.202  42.538  1.00 157.31 ? 438  ASP B OD2 1 
ATOM   15686 N  N   . ALA C 1 439  ? 34.880  38.690  42.432  1.00 166.00 ? 439  ALA B N   1 
ATOM   15687 C  CA  . ALA C 1 439  ? 35.406  37.625  41.626  1.00 169.31 ? 439  ALA B CA  1 
ATOM   15688 C  C   . ALA C 1 439  ? 34.182  37.108  40.933  1.00 172.61 ? 439  ALA B C   1 
ATOM   15689 O  O   . ALA C 1 439  ? 33.086  37.083  41.487  1.00 175.68 ? 439  ALA B O   1 
ATOM   15690 C  CB  . ALA C 1 439  ? 36.019  36.563  42.477  1.00 171.53 ? 439  ALA B CB  1 
ATOM   15691 N  N   . PRO C 1 440  ? 34.348  36.730  39.691  1.00 136.63 ? 440  PRO B N   1 
ATOM   15692 C  CA  . PRO C 1 440  ? 33.156  36.519  38.889  1.00 133.85 ? 440  PRO B CA  1 
ATOM   15693 C  C   . PRO C 1 440  ? 32.774  35.073  38.997  1.00 131.64 ? 440  PRO B C   1 
ATOM   15694 O  O   . PRO C 1 440  ? 31.612  34.733  38.778  1.00 132.79 ? 440  PRO B O   1 
ATOM   15695 C  CB  . PRO C 1 440  ? 33.637  36.835  37.477  1.00 133.46 ? 440  PRO B CB  1 
ATOM   15696 C  CG  . PRO C 1 440  ? 35.204  36.980  37.581  1.00 139.09 ? 440  PRO B CG  1 
ATOM   15697 C  CD  . PRO C 1 440  ? 35.593  36.538  38.943  1.00 138.21 ? 440  PRO B CD  1 
ATOM   15698 N  N   . ASP C 1 441  ? 33.764  34.252  39.342  1.00 145.32 ? 441  ASP B N   1 
ATOM   15699 C  CA  . ASP C 1 441  ? 33.615  32.808  39.473  1.00 148.58 ? 441  ASP B CA  1 
ATOM   15700 C  C   . ASP C 1 441  ? 33.227  32.302  40.900  1.00 145.70 ? 441  ASP B C   1 
ATOM   15701 O  O   . ASP C 1 441  ? 32.802  31.146  41.086  1.00 146.25 ? 441  ASP B O   1 
ATOM   15702 C  CB  . ASP C 1 441  ? 34.882  32.104  38.970  1.00 158.24 ? 441  ASP B CB  1 
ATOM   15703 C  CG  . ASP C 1 441  ? 36.143  32.918  39.207  1.00 164.82 ? 441  ASP B CG  1 
ATOM   15704 O  OD1 . ASP C 1 441  ? 37.233  32.318  39.295  1.00 170.53 ? 441  ASP B OD1 1 
ATOM   15705 O  OD2 . ASP C 1 441  ? 36.057  34.152  39.303  1.00 162.86 ? 441  ASP B OD2 1 
ATOM   15706 N  N   . LEU C 1 442  ? 33.358  33.155  41.914  1.00 114.71 ? 442  LEU B N   1 
ATOM   15707 C  CA  . LEU C 1 442  ? 33.132  32.710  43.286  1.00 111.67 ? 442  LEU B CA  1 
ATOM   15708 C  C   . LEU C 1 442  ? 31.686  32.765  43.713  1.00 114.68 ? 442  LEU B C   1 
ATOM   15709 O  O   . LEU C 1 442  ? 30.989  33.730  43.480  1.00 115.10 ? 442  LEU B O   1 
ATOM   15710 C  CB  . LEU C 1 442  ? 33.973  33.552  44.218  1.00 104.59 ? 442  LEU B CB  1 
ATOM   15711 C  CG  . LEU C 1 442  ? 35.447  33.385  43.854  1.00 99.18  ? 442  LEU B CG  1 
ATOM   15712 C  CD1 . LEU C 1 442  ? 36.410  34.199  44.749  1.00 97.57  ? 442  LEU B CD1 1 
ATOM   15713 C  CD2 . LEU C 1 442  ? 35.816  31.894  43.828  1.00 97.49  ? 442  LEU B CD2 1 
ATOM   15714 N  N   . PRO C 1 443  ? 31.228  31.724  44.373  1.00 256.32 ? 443  PRO B N   1 
ATOM   15715 C  CA  . PRO C 1 443  ? 29.909  31.925  44.953  1.00 259.86 ? 443  PRO B CA  1 
ATOM   15716 C  C   . PRO C 1 443  ? 29.912  33.298  45.591  1.00 267.04 ? 443  PRO B C   1 
ATOM   15717 O  O   . PRO C 1 443  ? 30.936  33.704  46.149  1.00 268.19 ? 443  PRO B O   1 
ATOM   15718 C  CB  . PRO C 1 443  ? 29.855  30.870  46.050  1.00 256.85 ? 443  PRO B CB  1 
ATOM   15719 C  CG  . PRO C 1 443  ? 30.792  29.812  45.605  1.00 255.93 ? 443  PRO B CG  1 
ATOM   15720 C  CD  . PRO C 1 443  ? 31.857  30.466  44.780  1.00 254.37 ? 443  PRO B CD  1 
ATOM   15721 N  N   . GLU C 1 444  ? 28.809  34.021  45.472  1.00 161.91 ? 444  GLU B N   1 
ATOM   15722 C  CA  . GLU C 1 444  ? 28.633  35.197  46.281  1.00 165.03 ? 444  GLU B CA  1 
ATOM   15723 C  C   . GLU C 1 444  ? 29.120  34.817  47.670  1.00 157.52 ? 444  GLU B C   1 
ATOM   15724 O  O   . GLU C 1 444  ? 30.183  35.268  48.105  1.00 151.26 ? 444  GLU B O   1 
ATOM   15725 C  CB  . GLU C 1 444  ? 27.163  35.579  46.317  1.00 179.79 ? 444  GLU B CB  1 
ATOM   15726 C  CG  . GLU C 1 444  ? 26.944  37.067  46.468  1.00 192.55 ? 444  GLU B CG  1 
ATOM   15727 C  CD  . GLU C 1 444  ? 27.498  37.599  47.773  1.00 202.45 ? 444  GLU B CD  1 
ATOM   15728 O  OE1 . GLU C 1 444  ? 27.536  36.829  48.763  1.00 206.34 ? 444  GLU B OE1 1 
ATOM   15729 O  OE2 . GLU C 1 444  ? 27.882  38.792  47.811  1.00 204.39 ? 444  GLU B OE2 1 
ATOM   15730 N  N   . GLU C 1 445  ? 28.365  33.955  48.346  1.00 153.83 ? 445  GLU B N   1 
ATOM   15731 C  CA  . GLU C 1 445  ? 28.761  33.469  49.662  1.00 155.27 ? 445  GLU B CA  1 
ATOM   15732 C  C   . GLU C 1 445  ? 30.230  33.686  49.901  1.00 147.89 ? 445  GLU B C   1 
ATOM   15733 O  O   . GLU C 1 445  ? 30.637  34.452  50.749  1.00 147.80 ? 445  GLU B O   1 
ATOM   15734 C  CB  . GLU C 1 445  ? 28.537  31.970  49.762  1.00 162.68 ? 445  GLU B CB  1 
ATOM   15735 C  CG  . GLU C 1 445  ? 27.130  31.526  49.968  1.00 172.41 ? 445  GLU B CG  1 
ATOM   15736 C  CD  . GLU C 1 445  ? 27.074  30.030  50.174  1.00 181.44 ? 445  GLU B CD  1 
ATOM   15737 O  OE1 . GLU C 1 445  ? 28.003  29.336  49.702  1.00 182.73 ? 445  GLU B OE1 1 
ATOM   15738 O  OE2 . GLU C 1 445  ? 26.117  29.544  50.809  1.00 186.31 ? 445  GLU B OE2 1 
ATOM   15739 N  N   . ASN C 1 446  ? 31.025  33.015  49.102  1.00 101.47 ? 446  ASN B N   1 
ATOM   15740 C  CA  . ASN C 1 446  ? 32.411  32.831  49.414  1.00 100.46 ? 446  ASN B CA  1 
ATOM   15741 C  C   . ASN C 1 446  ? 33.309  33.934  48.950  1.00 100.62 ? 446  ASN B C   1 
ATOM   15742 O  O   . ASN C 1 446  ? 34.463  33.703  48.691  1.00 99.40  ? 446  ASN B O   1 
ATOM   15743 C  CB  . ASN C 1 446  ? 32.830  31.516  48.800  1.00 101.25 ? 446  ASN B CB  1 
ATOM   15744 C  CG  . ASN C 1 446  ? 31.935  30.368  49.258  1.00 107.98 ? 446  ASN B CG  1 
ATOM   15745 O  OD1 . ASN C 1 446  ? 31.072  29.870  48.518  1.00 109.14 ? 446  ASN B OD1 1 
ATOM   15746 N  ND2 . ASN C 1 446  ? 32.119  29.965  50.514  1.00 112.53 ? 446  ASN B ND2 1 
ATOM   15747 N  N   . GLN C 1 447  ? 32.776  35.133  48.841  1.00 129.87 ? 447  GLN B N   1 
ATOM   15748 C  CA  . GLN C 1 447  ? 33.558  36.256  48.382  1.00 133.01 ? 447  GLN B CA  1 
ATOM   15749 C  C   . GLN C 1 447  ? 34.192  36.938  49.565  1.00 133.61 ? 447  GLN B C   1 
ATOM   15750 O  O   . GLN C 1 447  ? 33.491  37.324  50.501  1.00 132.44 ? 447  GLN B O   1 
ATOM   15751 C  CB  . GLN C 1 447  ? 32.647  37.263  47.700  1.00 134.21 ? 447  GLN B CB  1 
ATOM   15752 C  CG  . GLN C 1 447  ? 32.186  36.872  46.318  1.00 137.33 ? 447  GLN B CG  1 
ATOM   15753 C  CD  . GLN C 1 447  ? 33.224  37.207  45.280  1.00 137.97 ? 447  GLN B CD  1 
ATOM   15754 O  OE1 . GLN C 1 447  ? 34.380  37.469  45.611  1.00 137.48 ? 447  GLN B OE1 1 
ATOM   15755 N  NE2 . GLN C 1 447  ? 32.821  37.208  44.019  1.00 139.54 ? 447  GLN B NE2 1 
ATOM   15756 N  N   . ALA C 1 448  ? 35.506  37.131  49.514  1.00 107.38 ? 448  ALA B N   1 
ATOM   15757 C  CA  . ALA C 1 448  ? 36.213  37.827  50.596  1.00 110.06 ? 448  ALA B CA  1 
ATOM   15758 C  C   . ALA C 1 448  ? 35.752  39.270  50.761  1.00 120.78 ? 448  ALA B C   1 
ATOM   15759 O  O   . ALA C 1 448  ? 35.618  39.981  49.773  1.00 116.60 ? 448  ALA B O   1 
ATOM   15760 C  CB  . ALA C 1 448  ? 37.713  37.788  50.387  1.00 113.02 ? 448  ALA B CB  1 
ATOM   15761 N  N   . ARG C 1 449  ? 35.559  39.702  52.014  1.00 120.47 ? 449  ARG B N   1 
ATOM   15762 C  CA  . ARG C 1 449  ? 35.027  41.035  52.327  1.00 122.23 ? 449  ARG B CA  1 
ATOM   15763 C  C   . ARG C 1 449  ? 35.441  41.626  53.692  1.00 128.19 ? 449  ARG B C   1 
ATOM   15764 O  O   . ARG C 1 449  ? 35.940  40.924  54.572  1.00 130.51 ? 449  ARG B O   1 
ATOM   15765 C  CB  . ARG C 1 449  ? 33.513  41.017  52.228  1.00 120.70 ? 449  ARG B CB  1 
ATOM   15766 C  CG  . ARG C 1 449  ? 32.856  40.076  53.162  1.00 124.39 ? 449  ARG B CG  1 
ATOM   15767 C  CD  . ARG C 1 449  ? 31.425  40.144  52.895  1.00 128.87 ? 449  ARG B CD  1 
ATOM   15768 N  NE  . ARG C 1 449  ? 30.993  38.972  52.183  1.00 130.39 ? 449  ARG B NE  1 
ATOM   15769 C  CZ  . ARG C 1 449  ? 29.923  38.952  51.414  1.00 132.50 ? 449  ARG B CZ  1 
ATOM   15770 N  NH1 . ARG C 1 449  ? 29.195  40.057  51.239  1.00 134.01 ? 449  ARG B NH1 1 
ATOM   15771 N  NH2 . ARG C 1 449  ? 29.595  37.827  50.817  1.00 132.23 ? 449  ARG B NH2 1 
ATOM   15772 N  N   . GLU C 1 450  ? 35.210  42.927  53.854  1.00 125.11 ? 450  GLU B N   1 
ATOM   15773 C  CA  . GLU C 1 450  ? 35.574  43.653  55.062  1.00 130.73 ? 450  GLU B CA  1 
ATOM   15774 C  C   . GLU C 1 450  ? 34.614  44.784  55.240  1.00 129.24 ? 450  GLU B C   1 
ATOM   15775 O  O   . GLU C 1 450  ? 33.638  44.917  54.506  1.00 125.92 ? 450  GLU B O   1 
ATOM   15776 C  CB  . GLU C 1 450  ? 36.950  44.271  54.912  1.00 130.44 ? 450  GLU B CB  1 
ATOM   15777 C  CG  . GLU C 1 450  ? 38.054  43.294  54.978  1.00 128.87 ? 450  GLU B CG  1 
ATOM   15778 C  CD  . GLU C 1 450  ? 38.274  42.860  56.383  1.00 138.67 ? 450  GLU B CD  1 
ATOM   15779 O  OE1 . GLU C 1 450  ? 38.014  43.713  57.265  1.00 144.74 ? 450  GLU B OE1 1 
ATOM   15780 O  OE2 . GLU C 1 450  ? 38.679  41.690  56.603  1.00 139.63 ? 450  GLU B OE2 1 
ATOM   15781 N  N   . GLY C 1 451  ? 34.906  45.623  56.210  1.00 121.78 ? 451  GLY B N   1 
ATOM   15782 C  CA  . GLY C 1 451  ? 34.110  46.807  56.399  1.00 119.89 ? 451  GLY B CA  1 
ATOM   15783 C  C   . GLY C 1 451  ? 34.968  47.643  57.287  1.00 123.57 ? 451  GLY B C   1 
ATOM   15784 O  O   . GLY C 1 451  ? 35.866  47.084  57.915  1.00 129.43 ? 451  GLY B O   1 
ATOM   15785 N  N   . TYR C 1 452  ? 34.717  48.954  57.330  1.00 110.16 ? 452  TYR B N   1 
ATOM   15786 C  CA  . TYR C 1 452  ? 35.491  49.867  58.186  1.00 115.63 ? 452  TYR B CA  1 
ATOM   15787 C  C   . TYR C 1 452  ? 34.727  51.137  58.661  1.00 120.41 ? 452  TYR B C   1 
ATOM   15788 O  O   . TYR C 1 452  ? 33.502  51.120  58.803  1.00 117.54 ? 452  TYR B O   1 
ATOM   15789 C  CB  . TYR C 1 452  ? 36.823  50.231  57.509  1.00 116.50 ? 452  TYR B CB  1 
ATOM   15790 C  CG  . TYR C 1 452  ? 37.726  49.053  57.193  1.00 116.94 ? 452  TYR B CG  1 
ATOM   15791 C  CD1 . TYR C 1 452  ? 38.879  48.824  57.920  1.00 125.17 ? 452  TYR B CD1 1 
ATOM   15792 C  CD2 . TYR C 1 452  ? 37.422  48.175  56.174  1.00 112.59 ? 452  TYR B CD2 1 
ATOM   15793 C  CE1 . TYR C 1 452  ? 39.700  47.752  57.638  1.00 126.98 ? 452  TYR B CE1 1 
ATOM   15794 C  CE2 . TYR C 1 452  ? 38.230  47.094  55.895  1.00 113.77 ? 452  TYR B CE2 1 
ATOM   15795 C  CZ  . TYR C 1 452  ? 39.368  46.895  56.626  1.00 119.92 ? 452  TYR B CZ  1 
ATOM   15796 O  OH  . TYR C 1 452  ? 40.177  45.826  56.350  1.00 117.97 ? 452  TYR B OH  1 
ATOM   15797 N  N   . ARG C 1 453  ? 35.460  52.223  58.917  1.00 126.58 ? 453  ARG B N   1 
ATOM   15798 C  CA  . ARG C 1 453  ? 34.856  53.477  59.368  1.00 126.87 ? 453  ARG B CA  1 
ATOM   15799 C  C   . ARG C 1 453  ? 35.843  54.656  59.416  1.00 132.01 ? 453  ARG B C   1 
ATOM   15800 O  O   . ARG C 1 453  ? 36.958  54.520  59.912  1.00 136.12 ? 453  ARG B O   1 
ATOM   15801 C  CB  . ARG C 1 453  ? 34.243  53.260  60.751  1.00 129.71 ? 453  ARG B CB  1 
ATOM   15802 C  CG  . ARG C 1 453  ? 33.385  54.412  61.251  1.00 133.09 ? 453  ARG B CG  1 
ATOM   15803 C  CD  . ARG C 1 453  ? 33.194  54.352  62.766  1.00 139.38 ? 453  ARG B CD  1 
ATOM   15804 N  NE  . ARG C 1 453  ? 31.871  53.859  63.125  1.00 140.00 ? 453  ARG B NE  1 
ATOM   15805 C  CZ  . ARG C 1 453  ? 31.575  52.578  63.325  1.00 142.21 ? 453  ARG B CZ  1 
ATOM   15806 N  NH1 . ARG C 1 453  ? 32.510  51.642  63.207  1.00 143.81 ? 453  ARG B NH1 1 
ATOM   15807 N  NH2 . ARG C 1 453  ? 30.337  52.225  63.646  1.00 141.10 ? 453  ARG B NH2 1 
ATOM   15808 N  N   . ALA C 1 454  ? 35.430  55.813  58.902  1.00 144.66 ? 454  ALA B N   1 
ATOM   15809 C  CA  . ALA C 1 454  ? 36.270  57.015  58.956  1.00 155.12 ? 454  ALA B CA  1 
ATOM   15810 C  C   . ALA C 1 454  ? 35.550  58.150  59.655  1.00 161.55 ? 454  ALA B C   1 
ATOM   15811 O  O   . ALA C 1 454  ? 34.321  58.202  59.683  1.00 160.80 ? 454  ALA B O   1 
ATOM   15812 C  CB  . ALA C 1 454  ? 36.687  57.445  57.587  1.00 149.69 ? 454  ALA B CB  1 
ATOM   15813 N  N   . ILE C 1 455  ? 36.313  59.071  60.218  1.00 207.02 ? 455  ILE B N   1 
ATOM   15814 C  CA  . ILE C 1 455  ? 35.699  60.116  61.007  1.00 212.28 ? 455  ILE B CA  1 
ATOM   15815 C  C   . ILE C 1 455  ? 36.437  61.423  60.902  1.00 214.98 ? 455  ILE B C   1 
ATOM   15816 O  O   . ILE C 1 455  ? 37.667  61.465  60.916  1.00 217.54 ? 455  ILE B O   1 
ATOM   15817 C  CB  . ILE C 1 455  ? 35.657  59.716  62.459  1.00 205.96 ? 455  ILE B CB  1 
ATOM   15818 C  CG1 . ILE C 1 455  ? 34.695  58.548  62.643  1.00 201.56 ? 455  ILE B CG1 1 
ATOM   15819 C  CG2 . ILE C 1 455  ? 35.240  60.891  63.306  1.00 211.47 ? 455  ILE B CG2 1 
ATOM   15820 C  CD1 . ILE C 1 455  ? 34.894  57.805  63.967  1.00 207.16 ? 455  ILE B CD1 1 
ATOM   15821 N  N   . ALA C 1 456  ? 35.661  62.495  60.826  1.00 131.71 ? 456  ALA B N   1 
ATOM   15822 C  CA  . ALA C 1 456  ? 36.199  63.824  60.590  1.00 134.39 ? 456  ALA B CA  1 
ATOM   15823 C  C   . ALA C 1 456  ? 36.905  64.481  61.800  1.00 143.83 ? 456  ALA B C   1 
ATOM   15824 O  O   . ALA C 1 456  ? 36.259  64.804  62.815  1.00 145.93 ? 456  ALA B O   1 
ATOM   15825 C  CB  . ALA C 1 456  ? 35.093  64.722  60.070  1.00 132.72 ? 456  ALA B CB  1 
ATOM   15826 N  N   . TYR C 1 457  ? 38.225  64.679  61.663  1.00 131.03 ? 457  TYR B N   1 
ATOM   15827 C  CA  . TYR C 1 457  ? 39.034  65.518  62.567  1.00 137.66 ? 457  TYR B CA  1 
ATOM   15828 C  C   . TYR C 1 457  ? 38.290  66.812  62.866  1.00 142.11 ? 457  TYR B C   1 
ATOM   15829 O  O   . TYR C 1 457  ? 38.588  67.860  62.309  1.00 141.98 ? 457  TYR B O   1 
ATOM   15830 C  CB  . TYR C 1 457  ? 40.406  65.820  61.929  1.00 144.71 ? 457  TYR B CB  1 
ATOM   15831 C  CG  . TYR C 1 457  ? 41.292  66.836  62.640  1.00 158.35 ? 457  TYR B CG  1 
ATOM   15832 C  CD1 . TYR C 1 457  ? 42.634  67.001  62.269  1.00 164.43 ? 457  TYR B CD1 1 
ATOM   15833 C  CD2 . TYR C 1 457  ? 40.796  67.625  63.676  1.00 165.11 ? 457  TYR B CD2 1 
ATOM   15834 C  CE1 . TYR C 1 457  ? 43.449  67.932  62.920  1.00 172.70 ? 457  TYR B CE1 1 
ATOM   15835 C  CE2 . TYR C 1 457  ? 41.594  68.553  64.329  1.00 173.65 ? 457  TYR B CE2 1 
ATOM   15836 C  CZ  . TYR C 1 457  ? 42.917  68.710  63.955  1.00 176.46 ? 457  TYR B CZ  1 
ATOM   15837 O  OH  . TYR C 1 457  ? 43.684  69.645  64.634  1.00 183.44 ? 457  TYR B OH  1 
ATOM   15838 N  N   . SER C 1 458  ? 37.314  66.721  63.753  1.00 179.24 ? 458  SER B N   1 
ATOM   15839 C  CA  . SER C 1 458  ? 36.552  67.877  64.138  1.00 186.71 ? 458  SER B CA  1 
ATOM   15840 C  C   . SER C 1 458  ? 37.560  68.870  64.711  1.00 195.12 ? 458  SER B C   1 
ATOM   15841 O  O   . SER C 1 458  ? 38.617  68.474  65.211  1.00 195.84 ? 458  SER B O   1 
ATOM   15842 C  CB  . SER C 1 458  ? 35.483  67.465  65.147  1.00 188.59 ? 458  SER B CB  1 
ATOM   15843 O  OG  . SER C 1 458  ? 34.905  66.224  64.764  1.00 182.08 ? 458  SER B OG  1 
ATOM   15844 N  N   . SER C 1 459  ? 37.242  70.155  64.592  1.00 177.86 ? 459  SER B N   1 
ATOM   15845 C  CA  . SER C 1 459  ? 38.143  71.251  64.943  1.00 187.23 ? 459  SER B CA  1 
ATOM   15846 C  C   . SER C 1 459  ? 37.342  72.519  64.741  1.00 191.39 ? 459  SER B C   1 
ATOM   15847 O  O   . SER C 1 459  ? 36.875  72.792  63.638  1.00 186.30 ? 459  SER B O   1 
ATOM   15848 C  CB  . SER C 1 459  ? 39.383  71.257  64.038  1.00 186.43 ? 459  SER B CB  1 
ATOM   15849 O  OG  . SER C 1 459  ? 40.336  72.229  64.441  1.00 193.39 ? 459  SER B OG  1 
ATOM   15850 N  N   . LEU C 1 460  ? 37.170  73.292  65.802  1.00 262.79 ? 460  LEU B N   1 
ATOM   15851 C  CA  . LEU C 1 460  ? 36.241  74.407  65.734  1.00 272.74 ? 460  LEU B CA  1 
ATOM   15852 C  C   . LEU C 1 460  ? 36.690  75.560  64.821  1.00 280.70 ? 460  LEU B C   1 
ATOM   15853 O  O   . LEU C 1 460  ? 35.850  76.217  64.212  1.00 280.89 ? 460  LEU B O   1 
ATOM   15854 C  CB  . LEU C 1 460  ? 35.867  74.909  67.126  1.00 284.30 ? 460  LEU B CB  1 
ATOM   15855 C  CG  . LEU C 1 460  ? 34.464  75.515  67.127  1.00 288.58 ? 460  LEU B CG  1 
ATOM   15856 C  CD1 . LEU C 1 460  ? 33.402  74.423  67.267  1.00 283.12 ? 460  LEU B CD1 1 
ATOM   15857 C  CD2 . LEU C 1 460  ? 34.313  76.570  68.213  1.00 299.78 ? 460  LEU B CD2 1 
ATOM   15858 N  N   . SER C 1 461  ? 37.999  75.800  64.715  1.00 209.95 ? 461  SER B N   1 
ATOM   15859 C  CA  . SER C 1 461  ? 38.530  76.812  63.782  1.00 214.14 ? 461  SER B CA  1 
ATOM   15860 C  C   . SER C 1 461  ? 38.201  76.455  62.328  1.00 208.92 ? 461  SER B C   1 
ATOM   15861 O  O   . SER C 1 461  ? 38.642  77.129  61.398  1.00 209.29 ? 461  SER B O   1 
ATOM   15862 C  CB  . SER C 1 461  ? 40.048  76.997  63.953  1.00 216.55 ? 461  SER B CB  1 
ATOM   15863 O  OG  . SER C 1 461  ? 40.374  78.073  64.826  1.00 223.87 ? 461  SER B OG  1 
ATOM   15864 N  N   . GLN C 1 462  ? 37.431  75.384  62.152  1.00 172.97 ? 462  GLN B N   1 
ATOM   15865 C  CA  . GLN C 1 462  ? 37.062  74.882  60.838  1.00 166.15 ? 462  GLN B CA  1 
ATOM   15866 C  C   . GLN C 1 462  ? 38.283  74.362  60.106  1.00 162.50 ? 462  GLN B C   1 
ATOM   15867 O  O   . GLN C 1 462  ? 38.177  73.807  59.019  1.00 159.98 ? 462  GLN B O   1 
ATOM   15868 C  CB  . GLN C 1 462  ? 36.365  75.971  60.017  1.00 168.20 ? 462  GLN B CB  1 
ATOM   15869 C  CG  . GLN C 1 462  ? 34.853  75.977  60.166  1.00 170.13 ? 462  GLN B CG  1 
ATOM   15870 C  CD  . GLN C 1 462  ? 34.182  74.743  59.547  1.00 167.71 ? 462  GLN B CD  1 
ATOM   15871 O  OE1 . GLN C 1 462  ? 34.841  73.760  59.206  1.00 164.46 ? 462  GLN B OE1 1 
ATOM   15872 N  NE2 . GLN C 1 462  ? 32.863  74.799  59.403  1.00 169.40 ? 462  GLN B NE2 1 
ATOM   15873 N  N   . SER C 1 463  ? 39.439  74.541  60.728  1.00 197.22 ? 463  SER B N   1 
ATOM   15874 C  CA  . SER C 1 463  ? 40.723  74.257  60.107  1.00 191.40 ? 463  SER B CA  1 
ATOM   15875 C  C   . SER C 1 463  ? 41.124  72.790  60.189  1.00 181.47 ? 463  SER B C   1 
ATOM   15876 O  O   . SER C 1 463  ? 41.007  72.178  61.251  1.00 183.12 ? 463  SER B O   1 
ATOM   15877 C  CB  . SER C 1 463  ? 41.793  75.099  60.791  1.00 196.38 ? 463  SER B CB  1 
ATOM   15878 O  OG  . SER C 1 463  ? 42.955  74.342  61.057  1.00 195.15 ? 463  SER B OG  1 
ATOM   15879 N  N   . TYR C 1 464  ? 41.619  72.234  59.082  1.00 163.08 ? 464  TYR B N   1 
ATOM   15880 C  CA  . TYR C 1 464  ? 42.133  70.867  59.091  1.00 154.75 ? 464  TYR B CA  1 
ATOM   15881 C  C   . TYR C 1 464  ? 43.486  70.773  58.433  1.00 151.95 ? 464  TYR B C   1 
ATOM   15882 O  O   . TYR C 1 464  ? 44.060  71.769  57.999  1.00 153.53 ? 464  TYR B O   1 
ATOM   15883 C  CB  . TYR C 1 464  ? 41.171  69.915  58.399  1.00 150.48 ? 464  TYR B CB  1 
ATOM   15884 C  CG  . TYR C 1 464  ? 39.750  70.280  58.663  1.00 154.18 ? 464  TYR B CG  1 
ATOM   15885 C  CD1 . TYR C 1 464  ? 39.250  70.300  59.961  1.00 157.83 ? 464  TYR B CD1 1 
ATOM   15886 C  CD2 . TYR C 1 464  ? 38.906  70.636  57.631  1.00 154.57 ? 464  TYR B CD2 1 
ATOM   15887 C  CE1 . TYR C 1 464  ? 37.930  70.658  60.225  1.00 161.76 ? 464  TYR B CE1 1 
ATOM   15888 C  CE2 . TYR C 1 464  ? 37.585  70.992  57.881  1.00 158.93 ? 464  TYR B CE2 1 
ATOM   15889 C  CZ  . TYR C 1 464  ? 37.098  71.000  59.184  1.00 162.70 ? 464  TYR B CZ  1 
ATOM   15890 O  OH  . TYR C 1 464  ? 35.783  71.352  59.453  1.00 165.71 ? 464  TYR B OH  1 
ATOM   15891 N  N   . LEU C 1 465  ? 44.003  69.560  58.377  1.00 144.68 ? 465  LEU B N   1 
ATOM   15892 C  CA  . LEU C 1 465  ? 45.216  69.303  57.628  1.00 141.90 ? 465  LEU B CA  1 
ATOM   15893 C  C   . LEU C 1 465  ? 45.036  67.941  56.976  1.00 138.91 ? 465  LEU B C   1 
ATOM   15894 O  O   . LEU C 1 465  ? 44.174  67.153  57.404  1.00 139.11 ? 465  LEU B O   1 
ATOM   15895 C  CB  . LEU C 1 465  ? 46.452  69.312  58.536  1.00 141.88 ? 465  LEU B CB  1 
ATOM   15896 C  CG  . LEU C 1 465  ? 47.824  69.556  57.898  1.00 140.55 ? 465  LEU B CG  1 
ATOM   15897 C  CD1 . LEU C 1 465  ? 48.071  71.033  57.799  1.00 146.23 ? 465  LEU B CD1 1 
ATOM   15898 C  CD2 . LEU C 1 465  ? 48.932  68.910  58.690  1.00 141.88 ? 465  LEU B CD2 1 
ATOM   15899 N  N   . TYR C 1 466  ? 45.824  67.695  55.923  1.00 148.18 ? 466  TYR B N   1 
ATOM   15900 C  CA  . TYR C 1 466  ? 45.939  66.397  55.248  1.00 140.01 ? 466  TYR B CA  1 
ATOM   15901 C  C   . TYR C 1 466  ? 47.280  66.389  54.559  1.00 143.68 ? 466  TYR B C   1 
ATOM   15902 O  O   . TYR C 1 466  ? 47.576  67.255  53.745  1.00 144.81 ? 466  TYR B O   1 
ATOM   15903 C  CB  . TYR C 1 466  ? 44.826  66.166  54.215  1.00 139.30 ? 466  TYR B CB  1 
ATOM   15904 C  CG  . TYR C 1 466  ? 45.019  64.939  53.321  1.00 136.28 ? 466  TYR B CG  1 
ATOM   15905 C  CD1 . TYR C 1 466  ? 46.039  64.022  53.568  1.00 143.37 ? 466  TYR B CD1 1 
ATOM   15906 C  CD2 . TYR C 1 466  ? 44.168  64.687  52.243  1.00 140.71 ? 466  TYR B CD2 1 
ATOM   15907 C  CE1 . TYR C 1 466  ? 46.220  62.891  52.760  1.00 139.15 ? 466  TYR B CE1 1 
ATOM   15908 C  CE2 . TYR C 1 466  ? 44.336  63.555  51.425  1.00 136.99 ? 466  TYR B CE2 1 
ATOM   15909 C  CZ  . TYR C 1 466  ? 45.372  62.657  51.687  1.00 135.08 ? 466  TYR B CZ  1 
ATOM   15910 O  OH  . TYR C 1 466  ? 45.574  61.526  50.904  1.00 134.25 ? 466  TYR B OH  1 
ATOM   15911 N  N   . ILE C 1 467  ? 48.098  65.410  54.901  1.00 147.82 ? 467  ILE B N   1 
ATOM   15912 C  CA  . ILE C 1 467  ? 49.355  65.244  54.218  1.00 146.69 ? 467  ILE B CA  1 
ATOM   15913 C  C   . ILE C 1 467  ? 49.350  63.904  53.485  1.00 143.46 ? 467  ILE B C   1 
ATOM   15914 O  O   . ILE C 1 467  ? 48.738  62.938  53.960  1.00 140.39 ? 467  ILE B O   1 
ATOM   15915 C  CB  . ILE C 1 467  ? 50.556  65.371  55.178  1.00 146.67 ? 467  ILE B CB  1 
ATOM   15916 C  CG1 . ILE C 1 467  ? 50.813  64.072  55.928  1.00 146.94 ? 467  ILE B CG1 1 
ATOM   15917 C  CG2 . ILE C 1 467  ? 50.330  66.508  56.161  1.00 151.68 ? 467  ILE B CG2 1 
ATOM   15918 C  CD1 . ILE C 1 467  ? 52.132  64.083  56.671  1.00 147.75 ? 467  ILE B CD1 1 
ATOM   15919 N  N   . ASP C 1 468  ? 50.003  63.875  52.314  1.00 130.61 ? 468  ASP B N   1 
ATOM   15920 C  CA  . ASP C 1 468  ? 50.176  62.660  51.501  1.00 128.41 ? 468  ASP B CA  1 
ATOM   15921 C  C   . ASP C 1 468  ? 51.599  62.626  50.916  1.00 129.82 ? 468  ASP B C   1 
ATOM   15922 O  O   . ASP C 1 468  ? 52.494  63.332  51.388  1.00 131.51 ? 468  ASP B O   1 
ATOM   15923 C  CB  . ASP C 1 468  ? 49.100  62.571  50.399  1.00 134.02 ? 468  ASP B CB  1 
ATOM   15924 C  CG  . ASP C 1 468  ? 48.628  61.133  50.122  1.00 123.46 ? 468  ASP B CG  1 
ATOM   15925 O  OD1 . ASP C 1 468  ? 49.093  60.174  50.778  1.00 123.66 ? 468  ASP B OD1 1 
ATOM   15926 O  OD2 . ASP C 1 468  ? 47.769  60.967  49.229  1.00 124.09 ? 468  ASP B OD2 1 
ATOM   15927 N  N   . TRP C 1 469  ? 51.790  61.779  49.910  1.00 182.03 ? 469  TRP B N   1 
ATOM   15928 C  CA  . TRP C 1 469  ? 53.054  61.611  49.199  1.00 191.81 ? 469  TRP B CA  1 
ATOM   15929 C  C   . TRP C 1 469  ? 52.802  60.463  48.237  1.00 201.86 ? 469  TRP B C   1 
ATOM   15930 O  O   . TRP C 1 469  ? 51.840  59.708  48.426  1.00 198.91 ? 469  TRP B O   1 
ATOM   15931 C  CB  . TRP C 1 469  ? 54.219  61.292  50.155  1.00 190.30 ? 469  TRP B CB  1 
ATOM   15932 C  CG  . TRP C 1 469  ? 54.318  59.861  50.762  1.00 185.01 ? 469  TRP B CG  1 
ATOM   15933 C  CD1 . TRP C 1 469  ? 55.448  59.076  50.821  1.00 184.27 ? 469  TRP B CD1 1 
ATOM   15934 C  CD2 . TRP C 1 469  ? 53.279  59.095  51.425  1.00 181.96 ? 469  TRP B CD2 1 
ATOM   15935 N  NE1 . TRP C 1 469  ? 55.176  57.884  51.456  1.00 179.68 ? 469  TRP B NE1 1 
ATOM   15936 C  CE2 . TRP C 1 469  ? 53.858  57.867  51.831  1.00 178.90 ? 469  TRP B CE2 1 
ATOM   15937 C  CE3 . TRP C 1 469  ? 51.923  59.322  51.704  1.00 182.15 ? 469  TRP B CE3 1 
ATOM   15938 C  CZ2 . TRP C 1 469  ? 53.124  56.882  52.503  1.00 176.50 ? 469  TRP B CZ2 1 
ATOM   15939 C  CZ3 . TRP C 1 469  ? 51.199  58.333  52.374  1.00 178.54 ? 469  TRP B CZ3 1 
ATOM   15940 C  CH2 . TRP C 1 469  ? 51.800  57.137  52.762  1.00 175.69 ? 469  TRP B CH2 1 
ATOM   15941 N  N   . THR C 1 470  ? 53.608  60.316  47.192  1.00 214.69 ? 470  THR B N   1 
ATOM   15942 C  CA  . THR C 1 470  ? 53.466  59.076  46.441  1.00 223.01 ? 470  THR B CA  1 
ATOM   15943 C  C   . THR C 1 470  ? 54.756  58.356  46.090  1.00 238.78 ? 470  THR B C   1 
ATOM   15944 O  O   . THR C 1 470  ? 55.766  58.975  45.754  1.00 244.22 ? 470  THR B O   1 
ATOM   15945 C  CB  . THR C 1 470  ? 52.567  59.214  45.209  1.00 219.00 ? 470  THR B CB  1 
ATOM   15946 O  OG1 . THR C 1 470  ? 51.352  59.867  45.590  1.00 217.92 ? 470  THR B OG1 1 
ATOM   15947 C  CG2 . THR C 1 470  ? 52.222  57.825  44.666  1.00 211.91 ? 470  THR B CG2 1 
ATOM   15948 N  N   . ASP C 1 471  ? 54.677  57.031  46.216  1.00 179.10 ? 471  ASP B N   1 
ATOM   15949 C  CA  . ASP C 1 471  ? 55.654  56.073  45.717  1.00 195.94 ? 471  ASP B CA  1 
ATOM   15950 C  C   . ASP C 1 471  ? 54.888  54.842  45.149  1.00 204.99 ? 471  ASP B C   1 
ATOM   15951 O  O   . ASP C 1 471  ? 53.915  54.376  45.768  1.00 202.16 ? 471  ASP B O   1 
ATOM   15952 C  CB  . ASP C 1 471  ? 56.574  55.638  46.849  1.00 202.61 ? 471  ASP B CB  1 
ATOM   15953 C  CG  . ASP C 1 471  ? 57.935  55.043  46.351  1.00 211.92 ? 471  ASP B CG  1 
ATOM   15954 O  OD1 . ASP C 1 471  ? 58.787  55.728  45.681  1.00 218.69 ? 471  ASP B OD1 1 
ATOM   15955 O  OD2 . ASP C 1 471  ? 58.234  53.899  46.742  1.00 212.93 ? 471  ASP B OD2 1 
ATOM   15956 N  N   . ASN C 1 472  ? 55.349  54.315  44.001  1.00 341.16 ? 472  ASN B N   1 
ATOM   15957 C  CA  . ASN C 1 472  ? 54.785  53.115  43.350  1.00 347.43 ? 472  ASN B CA  1 
ATOM   15958 C  C   . ASN C 1 472  ? 55.201  51.769  43.970  1.00 351.98 ? 472  ASN B C   1 
ATOM   15959 O  O   . ASN C 1 472  ? 54.582  50.748  43.695  1.00 348.74 ? 472  ASN B O   1 
ATOM   15960 C  CB  . ASN C 1 472  ? 55.016  53.121  41.812  1.00 348.47 ? 472  ASN B CB  1 
ATOM   15961 C  CG  . ASN C 1 472  ? 56.477  53.359  41.409  1.00 349.98 ? 472  ASN B CG  1 
ATOM   15962 O  OD1 . ASN C 1 472  ? 57.356  53.484  42.256  1.00 350.33 ? 472  ASN B OD1 1 
ATOM   15963 N  ND2 . ASN C 1 472  ? 56.728  53.425  40.098  1.00 350.89 ? 472  ASN B ND2 1 
ATOM   15964 N  N   . HIS C 1 473  ? 56.237  51.784  44.812  1.00 252.86 ? 473  HIS B N   1 
ATOM   15965 C  CA  . HIS C 1 473  ? 56.727  50.573  45.487  1.00 258.95 ? 473  HIS B CA  1 
ATOM   15966 C  C   . HIS C 1 473  ? 56.319  50.476  46.954  1.00 243.36 ? 473  HIS B C   1 
ATOM   15967 O  O   . HIS C 1 473  ? 56.360  51.468  47.695  1.00 244.17 ? 473  HIS B O   1 
ATOM   15968 C  CB  . HIS C 1 473  ? 58.254  50.417  45.361  1.00 283.72 ? 473  HIS B CB  1 
ATOM   15969 C  CG  . HIS C 1 473  ? 58.876  51.227  44.268  1.00 308.28 ? 473  HIS B CG  1 
ATOM   15970 N  ND1 . HIS C 1 473  ? 59.274  52.549  44.451  1.00 319.18 ? 473  HIS B ND1 1 
ATOM   15971 C  CD2 . HIS C 1 473  ? 59.213  50.927  42.991  1.00 319.65 ? 473  HIS B CD2 1 
ATOM   15972 C  CE1 . HIS C 1 473  ? 59.803  53.005  43.337  1.00 337.35 ? 473  HIS B CE1 1 
ATOM   15973 N  NE2 . HIS C 1 473  ? 59.779  52.047  42.431  1.00 328.62 ? 473  HIS B NE2 1 
ATOM   15974 N  N   . LYS C 1 474  ? 55.981  49.251  47.358  1.00 307.01 ? 474  LYS B N   1 
ATOM   15975 C  CA  . LYS C 1 474  ? 55.374  48.969  48.653  1.00 293.86 ? 474  LYS B CA  1 
ATOM   15976 C  C   . LYS C 1 474  ? 56.292  49.395  49.775  1.00 283.05 ? 474  LYS B C   1 
ATOM   15977 O  O   . LYS C 1 474  ? 55.912  49.376  50.947  1.00 283.80 ? 474  LYS B O   1 
ATOM   15978 C  CB  . LYS C 1 474  ? 55.092  47.477  48.786  1.00 293.43 ? 474  LYS B CB  1 
ATOM   15979 C  CG  . LYS C 1 474  ? 56.233  46.587  48.324  1.00 295.97 ? 474  LYS B CG  1 
ATOM   15980 C  CD  . LYS C 1 474  ? 55.925  45.143  48.610  1.00 294.43 ? 474  LYS B CD  1 
ATOM   15981 C  CE  . LYS C 1 474  ? 55.901  44.895  50.102  1.00 294.38 ? 474  LYS B CE  1 
ATOM   15982 N  NZ  . LYS C 1 474  ? 55.629  43.468  50.412  1.00 292.05 ? 474  LYS B NZ  1 
ATOM   15983 N  N   . ALA C 1 475  ? 57.499  49.796  49.411  1.00 238.24 ? 475  ALA B N   1 
ATOM   15984 C  CA  . ALA C 1 475  ? 58.414  50.295  50.397  1.00 223.19 ? 475  ALA B CA  1 
ATOM   15985 C  C   . ALA C 1 475  ? 59.314  51.328  49.774  1.00 211.55 ? 475  ALA B C   1 
ATOM   15986 O  O   . ALA C 1 475  ? 59.459  51.359  48.560  1.00 210.13 ? 475  ALA B O   1 
ATOM   15987 C  CB  . ALA C 1 475  ? 59.219  49.144  50.999  1.00 222.61 ? 475  ALA B CB  1 
ATOM   15988 N  N   . LEU C 1 476  ? 59.866  52.183  50.619  1.00 185.33 ? 476  LEU B N   1 
ATOM   15989 C  CA  . LEU C 1 476  ? 60.645  53.273  50.167  1.00 176.81 ? 476  LEU B CA  1 
ATOM   15990 C  C   . LEU C 1 476  ? 62.004  53.040  50.747  1.00 174.01 ? 476  LEU B C   1 
ATOM   15991 O  O   . LEU C 1 476  ? 62.195  53.099  51.948  1.00 176.12 ? 476  LEU B O   1 
ATOM   15992 C  CB  . LEU C 1 476  ? 60.006  54.545  50.682  1.00 169.93 ? 476  LEU B CB  1 
ATOM   15993 C  CG  . LEU C 1 476  ? 58.523  54.336  51.161  1.00 160.34 ? 476  LEU B CG  1 
ATOM   15994 C  CD1 . LEU C 1 476  ? 58.049  55.559  51.801  1.00 160.24 ? 476  LEU B CD1 1 
ATOM   15995 C  CD2 . LEU C 1 476  ? 57.500  53.936  50.139  1.00 158.25 ? 476  LEU B CD2 1 
ATOM   15996 N  N   . LEU C 1 477  ? 62.925  52.716  49.861  1.00 191.54 ? 477  LEU B N   1 
ATOM   15997 C  CA  . LEU C 1 477  ? 64.225  52.258  50.230  1.00 188.47 ? 477  LEU B CA  1 
ATOM   15998 C  C   . LEU C 1 477  ? 64.915  53.394  50.933  1.00 184.39 ? 477  LEU B C   1 
ATOM   15999 O  O   . LEU C 1 477  ? 64.485  54.538  50.841  1.00 185.67 ? 477  LEU B O   1 
ATOM   16000 C  CB  . LEU C 1 477  ? 64.982  51.849  48.965  1.00 194.40 ? 477  LEU B CB  1 
ATOM   16001 C  CG  . LEU C 1 477  ? 64.002  51.207  47.964  1.00 197.43 ? 477  LEU B CG  1 
ATOM   16002 C  CD1 . LEU C 1 477  ? 64.609  51.046  46.580  1.00 203.29 ? 477  LEU B CD1 1 
ATOM   16003 C  CD2 . LEU C 1 477  ? 63.458  49.882  48.475  1.00 195.35 ? 477  LEU B CD2 1 
ATOM   16004 N  N   . VAL C 1 478  ? 65.951  53.064  51.683  1.00 145.58 ? 478  VAL B N   1 
ATOM   16005 C  CA  . VAL C 1 478  ? 66.737  54.058  52.373  1.00 150.27 ? 478  VAL B CA  1 
ATOM   16006 C  C   . VAL C 1 478  ? 67.663  54.746  51.403  1.00 154.98 ? 478  VAL B C   1 
ATOM   16007 O  O   . VAL C 1 478  ? 68.227  54.114  50.523  1.00 153.92 ? 478  VAL B O   1 
ATOM   16008 C  CB  . VAL C 1 478  ? 67.618  53.414  53.447  1.00 151.11 ? 478  VAL B CB  1 
ATOM   16009 C  CG1 . VAL C 1 478  ? 68.876  52.834  52.818  1.00 154.71 ? 478  VAL B CG1 1 
ATOM   16010 C  CG2 . VAL C 1 478  ? 67.976  54.434  54.503  1.00 153.26 ? 478  VAL B CG2 1 
ATOM   16011 N  N   . GLY C 1 479  ? 67.856  56.042  51.595  1.00 122.82 ? 479  GLY B N   1 
ATOM   16012 C  CA  . GLY C 1 479  ? 68.632  56.849  50.674  1.00 130.57 ? 479  GLY B CA  1 
ATOM   16013 C  C   . GLY C 1 479  ? 67.731  57.700  49.798  1.00 131.88 ? 479  GLY B C   1 
ATOM   16014 O  O   . GLY C 1 479  ? 68.094  58.817  49.432  1.00 137.11 ? 479  GLY B O   1 
ATOM   16015 N  N   . GLU C 1 480  ? 66.557  57.160  49.466  1.00 183.68 ? 480  GLU B N   1 
ATOM   16016 C  CA  . GLU C 1 480  ? 65.579  57.840  48.624  1.00 182.69 ? 480  GLU B CA  1 
ATOM   16017 C  C   . GLU C 1 480  ? 65.205  59.173  49.220  1.00 183.87 ? 480  GLU B C   1 
ATOM   16018 O  O   . GLU C 1 480  ? 65.792  59.627  50.203  1.00 184.69 ? 480  GLU B O   1 
ATOM   16019 C  CB  . GLU C 1 480  ? 64.327  56.994  48.433  1.00 180.79 ? 480  GLU B CB  1 
ATOM   16020 C  CG  . GLU C 1 480  ? 64.434  56.104  47.220  1.00 188.07 ? 480  GLU B CG  1 
ATOM   16021 C  CD  . GLU C 1 480  ? 63.093  55.393  46.884  1.00 192.25 ? 480  GLU B CD  1 
ATOM   16022 O  OE1 . GLU C 1 480  ? 62.728  55.132  45.673  1.00 193.50 ? 480  GLU B OE1 1 
ATOM   16023 O  OE2 . GLU C 1 480  ? 62.344  55.085  47.826  1.00 193.14 ? 480  GLU B OE2 1 
ATOM   16024 N  N   . HIS C 1 481  ? 64.211  59.805  48.627  1.00 191.39 ? 481  HIS B N   1 
ATOM   16025 C  CA  . HIS C 1 481  ? 63.788  61.088  49.130  1.00 195.81 ? 481  HIS B CA  1 
ATOM   16026 C  C   . HIS C 1 481  ? 62.288  61.201  49.137  1.00 189.20 ? 481  HIS B C   1 
ATOM   16027 O  O   . HIS C 1 481  ? 61.626  60.937  48.140  1.00 186.36 ? 481  HIS B O   1 
ATOM   16028 C  CB  . HIS C 1 481  ? 64.441  62.203  48.323  1.00 208.08 ? 481  HIS B CB  1 
ATOM   16029 C  CG  . HIS C 1 481  ? 65.848  62.489  48.737  1.00 217.54 ? 481  HIS B CG  1 
ATOM   16030 N  ND1 . HIS C 1 481  ? 66.157  63.266  49.842  1.00 222.76 ? 481  HIS B ND1 1 
ATOM   16031 C  CD2 . HIS C 1 481  ? 67.038  62.101  48.220  1.00 218.63 ? 481  HIS B CD2 1 
ATOM   16032 C  CE1 . HIS C 1 481  ? 67.463  63.350  49.972  1.00 225.71 ? 481  HIS B CE1 1 
ATOM   16033 N  NE2 . HIS C 1 481  ? 68.027  62.647  48.998  1.00 222.39 ? 481  HIS B NE2 1 
ATOM   16034 N  N   . LEU C 1 482  ? 61.751  61.573  50.288  1.00 174.40 ? 482  LEU B N   1 
ATOM   16035 C  CA  . LEU C 1 482  ? 60.311  61.601  50.431  1.00 171.49 ? 482  LEU B CA  1 
ATOM   16036 C  C   . LEU C 1 482  ? 59.654  62.932  50.080  1.00 175.01 ? 482  LEU B C   1 
ATOM   16037 O  O   . LEU C 1 482  ? 59.756  63.913  50.828  1.00 179.36 ? 482  LEU B O   1 
ATOM   16038 C  CB  . LEU C 1 482  ? 59.892  61.149  51.827  1.00 167.59 ? 482  LEU B CB  1 
ATOM   16039 C  CG  . LEU C 1 482  ? 58.509  60.481  51.830  1.00 161.22 ? 482  LEU B CG  1 
ATOM   16040 C  CD1 . LEU C 1 482  ? 58.378  59.524  53.003  1.00 156.16 ? 482  LEU B CD1 1 
ATOM   16041 C  CD2 . LEU C 1 482  ? 57.363  61.502  51.782  1.00 162.50 ? 482  LEU B CD2 1 
ATOM   16042 N  N   . ASN C 1 483  ? 58.966  62.944  48.940  1.00 196.05 ? 483  ASN B N   1 
ATOM   16043 C  CA  . ASN C 1 483  ? 58.109  64.063  48.583  1.00 196.98 ? 483  ASN B CA  1 
ATOM   16044 C  C   . ASN C 1 483  ? 56.697  63.932  49.124  1.00 191.97 ? 483  ASN B C   1 
ATOM   16045 O  O   . ASN C 1 483  ? 55.895  63.141  48.598  1.00 189.24 ? 483  ASN B O   1 
ATOM   16046 C  CB  . ASN C 1 483  ? 58.032  64.255  47.079  1.00 201.25 ? 483  ASN B CB  1 
ATOM   16047 C  CG  . ASN C 1 483  ? 57.626  65.658  46.717  1.00 207.43 ? 483  ASN B CG  1 
ATOM   16048 O  OD1 . ASN C 1 483  ? 58.122  66.623  47.298  1.00 211.34 ? 483  ASN B OD1 1 
ATOM   16049 N  ND2 . ASN C 1 483  ? 56.717  65.786  45.764  1.00 207.76 ? 483  ASN B ND2 1 
ATOM   16050 N  N   . ILE C 1 484  ? 56.410  64.743  50.148  1.00 162.36 ? 484  ILE B N   1 
ATOM   16051 C  CA  . ILE C 1 484  ? 55.098  64.809  50.801  1.00 155.61 ? 484  ILE B CA  1 
ATOM   16052 C  C   . ILE C 1 484  ? 54.375  66.161  50.641  1.00 154.34 ? 484  ILE B C   1 
ATOM   16053 O  O   . ILE C 1 484  ? 54.960  67.230  50.842  1.00 157.89 ? 484  ILE B O   1 
ATOM   16054 C  CB  . ILE C 1 484  ? 55.218  64.503  52.289  1.00 153.74 ? 484  ILE B CB  1 
ATOM   16055 C  CG1 . ILE C 1 484  ? 54.027  65.108  53.042  1.00 152.34 ? 484  ILE B CG1 1 
ATOM   16056 C  CG2 . ILE C 1 484  ? 56.560  64.997  52.815  1.00 157.26 ? 484  ILE B CG2 1 
ATOM   16057 C  CD1 . ILE C 1 484  ? 54.342  65.582  54.441  1.00 150.85 ? 484  ILE B CD1 1 
ATOM   16058 N  N   . ILE C 1 485  ? 53.092  66.083  50.290  1.00 161.92 ? 485  ILE B N   1 
ATOM   16059 C  CA  . ILE C 1 485  ? 52.268  67.248  49.991  1.00 163.69 ? 485  ILE B CA  1 
ATOM   16060 C  C   . ILE C 1 485  ? 51.438  67.606  51.195  1.00 166.85 ? 485  ILE B C   1 
ATOM   16061 O  O   . ILE C 1 485  ? 50.787  66.748  51.781  1.00 165.25 ? 485  ILE B O   1 
ATOM   16062 C  CB  . ILE C 1 485  ? 51.308  66.978  48.829  1.00 159.92 ? 485  ILE B CB  1 
ATOM   16063 C  CG1 . ILE C 1 485  ? 52.021  67.197  47.494  1.00 160.85 ? 485  ILE B CG1 1 
ATOM   16064 C  CG2 . ILE C 1 485  ? 50.074  67.846  48.939  1.00 162.73 ? 485  ILE B CG2 1 
ATOM   16065 C  CD1 . ILE C 1 485  ? 52.930  66.050  47.072  1.00 161.36 ? 485  ILE B CD1 1 
ATOM   16066 N  N   . VAL C 1 486  ? 51.453  68.889  51.533  1.00 129.51 ? 486  VAL B N   1 
ATOM   16067 C  CA  . VAL C 1 486  ? 50.896  69.392  52.773  1.00 130.44 ? 486  VAL B CA  1 
ATOM   16068 C  C   . VAL C 1 486  ? 49.704  70.266  52.461  1.00 132.63 ? 486  VAL B C   1 
ATOM   16069 O  O   . VAL C 1 486  ? 49.812  71.476  52.464  1.00 134.69 ? 486  VAL B O   1 
ATOM   16070 C  CB  . VAL C 1 486  ? 51.938  70.247  53.502  1.00 133.05 ? 486  VAL B CB  1 
ATOM   16071 C  CG1 . VAL C 1 486  ? 51.334  70.903  54.724  1.00 135.02 ? 486  VAL B CG1 1 
ATOM   16072 C  CG2 . VAL C 1 486  ? 53.166  69.409  53.864  1.00 133.59 ? 486  VAL B CG2 1 
ATOM   16073 N  N   . THR C 1 487  ? 48.565  69.652  52.181  1.00 188.79 ? 487  THR B N   1 
ATOM   16074 C  CA  . THR C 1 487  ? 47.401  70.402  51.736  1.00 190.00 ? 487  THR B CA  1 
ATOM   16075 C  C   . THR C 1 487  ? 46.558  70.881  52.909  1.00 192.15 ? 487  THR B C   1 
ATOM   16076 O  O   . THR C 1 487  ? 45.698  70.146  53.381  1.00 188.14 ? 487  THR B O   1 
ATOM   16077 C  CB  . THR C 1 487  ? 46.517  69.536  50.828  1.00 188.87 ? 487  THR B CB  1 
ATOM   16078 O  OG1 . THR C 1 487  ? 46.171  68.330  51.520  1.00 185.59 ? 487  THR B OG1 1 
ATOM   16079 C  CG2 . THR C 1 487  ? 47.258  69.178  49.549  1.00 186.77 ? 487  THR B CG2 1 
ATOM   16080 N  N   . PRO C 1 488  ? 46.784  72.122  53.379  1.00 139.76 ? 488  PRO B N   1 
ATOM   16081 C  CA  . PRO C 1 488  ? 46.063  72.575  54.578  1.00 142.87 ? 488  PRO B CA  1 
ATOM   16082 C  C   . PRO C 1 488  ? 44.597  72.862  54.311  1.00 149.44 ? 488  PRO B C   1 
ATOM   16083 O  O   . PRO C 1 488  ? 43.922  73.344  55.214  1.00 147.23 ? 488  PRO B O   1 
ATOM   16084 C  CB  . PRO C 1 488  ? 46.782  73.876  54.966  1.00 146.10 ? 488  PRO B CB  1 
ATOM   16085 C  CG  . PRO C 1 488  ? 48.035  73.892  54.168  1.00 145.90 ? 488  PRO B CG  1 
ATOM   16086 C  CD  . PRO C 1 488  ? 47.733  73.140  52.907  1.00 142.29 ? 488  PRO B CD  1 
ATOM   16087 N  N   . LYS C 1 489  ? 44.131  72.554  53.103  1.00 195.80 ? 489  LYS B N   1 
ATOM   16088 C  CA  . LYS C 1 489  ? 42.767  72.851  52.653  1.00 208.93 ? 489  LYS B CA  1 
ATOM   16089 C  C   . LYS C 1 489  ? 41.743  73.114  53.758  1.00 219.14 ? 489  LYS B C   1 
ATOM   16090 O  O   . LYS C 1 489  ? 41.630  72.348  54.714  1.00 218.81 ? 489  LYS B O   1 
ATOM   16091 C  CB  . LYS C 1 489  ? 42.254  71.729  51.740  1.00 206.82 ? 489  LYS B CB  1 
ATOM   16092 C  CG  . LYS C 1 489  ? 40.842  71.952  51.194  1.00 208.61 ? 489  LYS B CG  1 
ATOM   16093 C  CD  . LYS C 1 489  ? 40.601  71.134  49.919  1.00 208.07 ? 489  LYS B CD  1 
ATOM   16094 C  CE  . LYS C 1 489  ? 39.260  71.463  49.263  1.00 210.23 ? 489  LYS B CE  1 
ATOM   16095 N  NZ  . LYS C 1 489  ? 39.152  72.881  48.805  1.00 217.05 ? 489  LYS B NZ  1 
ATOM   16096 N  N   . SER C 1 490  ? 41.013  74.214  53.599  1.00 219.44 ? 490  SER B N   1 
ATOM   16097 C  CA  . SER C 1 490  ? 39.847  74.553  54.418  1.00 226.34 ? 490  SER B CA  1 
ATOM   16098 C  C   . SER C 1 490  ? 40.023  75.717  55.424  1.00 234.09 ? 490  SER B C   1 
ATOM   16099 O  O   . SER C 1 490  ? 39.373  76.762  55.258  1.00 239.55 ? 490  SER B O   1 
ATOM   16100 C  CB  . SER C 1 490  ? 39.217  73.305  55.047  1.00 225.72 ? 490  SER B CB  1 
ATOM   16101 O  OG  . SER C 1 490  ? 38.820  72.392  54.036  1.00 223.40 ? 490  SER B OG  1 
ATOM   16102 N  N   . PRO C 1 491  ? 40.901  75.562  56.442  1.00 214.12 ? 491  PRO B N   1 
ATOM   16103 C  CA  . PRO C 1 491  ? 40.995  76.633  57.441  1.00 214.93 ? 491  PRO B CA  1 
ATOM   16104 C  C   . PRO C 1 491  ? 40.444  77.966  56.950  1.00 208.45 ? 491  PRO B C   1 
ATOM   16105 O  O   . PRO C 1 491  ? 40.908  78.510  55.942  1.00 205.59 ? 491  PRO B O   1 
ATOM   16106 C  CB  . PRO C 1 491  ? 42.498  76.703  57.706  1.00 220.39 ? 491  PRO B CB  1 
ATOM   16107 C  CG  . PRO C 1 491  ? 42.930  75.227  57.609  1.00 217.45 ? 491  PRO B CG  1 
ATOM   16108 C  CD  . PRO C 1 491  ? 41.922  74.524  56.687  1.00 213.07 ? 491  PRO B CD  1 
ATOM   16109 N  N   . TYR C 1 492  ? 39.434  78.462  57.656  1.00 222.90 ? 492  TYR B N   1 
ATOM   16110 C  CA  . TYR C 1 492  ? 38.764  79.661  57.232  1.00 223.68 ? 492  TYR B CA  1 
ATOM   16111 C  C   . TYR C 1 492  ? 39.837  80.600  56.759  1.00 226.88 ? 492  TYR B C   1 
ATOM   16112 O  O   . TYR C 1 492  ? 39.560  81.470  55.949  1.00 231.16 ? 492  TYR B O   1 
ATOM   16113 C  CB  . TYR C 1 492  ? 37.947  80.292  58.357  1.00 227.02 ? 492  TYR B CB  1 
ATOM   16114 C  CG  . TYR C 1 492  ? 38.759  80.951  59.453  1.00 228.95 ? 492  TYR B CG  1 
ATOM   16115 C  CD1 . TYR C 1 492  ? 38.161  81.850  60.341  1.00 232.73 ? 492  TYR B CD1 1 
ATOM   16116 C  CD2 . TYR C 1 492  ? 40.114  80.671  59.619  1.00 225.81 ? 492  TYR B CD2 1 
ATOM   16117 C  CE1 . TYR C 1 492  ? 38.897  82.456  61.367  1.00 235.64 ? 492  TYR B CE1 1 
ATOM   16118 C  CE2 . TYR C 1 492  ? 40.861  81.274  60.632  1.00 228.79 ? 492  TYR B CE2 1 
ATOM   16119 C  CZ  . TYR C 1 492  ? 40.247  82.164  61.510  1.00 234.41 ? 492  TYR B CZ  1 
ATOM   16120 O  OH  . TYR C 1 492  ? 40.983  82.757  62.522  1.00 239.89 ? 492  TYR B OH  1 
ATOM   16121 N  N   . ILE C 1 493  ? 41.070  80.423  57.241  1.00 191.48 ? 493  ILE B N   1 
ATOM   16122 C  CA  . ILE C 1 493  ? 42.181  81.217  56.696  1.00 198.59 ? 493  ILE B CA  1 
ATOM   16123 C  C   . ILE C 1 493  ? 43.576  80.555  56.567  1.00 200.38 ? 493  ILE B C   1 
ATOM   16124 O  O   . ILE C 1 493  ? 43.848  79.492  57.125  1.00 198.27 ? 493  ILE B O   1 
ATOM   16125 C  CB  . ILE C 1 493  ? 42.233  82.694  57.274  1.00 273.60 ? 493  ILE B CB  1 
ATOM   16126 C  CG1 . ILE C 1 493  ? 41.634  83.692  56.258  1.00 276.08 ? 493  ILE B CG1 1 
ATOM   16127 C  CG2 . ILE C 1 493  ? 43.648  83.103  57.633  1.00 276.74 ? 493  ILE B CG2 1 
ATOM   16128 C  CD1 . ILE C 1 493  ? 41.811  85.178  56.589  1.00 283.44 ? 493  ILE B CD1 1 
ATOM   16129 N  N   . ASP C 1 494  ? 44.419  81.227  55.781  1.00 228.16 ? 494  ASP B N   1 
ATOM   16130 C  CA  . ASP C 1 494  ? 45.723  80.761  55.324  1.00 226.67 ? 494  ASP B CA  1 
ATOM   16131 C  C   . ASP C 1 494  ? 46.900  81.469  55.993  1.00 231.88 ? 494  ASP B C   1 
ATOM   16132 O  O   . ASP C 1 494  ? 48.037  81.302  55.559  1.00 232.31 ? 494  ASP B O   1 
ATOM   16133 C  CB  . ASP C 1 494  ? 45.843  81.010  53.811  1.00 227.67 ? 494  ASP B CB  1 
ATOM   16134 C  CG  . ASP C 1 494  ? 45.785  82.509  53.443  1.00 227.44 ? 494  ASP B CG  1 
ATOM   16135 O  OD1 . ASP C 1 494  ? 45.002  83.258  54.073  1.00 228.91 ? 494  ASP B OD1 1 
ATOM   16136 O  OD2 . ASP C 1 494  ? 46.512  82.942  52.516  1.00 229.58 ? 494  ASP B OD2 1 
ATOM   16137 N  N   . LYS C 1 495  ? 46.637  82.275  57.018  1.00 210.91 ? 495  LYS B N   1 
ATOM   16138 C  CA  . LYS C 1 495  ? 47.678  83.120  57.621  1.00 214.34 ? 495  LYS B CA  1 
ATOM   16139 C  C   . LYS C 1 495  ? 48.789  82.310  58.257  1.00 207.36 ? 495  LYS B C   1 
ATOM   16140 O  O   . LYS C 1 495  ? 49.339  82.675  59.300  1.00 208.51 ? 495  LYS B O   1 
ATOM   16141 C  CB  . LYS C 1 495  ? 47.086  84.103  58.636  1.00 222.05 ? 495  LYS B CB  1 
ATOM   16142 C  CG  . LYS C 1 495  ? 46.380  85.303  57.998  1.00 228.06 ? 495  LYS B CG  1 
ATOM   16143 C  CD  . LYS C 1 495  ? 47.146  85.831  56.791  1.00 229.00 ? 495  LYS B CD  1 
ATOM   16144 C  CE  . LYS C 1 495  ? 46.598  85.247  55.497  1.00 222.67 ? 495  LYS B CE  1 
ATOM   16145 N  NZ  . LYS C 1 495  ? 47.609  85.249  54.395  1.00 219.86 ? 495  LYS B NZ  1 
ATOM   16146 N  N   . ILE C 1 496  ? 49.117  81.207  57.602  1.00 203.24 ? 496  ILE B N   1 
ATOM   16147 C  CA  . ILE C 1 496  ? 50.022  80.238  58.165  1.00 198.34 ? 496  ILE B CA  1 
ATOM   16148 C  C   . ILE C 1 496  ? 51.449  80.696  58.097  1.00 203.92 ? 496  ILE B C   1 
ATOM   16149 O  O   . ILE C 1 496  ? 51.959  81.038  57.039  1.00 205.19 ? 496  ILE B O   1 
ATOM   16150 C  CB  . ILE C 1 496  ? 49.932  78.912  57.445  1.00 188.10 ? 496  ILE B CB  1 
ATOM   16151 C  CG1 . ILE C 1 496  ? 48.460  78.529  57.235  1.00 179.76 ? 496  ILE B CG1 1 
ATOM   16152 C  CG2 . ILE C 1 496  ? 50.731  77.852  58.219  1.00 188.14 ? 496  ILE B CG2 1 
ATOM   16153 C  CD1 . ILE C 1 496  ? 47.994  78.624  55.794  1.00 175.86 ? 496  ILE B CD1 1 
ATOM   16154 N  N   . THR C 1 497  ? 52.094  80.689  59.247  1.00 161.99 ? 497  THR B N   1 
ATOM   16155 C  CA  . THR C 1 497  ? 53.498  80.993  59.309  1.00 169.40 ? 497  THR B CA  1 
ATOM   16156 C  C   . THR C 1 497  ? 54.300  79.828  58.762  1.00 166.26 ? 497  THR B C   1 
ATOM   16157 O  O   . THR C 1 497  ? 54.782  79.863  57.635  1.00 167.76 ? 497  THR B O   1 
ATOM   16158 C  CB  . THR C 1 497  ? 53.940  81.249  60.745  1.00 177.59 ? 497  THR B CB  1 
ATOM   16159 O  OG1 . THR C 1 497  ? 55.365  81.130  60.815  1.00 180.41 ? 497  THR B OG1 1 
ATOM   16160 C  CG2 . THR C 1 497  ? 53.290  80.237  61.720  1.00 174.72 ? 497  THR B CG2 1 
ATOM   16161 N  N   . HIS C 1 498  ? 54.434  78.783  59.564  1.00 215.57 ? 498  HIS B N   1 
ATOM   16162 C  CA  . HIS C 1 498  ? 55.343  77.717  59.210  1.00 209.92 ? 498  HIS B CA  1 
ATOM   16163 C  C   . HIS C 1 498  ? 54.650  76.370  59.209  1.00 199.48 ? 498  HIS B C   1 
ATOM   16164 O  O   . HIS C 1 498  ? 53.625  76.185  59.866  1.00 198.64 ? 498  HIS B O   1 
ATOM   16165 C  CB  . HIS C 1 498  ? 56.546  77.715  60.162  1.00 215.53 ? 498  HIS B CB  1 
ATOM   16166 C  CG  . HIS C 1 498  ? 57.418  78.936  60.045  1.00 225.56 ? 498  HIS B CG  1 
ATOM   16167 N  ND1 . HIS C 1 498  ? 57.622  79.809  61.084  1.00 231.95 ? 498  HIS B ND1 1 
ATOM   16168 C  CD2 . HIS C 1 498  ? 58.132  79.414  58.996  1.00 228.49 ? 498  HIS B CD2 1 
ATOM   16169 C  CE1 . HIS C 1 498  ? 58.432  80.783  60.685  1.00 237.95 ? 498  HIS B CE1 1 
ATOM   16170 N  NE2 . HIS C 1 498  ? 58.752  80.566  59.427  1.00 235.98 ? 498  HIS B NE2 1 
ATOM   16171 N  N   . TYR C 1 499  ? 55.195  75.447  58.427  1.00 187.44 ? 499  TYR B N   1 
ATOM   16172 C  CA  . TYR C 1 499  ? 54.874  74.051  58.610  1.00 174.33 ? 499  TYR B CA  1 
ATOM   16173 C  C   . TYR C 1 499  ? 55.935  73.455  59.492  1.00 168.43 ? 499  TYR B C   1 
ATOM   16174 O  O   . TYR C 1 499  ? 57.118  73.774  59.338  1.00 168.87 ? 499  TYR B O   1 
ATOM   16175 C  CB  . TYR C 1 499  ? 54.816  73.312  57.292  1.00 168.75 ? 499  TYR B CB  1 
ATOM   16176 C  CG  . TYR C 1 499  ? 53.650  73.752  56.484  1.00 168.23 ? 499  TYR B CG  1 
ATOM   16177 C  CD1 . TYR C 1 499  ? 52.352  73.424  56.860  1.00 165.34 ? 499  TYR B CD1 1 
ATOM   16178 C  CD2 . TYR C 1 499  ? 53.838  74.523  55.354  1.00 172.70 ? 499  TYR B CD2 1 
ATOM   16179 C  CE1 . TYR C 1 499  ? 51.268  73.844  56.107  1.00 165.82 ? 499  TYR B CE1 1 
ATOM   16180 C  CE2 . TYR C 1 499  ? 52.774  74.944  54.592  1.00 173.16 ? 499  TYR B CE2 1 
ATOM   16181 C  CZ  . TYR C 1 499  ? 51.488  74.604  54.967  1.00 169.70 ? 499  TYR B CZ  1 
ATOM   16182 O  OH  . TYR C 1 499  ? 50.433  75.042  54.191  1.00 169.28 ? 499  TYR B OH  1 
ATOM   16183 N  N   . ASN C 1 500  ? 55.488  72.610  60.428  1.00 187.86 ? 500  ASN B N   1 
ATOM   16184 C  CA  . ASN C 1 500  ? 56.355  71.920  61.388  1.00 185.03 ? 500  ASN B CA  1 
ATOM   16185 C  C   . ASN C 1 500  ? 56.162  70.386  61.411  1.00 174.58 ? 500  ASN B C   1 
ATOM   16186 O  O   . ASN C 1 500  ? 55.038  69.883  61.487  1.00 172.33 ? 500  ASN B O   1 
ATOM   16187 C  CB  . ASN C 1 500  ? 56.137  72.475  62.797  1.00 189.18 ? 500  ASN B CB  1 
ATOM   16188 C  CG  . ASN C 1 500  ? 55.803  73.958  62.808  1.00 195.69 ? 500  ASN B CG  1 
ATOM   16189 O  OD1 . ASN C 1 500  ? 56.145  74.706  61.880  1.00 199.44 ? 500  ASN B OD1 1 
ATOM   16190 N  ND2 . ASN C 1 500  ? 55.136  74.397  63.881  1.00 196.94 ? 500  ASN B ND2 1 
ATOM   16191 N  N   . TYR C 1 501  ? 57.260  69.640  61.359  1.00 175.67 ? 501  TYR B N   1 
ATOM   16192 C  CA  . TYR C 1 501  ? 57.139  68.197  61.327  1.00 168.61 ? 501  TYR B CA  1 
ATOM   16193 C  C   . TYR C 1 501  ? 57.851  67.461  62.439  1.00 167.63 ? 501  TYR B C   1 
ATOM   16194 O  O   . TYR C 1 501  ? 58.650  68.027  63.184  1.00 170.09 ? 501  TYR B O   1 
ATOM   16195 C  CB  . TYR C 1 501  ? 57.572  67.637  59.983  1.00 169.10 ? 501  TYR B CB  1 
ATOM   16196 C  CG  . TYR C 1 501  ? 59.054  67.742  59.642  1.00 174.67 ? 501  TYR B CG  1 
ATOM   16197 C  CD1 . TYR C 1 501  ? 59.951  66.744  60.014  1.00 174.40 ? 501  TYR B CD1 1 
ATOM   16198 C  CD2 . TYR C 1 501  ? 59.541  68.799  58.872  1.00 180.72 ? 501  TYR B CD2 1 
ATOM   16199 C  CE1 . TYR C 1 501  ? 61.300  66.815  59.662  1.00 178.52 ? 501  TYR B CE1 1 
ATOM   16200 C  CE2 . TYR C 1 501  ? 60.892  68.879  58.513  1.00 185.04 ? 501  TYR B CE2 1 
ATOM   16201 C  CZ  . TYR C 1 501  ? 61.763  67.884  58.913  1.00 184.10 ? 501  TYR B CZ  1 
ATOM   16202 O  OH  . TYR C 1 501  ? 63.094  67.950  58.566  1.00 187.94 ? 501  TYR B OH  1 
ATOM   16203 N  N   . LEU C 1 502  ? 57.552  66.171  62.517  1.00 147.25 ? 502  LEU B N   1 
ATOM   16204 C  CA  . LEU C 1 502  ? 57.992  65.336  63.611  1.00 144.12 ? 502  LEU B CA  1 
ATOM   16205 C  C   . LEU C 1 502  ? 58.022  63.900  63.144  1.00 140.69 ? 502  LEU B C   1 
ATOM   16206 O  O   . LEU C 1 502  ? 57.010  63.388  62.688  1.00 136.18 ? 502  LEU B O   1 
ATOM   16207 C  CB  . LEU C 1 502  ? 56.987  65.461  64.733  1.00 140.72 ? 502  LEU B CB  1 
ATOM   16208 C  CG  . LEU C 1 502  ? 57.573  65.637  66.122  1.00 139.70 ? 502  LEU B CG  1 
ATOM   16209 C  CD1 . LEU C 1 502  ? 58.951  66.297  66.061  1.00 140.88 ? 502  LEU B CD1 1 
ATOM   16210 C  CD2 . LEU C 1 502  ? 56.592  66.451  66.961  1.00 140.86 ? 502  LEU B CD2 1 
ATOM   16211 N  N   . ILE C 1 503  ? 59.169  63.244  63.279  1.00 147.45 ? 503  ILE B N   1 
ATOM   16212 C  CA  . ILE C 1 503  ? 59.330  61.882  62.775  1.00 144.40 ? 503  ILE B CA  1 
ATOM   16213 C  C   . ILE C 1 503  ? 59.898  60.919  63.811  1.00 143.54 ? 503  ILE B C   1 
ATOM   16214 O  O   . ILE C 1 503  ? 61.106  60.921  64.078  1.00 145.51 ? 503  ILE B O   1 
ATOM   16215 C  CB  . ILE C 1 503  ? 60.273  61.851  61.579  1.00 144.44 ? 503  ILE B CB  1 
ATOM   16216 C  CG1 . ILE C 1 503  ? 59.722  62.723  60.452  1.00 146.36 ? 503  ILE B CG1 1 
ATOM   16217 C  CG2 . ILE C 1 503  ? 60.476  60.416  61.109  1.00 140.04 ? 503  ILE B CG2 1 
ATOM   16218 C  CD1 . ILE C 1 503  ? 60.690  62.943  59.309  1.00 146.03 ? 503  ILE B CD1 1 
ATOM   16219 N  N   . LEU C 1 504  ? 59.005  60.102  64.375  1.00 142.97 ? 504  LEU B N   1 
ATOM   16220 C  CA  . LEU C 1 504  ? 59.314  59.102  65.404  1.00 142.70 ? 504  LEU B CA  1 
ATOM   16221 C  C   . LEU C 1 504  ? 59.536  57.769  64.725  1.00 143.74 ? 504  LEU B C   1 
ATOM   16222 O  O   . LEU C 1 504  ? 58.943  57.483  63.681  1.00 144.05 ? 504  LEU B O   1 
ATOM   16223 C  CB  . LEU C 1 504  ? 58.141  58.933  66.376  1.00 144.42 ? 504  LEU B CB  1 
ATOM   16224 C  CG  . LEU C 1 504  ? 57.809  59.949  67.466  1.00 144.80 ? 504  LEU B CG  1 
ATOM   16225 C  CD1 . LEU C 1 504  ? 57.964  61.338  66.979  1.00 147.56 ? 504  LEU B CD1 1 
ATOM   16226 C  CD2 . LEU C 1 504  ? 56.387  59.724  67.897  1.00 143.22 ? 504  LEU B CD2 1 
ATOM   16227 N  N   . SER C 1 505  ? 60.364  56.939  65.340  1.00 216.68 ? 505  SER B N   1 
ATOM   16228 C  CA  . SER C 1 505  ? 60.785  55.689  64.734  1.00 215.22 ? 505  SER B CA  1 
ATOM   16229 C  C   . SER C 1 505  ? 61.188  54.765  65.844  1.00 217.87 ? 505  SER B C   1 
ATOM   16230 O  O   . SER C 1 505  ? 62.168  55.028  66.539  1.00 219.00 ? 505  SER B O   1 
ATOM   16231 C  CB  . SER C 1 505  ? 62.005  55.926  63.854  1.00 215.50 ? 505  SER B CB  1 
ATOM   16232 O  OG  . SER C 1 505  ? 62.631  54.700  63.525  1.00 212.60 ? 505  SER B OG  1 
ATOM   16233 N  N   . LYS C 1 506  ? 60.463  53.670  66.002  1.00 161.28 ? 506  LYS B N   1 
ATOM   16234 C  CA  . LYS C 1 506  ? 60.700  52.827  67.151  1.00 162.52 ? 506  LYS B CA  1 
ATOM   16235 C  C   . LYS C 1 506  ? 60.441  53.644  68.396  1.00 168.10 ? 506  LYS B C   1 
ATOM   16236 O  O   . LYS C 1 506  ? 61.340  53.791  69.214  1.00 171.87 ? 506  LYS B O   1 
ATOM   16237 C  CB  . LYS C 1 506  ? 62.158  52.380  67.212  1.00 162.25 ? 506  LYS B CB  1 
ATOM   16238 C  CG  . LYS C 1 506  ? 62.673  51.720  65.961  1.00 157.28 ? 506  LYS B CG  1 
ATOM   16239 C  CD  . LYS C 1 506  ? 64.189  51.655  65.995  1.00 157.18 ? 506  LYS B CD  1 
ATOM   16240 C  CE  . LYS C 1 506  ? 64.812  53.015  65.773  1.00 159.80 ? 506  LYS B CE  1 
ATOM   16241 N  NZ  . LYS C 1 506  ? 64.631  53.468  64.377  1.00 158.13 ? 506  LYS B NZ  1 
ATOM   16242 N  N   . GLY C 1 507  ? 59.244  54.209  68.527  1.00 193.54 ? 507  GLY B N   1 
ATOM   16243 C  CA  . GLY C 1 507  ? 58.865  54.935  69.733  1.00 198.10 ? 507  GLY B CA  1 
ATOM   16244 C  C   . GLY C 1 507  ? 59.736  56.119  70.134  1.00 204.94 ? 507  GLY B C   1 
ATOM   16245 O  O   . GLY C 1 507  ? 59.593  56.645  71.245  1.00 207.10 ? 507  GLY B O   1 
ATOM   16246 N  N   . LYS C 1 508  ? 60.634  56.530  69.236  1.00 212.25 ? 508  LYS B N   1 
ATOM   16247 C  CA  . LYS C 1 508  ? 61.544  57.654  69.475  1.00 216.09 ? 508  LYS B CA  1 
ATOM   16248 C  C   . LYS C 1 508  ? 61.466  58.715  68.379  1.00 211.81 ? 508  LYS B C   1 
ATOM   16249 O  O   . LYS C 1 508  ? 61.668  58.422  67.200  1.00 208.69 ? 508  LYS B O   1 
ATOM   16250 C  CB  . LYS C 1 508  ? 62.992  57.161  69.556  1.00 218.24 ? 508  LYS B CB  1 
ATOM   16251 C  CG  . LYS C 1 508  ? 63.663  57.375  70.883  1.00 222.05 ? 508  LYS B CG  1 
ATOM   16252 C  CD  . LYS C 1 508  ? 65.065  56.833  70.839  1.00 222.25 ? 508  LYS B CD  1 
ATOM   16253 C  CE  . LYS C 1 508  ? 65.469  56.371  72.204  1.00 223.40 ? 508  LYS B CE  1 
ATOM   16254 N  NZ  . LYS C 1 508  ? 66.603  55.447  72.103  1.00 222.13 ? 508  LYS B NZ  1 
ATOM   16255 N  N   . ILE C 1 509  ? 61.188  59.954  68.765  1.00 166.95 ? 509  ILE B N   1 
ATOM   16256 C  CA  . ILE C 1 509  ? 61.328  61.045  67.824  1.00 164.11 ? 509  ILE B CA  1 
ATOM   16257 C  C   . ILE C 1 509  ? 62.788  61.059  67.402  1.00 162.64 ? 509  ILE B C   1 
ATOM   16258 O  O   . ILE C 1 509  ? 63.670  60.797  68.214  1.00 164.58 ? 509  ILE B O   1 
ATOM   16259 C  CB  . ILE C 1 509  ? 60.980  62.396  68.463  1.00 165.76 ? 509  ILE B CB  1 
ATOM   16260 C  CG1 . ILE C 1 509  ? 59.776  62.254  69.391  1.00 163.80 ? 509  ILE B CG1 1 
ATOM   16261 C  CG2 . ILE C 1 509  ? 60.720  63.448  67.391  1.00 168.37 ? 509  ILE B CG2 1 
ATOM   16262 C  CD1 . ILE C 1 509  ? 58.893  63.484  69.420  1.00 166.67 ? 509  ILE B CD1 1 
ATOM   16263 N  N   . ILE C 1 510  ? 63.049  61.350  66.134  1.00 168.48 ? 510  ILE B N   1 
ATOM   16264 C  CA  . ILE C 1 510  ? 64.419  61.430  65.653  1.00 169.17 ? 510  ILE B CA  1 
ATOM   16265 C  C   . ILE C 1 510  ? 64.586  62.568  64.665  1.00 172.55 ? 510  ILE B C   1 
ATOM   16266 O  O   . ILE C 1 510  ? 65.691  63.060  64.469  1.00 173.50 ? 510  ILE B O   1 
ATOM   16267 C  CB  . ILE C 1 510  ? 64.855  60.136  64.972  1.00 174.28 ? 510  ILE B CB  1 
ATOM   16268 C  CG1 . ILE C 1 510  ? 63.684  59.545  64.188  1.00 169.88 ? 510  ILE B CG1 1 
ATOM   16269 C  CG2 . ILE C 1 510  ? 65.397  59.143  65.994  1.00 173.35 ? 510  ILE B CG2 1 
ATOM   16270 C  CD1 . ILE C 1 510  ? 64.047  58.321  63.369  1.00 165.88 ? 510  ILE B CD1 1 
ATOM   16271 N  N   . HIS C 1 511  ? 63.493  62.990  64.042  1.00 187.54 ? 511  HIS B N   1 
ATOM   16272 C  CA  . HIS C 1 511  ? 63.567  64.131  63.151  1.00 195.23 ? 511  HIS B CA  1 
ATOM   16273 C  C   . HIS C 1 511  ? 62.442  65.100  63.400  1.00 199.01 ? 511  HIS B C   1 
ATOM   16274 O  O   . HIS C 1 511  ? 61.397  64.753  63.950  1.00 197.49 ? 511  HIS B O   1 
ATOM   16275 C  CB  . HIS C 1 511  ? 63.591  63.687  61.696  1.00 196.36 ? 511  HIS B CB  1 
ATOM   16276 C  CG  . HIS C 1 511  ? 64.700  62.734  61.389  1.00 196.73 ? 511  HIS B CG  1 
ATOM   16277 N  ND1 . HIS C 1 511  ? 65.933  63.142  60.924  1.00 200.45 ? 511  HIS B ND1 1 
ATOM   16278 C  CD2 . HIS C 1 511  ? 64.771  61.387  61.509  1.00 193.13 ? 511  HIS B CD2 1 
ATOM   16279 C  CE1 . HIS C 1 511  ? 66.711  62.088  60.759  1.00 197.76 ? 511  HIS B CE1 1 
ATOM   16280 N  NE2 . HIS C 1 511  ? 66.031  61.010  61.109  1.00 193.30 ? 511  HIS B NE2 1 
ATOM   16281 N  N   . PHE C 1 512  ? 62.684  66.333  62.992  1.00 185.54 ? 512  PHE B N   1 
ATOM   16282 C  CA  . PHE C 1 512  ? 61.746  67.414  63.190  1.00 190.64 ? 512  PHE B CA  1 
ATOM   16283 C  C   . PHE C 1 512  ? 62.410  68.643  62.600  1.00 193.09 ? 512  PHE B C   1 
ATOM   16284 O  O   . PHE C 1 512  ? 63.626  68.668  62.418  1.00 192.48 ? 512  PHE B O   1 
ATOM   16285 C  CB  . PHE C 1 512  ? 61.525  67.645  64.673  1.00 198.52 ? 512  PHE B CB  1 
ATOM   16286 C  CG  . PHE C 1 512  ? 62.686  68.294  65.337  1.00 207.53 ? 512  PHE B CG  1 
ATOM   16287 C  CD1 . PHE C 1 512  ? 62.556  69.524  65.955  1.00 213.54 ? 512  PHE B CD1 1 
ATOM   16288 C  CD2 . PHE C 1 512  ? 63.932  67.695  65.288  1.00 207.84 ? 512  PHE B CD2 1 
ATOM   16289 C  CE1 . PHE C 1 512  ? 63.648  70.126  66.546  1.00 218.63 ? 512  PHE B CE1 1 
ATOM   16290 C  CE2 . PHE C 1 512  ? 65.026  68.288  65.874  1.00 212.38 ? 512  PHE B CE2 1 
ATOM   16291 C  CZ  . PHE C 1 512  ? 64.886  69.506  66.505  1.00 217.58 ? 512  PHE B CZ  1 
ATOM   16292 N  N   . GLY C 1 513  ? 61.621  69.664  62.300  1.00 211.99 ? 513  GLY B N   1 
ATOM   16293 C  CA  . GLY C 1 513  ? 62.159  70.884  61.726  1.00 217.47 ? 513  GLY B CA  1 
ATOM   16294 C  C   . GLY C 1 513  ? 61.047  71.821  61.309  1.00 219.54 ? 513  GLY B C   1 
ATOM   16295 O  O   . GLY C 1 513  ? 59.922  71.705  61.792  1.00 216.44 ? 513  GLY B O   1 
ATOM   16296 N  N   . THR C 1 514  ? 61.351  72.757  60.416  1.00 208.69 ? 514  THR B N   1 
ATOM   16297 C  CA  . THR C 1 514  ? 60.306  73.605  59.848  1.00 212.04 ? 514  THR B CA  1 
ATOM   16298 C  C   . THR C 1 514  ? 60.603  74.103  58.441  1.00 212.04 ? 514  THR B C   1 
ATOM   16299 O  O   . THR C 1 514  ? 61.731  74.467  58.098  1.00 214.90 ? 514  THR B O   1 
ATOM   16300 C  CB  . THR C 1 514  ? 59.964  74.808  60.739  1.00 218.75 ? 514  THR B CB  1 
ATOM   16301 O  OG1 . THR C 1 514  ? 59.157  74.369  61.832  1.00 217.46 ? 514  THR B OG1 1 
ATOM   16302 C  CG2 . THR C 1 514  ? 59.176  75.840  59.949  1.00 223.25 ? 514  THR B CG2 1 
ATOM   16303 N  N   . ARG C 1 515  ? 59.558  74.108  57.631  1.00 205.85 ? 515  ARG B N   1 
ATOM   16304 C  CA  . ARG C 1 515  ? 59.632  74.666  56.313  1.00 211.13 ? 515  ARG B CA  1 
ATOM   16305 C  C   . ARG C 1 515  ? 58.726  75.878  56.332  1.00 213.30 ? 515  ARG B C   1 
ATOM   16306 O  O   . ARG C 1 515  ? 57.559  75.782  56.728  1.00 211.56 ? 515  ARG B O   1 
ATOM   16307 C  CB  . ARG C 1 515  ? 59.132  73.642  55.300  1.00 211.56 ? 515  ARG B CB  1 
ATOM   16308 C  CG  . ARG C 1 515  ? 59.718  72.246  55.476  1.00 211.80 ? 515  ARG B CG  1 
ATOM   16309 C  CD  . ARG C 1 515  ? 61.186  72.194  55.089  1.00 219.02 ? 515  ARG B CD  1 
ATOM   16310 N  NE  . ARG C 1 515  ? 61.645  70.817  54.920  1.00 218.94 ? 515  ARG B NE  1 
ATOM   16311 C  CZ  . ARG C 1 515  ? 61.492  70.104  53.802  1.00 220.51 ? 515  ARG B CZ  1 
ATOM   16312 N  NH1 . ARG C 1 515  ? 60.885  70.629  52.742  1.00 222.60 ? 515  ARG B NH1 1 
ATOM   16313 N  NH2 . ARG C 1 515  ? 61.943  68.857  53.740  1.00 218.59 ? 515  ARG B NH2 1 
ATOM   16314 N  N   . GLU C 1 516  ? 59.271  77.023  55.930  1.00 200.56 ? 516  GLU B N   1 
ATOM   16315 C  CA  . GLU C 1 516  ? 58.485  78.246  55.825  1.00 201.85 ? 516  GLU B CA  1 
ATOM   16316 C  C   . GLU C 1 516  ? 57.403  78.126  54.757  1.00 196.70 ? 516  GLU B C   1 
ATOM   16317 O  O   . GLU C 1 516  ? 57.655  77.666  53.640  1.00 192.41 ? 516  GLU B O   1 
ATOM   16318 C  CB  . GLU C 1 516  ? 59.384  79.454  55.543  1.00 209.82 ? 516  GLU B CB  1 
ATOM   16319 C  CG  . GLU C 1 516  ? 58.621  80.731  55.173  1.00 215.61 ? 516  GLU B CG  1 
ATOM   16320 C  CD  . GLU C 1 516  ? 59.185  81.977  55.841  1.00 223.22 ? 516  GLU B CD  1 
ATOM   16321 O  OE1 . GLU C 1 516  ? 58.993  83.087  55.280  1.00 227.68 ? 516  GLU B OE1 1 
ATOM   16322 O  OE2 . GLU C 1 516  ? 59.809  81.839  56.924  1.00 225.07 ? 516  GLU B OE2 1 
ATOM   16323 N  N   . LYS C 1 517  ? 56.198  78.552  55.112  1.00 183.29 ? 517  LYS B N   1 
ATOM   16324 C  CA  . LYS C 1 517  ? 55.049  78.418  54.234  1.00 182.04 ? 517  LYS B CA  1 
ATOM   16325 C  C   . LYS C 1 517  ? 55.119  79.286  52.981  1.00 191.87 ? 517  LYS B C   1 
ATOM   16326 O  O   . LYS C 1 517  ? 55.456  80.472  53.041  1.00 199.90 ? 517  LYS B O   1 
ATOM   16327 C  CB  . LYS C 1 517  ? 53.765  78.724  54.995  1.00 177.78 ? 517  LYS B CB  1 
ATOM   16328 C  CG  . LYS C 1 517  ? 52.550  78.133  54.326  1.00 171.04 ? 517  LYS B CG  1 
ATOM   16329 C  CD  . LYS C 1 517  ? 51.724  79.155  53.577  1.00 172.13 ? 517  LYS B CD  1 
ATOM   16330 C  CE  . LYS C 1 517  ? 50.568  78.466  52.861  1.00 166.03 ? 517  LYS B CE  1 
ATOM   16331 N  NZ  . LYS C 1 517  ? 49.264  79.124  53.151  1.00 167.41 ? 517  LYS B NZ  1 
ATOM   16332 N  N   . PHE C 1 518  ? 54.773  78.676  51.849  1.00 247.78 ? 518  PHE B N   1 
ATOM   16333 C  CA  . PHE C 1 518  ? 54.708  79.365  50.566  1.00 255.60 ? 518  PHE B CA  1 
ATOM   16334 C  C   . PHE C 1 518  ? 53.568  80.359  50.527  1.00 260.92 ? 518  PHE B C   1 
ATOM   16335 O  O   . PHE C 1 518  ? 52.419  80.008  50.251  1.00 255.34 ? 518  PHE B O   1 
ATOM   16336 C  CB  . PHE C 1 518  ? 54.580  78.356  49.433  1.00 255.06 ? 518  PHE B CB  1 
ATOM   16337 C  CG  . PHE C 1 518  ? 55.891  78.000  48.809  1.00 260.02 ? 518  PHE B CG  1 
ATOM   16338 C  CD1 . PHE C 1 518  ? 57.074  78.445  49.384  1.00 265.56 ? 518  PHE B CD1 1 
ATOM   16339 C  CD2 . PHE C 1 518  ? 55.949  77.233  47.648  1.00 259.12 ? 518  PHE B CD2 1 
ATOM   16340 C  CE1 . PHE C 1 518  ? 58.292  78.132  48.818  1.00 267.63 ? 518  PHE B CE1 1 
ATOM   16341 C  CE2 . PHE C 1 518  ? 57.168  76.912  47.068  1.00 261.27 ? 518  PHE B CE2 1 
ATOM   16342 C  CZ  . PHE C 1 518  ? 58.342  77.362  47.656  1.00 265.32 ? 518  PHE B CZ  1 
ATOM   16343 N  N   . SER C 1 519  ? 53.921  81.611  50.784  1.00 188.20 ? 519  SER B N   1 
ATOM   16344 C  CA  . SER C 1 519  ? 52.952  82.666  51.003  1.00 196.02 ? 519  SER B CA  1 
ATOM   16345 C  C   . SER C 1 519  ? 51.762  82.500  50.088  1.00 197.10 ? 519  SER B C   1 
ATOM   16346 O  O   . SER C 1 519  ? 50.721  81.999  50.500  1.00 197.50 ? 519  SER B O   1 
ATOM   16347 C  CB  . SER C 1 519  ? 53.605  84.027  50.777  1.00 202.61 ? 519  SER B CB  1 
ATOM   16348 O  OG  . SER C 1 519  ? 54.843  84.105  51.463  1.00 203.91 ? 519  SER B OG  1 
ATOM   16349 N  N   . ASP C 1 520  ? 51.937  82.904  48.838  1.00 289.28 ? 520  ASP B N   1 
ATOM   16350 C  CA  . ASP C 1 520  ? 50.855  82.910  47.868  1.00 290.58 ? 520  ASP B CA  1 
ATOM   16351 C  C   . ASP C 1 520  ? 50.019  81.643  47.911  1.00 281.43 ? 520  ASP B C   1 
ATOM   16352 O  O   . ASP C 1 520  ? 49.056  81.539  48.666  1.00 280.05 ? 520  ASP B O   1 
ATOM   16353 C  CB  . ASP C 1 520  ? 51.423  83.074  46.459  1.00 300.71 ? 520  ASP B CB  1 
ATOM   16354 C  CG  . ASP C 1 520  ? 52.490  82.040  46.139  1.00 308.63 ? 520  ASP B CG  1 
ATOM   16355 O  OD1 . ASP C 1 520  ? 52.972  81.377  47.085  1.00 309.47 ? 520  ASP B OD1 1 
ATOM   16356 O  OD2 . ASP C 1 520  ? 52.843  81.883  44.949  1.00 313.34 ? 520  ASP B OD2 1 
ATOM   16357 N  N   . ALA C 1 521  ? 50.406  80.679  47.087  1.00 267.63 ? 521  ALA B N   1 
ATOM   16358 C  CA  . ALA C 1 521  ? 49.583  79.515  46.816  1.00 255.20 ? 521  ALA B CA  1 
ATOM   16359 C  C   . ALA C 1 521  ? 49.334  78.639  48.029  1.00 239.00 ? 521  ALA B C   1 
ATOM   16360 O  O   . ALA C 1 521  ? 49.987  78.760  49.073  1.00 238.30 ? 521  ALA B O   1 
ATOM   16361 C  CB  . ALA C 1 521  ? 50.176  78.686  45.666  1.00 255.29 ? 521  ALA B CB  1 
ATOM   16362 N  N   . SER C 1 522  ? 48.367  77.750  47.842  1.00 246.16 ? 522  SER B N   1 
ATOM   16363 C  CA  . SER C 1 522  ? 47.937  76.787  48.836  1.00 234.56 ? 522  SER B CA  1 
ATOM   16364 C  C   . SER C 1 522  ? 49.105  75.982  49.369  1.00 226.91 ? 522  SER B C   1 
ATOM   16365 O  O   . SER C 1 522  ? 49.975  76.485  50.088  1.00 229.66 ? 522  SER B O   1 
ATOM   16366 C  CB  . SER C 1 522  ? 46.909  75.840  48.194  1.00 228.39 ? 522  SER B CB  1 
ATOM   16367 O  OG  . SER C 1 522  ? 46.556  74.762  49.043  1.00 223.75 ? 522  SER B OG  1 
ATOM   16368 N  N   . TYR C 1 523  ? 49.109  74.717  48.986  1.00 170.28 ? 523  TYR B N   1 
ATOM   16369 C  CA  . TYR C 1 523  ? 50.007  73.735  49.545  1.00 160.85 ? 523  TYR B CA  1 
ATOM   16370 C  C   . TYR C 1 523  ? 51.431  73.874  49.084  1.00 159.12 ? 523  TYR B C   1 
ATOM   16371 O  O   . TYR C 1 523  ? 51.825  74.866  48.470  1.00 160.57 ? 523  TYR B O   1 
ATOM   16372 C  CB  . TYR C 1 523  ? 49.527  72.359  49.147  1.00 155.04 ? 523  TYR B CB  1 
ATOM   16373 C  CG  . TYR C 1 523  ? 49.293  72.262  47.669  1.00 153.70 ? 523  TYR B CG  1 
ATOM   16374 C  CD1 . TYR C 1 523  ? 50.333  71.938  46.807  1.00 153.66 ? 523  TYR B CD1 1 
ATOM   16375 C  CD2 . TYR C 1 523  ? 48.034  72.508  47.130  1.00 151.51 ? 523  TYR B CD2 1 
ATOM   16376 C  CE1 . TYR C 1 523  ? 50.126  71.840  45.452  1.00 152.57 ? 523  TYR B CE1 1 
ATOM   16377 C  CE2 . TYR C 1 523  ? 47.814  72.412  45.782  1.00 149.68 ? 523  TYR B CE2 1 
ATOM   16378 C  CZ  . TYR C 1 523  ? 48.864  72.076  44.945  1.00 151.17 ? 523  TYR B CZ  1 
ATOM   16379 O  OH  . TYR C 1 523  ? 48.658  71.977  43.586  1.00 152.89 ? 523  TYR B OH  1 
ATOM   16380 N  N   . GLN C 1 524  ? 52.199  72.845  49.408  1.00 134.64 ? 524  GLN B N   1 
ATOM   16381 C  CA  . GLN C 1 524  ? 53.578  72.765  48.991  1.00 139.64 ? 524  GLN B CA  1 
ATOM   16382 C  C   . GLN C 1 524  ? 54.262  71.482  49.431  1.00 138.84 ? 524  GLN B C   1 
ATOM   16383 O  O   . GLN C 1 524  ? 53.762  70.722  50.264  1.00 135.61 ? 524  GLN B O   1 
ATOM   16384 C  CB  . GLN C 1 524  ? 54.368  73.948  49.516  1.00 145.37 ? 524  GLN B CB  1 
ATOM   16385 C  CG  . GLN C 1 524  ? 54.717  73.858  50.964  1.00 145.46 ? 524  GLN B CG  1 
ATOM   16386 C  CD  . GLN C 1 524  ? 54.575  75.201  51.614  1.00 152.43 ? 524  GLN B CD  1 
ATOM   16387 O  OE1 . GLN C 1 524  ? 53.534  75.843  51.484  1.00 153.89 ? 524  GLN B OE1 1 
ATOM   16388 N  NE2 . GLN C 1 524  ? 55.624  75.657  52.288  1.00 156.63 ? 524  GLN B NE2 1 
ATOM   16389 N  N   . SER C 1 525  ? 55.429  71.268  48.844  1.00 237.17 ? 525  SER B N   1 
ATOM   16390 C  CA  . SER C 1 525  ? 56.197  70.059  49.046  1.00 234.66 ? 525  SER B CA  1 
ATOM   16391 C  C   . SER C 1 525  ? 57.097  70.202  50.271  1.00 237.00 ? 525  SER B C   1 
ATOM   16392 O  O   . SER C 1 525  ? 57.619  71.283  50.555  1.00 239.40 ? 525  SER B O   1 
ATOM   16393 C  CB  . SER C 1 525  ? 57.026  69.768  47.789  1.00 238.67 ? 525  SER B CB  1 
ATOM   16394 O  OG  . SER C 1 525  ? 56.263  69.972  46.605  1.00 239.96 ? 525  SER B OG  1 
ATOM   16395 N  N   . ILE C 1 526  ? 57.257  69.107  51.003  1.00 179.00 ? 526  ILE B N   1 
ATOM   16396 C  CA  . ILE C 1 526  ? 58.257  69.032  52.053  1.00 176.78 ? 526  ILE B CA  1 
ATOM   16397 C  C   . ILE C 1 526  ? 59.149  67.845  51.753  1.00 172.85 ? 526  ILE B C   1 
ATOM   16398 O  O   . ILE C 1 526  ? 58.655  66.725  51.588  1.00 162.67 ? 526  ILE B O   1 
ATOM   16399 C  CB  . ILE C 1 526  ? 57.617  68.806  53.426  1.00 168.84 ? 526  ILE B CB  1 
ATOM   16400 C  CG1 . ILE C 1 526  ? 56.618  69.911  53.743  1.00 164.91 ? 526  ILE B CG1 1 
ATOM   16401 C  CG2 . ILE C 1 526  ? 58.677  68.765  54.494  1.00 170.72 ? 526  ILE B CG2 1 
ATOM   16402 C  CD1 . ILE C 1 526  ? 56.180  69.914  55.179  1.00 164.60 ? 526  ILE B CD1 1 
ATOM   16403 N  N   . ASN C 1 527  ? 60.457  68.062  51.681  1.00 208.07 ? 527  ASN B N   1 
ATOM   16404 C  CA  . ASN C 1 527  ? 61.307  66.940  51.321  1.00 211.92 ? 527  ASN B CA  1 
ATOM   16405 C  C   . ASN C 1 527  ? 62.337  66.435  52.312  1.00 216.28 ? 527  ASN B C   1 
ATOM   16406 O  O   . ASN C 1 527  ? 63.431  66.987  52.444  1.00 221.23 ? 527  ASN B O   1 
ATOM   16407 C  CB  . ASN C 1 527  ? 61.938  67.110  49.951  1.00 216.88 ? 527  ASN B CB  1 
ATOM   16408 C  CG  . ASN C 1 527  ? 62.152  65.778  49.272  1.00 215.92 ? 527  ASN B CG  1 
ATOM   16409 O  OD1 . ASN C 1 527  ? 62.672  64.841  49.885  1.00 213.72 ? 527  ASN B OD1 1 
ATOM   16410 N  ND2 . ASN C 1 527  ? 61.719  65.667  48.018  1.00 218.08 ? 527  ASN B ND2 1 
ATOM   16411 N  N   . ILE C 1 528  ? 61.967  65.329  52.950  1.00 166.34 ? 528  ILE B N   1 
ATOM   16412 C  CA  . ILE C 1 528  ? 62.795  64.664  53.940  1.00 167.96 ? 528  ILE B CA  1 
ATOM   16413 C  C   . ILE C 1 528  ? 63.418  63.385  53.391  1.00 167.63 ? 528  ILE B C   1 
ATOM   16414 O  O   . ILE C 1 528  ? 62.710  62.449  52.981  1.00 163.95 ? 528  ILE B O   1 
ATOM   16415 C  CB  . ILE C 1 528  ? 62.007  64.333  55.224  1.00 168.76 ? 528  ILE B CB  1 
ATOM   16416 C  CG1 . ILE C 1 528  ? 60.751  65.205  55.315  1.00 170.54 ? 528  ILE B CG1 1 
ATOM   16417 C  CG2 . ILE C 1 528  ? 62.906  64.479  56.463  1.00 170.53 ? 528  ILE B CG2 1 
ATOM   16418 C  CD1 . ILE C 1 528  ? 59.645  64.833  54.318  1.00 168.69 ? 528  ILE B CD1 1 
ATOM   16419 N  N   . PRO C 1 529  ? 64.762  63.367  53.362  1.00 209.37 ? 529  PRO B N   1 
ATOM   16420 C  CA  . PRO C 1 529  ? 65.629  62.213  53.128  1.00 209.65 ? 529  PRO B CA  1 
ATOM   16421 C  C   . PRO C 1 529  ? 65.323  61.136  54.141  1.00 205.66 ? 529  PRO B C   1 
ATOM   16422 O  O   . PRO C 1 529  ? 65.530  61.339  55.344  1.00 207.20 ? 529  PRO B O   1 
ATOM   16423 C  CB  . PRO C 1 529  ? 67.025  62.766  53.425  1.00 212.67 ? 529  PRO B CB  1 
ATOM   16424 C  CG  . PRO C 1 529  ? 66.928  64.193  53.082  1.00 217.38 ? 529  PRO B CG  1 
ATOM   16425 C  CD  . PRO C 1 529  ? 65.536  64.617  53.458  1.00 215.26 ? 529  PRO B CD  1 
ATOM   16426 N  N   . VAL C 1 530  ? 64.832  60.004  53.663  1.00 181.57 ? 530  VAL B N   1 
ATOM   16427 C  CA  . VAL C 1 530  ? 64.618  58.885  54.547  1.00 176.40 ? 530  VAL B CA  1 
ATOM   16428 C  C   . VAL C 1 530  ? 65.978  58.426  55.082  1.00 175.94 ? 530  VAL B C   1 
ATOM   16429 O  O   . VAL C 1 530  ? 66.906  58.145  54.327  1.00 176.64 ? 530  VAL B O   1 
ATOM   16430 C  CB  . VAL C 1 530  ? 63.854  57.761  53.841  1.00 148.99 ? 530  VAL B CB  1 
ATOM   16431 C  CG1 . VAL C 1 530  ? 64.766  56.972  52.936  1.00 148.50 ? 530  VAL B CG1 1 
ATOM   16432 C  CG2 . VAL C 1 530  ? 63.222  56.860  54.843  1.00 145.23 ? 530  VAL B CG2 1 
ATOM   16433 N  N   . THR C 1 531  ? 66.113  58.397  56.395  1.00 202.26 ? 531  THR B N   1 
ATOM   16434 C  CA  . THR C 1 531  ? 67.400  58.077  56.970  1.00 204.65 ? 531  THR B CA  1 
ATOM   16435 C  C   . THR C 1 531  ? 67.424  56.690  57.580  1.00 201.62 ? 531  THR B C   1 
ATOM   16436 O  O   . THR C 1 531  ? 66.421  56.201  58.109  1.00 197.75 ? 531  THR B O   1 
ATOM   16437 C  CB  . THR C 1 531  ? 67.816  59.098  58.039  1.00 208.62 ? 531  THR B CB  1 
ATOM   16438 O  OG1 . THR C 1 531  ? 69.232  59.017  58.243  1.00 210.73 ? 531  THR B OG1 1 
ATOM   16439 C  CG2 . THR C 1 531  ? 67.097  58.828  59.356  1.00 207.07 ? 531  THR B CG2 1 
ATOM   16440 N  N   . GLN C 1 532  ? 68.592  56.068  57.512  1.00 173.04 ? 532  GLN B N   1 
ATOM   16441 C  CA  . GLN C 1 532  ? 68.796  54.757  58.106  1.00 172.59 ? 532  GLN B CA  1 
ATOM   16442 C  C   . GLN C 1 532  ? 68.059  54.680  59.447  1.00 172.19 ? 532  GLN B C   1 
ATOM   16443 O  O   . GLN C 1 532  ? 67.464  53.661  59.780  1.00 170.10 ? 532  GLN B O   1 
ATOM   16444 C  CB  . GLN C 1 532  ? 70.303  54.498  58.257  1.00 175.89 ? 532  GLN B CB  1 
ATOM   16445 C  CG  . GLN C 1 532  ? 70.691  53.214  58.985  1.00 174.67 ? 532  GLN B CG  1 
ATOM   16446 C  CD  . GLN C 1 532  ? 70.370  51.950  58.208  1.00 170.79 ? 532  GLN B CD  1 
ATOM   16447 O  OE1 . GLN C 1 532  ? 69.759  51.993  57.145  1.00 170.78 ? 532  GLN B OE1 1 
ATOM   16448 N  NE2 . GLN C 1 532  ? 70.780  50.811  58.743  1.00 166.88 ? 532  GLN B NE2 1 
ATOM   16449 N  N   . ASN C 1 533  ? 68.047  55.791  60.178  1.00 192.42 ? 533  ASN B N   1 
ATOM   16450 C  CA  . ASN C 1 533  ? 67.516  55.815  61.535  1.00 191.79 ? 533  ASN B CA  1 
ATOM   16451 C  C   . ASN C 1 533  ? 66.040  55.508  61.632  1.00 187.47 ? 533  ASN B C   1 
ATOM   16452 O  O   . ASN C 1 533  ? 65.486  55.435  62.725  1.00 187.14 ? 533  ASN B O   1 
ATOM   16453 C  CB  . ASN C 1 533  ? 67.759  57.173  62.188  1.00 198.22 ? 533  ASN B CB  1 
ATOM   16454 C  CG  . ASN C 1 533  ? 69.220  57.472  62.385  1.00 204.68 ? 533  ASN B CG  1 
ATOM   16455 O  OD1 . ASN C 1 533  ? 69.745  58.413  61.792  1.00 209.99 ? 533  ASN B OD1 1 
ATOM   16456 N  ND2 . ASN C 1 533  ? 69.890  56.680  63.229  1.00 204.16 ? 533  ASN B ND2 1 
ATOM   16457 N  N   . MET C 1 534  ? 65.387  55.349  60.498  1.00 162.39 ? 534  MET B N   1 
ATOM   16458 C  CA  . MET C 1 534  ? 63.970  55.090  60.534  1.00 156.18 ? 534  MET B CA  1 
ATOM   16459 C  C   . MET C 1 534  ? 63.789  53.677  60.079  1.00 150.42 ? 534  MET B C   1 
ATOM   16460 O  O   . MET C 1 534  ? 62.684  53.227  59.797  1.00 146.39 ? 534  MET B O   1 
ATOM   16461 C  CB  . MET C 1 534  ? 63.297  56.049  59.599  1.00 156.38 ? 534  MET B CB  1 
ATOM   16462 C  CG  . MET C 1 534  ? 64.087  57.320  59.513  1.00 160.11 ? 534  MET B CG  1 
ATOM   16463 S  SD  . MET C 1 534  ? 63.736  58.291  58.045  1.00 158.33 ? 534  MET B SD  1 
ATOM   16464 C  CE  . MET C 1 534  ? 62.019  58.723  58.337  1.00 143.70 ? 534  MET B CE  1 
ATOM   16465 N  N   . VAL C 1 535  ? 64.911  52.974  60.049  1.00 161.96 ? 535  VAL B N   1 
ATOM   16466 C  CA  . VAL C 1 535  ? 65.017  51.699  59.359  1.00 158.82 ? 535  VAL B CA  1 
ATOM   16467 C  C   . VAL C 1 535  ? 63.777  50.803  59.392  1.00 155.01 ? 535  VAL B C   1 
ATOM   16468 O  O   . VAL C 1 535  ? 63.265  50.401  58.364  1.00 154.78 ? 535  VAL B O   1 
ATOM   16469 C  CB  . VAL C 1 535  ? 66.255  50.898  59.819  1.00 159.88 ? 535  VAL B CB  1 
ATOM   16470 C  CG1 . VAL C 1 535  ? 67.401  51.072  58.834  1.00 162.78 ? 535  VAL B CG1 1 
ATOM   16471 C  CG2 . VAL C 1 535  ? 66.661  51.311  61.236  1.00 165.49 ? 535  VAL B CG2 1 
ATOM   16472 N  N   . PRO C 1 536  ? 63.283  50.469  60.570  1.00 130.52 ? 536  PRO B N   1 
ATOM   16473 C  CA  . PRO C 1 536  ? 62.240  49.449  60.456  1.00 133.68 ? 536  PRO B CA  1 
ATOM   16474 C  C   . PRO C 1 536  ? 60.934  50.063  59.972  1.00 128.89 ? 536  PRO B C   1 
ATOM   16475 O  O   . PRO C 1 536  ? 60.410  49.679  58.936  1.00 127.38 ? 536  PRO B O   1 
ATOM   16476 C  CB  . PRO C 1 536  ? 62.121  48.929  61.894  1.00 135.95 ? 536  PRO B CB  1 
ATOM   16477 C  CG  . PRO C 1 536  ? 63.431  49.369  62.580  1.00 131.98 ? 536  PRO B CG  1 
ATOM   16478 C  CD  . PRO C 1 536  ? 63.727  50.680  61.957  1.00 133.82 ? 536  PRO B CD  1 
ATOM   16479 N  N   . SER C 1 537  ? 60.408  51.008  60.732  1.00 124.41 ? 537  SER B N   1 
ATOM   16480 C  CA  . SER C 1 537  ? 59.239  51.761  60.301  1.00 121.72 ? 537  SER B CA  1 
ATOM   16481 C  C   . SER C 1 537  ? 59.487  53.214  60.657  1.00 126.37 ? 537  SER B C   1 
ATOM   16482 O  O   . SER C 1 537  ? 60.639  53.658  60.769  1.00 130.26 ? 537  SER B O   1 
ATOM   16483 C  CB  . SER C 1 537  ? 57.932  51.241  60.918  1.00 122.34 ? 537  SER B CB  1 
ATOM   16484 O  OG  . SER C 1 537  ? 57.804  51.563  62.285  1.00 122.30 ? 537  SER B OG  1 
ATOM   16485 N  N   . SER C 1 538  ? 58.402  53.956  60.810  1.00 133.23 ? 538  SER B N   1 
ATOM   16486 C  CA  . SER C 1 538  ? 58.483  55.360  61.175  1.00 131.18 ? 538  SER B CA  1 
ATOM   16487 C  C   . SER C 1 538  ? 57.085  55.953  61.107  1.00 130.60 ? 538  SER B C   1 
ATOM   16488 O  O   . SER C 1 538  ? 56.202  55.409  60.433  1.00 128.35 ? 538  SER B O   1 
ATOM   16489 C  CB  . SER C 1 538  ? 59.440  56.136  60.249  1.00 132.37 ? 538  SER B CB  1 
ATOM   16490 O  OG  . SER C 1 538  ? 60.793  56.007  60.642  1.00 130.26 ? 538  SER B OG  1 
ATOM   16491 N  N   . ARG C 1 539  ? 56.873  57.041  61.839  1.00 132.04 ? 539  ARG B N   1 
ATOM   16492 C  CA  . ARG C 1 539  ? 55.747  57.898  61.554  1.00 132.07 ? 539  ARG B CA  1 
ATOM   16493 C  C   . ARG C 1 539  ? 56.213  59.306  61.662  1.00 136.33 ? 539  ARG B C   1 
ATOM   16494 O  O   . ARG C 1 539  ? 57.242  59.601  62.266  1.00 138.73 ? 539  ARG B O   1 
ATOM   16495 C  CB  . ARG C 1 539  ? 54.573  57.701  62.498  1.00 131.64 ? 539  ARG B CB  1 
ATOM   16496 C  CG  . ARG C 1 539  ? 54.680  56.559  63.466  1.00 130.11 ? 539  ARG B CG  1 
ATOM   16497 C  CD  . ARG C 1 539  ? 53.577  56.686  64.519  1.00 135.10 ? 539  ARG B CD  1 
ATOM   16498 N  NE  . ARG C 1 539  ? 52.242  56.438  63.980  1.00 129.72 ? 539  ARG B NE  1 
ATOM   16499 C  CZ  . ARG C 1 539  ? 51.642  55.254  64.028  1.00 129.39 ? 539  ARG B CZ  1 
ATOM   16500 N  NH1 . ARG C 1 539  ? 52.255  54.207  64.592  1.00 130.01 ? 539  ARG B NH1 1 
ATOM   16501 N  NH2 . ARG C 1 539  ? 50.430  55.120  63.508  1.00 130.81 ? 539  ARG B NH2 1 
ATOM   16502 N  N   . LEU C 1 540  ? 55.441  60.172  61.033  1.00 133.42 ? 540  LEU B N   1 
ATOM   16503 C  CA  . LEU C 1 540  ? 55.641  61.593  61.156  1.00 139.39 ? 540  LEU B CA  1 
ATOM   16504 C  C   . LEU C 1 540  ? 54.293  62.271  61.151  1.00 140.39 ? 540  LEU B C   1 
ATOM   16505 O  O   . LEU C 1 540  ? 53.286  61.684  60.747  1.00 134.60 ? 540  LEU B O   1 
ATOM   16506 C  CB  . LEU C 1 540  ? 56.502  62.140  60.028  1.00 144.79 ? 540  LEU B CB  1 
ATOM   16507 C  CG  . LEU C 1 540  ? 56.040  62.284  58.568  1.00 147.91 ? 540  LEU B CG  1 
ATOM   16508 C  CD1 . LEU C 1 540  ? 54.537  62.513  58.324  1.00 149.30 ? 540  LEU B CD1 1 
ATOM   16509 C  CD2 . LEU C 1 540  ? 56.863  63.420  57.988  1.00 152.29 ? 540  LEU B CD2 1 
ATOM   16510 N  N   . LEU C 1 541  ? 54.292  63.517  61.596  1.00 146.43 ? 541  LEU B N   1 
ATOM   16511 C  CA  . LEU C 1 541  ? 53.082  64.291  61.696  1.00 148.41 ? 541  LEU B CA  1 
ATOM   16512 C  C   . LEU C 1 541  ? 53.486  65.736  61.546  1.00 157.30 ? 541  LEU B C   1 
ATOM   16513 O  O   . LEU C 1 541  ? 54.657  66.092  61.705  1.00 159.41 ? 541  LEU B O   1 
ATOM   16514 C  CB  . LEU C 1 541  ? 52.405  64.029  63.033  1.00 146.41 ? 541  LEU B CB  1 
ATOM   16515 C  CG  . LEU C 1 541  ? 52.055  65.121  64.036  1.00 153.19 ? 541  LEU B CG  1 
ATOM   16516 C  CD1 . LEU C 1 541  ? 51.165  64.511  65.133  1.00 148.81 ? 541  LEU B CD1 1 
ATOM   16517 C  CD2 . LEU C 1 541  ? 53.311  65.762  64.627  1.00 156.72 ? 541  LEU B CD2 1 
ATOM   16518 N  N   . VAL C 1 542  ? 52.524  66.581  61.236  1.00 146.49 ? 542  VAL B N   1 
ATOM   16519 C  CA  . VAL C 1 542  ? 52.868  67.912  60.813  1.00 153.95 ? 542  VAL B CA  1 
ATOM   16520 C  C   . VAL C 1 542  ? 51.781  68.850  61.256  1.00 162.13 ? 542  VAL B C   1 
ATOM   16521 O  O   . VAL C 1 542  ? 50.638  68.708  60.838  1.00 160.32 ? 542  VAL B O   1 
ATOM   16522 C  CB  . VAL C 1 542  ? 52.978  67.953  59.301  1.00 151.34 ? 542  VAL B CB  1 
ATOM   16523 C  CG1 . VAL C 1 542  ? 52.790  69.367  58.805  1.00 154.66 ? 542  VAL B CG1 1 
ATOM   16524 C  CG2 . VAL C 1 542  ? 54.305  67.364  58.863  1.00 150.17 ? 542  VAL B CG2 1 
ATOM   16525 N  N   . TYR C 1 543  ? 52.139  69.808  62.103  1.00 175.04 ? 543  TYR B N   1 
ATOM   16526 C  CA  . TYR C 1 543  ? 51.173  70.760  62.624  1.00 181.99 ? 543  TYR B CA  1 
ATOM   16527 C  C   . TYR C 1 543  ? 51.507  72.175  62.209  1.00 188.27 ? 543  TYR B C   1 
ATOM   16528 O  O   . TYR C 1 543  ? 52.680  72.539  62.127  1.00 190.47 ? 543  TYR B O   1 
ATOM   16529 C  CB  . TYR C 1 543  ? 51.123  70.687  64.145  1.00 185.14 ? 543  TYR B CB  1 
ATOM   16530 C  CG  . TYR C 1 543  ? 52.433  71.037  64.840  1.00 189.80 ? 543  TYR B CG  1 
ATOM   16531 C  CD1 . TYR C 1 543  ? 53.388  70.059  65.100  1.00 188.93 ? 543  TYR B CD1 1 
ATOM   16532 C  CD2 . TYR C 1 543  ? 52.705  72.341  65.259  1.00 195.22 ? 543  TYR B CD2 1 
ATOM   16533 C  CE1 . TYR C 1 543  ? 54.578  70.366  65.747  1.00 191.74 ? 543  TYR B CE1 1 
ATOM   16534 C  CE2 . TYR C 1 543  ? 53.897  72.655  65.904  1.00 197.87 ? 543  TYR B CE2 1 
ATOM   16535 C  CZ  . TYR C 1 543  ? 54.827  71.660  66.142  1.00 195.06 ? 543  TYR B CZ  1 
ATOM   16536 O  OH  . TYR C 1 543  ? 56.012  71.940  66.771  1.00 195.53 ? 543  TYR B OH  1 
ATOM   16537 N  N   . TYR C 1 544  ? 50.472  72.967  61.941  1.00 204.36 ? 544  TYR B N   1 
ATOM   16538 C  CA  . TYR C 1 544  ? 50.631  74.410  61.764  1.00 210.69 ? 544  TYR B CA  1 
ATOM   16539 C  C   . TYR C 1 544  ? 49.861  75.137  62.858  1.00 213.92 ? 544  TYR B C   1 
ATOM   16540 O  O   . TYR C 1 544  ? 48.716  74.786  63.154  1.00 212.43 ? 544  TYR B O   1 
ATOM   16541 C  CB  . TYR C 1 544  ? 50.146  74.864  60.392  1.00 211.37 ? 544  TYR B CB  1 
ATOM   16542 C  CG  . TYR C 1 544  ? 48.691  74.577  60.135  1.00 209.26 ? 544  TYR B CG  1 
ATOM   16543 C  CD1 . TYR C 1 544  ? 48.182  73.302  60.298  1.00 203.88 ? 544  TYR B CD1 1 
ATOM   16544 C  CD2 . TYR C 1 544  ? 47.829  75.576  59.707  1.00 211.27 ? 544  TYR B CD2 1 
ATOM   16545 C  CE1 . TYR C 1 544  ? 46.866  73.030  60.049  1.00 202.02 ? 544  TYR B CE1 1 
ATOM   16546 C  CE2 . TYR C 1 544  ? 46.501  75.308  59.456  1.00 208.91 ? 544  TYR B CE2 1 
ATOM   16547 C  CZ  . TYR C 1 544  ? 46.028  74.031  59.632  1.00 204.66 ? 544  TYR B CZ  1 
ATOM   16548 O  OH  . TYR C 1 544  ? 44.716  73.733  59.385  1.00 203.05 ? 544  TYR B OH  1 
ATOM   16549 N  N   . ILE C 1 545  ? 50.504  76.147  63.448  1.00 177.21 ? 545  ILE B N   1 
ATOM   16550 C  CA  . ILE C 1 545  ? 49.981  76.865  64.609  1.00 179.65 ? 545  ILE B CA  1 
ATOM   16551 C  C   . ILE C 1 545  ? 49.047  78.018  64.197  1.00 183.97 ? 545  ILE B C   1 
ATOM   16552 O  O   . ILE C 1 545  ? 49.508  79.109  63.843  1.00 185.95 ? 545  ILE B O   1 
ATOM   16553 C  CB  . ILE C 1 545  ? 51.145  77.390  65.478  1.00 179.10 ? 545  ILE B CB  1 
ATOM   16554 C  CG1 . ILE C 1 545  ? 52.240  76.322  65.606  1.00 173.66 ? 545  ILE B CG1 1 
ATOM   16555 C  CG2 . ILE C 1 545  ? 50.639  77.809  66.837  1.00 184.13 ? 545  ILE B CG2 1 
ATOM   16556 C  CD1 . ILE C 1 545  ? 53.549  76.823  66.187  1.00 166.57 ? 545  ILE B CD1 1 
ATOM   16557 N  N   . VAL C 1 546  ? 47.739  77.754  64.255  1.00 198.09 ? 546  VAL B N   1 
ATOM   16558 C  CA  . VAL C 1 546  ? 46.692  78.663  63.764  1.00 206.17 ? 546  VAL B CA  1 
ATOM   16559 C  C   . VAL C 1 546  ? 46.205  79.700  64.771  1.00 222.53 ? 546  VAL B C   1 
ATOM   16560 O  O   . VAL C 1 546  ? 45.682  79.356  65.833  1.00 223.57 ? 546  VAL B O   1 
ATOM   16561 C  CB  . VAL C 1 546  ? 45.442  77.881  63.289  1.00 196.08 ? 546  VAL B CB  1 
ATOM   16562 C  CG1 . VAL C 1 546  ? 44.184  78.738  63.434  1.00 197.76 ? 546  VAL B CG1 1 
ATOM   16563 C  CG2 . VAL C 1 546  ? 45.617  77.395  61.860  1.00 191.26 ? 546  VAL B CG2 1 
ATOM   16564 N  N   . THR C 1 547  ? 46.349  80.971  64.409  1.00 215.78 ? 547  THR B N   1 
ATOM   16565 C  CA  . THR C 1 547  ? 45.856  82.071  65.232  1.00 234.54 ? 547  THR B CA  1 
ATOM   16566 C  C   . THR C 1 547  ? 44.412  82.448  64.903  1.00 250.00 ? 547  THR B C   1 
ATOM   16567 O  O   . THR C 1 547  ? 44.156  83.451  64.231  1.00 254.70 ? 547  THR B O   1 
ATOM   16568 C  CB  . THR C 1 547  ? 46.744  83.319  65.093  1.00 239.54 ? 547  THR B CB  1 
ATOM   16569 O  OG1 . THR C 1 547  ? 48.056  83.021  65.579  1.00 237.88 ? 547  THR B OG1 1 
ATOM   16570 C  CG2 . THR C 1 547  ? 46.177  84.477  65.893  1.00 246.26 ? 547  THR B CG2 1 
ATOM   16571 N  N   . GLY C 1 548  ? 43.471  81.632  65.367  1.00 334.44 ? 548  GLY B N   1 
ATOM   16572 C  CA  . GLY C 1 548  ? 42.075  82.023  65.365  1.00 350.17 ? 548  GLY B CA  1 
ATOM   16573 C  C   . GLY C 1 548  ? 41.951  83.207  66.303  1.00 372.48 ? 548  GLY B C   1 
ATOM   16574 O  O   . GLY C 1 548  ? 42.663  83.281  67.306  1.00 377.17 ? 548  GLY B O   1 
ATOM   16575 N  N   . GLU C 1 549  ? 41.062  84.142  65.985  1.00 371.52 ? 549  GLU B N   1 
ATOM   16576 C  CA  . GLU C 1 549  ? 40.949  85.356  66.785  1.00 388.96 ? 549  GLU B CA  1 
ATOM   16577 C  C   . GLU C 1 549  ? 40.605  85.016  68.225  1.00 391.10 ? 549  GLU B C   1 
ATOM   16578 O  O   . GLU C 1 549  ? 40.943  85.760  69.143  1.00 393.39 ? 549  GLU B O   1 
ATOM   16579 C  CB  . GLU C 1 549  ? 39.910  86.324  66.205  1.00 398.35 ? 549  GLU B CB  1 
ATOM   16580 C  CG  . GLU C 1 549  ? 38.470  85.856  66.321  1.00 402.34 ? 549  GLU B CG  1 
ATOM   16581 C  CD  . GLU C 1 549  ? 38.105  84.835  65.265  1.00 403.39 ? 549  GLU B CD  1 
ATOM   16582 O  OE1 . GLU C 1 549  ? 38.902  84.643  64.323  1.00 403.93 ? 549  GLU B OE1 1 
ATOM   16583 O  OE2 . GLU C 1 549  ? 37.018  84.229  65.372  1.00 403.50 ? 549  GLU B OE2 1 
ATOM   16584 N  N   . GLN C 1 550  ? 39.942  83.883  68.420  1.00 350.83 ? 550  GLN B N   1 
ATOM   16585 C  CA  . GLN C 1 550  ? 39.484  83.507  69.751  1.00 349.83 ? 550  GLN B CA  1 
ATOM   16586 C  C   . GLN C 1 550  ? 40.556  82.833  70.600  1.00 340.21 ? 550  GLN B C   1 
ATOM   16587 O  O   . GLN C 1 550  ? 40.642  83.084  71.800  1.00 345.96 ? 550  GLN B O   1 
ATOM   16588 C  CB  . GLN C 1 550  ? 38.239  82.618  69.682  1.00 350.11 ? 550  GLN B CB  1 
ATOM   16589 C  CG  . GLN C 1 550  ? 38.460  81.266  69.035  1.00 344.48 ? 550  GLN B CG  1 
ATOM   16590 C  CD  . GLN C 1 550  ? 38.210  81.293  67.546  1.00 342.00 ? 550  GLN B CD  1 
ATOM   16591 O  OE1 . GLN C 1 550  ? 37.792  82.310  66.996  1.00 345.94 ? 550  GLN B OE1 1 
ATOM   16592 N  NE2 . GLN C 1 550  ? 38.460  80.172  66.882  1.00 334.98 ? 550  GLN B NE2 1 
ATOM   16593 N  N   . THR C 1 551  ? 41.376  81.987  69.986  1.00 319.75 ? 551  THR B N   1 
ATOM   16594 C  CA  . THR C 1 551  ? 42.324  81.191  70.754  1.00 308.55 ? 551  THR B CA  1 
ATOM   16595 C  C   . THR C 1 551  ? 43.403  80.541  69.901  1.00 291.12 ? 551  THR B C   1 
ATOM   16596 O  O   . THR C 1 551  ? 43.165  80.182  68.751  1.00 286.15 ? 551  THR B O   1 
ATOM   16597 C  CB  . THR C 1 551  ? 41.596  80.078  71.522  1.00 307.99 ? 551  THR B CB  1 
ATOM   16598 O  OG1 . THR C 1 551  ? 40.684  80.655  72.465  1.00 315.55 ? 551  THR B OG1 1 
ATOM   16599 C  CG2 . THR C 1 551  ? 42.594  79.196  72.256  1.00 305.99 ? 551  THR B CG2 1 
ATOM   16600 N  N   . ALA C 1 552  ? 44.589  80.387  70.484  1.00 269.82 ? 552  ALA B N   1 
ATOM   16601 C  CA  . ALA C 1 552  ? 45.690  79.701  69.823  1.00 253.31 ? 552  ALA B CA  1 
ATOM   16602 C  C   . ALA C 1 552  ? 45.299  78.256  69.499  1.00 234.33 ? 552  ALA B C   1 
ATOM   16603 O  O   . ALA C 1 552  ? 45.108  77.453  70.416  1.00 232.18 ? 552  ALA B O   1 
ATOM   16604 C  CB  . ALA C 1 552  ? 46.934  79.737  70.709  1.00 255.37 ? 552  ALA B CB  1 
ATOM   16605 N  N   . GLU C 1 553  ? 45.184  77.933  68.202  1.00 240.88 ? 553  GLU B N   1 
ATOM   16606 C  CA  . GLU C 1 553  ? 44.806  76.579  67.749  1.00 222.89 ? 553  GLU B CA  1 
ATOM   16607 C  C   . GLU C 1 553  ? 45.891  75.816  66.980  1.00 210.79 ? 553  GLU B C   1 
ATOM   16608 O  O   . GLU C 1 553  ? 46.258  76.175  65.864  1.00 208.32 ? 553  GLU B O   1 
ATOM   16609 C  CB  . GLU C 1 553  ? 43.516  76.595  66.911  1.00 215.92 ? 553  GLU B CB  1 
ATOM   16610 C  CG  . GLU C 1 553  ? 42.596  75.412  67.209  1.00 209.84 ? 553  GLU B CG  1 
ATOM   16611 C  CD  . GLU C 1 553  ? 41.996  74.783  65.973  1.00 202.44 ? 553  GLU B CD  1 
ATOM   16612 O  OE1 . GLU C 1 553  ? 42.760  74.448  65.053  1.00 199.06 ? 553  GLU B OE1 1 
ATOM   16613 O  OE2 . GLU C 1 553  ? 40.762  74.605  65.929  1.00 200.61 ? 553  GLU B OE2 1 
ATOM   16614 N  N   . LEU C 1 554  ? 46.395  74.754  67.594  1.00 203.08 ? 554  LEU B N   1 
ATOM   16615 C  CA  . LEU C 1 554  ? 47.254  73.817  66.896  1.00 195.22 ? 554  LEU B CA  1 
ATOM   16616 C  C   . LEU C 1 554  ? 46.379  72.956  65.993  1.00 188.26 ? 554  LEU B C   1 
ATOM   16617 O  O   . LEU C 1 554  ? 45.196  72.754  66.265  1.00 188.01 ? 554  LEU B O   1 
ATOM   16618 C  CB  . LEU C 1 554  ? 48.038  72.936  67.886  1.00 194.34 ? 554  LEU B CB  1 
ATOM   16619 C  CG  . LEU C 1 554  ? 49.461  73.347  68.287  1.00 198.76 ? 554  LEU B CG  1 
ATOM   16620 C  CD1 . LEU C 1 554  ? 50.254  72.193  68.939  1.00 195.75 ? 554  LEU B CD1 1 
ATOM   16621 C  CD2 . LEU C 1 554  ? 50.210  73.906  67.074  1.00 200.35 ? 554  LEU B CD2 1 
ATOM   16622 N  N   . VAL C 1 555  ? 46.966  72.456  64.915  1.00 255.56 ? 555  VAL B N   1 
ATOM   16623 C  CA  . VAL C 1 555  ? 46.275  71.541  64.024  1.00 248.84 ? 555  VAL B CA  1 
ATOM   16624 C  C   . VAL C 1 555  ? 47.296  70.685  63.302  1.00 240.39 ? 555  VAL B C   1 
ATOM   16625 O  O   . VAL C 1 555  ? 48.354  71.177  62.912  1.00 240.53 ? 555  VAL B O   1 
ATOM   16626 C  CB  . VAL C 1 555  ? 45.408  72.290  62.990  1.00 251.62 ? 555  VAL B CB  1 
ATOM   16627 C  CG1 . VAL C 1 555  ? 45.095  71.399  61.815  1.00 247.85 ? 555  VAL B CG1 1 
ATOM   16628 C  CG2 . VAL C 1 555  ? 44.124  72.758  63.621  1.00 254.32 ? 555  VAL B CG2 1 
ATOM   16629 N  N   . SER C 1 556  ? 46.987  69.402  63.132  1.00 168.76 ? 556  SER B N   1 
ATOM   16630 C  CA  . SER C 1 556  ? 47.860  68.557  62.336  1.00 164.30 ? 556  SER B CA  1 
ATOM   16631 C  C   . SER C 1 556  ? 47.272  67.265  61.775  1.00 160.85 ? 556  SER B C   1 
ATOM   16632 O  O   . SER C 1 556  ? 46.072  66.973  61.871  1.00 162.70 ? 556  SER B O   1 
ATOM   16633 C  CB  . SER C 1 556  ? 49.121  68.216  63.126  1.00 163.23 ? 556  SER B CB  1 
ATOM   16634 O  OG  . SER C 1 556  ? 49.028  66.906  63.637  1.00 160.26 ? 556  SER B OG  1 
ATOM   16635 N  N   . ASP C 1 557  ? 48.175  66.517  61.159  1.00 187.15 ? 557  ASP B N   1 
ATOM   16636 C  CA  . ASP C 1 557  ? 47.916  65.159  60.752  1.00 176.55 ? 557  ASP B CA  1 
ATOM   16637 C  C   . ASP C 1 557  ? 49.244  64.411  60.644  1.00 170.31 ? 557  ASP B C   1 
ATOM   16638 O  O   . ASP C 1 557  ? 50.321  64.999  60.779  1.00 169.90 ? 557  ASP B O   1 
ATOM   16639 C  CB  . ASP C 1 557  ? 47.135  65.113  59.439  1.00 176.22 ? 557  ASP B CB  1 
ATOM   16640 C  CG  . ASP C 1 557  ? 46.683  63.706  59.078  1.00 173.18 ? 557  ASP B CG  1 
ATOM   16641 O  OD1 . ASP C 1 557  ? 46.550  62.881  60.002  1.00 172.99 ? 557  ASP B OD1 1 
ATOM   16642 O  OD2 . ASP C 1 557  ? 46.462  63.431  57.876  1.00 170.56 ? 557  ASP B OD2 1 
ATOM   16643 N  N   . SER C 1 558  ? 49.155  63.108  60.411  1.00 138.87 ? 558  SER B N   1 
ATOM   16644 C  CA  . SER C 1 558  ? 50.316  62.238  60.434  1.00 137.93 ? 558  SER B CA  1 
ATOM   16645 C  C   . SER C 1 558  ? 50.053  60.992  59.612  1.00 133.28 ? 558  SER B C   1 
ATOM   16646 O  O   . SER C 1 558  ? 48.901  60.674  59.308  1.00 130.28 ? 558  SER B O   1 
ATOM   16647 C  CB  . SER C 1 558  ? 50.577  61.789  61.857  1.00 139.35 ? 558  SER B CB  1 
ATOM   16648 O  OG  . SER C 1 558  ? 49.518  60.973  62.321  1.00 137.73 ? 558  SER B OG  1 
ATOM   16649 N  N   . VAL C 1 559  ? 51.118  60.264  59.285  1.00 188.72 ? 559  VAL B N   1 
ATOM   16650 C  CA  . VAL C 1 559  ? 50.991  59.023  58.531  1.00 183.36 ? 559  VAL B CA  1 
ATOM   16651 C  C   . VAL C 1 559  ? 51.950  57.961  59.031  1.00 184.46 ? 559  VAL B C   1 
ATOM   16652 O  O   . VAL C 1 559  ? 53.012  58.272  59.573  1.00 189.90 ? 559  VAL B O   1 
ATOM   16653 C  CB  . VAL C 1 559  ? 51.298  59.257  57.061  1.00 177.30 ? 559  VAL B CB  1 
ATOM   16654 C  CG1 . VAL C 1 559  ? 50.110  59.928  56.374  1.00 173.43 ? 559  VAL B CG1 1 
ATOM   16655 C  CG2 . VAL C 1 559  ? 52.554  60.097  56.942  1.00 175.34 ? 559  VAL B CG2 1 
ATOM   16656 N  N   . TRP C 1 560  ? 51.576  56.702  58.853  1.00 186.02 ? 560  TRP B N   1 
ATOM   16657 C  CA  . TRP C 1 560  ? 52.491  55.627  59.187  1.00 184.27 ? 560  TRP B CA  1 
ATOM   16658 C  C   . TRP C 1 560  ? 53.335  55.324  57.955  1.00 179.76 ? 560  TRP B C   1 
ATOM   16659 O  O   . TRP C 1 560  ? 52.873  55.541  56.833  1.00 179.37 ? 560  TRP B O   1 
ATOM   16660 C  CB  . TRP C 1 560  ? 51.743  54.400  59.705  1.00 187.73 ? 560  TRP B CB  1 
ATOM   16661 C  CG  . TRP C 1 560  ? 52.678  53.337  60.119  1.00 192.62 ? 560  TRP B CG  1 
ATOM   16662 C  CD1 . TRP C 1 560  ? 53.335  53.231  61.306  1.00 197.66 ? 560  TRP B CD1 1 
ATOM   16663 C  CD2 . TRP C 1 560  ? 53.099  52.236  59.327  1.00 192.64 ? 560  TRP B CD2 1 
ATOM   16664 N  NE1 . TRP C 1 560  ? 54.139  52.120  61.304  1.00 197.08 ? 560  TRP B NE1 1 
ATOM   16665 C  CE2 . TRP C 1 560  ? 54.014  51.492  60.095  1.00 193.49 ? 560  TRP B CE2 1 
ATOM   16666 C  CE3 . TRP C 1 560  ? 52.789  51.806  58.037  1.00 192.67 ? 560  TRP B CE3 1 
ATOM   16667 C  CZ2 . TRP C 1 560  ? 54.619  50.332  59.617  1.00 191.86 ? 560  TRP B CZ2 1 
ATOM   16668 C  CZ3 . TRP C 1 560  ? 53.385  50.655  57.562  1.00 191.68 ? 560  TRP B CZ3 1 
ATOM   16669 C  CH2 . TRP C 1 560  ? 54.289  49.927  58.351  1.00 190.49 ? 560  TRP B CH2 1 
ATOM   16670 N  N   . LEU C 1 561  ? 54.560  54.836  58.155  1.00 113.15 ? 561  LEU B N   1 
ATOM   16671 C  CA  . LEU C 1 561  ? 55.544  54.830  57.062  1.00 110.90 ? 561  LEU B CA  1 
ATOM   16672 C  C   . LEU C 1 561  ? 56.424  53.596  56.863  1.00 108.54 ? 561  LEU B C   1 
ATOM   16673 O  O   . LEU C 1 561  ? 57.654  53.726  56.914  1.00 107.86 ? 561  LEU B O   1 
ATOM   16674 C  CB  . LEU C 1 561  ? 56.513  55.988  57.218  1.00 111.75 ? 561  LEU B CB  1 
ATOM   16675 C  CG  . LEU C 1 561  ? 56.102  57.431  57.048  1.00 113.63 ? 561  LEU B CG  1 
ATOM   16676 C  CD1 . LEU C 1 561  ? 57.374  58.264  57.207  1.00 113.95 ? 561  LEU B CD1 1 
ATOM   16677 C  CD2 . LEU C 1 561  ? 55.416  57.674  55.696  1.00 112.73 ? 561  LEU B CD2 1 
ATOM   16678 N  N   . ASN C 1 562  ? 55.841  52.431  56.582  1.00 144.51 ? 562  ASN B N   1 
ATOM   16679 C  CA  . ASN C 1 562  ? 56.657  51.222  56.440  1.00 143.50 ? 562  ASN B CA  1 
ATOM   16680 C  C   . ASN C 1 562  ? 57.808  51.450  55.519  1.00 133.60 ? 562  ASN B C   1 
ATOM   16681 O  O   . ASN C 1 562  ? 57.671  52.090  54.490  1.00 134.96 ? 562  ASN B O   1 
ATOM   16682 C  CB  . ASN C 1 562  ? 55.877  50.064  55.844  1.00 136.75 ? 562  ASN B CB  1 
ATOM   16683 C  CG  . ASN C 1 562  ? 56.636  48.748  55.943  1.00 149.20 ? 562  ASN B CG  1 
ATOM   16684 O  OD1 . ASN C 1 562  ? 57.828  48.679  55.631  1.00 148.75 ? 562  ASN B OD1 1 
ATOM   16685 N  ND2 . ASN C 1 562  ? 55.943  47.695  56.383  1.00 147.25 ? 562  ASN B ND2 1 
ATOM   16686 N  N   . ILE C 1 563  ? 58.958  50.922  55.873  1.00 146.87 ? 563  ILE B N   1 
ATOM   16687 C  CA  . ILE C 1 563  ? 60.022  51.044  54.933  1.00 148.63 ? 563  ILE B CA  1 
ATOM   16688 C  C   . ILE C 1 563  ? 60.869  49.783  54.788  1.00 150.95 ? 563  ILE B C   1 
ATOM   16689 O  O   . ILE C 1 563  ? 60.526  48.714  55.311  1.00 149.49 ? 563  ILE B O   1 
ATOM   16690 C  CB  . ILE C 1 563  ? 60.817  52.315  55.179  1.00 150.27 ? 563  ILE B CB  1 
ATOM   16691 C  CG1 . ILE C 1 563  ? 62.049  52.035  55.993  1.00 152.01 ? 563  ILE B CG1 1 
ATOM   16692 C  CG2 . ILE C 1 563  ? 59.986  53.336  55.912  1.00 148.82 ? 563  ILE B CG2 1 
ATOM   16693 C  CD1 . ILE C 1 563  ? 62.995  53.192  55.956  1.00 156.87 ? 563  ILE B CD1 1 
ATOM   16694 N  N   . GLU C 1 564  ? 61.965  49.917  54.051  1.00 157.23 ? 564  GLU B N   1 
ATOM   16695 C  CA  . GLU C 1 564  ? 62.809  48.780  53.730  1.00 158.61 ? 564  GLU B CA  1 
ATOM   16696 C  C   . GLU C 1 564  ? 63.619  48.275  54.913  1.00 162.42 ? 564  GLU B C   1 
ATOM   16697 O  O   . GLU C 1 564  ? 64.438  48.995  55.480  1.00 166.10 ? 564  GLU B O   1 
ATOM   16698 C  CB  . GLU C 1 564  ? 63.745  49.107  52.573  1.00 162.40 ? 564  GLU B CB  1 
ATOM   16699 C  CG  . GLU C 1 564  ? 64.803  50.173  52.862  1.00 168.38 ? 564  GLU B CG  1 
ATOM   16700 C  CD  . GLU C 1 564  ? 66.090  49.914  52.079  1.00 174.08 ? 564  GLU B CD  1 
ATOM   16701 O  OE1 . GLU C 1 564  ? 66.872  50.865  51.864  1.00 178.60 ? 564  GLU B OE1 1 
ATOM   16702 O  OE2 . GLU C 1 564  ? 66.329  48.748  51.681  1.00 173.59 ? 564  GLU B OE2 1 
ATOM   16703 N  N   . GLU C 1 565  ? 63.399  47.016  55.259  1.00 139.46 ? 565  GLU B N   1 
ATOM   16704 C  CA  . GLU C 1 565  ? 64.138  46.373  56.329  1.00 144.94 ? 565  GLU B CA  1 
ATOM   16705 C  C   . GLU C 1 565  ? 65.625  46.180  56.001  1.00 146.24 ? 565  GLU B C   1 
ATOM   16706 O  O   . GLU C 1 565  ? 66.144  45.065  56.061  1.00 143.91 ? 565  GLU B O   1 
ATOM   16707 C  CB  . GLU C 1 565  ? 63.468  45.054  56.642  1.00 148.22 ? 565  GLU B CB  1 
ATOM   16708 C  CG  . GLU C 1 565  ? 61.977  45.233  56.783  1.00 151.78 ? 565  GLU B CG  1 
ATOM   16709 C  CD  . GLU C 1 565  ? 61.354  43.999  57.327  1.00 153.30 ? 565  GLU B CD  1 
ATOM   16710 O  OE1 . GLU C 1 565  ? 62.099  43.004  57.438  1.00 153.67 ? 565  GLU B OE1 1 
ATOM   16711 O  OE2 . GLU C 1 565  ? 60.149  44.011  57.650  1.00 153.01 ? 565  GLU B OE2 1 
ATOM   16712 N  N   . LYS C 1 566  ? 66.291  47.277  55.646  1.00 159.12 ? 566  LYS B N   1 
ATOM   16713 C  CA  . LYS C 1 566  ? 67.744  47.334  55.507  1.00 163.79 ? 566  LYS B CA  1 
ATOM   16714 C  C   . LYS C 1 566  ? 68.366  47.308  56.895  1.00 166.16 ? 566  LYS B C   1 
ATOM   16715 O  O   . LYS C 1 566  ? 68.144  48.224  57.681  1.00 165.55 ? 566  LYS B O   1 
ATOM   16716 C  CB  . LYS C 1 566  ? 68.128  48.643  54.805  1.00 166.86 ? 566  LYS B CB  1 
ATOM   16717 C  CG  . LYS C 1 566  ? 69.620  48.846  54.494  1.00 170.36 ? 566  LYS B CG  1 
ATOM   16718 C  CD  . LYS C 1 566  ? 69.786  49.801  53.291  1.00 174.71 ? 566  LYS B CD  1 
ATOM   16719 C  CE  . LYS C 1 566  ? 71.231  49.953  52.795  1.00 180.09 ? 566  LYS B CE  1 
ATOM   16720 N  NZ  . LYS C 1 566  ? 72.047  50.903  53.609  1.00 182.96 ? 566  LYS B NZ  1 
ATOM   16721 N  N   . CYS C 1 567  ? 69.136  46.266  57.203  1.00 209.16 ? 567  CYS B N   1 
ATOM   16722 C  CA  . CYS C 1 567  ? 69.800  46.166  58.508  1.00 210.19 ? 567  CYS B CA  1 
ATOM   16723 C  C   . CYS C 1 567  ? 70.873  47.240  58.677  1.00 211.74 ? 567  CYS B C   1 
ATOM   16724 O  O   . CYS C 1 567  ? 71.127  48.031  57.764  1.00 212.41 ? 567  CYS B O   1 
ATOM   16725 C  CB  . CYS C 1 567  ? 70.415  44.778  58.722  1.00 210.42 ? 567  CYS B CB  1 
ATOM   16726 S  SG  . CYS C 1 567  ? 69.235  43.440  59.003  1.00 273.91 ? 567  CYS B SG  1 
ATOM   16727 N  N   . GLY C 1 568  ? 71.488  47.268  59.856  1.00 171.84 ? 568  GLY B N   1 
ATOM   16728 C  CA  . GLY C 1 568  ? 72.560  48.204  60.138  1.00 173.41 ? 568  GLY B CA  1 
ATOM   16729 C  C   . GLY C 1 568  ? 73.858  47.646  59.613  1.00 173.32 ? 568  GLY B C   1 
ATOM   16730 O  O   . GLY C 1 568  ? 74.373  48.099  58.597  1.00 174.22 ? 568  GLY B O   1 
ATOM   16731 N  N   . ASN C 1 569  ? 74.389  46.652  60.309  1.00 224.89 ? 569  ASN B N   1 
ATOM   16732 C  CA  . ASN C 1 569  ? 75.549  45.943  59.808  1.00 224.48 ? 569  ASN B CA  1 
ATOM   16733 C  C   . ASN C 1 569  ? 75.150  44.851  58.822  1.00 221.86 ? 569  ASN B C   1 
ATOM   16734 O  O   . ASN C 1 569  ? 74.481  43.889  59.196  1.00 222.75 ? 569  ASN B O   1 
ATOM   16735 C  CB  . ASN C 1 569  ? 76.352  45.360  60.968  1.00 225.50 ? 569  ASN B CB  1 
ATOM   16736 C  CG  . ASN C 1 569  ? 77.540  46.218  61.334  1.00 227.52 ? 569  ASN B CG  1 
ATOM   16737 O  OD1 . ASN C 1 569  ? 78.020  46.999  60.517  1.00 228.49 ? 569  ASN B OD1 1 
ATOM   16738 N  ND2 . ASN C 1 569  ? 78.025  46.073  62.560  1.00 227.64 ? 569  ASN B ND2 1 
ATOM   16739 N  N   . GLN C 1 570  ? 75.541  45.005  57.560  1.00 273.64 ? 570  GLN B N   1 
ATOM   16740 C  CA  . GLN C 1 570  ? 75.293  43.954  56.584  1.00 271.94 ? 570  GLN B CA  1 
ATOM   16741 C  C   . GLN C 1 570  ? 76.143  42.754  56.964  1.00 275.26 ? 570  GLN B C   1 
ATOM   16742 O  O   . GLN C 1 570  ? 77.347  42.726  56.712  1.00 275.46 ? 570  GLN B O   1 
ATOM   16743 C  CB  . GLN C 1 570  ? 75.627  44.411  55.156  1.00 268.48 ? 570  GLN B CB  1 
ATOM   16744 C  CG  . GLN C 1 570  ? 74.446  44.410  54.175  1.00 303.80 ? 570  GLN B CG  1 
ATOM   16745 C  CD  . GLN C 1 570  ? 73.788  45.772  54.049  1.00 303.06 ? 570  GLN B CD  1 
ATOM   16746 O  OE1 . GLN C 1 570  ? 73.703  46.522  55.021  1.00 302.17 ? 570  GLN B OE1 1 
ATOM   16747 N  NE2 . GLN C 1 570  ? 73.319  46.098  52.848  1.00 302.95 ? 570  GLN B NE2 1 
ATOM   16748 N  N   . LEU C 1 571  ? 75.520  41.774  57.606  1.00 195.42 ? 571  LEU B N   1 
ATOM   16749 C  CA  . LEU C 1 571  ? 76.198  40.521  57.862  1.00 195.86 ? 571  LEU B CA  1 
ATOM   16750 C  C   . LEU C 1 571  ? 75.758  39.485  56.865  1.00 199.13 ? 571  LEU B C   1 
ATOM   16751 O  O   . LEU C 1 571  ? 74.566  39.213  56.728  1.00 200.51 ? 571  LEU B O   1 
ATOM   16752 C  CB  . LEU C 1 571  ? 75.897  39.992  59.258  1.00 188.23 ? 571  LEU B CB  1 
ATOM   16753 C  CG  . LEU C 1 571  ? 76.276  38.506  59.404  1.00 180.78 ? 571  LEU B CG  1 
ATOM   16754 C  CD1 . LEU C 1 571  ? 77.612  38.188  58.729  1.00 174.20 ? 571  LEU B CD1 1 
ATOM   16755 C  CD2 . LEU C 1 571  ? 76.299  38.039  60.862  1.00 175.39 ? 571  LEU B CD2 1 
ATOM   16756 N  N   . GLN C 1 572  ? 76.735  38.889  56.194  1.00 205.71 ? 572  GLN B N   1 
ATOM   16757 C  CA  . GLN C 1 572  ? 76.476  37.801  55.272  1.00 207.73 ? 572  GLN B CA  1 
ATOM   16758 C  C   . GLN C 1 572  ? 77.464  36.654  55.527  1.00 203.56 ? 572  GLN B C   1 
ATOM   16759 O  O   . GLN C 1 572  ? 78.594  36.866  55.967  1.00 201.66 ? 572  GLN B O   1 
ATOM   16760 C  CB  . GLN C 1 572  ? 76.552  38.320  53.826  1.00 218.80 ? 572  GLN B CB  1 
ATOM   16761 C  CG  . GLN C 1 572  ? 76.080  37.347  52.728  1.00 229.24 ? 572  GLN B CG  1 
ATOM   16762 C  CD  . GLN C 1 572  ? 74.588  37.038  52.766  1.00 237.47 ? 572  GLN B CD  1 
ATOM   16763 O  OE1 . GLN C 1 572  ? 73.777  37.853  53.208  1.00 239.84 ? 572  GLN B OE1 1 
ATOM   16764 N  NE2 . GLN C 1 572  ? 74.221  35.853  52.282  1.00 241.06 ? 572  GLN B NE2 1 
ATOM   16765 N  N   . VAL C 1 573  ? 77.012  35.435  55.260  1.00 175.21 ? 573  VAL B N   1 
ATOM   16766 C  CA  . VAL C 1 573  ? 77.836  34.242  55.399  1.00 171.62 ? 573  VAL B CA  1 
ATOM   16767 C  C   . VAL C 1 573  ? 77.914  33.417  54.093  1.00 173.77 ? 573  VAL B C   1 
ATOM   16768 O  O   . VAL C 1 573  ? 76.884  33.011  53.543  1.00 174.93 ? 573  VAL B O   1 
ATOM   16769 C  CB  . VAL C 1 573  ? 77.253  33.371  56.489  1.00 161.83 ? 573  VAL B CB  1 
ATOM   16770 C  CG1 . VAL C 1 573  ? 77.985  33.622  57.768  1.00 159.08 ? 573  VAL B CG1 1 
ATOM   16771 C  CG2 . VAL C 1 573  ? 75.764  33.677  56.636  1.00 157.71 ? 573  VAL B CG2 1 
ATOM   16772 N  N   . HIS C 1 574  ? 79.127  33.160  53.598  1.00 193.06 ? 574  HIS B N   1 
ATOM   16773 C  CA  . HIS C 1 574  ? 79.293  32.396  52.357  1.00 194.51 ? 574  HIS B CA  1 
ATOM   16774 C  C   . HIS C 1 574  ? 80.174  31.166  52.545  1.00 198.57 ? 574  HIS B C   1 
ATOM   16775 O  O   . HIS C 1 574  ? 81.229  31.241  53.167  1.00 197.34 ? 574  HIS B O   1 
ATOM   16776 C  CB  . HIS C 1 574  ? 79.899  33.269  51.253  1.00 197.75 ? 574  HIS B CB  1 
ATOM   16777 C  CG  . HIS C 1 574  ? 78.958  34.286  50.683  1.00 201.21 ? 574  HIS B CG  1 
ATOM   16778 N  ND1 . HIS C 1 574  ? 77.661  33.987  50.325  1.00 201.84 ? 574  HIS B ND1 1 
ATOM   16779 C  CD2 . HIS C 1 574  ? 79.142  35.594  50.377  1.00 202.93 ? 574  HIS B CD2 1 
ATOM   16780 C  CE1 . HIS C 1 574  ? 77.079  35.072  49.845  1.00 202.48 ? 574  HIS B CE1 1 
ATOM   16781 N  NE2 . HIS C 1 574  ? 77.956  36.060  49.862  1.00 203.38 ? 574  HIS B NE2 1 
ATOM   16782 N  N   . LEU C 1 575  ? 79.744  30.044  51.979  1.00 168.15 ? 575  LEU B N   1 
ATOM   16783 C  CA  . LEU C 1 575  ? 80.504  28.795  52.034  1.00 176.53 ? 575  LEU B CA  1 
ATOM   16784 C  C   . LEU C 1 575  ? 81.571  28.641  50.949  1.00 188.21 ? 575  LEU B C   1 
ATOM   16785 O  O   . LEU C 1 575  ? 81.259  28.736  49.766  1.00 192.84 ? 575  LEU B O   1 
ATOM   16786 C  CB  . LEU C 1 575  ? 79.539  27.640  51.920  1.00 171.50 ? 575  LEU B CB  1 
ATOM   16787 C  CG  . LEU C 1 575  ? 78.622  27.673  53.114  1.00 164.52 ? 575  LEU B CG  1 
ATOM   16788 C  CD1 . LEU C 1 575  ? 77.622  26.573  52.985  1.00 162.05 ? 575  LEU B CD1 1 
ATOM   16789 C  CD2 . LEU C 1 575  ? 79.497  27.469  54.314  1.00 164.22 ? 575  LEU B CD2 1 
ATOM   16790 N  N   . SER C 1 576  ? 82.807  28.336  51.349  1.00 280.92 ? 576  SER B N   1 
ATOM   16791 C  CA  . SER C 1 576  ? 83.950  28.319  50.421  1.00 289.77 ? 576  SER B CA  1 
ATOM   16792 C  C   . SER C 1 576  ? 83.671  27.646  49.078  1.00 292.40 ? 576  SER B C   1 
ATOM   16793 O  O   . SER C 1 576  ? 83.680  28.316  48.045  1.00 292.84 ? 576  SER B O   1 
ATOM   16794 C  CB  . SER C 1 576  ? 85.210  27.742  51.075  1.00 295.26 ? 576  SER B CB  1 
ATOM   16795 O  OG  . SER C 1 576  ? 85.944  28.760  51.722  1.00 298.84 ? 576  SER B OG  1 
ATOM   16796 N  N   . PRO C 1 577  ? 83.461  26.320  49.075  1.00 229.31 ? 577  PRO B N   1 
ATOM   16797 C  CA  . PRO C 1 577  ? 82.861  25.749  47.869  1.00 230.87 ? 577  PRO B CA  1 
ATOM   16798 C  C   . PRO C 1 577  ? 81.371  26.074  47.844  1.00 228.92 ? 577  PRO B C   1 
ATOM   16799 O  O   . PRO C 1 577  ? 80.634  25.562  48.683  1.00 229.36 ? 577  PRO B O   1 
ATOM   16800 C  CB  . PRO C 1 577  ? 83.071  24.239  48.053  1.00 234.36 ? 577  PRO B CB  1 
ATOM   16801 C  CG  . PRO C 1 577  ? 84.188  24.122  49.014  1.00 234.81 ? 577  PRO B CG  1 
ATOM   16802 C  CD  . PRO C 1 577  ? 83.997  25.270  49.954  1.00 230.98 ? 577  PRO B CD  1 
ATOM   16803 N  N   . ASP C 1 578  ? 80.936  26.911  46.904  1.00 232.69 ? 578  ASP B N   1 
ATOM   16804 C  CA  . ASP C 1 578  ? 79.541  27.336  46.848  1.00 228.06 ? 578  ASP B CA  1 
ATOM   16805 C  C   . ASP C 1 578  ? 78.628  26.291  46.219  1.00 225.27 ? 578  ASP B C   1 
ATOM   16806 O  O   . ASP C 1 578  ? 77.454  26.556  45.950  1.00 221.76 ? 578  ASP B O   1 
ATOM   16807 C  CB  . ASP C 1 578  ? 79.407  28.656  46.104  1.00 230.36 ? 578  ASP B CB  1 
ATOM   16808 C  CG  . ASP C 1 578  ? 78.237  29.463  46.593  1.00 231.95 ? 578  ASP B CG  1 
ATOM   16809 O  OD1 . ASP C 1 578  ? 77.270  28.851  47.094  1.00 231.53 ? 578  ASP B OD1 1 
ATOM   16810 O  OD2 . ASP C 1 578  ? 78.287  30.705  46.495  1.00 233.11 ? 578  ASP B OD2 1 
ATOM   16811 N  N   . ALA C 1 579  ? 79.184  25.108  45.983  1.00 230.14 ? 579  ALA B N   1 
ATOM   16812 C  CA  . ALA C 1 579  ? 78.432  23.977  45.454  1.00 229.92 ? 579  ALA B CA  1 
ATOM   16813 C  C   . ALA C 1 579  ? 77.195  23.746  46.297  1.00 223.83 ? 579  ALA B C   1 
ATOM   16814 O  O   . ALA C 1 579  ? 77.226  23.921  47.515  1.00 223.95 ? 579  ALA B O   1 
ATOM   16815 C  CB  . ALA C 1 579  ? 79.291  22.725  45.446  1.00 233.37 ? 579  ALA B CB  1 
ATOM   16816 N  N   . ASP C 1 580  ? 76.111  23.348  45.641  1.00 219.47 ? 580  ASP B N   1 
ATOM   16817 C  CA  . ASP C 1 580  ? 74.836  23.141  46.315  1.00 216.41 ? 580  ASP B CA  1 
ATOM   16818 C  C   . ASP C 1 580  ? 74.729  21.718  46.845  1.00 214.30 ? 580  ASP B C   1 
ATOM   16819 O  O   . ASP C 1 580  ? 73.638  21.157  46.956  1.00 213.48 ? 580  ASP B O   1 
ATOM   16820 C  CB  . ASP C 1 580  ? 73.682  23.454  45.368  1.00 220.88 ? 580  ASP B CB  1 
ATOM   16821 C  CG  . ASP C 1 580  ? 73.687  22.568  44.147  1.00 229.34 ? 580  ASP B CG  1 
ATOM   16822 O  OD1 . ASP C 1 580  ? 73.975  21.361  44.290  1.00 232.84 ? 580  ASP B OD1 1 
ATOM   16823 O  OD2 . ASP C 1 580  ? 73.407  23.078  43.044  1.00 232.45 ? 580  ASP B OD2 1 
ATOM   16824 N  N   . ALA C 1 581  ? 75.879  21.147  47.173  1.00 222.07 ? 581  ALA B N   1 
ATOM   16825 C  CA  . ALA C 1 581  ? 75.938  19.817  47.747  1.00 220.00 ? 581  ALA B CA  1 
ATOM   16826 C  C   . ALA C 1 581  ? 77.336  19.591  48.309  1.00 219.25 ? 581  ALA B C   1 
ATOM   16827 O  O   . ALA C 1 581  ? 78.303  20.129  47.768  1.00 220.13 ? 581  ALA B O   1 
ATOM   16828 C  CB  . ALA C 1 581  ? 75.609  18.788  46.694  1.00 222.75 ? 581  ALA B CB  1 
ATOM   16829 N  N   . TYR C 1 582  ? 77.444  18.803  49.385  1.00 185.28 ? 582  TYR B N   1 
ATOM   16830 C  CA  . TYR C 1 582  ? 78.736  18.573  50.042  1.00 181.96 ? 582  TYR B CA  1 
ATOM   16831 C  C   . TYR C 1 582  ? 79.108  17.110  50.285  1.00 178.90 ? 582  TYR B C   1 
ATOM   16832 O  O   . TYR C 1 582  ? 78.246  16.273  50.532  1.00 179.07 ? 582  TYR B O   1 
ATOM   16833 C  CB  . TYR C 1 582  ? 78.796  19.356  51.344  1.00 178.54 ? 582  TYR B CB  1 
ATOM   16834 C  CG  . TYR C 1 582  ? 78.889  20.839  51.109  1.00 176.03 ? 582  TYR B CG  1 
ATOM   16835 C  CD1 . TYR C 1 582  ? 80.122  21.453  50.939  1.00 176.95 ? 582  TYR B CD1 1 
ATOM   16836 C  CD2 . TYR C 1 582  ? 77.749  21.623  51.029  1.00 173.04 ? 582  TYR B CD2 1 
ATOM   16837 C  CE1 . TYR C 1 582  ? 80.221  22.816  50.711  1.00 176.06 ? 582  TYR B CE1 1 
ATOM   16838 C  CE2 . TYR C 1 582  ? 77.834  22.989  50.804  1.00 171.99 ? 582  TYR B CE2 1 
ATOM   16839 C  CZ  . TYR C 1 582  ? 79.074  23.580  50.645  1.00 173.65 ? 582  TYR B CZ  1 
ATOM   16840 O  OH  . TYR C 1 582  ? 79.178  24.935  50.423  1.00 172.93 ? 582  TYR B OH  1 
ATOM   16841 N  N   . SER C 1 583  ? 80.404  16.820  50.196  1.00 242.44 ? 583  SER B N   1 
ATOM   16842 C  CA  . SER C 1 583  ? 80.945  15.504  50.519  1.00 241.70 ? 583  SER B CA  1 
ATOM   16843 C  C   . SER C 1 583  ? 81.049  15.362  52.031  1.00 239.64 ? 583  SER B C   1 
ATOM   16844 O  O   . SER C 1 583  ? 81.609  16.226  52.695  1.00 234.50 ? 583  SER B O   1 
ATOM   16845 C  CB  . SER C 1 583  ? 82.327  15.349  49.897  1.00 248.87 ? 583  SER B CB  1 
ATOM   16846 O  OG  . SER C 1 583  ? 83.113  16.499  50.160  1.00 250.72 ? 583  SER B OG  1 
ATOM   16847 N  N   . PRO C 1 584  ? 80.533  14.255  52.579  1.00 177.39 ? 584  PRO B N   1 
ATOM   16848 C  CA  . PRO C 1 584  ? 80.307  14.125  54.024  1.00 177.39 ? 584  PRO B CA  1 
ATOM   16849 C  C   . PRO C 1 584  ? 81.604  14.076  54.819  1.00 174.68 ? 584  PRO B C   1 
ATOM   16850 O  O   . PRO C 1 584  ? 82.186  13.005  54.928  1.00 176.89 ? 584  PRO B O   1 
ATOM   16851 C  CB  . PRO C 1 584  ? 79.575  12.780  54.143  1.00 177.65 ? 584  PRO B CB  1 
ATOM   16852 C  CG  . PRO C 1 584  ? 79.168  12.412  52.731  1.00 179.77 ? 584  PRO B CG  1 
ATOM   16853 C  CD  . PRO C 1 584  ? 80.198  13.021  51.855  1.00 181.67 ? 584  PRO B CD  1 
ATOM   16854 N  N   . GLY C 1 585  ? 82.037  15.204  55.377  1.00 209.76 ? 585  GLY B N   1 
ATOM   16855 C  CA  . GLY C 1 585  ? 83.289  15.263  56.114  1.00 211.89 ? 585  GLY B CA  1 
ATOM   16856 C  C   . GLY C 1 585  ? 84.290  16.223  55.496  1.00 213.14 ? 585  GLY B C   1 
ATOM   16857 O  O   . GLY C 1 585  ? 85.385  16.431  56.023  1.00 214.21 ? 585  GLY B O   1 
ATOM   16858 N  N   . GLN C 1 586  ? 83.903  16.804  54.363  1.00 191.48 ? 586  GLN B N   1 
ATOM   16859 C  CA  . GLN C 1 586  ? 84.763  17.695  53.586  1.00 194.92 ? 586  GLN B CA  1 
ATOM   16860 C  C   . GLN C 1 586  ? 85.171  18.907  54.401  1.00 196.14 ? 586  GLN B C   1 
ATOM   16861 O  O   . GLN C 1 586  ? 84.336  19.586  54.987  1.00 193.74 ? 586  GLN B O   1 
ATOM   16862 C  CB  . GLN C 1 586  ? 84.034  18.149  52.308  1.00 193.64 ? 586  GLN B CB  1 
ATOM   16863 C  CG  . GLN C 1 586  ? 84.779  19.148  51.417  1.00 196.35 ? 586  GLN B CG  1 
ATOM   16864 C  CD  . GLN C 1 586  ? 83.910  19.676  50.280  1.00 198.59 ? 586  GLN B CD  1 
ATOM   16865 O  OE1 . GLN C 1 586  ? 82.924  19.050  49.889  1.00 198.24 ? 586  GLN B OE1 1 
ATOM   16866 N  NE2 . GLN C 1 586  ? 84.274  20.836  49.749  1.00 200.71 ? 586  GLN B NE2 1 
ATOM   16867 N  N   . THR C 1 587  ? 86.463  19.174  54.448  1.00 208.51 ? 587  THR B N   1 
ATOM   16868 C  CA  . THR C 1 587  ? 86.918  20.440  54.966  1.00 213.02 ? 587  THR B CA  1 
ATOM   16869 C  C   . THR C 1 587  ? 86.399  21.511  53.994  1.00 214.00 ? 587  THR B C   1 
ATOM   16870 O  O   . THR C 1 587  ? 86.534  21.357  52.774  1.00 212.56 ? 587  THR B O   1 
ATOM   16871 C  CB  . THR C 1 587  ? 88.435  20.441  55.039  1.00 218.87 ? 587  THR B CB  1 
ATOM   16872 O  OG1 . THR C 1 587  ? 88.953  20.034  53.770  1.00 221.90 ? 587  THR B OG1 1 
ATOM   16873 C  CG2 . THR C 1 587  ? 88.901  19.440  56.080  1.00 221.61 ? 587  THR B CG2 1 
ATOM   16874 N  N   . VAL C 1 588  ? 85.785  22.569  54.532  1.00 195.11 ? 588  VAL B N   1 
ATOM   16875 C  CA  . VAL C 1 588  ? 85.213  23.664  53.730  1.00 195.65 ? 588  VAL B CA  1 
ATOM   16876 C  C   . VAL C 1 588  ? 85.202  24.993  54.479  1.00 194.35 ? 588  VAL B C   1 
ATOM   16877 O  O   . VAL C 1 588  ? 84.678  25.087  55.583  1.00 195.42 ? 588  VAL B O   1 
ATOM   16878 C  CB  . VAL C 1 588  ? 83.760  23.383  53.305  1.00 194.53 ? 588  VAL B CB  1 
ATOM   16879 C  CG1 . VAL C 1 588  ? 83.061  22.572  54.347  1.00 192.70 ? 588  VAL B CG1 1 
ATOM   16880 C  CG2 . VAL C 1 588  ? 83.015  24.689  53.092  1.00 192.76 ? 588  VAL B CG2 1 
ATOM   16881 N  N   . SER C 1 589  ? 85.744  26.033  53.859  1.00 260.40 ? 589  SER B N   1 
ATOM   16882 C  CA  . SER C 1 589  ? 85.913  27.311  54.543  1.00 260.15 ? 589  SER B CA  1 
ATOM   16883 C  C   . SER C 1 589  ? 84.645  28.180  54.572  1.00 255.74 ? 589  SER B C   1 
ATOM   16884 O  O   . SER C 1 589  ? 84.009  28.396  53.547  1.00 253.98 ? 589  SER B O   1 
ATOM   16885 C  CB  . SER C 1 589  ? 87.088  28.070  53.924  1.00 265.73 ? 589  SER B CB  1 
ATOM   16886 O  OG  . SER C 1 589  ? 87.986  27.173  53.290  1.00 270.82 ? 589  SER B OG  1 
ATOM   16887 N  N   . LEU C 1 590  ? 84.281  28.674  55.755  1.00 189.01 ? 590  LEU B N   1 
ATOM   16888 C  CA  . LEU C 1 590  ? 83.140  29.583  55.893  1.00 183.48 ? 590  LEU B CA  1 
ATOM   16889 C  C   . LEU C 1 590  ? 83.554  31.046  56.103  1.00 181.72 ? 590  LEU B C   1 
ATOM   16890 O  O   . LEU C 1 590  ? 84.449  31.347  56.899  1.00 185.06 ? 590  LEU B O   1 
ATOM   16891 C  CB  . LEU C 1 590  ? 82.232  29.145  57.039  1.00 177.55 ? 590  LEU B CB  1 
ATOM   16892 C  CG  . LEU C 1 590  ? 81.418  30.303  57.622  1.00 169.10 ? 590  LEU B CG  1 
ATOM   16893 C  CD1 . LEU C 1 590  ? 80.353  30.770  56.651  1.00 165.65 ? 590  LEU B CD1 1 
ATOM   16894 C  CD2 . LEU C 1 590  ? 80.793  29.924  58.945  1.00 165.32 ? 590  LEU B CD2 1 
ATOM   16895 N  N   . ASN C 1 591  ? 82.870  31.949  55.402  1.00 196.28 ? 591  ASN B N   1 
ATOM   16896 C  CA  . ASN C 1 591  ? 83.211  33.374  55.403  1.00 194.00 ? 591  ASN B CA  1 
ATOM   16897 C  C   . ASN C 1 591  ? 82.266  34.288  56.198  1.00 190.77 ? 591  ASN B C   1 
ATOM   16898 O  O   . ASN C 1 591  ? 81.047  34.101  56.195  1.00 189.35 ? 591  ASN B O   1 
ATOM   16899 C  CB  . ASN C 1 591  ? 83.330  33.886  53.959  1.00 195.22 ? 591  ASN B CB  1 
ATOM   16900 C  CG  . ASN C 1 591  ? 84.605  33.423  53.277  1.00 200.02 ? 591  ASN B CG  1 
ATOM   16901 O  OD1 . ASN C 1 591  ? 85.659  34.054  53.401  1.00 202.28 ? 591  ASN B OD1 1 
ATOM   16902 N  ND2 . ASN C 1 591  ? 84.515  32.316  52.552  1.00 201.76 ? 591  ASN B ND2 1 
ATOM   16903 N  N   . MET C 1 592  ? 82.842  35.281  56.869  1.00 208.98 ? 592  MET B N   1 
ATOM   16904 C  CA  . MET C 1 592  ? 82.058  36.335  57.503  1.00 205.35 ? 592  MET B CA  1 
ATOM   16905 C  C   . MET C 1 592  ? 82.308  37.691  56.835  1.00 206.94 ? 592  MET B C   1 
ATOM   16906 O  O   . MET C 1 592  ? 83.384  37.936  56.278  1.00 208.24 ? 592  MET B O   1 
ATOM   16907 C  CB  . MET C 1 592  ? 82.360  36.426  59.001  1.00 204.48 ? 592  MET B CB  1 
ATOM   16908 C  CG  . MET C 1 592  ? 81.442  35.592  59.878  1.00 202.08 ? 592  MET B CG  1 
ATOM   16909 S  SD  . MET C 1 592  ? 82.096  33.945  60.176  1.00 223.21 ? 592  MET B SD  1 
ATOM   16910 C  CE  . MET C 1 592  ? 83.675  34.384  60.894  1.00 212.46 ? 592  MET B CE  1 
ATOM   16911 N  N   . ALA C 1 593  ? 81.314  38.575  56.905  1.00 182.26 ? 593  ALA B N   1 
ATOM   16912 C  CA  . ALA C 1 593  ? 81.412  39.883  56.259  1.00 185.28 ? 593  ALA B CA  1 
ATOM   16913 C  C   . ALA C 1 593  ? 80.596  40.994  56.925  1.00 188.46 ? 593  ALA B C   1 
ATOM   16914 O  O   . ALA C 1 593  ? 79.479  40.771  57.406  1.00 185.97 ? 593  ALA B O   1 
ATOM   16915 C  CB  . ALA C 1 593  ? 81.026  39.770  54.788  1.00 183.39 ? 593  ALA B CB  1 
ATOM   16916 N  N   . THR C 1 594  ? 81.160  42.200  56.919  1.00 189.86 ? 594  THR B N   1 
ATOM   16917 C  CA  . THR C 1 594  ? 80.449  43.373  57.413  1.00 194.31 ? 594  THR B CA  1 
ATOM   16918 C  C   . THR C 1 594  ? 81.016  44.714  56.952  1.00 199.10 ? 594  THR B C   1 
ATOM   16919 O  O   . THR C 1 594  ? 82.229  44.890  56.833  1.00 202.83 ? 594  THR B O   1 
ATOM   16920 C  CB  . THR C 1 594  ? 80.415  43.392  58.922  1.00 195.48 ? 594  THR B CB  1 
ATOM   16921 O  OG1 . THR C 1 594  ? 80.714  42.084  59.421  1.00 195.34 ? 594  THR B OG1 1 
ATOM   16922 C  CG2 . THR C 1 594  ? 79.048  43.835  59.388  1.00 194.07 ? 594  THR B CG2 1 
ATOM   16923 N  N   . GLY C 1 595  ? 80.115  45.660  56.705  1.00 228.84 ? 595  GLY B N   1 
ATOM   16924 C  CA  . GLY C 1 595  ? 80.496  47.015  56.357  1.00 234.07 ? 595  GLY B CA  1 
ATOM   16925 C  C   . GLY C 1 595  ? 81.060  47.717  57.574  1.00 241.95 ? 595  GLY B C   1 
ATOM   16926 O  O   . GLY C 1 595  ? 81.705  48.754  57.449  1.00 242.29 ? 595  GLY B O   1 
ATOM   16927 N  N   . MET C 1 596  ? 80.813  47.136  58.749  1.00 207.11 ? 596  MET B N   1 
ATOM   16928 C  CA  . MET C 1 596  ? 81.319  47.650  60.024  1.00 211.86 ? 596  MET B CA  1 
ATOM   16929 C  C   . MET C 1 596  ? 81.716  46.492  60.953  1.00 211.78 ? 596  MET B C   1 
ATOM   16930 O  O   . MET C 1 596  ? 81.114  45.422  60.898  1.00 212.63 ? 596  MET B O   1 
ATOM   16931 C  CB  . MET C 1 596  ? 80.248  48.500  60.713  1.00 212.07 ? 596  MET B CB  1 
ATOM   16932 C  CG  . MET C 1 596  ? 79.924  49.808  60.028  1.00 212.80 ? 596  MET B CG  1 
ATOM   16933 S  SD  . MET C 1 596  ? 81.182  51.030  60.396  1.00 238.98 ? 596  MET B SD  1 
ATOM   16934 C  CE  . MET C 1 596  ? 81.335  50.806  62.168  1.00 189.70 ? 596  MET B CE  1 
ATOM   16935 N  N   . ASP C 1 597  ? 82.716  46.703  61.809  1.00 248.60 ? 597  ASP B N   1 
ATOM   16936 C  CA  . ASP C 1 597  ? 83.117  45.674  62.769  1.00 247.32 ? 597  ASP B CA  1 
ATOM   16937 C  C   . ASP C 1 597  ? 81.880  45.161  63.493  1.00 238.82 ? 597  ASP B C   1 
ATOM   16938 O  O   . ASP C 1 597  ? 81.018  45.958  63.868  1.00 236.09 ? 597  ASP B O   1 
ATOM   16939 C  CB  . ASP C 1 597  ? 84.098  46.243  63.796  1.00 254.90 ? 597  ASP B CB  1 
ATOM   16940 C  CG  . ASP C 1 597  ? 85.307  46.888  63.159  1.00 263.44 ? 597  ASP B CG  1 
ATOM   16941 O  OD1 . ASP C 1 597  ? 85.850  46.321  62.187  1.00 266.26 ? 597  ASP B OD1 1 
ATOM   16942 O  OD2 . ASP C 1 597  ? 85.718  47.966  63.639  1.00 266.47 ? 597  ASP B OD2 1 
ATOM   16943 N  N   . SER C 1 598  ? 81.787  43.844  63.695  1.00 184.16 ? 598  SER B N   1 
ATOM   16944 C  CA  . SER C 1 598  ? 80.613  43.269  64.375  1.00 175.98 ? 598  SER B CA  1 
ATOM   16945 C  C   . SER C 1 598  ? 80.756  41.848  64.971  1.00 167.28 ? 598  SER B C   1 
ATOM   16946 O  O   . SER C 1 598  ? 81.662  41.081  64.632  1.00 167.09 ? 598  SER B O   1 
ATOM   16947 C  CB  . SER C 1 598  ? 79.366  43.358  63.476  1.00 173.46 ? 598  SER B CB  1 
ATOM   16948 O  OG  . SER C 1 598  ? 78.171  43.071  64.189  1.00 171.00 ? 598  SER B OG  1 
ATOM   16949 N  N   . TRP C 1 599  ? 79.834  41.540  65.879  1.00 209.14 ? 599  TRP B N   1 
ATOM   16950 C  CA  . TRP C 1 599  ? 79.790  40.282  66.603  1.00 204.33 ? 599  TRP B CA  1 
ATOM   16951 C  C   . TRP C 1 599  ? 78.831  39.318  65.950  1.00 199.09 ? 599  TRP B C   1 
ATOM   16952 O  O   . TRP C 1 599  ? 77.635  39.583  65.902  1.00 199.33 ? 599  TRP B O   1 
ATOM   16953 C  CB  . TRP C 1 599  ? 79.288  40.531  68.020  1.00 206.44 ? 599  TRP B CB  1 
ATOM   16954 C  CG  . TRP C 1 599  ? 80.334  41.010  68.950  1.00 212.93 ? 599  TRP B CG  1 
ATOM   16955 C  CD1 . TRP C 1 599  ? 80.372  42.210  69.598  1.00 215.83 ? 599  TRP B CD1 1 
ATOM   16956 C  CD2 . TRP C 1 599  ? 81.510  40.300  69.346  1.00 216.07 ? 599  TRP B CD2 1 
ATOM   16957 N  NE1 . TRP C 1 599  ? 81.503  42.290  70.375  1.00 217.86 ? 599  TRP B NE1 1 
ATOM   16958 C  CE2 . TRP C 1 599  ? 82.215  41.128  70.238  1.00 217.49 ? 599  TRP B CE2 1 
ATOM   16959 C  CE3 . TRP C 1 599  ? 82.032  39.042  69.034  1.00 216.99 ? 599  TRP B CE3 1 
ATOM   16960 C  CZ2 . TRP C 1 599  ? 83.419  40.736  70.817  1.00 218.24 ? 599  TRP B CZ2 1 
ATOM   16961 C  CZ3 . TRP C 1 599  ? 83.221  38.658  69.611  1.00 217.93 ? 599  TRP B CZ3 1 
ATOM   16962 C  CH2 . TRP C 1 599  ? 83.902  39.499  70.491  1.00 218.51 ? 599  TRP B CH2 1 
ATOM   16963 N  N   . VAL C 1 600  ? 79.347  38.188  65.475  1.00 199.40 ? 600  VAL B N   1 
ATOM   16964 C  CA  . VAL C 1 600  ? 78.516  37.185  64.810  1.00 192.35 ? 600  VAL B CA  1 
ATOM   16965 C  C   . VAL C 1 600  ? 78.140  36.086  65.803  1.00 189.10 ? 600  VAL B C   1 
ATOM   16966 O  O   . VAL C 1 600  ? 78.671  36.034  66.910  1.00 190.59 ? 600  VAL B O   1 
ATOM   16967 C  CB  . VAL C 1 600  ? 79.227  36.575  63.561  1.00 191.66 ? 600  VAL B CB  1 
ATOM   16968 C  CG1 . VAL C 1 600  ? 78.220  35.946  62.591  1.00 190.53 ? 600  VAL B CG1 1 
ATOM   16969 C  CG2 . VAL C 1 600  ? 80.053  37.638  62.831  1.00 191.38 ? 600  VAL B CG2 1 
ATOM   16970 N  N   . ALA C 1 601  ? 77.222  35.217  65.392  1.00 173.33 ? 601  ALA B N   1 
ATOM   16971 C  CA  . ALA C 1 601  ? 76.749  34.112  66.222  1.00 172.23 ? 601  ALA B CA  1 
ATOM   16972 C  C   . ALA C 1 601  ? 76.221  32.941  65.377  1.00 171.95 ? 601  ALA B C   1 
ATOM   16973 O  O   . ALA C 1 601  ? 75.014  32.782  65.194  1.00 172.88 ? 601  ALA B O   1 
ATOM   16974 C  CB  . ALA C 1 601  ? 75.675  34.591  67.195  1.00 170.41 ? 601  ALA B CB  1 
ATOM   16975 N  N   . LEU C 1 602  ? 77.135  32.111  64.888  1.00 164.02 ? 602  LEU B N   1 
ATOM   16976 C  CA  . LEU C 1 602  ? 76.785  30.989  64.024  1.00 162.93 ? 602  LEU B CA  1 
ATOM   16977 C  C   . LEU C 1 602  ? 75.858  29.985  64.709  1.00 165.21 ? 602  LEU B C   1 
ATOM   16978 O  O   . LEU C 1 602  ? 75.735  29.974  65.931  1.00 165.95 ? 602  LEU B O   1 
ATOM   16979 C  CB  . LEU C 1 602  ? 78.057  30.283  63.549  1.00 161.44 ? 602  LEU B CB  1 
ATOM   16980 C  CG  . LEU C 1 602  ? 79.234  31.191  63.148  1.00 160.06 ? 602  LEU B CG  1 
ATOM   16981 C  CD1 . LEU C 1 602  ? 80.325  30.420  62.381  1.00 160.59 ? 602  LEU B CD1 1 
ATOM   16982 C  CD2 . LEU C 1 602  ? 78.771  32.420  62.343  1.00 159.42 ? 602  LEU B CD2 1 
ATOM   16983 N  N   . ALA C 1 603  ? 75.205  29.145  63.913  1.00 207.32 ? 603  ALA B N   1 
ATOM   16984 C  CA  . ALA C 1 603  ? 74.263  28.162  64.436  1.00 202.65 ? 603  ALA B CA  1 
ATOM   16985 C  C   . ALA C 1 603  ? 73.812  27.167  63.357  1.00 200.82 ? 603  ALA B C   1 
ATOM   16986 O  O   . ALA C 1 603  ? 72.875  27.448  62.608  1.00 198.81 ? 603  ALA B O   1 
ATOM   16987 C  CB  . ALA C 1 603  ? 73.058  28.873  65.021  1.00 200.55 ? 603  ALA B CB  1 
ATOM   16988 N  N   . ALA C 1 604  ? 74.457  26.000  63.296  1.00 214.31 ? 604  ALA B N   1 
ATOM   16989 C  CA  . ALA C 1 604  ? 74.190  25.021  62.236  1.00 213.49 ? 604  ALA B CA  1 
ATOM   16990 C  C   . ALA C 1 604  ? 73.198  23.936  62.643  1.00 213.27 ? 604  ALA B C   1 
ATOM   16991 O  O   . ALA C 1 604  ? 73.591  22.869  63.110  1.00 215.23 ? 604  ALA B O   1 
ATOM   16992 C  CB  . ALA C 1 604  ? 75.487  24.392  61.744  1.00 212.24 ? 604  ALA B CB  1 
ATOM   16993 N  N   . VAL C 1 605  ? 71.916  24.222  62.447  1.00 142.79 ? 605  VAL B N   1 
ATOM   16994 C  CA  . VAL C 1 605  ? 70.831  23.287  62.720  1.00 142.83 ? 605  VAL B CA  1 
ATOM   16995 C  C   . VAL C 1 605  ? 70.699  22.187  61.660  1.00 145.00 ? 605  VAL B C   1 
ATOM   16996 O  O   . VAL C 1 605  ? 71.234  22.292  60.555  1.00 145.89 ? 605  VAL B O   1 
ATOM   16997 C  CB  . VAL C 1 605  ? 69.490  24.040  62.754  1.00 141.95 ? 605  VAL B CB  1 
ATOM   16998 C  CG1 . VAL C 1 605  ? 68.360  23.103  63.122  1.00 142.55 ? 605  VAL B CG1 1 
ATOM   16999 C  CG2 . VAL C 1 605  ? 69.563  25.222  63.707  1.00 142.30 ? 605  VAL B CG2 1 
ATOM   17000 N  N   . ASP C 1 606  ? 69.988  21.120  62.003  1.00 169.85 ? 606  ASP B N   1 
ATOM   17001 C  CA  . ASP C 1 606  ? 69.496  20.218  60.979  1.00 170.62 ? 606  ASP B CA  1 
ATOM   17002 C  C   . ASP C 1 606  ? 68.171  20.764  60.505  1.00 168.40 ? 606  ASP B C   1 
ATOM   17003 O  O   . ASP C 1 606  ? 67.161  20.656  61.207  1.00 169.64 ? 606  ASP B O   1 
ATOM   17004 C  CB  . ASP C 1 606  ? 69.283  18.807  61.503  1.00 173.99 ? 606  ASP B CB  1 
ATOM   17005 C  CG  . ASP C 1 606  ? 68.828  17.849  60.413  1.00 173.30 ? 606  ASP B CG  1 
ATOM   17006 O  OD1 . ASP C 1 606  ? 68.980  18.195  59.219  1.00 173.35 ? 606  ASP B OD1 1 
ATOM   17007 O  OD2 . ASP C 1 606  ? 68.327  16.751  60.747  1.00 173.25 ? 606  ASP B OD2 1 
ATOM   17008 N  N   . SER C 1 607  ? 68.195  21.335  59.302  1.00 185.66 ? 607  SER B N   1 
ATOM   17009 C  CA  . SER C 1 607  ? 67.043  21.979  58.676  1.00 182.38 ? 607  SER B CA  1 
ATOM   17010 C  C   . SER C 1 607  ? 65.775  21.169  58.854  1.00 179.07 ? 607  SER B C   1 
ATOM   17011 O  O   . SER C 1 607  ? 64.669  21.656  58.617  1.00 174.79 ? 607  SER B O   1 
ATOM   17012 C  CB  . SER C 1 607  ? 67.300  22.135  57.182  1.00 185.34 ? 607  SER B CB  1 
ATOM   17013 O  OG  . SER C 1 607  ? 67.489  20.859  56.581  1.00 188.64 ? 607  SER B OG  1 
ATOM   17014 N  N   . ALA C 1 608  ? 65.956  19.923  59.263  1.00 149.15 ? 608  ALA B N   1 
ATOM   17015 C  CA  . ALA C 1 608  ? 64.869  18.980  59.361  1.00 146.21 ? 608  ALA B CA  1 
ATOM   17016 C  C   . ALA C 1 608  ? 63.730  19.556  60.172  1.00 141.54 ? 608  ALA B C   1 
ATOM   17017 O  O   . ALA C 1 608  ? 62.614  19.708  59.684  1.00 136.85 ? 608  ALA B O   1 
ATOM   17018 C  CB  . ALA C 1 608  ? 65.366  17.692  59.982  1.00 153.68 ? 608  ALA B CB  1 
ATOM   17019 N  N   . VAL C 1 609  ? 64.029  19.873  61.417  1.00 160.83 ? 609  VAL B N   1 
ATOM   17020 C  CA  . VAL C 1 609  ? 63.053  20.469  62.302  1.00 156.95 ? 609  VAL B CA  1 
ATOM   17021 C  C   . VAL C 1 609  ? 61.981  21.222  61.528  1.00 151.95 ? 609  VAL B C   1 
ATOM   17022 O  O   . VAL C 1 609  ? 60.990  20.627  61.094  1.00 149.11 ? 609  VAL B O   1 
ATOM   17023 C  CB  . VAL C 1 609  ? 63.741  21.425  63.283  1.00 157.04 ? 609  VAL B CB  1 
ATOM   17024 C  CG1 . VAL C 1 609  ? 64.688  20.651  64.174  1.00 164.79 ? 609  VAL B CG1 1 
ATOM   17025 C  CG2 . VAL C 1 609  ? 64.522  22.488  62.541  1.00 154.79 ? 609  VAL B CG2 1 
ATOM   17026 N  N   . TYR C 1 610  ? 62.198  22.523  61.349  1.00 161.40 ? 610  TYR B N   1 
ATOM   17027 C  CA  . TYR C 1 610  ? 61.269  23.403  60.657  1.00 154.88 ? 610  TYR B CA  1 
ATOM   17028 C  C   . TYR C 1 610  ? 60.569  22.657  59.506  1.00 208.22 ? 610  TYR B C   1 
ATOM   17029 O  O   . TYR C 1 610  ? 59.532  22.014  59.712  1.00 201.60 ? 610  TYR B O   1 
ATOM   17030 C  CB  . TYR C 1 610  ? 62.020  24.634  60.123  1.00 151.66 ? 610  TYR B CB  1 
ATOM   17031 C  CG  . TYR C 1 610  ? 63.139  25.196  61.012  1.00 158.39 ? 610  TYR B CG  1 
ATOM   17032 C  CD1 . TYR C 1 610  ? 62.856  25.975  62.132  1.00 162.25 ? 610  TYR B CD1 1 
ATOM   17033 C  CD2 . TYR C 1 610  ? 64.481  24.988  60.697  1.00 158.62 ? 610  TYR B CD2 1 
ATOM   17034 C  CE1 . TYR C 1 610  ? 63.886  26.512  62.936  1.00 169.83 ? 610  TYR B CE1 1 
ATOM   17035 C  CE2 . TYR C 1 610  ? 65.518  25.514  61.497  1.00 166.54 ? 610  TYR B CE2 1 
ATOM   17036 C  CZ  . TYR C 1 610  ? 65.215  26.277  62.618  1.00 171.03 ? 610  TYR B CZ  1 
ATOM   17037 O  OH  . TYR C 1 610  ? 66.217  26.810  63.419  1.00 172.42 ? 610  TYR B OH  1 
ATOM   17038 N  N   . GLY C 1 611  ? 61.133  22.784  58.302  1.00 226.86 ? 611  GLY B N   1 
ATOM   17039 C  CA  . GLY C 1 611  ? 60.886  21.888  57.171  1.00 231.20 ? 611  GLY B CA  1 
ATOM   17040 C  C   . GLY C 1 611  ? 59.590  21.869  56.366  1.00 233.92 ? 611  GLY B C   1 
ATOM   17041 O  O   . GLY C 1 611  ? 59.361  22.719  55.499  1.00 231.95 ? 611  GLY B O   1 
ATOM   17042 N  N   . VAL C 1 612  ? 58.775  20.847  56.633  1.00 208.48 ? 612  VAL B N   1 
ATOM   17043 C  CA  . VAL C 1 612  ? 57.491  20.614  55.973  1.00 212.26 ? 612  VAL B CA  1 
ATOM   17044 C  C   . VAL C 1 612  ? 56.673  21.887  55.894  1.00 219.50 ? 612  VAL B C   1 
ATOM   17045 O  O   . VAL C 1 612  ? 55.994  22.270  56.846  1.00 221.70 ? 612  VAL B O   1 
ATOM   17046 C  CB  . VAL C 1 612  ? 56.664  19.543  56.723  1.00 294.59 ? 612  VAL B CB  1 
ATOM   17047 C  CG1 . VAL C 1 612  ? 57.189  18.149  56.418  1.00 297.42 ? 612  VAL B CG1 1 
ATOM   17048 C  CG2 . VAL C 1 612  ? 56.679  19.806  58.229  1.00 298.40 ? 612  VAL B CG2 1 
ATOM   17049 N  N   . GLN C 1 613  ? 56.730  22.531  54.739  1.00 282.08 ? 613  GLN B N   1 
ATOM   17050 C  CA  . GLN C 1 613  ? 56.158  23.854  54.580  1.00 289.12 ? 613  GLN B CA  1 
ATOM   17051 C  C   . GLN C 1 613  ? 56.636  24.751  55.717  1.00 301.24 ? 613  GLN B C   1 
ATOM   17052 O  O   . GLN C 1 613  ? 55.914  24.987  56.688  1.00 300.98 ? 613  GLN B O   1 
ATOM   17053 C  CB  . GLN C 1 613  ? 54.627  23.808  54.525  1.00 287.13 ? 613  GLN B CB  1 
ATOM   17054 C  CG  . GLN C 1 613  ? 53.998  25.189  54.366  1.00 281.89 ? 613  GLN B CG  1 
ATOM   17055 C  CD  . GLN C 1 613  ? 52.687  25.173  53.607  1.00 276.01 ? 613  GLN B CD  1 
ATOM   17056 O  OE1 . GLN C 1 613  ? 52.430  24.280  52.800  1.00 274.21 ? 613  GLN B OE1 1 
ATOM   17057 N  NE2 . GLN C 1 613  ? 51.853  26.177  53.855  1.00 272.97 ? 613  GLN B NE2 1 
ATOM   17058 N  N   . ARG C 1 614  ? 57.870  25.229  55.603  1.00 254.15 ? 614  ARG B N   1 
ATOM   17059 C  CA  . ARG C 1 614  ? 58.389  26.208  56.545  1.00 262.64 ? 614  ARG B CA  1 
ATOM   17060 C  C   . ARG C 1 614  ? 57.707  27.539  56.270  1.00 263.71 ? 614  ARG B C   1 
ATOM   17061 O  O   . ARG C 1 614  ? 58.156  28.309  55.419  1.00 263.57 ? 614  ARG B O   1 
ATOM   17062 C  CB  . ARG C 1 614  ? 59.902  26.341  56.397  1.00 266.28 ? 614  ARG B CB  1 
ATOM   17063 C  CG  . ARG C 1 614  ? 60.547  27.263  57.412  1.00 268.28 ? 614  ARG B CG  1 
ATOM   17064 C  CD  . ARG C 1 614  ? 61.957  26.804  57.697  1.00 272.53 ? 614  ARG B CD  1 
ATOM   17065 N  NE  . ARG C 1 614  ? 62.865  27.921  57.889  1.00 274.97 ? 614  ARG B NE  1 
ATOM   17066 C  CZ  . ARG C 1 614  ? 64.112  27.943  57.441  1.00 278.67 ? 614  ARG B CZ  1 
ATOM   17067 N  NH1 . ARG C 1 614  ? 64.596  26.904  56.776  1.00 279.51 ? 614  ARG B NH1 1 
ATOM   17068 N  NH2 . ARG C 1 614  ? 64.870  29.005  57.655  1.00 282.05 ? 614  ARG B NH2 1 
ATOM   17069 N  N   . GLY C 1 615  ? 56.622  27.797  56.995  1.00 410.83 ? 615  GLY B N   1 
ATOM   17070 C  CA  . GLY C 1 615  ? 55.750  28.925  56.719  1.00 409.29 ? 615  GLY B CA  1 
ATOM   17071 C  C   . GLY C 1 615  ? 56.438  30.128  56.103  1.00 412.19 ? 615  GLY B C   1 
ATOM   17072 O  O   . GLY C 1 615  ? 57.505  30.542  56.560  1.00 416.97 ? 615  GLY B O   1 
ATOM   17073 N  N   . ALA C 1 616  ? 55.820  30.688  55.065  1.00 282.19 ? 616  ALA B N   1 
ATOM   17074 C  CA  . ALA C 1 616  ? 56.350  31.872  54.406  1.00 283.21 ? 616  ALA B CA  1 
ATOM   17075 C  C   . ALA C 1 616  ? 56.774  32.914  55.440  1.00 286.62 ? 616  ALA B C   1 
ATOM   17076 O  O   . ALA C 1 616  ? 57.950  33.267  55.512  1.00 290.97 ? 616  ALA B O   1 
ATOM   17077 C  CB  . ALA C 1 616  ? 55.320  32.452  53.440  1.00 278.28 ? 616  ALA B CB  1 
ATOM   17078 N  N   . LYS C 1 617  ? 55.820  33.379  56.249  1.00 295.09 ? 617  LYS B N   1 
ATOM   17079 C  CA  . LYS C 1 617  ? 56.080  34.391  57.277  1.00 295.92 ? 617  LYS B CA  1 
ATOM   17080 C  C   . LYS C 1 617  ? 57.281  35.251  56.895  1.00 293.68 ? 617  LYS B C   1 
ATOM   17081 O  O   . LYS C 1 617  ? 57.225  35.961  55.895  1.00 291.63 ? 617  LYS B O   1 
ATOM   17082 C  CB  . LYS C 1 617  ? 56.284  33.747  58.650  1.00 302.20 ? 617  LYS B CB  1 
ATOM   17083 C  CG  . LYS C 1 617  ? 56.086  34.708  59.816  1.00 306.06 ? 617  LYS B CG  1 
ATOM   17084 C  CD  . LYS C 1 617  ? 54.746  35.418  59.710  1.00 302.57 ? 617  LYS B CD  1 
ATOM   17085 C  CE  . LYS C 1 617  ? 54.429  36.206  60.963  1.00 306.29 ? 617  LYS B CE  1 
ATOM   17086 N  NZ  . LYS C 1 617  ? 53.162  36.965  60.800  1.00 302.50 ? 617  LYS B NZ  1 
ATOM   17087 N  N   . LYS C 1 618  ? 58.357  35.175  57.684  1.00 263.03 ? 618  LYS B N   1 
ATOM   17088 C  CA  . LYS C 1 618  ? 59.651  35.784  57.329  1.00 260.62 ? 618  LYS B CA  1 
ATOM   17089 C  C   . LYS C 1 618  ? 60.805  35.347  58.252  1.00 254.89 ? 618  LYS B C   1 
ATOM   17090 O  O   . LYS C 1 618  ? 60.587  35.025  59.424  1.00 254.40 ? 618  LYS B O   1 
ATOM   17091 C  CB  . LYS C 1 618  ? 59.569  37.312  57.307  1.00 266.23 ? 618  LYS B CB  1 
ATOM   17092 C  CG  . LYS C 1 618  ? 58.717  37.929  56.207  1.00 265.41 ? 618  LYS B CG  1 
ATOM   17093 C  CD  . LYS C 1 618  ? 59.448  38.127  54.898  1.00 267.12 ? 618  LYS B CD  1 
ATOM   17094 C  CE  . LYS C 1 618  ? 58.657  39.066  53.990  1.00 262.88 ? 618  LYS B CE  1 
ATOM   17095 N  NZ  . LYS C 1 618  ? 57.179  38.841  54.055  1.00 258.13 ? 618  LYS B NZ  1 
ATOM   17096 N  N   . PRO C 1 619  ? 62.041  35.333  57.715  1.00 360.29 ? 619  PRO B N   1 
ATOM   17097 C  CA  . PRO C 1 619  ? 63.244  34.973  58.477  1.00 361.07 ? 619  PRO B CA  1 
ATOM   17098 C  C   . PRO C 1 619  ? 63.709  36.104  59.395  1.00 359.84 ? 619  PRO B C   1 
ATOM   17099 O  O   . PRO C 1 619  ? 63.581  35.986  60.613  1.00 362.21 ? 619  PRO B O   1 
ATOM   17100 C  CB  . PRO C 1 619  ? 64.297  34.729  57.385  1.00 364.03 ? 619  PRO B CB  1 
ATOM   17101 C  CG  . PRO C 1 619  ? 63.536  34.664  56.088  1.00 359.07 ? 619  PRO B CG  1 
ATOM   17102 C  CD  . PRO C 1 619  ? 62.345  35.542  56.291  1.00 355.94 ? 619  PRO B CD  1 
ATOM   17103 N  N   . LEU C 1 620  ? 64.250  37.174  58.813  1.00 284.82 ? 620  LEU B N   1 
ATOM   17104 C  CA  . LEU C 1 620  ? 64.716  38.331  59.587  1.00 284.01 ? 620  LEU B CA  1 
ATOM   17105 C  C   . LEU C 1 620  ? 63.559  39.216  60.063  1.00 281.00 ? 620  LEU B C   1 
ATOM   17106 O  O   . LEU C 1 620  ? 63.713  40.017  60.990  1.00 285.64 ? 620  LEU B O   1 
ATOM   17107 C  CB  . LEU C 1 620  ? 65.719  39.163  58.779  1.00 281.03 ? 620  LEU B CB  1 
ATOM   17108 C  CG  . LEU C 1 620  ? 65.997  40.591  59.268  1.00 281.03 ? 620  LEU B CG  1 
ATOM   17109 C  CD1 . LEU C 1 620  ? 66.835  40.591  60.531  1.00 288.01 ? 620  LEU B CD1 1 
ATOM   17110 C  CD2 . LEU C 1 620  ? 66.671  41.410  58.182  1.00 279.95 ? 620  LEU B CD2 1 
ATOM   17111 N  N   . GLU C 1 621  ? 62.404  39.068  59.416  1.00 246.94 ? 621  GLU B N   1 
ATOM   17112 C  CA  . GLU C 1 621  ? 61.198  39.803  59.796  1.00 244.23 ? 621  GLU B CA  1 
ATOM   17113 C  C   . GLU C 1 621  ? 60.603  39.269  61.115  1.00 241.23 ? 621  GLU B C   1 
ATOM   17114 O  O   . GLU C 1 621  ? 60.126  40.053  61.941  1.00 241.94 ? 621  GLU B O   1 
ATOM   17115 C  CB  . GLU C 1 621  ? 60.185  39.795  58.635  1.00 242.99 ? 621  GLU B CB  1 
ATOM   17116 C  CG  . GLU C 1 621  ? 58.757  40.232  58.956  1.00 244.95 ? 621  GLU B CG  1 
ATOM   17117 C  CD  . GLU C 1 621  ? 57.802  40.069  57.771  1.00 241.79 ? 621  GLU B CD  1 
ATOM   17118 O  OE1 . GLU C 1 621  ? 58.128  40.551  56.666  1.00 240.94 ? 621  GLU B OE1 1 
ATOM   17119 O  OE2 . GLU C 1 621  ? 56.728  39.446  57.936  1.00 239.42 ? 621  GLU B OE2 1 
ATOM   17120 N  N   . ARG C 1 622  ? 60.663  37.947  61.315  1.00 207.30 ? 622  ARG B N   1 
ATOM   17121 C  CA  . ARG C 1 622  ? 60.258  37.312  62.576  1.00 203.70 ? 622  ARG B CA  1 
ATOM   17122 C  C   . ARG C 1 622  ? 60.618  38.267  63.712  1.00 202.50 ? 622  ARG B C   1 
ATOM   17123 O  O   . ARG C 1 622  ? 59.755  38.748  64.454  1.00 202.51 ? 622  ARG B O   1 
ATOM   17124 C  CB  . ARG C 1 622  ? 60.980  35.960  62.741  1.00 207.26 ? 622  ARG B CB  1 
ATOM   17125 C  CG  . ARG C 1 622  ? 60.391  35.025  63.791  1.00 208.55 ? 622  ARG B CG  1 
ATOM   17126 C  CD  . ARG C 1 622  ? 60.913  33.585  63.641  1.00 193.82 ? 622  ARG B CD  1 
ATOM   17127 N  NE  . ARG C 1 622  ? 62.300  33.422  64.081  1.00 201.21 ? 622  ARG B NE  1 
ATOM   17128 C  CZ  . ARG C 1 622  ? 62.926  32.249  64.193  1.00 203.80 ? 622  ARG B CZ  1 
ATOM   17129 N  NH1 . ARG C 1 622  ? 62.297  31.115  63.904  1.00 201.25 ? 622  ARG B NH1 1 
ATOM   17130 N  NH2 . ARG C 1 622  ? 64.189  32.210  64.600  1.00 208.79 ? 622  ARG B NH2 1 
ATOM   17131 N  N   . VAL C 1 623  ? 61.904  38.573  63.803  1.00 240.82 ? 623  VAL B N   1 
ATOM   17132 C  CA  . VAL C 1 623  ? 62.393  39.560  64.744  1.00 241.71 ? 623  VAL B CA  1 
ATOM   17133 C  C   . VAL C 1 623  ? 61.837  40.960  64.457  1.00 234.64 ? 623  VAL B C   1 
ATOM   17134 O  O   . VAL C 1 623  ? 61.158  41.540  65.299  1.00 235.47 ? 623  VAL B O   1 
ATOM   17135 C  CB  . VAL C 1 623  ? 63.924  39.570  64.754  1.00 203.91 ? 623  VAL B CB  1 
ATOM   17136 C  CG1 . VAL C 1 623  ? 64.443  40.909  65.233  1.00 207.13 ? 623  VAL B CG1 1 
ATOM   17137 C  CG2 . VAL C 1 623  ? 64.453  38.410  65.613  1.00 206.27 ? 623  VAL B CG2 1 
ATOM   17138 N  N   . PHE C 1 624  ? 62.101  41.490  63.267  1.00 264.91 ? 624  PHE B N   1 
ATOM   17139 C  CA  . PHE C 1 624  ? 61.666  42.846  62.927  1.00 258.20 ? 624  PHE B CA  1 
ATOM   17140 C  C   . PHE C 1 624  ? 60.181  43.112  63.204  1.00 258.49 ? 624  PHE B C   1 
ATOM   17141 O  O   . PHE C 1 624  ? 59.789  44.257  63.416  1.00 259.33 ? 624  PHE B O   1 
ATOM   17142 C  CB  . PHE C 1 624  ? 62.004  43.192  61.471  1.00 244.44 ? 624  PHE B CB  1 
ATOM   17143 C  CG  . PHE C 1 624  ? 63.130  44.196  61.320  1.00 238.06 ? 624  PHE B CG  1 
ATOM   17144 C  CD1 . PHE C 1 624  ? 64.195  43.948  60.455  1.00 234.77 ? 624  PHE B CD1 1 
ATOM   17145 C  CD2 . PHE C 1 624  ? 63.121  45.388  62.031  1.00 236.53 ? 624  PHE B CD2 1 
ATOM   17146 C  CE1 . PHE C 1 624  ? 65.231  44.870  60.307  1.00 236.43 ? 624  PHE B CE1 1 
ATOM   17147 C  CE2 . PHE C 1 624  ? 64.155  46.310  61.891  1.00 237.93 ? 624  PHE B CE2 1 
ATOM   17148 C  CZ  . PHE C 1 624  ? 65.209  46.052  61.028  1.00 238.56 ? 624  PHE B CZ  1 
ATOM   17149 N  N   . GLN C 1 625  ? 59.356  42.067  63.193  1.00 215.31 ? 625  GLN B N   1 
ATOM   17150 C  CA  . GLN C 1 625  ? 57.955  42.212  63.577  1.00 217.76 ? 625  GLN B CA  1 
ATOM   17151 C  C   . GLN C 1 625  ? 57.928  42.561  65.039  1.00 221.60 ? 625  GLN B C   1 
ATOM   17152 O  O   . GLN C 1 625  ? 57.813  43.724  65.418  1.00 222.89 ? 625  GLN B O   1 
ATOM   17153 C  CB  . GLN C 1 625  ? 57.182  40.909  63.382  1.00 222.72 ? 625  GLN B CB  1 
ATOM   17154 C  CG  . GLN C 1 625  ? 57.148  40.395  61.955  1.00 225.85 ? 625  GLN B CG  1 
ATOM   17155 C  CD  . GLN C 1 625  ? 56.003  39.422  61.705  1.00 229.49 ? 625  GLN B CD  1 
ATOM   17156 O  OE1 . GLN C 1 625  ? 55.006  39.431  62.425  1.00 231.88 ? 625  GLN B OE1 1 
ATOM   17157 N  NE2 . GLN C 1 625  ? 56.137  38.587  60.672  1.00 229.34 ? 625  GLN B NE2 1 
ATOM   17158 N  N   . PHE C 1 626  ? 58.056  41.530  65.859  1.00 226.01 ? 626  PHE B N   1 
ATOM   17159 C  CA  . PHE C 1 626  ? 58.162  41.714  67.289  1.00 229.76 ? 626  PHE B CA  1 
ATOM   17160 C  C   . PHE C 1 626  ? 58.938  43.001  67.601  1.00 224.24 ? 626  PHE B C   1 
ATOM   17161 O  O   . PHE C 1 626  ? 58.371  43.988  68.064  1.00 221.46 ? 626  PHE B O   1 
ATOM   17162 C  CB  . PHE C 1 626  ? 58.857  40.498  67.900  1.00 239.46 ? 626  PHE B CB  1 
ATOM   17163 C  CG  . PHE C 1 626  ? 59.276  40.690  69.327  1.00 252.78 ? 626  PHE B CG  1 
ATOM   17164 C  CD1 . PHE C 1 626  ? 58.458  40.272  70.366  1.00 257.45 ? 626  PHE B CD1 1 
ATOM   17165 C  CD2 . PHE C 1 626  ? 60.498  41.283  69.633  1.00 260.22 ? 626  PHE B CD2 1 
ATOM   17166 C  CE1 . PHE C 1 626  ? 58.848  40.447  71.690  1.00 265.85 ? 626  PHE B CE1 1 
ATOM   17167 C  CE2 . PHE C 1 626  ? 60.895  41.462  70.950  1.00 268.75 ? 626  PHE B CE2 1 
ATOM   17168 C  CZ  . PHE C 1 626  ? 60.071  41.043  71.983  1.00 271.35 ? 626  PHE B CZ  1 
ATOM   17169 N  N   . LEU C 1 627  ? 60.226  42.998  67.290  1.00 167.68 ? 627  LEU B N   1 
ATOM   17170 C  CA  . LEU C 1 627  ? 61.148  44.032  67.744  1.00 167.51 ? 627  LEU B CA  1 
ATOM   17171 C  C   . LEU C 1 627  ? 60.657  45.469  67.575  1.00 164.95 ? 627  LEU B C   1 
ATOM   17172 O  O   . LEU C 1 627  ? 61.238  46.390  68.126  1.00 172.94 ? 627  LEU B O   1 
ATOM   17173 C  CB  . LEU C 1 627  ? 62.508  43.825  67.075  1.00 163.87 ? 627  LEU B CB  1 
ATOM   17174 C  CG  . LEU C 1 627  ? 63.602  44.890  67.018  1.00 162.81 ? 627  LEU B CG  1 
ATOM   17175 C  CD1 . LEU C 1 627  ? 64.948  44.207  66.790  1.00 165.86 ? 627  LEU B CD1 1 
ATOM   17176 C  CD2 . LEU C 1 627  ? 63.318  45.932  65.933  1.00 156.31 ? 627  LEU B CD2 1 
ATOM   17177 N  N   . GLU C 1 628  ? 59.598  45.682  66.817  1.00 216.73 ? 628  GLU B N   1 
ATOM   17178 C  CA  . GLU C 1 628  ? 59.041  47.017  66.786  1.00 214.62 ? 628  GLU B CA  1 
ATOM   17179 C  C   . GLU C 1 628  ? 57.594  46.983  67.209  1.00 210.99 ? 628  GLU B C   1 
ATOM   17180 O  O   . GLU C 1 628  ? 56.702  47.382  66.460  1.00 206.39 ? 628  GLU B O   1 
ATOM   17181 C  CB  . GLU C 1 628  ? 59.204  47.700  65.425  1.00 213.72 ? 628  GLU B CB  1 
ATOM   17182 C  CG  . GLU C 1 628  ? 58.334  47.128  64.320  1.00 236.32 ? 628  GLU B CG  1 
ATOM   17183 C  CD  . GLU C 1 628  ? 58.078  48.124  63.203  1.00 234.78 ? 628  GLU B CD  1 
ATOM   17184 O  OE1 . GLU C 1 628  ? 57.759  49.297  63.516  1.00 237.61 ? 628  GLU B OE1 1 
ATOM   17185 O  OE2 . GLU C 1 628  ? 58.189  47.726  62.019  1.00 230.20 ? 628  GLU B OE2 1 
ATOM   17186 N  N   . LYS C 1 629  ? 57.363  46.474  68.411  1.00 166.04 ? 629  LYS B N   1 
ATOM   17187 C  CA  . LYS C 1 629  ? 56.085  46.689  69.071  1.00 163.31 ? 629  LYS B CA  1 
ATOM   17188 C  C   . LYS C 1 629  ? 56.329  47.817  70.040  1.00 165.87 ? 629  LYS B C   1 
ATOM   17189 O  O   . LYS C 1 629  ? 55.450  48.271  70.765  1.00 162.54 ? 629  LYS B O   1 
ATOM   17190 C  CB  . LYS C 1 629  ? 55.570  45.412  69.727  1.00 164.26 ? 629  LYS B CB  1 
ATOM   17191 C  CG  . LYS C 1 629  ? 55.295  44.342  68.678  1.00 158.63 ? 629  LYS B CG  1 
ATOM   17192 C  CD  . LYS C 1 629  ? 55.193  44.988  67.274  1.00 177.15 ? 629  LYS B CD  1 
ATOM   17193 C  CE  . LYS C 1 629  ? 55.166  43.982  66.131  1.00 157.07 ? 629  LYS B CE  1 
ATOM   17194 N  NZ  . LYS C 1 629  ? 55.210  44.703  64.828  1.00 150.95 ? 629  LYS B NZ  1 
ATOM   17195 N  N   . SER C 1 630  ? 57.570  48.267  69.985  1.00 130.75 ? 630  SER B N   1 
ATOM   17196 C  CA  . SER C 1 630  ? 58.024  49.467  70.638  1.00 135.71 ? 630  SER B CA  1 
ATOM   17197 C  C   . SER C 1 630  ? 57.455  50.706  69.974  1.00 134.74 ? 630  SER B C   1 
ATOM   17198 O  O   . SER C 1 630  ? 57.724  51.826  70.390  1.00 133.16 ? 630  SER B O   1 
ATOM   17199 C  CB  . SER C 1 630  ? 59.546  49.531  70.580  1.00 136.85 ? 630  SER B CB  1 
ATOM   17200 O  OG  . SER C 1 630  ? 60.017  49.594  69.246  1.00 135.63 ? 630  SER B OG  1 
ATOM   17201 N  N   . ASP C 1 631  ? 56.706  50.528  68.903  1.00 201.88 ? 631  ASP B N   1 
ATOM   17202 C  CA  . ASP C 1 631  ? 56.053  51.685  68.331  1.00 199.84 ? 631  ASP B CA  1 
ATOM   17203 C  C   . ASP C 1 631  ? 54.938  51.976  69.308  1.00 201.68 ? 631  ASP B C   1 
ATOM   17204 O  O   . ASP C 1 631  ? 54.011  51.180  69.476  1.00 197.89 ? 631  ASP B O   1 
ATOM   17205 C  CB  . ASP C 1 631  ? 55.541  51.425  66.906  1.00 197.95 ? 631  ASP B CB  1 
ATOM   17206 C  CG  . ASP C 1 631  ? 55.468  52.699  66.059  1.00 207.86 ? 631  ASP B CG  1 
ATOM   17207 O  OD1 . ASP C 1 631  ? 54.368  53.284  65.971  1.00 208.36 ? 631  ASP B OD1 1 
ATOM   17208 O  OD2 . ASP C 1 631  ? 56.504  53.107  65.477  1.00 212.28 ? 631  ASP B OD2 1 
ATOM   17209 N  N   . LEU C 1 632  ? 55.083  53.100  69.996  1.00 181.57 ? 632  LEU B N   1 
ATOM   17210 C  CA  . LEU C 1 632  ? 54.144  53.512  71.027  1.00 183.82 ? 632  LEU B CA  1 
ATOM   17211 C  C   . LEU C 1 632  ? 52.785  53.826  70.374  1.00 176.50 ? 632  LEU B C   1 
ATOM   17212 O  O   . LEU C 1 632  ? 51.730  53.400  70.859  1.00 176.32 ? 632  LEU B O   1 
ATOM   17213 C  CB  . LEU C 1 632  ? 54.720  54.717  71.811  1.00 192.05 ? 632  LEU B CB  1 
ATOM   17214 C  CG  . LEU C 1 632  ? 56.139  54.599  72.415  1.00 197.70 ? 632  LEU B CG  1 
ATOM   17215 C  CD1 . LEU C 1 632  ? 56.780  55.950  72.721  1.00 200.74 ? 632  LEU B CD1 1 
ATOM   17216 C  CD2 . LEU C 1 632  ? 56.150  53.716  73.650  1.00 202.62 ? 632  LEU B CD2 1 
ATOM   17217 N  N   . GLY C 1 633  ? 52.825  54.538  69.249  1.00 194.75 ? 633  GLY B N   1 
ATOM   17218 C  CA  . GLY C 1 633  ? 51.621  54.965  68.563  1.00 185.45 ? 633  GLY B CA  1 
ATOM   17219 C  C   . GLY C 1 633  ? 50.937  53.870  67.782  1.00 173.67 ? 633  GLY B C   1 
ATOM   17220 O  O   . GLY C 1 633  ? 51.281  52.693  67.901  1.00 173.74 ? 633  GLY B O   1 
ATOM   17221 N  N   . CYS C 1 634  ? 49.974  54.265  66.961  1.00 158.67 ? 634  CYS B N   1 
ATOM   17222 C  CA  . CYS C 1 634  ? 49.183  53.296  66.228  1.00 154.16 ? 634  CYS B CA  1 
ATOM   17223 C  C   . CYS C 1 634  ? 48.385  53.857  65.045  1.00 150.51 ? 634  CYS B C   1 
ATOM   17224 O  O   . CYS C 1 634  ? 48.182  55.063  64.938  1.00 155.41 ? 634  CYS B O   1 
ATOM   17225 C  CB  . CYS C 1 634  ? 48.231  52.605  67.181  1.00 156.58 ? 634  CYS B CB  1 
ATOM   17226 S  SG  . CYS C 1 634  ? 47.297  51.309  66.396  1.00 187.05 ? 634  CYS B SG  1 
ATOM   17227 N  N   . GLY C 1 635  ? 47.936  52.966  64.161  1.00 177.07 ? 635  GLY B N   1 
ATOM   17228 C  CA  . GLY C 1 635  ? 47.079  53.333  63.045  1.00 169.96 ? 635  GLY B CA  1 
ATOM   17229 C  C   . GLY C 1 635  ? 47.701  53.379  61.658  1.00 167.37 ? 635  GLY B C   1 
ATOM   17230 O  O   . GLY C 1 635  ? 48.883  53.057  61.454  1.00 168.08 ? 635  GLY B O   1 
ATOM   17231 N  N   . ALA C 1 636  ? 46.867  53.752  60.691  1.00 176.41 ? 636  ALA B N   1 
ATOM   17232 C  CA  . ALA C 1 636  ? 47.343  54.169  59.388  1.00 173.41 ? 636  ALA B CA  1 
ATOM   17233 C  C   . ALA C 1 636  ? 47.952  55.552  59.592  1.00 174.87 ? 636  ALA B C   1 
ATOM   17234 O  O   . ALA C 1 636  ? 48.626  56.102  58.717  1.00 174.49 ? 636  ALA B O   1 
ATOM   17235 C  CB  . ALA C 1 636  ? 46.187  54.232  58.411  1.00 172.04 ? 636  ALA B CB  1 
ATOM   17236 N  N   . GLY C 1 637  ? 47.694  56.103  60.775  1.00 172.60 ? 637  GLY B N   1 
ATOM   17237 C  CA  . GLY C 1 637  ? 48.228  57.390  61.185  1.00 178.22 ? 637  GLY B CA  1 
ATOM   17238 C  C   . GLY C 1 637  ? 47.137  58.366  61.592  1.00 184.11 ? 637  GLY B C   1 
ATOM   17239 O  O   . GLY C 1 637  ? 45.951  58.064  61.442  1.00 178.42 ? 637  GLY B O   1 
ATOM   17240 N  N   . GLY C 1 638  ? 47.542  59.513  62.138  1.00 151.16 ? 638  GLY B N   1 
ATOM   17241 C  CA  . GLY C 1 638  ? 46.679  60.680  62.285  1.00 153.11 ? 638  GLY B CA  1 
ATOM   17242 C  C   . GLY C 1 638  ? 45.356  60.524  63.007  1.00 152.18 ? 638  GLY B C   1 
ATOM   17243 O  O   . GLY C 1 638  ? 44.635  59.555  62.800  1.00 153.31 ? 638  GLY B O   1 
ATOM   17244 N  N   . GLY C 1 639  ? 45.017  61.515  63.822  1.00 202.75 ? 639  GLY B N   1 
ATOM   17245 C  CA  . GLY C 1 639  ? 43.883  61.411  64.721  1.00 201.59 ? 639  GLY B CA  1 
ATOM   17246 C  C   . GLY C 1 639  ? 42.538  62.030  64.352  1.00 199.41 ? 639  GLY B C   1 
ATOM   17247 O  O   . GLY C 1 639  ? 41.994  61.814  63.254  1.00 190.36 ? 639  GLY B O   1 
ATOM   17248 N  N   . LEU C 1 640  ? 42.014  62.806  65.307  1.00 130.30 ? 640  LEU B N   1 
ATOM   17249 C  CA  . LEU C 1 640  ? 40.610  63.230  65.368  1.00 129.19 ? 640  LEU B CA  1 
ATOM   17250 C  C   . LEU C 1 640  ? 40.600  64.608  66.049  1.00 132.64 ? 640  LEU B C   1 
ATOM   17251 O  O   . LEU C 1 640  ? 39.706  65.430  65.820  1.00 132.08 ? 640  LEU B O   1 
ATOM   17252 C  CB  . LEU C 1 640  ? 39.791  62.167  66.148  1.00 129.34 ? 640  LEU B CB  1 
ATOM   17253 C  CG  . LEU C 1 640  ? 38.274  62.025  66.420  1.00 116.99 ? 640  LEU B CG  1 
ATOM   17254 C  CD1 . LEU C 1 640  ? 37.367  62.863  65.504  1.00 118.22 ? 640  LEU B CD1 1 
ATOM   17255 C  CD2 . LEU C 1 640  ? 37.882  60.522  66.431  1.00 117.20 ? 640  LEU B CD2 1 
ATOM   17256 N  N   . ASN C 1 641  ? 41.637  64.840  66.861  1.00 166.26 ? 641  ASN B N   1 
ATOM   17257 C  CA  . ASN C 1 641  ? 41.978  66.144  67.430  1.00 170.24 ? 641  ASN B CA  1 
ATOM   17258 C  C   . ASN C 1 641  ? 43.466  66.256  67.352  1.00 173.99 ? 641  ASN B C   1 
ATOM   17259 O  O   . ASN C 1 641  ? 44.153  65.249  67.497  1.00 175.33 ? 641  ASN B O   1 
ATOM   17260 C  CB  . ASN C 1 641  ? 41.639  66.168  68.894  1.00 178.71 ? 641  ASN B CB  1 
ATOM   17261 C  CG  . ASN C 1 641  ? 40.667  65.095  69.252  1.00 180.97 ? 641  ASN B CG  1 
ATOM   17262 O  OD1 . ASN C 1 641  ? 39.560  65.069  68.723  1.00 178.33 ? 641  ASN B OD1 1 
ATOM   17263 N  ND2 . ASN C 1 641  ? 41.071  64.178  70.130  1.00 185.92 ? 641  ASN B ND2 1 
ATOM   17264 N  N   . ASN C 1 642  ? 43.976  67.468  67.147  1.00 209.90 ? 642  ASN B N   1 
ATOM   17265 C  CA  . ASN C 1 642  ? 45.416  67.646  67.026  1.00 213.15 ? 642  ASN B CA  1 
ATOM   17266 C  C   . ASN C 1 642  ? 46.036  66.906  68.182  1.00 216.12 ? 642  ASN B C   1 
ATOM   17267 O  O   . ASN C 1 642  ? 47.158  66.397  68.119  1.00 213.58 ? 642  ASN B O   1 
ATOM   17268 C  CB  . ASN C 1 642  ? 45.809  69.116  67.077  1.00 222.13 ? 642  ASN B CB  1 
ATOM   17269 C  CG  . ASN C 1 642  ? 47.303  69.302  67.200  1.00 230.49 ? 642  ASN B CG  1 
ATOM   17270 O  OD1 . ASN C 1 642  ? 47.775  70.148  67.954  1.00 239.21 ? 642  ASN B OD1 1 
ATOM   17271 N  ND2 . ASN C 1 642  ? 48.060  68.490  66.477  1.00 228.30 ? 642  ASN B ND2 1 
ATOM   17272 N  N   . ALA C 1 643  ? 45.258  66.841  69.248  1.00 183.42 ? 643  ALA B N   1 
ATOM   17273 C  CA  . ALA C 1 643  ? 45.569  65.965  70.344  1.00 188.78 ? 643  ALA B CA  1 
ATOM   17274 C  C   . ALA C 1 643  ? 45.551  64.503  69.866  1.00 178.76 ? 643  ALA B C   1 
ATOM   17275 O  O   . ALA C 1 643  ? 46.588  63.844  69.872  1.00 176.26 ? 643  ALA B O   1 
ATOM   17276 C  CB  . ALA C 1 643  ? 44.584  66.199  71.475  1.00 197.68 ? 643  ALA B CB  1 
ATOM   17277 N  N   . ASN C 1 644  ? 44.396  64.000  69.430  1.00 163.37 ? 644  ASN B N   1 
ATOM   17278 C  CA  . ASN C 1 644  ? 44.299  62.604  68.996  1.00 158.66 ? 644  ASN B CA  1 
ATOM   17279 C  C   . ASN C 1 644  ? 45.383  62.268  67.969  1.00 157.47 ? 644  ASN B C   1 
ATOM   17280 O  O   . ASN C 1 644  ? 45.978  61.193  68.017  1.00 161.15 ? 644  ASN B O   1 
ATOM   17281 C  CB  . ASN C 1 644  ? 42.888  62.290  68.461  1.00 150.80 ? 644  ASN B CB  1 
ATOM   17282 C  CG  . ASN C 1 644  ? 42.652  60.787  68.215  1.00 146.90 ? 644  ASN B CG  1 
ATOM   17283 O  OD1 . ASN C 1 644  ? 41.534  60.348  67.898  1.00 141.87 ? 644  ASN B OD1 1 
ATOM   17284 N  ND2 . ASN C 1 644  ? 43.708  60.002  68.355  1.00 149.59 ? 644  ASN B ND2 1 
ATOM   17285 N  N   . VAL C 1 645  ? 45.648  63.194  67.054  1.00 211.58 ? 645  VAL B N   1 
ATOM   17286 C  CA  . VAL C 1 645  ? 46.692  63.014  66.046  1.00 208.73 ? 645  VAL B CA  1 
ATOM   17287 C  C   . VAL C 1 645  ? 48.073  62.821  66.667  1.00 214.62 ? 645  VAL B C   1 
ATOM   17288 O  O   . VAL C 1 645  ? 48.817  61.922  66.282  1.00 212.41 ? 645  VAL B O   1 
ATOM   17289 C  CB  . VAL C 1 645  ? 46.760  64.224  65.109  1.00 208.88 ? 645  VAL B CB  1 
ATOM   17290 C  CG1 . VAL C 1 645  ? 47.842  64.018  64.067  1.00 207.32 ? 645  VAL B CG1 1 
ATOM   17291 C  CG2 . VAL C 1 645  ? 45.416  64.452  64.453  1.00 203.12 ? 645  VAL B CG2 1 
ATOM   17292 N  N   . PHE C 1 646  ? 48.403  63.688  67.620  1.00 160.69 ? 646  PHE B N   1 
ATOM   17293 C  CA  . PHE C 1 646  ? 49.624  63.600  68.413  1.00 164.12 ? 646  PHE B CA  1 
ATOM   17294 C  C   . PHE C 1 646  ? 49.682  62.389  69.315  1.00 168.54 ? 646  PHE B C   1 
ATOM   17295 O  O   . PHE C 1 646  ? 50.757  61.873  69.635  1.00 170.90 ? 646  PHE B O   1 
ATOM   17296 C  CB  . PHE C 1 646  ? 49.680  64.807  69.310  1.00 168.11 ? 646  PHE B CB  1 
ATOM   17297 C  CG  . PHE C 1 646  ? 50.547  65.867  68.796  1.00 165.05 ? 646  PHE B CG  1 
ATOM   17298 C  CD1 . PHE C 1 646  ? 50.019  67.086  68.427  1.00 160.86 ? 646  PHE B CD1 1 
ATOM   17299 C  CD2 . PHE C 1 646  ? 51.905  65.642  68.662  1.00 164.72 ? 646  PHE B CD2 1 
ATOM   17300 C  CE1 . PHE C 1 646  ? 50.840  68.084  67.949  1.00 160.73 ? 646  PHE B CE1 1 
ATOM   17301 C  CE2 . PHE C 1 646  ? 52.735  66.627  68.186  1.00 164.26 ? 646  PHE B CE2 1 
ATOM   17302 C  CZ  . PHE C 1 646  ? 52.203  67.855  67.825  1.00 162.45 ? 646  PHE B CZ  1 
ATOM   17303 N  N   . HIS C 1 647  ? 48.507  61.981  69.767  1.00 197.56 ? 647  HIS B N   1 
ATOM   17304 C  CA  . HIS C 1 647  ? 48.388  60.825  70.613  1.00 201.78 ? 647  HIS B CA  1 
ATOM   17305 C  C   . HIS C 1 647  ? 48.804  59.638  69.775  1.00 187.75 ? 647  HIS B C   1 
ATOM   17306 O  O   . HIS C 1 647  ? 49.911  59.137  69.933  1.00 187.34 ? 647  HIS B O   1 
ATOM   17307 C  CB  . HIS C 1 647  ? 46.946  60.669  71.092  1.00 211.19 ? 647  HIS B CB  1 
ATOM   17308 C  CG  . HIS C 1 647  ? 46.815  59.812  72.309  1.00 227.17 ? 647  HIS B CG  1 
ATOM   17309 N  ND1 . HIS C 1 647  ? 47.585  58.704  72.551  1.00 232.20 ? 647  HIS B ND1 1 
ATOM   17310 C  CD2 . HIS C 1 647  ? 45.943  59.900  73.362  1.00 237.04 ? 647  HIS B CD2 1 
ATOM   17311 C  CE1 . HIS C 1 647  ? 47.228  58.145  73.685  1.00 238.85 ? 647  HIS B CE1 1 
ATOM   17312 N  NE2 . HIS C 1 647  ? 46.243  58.847  74.200  1.00 242.36 ? 647  HIS B NE2 1 
ATOM   17313 N  N   . LEU C 1 648  ? 47.941  59.222  68.849  1.00 150.45 ? 648  LEU B N   1 
ATOM   17314 C  CA  . LEU C 1 648  ? 48.168  57.997  68.072  1.00 143.73 ? 648  LEU B CA  1 
ATOM   17315 C  C   . LEU C 1 648  ? 49.548  57.954  67.481  1.00 141.43 ? 648  LEU B C   1 
ATOM   17316 O  O   . LEU C 1 648  ? 50.007  56.924  67.001  1.00 139.35 ? 648  LEU B O   1 
ATOM   17317 C  CB  . LEU C 1 648  ? 47.133  57.850  66.969  1.00 133.84 ? 648  LEU B CB  1 
ATOM   17318 C  CG  . LEU C 1 648  ? 45.942  57.010  67.429  1.00 130.12 ? 648  LEU B CG  1 
ATOM   17319 C  CD1 . LEU C 1 648  ? 44.645  57.568  66.871  1.00 124.67 ? 648  LEU B CD1 1 
ATOM   17320 C  CD2 . LEU C 1 648  ? 46.116  55.522  67.094  1.00 126.37 ? 648  LEU B CD2 1 
ATOM   17321 N  N   . ALA C 1 649  ? 50.206  59.096  67.524  1.00 146.35 ? 649  ALA B N   1 
ATOM   17322 C  CA  . ALA C 1 649  ? 51.586  59.192  67.111  1.00 145.55 ? 649  ALA B CA  1 
ATOM   17323 C  C   . ALA C 1 649  ? 52.472  58.528  68.141  1.00 148.60 ? 649  ALA B C   1 
ATOM   17324 O  O   . ALA C 1 649  ? 53.689  58.548  68.018  1.00 148.28 ? 649  ALA B O   1 
ATOM   17325 C  CB  . ALA C 1 649  ? 51.969  60.656  66.977  1.00 151.13 ? 649  ALA B CB  1 
ATOM   17326 N  N   . GLY C 1 650  ? 51.864  57.944  69.165  1.00 212.54 ? 650  GLY B N   1 
ATOM   17327 C  CA  . GLY C 1 650  ? 52.628  57.462  70.298  1.00 220.25 ? 650  GLY B CA  1 
ATOM   17328 C  C   . GLY C 1 650  ? 53.239  58.622  71.057  1.00 228.34 ? 650  GLY B C   1 
ATOM   17329 O  O   . GLY C 1 650  ? 54.054  58.433  71.964  1.00 232.25 ? 650  GLY B O   1 
ATOM   17330 N  N   . LEU C 1 651  ? 52.850  59.830  70.669  1.00 183.45 ? 651  LEU B N   1 
ATOM   17331 C  CA  . LEU C 1 651  ? 53.288  61.015  71.371  1.00 192.79 ? 651  LEU B CA  1 
ATOM   17332 C  C   . LEU C 1 651  ? 52.274  61.513  72.384  1.00 197.69 ? 651  LEU B C   1 
ATOM   17333 O  O   . LEU C 1 651  ? 51.087  61.179  72.334  1.00 194.17 ? 651  LEU B O   1 
ATOM   17334 C  CB  . LEU C 1 651  ? 53.561  62.153  70.383  1.00 189.94 ? 651  LEU B CB  1 
ATOM   17335 C  CG  . LEU C 1 651  ? 54.918  62.181  69.696  1.00 188.20 ? 651  LEU B CG  1 
ATOM   17336 C  CD1 . LEU C 1 651  ? 55.101  63.530  69.039  1.00 186.28 ? 651  LEU B CD1 1 
ATOM   17337 C  CD2 . LEU C 1 651  ? 56.022  61.922  70.697  1.00 196.18 ? 651  LEU B CD2 1 
ATOM   17338 N  N   . THR C 1 652  ? 52.789  62.297  73.325  1.00 164.01 ? 652  THR B N   1 
ATOM   17339 C  CA  . THR C 1 652  ? 52.049  63.423  73.878  1.00 165.71 ? 652  THR B CA  1 
ATOM   17340 C  C   . THR C 1 652  ? 53.062  64.568  74.113  1.00 167.67 ? 652  THR B C   1 
ATOM   17341 O  O   . THR C 1 652  ? 54.244  64.338  74.364  1.00 169.78 ? 652  THR B O   1 
ATOM   17342 C  CB  . THR C 1 652  ? 51.099  63.033  75.055  1.00 168.03 ? 652  THR B CB  1 
ATOM   17343 O  OG1 . THR C 1 652  ? 49.906  63.835  75.011  1.00 166.69 ? 652  THR B OG1 1 
ATOM   17344 C  CG2 . THR C 1 652  ? 51.780  63.181  76.385  1.00 177.47 ? 652  THR B CG2 1 
ATOM   17345 N  N   . PHE C 1 653  ? 52.573  65.794  73.989  1.00 173.08 ? 653  PHE B N   1 
ATOM   17346 C  CA  . PHE C 1 653  ? 53.365  66.960  73.622  1.00 179.04 ? 653  PHE B CA  1 
ATOM   17347 C  C   . PHE C 1 653  ? 53.072  68.072  74.593  1.00 189.30 ? 653  PHE B C   1 
ATOM   17348 O  O   . PHE C 1 653  ? 51.987  68.128  75.174  1.00 188.11 ? 653  PHE B O   1 
ATOM   17349 C  CB  . PHE C 1 653  ? 52.833  67.441  72.308  1.00 174.99 ? 653  PHE B CB  1 
ATOM   17350 C  CG  . PHE C 1 653  ? 51.332  67.549  72.297  1.00 175.89 ? 653  PHE B CG  1 
ATOM   17351 C  CD1 . PHE C 1 653  ? 50.704  68.716  71.931  1.00 177.43 ? 653  PHE B CD1 1 
ATOM   17352 C  CD2 . PHE C 1 653  ? 50.546  66.482  72.690  1.00 174.19 ? 653  PHE B CD2 1 
ATOM   17353 C  CE1 . PHE C 1 653  ? 49.320  68.803  71.925  1.00 175.00 ? 653  PHE B CE1 1 
ATOM   17354 C  CE2 . PHE C 1 653  ? 49.171  66.568  72.687  1.00 171.84 ? 653  PHE B CE2 1 
ATOM   17355 C  CZ  . PHE C 1 653  ? 48.559  67.725  72.292  1.00 171.98 ? 653  PHE B CZ  1 
ATOM   17356 N  N   . LEU C 1 654  ? 54.010  68.996  74.736  1.00 219.54 ? 654  LEU B N   1 
ATOM   17357 C  CA  . LEU C 1 654  ? 53.885  70.020  75.757  1.00 233.05 ? 654  LEU B CA  1 
ATOM   17358 C  C   . LEU C 1 654  ? 53.704  71.388  75.135  1.00 242.97 ? 654  LEU B C   1 
ATOM   17359 O  O   . LEU C 1 654  ? 54.680  72.023  74.748  1.00 250.20 ? 654  LEU B O   1 
ATOM   17360 C  CB  . LEU C 1 654  ? 55.122  70.007  76.644  1.00 235.99 ? 654  LEU B CB  1 
ATOM   17361 C  CG  . LEU C 1 654  ? 54.755  70.226  78.101  1.00 242.54 ? 654  LEU B CG  1 
ATOM   17362 C  CD1 . LEU C 1 654  ? 53.363  69.666  78.342  1.00 239.40 ? 654  LEU B CD1 1 
ATOM   17363 C  CD2 . LEU C 1 654  ? 55.785  69.593  79.030  1.00 248.05 ? 654  LEU B CD2 1 
ATOM   17364 N  N   . THR C 1 655  ? 52.457  71.846  75.037  1.00 238.13 ? 655  THR B N   1 
ATOM   17365 C  CA  . THR C 1 655  ? 52.183  73.146  74.424  1.00 241.03 ? 655  THR B CA  1 
ATOM   17366 C  C   . THR C 1 655  ? 51.025  73.873  75.081  1.00 251.34 ? 655  THR B C   1 
ATOM   17367 O  O   . THR C 1 655  ? 49.903  73.363  75.183  1.00 245.88 ? 655  THR B O   1 
ATOM   17368 C  CB  . THR C 1 655  ? 51.933  73.057  72.889  1.00 257.30 ? 655  THR B CB  1 
ATOM   17369 O  OG1 . THR C 1 655  ? 53.148  72.701  72.215  1.00 253.85 ? 655  THR B OG1 1 
ATOM   17370 C  CG2 . THR C 1 655  ? 51.434  74.395  72.345  1.00 255.88 ? 655  THR B CG2 1 
ATOM   17371 N  N   . ASN C 1 656  ? 51.318  75.077  75.540  1.00 225.36 ? 656  ASN B N   1 
ATOM   17372 C  CA  . ASN C 1 656  ? 50.254  75.946  75.953  1.00 237.82 ? 656  ASN B CA  1 
ATOM   17373 C  C   . ASN C 1 656  ? 49.668  76.652  74.754  1.00 232.64 ? 656  ASN B C   1 
ATOM   17374 O  O   . ASN C 1 656  ? 50.340  77.401  74.030  1.00 234.17 ? 656  ASN B O   1 
ATOM   17375 C  CB  . ASN C 1 656  ? 50.675  76.892  77.078  1.00 252.49 ? 656  ASN B CB  1 
ATOM   17376 C  CG  . ASN C 1 656  ? 50.484  76.262  78.459  1.00 257.42 ? 656  ASN B CG  1 
ATOM   17377 O  OD1 . ASN C 1 656  ? 50.699  76.894  79.501  1.00 265.99 ? 656  ASN B OD1 1 
ATOM   17378 N  ND2 . ASN C 1 656  ? 50.065  75.004  78.463  1.00 251.23 ? 656  ASN B ND2 1 
ATOM   17379 N  N   . ALA C 1 657  ? 48.396  76.335  74.560  1.00 277.72 ? 657  ALA B N   1 
ATOM   17380 C  CA  . ALA C 1 657  ? 47.554  76.854  73.508  1.00 269.81 ? 657  ALA B CA  1 
ATOM   17381 C  C   . ALA C 1 657  ? 46.418  75.848  73.449  1.00 263.66 ? 657  ALA B C   1 
ATOM   17382 O  O   . ALA C 1 657  ? 45.271  76.155  73.765  1.00 264.02 ? 657  ALA B O   1 
ATOM   17383 C  CB  . ALA C 1 657  ? 48.302  76.921  72.189  1.00 262.45 ? 657  ALA B CB  1 
ATOM   17384 N  N   . ASN C 1 658  ? 46.758  74.622  73.085  1.00 266.35 ? 658  ASN B N   1 
ATOM   17385 C  CA  . ASN C 1 658  ? 45.767  73.565  72.971  1.00 260.08 ? 658  ASN B CA  1 
ATOM   17386 C  C   . ASN C 1 658  ? 45.843  72.578  74.123  1.00 262.38 ? 658  ASN B C   1 
ATOM   17387 O  O   . ASN C 1 658  ? 46.834  72.562  74.853  1.00 267.04 ? 658  ASN B O   1 
ATOM   17388 C  CB  . ASN C 1 658  ? 45.937  72.836  71.641  1.00 249.33 ? 658  ASN B CB  1 
ATOM   17389 C  CG  . ASN C 1 658  ? 45.196  73.510  70.516  1.00 239.64 ? 658  ASN B CG  1 
ATOM   17390 O  OD1 . ASN C 1 658  ? 45.370  73.164  69.347  1.00 231.08 ? 658  ASN B OD1 1 
ATOM   17391 N  ND2 . ASN C 1 658  ? 44.356  74.477  70.861  1.00 241.02 ? 658  ASN B ND2 1 
ATOM   17392 N  N   . ALA C 1 659  ? 44.789  71.766  74.269  1.00 208.22 ? 659  ALA B N   1 
ATOM   17393 C  CA  . ALA C 1 659  ? 44.736  70.659  75.239  1.00 211.50 ? 659  ALA B CA  1 
ATOM   17394 C  C   . ALA C 1 659  ? 45.611  69.471  74.837  1.00 207.06 ? 659  ALA B C   1 
ATOM   17395 O  O   . ALA C 1 659  ? 45.121  68.541  74.190  1.00 201.95 ? 659  ALA B O   1 
ATOM   17396 C  CB  . ALA C 1 659  ? 43.292  70.184  75.439  1.00 209.99 ? 659  ALA B CB  1 
ATOM   17397 N  N   . ASP C 1 660  ? 46.888  69.492  75.238  1.00 207.41 ? 660  ASP B N   1 
ATOM   17398 C  CA  . ASP C 1 660  ? 47.828  68.412  74.892  1.00 203.47 ? 660  ASP B CA  1 
ATOM   17399 C  C   . ASP C 1 660  ? 47.503  67.052  75.510  1.00 201.50 ? 660  ASP B C   1 
ATOM   17400 O  O   . ASP C 1 660  ? 48.350  66.153  75.574  1.00 197.91 ? 660  ASP B O   1 
ATOM   17401 C  CB  . ASP C 1 660  ? 49.319  68.799  75.066  1.00 211.13 ? 660  ASP B CB  1 
ATOM   17402 C  CG  . ASP C 1 660  ? 49.601  69.596  76.321  1.00 224.69 ? 660  ASP B CG  1 
ATOM   17403 O  OD1 . ASP C 1 660  ? 49.246  69.125  77.418  1.00 229.66 ? 660  ASP B OD1 1 
ATOM   17404 O  OD2 . ASP C 1 660  ? 50.217  70.679  76.207  1.00 229.83 ? 660  ASP B OD2 1 
ATOM   17405 N  N   . ASP C 1 661  ? 46.243  66.912  75.911  1.00 192.83 ? 661  ASP B N   1 
ATOM   17406 C  CA  . ASP C 1 661  ? 45.763  65.757  76.654  1.00 192.32 ? 661  ASP B CA  1 
ATOM   17407 C  C   . ASP C 1 661  ? 45.957  64.411  75.941  1.00 188.26 ? 661  ASP B C   1 
ATOM   17408 O  O   . ASP C 1 661  ? 46.781  64.261  75.032  1.00 184.09 ? 661  ASP B O   1 
ATOM   17409 C  CB  . ASP C 1 661  ? 44.297  65.968  77.078  1.00 186.78 ? 661  ASP B CB  1 
ATOM   17410 C  CG  . ASP C 1 661  ? 43.328  65.902  75.914  1.00 168.99 ? 661  ASP B CG  1 
ATOM   17411 O  OD1 . ASP C 1 661  ? 42.971  66.965  75.353  1.00 161.19 ? 661  ASP B OD1 1 
ATOM   17412 O  OD2 . ASP C 1 661  ? 42.915  64.776  75.576  1.00 163.28 ? 661  ASP B OD2 1 
ATOM   17413 N  N   . SER C 1 662  ? 45.202  63.422  76.389  1.00 301.54 ? 662  SER B N   1 
ATOM   17414 C  CA  . SER C 1 662  ? 45.315  62.072  75.864  1.00 299.07 ? 662  SER B CA  1 
ATOM   17415 C  C   . SER C 1 662  ? 44.317  61.200  76.613  1.00 304.25 ? 662  SER B C   1 
ATOM   17416 O  O   . SER C 1 662  ? 44.687  60.299  77.357  1.00 304.14 ? 662  SER B O   1 
ATOM   17417 C  CB  . SER C 1 662  ? 46.746  61.555  76.028  1.00 303.50 ? 662  SER B CB  1 
ATOM   17418 O  OG  . SER C 1 662  ? 47.212  61.760  77.352  1.00 312.20 ? 662  SER B OG  1 
ATOM   17419 N  N   . GLN C 1 663  ? 43.042  61.488  76.375  1.00 205.39 ? 663  GLN B N   1 
ATOM   17420 C  CA  . GLN C 1 663  ? 41.905  60.997  77.156  1.00 213.93 ? 663  GLN B CA  1 
ATOM   17421 C  C   . GLN C 1 663  ? 42.089  59.732  78.016  1.00 227.17 ? 663  GLN B C   1 
ATOM   17422 O  O   . GLN C 1 663  ? 42.186  58.615  77.525  1.00 221.97 ? 663  GLN B O   1 
ATOM   17423 C  CB  . GLN C 1 663  ? 40.673  60.878  76.257  1.00 201.33 ? 663  GLN B CB  1 
ATOM   17424 C  CG  . GLN C 1 663  ? 40.517  62.031  75.275  1.00 191.70 ? 663  GLN B CG  1 
ATOM   17425 C  CD  . GLN C 1 663  ? 40.478  63.424  75.930  1.00 193.05 ? 663  GLN B CD  1 
ATOM   17426 O  OE1 . GLN C 1 663  ? 40.374  63.538  77.143  1.00 198.44 ? 663  GLN B OE1 1 
ATOM   17427 N  NE2 . GLN C 1 663  ? 40.557  64.470  75.127  1.00 189.00 ? 663  GLN B NE2 1 
ATOM   17428 N  N   . GLU C 1 664  ? 42.104  59.953  79.327  1.00 310.08 ? 664  GLU B N   1 
ATOM   17429 C  CA  . GLU C 1 664  ? 41.999  58.903  80.355  1.00 326.14 ? 664  GLU B CA  1 
ATOM   17430 C  C   . GLU C 1 664  ? 43.277  58.107  80.614  1.00 333.21 ? 664  GLU B C   1 
ATOM   17431 O  O   . GLU C 1 664  ? 43.984  58.318  81.607  1.00 330.24 ? 664  GLU B O   1 
ATOM   17432 C  CB  . GLU C 1 664  ? 40.887  57.922  79.994  1.00 327.83 ? 664  GLU B CB  1 
ATOM   17433 C  CG  . GLU C 1 664  ? 39.517  58.583  79.852  1.00 324.78 ? 664  GLU B CG  1 
ATOM   17434 C  CD  . GLU C 1 664  ? 38.416  57.783  80.521  1.00 331.55 ? 664  GLU B CD  1 
ATOM   17435 O  OE1 . GLU C 1 664  ? 38.727  56.892  81.347  1.00 337.44 ? 664  GLU B OE1 1 
ATOM   17436 O  OE2 . GLU C 1 664  ? 37.235  58.057  80.231  1.00 331.28 ? 664  GLU B OE2 1 
ATOM   17437 N  N   . ASN C 1 665  ? 43.545  57.179  79.707  1.00 204.30 ? 665  ASN B N   1 
ATOM   17438 C  CA  . ASN C 1 665  ? 44.438  56.082  79.988  1.00 211.23 ? 665  ASN B CA  1 
ATOM   17439 C  C   . ASN C 1 665  ? 45.504  56.141  78.921  1.00 210.92 ? 665  ASN B C   1 
ATOM   17440 O  O   . ASN C 1 665  ? 46.299  57.074  78.877  1.00 214.02 ? 665  ASN B O   1 
ATOM   17441 C  CB  . ASN C 1 665  ? 43.616  54.783  79.917  1.00 209.04 ? 665  ASN B CB  1 
ATOM   17442 C  CG  . ASN C 1 665  ? 44.408  53.539  80.255  1.00 207.91 ? 665  ASN B CG  1 
ATOM   17443 O  OD1 . ASN C 1 665  ? 44.588  52.661  79.397  1.00 200.76 ? 665  ASN B OD1 1 
ATOM   17444 N  ND2 . ASN C 1 665  ? 44.851  53.432  81.491  1.00 215.28 ? 665  ASN B ND2 1 
ATOM   17445 N  N   . ASP C 1 666  ? 45.495  55.137  78.056  1.00 359.71 ? 666  ASP B N   1 
ATOM   17446 C  CA  . ASP C 1 666  ? 46.247  55.162  76.816  1.00 355.89 ? 666  ASP B CA  1 
ATOM   17447 C  C   . ASP C 1 666  ? 46.035  53.924  75.938  1.00 344.43 ? 666  ASP B C   1 
ATOM   17448 O  O   . ASP C 1 666  ? 46.881  53.033  75.873  1.00 343.02 ? 666  ASP B O   1 
ATOM   17449 C  CB  . ASP C 1 666  ? 47.745  55.447  77.035  1.00 368.04 ? 666  ASP B CB  1 
ATOM   17450 C  CG  . ASP C 1 666  ? 48.479  54.299  77.693  1.00 379.99 ? 666  ASP B CG  1 
ATOM   17451 O  OD1 . ASP C 1 666  ? 47.845  53.567  78.479  1.00 385.61 ? 666  ASP B OD1 1 
ATOM   17452 O  OD2 . ASP C 1 666  ? 49.685  54.132  77.421  1.00 382.93 ? 666  ASP B OD2 1 
ATOM   17453 N  N   . GLU C 1 667  ? 44.861  53.865  75.324  1.00 350.64 ? 667  GLU B N   1 
ATOM   17454 C  CA  . GLU C 1 667  ? 44.596  53.059  74.137  1.00 337.66 ? 667  GLU B CA  1 
ATOM   17455 C  C   . GLU C 1 667  ? 45.411  51.780  73.954  1.00 336.18 ? 667  GLU B C   1 
ATOM   17456 O  O   . GLU C 1 667  ? 46.507  51.825  73.387  1.00 335.12 ? 667  GLU B O   1 
ATOM   17457 C  CB  . GLU C 1 667  ? 44.781  53.947  72.910  1.00 325.35 ? 667  GLU B CB  1 
ATOM   17458 C  CG  . GLU C 1 667  ? 45.178  55.372  73.252  1.00 322.59 ? 667  GLU B CG  1 
ATOM   17459 C  CD  . GLU C 1 667  ? 44.073  56.141  73.965  1.00 319.43 ? 667  GLU B CD  1 
ATOM   17460 O  OE1 . GLU C 1 667  ? 43.147  55.508  74.521  1.00 317.68 ? 667  GLU B OE1 1 
ATOM   17461 O  OE2 . GLU C 1 667  ? 44.127  57.388  73.968  1.00 319.40 ? 667  GLU B OE2 1 
ATOM   17462 N  N   . PRO C 1 668  ? 44.864  50.634  74.406  1.00 343.62 ? 668  PRO B N   1 
ATOM   17463 C  CA  . PRO C 1 668  ? 45.397  49.287  74.137  1.00 341.21 ? 668  PRO B CA  1 
ATOM   17464 C  C   . PRO C 1 668  ? 45.375  48.890  72.650  1.00 332.36 ? 668  PRO B C   1 
ATOM   17465 O  O   . PRO C 1 668  ? 45.121  47.725  72.331  1.00 329.26 ? 668  PRO B O   1 
ATOM   17466 C  CB  . PRO C 1 668  ? 44.459  48.375  74.940  1.00 342.88 ? 668  PRO B CB  1 
ATOM   17467 C  CG  . PRO C 1 668  ? 43.941  49.238  76.034  1.00 349.33 ? 668  PRO B CG  1 
ATOM   17468 C  CD  . PRO C 1 668  ? 43.809  50.610  75.436  1.00 347.34 ? 668  PRO B CD  1 
ATOM   17469 N  N   . CYS C 1 669  ? 45.652  49.852  71.772  1.00 295.00 ? 669  CYS B N   1 
ATOM   17470 C  CA  . CYS C 1 669  ? 45.672  49.647  70.325  1.00 287.86 ? 669  CYS B CA  1 
ATOM   17471 C  C   . CYS C 1 669  ? 46.157  48.248  69.902  1.00 285.70 ? 669  CYS B C   1 
ATOM   17472 O  O   . CYS C 1 669  ? 46.997  47.643  70.571  1.00 289.74 ? 669  CYS B O   1 
ATOM   17473 C  CB  . CYS C 1 669  ? 46.527  50.739  69.678  1.00 287.18 ? 669  CYS B CB  1 
ATOM   17474 S  SG  . CYS C 1 669  ? 47.297  50.256  68.134  1.00 329.94 ? 669  CYS B SG  1 
ATOM   17475 N  N   . LYS C 1 670  ? 45.626  47.741  68.788  1.00 259.29 ? 670  LYS B N   1 
ATOM   17476 C  CA  . LYS C 1 670  ? 45.920  46.373  68.347  1.00 255.44 ? 670  LYS B CA  1 
ATOM   17477 C  C   . LYS C 1 670  ? 45.584  46.107  66.866  1.00 244.73 ? 670  LYS B C   1 
ATOM   17478 O  O   . LYS C 1 670  ? 44.475  45.675  66.548  1.00 241.02 ? 670  LYS B O   1 
ATOM   17479 C  CB  . LYS C 1 670  ? 45.179  45.362  69.240  1.00 259.67 ? 670  LYS B CB  1 
ATOM   17480 C  CG  . LYS C 1 670  ? 45.319  43.896  68.822  1.00 258.25 ? 670  LYS B CG  1 
ATOM   17481 C  CD  . LYS C 1 670  ? 46.678  43.326  69.208  1.00 262.31 ? 670  LYS B CD  1 
ATOM   17482 C  CE  . LYS C 1 670  ? 46.862  41.887  68.718  1.00 260.12 ? 670  LYS B CE  1 
ATOM   17483 N  NZ  . LYS C 1 670  ? 46.008  40.900  69.438  1.00 262.69 ? 670  LYS B NZ  1 
ATOM   17484 N  N   . GLU C 1 671  ? 46.545  46.377  65.977  1.00 283.94 ? 671  GLU B N   1 
ATOM   17485 C  CA  . GLU C 1 671  ? 46.508  45.966  64.552  1.00 274.12 ? 671  GLU B CA  1 
ATOM   17486 C  C   . GLU C 1 671  ? 45.576  46.719  63.536  1.00 248.15 ? 671  GLU B C   1 
ATOM   17487 O  O   . GLU C 1 671  ? 44.926  46.077  62.707  1.00 245.89 ? 671  GLU B O   1 
ATOM   17488 C  CB  . GLU C 1 671  ? 46.328  44.434  64.439  1.00 272.58 ? 671  GLU B CB  1 
ATOM   17489 C  CG  . GLU C 1 671  ? 47.490  43.603  65.019  1.00 274.79 ? 671  GLU B CG  1 
ATOM   17490 C  CD  . GLU C 1 671  ? 47.260  42.097  64.922  1.00 271.66 ? 671  GLU B CD  1 
ATOM   17491 O  OE1 . GLU C 1 671  ? 46.371  41.676  64.154  1.00 266.13 ? 671  GLU B OE1 1 
ATOM   17492 O  OE2 . GLU C 1 671  ? 47.973  41.332  65.609  1.00 274.70 ? 671  GLU B OE2 1 
ATOM   17493 N  N   . ILE C 1 672  ? 45.551  48.061  63.582  1.00 217.63 ? 672  ILE B N   1 
ATOM   17494 C  CA  . ILE C 1 672  ? 44.749  48.931  62.679  1.00 204.99 ? 672  ILE B CA  1 
ATOM   17495 C  C   . ILE C 1 672  ? 45.616  49.591  61.598  1.00 194.54 ? 672  ILE B C   1 
ATOM   17496 O  O   . ILE C 1 672  ? 45.103  50.240  60.684  1.00 188.43 ? 672  ILE B O   1 
ATOM   17497 C  CB  . ILE C 1 672  ? 44.014  50.090  63.485  1.00 226.27 ? 672  ILE B CB  1 
ATOM   17498 C  CG1 . ILE C 1 672  ? 42.851  50.732  62.716  1.00 220.14 ? 672  ILE B CG1 1 
ATOM   17499 C  CG2 . ILE C 1 672  ? 44.974  51.204  63.863  1.00 230.39 ? 672  ILE B CG2 1 
ATOM   17500 C  CD1 . ILE C 1 672  ? 42.216  51.938  63.459  1.00 222.98 ? 672  ILE B CD1 1 
ATOM   17501 N  N   . LEU C 1 673  ? 46.931  49.422  61.715  1.00 166.27 ? 673  LEU B N   1 
ATOM   17502 C  CA  . LEU C 1 673  ? 47.880  50.291  61.020  1.00 156.44 ? 673  LEU B CA  1 
ATOM   17503 C  C   . LEU C 1 673  ? 48.016  50.022  59.537  1.00 148.45 ? 673  LEU B C   1 
ATOM   17504 O  O   . LEU C 1 673  ? 48.804  50.690  58.870  1.00 146.71 ? 673  LEU B O   1 
ATOM   17505 C  CB  . LEU C 1 673  ? 49.262  50.260  61.677  1.00 154.01 ? 673  LEU B CB  1 
ATOM   17506 C  CG  . LEU C 1 673  ? 50.348  49.387  61.069  1.00 144.26 ? 673  LEU B CG  1 
ATOM   17507 C  CD1 . LEU C 1 673  ? 51.682  49.897  61.546  1.00 146.20 ? 673  LEU B CD1 1 
ATOM   17508 C  CD2 . LEU C 1 673  ? 50.161  47.888  61.379  1.00 141.67 ? 673  LEU B CD2 1 
ATOM   17509 N  N   . LEU C 1 679  ? 31.623  0.681   64.122  1.00 315.27 ? 679  LEU B N   1 
ATOM   17510 C  CA  . LEU C 1 679  ? 31.298  -0.237  65.207  1.00 313.90 ? 679  LEU B CA  1 
ATOM   17511 C  C   . LEU C 1 679  ? 32.059  0.132   66.482  1.00 315.32 ? 679  LEU B C   1 
ATOM   17512 O  O   . LEU C 1 679  ? 31.666  -0.250  67.584  1.00 314.50 ? 679  LEU B O   1 
ATOM   17513 C  CB  . LEU C 1 679  ? 31.575  -1.680  64.782  1.00 310.52 ? 679  LEU B CB  1 
ATOM   17514 C  CG  . LEU C 1 679  ? 30.601  -2.193  63.715  1.00 308.20 ? 679  LEU B CG  1 
ATOM   17515 C  CD1 . LEU C 1 679  ? 31.210  -3.321  62.896  1.00 306.64 ? 679  LEU B CD1 1 
ATOM   17516 C  CD2 . LEU C 1 679  ? 29.271  -2.612  64.339  1.00 306.52 ? 679  LEU B CD2 1 
ATOM   17517 N  N   . GLN C 1 680  ? 33.145  0.883   66.325  1.00 271.97 ? 680  GLN B N   1 
ATOM   17518 C  CA  . GLN C 1 680  ? 33.824  1.485   67.469  1.00 272.35 ? 680  GLN B CA  1 
ATOM   17519 C  C   . GLN C 1 680  ? 33.148  2.806   67.863  1.00 266.78 ? 680  GLN B C   1 
ATOM   17520 O  O   . GLN C 1 680  ? 33.510  3.419   68.869  1.00 266.33 ? 680  GLN B O   1 
ATOM   17521 C  CB  . GLN C 1 680  ? 35.316  1.681   67.176  1.00 277.74 ? 680  GLN B CB  1 
ATOM   17522 C  CG  . GLN C 1 680  ? 35.778  3.129   67.129  1.00 278.61 ? 680  GLN B CG  1 
ATOM   17523 C  CD  . GLN C 1 680  ? 35.396  3.831   65.843  1.00 278.50 ? 680  GLN B CD  1 
ATOM   17524 O  OE1 . GLN C 1 680  ? 34.951  3.200   64.884  1.00 279.49 ? 680  GLN B OE1 1 
ATOM   17525 N  NE2 . GLN C 1 680  ? 35.572  5.148   65.816  1.00 277.51 ? 680  GLN B NE2 1 
ATOM   17526 N  N   . LYS C 1 681  ? 32.169  3.231   67.055  1.00 325.84 ? 681  LYS B N   1 
ATOM   17527 C  CA  . LYS C 1 681  ? 31.360  4.431   67.320  1.00 319.13 ? 681  LYS B CA  1 
ATOM   17528 C  C   . LYS C 1 681  ? 30.247  4.145   68.334  1.00 317.79 ? 681  LYS B C   1 
ATOM   17529 O  O   . LYS C 1 681  ? 29.845  5.026   69.097  1.00 316.14 ? 681  LYS B O   1 
ATOM   17530 C  CB  . LYS C 1 681  ? 30.710  4.972   66.033  1.00 314.16 ? 681  LYS B CB  1 
ATOM   17531 C  CG  . LYS C 1 681  ? 31.613  5.082   64.809  1.00 312.44 ? 681  LYS B CG  1 
ATOM   17532 C  CD  . LYS C 1 681  ? 30.798  5.486   63.590  1.00 308.44 ? 681  LYS B CD  1 
ATOM   17533 C  CE  . LYS C 1 681  ? 31.446  4.997   62.314  1.00 309.02 ? 681  LYS B CE  1 
ATOM   17534 N  NZ  . LYS C 1 681  ? 30.538  5.155   61.148  1.00 308.19 ? 681  LYS B NZ  1 
ATOM   17535 N  N   . LYS C 1 682  ? 29.740  2.914   68.311  1.00 326.96 ? 682  LYS B N   1 
ATOM   17536 C  CA  . LYS C 1 682  ? 28.687  2.474   69.224  1.00 326.42 ? 682  LYS B CA  1 
ATOM   17537 C  C   . LYS C 1 682  ? 29.118  2.613   70.684  1.00 330.15 ? 682  LYS B C   1 
ATOM   17538 O  O   . LYS C 1 682  ? 28.284  2.734   71.585  1.00 327.60 ? 682  LYS B O   1 
ATOM   17539 C  CB  . LYS C 1 682  ? 28.303  1.024   68.916  1.00 325.74 ? 682  LYS B CB  1 
ATOM   17540 C  CG  . LYS C 1 682  ? 27.707  0.271   70.089  1.00 324.30 ? 682  LYS B CG  1 
ATOM   17541 C  CD  . LYS C 1 682  ? 26.391  0.882   70.531  1.00 320.21 ? 682  LYS B CD  1 
ATOM   17542 C  CE  . LYS C 1 682  ? 25.927  0.276   71.840  1.00 319.37 ? 682  LYS B CE  1 
ATOM   17543 N  NZ  . LYS C 1 682  ? 24.678  0.916   72.331  1.00 316.33 ? 682  LYS B NZ  1 
ATOM   17544 N  N   . ILE C 1 683  ? 30.428  2.598   70.906  1.00 372.71 ? 683  ILE B N   1 
ATOM   17545 C  CA  . ILE C 1 683  ? 30.988  2.745   72.245  1.00 377.97 ? 683  ILE B CA  1 
ATOM   17546 C  C   . ILE C 1 683  ? 31.262  4.219   72.604  1.00 380.40 ? 683  ILE B C   1 
ATOM   17547 O  O   . ILE C 1 683  ? 31.041  4.630   73.744  1.00 381.84 ? 683  ILE B O   1 
ATOM   17548 C  CB  . ILE C 1 683  ? 32.277  1.898   72.410  1.00 343.25 ? 683  ILE B CB  1 
ATOM   17549 C  CG1 . ILE C 1 683  ? 32.152  0.572   71.649  1.00 343.00 ? 683  ILE B CG1 1 
ATOM   17550 C  CG2 . ILE C 1 683  ? 32.572  1.648   73.880  1.00 345.55 ? 683  ILE B CG2 1 
ATOM   17551 C  CD1 . ILE C 1 683  ? 33.469  -0.148  71.459  1.00 341.51 ? 683  ILE B CD1 1 
ATOM   17552 N  N   . GLU C 1 684  ? 31.722  5.010   71.630  1.00 321.04 ? 684  GLU B N   1 
ATOM   17553 C  CA  . GLU C 1 684  ? 32.092  6.420   71.860  1.00 321.66 ? 684  GLU B CA  1 
ATOM   17554 C  C   . GLU C 1 684  ? 30.905  7.350   72.165  1.00 315.70 ? 684  GLU B C   1 
ATOM   17555 O  O   . GLU C 1 684  ? 31.088  8.545   72.423  1.00 313.99 ? 684  GLU B O   1 
ATOM   17556 C  CB  . GLU C 1 684  ? 32.930  6.978   70.696  1.00 327.33 ? 684  GLU B CB  1 
ATOM   17557 C  CG  . GLU C 1 684  ? 34.368  6.463   70.650  1.00 335.14 ? 684  GLU B CG  1 
ATOM   17558 C  CD  . GLU C 1 684  ? 35.289  7.361   69.846  1.00 339.47 ? 684  GLU B CD  1 
ATOM   17559 O  OE1 . GLU C 1 684  ? 34.797  8.347   69.259  1.00 338.70 ? 684  GLU B OE1 1 
ATOM   17560 O  OE2 . GLU C 1 684  ? 36.505  7.084   69.807  1.00 343.46 ? 684  GLU B OE2 1 
ATOM   17561 N  N   . GLU C 1 685  ? 29.698  6.790   72.120  1.00 265.27 ? 685  GLU B N   1 
ATOM   17562 C  CA  . GLU C 1 685  ? 28.475  7.486   72.517  1.00 261.25 ? 685  GLU B CA  1 
ATOM   17563 C  C   . GLU C 1 685  ? 28.402  7.563   74.034  1.00 257.66 ? 685  GLU B C   1 
ATOM   17564 O  O   . GLU C 1 685  ? 28.011  8.578   74.617  1.00 256.66 ? 685  GLU B O   1 
ATOM   17565 C  CB  . GLU C 1 685  ? 27.244  6.731   71.994  1.00 262.04 ? 685  GLU B CB  1 
ATOM   17566 C  CG  . GLU C 1 685  ? 27.089  5.316   72.559  1.00 264.29 ? 685  GLU B CG  1 
ATOM   17567 C  CD  . GLU C 1 685  ? 25.938  4.529   71.946  1.00 265.00 ? 685  GLU B CD  1 
ATOM   17568 O  OE1 . GLU C 1 685  ? 25.289  5.030   71.007  1.00 264.03 ? 685  GLU B OE1 1 
ATOM   17569 O  OE2 . GLU C 1 685  ? 25.685  3.399   72.406  1.00 266.59 ? 685  GLU B OE2 1 
ATOM   17570 N  N   . ILE C 1 686  ? 28.786  6.463   74.665  1.00 288.32 ? 686  ILE B N   1 
ATOM   17571 C  CA  . ILE C 1 686  ? 28.713  6.338   76.105  1.00 285.44 ? 686  ILE B CA  1 
ATOM   17572 C  C   . ILE C 1 686  ? 29.776  7.209   76.779  1.00 282.36 ? 686  ILE B C   1 
ATOM   17573 O  O   . ILE C 1 686  ? 30.088  7.023   77.955  1.00 284.47 ? 686  ILE B O   1 
ATOM   17574 C  CB  . ILE C 1 686  ? 28.834  4.868   76.532  1.00 287.43 ? 686  ILE B CB  1 
ATOM   17575 C  CG1 . ILE C 1 686  ? 28.032  3.979   75.579  1.00 286.80 ? 686  ILE B CG1 1 
ATOM   17576 C  CG2 . ILE C 1 686  ? 28.344  4.681   77.956  1.00 288.27 ? 686  ILE B CG2 1 
ATOM   17577 C  CD1 . ILE C 1 686  ? 26.540  4.232   75.617  1.00 284.58 ? 686  ILE B CD1 1 
ATOM   17578 N  N   . ALA C 1 687  ? 30.336  8.154   76.023  1.00 290.02 ? 687  ALA B N   1 
ATOM   17579 C  CA  . ALA C 1 687  ? 31.089  9.252   76.617  1.00 284.08 ? 687  ALA B CA  1 
ATOM   17580 C  C   . ALA C 1 687  ? 30.041  10.017  77.386  1.00 277.37 ? 687  ALA B C   1 
ATOM   17581 O  O   . ALA C 1 687  ? 30.332  10.973  78.110  1.00 275.66 ? 687  ALA B O   1 
ATOM   17582 C  CB  . ALA C 1 687  ? 31.700  10.126  75.548  1.00 282.90 ? 687  ALA B CB  1 
ATOM   17583 N  N   . ALA C 1 688  ? 28.805  9.565   77.182  1.00 299.90 ? 688  ALA B N   1 
ATOM   17584 C  CA  . ALA C 1 688  ? 27.621  10.016  77.895  1.00 294.99 ? 688  ALA B CA  1 
ATOM   17585 C  C   . ALA C 1 688  ? 27.771  9.892   79.412  1.00 293.51 ? 688  ALA B C   1 
ATOM   17586 O  O   . ALA C 1 688  ? 27.023  10.518  80.165  1.00 290.95 ? 688  ALA B O   1 
ATOM   17587 C  CB  . ALA C 1 688  ? 26.402  9.225   77.418  1.00 294.13 ? 688  ALA B CB  1 
ATOM   17588 N  N   . LYS C 1 689  ? 28.726  9.079   79.860  1.00 320.66 ? 689  LYS B N   1 
ATOM   17589 C  CA  . LYS C 1 689  ? 29.003  8.959   81.292  1.00 323.00 ? 689  LYS B CA  1 
ATOM   17590 C  C   . LYS C 1 689  ? 30.116  9.894   81.781  1.00 330.27 ? 689  LYS B C   1 
ATOM   17591 O  O   . LYS C 1 689  ? 30.694  9.665   82.845  1.00 333.55 ? 689  LYS B O   1 
ATOM   17592 C  CB  . LYS C 1 689  ? 29.281  7.502   81.698  1.00 318.16 ? 689  LYS B CB  1 
ATOM   17593 C  CG  . LYS C 1 689  ? 30.227  6.744   80.784  1.00 313.76 ? 689  LYS B CG  1 
ATOM   17594 C  CD  . LYS C 1 689  ? 30.265  5.272   81.148  1.00 311.27 ? 689  LYS B CD  1 
ATOM   17595 C  CE  . LYS C 1 689  ? 28.867  4.685   81.198  1.00 306.70 ? 689  LYS B CE  1 
ATOM   17596 N  NZ  . LYS C 1 689  ? 28.870  3.321   81.792  1.00 306.48 ? 689  LYS B NZ  1 
ATOM   17597 N  N   . TYR C 1 690  ? 30.413  10.942  81.009  1.00 301.17 ? 690  TYR B N   1 
ATOM   17598 C  CA  . TYR C 1 690  ? 31.383  11.943  81.451  1.00 310.03 ? 690  TYR B CA  1 
ATOM   17599 C  C   . TYR C 1 690  ? 30.945  12.571  82.770  1.00 312.81 ? 690  TYR B C   1 
ATOM   17600 O  O   . TYR C 1 690  ? 29.776  12.894  82.970  1.00 310.80 ? 690  TYR B O   1 
ATOM   17601 C  CB  . TYR C 1 690  ? 31.617  13.043  80.408  1.00 315.51 ? 690  TYR B CB  1 
ATOM   17602 C  CG  . TYR C 1 690  ? 32.140  14.310  81.050  1.00 323.67 ? 690  TYR B CG  1 
ATOM   17603 C  CD1 . TYR C 1 690  ? 33.405  14.350  81.621  1.00 328.65 ? 690  TYR B CD1 1 
ATOM   17604 C  CD2 . TYR C 1 690  ? 31.358  15.453  81.119  1.00 325.52 ? 690  TYR B CD2 1 
ATOM   17605 C  CE1 . TYR C 1 690  ? 33.881  15.495  82.228  1.00 332.36 ? 690  TYR B CE1 1 
ATOM   17606 C  CE2 . TYR C 1 690  ? 31.827  16.605  81.724  1.00 329.24 ? 690  TYR B CE2 1 
ATOM   17607 C  CZ  . TYR C 1 690  ? 33.089  16.620  82.276  1.00 332.64 ? 690  TYR B CZ  1 
ATOM   17608 O  OH  . TYR C 1 690  ? 33.561  17.764  82.877  1.00 335.53 ? 690  TYR B OH  1 
ATOM   17609 N  N   . LYS C 1 691  ? 31.905  12.740  83.666  1.00 356.43 ? 691  LYS B N   1 
ATOM   17610 C  CA  . LYS C 1 691  ? 31.662  13.278  84.992  1.00 358.80 ? 691  LYS B CA  1 
ATOM   17611 C  C   . LYS C 1 691  ? 33.051  13.514  85.526  1.00 363.25 ? 691  LYS B C   1 
ATOM   17612 O  O   . LYS C 1 691  ? 33.260  13.865  86.686  1.00 365.22 ? 691  LYS B O   1 
ATOM   17613 C  CB  . LYS C 1 691  ? 30.893  12.276  85.858  1.00 358.86 ? 691  LYS B CB  1 
ATOM   17614 C  CG  . LYS C 1 691  ? 31.417  10.846  85.785  1.00 358.09 ? 691  LYS B CG  1 
ATOM   17615 C  CD  . LYS C 1 691  ? 30.370  9.844   86.254  1.00 355.93 ? 691  LYS B CD  1 
ATOM   17616 C  CE  . LYS C 1 691  ? 30.776  8.420   85.905  1.00 355.48 ? 691  LYS B CE  1 
ATOM   17617 N  NZ  . LYS C 1 691  ? 29.681  7.448   86.163  1.00 354.42 ? 691  LYS B NZ  1 
ATOM   17618 N  N   . HIS C 1 692  ? 33.999  13.298  84.627  1.00 258.89 ? 692  HIS B N   1 
ATOM   17619 C  CA  . HIS C 1 692  ? 35.402  13.518  84.879  1.00 261.41 ? 692  HIS B CA  1 
ATOM   17620 C  C   . HIS C 1 692  ? 36.135  12.975  83.678  1.00 256.25 ? 692  HIS B C   1 
ATOM   17621 O  O   . HIS C 1 692  ? 35.634  12.097  82.974  1.00 252.67 ? 692  HIS B O   1 
ATOM   17622 C  CB  . HIS C 1 692  ? 35.863  12.790  86.139  1.00 268.97 ? 692  HIS B CB  1 
ATOM   17623 C  CG  . HIS C 1 692  ? 37.286  13.073  86.514  1.00 277.99 ? 692  HIS B CG  1 
ATOM   17624 N  ND1 . HIS C 1 692  ? 37.743  14.344  86.795  1.00 282.14 ? 692  HIS B ND1 1 
ATOM   17625 C  CD2 . HIS C 1 692  ? 38.350  12.251  86.675  1.00 283.42 ? 692  HIS B CD2 1 
ATOM   17626 C  CE1 . HIS C 1 692  ? 39.027  14.292  87.100  1.00 287.08 ? 692  HIS B CE1 1 
ATOM   17627 N  NE2 . HIS C 1 692  ? 39.421  13.033  87.036  1.00 287.87 ? 692  HIS B NE2 1 
ATOM   17628 N  N   . SER C 1 693  ? 37.322  13.507  83.443  1.00 277.03 ? 693  SER B N   1 
ATOM   17629 C  CA  . SER C 1 693  ? 38.150  13.029  82.360  1.00 273.06 ? 693  SER B CA  1 
ATOM   17630 C  C   . SER C 1 693  ? 38.469  11.551  82.547  1.00 267.75 ? 693  SER B C   1 
ATOM   17631 O  O   . SER C 1 693  ? 38.178  10.727  81.680  1.00 266.03 ? 693  SER B O   1 
ATOM   17632 C  CB  . SER C 1 693  ? 39.444  13.834  82.315  1.00 276.39 ? 693  SER B CB  1 
ATOM   17633 O  OG  . SER C 1 693  ? 40.335  13.278  81.368  1.00 277.31 ? 693  SER B OG  1 
ATOM   17634 N  N   . VAL C 1 694  ? 39.053  11.229  83.699  1.00 373.00 ? 694  VAL B N   1 
ATOM   17635 C  CA  . VAL C 1 694  ? 39.577  9.892   83.970  1.00 370.42 ? 694  VAL B CA  1 
ATOM   17636 C  C   . VAL C 1 694  ? 38.545  8.783   83.750  1.00 364.50 ? 694  VAL B C   1 
ATOM   17637 O  O   . VAL C 1 694  ? 38.913  7.638   83.485  1.00 365.65 ? 694  VAL B O   1 
ATOM   17638 C  CB  . VAL C 1 694  ? 40.164  9.784   85.401  1.00 367.39 ? 694  VAL B CB  1 
ATOM   17639 C  CG1 . VAL C 1 694  ? 40.860  8.447   85.590  1.00 369.84 ? 694  VAL B CG1 1 
ATOM   17640 C  CG2 . VAL C 1 694  ? 41.134  10.923  85.666  1.00 369.68 ? 694  VAL B CG2 1 
ATOM   17641 N  N   . VAL C 1 695  ? 37.261  9.114   83.861  1.00 230.56 ? 695  VAL B N   1 
ATOM   17642 C  CA  . VAL C 1 695  ? 36.227  8.124   83.604  1.00 225.67 ? 695  VAL B CA  1 
ATOM   17643 C  C   . VAL C 1 695  ? 36.189  7.855   82.114  1.00 221.82 ? 695  VAL B C   1 
ATOM   17644 O  O   . VAL C 1 695  ? 36.026  6.711   81.696  1.00 220.99 ? 695  VAL B O   1 
ATOM   17645 C  CB  . VAL C 1 695  ? 34.835  8.551   84.120  1.00 223.75 ? 695  VAL B CB  1 
ATOM   17646 C  CG1 . VAL C 1 695  ? 33.777  7.560   83.666  1.00 221.28 ? 695  VAL B CG1 1 
ATOM   17647 C  CG2 . VAL C 1 695  ? 34.834  8.654   85.643  1.00 225.54 ? 695  VAL B CG2 1 
ATOM   17648 N  N   . LYS C 1 696  ? 36.356  8.909   81.319  1.00 327.31 ? 696  LYS B N   1 
ATOM   17649 C  CA  . LYS C 1 696  ? 36.492  8.759   79.875  1.00 325.07 ? 696  LYS B CA  1 
ATOM   17650 C  C   . LYS C 1 696  ? 37.638  7.799   79.567  1.00 327.59 ? 696  LYS B C   1 
ATOM   17651 O  O   . LYS C 1 696  ? 37.533  6.978   78.656  1.00 327.26 ? 696  LYS B O   1 
ATOM   17652 C  CB  . LYS C 1 696  ? 36.712  10.118  79.196  1.00 324.35 ? 696  LYS B CB  1 
ATOM   17653 C  CG  . LYS C 1 696  ? 37.390  10.059  77.818  1.00 325.35 ? 696  LYS B CG  1 
ATOM   17654 C  CD  . LYS C 1 696  ? 36.455  9.613   76.690  1.00 318.29 ? 696  LYS B CD  1 
ATOM   17655 C  CE  . LYS C 1 696  ? 37.156  9.714   75.325  1.00 317.70 ? 696  LYS B CE  1 
ATOM   17656 N  NZ  . LYS C 1 696  ? 36.279  9.346   74.169  1.00 313.58 ? 696  LYS B NZ  1 
ATOM   17657 N  N   . LYS C 1 697  ? 38.721  7.892   80.339  1.00 195.70 ? 697  LYS B N   1 
ATOM   17658 C  CA  . LYS C 1 697  ? 39.843  6.952   80.212  1.00 197.89 ? 697  LYS B CA  1 
ATOM   17659 C  C   . LYS C 1 697  ? 39.522  5.589   80.826  1.00 197.62 ? 697  LYS B C   1 
ATOM   17660 O  O   . LYS C 1 697  ? 40.106  4.579   80.438  1.00 200.59 ? 697  LYS B O   1 
ATOM   17661 C  CB  . LYS C 1 697  ? 41.125  7.512   80.840  1.00 201.33 ? 697  LYS B CB  1 
ATOM   17662 C  CG  . LYS C 1 697  ? 42.341  6.581   80.742  1.00 206.69 ? 697  LYS B CG  1 
ATOM   17663 C  CD  . LYS C 1 697  ? 43.038  6.715   79.390  1.00 208.95 ? 697  LYS B CD  1 
ATOM   17664 C  CE  . LYS C 1 697  ? 44.320  5.891   79.315  1.00 214.58 ? 697  LYS B CE  1 
ATOM   17665 N  NZ  . LYS C 1 697  ? 45.103  6.162   78.065  1.00 216.68 ? 697  LYS B NZ  1 
ATOM   17666 N  N   . CYS C 1 698  ? 38.606  5.569   81.793  1.00 263.72 ? 698  CYS B N   1 
ATOM   17667 C  CA  . CYS C 1 698  ? 38.139  4.319   82.393  1.00 263.39 ? 698  CYS B CA  1 
ATOM   17668 C  C   . CYS C 1 698  ? 37.377  3.497   81.366  1.00 260.00 ? 698  CYS B C   1 
ATOM   17669 O  O   . CYS C 1 698  ? 37.366  2.262   81.402  1.00 259.50 ? 698  CYS B O   1 
ATOM   17670 C  CB  . CYS C 1 698  ? 37.237  4.604   83.598  1.00 261.54 ? 698  CYS B CB  1 
ATOM   17671 S  SG  . CYS C 1 698  ? 38.099  4.731   85.200  1.00 297.60 ? 698  CYS B SG  1 
ATOM   17672 N  N   . CYS C 1 699  ? 36.740  4.209   80.447  1.00 228.47 ? 699  CYS B N   1 
ATOM   17673 C  CA  . CYS C 1 699  ? 35.942  3.597   79.400  1.00 230.21 ? 699  CYS B CA  1 
ATOM   17674 C  C   . CYS C 1 699  ? 36.772  3.358   78.151  1.00 234.94 ? 699  CYS B C   1 
ATOM   17675 O  O   . CYS C 1 699  ? 36.789  2.251   77.620  1.00 235.93 ? 699  CYS B O   1 
ATOM   17676 C  CB  . CYS C 1 699  ? 34.761  4.502   79.053  1.00 228.07 ? 699  CYS B CB  1 
ATOM   17677 S  SG  . CYS C 1 699  ? 33.193  3.642   78.832  1.00 225.25 ? 699  CYS B SG  1 
ATOM   17678 N  N   . TYR C 1 700  ? 37.454  4.407   77.691  1.00 213.01 ? 700  TYR B N   1 
ATOM   17679 C  CA  . TYR C 1 700  ? 38.220  4.362   76.443  1.00 221.58 ? 700  TYR B CA  1 
ATOM   17680 C  C   . TYR C 1 700  ? 39.093  3.108   76.403  1.00 229.03 ? 700  TYR B C   1 
ATOM   17681 O  O   . TYR C 1 700  ? 38.656  2.059   75.932  1.00 229.84 ? 700  TYR B O   1 
ATOM   17682 C  CB  . TYR C 1 700  ? 39.044  5.653   76.243  1.00 228.28 ? 700  TYR B CB  1 
ATOM   17683 C  CG  . TYR C 1 700  ? 39.072  6.167   74.808  1.00 234.73 ? 700  TYR B CG  1 
ATOM   17684 C  CD1 . TYR C 1 700  ? 40.232  6.104   74.048  1.00 241.26 ? 700  TYR B CD1 1 
ATOM   17685 C  CD2 . TYR C 1 700  ? 37.929  6.707   74.213  1.00 234.43 ? 700  TYR B CD2 1 
ATOM   17686 C  CE1 . TYR C 1 700  ? 40.250  6.561   72.735  1.00 243.13 ? 700  TYR B CE1 1 
ATOM   17687 C  CE2 . TYR C 1 700  ? 37.941  7.169   72.900  1.00 236.45 ? 700  TYR B CE2 1 
ATOM   17688 C  CZ  . TYR C 1 700  ? 39.103  7.095   72.168  1.00 240.65 ? 700  TYR B CZ  1 
ATOM   17689 O  OH  . TYR C 1 700  ? 39.114  7.554   70.870  1.00 241.09 ? 700  TYR B OH  1 
ATOM   17690 N  N   . ASP C 1 701  ? 40.312  3.194   76.916  1.00 244.57 ? 701  ASP B N   1 
ATOM   17691 C  CA  . ASP C 1 701  ? 41.131  1.998   77.031  1.00 248.14 ? 701  ASP B CA  1 
ATOM   17692 C  C   . ASP C 1 701  ? 40.292  0.910   77.685  1.00 243.15 ? 701  ASP B C   1 
ATOM   17693 O  O   . ASP C 1 701  ? 40.624  -0.272  77.622  1.00 242.37 ? 701  ASP B O   1 
ATOM   17694 C  CB  . ASP C 1 701  ? 42.390  2.275   77.861  1.00 252.96 ? 701  ASP B CB  1 
ATOM   17695 C  CG  . ASP C 1 701  ? 42.082  2.634   79.315  1.00 254.67 ? 701  ASP B CG  1 
ATOM   17696 O  OD1 . ASP C 1 701  ? 40.977  2.304   79.796  1.00 252.81 ? 701  ASP B OD1 1 
ATOM   17697 O  OD2 . ASP C 1 701  ? 42.952  3.239   79.985  1.00 257.46 ? 701  ASP B OD2 1 
ATOM   17698 N  N   . GLY C 1 702  ? 39.199  1.340   78.311  1.00 273.39 ? 702  GLY B N   1 
ATOM   17699 C  CA  . GLY C 1 702  ? 38.309  0.459   79.036  1.00 266.85 ? 702  GLY B CA  1 
ATOM   17700 C  C   . GLY C 1 702  ? 38.062  -0.824  78.282  1.00 260.34 ? 702  GLY B C   1 
ATOM   17701 O  O   . GLY C 1 702  ? 38.457  -1.891  78.736  1.00 258.02 ? 702  GLY B O   1 
ATOM   17702 N  N   . ALA C 1 703  ? 37.427  -0.727  77.123  1.00 180.57 ? 703  ALA B N   1 
ATOM   17703 C  CA  . ALA C 1 703  ? 37.199  -1.903  76.296  1.00 185.09 ? 703  ALA B CA  1 
ATOM   17704 C  C   . ALA C 1 703  ? 38.512  -2.461  75.733  1.00 182.23 ? 703  ALA B C   1 
ATOM   17705 O  O   . ALA C 1 703  ? 38.679  -3.687  75.617  1.00 181.03 ? 703  ALA B O   1 
ATOM   17706 C  CB  . ALA C 1 703  ? 36.261  -1.552  75.166  1.00 184.97 ? 703  ALA B CB  1 
ATOM   17707 N  N   . CYS C 1 704  ? 39.438  -1.542  75.431  1.00 187.91 ? 704  CYS B N   1 
ATOM   17708 C  CA  . CYS C 1 704  ? 40.599  -1.772  74.549  1.00 190.61 ? 704  CYS B CA  1 
ATOM   17709 C  C   . CYS C 1 704  ? 40.554  -3.099  73.768  1.00 188.03 ? 704  CYS B C   1 
ATOM   17710 O  O   . CYS C 1 704  ? 39.693  -3.283  72.910  1.00 186.26 ? 704  CYS B O   1 
ATOM   17711 C  CB  . CYS C 1 704  ? 41.942  -1.550  75.264  1.00 191.90 ? 704  CYS B CB  1 
ATOM   17712 S  SG  . CYS C 1 704  ? 43.248  -0.864  74.188  1.00 194.97 ? 704  CYS B SG  1 
ATOM   17713 N  N   . VAL C 1 705  ? 41.469  -4.019  74.046  1.00 243.62 ? 705  VAL B N   1 
ATOM   17714 C  CA  . VAL C 1 705  ? 41.496  -5.283  73.306  1.00 242.41 ? 705  VAL B CA  1 
ATOM   17715 C  C   . VAL C 1 705  ? 42.024  -6.442  74.147  1.00 244.87 ? 705  VAL B C   1 
ATOM   17716 O  O   . VAL C 1 705  ? 43.116  -6.957  73.893  1.00 248.80 ? 705  VAL B O   1 
ATOM   17717 C  CB  . VAL C 1 705  ? 42.324  -5.173  71.993  1.00 241.01 ? 705  VAL B CB  1 
ATOM   17718 C  CG1 . VAL C 1 705  ? 41.430  -4.810  70.810  1.00 240.25 ? 705  VAL B CG1 1 
ATOM   17719 C  CG2 . VAL C 1 705  ? 43.460  -4.167  72.147  1.00 242.97 ? 705  VAL B CG2 1 
ATOM   17720 N  N   . ASN C 1 706  ? 41.249  -6.857  75.145  1.00 276.01 ? 706  ASN B N   1 
ATOM   17721 C  CA  . ASN C 1 706  ? 41.714  -7.907  76.044  1.00 277.84 ? 706  ASN B CA  1 
ATOM   17722 C  C   . ASN C 1 706  ? 40.843  -9.155  76.047  1.00 273.10 ? 706  ASN B C   1 
ATOM   17723 O  O   . ASN C 1 706  ? 39.755  -9.180  76.628  1.00 271.70 ? 706  ASN B O   1 
ATOM   17724 C  CB  . ASN C 1 706  ? 41.910  -7.375  77.464  1.00 282.85 ? 706  ASN B CB  1 
ATOM   17725 C  CG  . ASN C 1 706  ? 43.243  -7.780  78.055  1.00 287.95 ? 706  ASN B CG  1 
ATOM   17726 O  OD1 . ASN C 1 706  ? 43.955  -8.612  77.488  1.00 289.13 ? 706  ASN B OD1 1 
ATOM   17727 N  ND2 . ASN C 1 706  ? 43.593  -7.192  79.197  1.00 291.30 ? 706  ASN B ND2 1 
ATOM   17728 N  N   . ASN C 1 707  ? 41.357  -10.190 75.391  1.00 238.28 ? 707  ASN B N   1 
ATOM   17729 C  CA  . ASN C 1 707  ? 40.667  -11.465 75.250  1.00 234.70 ? 707  ASN B CA  1 
ATOM   17730 C  C   . ASN C 1 707  ? 41.211  -12.596 76.135  1.00 231.65 ? 707  ASN B C   1 
ATOM   17731 O  O   . ASN C 1 707  ? 40.711  -13.717 76.072  1.00 227.27 ? 707  ASN B O   1 
ATOM   17732 C  CB  . ASN C 1 707  ? 40.615  -11.910 73.774  1.00 236.16 ? 707  ASN B CB  1 
ATOM   17733 C  CG  . ASN C 1 707  ? 41.835  -11.465 72.964  1.00 238.83 ? 707  ASN B CG  1 
ATOM   17734 O  OD1 . ASN C 1 707  ? 42.561  -10.553 73.353  1.00 240.34 ? 707  ASN B OD1 1 
ATOM   17735 N  ND2 . ASN C 1 707  ? 42.047  -12.105 71.818  1.00 239.04 ? 707  ASN B ND2 1 
ATOM   17736 N  N   . ASP C 1 708  ? 42.229  -12.304 76.950  1.00 199.19 ? 708  ASP B N   1 
ATOM   17737 C  CA  . ASP C 1 708  ? 42.855  -13.314 77.822  1.00 205.34 ? 708  ASP B CA  1 
ATOM   17738 C  C   . ASP C 1 708  ? 42.247  -13.377 79.227  1.00 204.50 ? 708  ASP B C   1 
ATOM   17739 O  O   . ASP C 1 708  ? 42.577  -14.256 80.017  1.00 203.79 ? 708  ASP B O   1 
ATOM   17740 C  CB  . ASP C 1 708  ? 44.372  -13.091 77.935  1.00 203.08 ? 708  ASP B CB  1 
ATOM   17741 C  CG  . ASP C 1 708  ? 45.167  -13.805 76.841  1.00 205.45 ? 708  ASP B CG  1 
ATOM   17742 O  OD1 . ASP C 1 708  ? 44.575  -14.571 76.054  1.00 199.22 ? 708  ASP B OD1 1 
ATOM   17743 O  OD2 . ASP C 1 708  ? 46.398  -13.604 76.775  1.00 205.10 ? 708  ASP B OD2 1 
ATOM   17744 N  N   . GLU C 1 709  ? 41.367  -12.439 79.537  1.00 216.81 ? 709  GLU B N   1 
ATOM   17745 C  CA  . GLU C 1 709  ? 40.765  -12.388 80.856  1.00 218.83 ? 709  GLU B CA  1 
ATOM   17746 C  C   . GLU C 1 709  ? 39.483  -11.581 80.782  1.00 218.59 ? 709  GLU B C   1 
ATOM   17747 O  O   . GLU C 1 709  ? 39.417  -10.588 80.061  1.00 221.90 ? 709  GLU B O   1 
ATOM   17748 C  CB  . GLU C 1 709  ? 41.748  -11.784 81.867  1.00 223.57 ? 709  GLU B CB  1 
ATOM   17749 C  CG  . GLU C 1 709  ? 42.623  -10.645 81.315  1.00 226.45 ? 709  GLU B CG  1 
ATOM   17750 C  CD  . GLU C 1 709  ? 43.649  -10.109 82.325  1.00 229.40 ? 709  GLU B CD  1 
ATOM   17751 O  OE1 . GLU C 1 709  ? 43.569  -10.474 83.521  1.00 229.29 ? 709  GLU B OE1 1 
ATOM   17752 O  OE2 . GLU C 1 709  ? 44.536  -9.318  81.918  1.00 231.12 ? 709  GLU B OE2 1 
ATOM   17753 N  N   . THR C 1 710  ? 38.468  -12.011 81.524  1.00 241.64 ? 710  THR B N   1 
ATOM   17754 C  CA  . THR C 1 710  ? 37.133  -11.438 81.411  1.00 241.77 ? 710  THR B CA  1 
ATOM   17755 C  C   . THR C 1 710  ? 37.134  -9.932  81.597  1.00 246.73 ? 710  THR B C   1 
ATOM   17756 O  O   . THR C 1 710  ? 38.183  -9.308  81.741  1.00 248.59 ? 710  THR B O   1 
ATOM   17757 C  CB  . THR C 1 710  ? 36.157  -12.060 82.421  1.00 261.71 ? 710  THR B CB  1 
ATOM   17758 O  OG1 . THR C 1 710  ? 36.166  -11.301 83.636  1.00 263.14 ? 710  THR B OG1 1 
ATOM   17759 C  CG2 . THR C 1 710  ? 36.539  -13.502 82.705  1.00 261.66 ? 710  THR B CG2 1 
ATOM   17760 N  N   . CYS C 1 711  ? 35.950  -9.340  81.576  1.00 252.32 ? 711  CYS B N   1 
ATOM   17761 C  CA  . CYS C 1 711  ? 35.872  -7.904  81.748  1.00 257.36 ? 711  CYS B CA  1 
ATOM   17762 C  C   . CYS C 1 711  ? 35.824  -7.493  83.211  1.00 259.58 ? 711  CYS B C   1 
ATOM   17763 O  O   . CYS C 1 711  ? 36.192  -6.369  83.536  1.00 263.36 ? 711  CYS B O   1 
ATOM   17764 C  CB  . CYS C 1 711  ? 34.715  -7.297  80.956  1.00 258.17 ? 711  CYS B CB  1 
ATOM   17765 S  SG  . CYS C 1 711  ? 35.268  -6.363  79.497  1.00 257.69 ? 711  CYS B SG  1 
ATOM   17766 N  N   . GLU C 1 712  ? 35.395  -8.386  84.099  1.00 228.97 ? 712  GLU B N   1 
ATOM   17767 C  CA  . GLU C 1 712  ? 35.446  -8.064  85.529  1.00 230.83 ? 712  GLU B CA  1 
ATOM   17768 C  C   . GLU C 1 712  ? 36.654  -8.653  86.263  1.00 227.55 ? 712  GLU B C   1 
ATOM   17769 O  O   . GLU C 1 712  ? 36.827  -8.454  87.469  1.00 227.62 ? 712  GLU B O   1 
ATOM   17770 C  CB  . GLU C 1 712  ? 34.144  -8.421  86.224  1.00 236.49 ? 712  GLU B CB  1 
ATOM   17771 C  CG  . GLU C 1 712  ? 33.466  -9.614  85.644  1.00 240.21 ? 712  GLU B CG  1 
ATOM   17772 C  CD  . GLU C 1 712  ? 32.131  -9.837  86.283  1.00 244.50 ? 712  GLU B CD  1 
ATOM   17773 O  OE1 . GLU C 1 712  ? 31.199  -9.078  85.961  1.00 246.19 ? 712  GLU B OE1 1 
ATOM   17774 O  OE2 . GLU C 1 712  ? 32.021  -10.755 87.118  1.00 245.91 ? 712  GLU B OE2 1 
ATOM   17775 N  N   . GLN C 1 713  ? 37.482  -9.382  85.522  1.00 262.79 ? 713  GLN B N   1 
ATOM   17776 C  CA  . GLN C 1 713  ? 38.818  -9.736  85.985  1.00 261.97 ? 713  GLN B CA  1 
ATOM   17777 C  C   . GLN C 1 713  ? 39.728  -8.513  85.867  1.00 260.74 ? 713  GLN B C   1 
ATOM   17778 O  O   . GLN C 1 713  ? 40.462  -8.186  86.794  1.00 263.82 ? 713  GLN B O   1 
ATOM   17779 C  CB  . GLN C 1 713  ? 39.389  -10.884 85.155  1.00 261.17 ? 713  GLN B CB  1 
ATOM   17780 C  CG  . GLN C 1 713  ? 38.673  -12.208 85.323  1.00 259.47 ? 713  GLN B CG  1 
ATOM   17781 C  CD  . GLN C 1 713  ? 39.259  -13.291 84.440  1.00 258.65 ? 713  GLN B CD  1 
ATOM   17782 O  OE1 . GLN C 1 713  ? 39.517  -13.073 83.263  1.00 258.03 ? 713  GLN B OE1 1 
ATOM   17783 N  NE2 . GLN C 1 713  ? 39.471  -14.468 85.008  1.00 258.82 ? 713  GLN B NE2 1 
ATOM   17784 N  N   . ARG C 1 714  ? 39.671  -7.847  84.714  1.00 284.13 ? 714  ARG B N   1 
ATOM   17785 C  CA  . ARG C 1 714  ? 40.404  -6.602  84.480  1.00 283.46 ? 714  ARG B CA  1 
ATOM   17786 C  C   . ARG C 1 714  ? 39.888  -5.498  85.398  1.00 280.58 ? 714  ARG B C   1 
ATOM   17787 O  O   . ARG C 1 714  ? 40.613  -4.557  85.724  1.00 281.44 ? 714  ARG B O   1 
ATOM   17788 C  CB  . ARG C 1 714  ? 40.248  -6.155  83.021  1.00 283.86 ? 714  ARG B CB  1 
ATOM   17789 C  CG  . ARG C 1 714  ? 40.781  -7.135  81.993  1.00 284.97 ? 714  ARG B CG  1 
ATOM   17790 C  CD  . ARG C 1 714  ? 40.000  -7.058  80.681  1.00 285.81 ? 714  ARG B CD  1 
ATOM   17791 N  NE  . ARG C 1 714  ? 40.259  -5.823  79.949  1.00 290.70 ? 714  ARG B NE  1 
ATOM   17792 C  CZ  . ARG C 1 714  ? 39.807  -5.571  78.722  1.00 292.84 ? 714  ARG B CZ  1 
ATOM   17793 N  NH1 . ARG C 1 714  ? 39.076  -6.471  78.072  1.00 290.66 ? 714  ARG B NH1 1 
ATOM   17794 N  NH2 . ARG C 1 714  ? 40.096  -4.419  78.135  1.00 295.59 ? 714  ARG B NH2 1 
ATOM   17795 N  N   . ALA C 1 715  ? 38.623  -5.626  85.795  1.00 221.29 ? 715  ALA B N   1 
ATOM   17796 C  CA  . ALA C 1 715  ? 37.929  -4.644  86.629  1.00 219.94 ? 715  ALA B CA  1 
ATOM   17797 C  C   . ALA C 1 715  ? 38.289  -4.789  88.107  1.00 219.89 ? 715  ALA B C   1 
ATOM   17798 O  O   . ALA C 1 715  ? 37.893  -3.971  88.946  1.00 222.94 ? 715  ALA B O   1 
ATOM   17799 C  CB  . ALA C 1 715  ? 36.425  -4.763  86.441  1.00 213.86 ? 715  ALA B CB  1 
ATOM   17800 N  N   . ALA C 1 716  ? 39.033  -5.845  88.419  1.00 242.93 ? 716  ALA B N   1 
ATOM   17801 C  CA  . ALA C 1 716  ? 39.546  -6.052  89.765  1.00 247.08 ? 716  ALA B CA  1 
ATOM   17802 C  C   . ALA C 1 716  ? 40.776  -5.176  89.998  1.00 250.82 ? 716  ALA B C   1 
ATOM   17803 O  O   . ALA C 1 716  ? 40.804  -4.354  90.915  1.00 253.32 ? 716  ALA B O   1 
ATOM   17804 C  CB  . ALA C 1 716  ? 39.887  -7.518  89.966  1.00 246.41 ? 716  ALA B CB  1 
ATOM   17805 N  N   . ARG C 1 717  ? 41.773  -5.355  89.133  1.00 197.34 ? 717  ARG B N   1 
ATOM   17806 C  CA  . ARG C 1 717  ? 43.045  -4.631  89.165  1.00 202.71 ? 717  ARG B CA  1 
ATOM   17807 C  C   . ARG C 1 717  ? 42.858  -3.120  89.160  1.00 203.96 ? 717  ARG B C   1 
ATOM   17808 O  O   . ARG C 1 717  ? 43.821  -2.358  89.307  1.00 206.35 ? 717  ARG B O   1 
ATOM   17809 C  CB  . ARG C 1 717  ? 43.877  -5.039  87.950  1.00 205.50 ? 717  ARG B CB  1 
ATOM   17810 C  CG  . ARG C 1 717  ? 45.374  -4.853  88.074  1.00 204.32 ? 717  ARG B CG  1 
ATOM   17811 C  CD  . ARG C 1 717  ? 46.069  -5.581  86.942  1.00 204.91 ? 717  ARG B CD  1 
ATOM   17812 N  NE  . ARG C 1 717  ? 45.353  -6.798  86.566  1.00 200.62 ? 717  ARG B NE  1 
ATOM   17813 C  CZ  . ARG C 1 717  ? 44.506  -6.887  85.541  1.00 202.85 ? 717  ARG B CZ  1 
ATOM   17814 N  NH1 . ARG C 1 717  ? 44.268  -5.828  84.775  1.00 201.55 ? 717  ARG B NH1 1 
ATOM   17815 N  NH2 . ARG C 1 717  ? 43.893  -8.036  85.279  1.00 200.20 ? 717  ARG B NH2 1 
ATOM   17816 N  N   . ILE C 1 718  ? 41.610  -2.698  88.974  1.00 247.33 ? 718  ILE B N   1 
ATOM   17817 C  CA  . ILE C 1 718  ? 41.265  -1.284  88.911  1.00 251.78 ? 718  ILE B CA  1 
ATOM   17818 C  C   . ILE C 1 718  ? 41.261  -0.610  90.284  1.00 259.93 ? 718  ILE B C   1 
ATOM   17819 O  O   . ILE C 1 718  ? 40.499  -0.977  91.186  1.00 257.51 ? 718  ILE B O   1 
ATOM   17820 C  CB  . ILE C 1 718  ? 39.926  -1.040  88.152  1.00 246.38 ? 718  ILE B CB  1 
ATOM   17821 C  CG1 . ILE C 1 718  ? 40.174  -0.999  86.641  1.00 246.25 ? 718  ILE B CG1 1 
ATOM   17822 C  CG2 . ILE C 1 718  ? 39.271  0.255   88.596  1.00 247.23 ? 718  ILE B CG2 1 
ATOM   17823 C  CD1 . ILE C 1 718  ? 39.031  -0.403  85.854  1.00 245.72 ? 718  ILE B CD1 1 
ATOM   17824 N  N   . SER C 1 719  ? 42.142  0.380   90.400  1.00 178.85 ? 719  SER B N   1 
ATOM   17825 C  CA  . SER C 1 719  ? 42.356  1.163   91.600  1.00 180.50 ? 719  SER B CA  1 
ATOM   17826 C  C   . SER C 1 719  ? 41.577  2.473   91.589  1.00 179.47 ? 719  SER B C   1 
ATOM   17827 O  O   . SER C 1 719  ? 40.503  2.570   92.175  1.00 178.51 ? 719  SER B O   1 
ATOM   17828 C  CB  . SER C 1 719  ? 43.842  1.485   91.706  1.00 183.15 ? 719  SER B CB  1 
ATOM   17829 O  OG  . SER C 1 719  ? 44.102  2.296   92.837  1.00 184.92 ? 719  SER B OG  1 
ATOM   17830 N  N   . LEU C 1 720  ? 42.141  3.465   90.904  1.00 276.80 ? 720  LEU B N   1 
ATOM   17831 C  CA  . LEU C 1 720  ? 41.640  4.847   90.851  1.00 281.82 ? 720  LEU B CA  1 
ATOM   17832 C  C   . LEU C 1 720  ? 40.293  5.131   91.528  1.00 285.16 ? 720  LEU B C   1 
ATOM   17833 O  O   . LEU C 1 720  ? 40.154  6.126   92.236  1.00 283.92 ? 720  LEU B O   1 
ATOM   17834 C  CB  . LEU C 1 720  ? 41.593  5.344   89.402  1.00 283.59 ? 720  LEU B CB  1 
ATOM   17835 C  CG  . LEU C 1 720  ? 42.812  5.147   88.494  1.00 292.87 ? 720  LEU B CG  1 
ATOM   17836 C  CD1 . LEU C 1 720  ? 42.504  5.661   87.087  1.00 291.94 ? 720  LEU B CD1 1 
ATOM   17837 C  CD2 . LEU C 1 720  ? 44.054  5.825   89.059  1.00 299.45 ? 720  LEU B CD2 1 
ATOM   17838 N  N   . GLY C 1 721  ? 39.295  4.289   91.279  1.00 267.29 ? 721  GLY B N   1 
ATOM   17839 C  CA  . GLY C 1 721  ? 38.017  4.425   91.951  1.00 271.56 ? 721  GLY B CA  1 
ATOM   17840 C  C   . GLY C 1 721  ? 36.887  3.660   91.292  1.00 272.57 ? 721  GLY B C   1 
ATOM   17841 O  O   . GLY C 1 721  ? 36.798  3.604   90.065  1.00 272.54 ? 721  GLY B O   1 
ATOM   17842 N  N   . PRO C 1 722  ? 36.010  3.063   92.113  1.00 299.31 ? 722  PRO B N   1 
ATOM   17843 C  CA  . PRO C 1 722  ? 34.794  2.373   91.671  1.00 294.85 ? 722  PRO B CA  1 
ATOM   17844 C  C   . PRO C 1 722  ? 33.888  3.293   90.852  1.00 287.65 ? 722  PRO B C   1 
ATOM   17845 O  O   . PRO C 1 722  ? 33.000  2.825   90.136  1.00 284.00 ? 722  PRO B O   1 
ATOM   17846 C  CB  . PRO C 1 722  ? 34.114  1.991   92.989  1.00 296.74 ? 722  PRO B CB  1 
ATOM   17847 C  CG  . PRO C 1 722  ? 35.223  1.892   93.965  1.00 300.04 ? 722  PRO B CG  1 
ATOM   17848 C  CD  . PRO C 1 722  ? 36.214  2.943   93.566  1.00 300.97 ? 722  PRO B CD  1 
ATOM   17849 N  N   . ARG C 1 723  ? 34.115  4.596   90.960  1.00 268.22 ? 723  ARG B N   1 
ATOM   17850 C  CA  . ARG C 1 723  ? 33.373  5.558   90.165  1.00 261.98 ? 723  ARG B CA  1 
ATOM   17851 C  C   . ARG C 1 723  ? 33.465  5.180   88.693  1.00 258.90 ? 723  ARG B C   1 
ATOM   17852 O  O   . ARG C 1 723  ? 32.498  5.310   87.947  1.00 257.10 ? 723  ARG B O   1 
ATOM   17853 C  CB  . ARG C 1 723  ? 33.955  6.956   90.357  1.00 258.69 ? 723  ARG B CB  1 
ATOM   17854 C  CG  . ARG C 1 723  ? 34.489  7.236   91.750  1.00 257.02 ? 723  ARG B CG  1 
ATOM   17855 C  CD  . ARG C 1 723  ? 35.180  8.587   91.789  1.00 253.94 ? 723  ARG B CD  1 
ATOM   17856 N  NE  . ARG C 1 723  ? 35.756  8.868   93.097  1.00 254.00 ? 723  ARG B NE  1 
ATOM   17857 C  CZ  . ARG C 1 723  ? 37.036  8.694   93.401  1.00 256.14 ? 723  ARG B CZ  1 
ATOM   17858 N  NH1 . ARG C 1 723  ? 37.885  8.244   92.485  1.00 256.65 ? 723  ARG B NH1 1 
ATOM   17859 N  NH2 . ARG C 1 723  ? 37.467  8.978   94.622  1.00 258.45 ? 723  ARG B NH2 1 
ATOM   17860 N  N   . CYS C 1 724  ? 34.636  4.710   88.279  1.00 279.28 ? 724  CYS B N   1 
ATOM   17861 C  CA  . CYS C 1 724  ? 34.866  4.413   86.870  1.00 276.01 ? 724  CYS B CA  1 
ATOM   17862 C  C   . CYS C 1 724  ? 34.727  2.929   86.517  1.00 276.83 ? 724  CYS B C   1 
ATOM   17863 O  O   . CYS C 1 724  ? 34.480  2.583   85.357  1.00 274.28 ? 724  CYS B O   1 
ATOM   17864 C  CB  . CYS C 1 724  ? 36.229  4.950   86.422  1.00 276.23 ? 724  CYS B CB  1 
ATOM   17865 S  SG  . CYS C 1 724  ? 37.659  4.052   87.072  1.00 248.74 ? 724  CYS B SG  1 
ATOM   17866 N  N   . ILE C 1 725  ? 34.883  2.056   87.509  1.00 279.47 ? 725  ILE B N   1 
ATOM   17867 C  CA  . ILE C 1 725  ? 34.771  0.620   87.268  1.00 280.79 ? 725  ILE B CA  1 
ATOM   17868 C  C   . ILE C 1 725  ? 33.543  0.325   86.400  1.00 279.35 ? 725  ILE B C   1 
ATOM   17869 O  O   . ILE C 1 725  ? 33.597  -0.508  85.494  1.00 279.78 ? 725  ILE B O   1 
ATOM   17870 C  CB  . ILE C 1 725  ? 34.726  -0.194  88.591  1.00 281.72 ? 725  ILE B CB  1 
ATOM   17871 C  CG1 . ILE C 1 725  ? 36.050  -0.055  89.358  1.00 283.63 ? 725  ILE B CG1 1 
ATOM   17872 C  CG2 . ILE C 1 725  ? 34.420  -1.660  88.309  1.00 278.06 ? 725  ILE B CG2 1 
ATOM   17873 C  CD1 . ILE C 1 725  ? 36.177  -0.958  90.589  1.00 283.62 ? 725  ILE B CD1 1 
ATOM   17874 N  N   . LYS C 1 726  ? 32.446  1.030   86.668  1.00 274.72 ? 726  LYS B N   1 
ATOM   17875 C  CA  . LYS C 1 726  ? 31.241  0.893   85.861  1.00 272.85 ? 726  LYS B CA  1 
ATOM   17876 C  C   . LYS C 1 726  ? 31.525  1.267   84.417  1.00 265.25 ? 726  LYS B C   1 
ATOM   17877 O  O   . LYS C 1 726  ? 31.158  0.538   83.501  1.00 262.20 ? 726  LYS B O   1 
ATOM   17878 C  CB  . LYS C 1 726  ? 30.106  1.760   86.408  1.00 278.38 ? 726  LYS B CB  1 
ATOM   17879 C  CG  . LYS C 1 726  ? 29.197  1.048   87.398  1.00 286.98 ? 726  LYS B CG  1 
ATOM   17880 C  CD  . LYS C 1 726  ? 27.814  1.686   87.428  1.00 290.28 ? 726  LYS B CD  1 
ATOM   17881 C  CE  . LYS C 1 726  ? 26.835  0.869   88.258  1.00 294.57 ? 726  LYS B CE  1 
ATOM   17882 N  NZ  . LYS C 1 726  ? 25.433  1.349   88.088  1.00 293.54 ? 726  LYS B NZ  1 
ATOM   17883 N  N   . ALA C 1 727  ? 32.184  2.406   84.223  1.00 324.22 ? 727  ALA B N   1 
ATOM   17884 C  CA  . ALA C 1 727  ? 32.526  2.887   82.889  1.00 320.49 ? 727  ALA B CA  1 
ATOM   17885 C  C   . ALA C 1 727  ? 33.495  1.935   82.202  1.00 316.99 ? 727  ALA B C   1 
ATOM   17886 O  O   . ALA C 1 727  ? 33.724  2.020   80.998  1.00 315.47 ? 727  ALA B O   1 
ATOM   17887 C  CB  . ALA C 1 727  ? 33.117  4.280   82.965  1.00 320.61 ? 727  ALA B CB  1 
ATOM   17888 N  N   . PHE C 1 728  ? 34.072  1.028   82.978  1.00 225.73 ? 728  PHE B N   1 
ATOM   17889 C  CA  . PHE C 1 728  ? 34.955  0.021   82.412  1.00 222.21 ? 728  PHE B CA  1 
ATOM   17890 C  C   . PHE C 1 728  ? 34.187  -1.195  81.849  1.00 221.42 ? 728  PHE B C   1 
ATOM   17891 O  O   . PHE C 1 728  ? 34.123  -1.383  80.624  1.00 221.57 ? 728  PHE B O   1 
ATOM   17892 C  CB  . PHE C 1 728  ? 35.982  -0.412  83.447  1.00 214.19 ? 728  PHE B CB  1 
ATOM   17893 C  CG  . PHE C 1 728  ? 37.085  -1.233  82.881  1.00 206.10 ? 728  PHE B CG  1 
ATOM   17894 C  CD1 . PHE C 1 728  ? 37.958  -0.692  81.955  1.00 204.78 ? 728  PHE B CD1 1 
ATOM   17895 C  CD2 . PHE C 1 728  ? 37.253  -2.547  83.272  1.00 201.96 ? 728  PHE B CD2 1 
ATOM   17896 C  CE1 . PHE C 1 728  ? 38.983  -1.447  81.428  1.00 203.17 ? 728  PHE B CE1 1 
ATOM   17897 C  CE2 . PHE C 1 728  ? 38.274  -3.311  82.750  1.00 200.01 ? 728  PHE B CE2 1 
ATOM   17898 C  CZ  . PHE C 1 728  ? 39.142  -2.762  81.825  1.00 201.15 ? 728  PHE B CZ  1 
ATOM   17899 N  N   . THR C 1 729  ? 33.593  -1.995  82.741  1.00 217.77 ? 729  THR B N   1 
ATOM   17900 C  CA  . THR C 1 729  ? 32.882  -3.241  82.383  1.00 214.54 ? 729  THR B CA  1 
ATOM   17901 C  C   . THR C 1 729  ? 31.613  -3.062  81.535  1.00 214.64 ? 729  THR B C   1 
ATOM   17902 O  O   . THR C 1 729  ? 31.154  -3.995  80.869  1.00 211.93 ? 729  THR B O   1 
ATOM   17903 C  CB  . THR C 1 729  ? 32.508  -4.040  83.657  1.00 241.80 ? 729  THR B CB  1 
ATOM   17904 O  OG1 . THR C 1 729  ? 32.615  -3.186  84.805  1.00 244.32 ? 729  THR B OG1 1 
ATOM   17905 C  CG2 . THR C 1 729  ? 33.430  -5.240  83.845  1.00 241.05 ? 729  THR B CG2 1 
ATOM   17906 N  N   . GLU C 1 730  ? 31.042  -1.866  81.597  1.00 281.11 ? 730  GLU B N   1 
ATOM   17907 C  CA  . GLU C 1 730  ? 29.946  -1.480  80.726  1.00 282.97 ? 730  GLU B CA  1 
ATOM   17908 C  C   . GLU C 1 730  ? 30.450  -1.426  79.304  1.00 283.16 ? 730  GLU B C   1 
ATOM   17909 O  O   . GLU C 1 730  ? 29.857  -1.990  78.384  1.00 280.56 ? 730  GLU B O   1 
ATOM   17910 C  CB  . GLU C 1 730  ? 29.459  -0.082  81.098  1.00 282.89 ? 730  GLU B CB  1 
ATOM   17911 C  CG  . GLU C 1 730  ? 28.575  -0.026  82.327  1.00 281.78 ? 730  GLU B CG  1 
ATOM   17912 C  CD  . GLU C 1 730  ? 27.112  -0.091  81.977  1.00 278.49 ? 730  GLU B CD  1 
ATOM   17913 O  OE1 . GLU C 1 730  ? 26.760  0.310   80.843  1.00 274.93 ? 730  GLU B OE1 1 
ATOM   17914 O  OE2 . GLU C 1 730  ? 26.322  -0.534  82.839  1.00 279.03 ? 730  GLU B OE2 1 
ATOM   17915 N  N   . CYS C 1 731  ? 31.565  -0.731  79.142  1.00 384.19 ? 731  CYS B N   1 
ATOM   17916 C  CA  . CYS C 1 731  ? 32.066  -0.373  77.832  1.00 386.15 ? 731  CYS B CA  1 
ATOM   17917 C  C   . CYS C 1 731  ? 32.914  -1.476  77.206  1.00 386.57 ? 731  CYS B C   1 
ATOM   17918 O  O   . CYS C 1 731  ? 33.015  -1.566  75.983  1.00 386.25 ? 731  CYS B O   1 
ATOM   17919 C  CB  . CYS C 1 731  ? 32.819  0.946   77.946  1.00 385.15 ? 731  CYS B CB  1 
ATOM   17920 S  SG  . CYS C 1 731  ? 31.894  2.098   78.994  1.00 429.74 ? 731  CYS B SG  1 
ATOM   17921 N  N   . CYS C 1 732  ? 33.507  -2.325  78.040  1.00 307.02 ? 732  CYS B N   1 
ATOM   17922 C  CA  . CYS C 1 732  ? 34.235  -3.482  77.527  1.00 306.97 ? 732  CYS B CA  1 
ATOM   17923 C  C   . CYS C 1 732  ? 33.285  -4.545  76.959  1.00 304.84 ? 732  CYS B C   1 
ATOM   17924 O  O   . CYS C 1 732  ? 33.499  -5.042  75.850  1.00 304.80 ? 732  CYS B O   1 
ATOM   17925 C  CB  . CYS C 1 732  ? 35.139  -4.091  78.598  1.00 307.36 ? 732  CYS B CB  1 
ATOM   17926 S  SG  . CYS C 1 732  ? 36.221  -5.402  77.976  1.00 299.32 ? 732  CYS B SG  1 
ATOM   17927 N  N   . VAL C 1 733  ? 32.241  -4.885  77.718  1.00 278.29 ? 733  VAL B N   1 
ATOM   17928 C  CA  . VAL C 1 733  ? 31.225  -5.837  77.262  1.00 274.57 ? 733  VAL B CA  1 
ATOM   17929 C  C   . VAL C 1 733  ? 30.662  -5.388  75.920  1.00 272.06 ? 733  VAL B C   1 
ATOM   17930 O  O   . VAL C 1 733  ? 30.504  -6.182  74.997  1.00 268.97 ? 733  VAL B O   1 
ATOM   17931 C  CB  . VAL C 1 733  ? 30.063  -5.965  78.275  1.00 273.72 ? 733  VAL B CB  1 
ATOM   17932 C  CG1 . VAL C 1 733  ? 28.922  -6.784  77.679  1.00 273.00 ? 733  VAL B CG1 1 
ATOM   17933 C  CG2 . VAL C 1 733  ? 30.552  -6.572  79.585  1.00 273.09 ? 733  VAL B CG2 1 
ATOM   17934 N  N   . VAL C 1 734  ? 30.374  -4.099  75.822  1.00 310.99 ? 734  VAL B N   1 
ATOM   17935 C  CA  . VAL C 1 734  ? 29.882  -3.519  74.588  1.00 311.47 ? 734  VAL B CA  1 
ATOM   17936 C  C   . VAL C 1 734  ? 30.797  -3.849  73.406  1.00 312.34 ? 734  VAL B C   1 
ATOM   17937 O  O   . VAL C 1 734  ? 30.331  -4.301  72.358  1.00 313.16 ? 734  VAL B O   1 
ATOM   17938 C  CB  . VAL C 1 734  ? 29.745  -1.995  74.731  1.00 312.96 ? 734  VAL B CB  1 
ATOM   17939 C  CG1 . VAL C 1 734  ? 29.438  -1.352  73.387  1.00 312.49 ? 734  VAL B CG1 1 
ATOM   17940 C  CG2 . VAL C 1 734  ? 28.674  -1.663  75.759  1.00 313.50 ? 734  VAL B CG2 1 
ATOM   17941 N  N   . ALA C 1 735  ? 32.097  -3.636  73.586  1.00 345.24 ? 735  ALA B N   1 
ATOM   17942 C  CA  . ALA C 1 735  ? 33.068  -3.815  72.508  1.00 344.93 ? 735  ALA B CA  1 
ATOM   17943 C  C   . ALA C 1 735  ? 33.454  -5.276  72.296  1.00 343.89 ? 735  ALA B C   1 
ATOM   17944 O  O   . ALA C 1 735  ? 34.020  -5.635  71.264  1.00 343.70 ? 735  ALA B O   1 
ATOM   17945 C  CB  . ALA C 1 735  ? 34.306  -2.976  72.772  1.00 346.49 ? 735  ALA B CB  1 
ATOM   17946 N  N   . SER C 1 736  ? 33.144  -6.113  73.279  1.00 273.94 ? 736  SER B N   1 
ATOM   17947 C  CA  . SER C 1 736  ? 33.456  -7.535  73.203  1.00 273.77 ? 736  SER B CA  1 
ATOM   17948 C  C   . SER C 1 736  ? 32.402  -8.321  72.421  1.00 272.31 ? 736  SER B C   1 
ATOM   17949 O  O   . SER C 1 736  ? 32.739  -9.128  71.548  1.00 272.24 ? 736  SER B O   1 
ATOM   17950 C  CB  . SER C 1 736  ? 33.626  -8.106  74.607  1.00 273.59 ? 736  SER B CB  1 
ATOM   17951 O  OG  . SER C 1 736  ? 34.636  -7.397  75.305  1.00 275.22 ? 736  SER B OG  1 
ATOM   17952 N  N   . GLN C 1 737  ? 31.130  -8.084  72.730  1.00 235.02 ? 737  GLN B N   1 
ATOM   17953 C  CA  . GLN C 1 737  ? 30.043  -8.687  71.968  1.00 232.64 ? 737  GLN B CA  1 
ATOM   17954 C  C   . GLN C 1 737  ? 30.229  -8.327  70.496  1.00 232.75 ? 737  GLN B C   1 
ATOM   17955 O  O   . GLN C 1 737  ? 29.809  -9.062  69.601  1.00 230.08 ? 737  GLN B O   1 
ATOM   17956 C  CB  . GLN C 1 737  ? 28.686  -8.168  72.456  1.00 231.76 ? 737  GLN B CB  1 
ATOM   17957 C  CG  . GLN C 1 737  ? 28.613  -7.809  73.943  1.00 232.26 ? 737  GLN B CG  1 
ATOM   17958 C  CD  . GLN C 1 737  ? 28.537  -9.018  74.861  1.00 231.76 ? 737  GLN B CD  1 
ATOM   17959 O  OE1 . GLN C 1 737  ? 27.600  -9.811  74.789  1.00 231.79 ? 737  GLN B OE1 1 
ATOM   17960 N  NE2 . GLN C 1 737  ? 29.517  -9.151  75.743  1.00 231.40 ? 737  GLN B NE2 1 
ATOM   17961 N  N   . LEU C 1 738  ? 30.887  -7.191  70.271  1.00 290.22 ? 738  LEU B N   1 
ATOM   17962 C  CA  . LEU C 1 738  ? 31.060  -6.583  68.947  1.00 294.37 ? 738  LEU B CA  1 
ATOM   17963 C  C   . LEU C 1 738  ? 32.061  -7.271  68.010  1.00 300.56 ? 738  LEU B C   1 
ATOM   17964 O  O   . LEU C 1 738  ? 31.855  -7.297  66.797  1.00 301.87 ? 738  LEU B O   1 
ATOM   17965 C  CB  . LEU C 1 738  ? 31.460  -5.116  69.110  1.00 293.97 ? 738  LEU B CB  1 
ATOM   17966 C  CG  . LEU C 1 738  ? 31.647  -4.314  67.825  1.00 292.36 ? 738  LEU B CG  1 
ATOM   17967 C  CD1 . LEU C 1 738  ? 30.295  -3.862  67.300  1.00 291.12 ? 738  LEU B CD1 1 
ATOM   17968 C  CD2 . LEU C 1 738  ? 32.555  -3.123  68.075  1.00 292.93 ? 738  LEU B CD2 1 
ATOM   17969 N  N   . ARG C 1 739  ? 33.156  -7.792  68.559  1.00 306.57 ? 739  ARG B N   1 
ATOM   17970 C  CA  . ARG C 1 739  ? 34.154  -8.494  67.751  1.00 313.81 ? 739  ARG B CA  1 
ATOM   17971 C  C   . ARG C 1 739  ? 33.660  -9.880  67.363  1.00 313.93 ? 739  ARG B C   1 
ATOM   17972 O  O   . ARG C 1 739  ? 34.295  -10.581 66.575  1.00 314.54 ? 739  ARG B O   1 
ATOM   17973 C  CB  . ARG C 1 739  ? 35.475  -8.621  68.501  1.00 321.45 ? 739  ARG B CB  1 
ATOM   17974 C  CG  . ARG C 1 739  ? 35.419  -9.569  69.679  1.00 327.52 ? 739  ARG B CG  1 
ATOM   17975 C  CD  . ARG C 1 739  ? 36.753  -9.607  70.389  1.00 335.82 ? 739  ARG B CD  1 
ATOM   17976 N  NE  . ARG C 1 739  ? 36.711  -10.419 71.601  1.00 341.46 ? 739  ARG B NE  1 
ATOM   17977 C  CZ  . ARG C 1 739  ? 37.730  -10.547 72.447  1.00 346.49 ? 739  ARG B CZ  1 
ATOM   17978 N  NH1 . ARG C 1 739  ? 38.872  -9.913  72.210  1.00 349.33 ? 739  ARG B NH1 1 
ATOM   17979 N  NH2 . ARG C 1 739  ? 37.610  -11.306 73.530  1.00 347.35 ? 739  ARG B NH2 1 
ATOM   17980 N  N   . ALA C 1 740  ? 32.537  -10.281 67.948  1.00 259.08 ? 740  ALA B N   1 
ATOM   17981 C  CA  . ALA C 1 740  ? 31.873  -11.513 67.558  1.00 258.97 ? 740  ALA B CA  1 
ATOM   17982 C  C   . ALA C 1 740  ? 30.966  -11.259 66.361  1.00 257.42 ? 740  ALA B C   1 
ATOM   17983 O  O   . ALA C 1 740  ? 30.332  -12.182 65.859  1.00 259.62 ? 740  ALA B O   1 
ATOM   17984 C  CB  . ALA C 1 740  ? 31.072  -12.081 68.719  1.00 258.50 ? 740  ALA B CB  1 
ATOM   17985 N  N   . ASN C 1 741  ? 30.906  -10.009 65.905  1.00 327.89 ? 741  ASN B N   1 
ATOM   17986 C  CA  . ASN C 1 741  ? 30.002  -9.640  64.814  1.00 323.53 ? 741  ASN B CA  1 
ATOM   17987 C  C   . ASN C 1 741  ? 30.630  -8.890  63.622  1.00 334.19 ? 741  ASN B C   1 
ATOM   17988 O  O   . ASN C 1 741  ? 30.126  -8.983  62.497  1.00 335.14 ? 741  ASN B O   1 
ATOM   17989 C  CB  . ASN C 1 741  ? 28.787  -8.878  65.358  1.00 310.66 ? 741  ASN B CB  1 
ATOM   17990 C  CG  . ASN C 1 741  ? 27.761  -9.799  66.001  1.00 300.53 ? 741  ASN B CG  1 
ATOM   17991 O  OD1 . ASN C 1 741  ? 27.468  -9.685  67.193  1.00 297.86 ? 741  ASN B OD1 1 
ATOM   17992 N  ND2 . ASN C 1 741  ? 27.221  -10.733 65.212  1.00 294.76 ? 741  ASN B ND2 1 
ATOM   17993 N  N   . ILE C 1 742  ? 31.710  -8.145  63.860  1.00 345.16 ? 742  ILE B N   1 
ATOM   17994 C  CA  . ILE C 1 742  ? 32.433  -7.490  62.765  1.00 355.23 ? 742  ILE B CA  1 
ATOM   17995 C  C   . ILE C 1 742  ? 33.080  -8.552  61.886  1.00 359.77 ? 742  ILE B C   1 
ATOM   17996 O  O   . ILE C 1 742  ? 33.439  -8.296  60.737  1.00 361.07 ? 742  ILE B O   1 
ATOM   17997 C  CB  . ILE C 1 742  ? 33.556  -6.547  63.269  1.00 359.21 ? 742  ILE B CB  1 
ATOM   17998 C  CG1 . ILE C 1 742  ? 33.062  -5.637  64.397  1.00 359.79 ? 742  ILE B CG1 1 
ATOM   17999 C  CG2 . ILE C 1 742  ? 34.124  -5.722  62.115  1.00 361.37 ? 742  ILE B CG2 1 
ATOM   18000 C  CD1 . ILE C 1 742  ? 34.116  -4.658  64.891  1.00 361.31 ? 742  ILE B CD1 1 
ATOM   18001 N  N   . SER C 1 743  ? 33.219  -9.749  62.448  1.00 344.75 ? 743  SER B N   1 
ATOM   18002 C  CA  . SER C 1 743  ? 33.908  -10.849 61.791  1.00 346.93 ? 743  SER B CA  1 
ATOM   18003 C  C   . SER C 1 743  ? 33.447  -12.184 62.369  1.00 345.97 ? 743  SER B C   1 
ATOM   18004 O  O   . SER C 1 743  ? 33.402  -12.362 63.588  1.00 344.63 ? 743  SER B O   1 
ATOM   18005 C  CB  . SER C 1 743  ? 35.416  -10.707 61.984  1.00 349.39 ? 743  SER B CB  1 
ATOM   18006 O  OG  . SER C 1 743  ? 35.750  -10.790 63.358  1.00 349.17 ? 743  SER B OG  1 
ATOM   18007 N  N   . GLY C 1 750  ? 41.718  -15.982 60.331  1.00 254.14 ? 750  GLY B N   1 
ATOM   18008 C  CA  . GLY C 1 750  ? 41.753  -15.856 61.776  1.00 255.50 ? 750  GLY B CA  1 
ATOM   18009 C  C   . GLY C 1 750  ? 42.306  -14.529 62.271  1.00 258.27 ? 750  GLY B C   1 
ATOM   18010 O  O   . GLY C 1 750  ? 42.816  -14.446 63.390  1.00 258.00 ? 750  GLY B O   1 
ATOM   18011 N  N   . ARG C 1 751  ? 42.222  -13.492 61.438  1.00 334.40 ? 751  ARG B N   1 
ATOM   18012 C  CA  . ARG C 1 751  ? 42.669  -12.150 61.827  1.00 336.56 ? 751  ARG B CA  1 
ATOM   18013 C  C   . ARG C 1 751  ? 41.503  -11.251 62.250  1.00 341.58 ? 751  ARG B C   1 
ATOM   18014 O  O   . ARG C 1 751  ? 40.673  -10.869 61.423  1.00 341.08 ? 751  ARG B O   1 
ATOM   18015 C  CB  . ARG C 1 751  ? 43.463  -11.473 60.694  1.00 332.32 ? 751  ARG B CB  1 
ATOM   18016 C  CG  . ARG C 1 751  ? 44.913  -11.937 60.543  1.00 328.02 ? 751  ARG B CG  1 
ATOM   18017 C  CD  . ARG C 1 751  ? 45.684  -11.071 59.546  1.00 320.43 ? 751  ARG B CD  1 
ATOM   18018 N  NE  . ARG C 1 751  ? 44.986  -10.957 58.268  1.00 311.14 ? 751  ARG B NE  1 
ATOM   18019 C  CZ  . ARG C 1 751  ? 45.154  -11.789 57.246  1.00 305.11 ? 751  ARG B CZ  1 
ATOM   18020 N  NH1 . ARG C 1 751  ? 46.007  -12.801 57.341  1.00 305.62 ? 751  ARG B NH1 1 
ATOM   18021 N  NH2 . ARG C 1 751  ? 44.467  -11.608 56.126  1.00 300.50 ? 751  ARG B NH2 1 
ATOM   18022 N  N   . LEU C 1 752  ? 41.443  -10.919 63.539  1.00 375.98 ? 752  LEU B N   1 
ATOM   18023 C  CA  . LEU C 1 752  ? 40.465  -9.957  64.061  1.00 378.60 ? 752  LEU B CA  1 
ATOM   18024 C  C   . LEU C 1 752  ? 41.118  -9.153  65.176  1.00 379.03 ? 752  LEU B C   1 
ATOM   18025 O  O   . LEU C 1 752  ? 41.769  -9.717  66.054  1.00 380.40 ? 752  LEU B O   1 
ATOM   18026 C  CB  . LEU C 1 752  ? 39.211  -10.664 64.593  1.00 380.86 ? 752  LEU B CB  1 
ATOM   18027 C  CG  . LEU C 1 752  ? 38.171  -9.786  65.306  1.00 383.13 ? 752  LEU B CG  1 
ATOM   18028 C  CD1 . LEU C 1 752  ? 37.525  -8.778  64.355  1.00 384.39 ? 752  LEU B CD1 1 
ATOM   18029 C  CD2 . LEU C 1 752  ? 37.117  -10.646 65.980  1.00 382.53 ? 752  LEU B CD2 1 
ATOM   18030 N  N   . HIS C 1 753  ? 40.943  -7.837  65.152  1.00 414.49 ? 753  HIS B N   1 
ATOM   18031 C  CA  . HIS C 1 753  ? 41.663  -6.978  66.080  1.00 412.14 ? 753  HIS B CA  1 
ATOM   18032 C  C   . HIS C 1 753  ? 40.967  -5.621  66.251  1.00 401.42 ? 753  HIS B C   1 
ATOM   18033 O  O   . HIS C 1 753  ? 41.323  -4.655  65.605  1.00 401.06 ? 753  HIS B O   1 
ATOM   18034 C  CB  . HIS C 1 753  ? 43.122  -6.818  65.662  1.00 421.44 ? 753  HIS B CB  1 
ATOM   18035 C  CG  . HIS C 1 753  ? 43.511  -7.614  64.464  1.00 427.74 ? 753  HIS B CG  1 
ATOM   18036 N  ND1 . HIS C 1 753  ? 43.044  -7.389  63.173  1.00 430.14 ? 753  HIS B ND1 1 
ATOM   18037 C  CD2 . HIS C 1 753  ? 44.319  -8.685  64.347  1.00 430.91 ? 753  HIS B CD2 1 
ATOM   18038 C  CE1 . HIS C 1 753  ? 43.575  -8.250  62.337  1.00 432.13 ? 753  HIS B CE1 1 
ATOM   18039 N  NE2 . HIS C 1 753  ? 44.349  -9.065  63.031  1.00 432.70 ? 753  HIS B NE2 1 
ATOM   18040 N  N   . MET C 1 754  ? 39.981  -5.554  67.145  1.00 337.11 ? 754  MET B N   1 
ATOM   18041 C  CA  . MET C 1 754  ? 39.257  -4.307  67.402  1.00 329.07 ? 754  MET B CA  1 
ATOM   18042 C  C   . MET C 1 754  ? 40.249  -3.216  67.782  1.00 326.59 ? 754  MET B C   1 
ATOM   18043 O  O   . MET C 1 754  ? 41.397  -3.505  68.132  1.00 328.38 ? 754  MET B O   1 
ATOM   18044 C  CB  . MET C 1 754  ? 38.254  -4.481  68.549  1.00 324.16 ? 754  MET B CB  1 
ATOM   18045 C  CG  . MET C 1 754  ? 37.277  -5.635  68.397  1.00 319.64 ? 754  MET B CG  1 
ATOM   18046 S  SD  . MET C 1 754  ? 36.453  -5.955  69.969  1.00 294.11 ? 754  MET B SD  1 
ATOM   18047 C  CE  . MET C 1 754  ? 36.609  -4.350  70.750  1.00 233.86 ? 754  MET B CE  1 
ATOM   18048 N  N   . LYS C 1 755  ? 39.796  -1.966  67.709  1.00 269.99 ? 755  LYS B N   1 
ATOM   18049 C  CA  . LYS C 1 755  ? 40.567  -0.802  68.160  1.00 270.15 ? 755  LYS B CA  1 
ATOM   18050 C  C   . LYS C 1 755  ? 39.696  0.463   68.164  1.00 272.96 ? 755  LYS B C   1 
ATOM   18051 O  O   . LYS C 1 755  ? 38.616  0.498   67.571  1.00 269.48 ? 755  LYS B O   1 
ATOM   18052 C  CB  . LYS C 1 755  ? 41.810  -0.563  67.283  1.00 269.50 ? 755  LYS B CB  1 
ATOM   18053 C  CG  . LYS C 1 755  ? 43.008  -1.487  67.525  1.00 267.82 ? 755  LYS B CG  1 
ATOM   18054 C  CD  . LYS C 1 755  ? 43.313  -1.687  69.008  1.00 266.50 ? 755  LYS B CD  1 
ATOM   18055 C  CE  . LYS C 1 755  ? 43.594  -0.375  69.716  1.00 268.03 ? 755  LYS B CE  1 
ATOM   18056 N  NZ  . LYS C 1 755  ? 43.952  -0.579  71.155  1.00 267.70 ? 755  LYS B NZ  1 
ATOM   18057 N  N   . THR C 1 756  ? 40.177  1.496   68.847  1.00 242.15 ? 756  THR B N   1 
ATOM   18058 C  CA  . THR C 1 756  ? 39.587  2.832   68.796  1.00 247.36 ? 756  THR B CA  1 
ATOM   18059 C  C   . THR C 1 756  ? 40.688  3.817   69.179  1.00 255.24 ? 756  THR B C   1 
ATOM   18060 O  O   . THR C 1 756  ? 40.927  4.072   70.361  1.00 256.72 ? 756  THR B O   1 
ATOM   18061 C  CB  . THR C 1 756  ? 38.370  2.981   69.742  1.00 241.62 ? 756  THR B CB  1 
ATOM   18062 O  OG1 . THR C 1 756  ? 37.276  2.203   69.244  1.00 239.22 ? 756  THR B OG1 1 
ATOM   18063 C  CG2 . THR C 1 756  ? 37.932  4.436   69.839  1.00 237.35 ? 756  THR B CG2 1 
ATOM   18064 N  N   . LEU C 1 757  ? 41.362  4.355   68.163  1.00 217.97 ? 757  LEU B N   1 
ATOM   18065 C  CA  . LEU C 1 757  ? 42.618  5.088   68.351  1.00 227.02 ? 757  LEU B CA  1 
ATOM   18066 C  C   . LEU C 1 757  ? 42.512  6.316   69.278  1.00 228.67 ? 757  LEU B C   1 
ATOM   18067 O  O   . LEU C 1 757  ? 41.455  6.940   69.406  1.00 222.84 ? 757  LEU B O   1 
ATOM   18068 C  CB  . LEU C 1 757  ? 43.247  5.463   66.988  1.00 232.46 ? 757  LEU B CB  1 
ATOM   18069 C  CG  . LEU C 1 757  ? 44.702  5.969   66.908  1.00 240.41 ? 757  LEU B CG  1 
ATOM   18070 C  CD1 . LEU C 1 757  ? 45.723  4.837   67.029  1.00 246.33 ? 757  LEU B CD1 1 
ATOM   18071 C  CD2 . LEU C 1 757  ? 44.939  6.746   65.620  1.00 241.89 ? 757  LEU B CD2 1 
ATOM   18072 N  N   . LEU C 1 758  ? 43.629  6.619   69.935  1.00 285.28 ? 758  LEU B N   1 
ATOM   18073 C  CA  . LEU C 1 758  ? 43.818  7.831   70.728  1.00 288.96 ? 758  LEU B CA  1 
ATOM   18074 C  C   . LEU C 1 758  ? 45.206  7.745   71.355  1.00 306.72 ? 758  LEU B C   1 
ATOM   18075 O  O   . LEU C 1 758  ? 45.374  7.096   72.392  1.00 308.89 ? 758  LEU B O   1 
ATOM   18076 C  CB  . LEU C 1 758  ? 42.762  7.962   71.830  1.00 275.57 ? 758  LEU B CB  1 
ATOM   18077 C  CG  . LEU C 1 758  ? 42.344  9.374   72.271  1.00 262.52 ? 758  LEU B CG  1 
ATOM   18078 C  CD1 . LEU C 1 758  ? 41.569  9.348   73.584  1.00 257.06 ? 758  LEU B CD1 1 
ATOM   18079 C  CD2 . LEU C 1 758  ? 43.541  10.297  72.398  1.00 261.62 ? 758  LEU B CD2 1 
ATOM   18080 N  N   . PRO C 1 759  ? 46.210  8.381   70.720  1.00 445.02 ? 759  PRO B N   1 
ATOM   18081 C  CA  . PRO C 1 759  ? 47.587  8.377   71.232  1.00 457.65 ? 759  PRO B CA  1 
ATOM   18082 C  C   . PRO C 1 759  ? 47.686  8.947   72.648  1.00 464.90 ? 759  PRO B C   1 
ATOM   18083 O  O   . PRO C 1 759  ? 48.789  9.227   73.119  1.00 471.85 ? 759  PRO B O   1 
ATOM   18084 C  CB  . PRO C 1 759  ? 48.330  9.285   70.245  1.00 457.52 ? 759  PRO B CB  1 
ATOM   18085 C  CG  . PRO C 1 759  ? 47.546  9.191   68.986  1.00 452.93 ? 759  PRO B CG  1 
ATOM   18086 C  CD  . PRO C 1 759  ? 46.111  9.063   69.417  1.00 445.99 ? 759  PRO B CD  1 
ATOM   18087 N  N   . VAL C 1 760  ? 46.541  9.111   73.308  1.00 377.95 ? 760  VAL B N   1 
ATOM   18088 C  CA  . VAL C 1 760  ? 46.477  9.664   74.656  1.00 384.34 ? 760  VAL B CA  1 
ATOM   18089 C  C   . VAL C 1 760  ? 47.018  11.096  74.644  1.00 373.10 ? 760  VAL B C   1 
ATOM   18090 O  O   . VAL C 1 760  ? 47.278  11.689  75.691  1.00 375.03 ? 760  VAL B O   1 
ATOM   18091 C  CB  . VAL C 1 760  ? 47.239  8.782   75.674  1.00 404.76 ? 760  VAL B CB  1 
ATOM   18092 C  CG1 . VAL C 1 760  ? 46.810  9.117   77.089  1.00 413.53 ? 760  VAL B CG1 1 
ATOM   18093 C  CG2 . VAL C 1 760  ? 46.989  7.305   75.390  1.00 410.71 ? 760  VAL B CG2 1 
ATOM   18094 N  N   . SER C 1 761  ? 47.172  11.635  73.435  1.00 314.17 ? 761  SER B N   1 
ATOM   18095 C  CA  . SER C 1 761  ? 47.675  12.988  73.218  1.00 298.95 ? 761  SER B CA  1 
ATOM   18096 C  C   . SER C 1 761  ? 49.196  13.083  73.398  1.00 281.79 ? 761  SER B C   1 
ATOM   18097 O  O   . SER C 1 761  ? 49.737  14.170  73.596  1.00 279.68 ? 761  SER B O   1 
ATOM   18098 C  CB  . SER C 1 761  ? 46.946  13.982  74.129  1.00 303.46 ? 761  SER B CB  1 
ATOM   18099 O  OG  . SER C 1 761  ? 47.280  15.321  73.808  1.00 301.35 ? 761  SER B OG  1 
ATOM   18100 N  N   . LYS C 1 762  ? 49.879  11.943  73.311  1.00 228.76 ? 762  LYS B N   1 
ATOM   18101 C  CA  . LYS C 1 762  ? 51.324  11.877  73.555  1.00 208.91 ? 762  LYS B CA  1 
ATOM   18102 C  C   . LYS C 1 762  ? 52.171  12.335  72.372  1.00 196.81 ? 762  LYS B C   1 
ATOM   18103 O  O   . LYS C 1 762  ? 52.025  11.808  71.269  1.00 196.04 ? 762  LYS B O   1 
ATOM   18104 C  CB  . LYS C 1 762  ? 51.747  10.453  73.939  1.00 200.70 ? 762  LYS B CB  1 
ATOM   18105 C  CG  . LYS C 1 762  ? 51.525  10.053  75.409  1.00 193.74 ? 762  LYS B CG  1 
ATOM   18106 C  CD  . LYS C 1 762  ? 52.078  8.643   75.668  1.00 186.27 ? 762  LYS B CD  1 
ATOM   18107 C  CE  . LYS C 1 762  ? 51.564  8.018   76.948  1.00 183.76 ? 762  LYS B CE  1 
ATOM   18108 N  NZ  . LYS C 1 762  ? 51.880  6.565   76.946  1.00 182.12 ? 762  LYS B NZ  1 
ATOM   18109 N  N   . PRO C 1 763  ? 53.076  13.304  72.610  1.00 263.30 ? 763  PRO B N   1 
ATOM   18110 C  CA  . PRO C 1 763  ? 54.029  13.769  71.594  1.00 254.09 ? 763  PRO B CA  1 
ATOM   18111 C  C   . PRO C 1 763  ? 55.018  12.686  71.161  1.00 245.38 ? 763  PRO B C   1 
ATOM   18112 O  O   . PRO C 1 763  ? 56.048  12.502  71.815  1.00 246.03 ? 763  PRO B O   1 
ATOM   18113 C  CB  . PRO C 1 763  ? 54.780  14.900  72.311  1.00 251.95 ? 763  PRO B CB  1 
ATOM   18114 C  CG  . PRO C 1 763  ? 53.852  15.364  73.377  1.00 255.58 ? 763  PRO B CG  1 
ATOM   18115 C  CD  . PRO C 1 763  ? 53.131  14.127  73.831  1.00 261.63 ? 763  PRO B CD  1 
ATOM   18116 N  N   . GLU C 1 764  ? 54.701  11.983  70.077  1.00 233.91 ? 764  GLU B N   1 
ATOM   18117 C  CA  . GLU C 1 764  ? 55.639  11.043  69.475  1.00 224.20 ? 764  GLU B CA  1 
ATOM   18118 C  C   . GLU C 1 764  ? 55.993  11.477  68.075  1.00 212.94 ? 764  GLU B C   1 
ATOM   18119 O  O   . GLU C 1 764  ? 55.249  12.204  67.424  1.00 210.99 ? 764  GLU B O   1 
ATOM   18120 C  CB  . GLU C 1 764  ? 55.090  9.619   69.458  1.00 225.95 ? 764  GLU B CB  1 
ATOM   18121 C  CG  . GLU C 1 764  ? 53.782  9.455   68.723  1.00 226.56 ? 764  GLU B CG  1 
ATOM   18122 C  CD  . GLU C 1 764  ? 53.009  8.256   69.231  1.00 230.03 ? 764  GLU B CD  1 
ATOM   18123 O  OE1 . GLU C 1 764  ? 53.620  7.171   69.371  1.00 230.20 ? 764  GLU B OE1 1 
ATOM   18124 O  OE2 . GLU C 1 764  ? 51.795  8.403   69.499  1.00 232.07 ? 764  GLU B OE2 1 
ATOM   18125 N  N   . ILE C 1 765  ? 57.135  11.003  67.612  1.00 175.96 ? 765  ILE B N   1 
ATOM   18126 C  CA  . ILE C 1 765  ? 57.737  11.541  66.421  1.00 168.81 ? 765  ILE B CA  1 
ATOM   18127 C  C   . ILE C 1 765  ? 58.694  10.512  65.898  1.00 168.29 ? 765  ILE B C   1 
ATOM   18128 O  O   . ILE C 1 765  ? 59.604  10.090  66.600  1.00 171.05 ? 765  ILE B O   1 
ATOM   18129 C  CB  . ILE C 1 765  ? 58.531  12.799  66.751  1.00 162.37 ? 765  ILE B CB  1 
ATOM   18130 C  CG1 . ILE C 1 765  ? 59.276  13.278  65.508  1.00 159.51 ? 765  ILE B CG1 1 
ATOM   18131 C  CG2 . ILE C 1 765  ? 59.520  12.524  67.873  1.00 161.99 ? 765  ILE B CG2 1 
ATOM   18132 C  CD1 . ILE C 1 765  ? 59.426  14.793  65.433  1.00 157.27 ? 765  ILE B CD1 1 
ATOM   18133 N  N   . ARG C 1 766  ? 58.495  10.100  64.661  1.00 190.22 ? 766  ARG B N   1 
ATOM   18134 C  CA  . ARG C 1 766  ? 59.252  8.980   64.152  1.00 188.18 ? 766  ARG B CA  1 
ATOM   18135 C  C   . ARG C 1 766  ? 60.558  9.397   63.501  1.00 188.75 ? 766  ARG B C   1 
ATOM   18136 O  O   . ARG C 1 766  ? 60.953  8.840   62.481  1.00 188.34 ? 766  ARG B O   1 
ATOM   18137 C  CB  . ARG C 1 766  ? 58.384  8.194   63.188  1.00 185.46 ? 766  ARG B CB  1 
ATOM   18138 C  CG  . ARG C 1 766  ? 57.024  7.930   63.768  1.00 184.90 ? 766  ARG B CG  1 
ATOM   18139 C  CD  . ARG C 1 766  ? 57.164  7.146   65.050  1.00 187.12 ? 766  ARG B CD  1 
ATOM   18140 N  NE  . ARG C 1 766  ? 55.878  6.658   65.530  1.00 191.43 ? 766  ARG B NE  1 
ATOM   18141 C  CZ  . ARG C 1 766  ? 55.638  5.397   65.882  1.00 197.40 ? 766  ARG B CZ  1 
ATOM   18142 N  NH1 . ARG C 1 766  ? 56.599  4.481   65.812  1.00 201.11 ? 766  ARG B NH1 1 
ATOM   18143 N  NH2 . ARG C 1 766  ? 54.430  5.051   66.310  1.00 198.72 ? 766  ARG B NH2 1 
ATOM   18144 N  N   . SER C 1 767  ? 61.238  10.366  64.097  1.00 162.79 ? 767  SER B N   1 
ATOM   18145 C  CA  . SER C 1 767  ? 62.490  10.840  63.530  1.00 166.38 ? 767  SER B CA  1 
ATOM   18146 C  C   . SER C 1 767  ? 63.401  11.506  64.554  1.00 168.17 ? 767  SER B C   1 
ATOM   18147 O  O   . SER C 1 767  ? 62.951  12.254  65.425  1.00 168.10 ? 767  SER B O   1 
ATOM   18148 C  CB  . SER C 1 767  ? 62.210  11.779  62.356  1.00 168.19 ? 767  SER B CB  1 
ATOM   18149 O  OG  . SER C 1 767  ? 60.912  12.339  62.458  1.00 168.43 ? 767  SER B OG  1 
ATOM   18150 N  N   . TYR C 1 768  ? 64.690  11.204  64.444  1.00 247.44 ? 768  TYR B N   1 
ATOM   18151 C  CA  . TYR C 1 768  ? 65.709  11.809  65.289  1.00 250.66 ? 768  TYR B CA  1 
ATOM   18152 C  C   . TYR C 1 768  ? 66.183  13.086  64.630  1.00 243.14 ? 768  TYR B C   1 
ATOM   18153 O  O   . TYR C 1 768  ? 66.171  13.208  63.403  1.00 243.16 ? 768  TYR B O   1 
ATOM   18154 C  CB  . TYR C 1 768  ? 66.887  10.847  65.482  1.00 260.99 ? 768  TYR B CB  1 
ATOM   18155 C  CG  . TYR C 1 768  ? 68.056  11.408  66.277  1.00 267.88 ? 768  TYR B CG  1 
ATOM   18156 C  CD1 . TYR C 1 768  ? 68.085  11.327  67.666  1.00 273.42 ? 768  TYR B CD1 1 
ATOM   18157 C  CD2 . TYR C 1 768  ? 69.141  11.998  65.637  1.00 270.01 ? 768  TYR B CD2 1 
ATOM   18158 C  CE1 . TYR C 1 768  ? 69.157  11.833  68.397  1.00 276.62 ? 768  TYR B CE1 1 
ATOM   18159 C  CE2 . TYR C 1 768  ? 70.217  12.504  66.361  1.00 273.38 ? 768  TYR B CE2 1 
ATOM   18160 C  CZ  . TYR C 1 768  ? 70.220  12.422  67.739  1.00 277.04 ? 768  TYR B CZ  1 
ATOM   18161 O  OH  . TYR C 1 768  ? 71.287  12.927  68.458  1.00 279.03 ? 768  TYR B OH  1 
ATOM   18162 N  N   . PHE C 1 769  ? 66.602  14.039  65.448  1.00 195.54 ? 769  PHE B N   1 
ATOM   18163 C  CA  . PHE C 1 769  ? 67.072  15.313  64.940  1.00 190.10 ? 769  PHE B CA  1 
ATOM   18164 C  C   . PHE C 1 769  ? 68.409  15.658  65.571  1.00 189.64 ? 769  PHE B C   1 
ATOM   18165 O  O   . PHE C 1 769  ? 68.450  16.245  66.653  1.00 191.69 ? 769  PHE B O   1 
ATOM   18166 C  CB  . PHE C 1 769  ? 66.073  16.404  65.284  1.00 186.96 ? 769  PHE B CB  1 
ATOM   18167 C  CG  . PHE C 1 769  ? 64.811  16.376  64.459  1.00 183.97 ? 769  PHE B CG  1 
ATOM   18168 C  CD1 . PHE C 1 769  ? 64.794  16.877  63.167  1.00 182.15 ? 769  PHE B CD1 1 
ATOM   18169 C  CD2 . PHE C 1 769  ? 63.626  15.902  64.997  1.00 182.27 ? 769  PHE B CD2 1 
ATOM   18170 C  CE1 . PHE C 1 769  ? 63.621  16.882  62.427  1.00 182.47 ? 769  PHE B CE1 1 
ATOM   18171 C  CE2 . PHE C 1 769  ? 62.452  15.908  64.255  1.00 177.43 ? 769  PHE B CE2 1 
ATOM   18172 C  CZ  . PHE C 1 769  ? 62.452  16.397  62.976  1.00 181.91 ? 769  PHE B CZ  1 
ATOM   18173 N  N   . PRO C 1 770  ? 69.507  15.313  64.884  1.00 158.21 ? 770  PRO B N   1 
ATOM   18174 C  CA  . PRO C 1 770  ? 70.882  15.411  65.401  1.00 162.52 ? 770  PRO B CA  1 
ATOM   18175 C  C   . PRO C 1 770  ? 71.189  16.696  66.180  1.00 167.53 ? 770  PRO B C   1 
ATOM   18176 O  O   . PRO C 1 770  ? 70.590  17.743  65.937  1.00 168.28 ? 770  PRO B O   1 
ATOM   18177 C  CB  . PRO C 1 770  ? 71.731  15.328  64.133  1.00 161.25 ? 770  PRO B CB  1 
ATOM   18178 C  CG  . PRO C 1 770  ? 70.895  14.484  63.178  1.00 160.63 ? 770  PRO B CG  1 
ATOM   18179 C  CD  . PRO C 1 770  ? 69.452  14.752  63.519  1.00 158.53 ? 770  PRO B CD  1 
ATOM   18180 N  N   . GLU C 1 771  ? 72.106  16.605  67.132  1.00 214.92 ? 771  GLU B N   1 
ATOM   18181 C  CA  . GLU C 1 771  ? 72.539  17.792  67.835  1.00 218.78 ? 771  GLU B CA  1 
ATOM   18182 C  C   . GLU C 1 771  ? 73.178  18.685  66.791  1.00 214.86 ? 771  GLU B C   1 
ATOM   18183 O  O   . GLU C 1 771  ? 73.897  18.201  65.916  1.00 213.51 ? 771  GLU B O   1 
ATOM   18184 C  CB  . GLU C 1 771  ? 73.551  17.420  68.904  1.00 227.62 ? 771  GLU B CB  1 
ATOM   18185 C  CG  . GLU C 1 771  ? 74.114  18.588  69.678  1.00 234.26 ? 771  GLU B CG  1 
ATOM   18186 C  CD  . GLU C 1 771  ? 75.222  18.153  70.613  1.00 241.17 ? 771  GLU B CD  1 
ATOM   18187 O  OE1 . GLU C 1 771  ? 75.168  18.515  71.809  1.00 242.86 ? 771  GLU B OE1 1 
ATOM   18188 O  OE2 . GLU C 1 771  ? 76.138  17.435  70.152  1.00 244.20 ? 771  GLU B OE2 1 
ATOM   18189 N  N   . SER C 1 772  ? 72.905  19.981  66.867  1.00 191.99 ? 772  SER B N   1 
ATOM   18190 C  CA  . SER C 1 772  ? 73.394  20.932  65.866  1.00 188.72 ? 772  SER B CA  1 
ATOM   18191 C  C   . SER C 1 772  ? 74.880  21.234  66.055  1.00 185.85 ? 772  SER B C   1 
ATOM   18192 O  O   . SER C 1 772  ? 75.568  20.457  66.704  1.00 187.01 ? 772  SER B O   1 
ATOM   18193 C  CB  . SER C 1 772  ? 72.565  22.208  65.921  1.00 188.00 ? 772  SER B CB  1 
ATOM   18194 O  OG  . SER C 1 772  ? 71.183  21.891  65.944  1.00 187.67 ? 772  SER B OG  1 
ATOM   18195 N  N   . TRP C 1 773  ? 75.375  22.340  65.490  1.00 169.08 ? 773  TRP B N   1 
ATOM   18196 C  CA  . TRP C 1 773  ? 76.788  22.711  65.645  1.00 171.54 ? 773  TRP B CA  1 
ATOM   18197 C  C   . TRP C 1 773  ? 77.151  24.092  65.088  1.00 174.97 ? 773  TRP B C   1 
ATOM   18198 O  O   . TRP C 1 773  ? 76.279  24.820  64.627  1.00 177.13 ? 773  TRP B O   1 
ATOM   18199 C  CB  . TRP C 1 773  ? 77.685  21.651  65.025  1.00 171.73 ? 773  TRP B CB  1 
ATOM   18200 C  CG  . TRP C 1 773  ? 77.312  21.359  63.623  1.00 170.98 ? 773  TRP B CG  1 
ATOM   18201 C  CD1 . TRP C 1 773  ? 76.314  20.534  63.192  1.00 170.81 ? 773  TRP B CD1 1 
ATOM   18202 C  CD2 . TRP C 1 773  ? 77.922  21.901  62.449  1.00 172.13 ? 773  TRP B CD2 1 
ATOM   18203 N  NE1 . TRP C 1 773  ? 76.268  20.526  61.817  1.00 170.17 ? 773  TRP B NE1 1 
ATOM   18204 C  CE2 . TRP C 1 773  ? 77.247  21.358  61.339  1.00 170.98 ? 773  TRP B CE2 1 
ATOM   18205 C  CE3 . TRP C 1 773  ? 78.982  22.794  62.227  1.00 172.32 ? 773  TRP B CE3 1 
ATOM   18206 C  CZ2 . TRP C 1 773  ? 77.603  21.674  60.026  1.00 171.49 ? 773  TRP B CZ2 1 
ATOM   18207 C  CZ3 . TRP C 1 773  ? 79.331  23.110  60.913  1.00 172.41 ? 773  TRP B CZ3 1 
ATOM   18208 C  CH2 . TRP C 1 773  ? 78.645  22.551  59.836  1.00 172.15 ? 773  TRP B CH2 1 
ATOM   18209 N  N   . LEU C 1 774  ? 78.443  24.429  65.131  1.00 226.36 ? 774  LEU B N   1 
ATOM   18210 C  CA  . LEU C 1 774  ? 78.942  25.785  64.838  1.00 227.44 ? 774  LEU B CA  1 
ATOM   18211 C  C   . LEU C 1 774  ? 78.288  26.855  65.708  1.00 224.93 ? 774  LEU B C   1 
ATOM   18212 O  O   . LEU C 1 774  ? 77.934  27.933  65.224  1.00 221.58 ? 774  LEU B O   1 
ATOM   18213 C  CB  . LEU C 1 774  ? 78.785  26.148  63.358  1.00 229.33 ? 774  LEU B CB  1 
ATOM   18214 C  CG  . LEU C 1 774  ? 80.102  26.260  62.595  1.00 234.16 ? 774  LEU B CG  1 
ATOM   18215 C  CD1 . LEU C 1 774  ? 79.849  26.562  61.127  1.00 233.79 ? 774  LEU B CD1 1 
ATOM   18216 C  CD2 . LEU C 1 774  ? 81.005  27.315  63.226  1.00 236.62 ? 774  LEU B CD2 1 
ATOM   18217 N  N   . TRP C 1 775  ? 78.152  26.554  66.996  1.00 166.43 ? 775  TRP B N   1 
ATOM   18218 C  CA  . TRP C 1 775  ? 77.374  27.372  67.904  1.00 163.90 ? 775  TRP B CA  1 
ATOM   18219 C  C   . TRP C 1 775  ? 78.219  28.437  68.575  1.00 166.10 ? 775  TRP B C   1 
ATOM   18220 O  O   . TRP C 1 775  ? 77.721  29.202  69.389  1.00 165.41 ? 775  TRP B O   1 
ATOM   18221 C  CB  . TRP C 1 775  ? 76.737  26.469  68.932  1.00 161.91 ? 775  TRP B CB  1 
ATOM   18222 C  CG  . TRP C 1 775  ? 75.764  27.144  69.777  1.00 161.79 ? 775  TRP B CG  1 
ATOM   18223 C  CD1 . TRP C 1 775  ? 75.984  27.620  71.015  1.00 165.21 ? 775  TRP B CD1 1 
ATOM   18224 C  CD2 . TRP C 1 775  ? 74.386  27.413  69.481  1.00 160.52 ? 775  TRP B CD2 1 
ATOM   18225 N  NE1 . TRP C 1 775  ? 74.836  28.179  71.527  1.00 164.63 ? 775  TRP B NE1 1 
ATOM   18226 C  CE2 . TRP C 1 775  ? 73.839  28.061  70.601  1.00 161.19 ? 775  TRP B CE2 1 
ATOM   18227 C  CE3 . TRP C 1 775  ? 73.564  27.170  68.387  1.00 158.92 ? 775  TRP B CE3 1 
ATOM   18228 C  CZ2 . TRP C 1 775  ? 72.509  28.470  70.658  1.00 159.52 ? 775  TRP B CZ2 1 
ATOM   18229 C  CZ3 . TRP C 1 775  ? 72.238  27.580  68.448  1.00 157.84 ? 775  TRP B CZ3 1 
ATOM   18230 C  CH2 . TRP C 1 775  ? 71.729  28.221  69.573  1.00 158.35 ? 775  TRP B CH2 1 
ATOM   18231 N  N   . GLU C 1 776  ? 79.501  28.479  68.216  1.00 238.97 ? 776  GLU B N   1 
ATOM   18232 C  CA  . GLU C 1 776  ? 80.455  29.465  68.736  1.00 243.83 ? 776  GLU B CA  1 
ATOM   18233 C  C   . GLU C 1 776  ? 80.112  30.901  68.320  1.00 243.30 ? 776  GLU B C   1 
ATOM   18234 O  O   . GLU C 1 776  ? 79.536  31.114  67.256  1.00 241.12 ? 776  GLU B O   1 
ATOM   18235 C  CB  . GLU C 1 776  ? 81.867  29.114  68.250  1.00 250.05 ? 776  GLU B CB  1 
ATOM   18236 C  CG  . GLU C 1 776  ? 81.965  28.848  66.746  1.00 253.98 ? 776  GLU B CG  1 
ATOM   18237 C  CD  . GLU C 1 776  ? 83.273  28.187  66.355  1.00 261.29 ? 776  GLU B CD  1 
ATOM   18238 O  OE1 . GLU C 1 776  ? 83.238  27.140  65.680  1.00 262.29 ? 776  GLU B OE1 1 
ATOM   18239 O  OE2 . GLU C 1 776  ? 84.340  28.707  66.730  1.00 265.66 ? 776  GLU B OE2 1 
ATOM   18240 N  N   . VAL C 1 777  ? 80.459  31.884  69.151  1.00 142.85 ? 777  VAL B N   1 
ATOM   18241 C  CA  . VAL C 1 777  ? 80.320  33.288  68.746  1.00 140.90 ? 777  VAL B CA  1 
ATOM   18242 C  C   . VAL C 1 777  ? 81.647  33.832  68.171  1.00 150.16 ? 777  VAL B C   1 
ATOM   18243 O  O   . VAL C 1 777  ? 82.696  33.230  68.391  1.00 153.92 ? 777  VAL B O   1 
ATOM   18244 C  CB  . VAL C 1 777  ? 79.773  34.153  69.899  1.00 140.50 ? 777  VAL B CB  1 
ATOM   18245 C  CG1 . VAL C 1 777  ? 79.789  35.608  69.520  1.00 140.41 ? 777  VAL B CG1 1 
ATOM   18246 C  CG2 . VAL C 1 777  ? 78.363  33.709  70.253  1.00 137.17 ? 777  VAL B CG2 1 
ATOM   18247 N  N   . HIS C 1 778  ? 81.609  34.930  67.411  1.00 179.53 ? 778  HIS B N   1 
ATOM   18248 C  CA  . HIS C 1 778  ? 82.848  35.490  66.853  1.00 187.14 ? 778  HIS B CA  1 
ATOM   18249 C  C   . HIS C 1 778  ? 82.926  37.010  66.737  1.00 199.14 ? 778  HIS B C   1 
ATOM   18250 O  O   . HIS C 1 778  ? 81.919  37.717  66.689  1.00 197.62 ? 778  HIS B O   1 
ATOM   18251 C  CB  . HIS C 1 778  ? 83.177  34.874  65.492  1.00 184.41 ? 778  HIS B CB  1 
ATOM   18252 C  CG  . HIS C 1 778  ? 83.901  33.570  65.578  1.00 183.43 ? 778  HIS B CG  1 
ATOM   18253 N  ND1 . HIS C 1 778  ? 85.269  33.488  65.737  1.00 184.60 ? 778  HIS B ND1 1 
ATOM   18254 C  CD2 . HIS C 1 778  ? 83.451  32.295  65.523  1.00 181.72 ? 778  HIS B CD2 1 
ATOM   18255 C  CE1 . HIS C 1 778  ? 85.627  32.217  65.777  1.00 184.49 ? 778  HIS B CE1 1 
ATOM   18256 N  NE2 . HIS C 1 778  ? 84.543  31.473  65.649  1.00 182.70 ? 778  HIS B NE2 1 
ATOM   18257 N  N   . LEU C 1 779  ? 84.161  37.491  66.690  1.00 186.36 ? 779  LEU B N   1 
ATOM   18258 C  CA  . LEU C 1 779  ? 84.443  38.887  66.449  1.00 197.18 ? 779  LEU B CA  1 
ATOM   18259 C  C   . LEU C 1 779  ? 84.865  38.992  64.997  1.00 204.94 ? 779  LEU B C   1 
ATOM   18260 O  O   . LEU C 1 779  ? 85.859  38.384  64.601  1.00 208.70 ? 779  LEU B O   1 
ATOM   18261 C  CB  . LEU C 1 779  ? 85.585  39.335  67.355  1.00 200.99 ? 779  LEU B CB  1 
ATOM   18262 C  CG  . LEU C 1 779  ? 85.948  40.813  67.307  1.00 202.16 ? 779  LEU B CG  1 
ATOM   18263 C  CD1 . LEU C 1 779  ? 84.707  41.640  67.579  1.00 201.22 ? 779  LEU B CD1 1 
ATOM   18264 C  CD2 . LEU C 1 779  ? 87.054  41.136  68.303  1.00 205.25 ? 779  LEU B CD2 1 
ATOM   18265 N  N   . VAL C 1 780  ? 84.116  39.750  64.199  1.00 226.67 ? 780  VAL B N   1 
ATOM   18266 C  CA  . VAL C 1 780  ? 84.448  39.906  62.783  1.00 233.00 ? 780  VAL B CA  1 
ATOM   18267 C  C   . VAL C 1 780  ? 84.517  41.368  62.334  1.00 231.18 ? 780  VAL B C   1 
ATOM   18268 O  O   . VAL C 1 780  ? 83.492  42.040  62.220  1.00 228.26 ? 780  VAL B O   1 
ATOM   18269 C  CB  . VAL C 1 780  ? 83.459  39.141  61.875  1.00 237.73 ? 780  VAL B CB  1 
ATOM   18270 C  CG1 . VAL C 1 780  ? 83.773  39.404  60.411  1.00 243.25 ? 780  VAL B CG1 1 
ATOM   18271 C  CG2 . VAL C 1 780  ? 83.504  37.651  62.171  1.00 241.43 ? 780  VAL B CG2 1 
ATOM   18272 N  N   . PRO C 1 781  ? 85.740  41.865  62.091  1.00 232.13 ? 781  PRO B N   1 
ATOM   18273 C  CA  . PRO C 1 781  ? 85.990  43.207  61.554  1.00 232.34 ? 781  PRO B CA  1 
ATOM   18274 C  C   . PRO C 1 781  ? 85.848  43.250  60.034  1.00 231.78 ? 781  PRO B C   1 
ATOM   18275 O  O   . PRO C 1 781  ? 86.840  43.478  59.335  1.00 234.59 ? 781  PRO B O   1 
ATOM   18276 C  CB  . PRO C 1 781  ? 87.450  43.475  61.947  1.00 236.91 ? 781  PRO B CB  1 
ATOM   18277 C  CG  . PRO C 1 781  ? 87.796  42.412  62.961  1.00 238.41 ? 781  PRO B CG  1 
ATOM   18278 C  CD  . PRO C 1 781  ? 86.984  41.232  62.551  1.00 235.93 ? 781  PRO B CD  1 
ATOM   18279 N  N   . ARG C 1 782  ? 84.632  43.026  59.542  1.00 252.19 ? 782  ARG B N   1 
ATOM   18280 C  CA  . ARG C 1 782  ? 84.344  43.052  58.111  1.00 252.62 ? 782  ARG B CA  1 
ATOM   18281 C  C   . ARG C 1 782  ? 84.660  41.734  57.397  1.00 249.17 ? 782  ARG B C   1 
ATOM   18282 O  O   . ARG C 1 782  ? 84.052  41.417  56.379  1.00 249.35 ? 782  ARG B O   1 
ATOM   18283 C  CB  . ARG C 1 782  ? 85.074  44.210  57.431  1.00 259.92 ? 782  ARG B CB  1 
ATOM   18284 C  CG  . ARG C 1 782  ? 84.736  45.577  57.995  1.00 266.26 ? 782  ARG B CG  1 
ATOM   18285 C  CD  . ARG C 1 782  ? 85.426  46.679  57.208  1.00 274.26 ? 782  ARG B CD  1 
ATOM   18286 N  NE  . ARG C 1 782  ? 86.872  46.663  57.404  1.00 281.48 ? 782  ARG B NE  1 
ATOM   18287 C  CZ  . ARG C 1 782  ? 87.721  47.491  56.800  1.00 286.88 ? 782  ARG B CZ  1 
ATOM   18288 N  NH1 . ARG C 1 782  ? 87.274  48.407  55.948  1.00 288.05 ? 782  ARG B NH1 1 
ATOM   18289 N  NH2 . ARG C 1 782  ? 89.021  47.401  57.045  1.00 290.14 ? 782  ARG B NH2 1 
ATOM   18290 N  N   . ARG C 1 783  ? 85.612  40.972  57.924  1.00 246.55 ? 783  ARG B N   1 
ATOM   18291 C  CA  . ARG C 1 783  ? 85.953  39.669  57.348  1.00 243.56 ? 783  ARG B CA  1 
ATOM   18292 C  C   . ARG C 1 783  ? 86.479  38.699  58.416  1.00 239.11 ? 783  ARG B C   1 
ATOM   18293 O  O   . ARG C 1 783  ? 87.185  39.106  59.345  1.00 239.86 ? 783  ARG B O   1 
ATOM   18294 C  CB  . ARG C 1 783  ? 86.999  39.814  56.229  1.00 247.28 ? 783  ARG B CB  1 
ATOM   18295 C  CG  . ARG C 1 783  ? 86.508  40.474  54.948  1.00 248.22 ? 783  ARG B CG  1 
ATOM   18296 C  CD  . ARG C 1 783  ? 87.683  40.980  54.110  1.00 252.05 ? 783  ARG B CD  1 
ATOM   18297 N  NE  . ARG C 1 783  ? 87.358  42.210  53.387  1.00 253.62 ? 783  ARG B NE  1 
ATOM   18298 C  CZ  . ARG C 1 783  ? 88.186  43.244  53.247  1.00 255.94 ? 783  ARG B CZ  1 
ATOM   18299 N  NH1 . ARG C 1 783  ? 89.398  43.204  53.775  1.00 257.96 ? 783  ARG B NH1 1 
ATOM   18300 N  NH2 . ARG C 1 783  ? 87.804  44.323  52.579  1.00 255.52 ? 783  ARG B NH2 1 
ATOM   18301 N  N   . LYS C 1 784  ? 86.114  37.422  58.282  1.00 191.65 ? 784  LYS B N   1 
ATOM   18302 C  CA  . LYS C 1 784  ? 86.693  36.328  59.075  1.00 188.31 ? 784  LYS B CA  1 
ATOM   18303 C  C   . LYS C 1 784  ? 86.318  34.992  58.436  1.00 185.52 ? 784  LYS B C   1 
ATOM   18304 O  O   . LYS C 1 784  ? 85.145  34.650  58.311  1.00 184.23 ? 784  LYS B O   1 
ATOM   18305 C  CB  . LYS C 1 784  ? 86.266  36.386  60.556  1.00 186.02 ? 784  LYS B CB  1 
ATOM   18306 C  CG  . LYS C 1 784  ? 87.070  35.464  61.505  1.00 185.89 ? 784  LYS B CG  1 
ATOM   18307 C  CD  . LYS C 1 784  ? 86.801  35.752  63.006  1.00 183.24 ? 784  LYS B CD  1 
ATOM   18308 C  CE  . LYS C 1 784  ? 87.659  34.861  63.940  1.00 182.72 ? 784  LYS B CE  1 
ATOM   18309 N  NZ  . LYS C 1 784  ? 87.507  35.152  65.401  1.00 180.75 ? 784  LYS B NZ  1 
ATOM   18310 N  N   . GLN C 1 785  ? 87.332  34.258  58.002  1.00 222.58 ? 785  GLN B N   1 
ATOM   18311 C  CA  . GLN C 1 785  ? 87.133  32.944  57.427  1.00 219.78 ? 785  GLN B CA  1 
ATOM   18312 C  C   . GLN C 1 785  ? 87.560  31.907  58.447  1.00 217.45 ? 785  GLN B C   1 
ATOM   18313 O  O   . GLN C 1 785  ? 88.537  32.104  59.162  1.00 217.81 ? 785  GLN B O   1 
ATOM   18314 C  CB  . GLN C 1 785  ? 87.969  32.806  56.157  1.00 222.93 ? 785  GLN B CB  1 
ATOM   18315 C  CG  . GLN C 1 785  ? 87.836  31.477  55.437  1.00 225.91 ? 785  GLN B CG  1 
ATOM   18316 C  CD  . GLN C 1 785  ? 88.547  31.494  54.103  1.00 230.90 ? 785  GLN B CD  1 
ATOM   18317 O  OE1 . GLN C 1 785  ? 89.563  32.167  53.941  1.00 233.96 ? 785  GLN B OE1 1 
ATOM   18318 N  NE2 . GLN C 1 785  ? 88.014  30.763  53.137  1.00 231.61 ? 785  GLN B NE2 1 
ATOM   18319 N  N   . LEU C 1 786  ? 86.824  30.807  58.526  1.00 199.04 ? 786  LEU B N   1 
ATOM   18320 C  CA  . LEU C 1 786  ? 87.187  29.725  59.436  1.00 199.99 ? 786  LEU B CA  1 
ATOM   18321 C  C   . LEU C 1 786  ? 86.856  28.371  58.840  1.00 202.12 ? 786  LEU B C   1 
ATOM   18322 O  O   . LEU C 1 786  ? 85.700  27.951  58.827  1.00 202.32 ? 786  LEU B O   1 
ATOM   18323 C  CB  . LEU C 1 786  ? 86.534  29.881  60.823  1.00 195.83 ? 786  LEU B CB  1 
ATOM   18324 C  CG  . LEU C 1 786  ? 85.031  30.115  60.972  1.00 190.03 ? 786  LEU B CG  1 
ATOM   18325 C  CD1 . LEU C 1 786  ? 84.628  30.136  62.434  1.00 187.51 ? 786  LEU B CD1 1 
ATOM   18326 C  CD2 . LEU C 1 786  ? 84.659  31.418  60.310  1.00 188.11 ? 786  LEU B CD2 1 
ATOM   18327 N  N   . GLN C 1 787  ? 87.881  27.688  58.343  1.00 224.45 ? 787  GLN B N   1 
ATOM   18328 C  CA  . GLN C 1 787  ? 87.680  26.376  57.747  1.00 224.58 ? 787  GLN B CA  1 
ATOM   18329 C  C   . GLN C 1 787  ? 87.386  25.307  58.802  1.00 220.34 ? 787  GLN B C   1 
ATOM   18330 O  O   . GLN C 1 787  ? 87.677  25.493  59.990  1.00 219.42 ? 787  GLN B O   1 
ATOM   18331 C  CB  . GLN C 1 787  ? 88.867  25.981  56.859  1.00 231.54 ? 787  GLN B CB  1 
ATOM   18332 C  CG  . GLN C 1 787  ? 90.229  26.320  57.431  1.00 238.69 ? 787  GLN B CG  1 
ATOM   18333 C  CD  . GLN C 1 787  ? 91.335  26.213  56.399  1.00 246.25 ? 787  GLN B CD  1 
ATOM   18334 O  OE1 . GLN C 1 787  ? 92.499  26.027  56.742  1.00 250.49 ? 787  GLN B OE1 1 
ATOM   18335 N  NE2 . GLN C 1 787  ? 90.976  26.332  55.129  1.00 247.51 ? 787  GLN B NE2 1 
ATOM   18336 N  N   . PHE C 1 788  ? 86.790  24.203  58.349  1.00 221.81 ? 788  PHE B N   1 
ATOM   18337 C  CA  . PHE C 1 788  ? 86.425  23.064  59.192  1.00 217.37 ? 788  PHE B CA  1 
ATOM   18338 C  C   . PHE C 1 788  ? 85.704  22.052  58.323  1.00 214.13 ? 788  PHE B C   1 
ATOM   18339 O  O   . PHE C 1 788  ? 85.080  22.417  57.333  1.00 215.31 ? 788  PHE B O   1 
ATOM   18340 C  CB  . PHE C 1 788  ? 85.503  23.494  60.332  1.00 212.60 ? 788  PHE B CB  1 
ATOM   18341 C  CG  . PHE C 1 788  ? 84.233  24.150  59.869  1.00 207.25 ? 788  PHE B CG  1 
ATOM   18342 C  CD1 . PHE C 1 788  ? 83.059  23.425  59.763  1.00 204.87 ? 788  PHE B CD1 1 
ATOM   18343 C  CD2 . PHE C 1 788  ? 84.220  25.495  59.532  1.00 204.17 ? 788  PHE B CD2 1 
ATOM   18344 C  CE1 . PHE C 1 788  ? 81.900  24.030  59.339  1.00 200.72 ? 788  PHE B CE1 1 
ATOM   18345 C  CE2 . PHE C 1 788  ? 83.063  26.104  59.104  1.00 200.35 ? 788  PHE B CE2 1 
ATOM   18346 C  CZ  . PHE C 1 788  ? 81.902  25.370  59.008  1.00 198.67 ? 788  PHE B CZ  1 
ATOM   18347 N  N   . ALA C 1 789  ? 85.787  20.780  58.672  1.00 227.10 ? 789  ALA B N   1 
ATOM   18348 C  CA  . ALA C 1 789  ? 85.072  19.785  57.892  1.00 221.76 ? 789  ALA B CA  1 
ATOM   18349 C  C   . ALA C 1 789  ? 83.675  19.578  58.470  1.00 216.87 ? 789  ALA B C   1 
ATOM   18350 O  O   . ALA C 1 789  ? 83.444  19.828  59.650  1.00 215.70 ? 789  ALA B O   1 
ATOM   18351 C  CB  . ALA C 1 789  ? 85.846  18.491  57.845  1.00 224.67 ? 789  ALA B CB  1 
ATOM   18352 N  N   . LEU C 1 790  ? 82.742  19.140  57.630  1.00 180.78 ? 790  LEU B N   1 
ATOM   18353 C  CA  . LEU C 1 790  ? 81.371  18.922  58.067  1.00 179.04 ? 790  LEU B CA  1 
ATOM   18354 C  C   . LEU C 1 790  ? 81.200  17.475  58.489  1.00 182.08 ? 790  LEU B C   1 
ATOM   18355 O  O   . LEU C 1 790  ? 81.803  16.577  57.912  1.00 181.48 ? 790  LEU B O   1 
ATOM   18356 C  CB  . LEU C 1 790  ? 80.386  19.289  56.962  1.00 174.31 ? 790  LEU B CB  1 
ATOM   18357 C  CG  . LEU C 1 790  ? 80.818  20.453  56.066  1.00 171.62 ? 790  LEU B CG  1 
ATOM   18358 C  CD1 . LEU C 1 790  ? 81.423  19.958  54.755  1.00 172.75 ? 790  LEU B CD1 1 
ATOM   18359 C  CD2 . LEU C 1 790  ? 79.636  21.344  55.782  1.00 167.08 ? 790  LEU B CD2 1 
ATOM   18360 N  N   . PRO C 1 791  ? 80.349  17.245  59.488  1.00 181.99 ? 791  PRO B N   1 
ATOM   18361 C  CA  . PRO C 1 791  ? 80.319  15.967  60.196  1.00 189.34 ? 791  PRO B CA  1 
ATOM   18362 C  C   . PRO C 1 791  ? 79.881  14.914  59.236  1.00 197.88 ? 791  PRO B C   1 
ATOM   18363 O  O   . PRO C 1 791  ? 79.035  15.199  58.390  1.00 200.39 ? 791  PRO B O   1 
ATOM   18364 C  CB  . PRO C 1 791  ? 79.201  16.153  61.226  1.00 186.07 ? 791  PRO B CB  1 
ATOM   18365 C  CG  . PRO C 1 791  ? 78.747  17.580  61.102  1.00 182.52 ? 791  PRO B CG  1 
ATOM   18366 C  CD  . PRO C 1 791  ? 79.146  18.042  59.747  1.00 180.48 ? 791  PRO B CD  1 
ATOM   18367 N  N   . ASP C 1 792  ? 80.444  13.723  59.347  1.00 214.70 ? 792  ASP B N   1 
ATOM   18368 C  CA  . ASP C 1 792  ? 79.897  12.618  58.601  1.00 221.58 ? 792  ASP B CA  1 
ATOM   18369 C  C   . ASP C 1 792  ? 78.475  12.467  59.134  1.00 215.36 ? 792  ASP B C   1 
ATOM   18370 O  O   . ASP C 1 792  ? 78.271  12.359  60.344  1.00 214.25 ? 792  ASP B O   1 
ATOM   18371 C  CB  . ASP C 1 792  ? 80.727  11.349  58.812  1.00 238.11 ? 792  ASP B CB  1 
ATOM   18372 C  CG  . ASP C 1 792  ? 80.501  10.303  57.718  1.00 256.98 ? 792  ASP B CG  1 
ATOM   18373 O  OD1 . ASP C 1 792  ? 79.478  10.383  57.002  1.00 263.92 ? 792  ASP B OD1 1 
ATOM   18374 O  OD2 . ASP C 1 792  ? 81.350  9.392   57.578  1.00 268.26 ? 792  ASP B OD2 1 
ATOM   18375 N  N   . SER C 1 793  ? 77.503  12.518  58.223  1.00 217.07 ? 793  SER B N   1 
ATOM   18376 C  CA  . SER C 1 793  ? 76.084  12.339  58.541  1.00 210.16 ? 793  SER B CA  1 
ATOM   18377 C  C   . SER C 1 793  ? 75.179  12.713  57.359  1.00 202.04 ? 793  SER B C   1 
ATOM   18378 O  O   . SER C 1 793  ? 75.453  13.660  56.618  1.00 201.01 ? 793  SER B O   1 
ATOM   18379 C  CB  . SER C 1 793  ? 75.685  13.149  59.775  1.00 208.12 ? 793  SER B CB  1 
ATOM   18380 O  OG  . SER C 1 793  ? 74.298  13.011  60.032  1.00 204.92 ? 793  SER B OG  1 
ATOM   18381 N  N   . LEU C 1 794  ? 74.094  11.970  57.184  1.00 224.13 ? 794  LEU B N   1 
ATOM   18382 C  CA  . LEU C 1 794  ? 73.142  12.294  56.134  1.00 216.82 ? 794  LEU B CA  1 
ATOM   18383 C  C   . LEU C 1 794  ? 72.139  13.329  56.601  1.00 214.16 ? 794  LEU B C   1 
ATOM   18384 O  O   . LEU C 1 794  ? 71.207  13.009  57.333  1.00 216.73 ? 794  LEU B O   1 
ATOM   18385 C  CB  . LEU C 1 794  ? 72.401  11.049  55.670  1.00 215.79 ? 794  LEU B CB  1 
ATOM   18386 C  CG  . LEU C 1 794  ? 73.092  10.291  54.544  1.00 218.11 ? 794  LEU B CG  1 
ATOM   18387 C  CD1 . LEU C 1 794  ? 74.385  9.655   55.052  1.00 220.44 ? 794  LEU B CD1 1 
ATOM   18388 C  CD2 . LEU C 1 794  ? 72.142  9.253   53.969  1.00 219.11 ? 794  LEU B CD2 1 
ATOM   18389 N  N   . THR C 1 795  ? 72.320  14.569  56.167  1.00 209.34 ? 795  THR B N   1 
ATOM   18390 C  CA  . THR C 1 795  ? 71.408  15.632  56.558  1.00 203.46 ? 795  THR B CA  1 
ATOM   18391 C  C   . THR C 1 795  ? 71.523  16.833  55.640  1.00 199.81 ? 795  THR B C   1 
ATOM   18392 O  O   . THR C 1 795  ? 72.374  16.881  54.745  1.00 196.85 ? 795  THR B O   1 
ATOM   18393 C  CB  . THR C 1 795  ? 71.657  16.108  58.013  1.00 259.98 ? 795  THR B CB  1 
ATOM   18394 O  OG1 . THR C 1 795  ? 73.055  16.027  58.320  1.00 261.44 ? 795  THR B OG1 1 
ATOM   18395 C  CG2 . THR C 1 795  ? 70.873  15.268  59.009  1.00 260.16 ? 795  THR B CG2 1 
ATOM   18396 N  N   . THR C 1 796  ? 70.637  17.795  55.859  1.00 205.03 ? 796  THR B N   1 
ATOM   18397 C  CA  . THR C 1 796  ? 70.768  19.096  55.235  1.00 203.58 ? 796  THR B CA  1 
ATOM   18398 C  C   . THR C 1 796  ? 70.935  20.120  56.341  1.00 206.53 ? 796  THR B C   1 
ATOM   18399 O  O   . THR C 1 796  ? 69.987  20.438  57.062  1.00 207.57 ? 796  THR B O   1 
ATOM   18400 C  CB  . THR C 1 796  ? 69.554  19.442  54.370  1.00 199.97 ? 796  THR B CB  1 
ATOM   18401 O  OG1 . THR C 1 796  ? 69.421  18.468  53.328  1.00 201.08 ? 796  THR B OG1 1 
ATOM   18402 C  CG2 . THR C 1 796  ? 69.731  20.813  53.744  1.00 197.23 ? 796  THR B CG2 1 
ATOM   18403 N  N   . TRP C 1 797  ? 72.163  20.603  56.486  1.00 187.25 ? 797  TRP B N   1 
ATOM   18404 C  CA  . TRP C 1 797  ? 72.506  21.578  57.513  1.00 184.75 ? 797  TRP B CA  1 
ATOM   18405 C  C   . TRP C 1 797  ? 72.030  22.978  57.128  1.00 178.53 ? 797  TRP B C   1 
ATOM   18406 O  O   . TRP C 1 797  ? 72.372  23.478  56.054  1.00 177.83 ? 797  TRP B O   1 
ATOM   18407 C  CB  . TRP C 1 797  ? 74.025  21.596  57.734  1.00 189.22 ? 797  TRP B CB  1 
ATOM   18408 C  CG  . TRP C 1 797  ? 74.576  20.335  58.327  1.00 195.81 ? 797  TRP B CG  1 
ATOM   18409 C  CD1 . TRP C 1 797  ? 75.646  19.604  57.884  1.00 200.05 ? 797  TRP B CD1 1 
ATOM   18410 C  CD2 . TRP C 1 797  ? 74.075  19.659  59.473  1.00 199.14 ? 797  TRP B CD2 1 
ATOM   18411 N  NE1 . TRP C 1 797  ? 75.837  18.513  58.696  1.00 203.90 ? 797  TRP B NE1 1 
ATOM   18412 C  CE2 . TRP C 1 797  ? 74.882  18.527  59.677  1.00 203.62 ? 797  TRP B CE2 1 
ATOM   18413 C  CE3 . TRP C 1 797  ? 73.018  19.903  60.348  1.00 199.39 ? 797  TRP B CE3 1 
ATOM   18414 C  CZ2 . TRP C 1 797  ? 74.663  17.646  60.714  1.00 205.41 ? 797  TRP B CZ2 1 
ATOM   18415 C  CZ3 . TRP C 1 797  ? 72.806  19.033  61.370  1.00 201.56 ? 797  TRP B CZ3 1 
ATOM   18416 C  CH2 . TRP C 1 797  ? 73.622  17.915  61.551  1.00 204.35 ? 797  TRP B CH2 1 
ATOM   18417 N  N   . GLU C 1 798  ? 71.244  23.611  57.994  1.00 175.56 ? 798  GLU B N   1 
ATOM   18418 C  CA  . GLU C 1 798  ? 70.882  25.006  57.773  1.00 173.17 ? 798  GLU B CA  1 
ATOM   18419 C  C   . GLU C 1 798  ? 71.618  25.908  58.738  1.00 172.39 ? 798  GLU B C   1 
ATOM   18420 O  O   . GLU C 1 798  ? 71.144  26.162  59.835  1.00 171.63 ? 798  GLU B O   1 
ATOM   18421 C  CB  . GLU C 1 798  ? 69.381  25.230  57.920  1.00 172.44 ? 798  GLU B CB  1 
ATOM   18422 C  CG  . GLU C 1 798  ? 69.003  26.690  57.760  1.00 172.58 ? 798  GLU B CG  1 
ATOM   18423 C  CD  . GLU C 1 798  ? 67.503  26.915  57.771  1.00 174.37 ? 798  GLU B CD  1 
ATOM   18424 O  OE1 . GLU C 1 798  ? 66.745  25.929  57.873  1.00 175.90 ? 798  GLU B OE1 1 
ATOM   18425 O  OE2 . GLU C 1 798  ? 67.078  28.083  57.675  1.00 174.84 ? 798  GLU B OE2 1 
ATOM   18426 N  N   . ILE C 1 799  ? 72.774  26.396  58.317  1.00 138.39 ? 799  ILE B N   1 
ATOM   18427 C  CA  . ILE C 1 799  ? 73.608  27.214  59.177  1.00 140.83 ? 799  ILE B CA  1 
ATOM   18428 C  C   . ILE C 1 799  ? 73.200  28.688  59.114  1.00 141.44 ? 799  ILE B C   1 
ATOM   18429 O  O   . ILE C 1 799  ? 73.622  29.422  58.236  1.00 142.34 ? 799  ILE B O   1 
ATOM   18430 C  CB  . ILE C 1 799  ? 75.110  26.916  58.916  1.00 135.80 ? 799  ILE B CB  1 
ATOM   18431 C  CG1 . ILE C 1 799  ? 75.902  28.098  58.370  1.00 135.18 ? 799  ILE B CG1 1 
ATOM   18432 C  CG2 . ILE C 1 799  ? 75.232  25.779  57.941  1.00 135.65 ? 799  ILE B CG2 1 
ATOM   18433 C  CD1 . ILE C 1 799  ? 77.290  27.666  57.894  1.00 134.55 ? 799  ILE B CD1 1 
ATOM   18434 N  N   . GLN C 1 800  ? 72.329  29.092  60.041  1.00 162.01 ? 800  GLN B N   1 
ATOM   18435 C  CA  . GLN C 1 800  ? 71.879  30.485  60.166  1.00 162.86 ? 800  GLN B CA  1 
ATOM   18436 C  C   . GLN C 1 800  ? 72.753  31.247  61.147  1.00 163.80 ? 800  GLN B C   1 
ATOM   18437 O  O   . GLN C 1 800  ? 73.195  30.707  62.159  1.00 164.76 ? 800  GLN B O   1 
ATOM   18438 C  CB  . GLN C 1 800  ? 70.411  30.575  60.615  1.00 164.02 ? 800  GLN B CB  1 
ATOM   18439 C  CG  . GLN C 1 800  ? 70.181  30.418  62.129  1.00 166.38 ? 800  GLN B CG  1 
ATOM   18440 C  CD  . GLN C 1 800  ? 69.440  29.127  62.495  1.00 167.24 ? 800  GLN B CD  1 
ATOM   18441 O  OE1 . GLN C 1 800  ? 69.286  28.235  61.664  1.00 168.26 ? 800  GLN B OE1 1 
ATOM   18442 N  NE2 . GLN C 1 800  ? 68.978  29.030  63.739  1.00 166.67 ? 800  GLN B NE2 1 
ATOM   18443 N  N   . GLY C 1 801  ? 72.994  32.514  60.853  1.00 136.83 ? 801  GLY B N   1 
ATOM   18444 C  CA  . GLY C 1 801  ? 73.949  33.273  61.630  1.00 136.55 ? 801  GLY B CA  1 
ATOM   18445 C  C   . GLY C 1 801  ? 73.451  34.668  61.904  1.00 136.85 ? 801  GLY B C   1 
ATOM   18446 O  O   . GLY C 1 801  ? 73.235  35.443  60.978  1.00 136.73 ? 801  GLY B O   1 
ATOM   18447 N  N   . ILE C 1 802  ? 73.242  34.960  63.188  1.00 173.17 ? 802  ILE B N   1 
ATOM   18448 C  CA  . ILE C 1 802  ? 72.874  36.290  63.675  1.00 173.58 ? 802  ILE B CA  1 
ATOM   18449 C  C   . ILE C 1 802  ? 74.112  37.029  64.205  1.00 174.75 ? 802  ILE B C   1 
ATOM   18450 O  O   . ILE C 1 802  ? 74.987  36.430  64.821  1.00 179.31 ? 802  ILE B O   1 
ATOM   18451 C  CB  . ILE C 1 802  ? 71.725  36.218  64.748  1.00 176.03 ? 802  ILE B CB  1 
ATOM   18452 C  CG1 . ILE C 1 802  ? 71.814  37.357  65.755  1.00 176.36 ? 802  ILE B CG1 1 
ATOM   18453 C  CG2 . ILE C 1 802  ? 71.743  34.908  65.505  1.00 176.41 ? 802  ILE B CG2 1 
ATOM   18454 C  CD1 . ILE C 1 802  ? 71.352  38.671  65.225  1.00 176.44 ? 802  ILE B CD1 1 
ATOM   18455 N  N   . GLY C 1 803  ? 74.193  38.326  63.936  1.00 191.00 ? 803  GLY B N   1 
ATOM   18456 C  CA  . GLY C 1 803  ? 75.299  39.134  64.418  1.00 189.87 ? 803  GLY B CA  1 
ATOM   18457 C  C   . GLY C 1 803  ? 74.788  40.442  64.985  1.00 193.61 ? 803  GLY B C   1 
ATOM   18458 O  O   . GLY C 1 803  ? 73.765  40.958  64.536  1.00 190.70 ? 803  GLY B O   1 
ATOM   18459 N  N   . ILE C 1 804  ? 75.491  40.989  65.969  1.00 153.64 ? 804  ILE B N   1 
ATOM   18460 C  CA  . ILE C 1 804  ? 75.024  42.209  66.603  1.00 154.13 ? 804  ILE B CA  1 
ATOM   18461 C  C   . ILE C 1 804  ? 76.178  43.078  67.063  1.00 156.66 ? 804  ILE B C   1 
ATOM   18462 O  O   . ILE C 1 804  ? 77.221  42.579  67.483  1.00 153.29 ? 804  ILE B O   1 
ATOM   18463 C  CB  . ILE C 1 804  ? 74.113  41.888  67.774  1.00 148.30 ? 804  ILE B CB  1 
ATOM   18464 C  CG1 . ILE C 1 804  ? 74.705  40.735  68.570  1.00 148.82 ? 804  ILE B CG1 1 
ATOM   18465 C  CG2 . ILE C 1 804  ? 72.741  41.488  67.279  1.00 146.40 ? 804  ILE B CG2 1 
ATOM   18466 C  CD1 . ILE C 1 804  ? 73.697  40.018  69.443  1.00 147.91 ? 804  ILE B CD1 1 
ATOM   18467 N  N   . SER C 1 805  ? 75.965  44.387  66.961  1.00 201.31 ? 805  SER B N   1 
ATOM   18468 C  CA  . SER C 1 805  ? 76.942  45.404  67.330  1.00 209.64 ? 805  SER B CA  1 
ATOM   18469 C  C   . SER C 1 805  ? 76.239  46.718  67.584  1.00 211.61 ? 805  SER B C   1 
ATOM   18470 O  O   . SER C 1 805  ? 75.050  46.762  67.897  1.00 212.86 ? 805  SER B O   1 
ATOM   18471 C  CB  . SER C 1 805  ? 77.970  45.621  66.223  1.00 207.95 ? 805  SER B CB  1 
ATOM   18472 O  OG  . SER C 1 805  ? 79.020  44.685  66.322  1.00 209.34 ? 805  SER B OG  1 
ATOM   18473 N  N   . ASN C 1 806  ? 76.989  47.793  67.420  1.00 235.50 ? 806  ASN B N   1 
ATOM   18474 C  CA  . ASN C 1 806  ? 76.510  49.104  67.798  1.00 243.78 ? 806  ASN B CA  1 
ATOM   18475 C  C   . ASN C 1 806  ? 75.405  49.643  66.891  1.00 246.07 ? 806  ASN B C   1 
ATOM   18476 O  O   . ASN C 1 806  ? 74.807  50.678  67.175  1.00 246.83 ? 806  ASN B O   1 
ATOM   18477 C  CB  . ASN C 1 806  ? 77.694  50.061  67.932  1.00 250.67 ? 806  ASN B CB  1 
ATOM   18478 C  CG  . ASN C 1 806  ? 78.685  49.599  68.991  1.00 257.44 ? 806  ASN B CG  1 
ATOM   18479 O  OD1 . ASN C 1 806  ? 79.780  49.132  68.677  1.00 260.04 ? 806  ASN B OD1 1 
ATOM   18480 N  ND2 . ASN C 1 806  ? 78.287  49.701  70.254  1.00 260.44 ? 806  ASN B ND2 1 
ATOM   18481 N  N   . THR C 1 807  ? 75.117  48.928  65.811  1.00 256.54 ? 807  THR B N   1 
ATOM   18482 C  CA  . THR C 1 807  ? 73.978  49.291  64.981  1.00 255.46 ? 807  THR B CA  1 
ATOM   18483 C  C   . THR C 1 807  ? 72.667  48.689  65.522  1.00 249.76 ? 807  THR B C   1 
ATOM   18484 O  O   . THR C 1 807  ? 71.609  49.307  65.428  1.00 252.73 ? 807  THR B O   1 
ATOM   18485 C  CB  . THR C 1 807  ? 74.213  48.963  63.480  1.00 257.18 ? 807  THR B CB  1 
ATOM   18486 O  OG1 . THR C 1 807  ? 74.736  47.636  63.342  1.00 257.58 ? 807  THR B OG1 1 
ATOM   18487 C  CG2 . THR C 1 807  ? 75.201  49.958  62.863  1.00 258.43 ? 807  THR B CG2 1 
ATOM   18488 N  N   . GLY C 1 808  ? 72.748  47.500  66.114  1.00 202.94 ? 808  GLY B N   1 
ATOM   18489 C  CA  . GLY C 1 808  ? 71.565  46.810  66.603  1.00 195.82 ? 808  GLY B CA  1 
ATOM   18490 C  C   . GLY C 1 808  ? 71.656  45.303  66.405  1.00 192.59 ? 808  GLY B C   1 
ATOM   18491 O  O   . GLY C 1 808  ? 72.715  44.712  66.618  1.00 190.58 ? 808  GLY B O   1 
ATOM   18492 N  N   . ILE C 1 809  ? 70.555  44.680  65.990  1.00 153.67 ? 809  ILE B N   1 
ATOM   18493 C  CA  . ILE C 1 809  ? 70.510  43.232  65.777  1.00 149.91 ? 809  ILE B CA  1 
ATOM   18494 C  C   . ILE C 1 809  ? 70.151  42.948  64.318  1.00 149.37 ? 809  ILE B C   1 
ATOM   18495 O  O   . ILE C 1 809  ? 69.160  43.487  63.846  1.00 151.82 ? 809  ILE B O   1 
ATOM   18496 C  CB  . ILE C 1 809  ? 69.446  42.580  66.710  1.00 146.91 ? 809  ILE B CB  1 
ATOM   18497 C  CG1 . ILE C 1 809  ? 69.311  41.079  66.463  1.00 149.63 ? 809  ILE B CG1 1 
ATOM   18498 C  CG2 . ILE C 1 809  ? 68.086  43.251  66.561  1.00 151.19 ? 809  ILE B CG2 1 
ATOM   18499 C  CD1 . ILE C 1 809  ? 67.951  40.524  66.841  1.00 148.62 ? 809  ILE B CD1 1 
ATOM   18500 N  N   . CYS C 1 810  ? 70.942  42.135  63.597  1.00 231.05 ? 810  CYS B N   1 
ATOM   18501 C  CA  . CYS C 1 810  ? 70.668  41.825  62.162  1.00 228.22 ? 810  CYS B CA  1 
ATOM   18502 C  C   . CYS C 1 810  ? 70.910  40.367  61.726  1.00 227.99 ? 810  CYS B C   1 
ATOM   18503 O  O   . CYS C 1 810  ? 72.026  39.856  61.818  1.00 227.05 ? 810  CYS B O   1 
ATOM   18504 C  CB  . CYS C 1 810  ? 71.439  42.774  61.223  1.00 226.31 ? 810  CYS B CB  1 
ATOM   18505 S  SG  . CYS C 1 810  ? 71.043  42.619  59.445  1.00 257.05 ? 810  CYS B SG  1 
ATOM   18506 N  N   . VAL C 1 811  ? 69.862  39.718  61.220  1.00 191.74 ? 811  VAL B N   1 
ATOM   18507 C  CA  . VAL C 1 811  ? 69.945  38.320  60.789  1.00 190.99 ? 811  VAL B CA  1 
ATOM   18508 C  C   . VAL C 1 811  ? 70.456  38.188  59.366  1.00 191.10 ? 811  VAL B C   1 
ATOM   18509 O  O   . VAL C 1 811  ? 69.853  38.726  58.445  1.00 191.60 ? 811  VAL B O   1 
ATOM   18510 C  CB  . VAL C 1 811  ? 68.568  37.647  60.806  1.00 191.18 ? 811  VAL B CB  1 
ATOM   18511 C  CG1 . VAL C 1 811  ? 68.685  36.190  60.375  1.00 191.88 ? 811  VAL B CG1 1 
ATOM   18512 C  CG2 . VAL C 1 811  ? 67.942  37.760  62.174  1.00 190.22 ? 811  VAL B CG2 1 
ATOM   18513 N  N   . ALA C 1 812  ? 71.546  37.453  59.171  1.00 236.72 ? 812  ALA B N   1 
ATOM   18514 C  CA  . ALA C 1 812  ? 72.023  37.189  57.818  1.00 235.38 ? 812  ALA B CA  1 
ATOM   18515 C  C   . ALA C 1 812  ? 71.092  36.210  57.117  1.00 233.85 ? 812  ALA B C   1 
ATOM   18516 O  O   . ALA C 1 812  ? 70.335  35.482  57.762  1.00 233.26 ? 812  ALA B O   1 
ATOM   18517 C  CB  . ALA C 1 812  ? 73.448  36.645  57.834  1.00 238.18 ? 812  ALA B CB  1 
ATOM   18518 N  N   . ASP C 1 813  ? 71.138  36.205  55.793  1.00 194.25 ? 813  ASP B N   1 
ATOM   18519 C  CA  . ASP C 1 813  ? 70.448  35.186  55.037  1.00 192.13 ? 813  ASP B CA  1 
ATOM   18520 C  C   . ASP C 1 813  ? 71.143  33.882  55.347  1.00 187.99 ? 813  ASP B C   1 
ATOM   18521 O  O   . ASP C 1 813  ? 72.373  33.807  55.291  1.00 186.21 ? 813  ASP B O   1 
ATOM   18522 C  CB  . ASP C 1 813  ? 70.541  35.498  53.553  1.00 196.58 ? 813  ASP B CB  1 
ATOM   18523 C  CG  . ASP C 1 813  ? 69.814  36.777  53.188  1.00 199.66 ? 813  ASP B CG  1 
ATOM   18524 O  OD1 . ASP C 1 813  ? 68.591  36.846  53.446  1.00 199.71 ? 813  ASP B OD1 1 
ATOM   18525 O  OD2 . ASP C 1 813  ? 70.459  37.712  52.655  1.00 201.25 ? 813  ASP B OD2 1 
ATOM   18526 N  N   . THR C 1 814  ? 70.356  32.865  55.692  1.00 154.20 ? 814  THR B N   1 
ATOM   18527 C  CA  . THR C 1 814  ? 70.893  31.539  55.993  1.00 153.07 ? 814  THR B CA  1 
ATOM   18528 C  C   . THR C 1 814  ? 71.790  31.057  54.862  1.00 152.63 ? 814  THR B C   1 
ATOM   18529 O  O   . THR C 1 814  ? 72.009  31.784  53.896  1.00 152.95 ? 814  THR B O   1 
ATOM   18530 C  CB  . THR C 1 814  ? 69.768  30.507  56.229  1.00 150.66 ? 814  THR B CB  1 
ATOM   18531 O  OG1 . THR C 1 814  ? 70.228  29.194  55.882  1.00 151.07 ? 814  THR B OG1 1 
ATOM   18532 C  CG2 . THR C 1 814  ? 68.546  30.848  55.390  1.00 150.46 ? 814  THR B CG2 1 
ATOM   18533 N  N   . VAL C 1 815  ? 72.320  29.843  54.996  1.00 219.48 ? 815  VAL B N   1 
ATOM   18534 C  CA  . VAL C 1 815  ? 73.079  29.182  53.935  1.00 222.75 ? 815  VAL B CA  1 
ATOM   18535 C  C   . VAL C 1 815  ? 72.990  27.671  54.137  1.00 224.07 ? 815  VAL B C   1 
ATOM   18536 O  O   . VAL C 1 815  ? 73.864  27.071  54.768  1.00 227.81 ? 815  VAL B O   1 
ATOM   18537 C  CB  . VAL C 1 815  ? 74.572  29.617  53.903  1.00 225.62 ? 815  VAL B CB  1 
ATOM   18538 C  CG1 . VAL C 1 815  ? 75.371  28.750  52.947  1.00 226.71 ? 815  VAL B CG1 1 
ATOM   18539 C  CG2 . VAL C 1 815  ? 74.704  31.077  53.506  1.00 225.66 ? 815  VAL B CG2 1 
ATOM   18540 N  N   . LYS C 1 816  ? 71.920  27.066  53.616  1.00 216.71 ? 816  LYS B N   1 
ATOM   18541 C  CA  . LYS C 1 816  ? 71.756  25.612  53.655  1.00 219.81 ? 816  LYS B CA  1 
ATOM   18542 C  C   . LYS C 1 816  ? 73.012  24.979  53.101  1.00 224.38 ? 816  LYS B C   1 
ATOM   18543 O  O   . LYS C 1 816  ? 73.862  25.671  52.535  1.00 222.98 ? 816  LYS B O   1 
ATOM   18544 C  CB  . LYS C 1 816  ? 70.558  25.151  52.817  1.00 243.91 ? 816  LYS B CB  1 
ATOM   18545 C  CG  . LYS C 1 816  ? 69.195  25.432  53.413  1.00 260.69 ? 816  LYS B CG  1 
ATOM   18546 C  CD  . LYS C 1 816  ? 68.776  26.867  53.175  1.00 258.87 ? 816  LYS B CD  1 
ATOM   18547 C  CE  . LYS C 1 816  ? 67.376  27.113  53.701  1.00 255.63 ? 816  LYS B CE  1 
ATOM   18548 N  NZ  . LYS C 1 816  ? 66.933  28.516  53.472  1.00 253.12 ? 816  LYS B NZ  1 
ATOM   18549 N  N   . ALA C 1 817  ? 73.130  23.667  53.248  1.00 180.73 ? 817  ALA B N   1 
ATOM   18550 C  CA  . ALA C 1 817  ? 74.326  22.988  52.776  1.00 188.62 ? 817  ALA B CA  1 
ATOM   18551 C  C   . ALA C 1 817  ? 74.303  21.500  53.108  1.00 189.70 ? 817  ALA B C   1 
ATOM   18552 O  O   . ALA C 1 817  ? 75.084  21.027  53.935  1.00 191.40 ? 817  ALA B O   1 
ATOM   18553 C  CB  . ALA C 1 817  ? 75.569  23.652  53.352  1.00 192.71 ? 817  ALA B CB  1 
ATOM   18554 N  N   . LYS C 1 818  ? 73.406  20.770  52.449  1.00 230.84 ? 818  LYS B N   1 
ATOM   18555 C  CA  . LYS C 1 818  ? 73.285  19.325  52.621  1.00 232.14 ? 818  LYS B CA  1 
ATOM   18556 C  C   . LYS C 1 818  ? 74.590  18.608  52.296  1.00 231.27 ? 818  LYS B C   1 
ATOM   18557 O  O   . LYS C 1 818  ? 75.253  18.899  51.298  1.00 229.34 ? 818  LYS B O   1 
ATOM   18558 C  CB  . LYS C 1 818  ? 72.162  18.767  51.737  1.00 235.52 ? 818  LYS B CB  1 
ATOM   18559 C  CG  . LYS C 1 818  ? 72.419  18.918  50.229  1.00 241.59 ? 818  LYS B CG  1 
ATOM   18560 C  CD  . LYS C 1 818  ? 71.235  18.443  49.371  1.00 246.81 ? 818  LYS B CD  1 
ATOM   18561 C  CE  . LYS C 1 818  ? 71.488  18.626  47.865  1.00 251.96 ? 818  LYS B CE  1 
ATOM   18562 N  NZ  . LYS C 1 818  ? 70.476  17.916  47.020  1.00 253.46 ? 818  LYS B NZ  1 
ATOM   18563 N  N   . VAL C 1 819  ? 74.965  17.681  53.161  1.00 214.11 ? 819  VAL B N   1 
ATOM   18564 C  CA  . VAL C 1 819  ? 76.079  16.810  52.875  1.00 215.68 ? 819  VAL B CA  1 
ATOM   18565 C  C   . VAL C 1 819  ? 75.443  15.475  52.619  1.00 216.96 ? 819  VAL B C   1 
ATOM   18566 O  O   . VAL C 1 819  ? 74.388  15.175  53.176  1.00 216.27 ? 819  VAL B O   1 
ATOM   18567 C  CB  . VAL C 1 819  ? 77.021  16.672  54.073  1.00 214.87 ? 819  VAL B CB  1 
ATOM   18568 C  CG1 . VAL C 1 819  ? 77.583  18.028  54.465  1.00 214.10 ? 819  VAL B CG1 1 
ATOM   18569 C  CG2 . VAL C 1 819  ? 76.294  16.034  55.246  1.00 213.04 ? 819  VAL B CG2 1 
ATOM   18570 N  N   . PHE C 1 820  ? 76.078  14.671  51.781  1.00 211.70 ? 820  PHE B N   1 
ATOM   18571 C  CA  . PHE C 1 820  ? 75.542  13.362  51.479  1.00 217.30 ? 820  PHE B CA  1 
ATOM   18572 C  C   . PHE C 1 820  ? 76.371  12.606  50.445  1.00 219.47 ? 820  PHE B C   1 
ATOM   18573 O  O   . PHE C 1 820  ? 76.887  13.192  49.493  1.00 217.22 ? 820  PHE B O   1 
ATOM   18574 C  CB  . PHE C 1 820  ? 74.110  13.494  50.988  1.00 224.98 ? 820  PHE B CB  1 
ATOM   18575 C  CG  . PHE C 1 820  ? 73.688  12.368  50.135  1.00 237.93 ? 820  PHE B CG  1 
ATOM   18576 C  CD1 . PHE C 1 820  ? 73.839  12.440  48.765  1.00 244.62 ? 820  PHE B CD1 1 
ATOM   18577 C  CD2 . PHE C 1 820  ? 73.185  11.217  50.699  1.00 243.81 ? 820  PHE B CD2 1 
ATOM   18578 C  CE1 . PHE C 1 820  ? 73.471  11.391  47.965  1.00 250.09 ? 820  PHE B CE1 1 
ATOM   18579 C  CE2 . PHE C 1 820  ? 72.815  10.166  49.909  1.00 248.49 ? 820  PHE B CE2 1 
ATOM   18580 C  CZ  . PHE C 1 820  ? 72.957  10.252  48.535  1.00 251.15 ? 820  PHE B CZ  1 
ATOM   18581 N  N   . LYS C 1 821  ? 76.483  11.297  50.640  1.00 249.42 ? 821  LYS B N   1 
ATOM   18582 C  CA  . LYS C 1 821  ? 77.260  10.435  49.756  1.00 253.85 ? 821  LYS B CA  1 
ATOM   18583 C  C   . LYS C 1 821  ? 76.336  9.722   48.768  1.00 255.48 ? 821  LYS B C   1 
ATOM   18584 O  O   . LYS C 1 821  ? 75.347  9.123   49.171  1.00 256.60 ? 821  LYS B O   1 
ATOM   18585 C  CB  . LYS C 1 821  ? 78.034  9.413   50.597  1.00 253.89 ? 821  LYS B CB  1 
ATOM   18586 C  CG  . LYS C 1 821  ? 78.957  8.479   49.827  1.00 252.95 ? 821  LYS B CG  1 
ATOM   18587 C  CD  . LYS C 1 821  ? 80.431  8.750   50.148  1.00 251.76 ? 821  LYS B CD  1 
ATOM   18588 C  CE  . LYS C 1 821  ? 81.323  7.585   49.718  1.00 253.36 ? 821  LYS B CE  1 
ATOM   18589 N  NZ  . LYS C 1 821  ? 82.780  7.843   49.939  1.00 254.85 ? 821  LYS B NZ  1 
ATOM   18590 N  N   . ASP C 1 822  ? 76.672  9.775   47.482  1.00 243.22 ? 822  ASP B N   1 
ATOM   18591 C  CA  . ASP C 1 822  ? 75.835  9.196   46.430  1.00 241.81 ? 822  ASP B CA  1 
ATOM   18592 C  C   . ASP C 1 822  ? 75.250  7.830   46.773  1.00 240.30 ? 822  ASP B C   1 
ATOM   18593 O  O   . ASP C 1 822  ? 74.041  7.680   46.950  1.00 234.06 ? 822  ASP B O   1 
ATOM   18594 C  CB  . ASP C 1 822  ? 76.629  9.074   45.127  1.00 249.45 ? 822  ASP B CB  1 
ATOM   18595 C  CG  . ASP C 1 822  ? 76.931  10.419  44.496  1.00 257.34 ? 822  ASP B CG  1 
ATOM   18596 O  OD1 . ASP C 1 822  ? 77.027  11.411  45.253  1.00 260.18 ? 822  ASP B OD1 1 
ATOM   18597 O  OD2 . ASP C 1 822  ? 77.072  10.478  43.248  1.00 260.55 ? 822  ASP B OD2 1 
ATOM   18598 N  N   . VAL C 1 823  ? 76.114  6.828   46.842  1.00 177.24 ? 823  VAL B N   1 
ATOM   18599 C  CA  . VAL C 1 823  ? 75.677  5.483   47.178  1.00 177.88 ? 823  VAL B CA  1 
ATOM   18600 C  C   . VAL C 1 823  ? 76.469  4.920   48.338  1.00 184.44 ? 823  VAL B C   1 
ATOM   18601 O  O   . VAL C 1 823  ? 77.671  5.155   48.454  1.00 191.34 ? 823  VAL B O   1 
ATOM   18602 C  CB  . VAL C 1 823  ? 75.852  4.545   46.016  1.00 174.53 ? 823  VAL B CB  1 
ATOM   18603 C  CG1 . VAL C 1 823  ? 75.758  3.100   46.488  1.00 173.06 ? 823  VAL B CG1 1 
ATOM   18604 C  CG2 . VAL C 1 823  ? 74.807  4.849   44.985  1.00 170.41 ? 823  VAL B CG2 1 
ATOM   18605 N  N   . PHE C 1 824  ? 75.806  4.153   49.193  1.00 182.86 ? 824  PHE B N   1 
ATOM   18606 C  CA  . PHE C 1 824  ? 76.454  3.717   50.414  1.00 184.09 ? 824  PHE B CA  1 
ATOM   18607 C  C   . PHE C 1 824  ? 75.764  2.530   51.056  1.00 178.75 ? 824  PHE B C   1 
ATOM   18608 O  O   . PHE C 1 824  ? 74.542  2.428   51.046  1.00 173.18 ? 824  PHE B O   1 
ATOM   18609 C  CB  . PHE C 1 824  ? 76.539  4.890   51.395  1.00 186.71 ? 824  PHE B CB  1 
ATOM   18610 C  CG  . PHE C 1 824  ? 75.208  5.546   51.698  1.00 186.01 ? 824  PHE B CG  1 
ATOM   18611 C  CD1 . PHE C 1 824  ? 74.506  5.224   52.850  1.00 188.54 ? 824  PHE B CD1 1 
ATOM   18612 C  CD2 . PHE C 1 824  ? 74.672  6.499   50.850  1.00 184.72 ? 824  PHE B CD2 1 
ATOM   18613 C  CE1 . PHE C 1 824  ? 73.289  5.834   53.146  1.00 186.55 ? 824  PHE B CE1 1 
ATOM   18614 C  CE2 . PHE C 1 824  ? 73.453  7.108   51.143  1.00 182.83 ? 824  PHE B CE2 1 
ATOM   18615 C  CZ  . PHE C 1 824  ? 72.763  6.768   52.290  1.00 183.45 ? 824  PHE B CZ  1 
ATOM   18616 N  N   . LEU C 1 825  ? 76.564  1.626   51.606  1.00 185.75 ? 825  LEU B N   1 
ATOM   18617 C  CA  . LEU C 1 825  ? 76.037  0.481   52.338  1.00 180.08 ? 825  LEU B CA  1 
ATOM   18618 C  C   . LEU C 1 825  ? 75.873  0.748   53.833  1.00 181.12 ? 825  LEU B C   1 
ATOM   18619 O  O   . LEU C 1 825  ? 76.701  1.415   54.459  1.00 184.30 ? 825  LEU B O   1 
ATOM   18620 C  CB  . LEU C 1 825  ? 76.953  -0.734  52.163  1.00 177.23 ? 825  LEU B CB  1 
ATOM   18621 C  CG  . LEU C 1 825  ? 76.743  -1.798  53.252  1.00 170.63 ? 825  LEU B CG  1 
ATOM   18622 C  CD1 . LEU C 1 825  ? 75.488  -2.605  52.966  1.00 163.59 ? 825  LEU B CD1 1 
ATOM   18623 C  CD2 . LEU C 1 825  ? 77.957  -2.707  53.426  1.00 173.09 ? 825  LEU B CD2 1 
ATOM   18624 N  N   . GLU C 1 826  ? 74.803  0.209   54.402  1.00 231.61 ? 826  GLU B N   1 
ATOM   18625 C  CA  . GLU C 1 826  ? 74.692  0.104   55.847  1.00 232.68 ? 826  GLU B CA  1 
ATOM   18626 C  C   . GLU C 1 826  ? 74.437  -1.358  56.188  1.00 232.44 ? 826  GLU B C   1 
ATOM   18627 O  O   . GLU C 1 826  ? 73.924  -2.117  55.364  1.00 228.32 ? 826  GLU B O   1 
ATOM   18628 C  CB  . GLU C 1 826  ? 73.567  0.982   56.383  1.00 230.84 ? 826  GLU B CB  1 
ATOM   18629 C  CG  . GLU C 1 826  ? 72.201  0.326   56.351  1.00 230.54 ? 826  GLU B CG  1 
ATOM   18630 C  CD  . GLU C 1 826  ? 71.318  0.789   57.492  1.00 232.21 ? 826  GLU B CD  1 
ATOM   18631 O  OE1 . GLU C 1 826  ? 70.469  -0.006  57.954  1.00 231.47 ? 826  GLU B OE1 1 
ATOM   18632 O  OE2 . GLU C 1 826  ? 71.487  1.944   57.936  1.00 233.63 ? 826  GLU B OE2 1 
ATOM   18633 N  N   . MET C 1 827  ? 74.798  -1.765  57.394  1.00 166.15 ? 827  MET B N   1 
ATOM   18634 C  CA  . MET C 1 827  ? 74.649  -3.157  57.760  1.00 165.72 ? 827  MET B CA  1 
ATOM   18635 C  C   . MET C 1 827  ? 73.980  -3.220  59.106  1.00 163.02 ? 827  MET B C   1 
ATOM   18636 O  O   . MET C 1 827  ? 74.482  -2.667  60.071  1.00 167.24 ? 827  MET B O   1 
ATOM   18637 C  CB  . MET C 1 827  ? 76.017  -3.836  57.825  1.00 171.22 ? 827  MET B CB  1 
ATOM   18638 C  CG  . MET C 1 827  ? 76.742  -3.932  56.481  1.00 171.92 ? 827  MET B CG  1 
ATOM   18639 S  SD  . MET C 1 827  ? 75.966  -5.084  55.329  1.00 157.53 ? 827  MET B SD  1 
ATOM   18640 C  CE  . MET C 1 827  ? 76.290  -6.664  56.120  1.00 144.14 ? 827  MET B CE  1 
ATOM   18641 N  N   . ASN C 1 828  ? 72.840  -3.885  59.173  1.00 189.70 ? 828  ASN B N   1 
ATOM   18642 C  CA  . ASN C 1 828  ? 72.184  -4.082  60.450  1.00 188.46 ? 828  ASN B CA  1 
ATOM   18643 C  C   . ASN C 1 828  ? 72.732  -5.331  61.187  1.00 186.50 ? 828  ASN B C   1 
ATOM   18644 O  O   . ASN C 1 828  ? 72.251  -6.448  60.958  1.00 184.91 ? 828  ASN B O   1 
ATOM   18645 C  CB  . ASN C 1 828  ? 70.669  -4.172  60.237  1.00 191.94 ? 828  ASN B CB  1 
ATOM   18646 C  CG  . ASN C 1 828  ? 69.870  -3.771  61.467  1.00 199.65 ? 828  ASN B CG  1 
ATOM   18647 O  OD1 . ASN C 1 828  ? 69.665  -2.582  61.726  1.00 202.51 ? 828  ASN B OD1 1 
ATOM   18648 N  ND2 . ASN C 1 828  ? 69.391  -4.764  62.215  1.00 202.97 ? 828  ASN B ND2 1 
ATOM   18649 N  N   . ILE C 1 829  ? 73.754  -5.128  62.037  1.00 156.02 ? 829  ILE B N   1 
ATOM   18650 C  CA  . ILE C 1 829  ? 74.304  -6.156  62.947  1.00 151.06 ? 829  ILE B CA  1 
ATOM   18651 C  C   . ILE C 1 829  ? 73.462  -6.230  64.230  1.00 150.01 ? 829  ILE B C   1 
ATOM   18652 O  O   . ILE C 1 829  ? 72.934  -5.217  64.680  1.00 144.29 ? 829  ILE B O   1 
ATOM   18653 C  CB  . ILE C 1 829  ? 75.779  -5.847  63.341  1.00 152.24 ? 829  ILE B CB  1 
ATOM   18654 C  CG1 . ILE C 1 829  ? 76.547  -5.272  62.156  1.00 149.92 ? 829  ILE B CG1 1 
ATOM   18655 C  CG2 . ILE C 1 829  ? 76.495  -7.083  63.900  1.00 154.76 ? 829  ILE B CG2 1 
ATOM   18656 C  CD1 . ILE C 1 829  ? 76.683  -6.232  60.990  1.00 153.94 ? 829  ILE B CD1 1 
ATOM   18657 N  N   . PRO C 1 830  ? 73.334  -7.429  64.820  1.00 158.32 ? 830  PRO B N   1 
ATOM   18658 C  CA  . PRO C 1 830  ? 72.549  -7.606  66.050  1.00 162.22 ? 830  PRO B CA  1 
ATOM   18659 C  C   . PRO C 1 830  ? 73.270  -7.038  67.256  1.00 174.11 ? 830  PRO B C   1 
ATOM   18660 O  O   . PRO C 1 830  ? 74.422  -6.618  67.144  1.00 188.70 ? 830  PRO B O   1 
ATOM   18661 C  CB  . PRO C 1 830  ? 72.484  -9.127  66.216  1.00 159.54 ? 830  PRO B CB  1 
ATOM   18662 C  CG  . PRO C 1 830  ? 73.052  -9.717  64.964  1.00 162.63 ? 830  PRO B CG  1 
ATOM   18663 C  CD  . PRO C 1 830  ? 73.927  -8.693  64.351  1.00 164.73 ? 830  PRO B CD  1 
ATOM   18664 N  N   . TYR C 1 831  ? 72.608  -7.039  68.407  1.00 218.17 ? 831  TYR B N   1 
ATOM   18665 C  CA  . TYR C 1 831  ? 73.298  -6.702  69.638  1.00 222.72 ? 831  TYR B CA  1 
ATOM   18666 C  C   . TYR C 1 831  ? 74.261  -7.837  69.941  1.00 223.39 ? 831  TYR B C   1 
ATOM   18667 O  O   . TYR C 1 831  ? 75.474  -7.651  69.950  1.00 227.54 ? 831  TYR B O   1 
ATOM   18668 C  CB  . TYR C 1 831  ? 72.316  -6.480  70.798  1.00 225.85 ? 831  TYR B CB  1 
ATOM   18669 C  CG  . TYR C 1 831  ? 73.001  -6.128  72.102  1.00 233.98 ? 831  TYR B CG  1 
ATOM   18670 C  CD1 . TYR C 1 831  ? 72.610  -6.710  73.296  1.00 236.19 ? 831  TYR B CD1 1 
ATOM   18671 C  CD2 . TYR C 1 831  ? 74.054  -5.226  72.130  1.00 237.12 ? 831  TYR B CD2 1 
ATOM   18672 C  CE1 . TYR C 1 831  ? 73.246  -6.396  74.485  1.00 241.53 ? 831  TYR B CE1 1 
ATOM   18673 C  CE2 . TYR C 1 831  ? 74.694  -4.906  73.311  1.00 242.65 ? 831  TYR B CE2 1 
ATOM   18674 C  CZ  . TYR C 1 831  ? 74.287  -5.494  74.486  1.00 244.96 ? 831  TYR B CZ  1 
ATOM   18675 O  OH  . TYR C 1 831  ? 74.924  -5.180  75.666  1.00 250.58 ? 831  TYR B OH  1 
ATOM   18676 N  N   . SER C 1 832  ? 73.715  -9.028  70.133  1.00 166.97 ? 832  SER B N   1 
ATOM   18677 C  CA  . SER C 1 832  ? 74.515  -10.145 70.583  1.00 174.06 ? 832  SER B CA  1 
ATOM   18678 C  C   . SER C 1 832  ? 74.202  -11.378 69.776  1.00 171.19 ? 832  SER B C   1 
ATOM   18679 O  O   . SER C 1 832  ? 73.184  -11.433 69.090  1.00 166.70 ? 832  SER B O   1 
ATOM   18680 C  CB  . SER C 1 832  ? 74.152  -10.461 72.013  1.00 179.70 ? 832  SER B CB  1 
ATOM   18681 O  OG  . SER C 1 832  ? 72.894  -11.108 72.039  1.00 179.09 ? 832  SER B OG  1 
ATOM   18682 N  N   . VAL C 1 833  ? 75.064  -12.382 69.905  1.00 187.52 ? 833  VAL B N   1 
ATOM   18683 C  CA  . VAL C 1 833  ? 74.898  -13.668 69.247  1.00 184.61 ? 833  VAL B CA  1 
ATOM   18684 C  C   . VAL C 1 833  ? 75.618  -14.712 70.089  1.00 186.53 ? 833  VAL B C   1 
ATOM   18685 O  O   . VAL C 1 833  ? 76.760  -14.490 70.499  1.00 190.26 ? 833  VAL B O   1 
ATOM   18686 C  CB  . VAL C 1 833  ? 75.570  -13.679 67.874  1.00 183.74 ? 833  VAL B CB  1 
ATOM   18687 C  CG1 . VAL C 1 833  ? 75.296  -14.990 67.189  1.00 182.06 ? 833  VAL B CG1 1 
ATOM   18688 C  CG2 . VAL C 1 833  ? 75.095  -12.516 67.027  1.00 181.50 ? 833  VAL B CG2 1 
ATOM   18689 N  N   . VAL C 1 834  ? 74.956  -15.841 70.347  1.00 183.87 ? 834  VAL B N   1 
ATOM   18690 C  CA  . VAL C 1 834  ? 75.564  -16.983 71.053  1.00 188.20 ? 834  VAL B CA  1 
ATOM   18691 C  C   . VAL C 1 834  ? 76.591  -17.693 70.155  1.00 194.13 ? 834  VAL B C   1 
ATOM   18692 O  O   . VAL C 1 834  ? 76.400  -17.784 68.939  1.00 191.86 ? 834  VAL B O   1 
ATOM   18693 C  CB  . VAL C 1 834  ? 74.470  -18.006 71.506  1.00 185.47 ? 834  VAL B CB  1 
ATOM   18694 C  CG1 . VAL C 1 834  ? 75.077  -19.258 72.111  1.00 190.03 ? 834  VAL B CG1 1 
ATOM   18695 C  CG2 . VAL C 1 834  ? 73.502  -17.356 72.478  1.00 182.61 ? 834  VAL B CG2 1 
ATOM   18696 N  N   . ARG C 1 835  ? 77.683  -18.180 70.741  1.00 187.19 ? 835  ARG B N   1 
ATOM   18697 C  CA  . ARG C 1 835  ? 78.605  -19.049 70.010  1.00 195.06 ? 835  ARG B CA  1 
ATOM   18698 C  C   . ARG C 1 835  ? 77.796  -20.188 69.421  1.00 193.13 ? 835  ARG B C   1 
ATOM   18699 O  O   . ARG C 1 835  ? 76.933  -20.751 70.095  1.00 192.11 ? 835  ARG B O   1 
ATOM   18700 C  CB  . ARG C 1 835  ? 79.703  -19.614 70.935  1.00 203.90 ? 835  ARG B CB  1 
ATOM   18701 C  CG  . ARG C 1 835  ? 80.235  -21.021 70.553  1.00 209.85 ? 835  ARG B CG  1 
ATOM   18702 C  CD  . ARG C 1 835  ? 81.604  -21.338 71.187  1.00 219.24 ? 835  ARG B CD  1 
ATOM   18703 N  NE  . ARG C 1 835  ? 81.614  -21.125 72.625  1.00 221.49 ? 835  ARG B NE  1 
ATOM   18704 C  CZ  . ARG C 1 835  ? 80.599  -21.433 73.420  1.00 218.68 ? 835  ARG B CZ  1 
ATOM   18705 N  NH1 . ARG C 1 835  ? 79.500  -21.979 72.929  1.00 212.96 ? 835  ARG B NH1 1 
ATOM   18706 N  NH2 . ARG C 1 835  ? 80.683  -21.203 74.711  1.00 220.96 ? 835  ARG B NH2 1 
ATOM   18707 N  N   . GLY C 1 836  ? 78.060  -20.518 68.163  1.00 218.15 ? 836  GLY B N   1 
ATOM   18708 C  CA  . GLY C 1 836  ? 77.472  -21.702 67.569  1.00 218.14 ? 836  GLY B CA  1 
ATOM   18709 C  C   . GLY C 1 836  ? 76.074  -21.548 67.007  1.00 213.44 ? 836  GLY B C   1 
ATOM   18710 O  O   . GLY C 1 836  ? 75.506  -22.504 66.487  1.00 210.70 ? 836  GLY B O   1 
ATOM   18711 N  N   . GLU C 1 837  ? 75.495  -20.365 67.122  1.00 202.10 ? 837  GLU B N   1 
ATOM   18712 C  CA  . GLU C 1 837  ? 74.250  -20.116 66.428  1.00 197.39 ? 837  GLU B CA  1 
ATOM   18713 C  C   . GLU C 1 837  ? 74.609  -19.657 65.013  1.00 199.76 ? 837  GLU B C   1 
ATOM   18714 O  O   . GLU C 1 837  ? 75.658  -19.048 64.811  1.00 202.88 ? 837  GLU B O   1 
ATOM   18715 C  CB  . GLU C 1 837  ? 73.428  -19.056 67.163  1.00 193.32 ? 837  GLU B CB  1 
ATOM   18716 C  CG  . GLU C 1 837  ? 72.746  -19.533 68.451  1.00 181.31 ? 837  GLU B CG  1 
ATOM   18717 C  CD  . GLU C 1 837  ? 71.935  -18.421 69.143  1.00 174.65 ? 837  GLU B CD  1 
ATOM   18718 O  OE1 . GLU C 1 837  ? 72.430  -17.274 69.241  1.00 175.02 ? 837  GLU B OE1 1 
ATOM   18719 O  OE2 . GLU C 1 837  ? 70.803  -18.685 69.604  1.00 169.29 ? 837  GLU B OE2 1 
ATOM   18720 N  N   . GLN C 1 838  ? 73.771  -19.982 64.032  1.00 187.41 ? 838  GLN B N   1 
ATOM   18721 C  CA  . GLN C 1 838  ? 73.958  -19.477 62.674  1.00 186.12 ? 838  GLN B CA  1 
ATOM   18722 C  C   . GLN C 1 838  ? 73.190  -18.164 62.571  1.00 181.07 ? 838  GLN B C   1 
ATOM   18723 O  O   . GLN C 1 838  ? 71.980  -18.126 62.755  1.00 174.52 ? 838  GLN B O   1 
ATOM   18724 C  CB  . GLN C 1 838  ? 73.453  -20.503 61.642  1.00 186.30 ? 838  GLN B CB  1 
ATOM   18725 C  CG  . GLN C 1 838  ? 73.759  -20.198 60.141  1.00 189.70 ? 838  GLN B CG  1 
ATOM   18726 C  CD  . GLN C 1 838  ? 73.166  -21.250 59.142  1.00 197.54 ? 838  GLN B CD  1 
ATOM   18727 O  OE1 . GLN C 1 838  ? 73.828  -22.232 58.769  1.00 203.52 ? 838  GLN B OE1 1 
ATOM   18728 N  NE2 . GLN C 1 838  ? 71.924  -21.021 58.702  1.00 193.95 ? 838  GLN B NE2 1 
ATOM   18729 N  N   . ILE C 1 839  ? 73.886  -17.072 62.310  1.00 214.91 ? 839  ILE B N   1 
ATOM   18730 C  CA  . ILE C 1 839  ? 73.192  -15.798 62.236  1.00 211.69 ? 839  ILE B CA  1 
ATOM   18731 C  C   . ILE C 1 839  ? 72.884  -15.403 60.793  1.00 211.81 ? 839  ILE B C   1 
ATOM   18732 O  O   . ILE C 1 839  ? 73.461  -15.962 59.862  1.00 215.93 ? 839  ILE B O   1 
ATOM   18733 C  CB  . ILE C 1 839  ? 74.008  -14.689 62.895  1.00 213.86 ? 839  ILE B CB  1 
ATOM   18734 C  CG1 . ILE C 1 839  ? 73.125  -13.468 63.171  1.00 209.62 ? 839  ILE B CG1 1 
ATOM   18735 C  CG2 . ILE C 1 839  ? 75.196  -14.323 62.031  1.00 216.16 ? 839  ILE B CG2 1 
ATOM   18736 C  CD1 . ILE C 1 839  ? 72.059  -13.710 64.228  1.00 208.27 ? 839  ILE B CD1 1 
ATOM   18737 N  N   . GLN C 1 840  ? 71.974  -14.449 60.607  1.00 198.72 ? 840  GLN B N   1 
ATOM   18738 C  CA  . GLN C 1 840  ? 71.765  -13.850 59.294  1.00 195.83 ? 840  GLN B CA  1 
ATOM   18739 C  C   . GLN C 1 840  ? 71.981  -12.339 59.329  1.00 188.46 ? 840  GLN B C   1 
ATOM   18740 O  O   . GLN C 1 840  ? 71.119  -11.581 59.757  1.00 183.71 ? 840  GLN B O   1 
ATOM   18741 C  CB  . GLN C 1 840  ? 70.381  -14.191 58.741  1.00 197.82 ? 840  GLN B CB  1 
ATOM   18742 C  CG  . GLN C 1 840  ? 70.391  -14.656 57.271  1.00 205.82 ? 840  GLN B CG  1 
ATOM   18743 C  CD  . GLN C 1 840  ? 69.820  -13.629 56.278  1.00 208.76 ? 840  GLN B CD  1 
ATOM   18744 O  OE1 . GLN C 1 840  ? 69.698  -13.910 55.081  1.00 210.89 ? 840  GLN B OE1 1 
ATOM   18745 N  NE2 . GLN C 1 840  ? 69.465  -12.444 56.775  1.00 207.69 ? 840  GLN B NE2 1 
ATOM   18746 N  N   . LEU C 1 841  ? 73.149  -11.927 58.852  1.00 209.33 ? 841  LEU B N   1 
ATOM   18747 C  CA  . LEU C 1 841  ? 73.581  -10.534 58.870  1.00 205.20 ? 841  LEU B CA  1 
ATOM   18748 C  C   . LEU C 1 841  ? 72.992  -9.680  57.748  1.00 199.43 ? 841  LEU B C   1 
ATOM   18749 O  O   . LEU C 1 841  ? 73.574  -9.609  56.665  1.00 198.33 ? 841  LEU B O   1 
ATOM   18750 C  CB  . LEU C 1 841  ? 75.103  -10.480 58.741  1.00 207.45 ? 841  LEU B CB  1 
ATOM   18751 C  CG  . LEU C 1 841  ? 75.915  -10.929 59.948  1.00 206.87 ? 841  LEU B CG  1 
ATOM   18752 C  CD1 . LEU C 1 841  ? 77.393  -10.644 59.708  1.00 209.81 ? 841  LEU B CD1 1 
ATOM   18753 C  CD2 . LEU C 1 841  ? 75.419  -10.199 61.192  1.00 203.46 ? 841  LEU B CD2 1 
ATOM   18754 N  N   . LYS C 1 842  ? 71.884  -8.989  57.998  1.00 213.78 ? 842  LYS B N   1 
ATOM   18755 C  CA  . LYS C 1 842  ? 71.254  -8.207  56.932  1.00 211.08 ? 842  LYS B CA  1 
ATOM   18756 C  C   . LYS C 1 842  ? 71.842  -6.808  56.720  1.00 213.12 ? 842  LYS B C   1 
ATOM   18757 O  O   . LYS C 1 842  ? 72.861  -6.450  57.306  1.00 215.84 ? 842  LYS B O   1 
ATOM   18758 C  CB  . LYS C 1 842  ? 69.743  -8.121  57.141  1.00 206.32 ? 842  LYS B CB  1 
ATOM   18759 C  CG  . LYS C 1 842  ? 69.036  -9.458  57.044  1.00 205.95 ? 842  LYS B CG  1 
ATOM   18760 C  CD  . LYS C 1 842  ? 67.538  -9.272  56.919  1.00 202.83 ? 842  LYS B CD  1 
ATOM   18761 C  CE  . LYS C 1 842  ? 66.832  -10.613 56.884  1.00 203.56 ? 842  LYS B CE  1 
ATOM   18762 N  NZ  . LYS C 1 842  ? 65.354  -10.463 56.794  1.00 202.07 ? 842  LYS B NZ  1 
ATOM   18763 N  N   . GLY C 1 843  ? 71.190  -6.035  55.858  1.00 149.69 ? 843  GLY B N   1 
ATOM   18764 C  CA  . GLY C 1 843  ? 71.632  -4.695  55.517  1.00 152.44 ? 843  GLY B CA  1 
ATOM   18765 C  C   . GLY C 1 843  ? 70.999  -4.276  54.199  1.00 151.28 ? 843  GLY B C   1 
ATOM   18766 O  O   . GLY C 1 843  ? 70.267  -5.062  53.610  1.00 150.39 ? 843  GLY B O   1 
ATOM   18767 N  N   . THR C 1 844  ? 71.270  -3.056  53.731  1.00 218.88 ? 844  THR B N   1 
ATOM   18768 C  CA  . THR C 1 844  ? 70.728  -2.571  52.455  1.00 219.35 ? 844  THR B CA  1 
ATOM   18769 C  C   . THR C 1 844  ? 71.614  -1.469  51.862  1.00 218.23 ? 844  THR B C   1 
ATOM   18770 O  O   . THR C 1 844  ? 71.826  -0.435  52.500  1.00 217.85 ? 844  THR B O   1 
ATOM   18771 C  CB  . THR C 1 844  ? 69.295  -2.001  52.619  1.00 197.26 ? 844  THR B CB  1 
ATOM   18772 O  OG1 . THR C 1 844  ? 69.340  -0.789  53.381  1.00 196.50 ? 844  THR B OG1 1 
ATOM   18773 C  CG2 . THR C 1 844  ? 68.370  -2.992  53.317  1.00 189.69 ? 844  THR B CG2 1 
ATOM   18774 N  N   . VAL C 1 845  ? 72.122  -1.679  50.645  1.00 160.62 ? 845  VAL B N   1 
ATOM   18775 C  CA  . VAL C 1 845  ? 72.991  -0.678  49.998  1.00 162.99 ? 845  VAL B CA  1 
ATOM   18776 C  C   . VAL C 1 845  ? 72.242  0.465   49.311  1.00 158.87 ? 845  VAL B C   1 
ATOM   18777 O  O   . VAL C 1 845  ? 71.315  0.240   48.537  1.00 154.14 ? 845  VAL B O   1 
ATOM   18778 C  CB  . VAL C 1 845  ? 73.943  -1.300  48.969  1.00 130.16 ? 845  VAL B CB  1 
ATOM   18779 C  CG1 . VAL C 1 845  ? 73.195  -2.306  48.115  1.00 128.03 ? 845  VAL B CG1 1 
ATOM   18780 C  CG2 . VAL C 1 845  ? 74.583  -0.191  48.114  1.00 130.57 ? 845  VAL B CG2 1 
ATOM   18781 N  N   . TYR C 1 846  ? 72.671  1.693   49.563  1.00 212.65 ? 846  TYR B N   1 
ATOM   18782 C  CA  . TYR C 1 846  ? 71.866  2.830   49.153  1.00 209.95 ? 846  TYR B CA  1 
ATOM   18783 C  C   . TYR C 1 846  ? 72.280  3.496   47.852  1.00 216.11 ? 846  TYR B C   1 
ATOM   18784 O  O   . TYR C 1 846  ? 73.377  4.034   47.723  1.00 218.11 ? 846  TYR B O   1 
ATOM   18785 C  CB  . TYR C 1 846  ? 71.745  3.852   50.285  1.00 203.37 ? 846  TYR B CB  1 
ATOM   18786 C  CG  . TYR C 1 846  ? 70.758  3.434   51.353  1.00 195.64 ? 846  TYR B CG  1 
ATOM   18787 C  CD1 . TYR C 1 846  ? 70.958  3.763   52.688  1.00 194.62 ? 846  TYR B CD1 1 
ATOM   18788 C  CD2 . TYR C 1 846  ? 69.627  2.700   51.024  1.00 190.72 ? 846  TYR B CD2 1 
ATOM   18789 C  CE1 . TYR C 1 846  ? 70.052  3.380   53.669  1.00 190.99 ? 846  TYR B CE1 1 
ATOM   18790 C  CE2 . TYR C 1 846  ? 68.719  2.308   51.996  1.00 186.58 ? 846  TYR B CE2 1 
ATOM   18791 C  CZ  . TYR C 1 846  ? 68.934  2.650   53.317  1.00 186.69 ? 846  TYR B CZ  1 
ATOM   18792 O  OH  . TYR C 1 846  ? 68.022  2.258   54.276  1.00 184.06 ? 846  TYR B OH  1 
ATOM   18793 N  N   . ASN C 1 847  ? 71.365  3.443   46.891  1.00 196.54 ? 847  ASN B N   1 
ATOM   18794 C  CA  . ASN C 1 847  ? 71.488  4.195   45.653  1.00 203.46 ? 847  ASN B CA  1 
ATOM   18795 C  C   . ASN C 1 847  ? 70.706  5.489   45.757  1.00 203.33 ? 847  ASN B C   1 
ATOM   18796 O  O   . ASN C 1 847  ? 69.520  5.495   46.091  1.00 197.54 ? 847  ASN B O   1 
ATOM   18797 C  CB  . ASN C 1 847  ? 70.987  3.381   44.453  1.00 205.97 ? 847  ASN B CB  1 
ATOM   18798 C  CG  . ASN C 1 847  ? 71.336  4.027   43.119  1.00 210.78 ? 847  ASN B CG  1 
ATOM   18799 O  OD1 . ASN C 1 847  ? 71.252  5.246   42.961  1.00 211.62 ? 847  ASN B OD1 1 
ATOM   18800 N  ND2 . ASN C 1 847  ? 71.728  3.208   42.152  1.00 213.35 ? 847  ASN B ND2 1 
ATOM   18801 N  N   . TYR C 1 848  ? 71.381  6.587   45.456  1.00 235.30 ? 848  TYR B N   1 
ATOM   18802 C  CA  . TYR C 1 848  ? 70.730  7.877   45.410  1.00 236.69 ? 848  TYR B CA  1 
ATOM   18803 C  C   . TYR C 1 848  ? 71.208  8.660   44.193  1.00 239.39 ? 848  TYR B C   1 
ATOM   18804 O  O   . TYR C 1 848  ? 70.843  9.814   44.003  1.00 237.31 ? 848  TYR B O   1 
ATOM   18805 C  CB  . TYR C 1 848  ? 70.973  8.640   46.706  1.00 238.66 ? 848  TYR B CB  1 
ATOM   18806 C  CG  . TYR C 1 848  ? 70.100  8.176   47.851  1.00 236.66 ? 848  TYR B CG  1 
ATOM   18807 C  CD1 . TYR C 1 848  ? 68.883  7.547   47.616  1.00 232.64 ? 848  TYR B CD1 1 
ATOM   18808 C  CD2 . TYR C 1 848  ? 70.482  8.389   49.165  1.00 237.67 ? 848  TYR B CD2 1 
ATOM   18809 C  CE1 . TYR C 1 848  ? 68.083  7.130   48.659  1.00 231.03 ? 848  TYR B CE1 1 
ATOM   18810 C  CE2 . TYR C 1 848  ? 69.690  7.983   50.212  1.00 236.00 ? 848  TYR B CE2 1 
ATOM   18811 C  CZ  . TYR C 1 848  ? 68.494  7.354   49.955  1.00 233.77 ? 848  TYR B CZ  1 
ATOM   18812 O  OH  . TYR C 1 848  ? 67.712  6.952   51.007  1.00 234.87 ? 848  TYR B OH  1 
ATOM   18813 N  N   . ARG C 1 849  ? 72.032  8.020   43.372  1.00 219.53 ? 849  ARG B N   1 
ATOM   18814 C  CA  . ARG C 1 849  ? 72.371  8.552   42.061  1.00 222.74 ? 849  ARG B CA  1 
ATOM   18815 C  C   . ARG C 1 849  ? 71.125  8.400   41.169  1.00 219.01 ? 849  ARG B C   1 
ATOM   18816 O  O   . ARG C 1 849  ? 70.323  7.485   41.391  1.00 215.92 ? 849  ARG B O   1 
ATOM   18817 C  CB  . ARG C 1 849  ? 73.586  7.805   41.509  1.00 230.73 ? 849  ARG B CB  1 
ATOM   18818 C  CG  . ARG C 1 849  ? 74.017  8.202   40.124  1.00 236.70 ? 849  ARG B CG  1 
ATOM   18819 C  CD  . ARG C 1 849  ? 74.528  9.623   40.054  1.00 242.56 ? 849  ARG B CD  1 
ATOM   18820 N  NE  . ARG C 1 849  ? 74.764  9.998   38.662  1.00 246.84 ? 849  ARG B NE  1 
ATOM   18821 C  CZ  . ARG C 1 849  ? 74.635  11.229  38.175  1.00 248.05 ? 849  ARG B CZ  1 
ATOM   18822 N  NH1 . ARG C 1 849  ? 74.274  12.227  38.967  1.00 247.47 ? 849  ARG B NH1 1 
ATOM   18823 N  NH2 . ARG C 1 849  ? 74.869  11.466  36.889  1.00 248.79 ? 849  ARG B NH2 1 
ATOM   18824 N  N   . THR C 1 850  ? 70.954  9.302   40.189  1.00 210.75 ? 850  THR B N   1 
ATOM   18825 C  CA  . THR C 1 850  ? 69.718  9.407   39.371  1.00 206.15 ? 850  THR B CA  1 
ATOM   18826 C  C   . THR C 1 850  ? 69.387  8.140   38.592  1.00 206.41 ? 850  THR B C   1 
ATOM   18827 O  O   . THR C 1 850  ? 68.258  7.644   38.607  1.00 205.78 ? 850  THR B O   1 
ATOM   18828 C  CB  . THR C 1 850  ? 69.772  10.584  38.330  1.00 203.01 ? 850  THR B CB  1 
ATOM   18829 O  OG1 . THR C 1 850  ? 70.958  10.485  37.533  1.00 205.45 ? 850  THR B OG1 1 
ATOM   18830 C  CG2 . THR C 1 850  ? 69.732  11.951  39.008  1.00 201.33 ? 850  THR B CG2 1 
ATOM   18831 N  N   . SER C 1 851  ? 70.392  7.658   37.879  1.00 249.45 ? 851  SER B N   1 
ATOM   18832 C  CA  . SER C 1 851  ? 70.330  6.401   37.167  1.00 251.24 ? 851  SER B CA  1 
ATOM   18833 C  C   . SER C 1 851  ? 70.663  5.281   38.141  1.00 254.48 ? 851  SER B C   1 
ATOM   18834 O  O   . SER C 1 851  ? 71.172  5.543   39.229  1.00 253.50 ? 851  SER B O   1 
ATOM   18835 C  CB  . SER C 1 851  ? 71.379  6.426   36.069  1.00 255.84 ? 851  SER B CB  1 
ATOM   18836 O  OG  . SER C 1 851  ? 72.631  6.832   36.605  1.00 261.46 ? 851  SER B OG  1 
ATOM   18837 N  N   . GLY C 1 852  ? 70.394  4.037   37.751  1.00 162.40 ? 852  GLY B N   1 
ATOM   18838 C  CA  . GLY C 1 852  ? 70.798  2.885   38.546  1.00 163.77 ? 852  GLY B CA  1 
ATOM   18839 C  C   . GLY C 1 852  ? 72.300  2.622   38.540  1.00 163.17 ? 852  GLY B C   1 
ATOM   18840 O  O   . GLY C 1 852  ? 73.065  3.451   38.039  1.00 164.91 ? 852  GLY B O   1 
ATOM   18841 N  N   . MET C 1 853  ? 72.725  1.485   39.108  1.00 154.40 ? 853  MET B N   1 
ATOM   18842 C  CA  . MET C 1 853  ? 74.126  1.029   38.990  1.00 154.23 ? 853  MET B CA  1 
ATOM   18843 C  C   . MET C 1 853  ? 74.487  -0.380  39.481  1.00 152.44 ? 853  MET B C   1 
ATOM   18844 O  O   . MET C 1 853  ? 73.668  -1.127  40.011  1.00 149.33 ? 853  MET B O   1 
ATOM   18845 C  CB  . MET C 1 853  ? 75.114  2.043   39.580  1.00 157.22 ? 853  MET B CB  1 
ATOM   18846 C  CG  . MET C 1 853  ? 74.827  2.513   40.989  1.00 157.35 ? 853  MET B CG  1 
ATOM   18847 S  SD  . MET C 1 853  ? 75.761  4.027   41.281  1.00 185.35 ? 853  MET B SD  1 
ATOM   18848 C  CE  . MET C 1 853  ? 74.778  5.187   40.343  1.00 190.75 ? 853  MET B CE  1 
ATOM   18849 N  N   . GLN C 1 854  ? 75.743  -0.729  39.272  1.00 252.39 ? 854  GLN B N   1 
ATOM   18850 C  CA  . GLN C 1 854  ? 76.224  -2.032  39.659  1.00 253.50 ? 854  GLN B CA  1 
ATOM   18851 C  C   . GLN C 1 854  ? 77.084  -1.934  40.904  1.00 254.62 ? 854  GLN B C   1 
ATOM   18852 O  O   . GLN C 1 854  ? 77.868  -0.992  41.049  1.00 256.21 ? 854  GLN B O   1 
ATOM   18853 C  CB  . GLN C 1 854  ? 77.023  -2.638  38.523  1.00 257.38 ? 854  GLN B CB  1 
ATOM   18854 C  CG  . GLN C 1 854  ? 76.268  -2.651  37.216  1.00 255.10 ? 854  GLN B CG  1 
ATOM   18855 C  CD  . GLN C 1 854  ? 77.068  -3.304  36.118  1.00 258.70 ? 854  GLN B CD  1 
ATOM   18856 O  OE1 . GLN C 1 854  ? 78.241  -3.636  36.312  1.00 262.72 ? 854  GLN B OE1 1 
ATOM   18857 N  NE2 . GLN C 1 854  ? 76.445  -3.496  34.955  1.00 256.84 ? 854  GLN B NE2 1 
ATOM   18858 N  N   . PHE C 1 855  ? 76.936  -2.912  41.800  1.00 194.94 ? 855  PHE B N   1 
ATOM   18859 C  CA  . PHE C 1 855  ? 77.721  -2.963  43.039  1.00 194.72 ? 855  PHE B CA  1 
ATOM   18860 C  C   . PHE C 1 855  ? 78.394  -4.298  43.227  1.00 199.74 ? 855  PHE B C   1 
ATOM   18861 O  O   . PHE C 1 855  ? 78.475  -5.100  42.312  1.00 201.97 ? 855  PHE B O   1 
ATOM   18862 C  CB  . PHE C 1 855  ? 76.867  -2.660  44.270  1.00 187.63 ? 855  PHE B CB  1 
ATOM   18863 C  CG  . PHE C 1 855  ? 75.731  -3.637  44.504  1.00 180.22 ? 855  PHE B CG  1 
ATOM   18864 C  CD1 . PHE C 1 855  ? 75.980  -4.966  44.835  1.00 180.94 ? 855  PHE B CD1 1 
ATOM   18865 C  CD2 . PHE C 1 855  ? 74.403  -3.200  44.442  1.00 173.37 ? 855  PHE B CD2 1 
ATOM   18866 C  CE1 . PHE C 1 855  ? 74.930  -5.833  45.073  1.00 177.47 ? 855  PHE B CE1 1 
ATOM   18867 C  CE2 . PHE C 1 855  ? 73.344  -4.062  44.674  1.00 169.84 ? 855  PHE B CE2 1 
ATOM   18868 C  CZ  . PHE C 1 855  ? 73.601  -5.372  44.995  1.00 171.68 ? 855  PHE B CZ  1 
ATOM   18869 N  N   . CYS C 1 856  ? 78.856  -4.542  44.435  1.00 241.51 ? 856  CYS B N   1 
ATOM   18870 C  CA  . CYS C 1 856  ? 79.614  -5.739  44.673  1.00 246.39 ? 856  CYS B CA  1 
ATOM   18871 C  C   . CYS C 1 856  ? 79.976  -5.772  46.150  1.00 250.72 ? 856  CYS B C   1 
ATOM   18872 O  O   . CYS C 1 856  ? 81.069  -5.354  46.532  1.00 254.65 ? 856  CYS B O   1 
ATOM   18873 C  CB  . CYS C 1 856  ? 80.877  -5.707  43.805  1.00 250.46 ? 856  CYS B CB  1 
ATOM   18874 S  SG  . CYS C 1 856  ? 81.516  -7.309  43.241  1.00 292.81 ? 856  CYS B SG  1 
ATOM   18875 N  N   . VAL C 1 857  ? 79.050  -6.240  46.986  1.00 195.17 ? 857  VAL B N   1 
ATOM   18876 C  CA  . VAL C 1 857  ? 79.298  -6.309  48.427  1.00 196.26 ? 857  VAL B CA  1 
ATOM   18877 C  C   . VAL C 1 857  ? 79.939  -7.642  48.807  1.00 201.18 ? 857  VAL B C   1 
ATOM   18878 O  O   . VAL C 1 857  ? 79.437  -8.704  48.441  1.00 201.59 ? 857  VAL B O   1 
ATOM   18879 C  CB  . VAL C 1 857  ? 78.006  -6.084  49.245  1.00 189.89 ? 857  VAL B CB  1 
ATOM   18880 C  CG1 . VAL C 1 857  ? 77.537  -4.628  49.129  1.00 186.02 ? 857  VAL B CG1 1 
ATOM   18881 C  CG2 . VAL C 1 857  ? 76.920  -7.057  48.803  1.00 185.98 ? 857  VAL B CG2 1 
ATOM   18882 N  N   . LYS C 1 858  ? 81.056  -7.575  49.528  1.00 245.95 ? 858  LYS B N   1 
ATOM   18883 C  CA  . LYS C 1 858  ? 81.731  -8.775  50.015  1.00 251.30 ? 858  LYS B CA  1 
ATOM   18884 C  C   . LYS C 1 858  ? 82.193  -8.620  51.475  1.00 251.60 ? 858  LYS B C   1 
ATOM   18885 O  O   . LYS C 1 858  ? 82.763  -7.593  51.859  1.00 253.15 ? 858  LYS B O   1 
ATOM   18886 C  CB  . LYS C 1 858  ? 82.899  -9.164  49.093  1.00 260.47 ? 858  LYS B CB  1 
ATOM   18887 C  CG  . LYS C 1 858  ? 83.823  -8.012  48.718  1.00 267.34 ? 858  LYS B CG  1 
ATOM   18888 C  CD  . LYS C 1 858  ? 84.976  -8.465  47.831  1.00 276.03 ? 858  LYS B CD  1 
ATOM   18889 C  CE  . LYS C 1 858  ? 85.959  -7.328  47.614  1.00 281.46 ? 858  LYS B CE  1 
ATOM   18890 N  NZ  . LYS C 1 858  ? 87.059  -7.705  46.692  1.00 287.18 ? 858  LYS B NZ  1 
ATOM   18891 N  N   . MET C 1 859  ? 81.929  -9.640  52.288  1.00 257.72 ? 859  MET B N   1 
ATOM   18892 C  CA  . MET C 1 859  ? 82.279  -9.608  53.705  1.00 255.93 ? 859  MET B CA  1 
ATOM   18893 C  C   . MET C 1 859  ? 83.637  -10.243 53.966  1.00 260.85 ? 859  MET B C   1 
ATOM   18894 O  O   . MET C 1 859  ? 83.952  -11.309 53.438  1.00 263.13 ? 859  MET B O   1 
ATOM   18895 C  CB  . MET C 1 859  ? 81.202  -10.309 54.528  1.00 251.17 ? 859  MET B CB  1 
ATOM   18896 C  CG  . MET C 1 859  ? 81.731  -11.081 55.712  1.00 254.05 ? 859  MET B CG  1 
ATOM   18897 S  SD  . MET C 1 859  ? 80.484  -12.169 56.420  1.00 213.04 ? 859  MET B SD  1 
ATOM   18898 C  CE  . MET C 1 859  ? 79.396  -10.990 57.206  1.00 281.47 ? 859  MET B CE  1 
ATOM   18899 N  N   . SER C 1 860  ? 84.441  -9.582  54.787  1.00 321.65 ? 860  SER B N   1 
ATOM   18900 C  CA  . SER C 1 860  ? 85.765  -10.087 55.129  1.00 329.28 ? 860  SER B CA  1 
ATOM   18901 C  C   . SER C 1 860  ? 85.692  -11.248 56.117  1.00 332.20 ? 860  SER B C   1 
ATOM   18902 O  O   . SER C 1 860  ? 85.186  -11.091 57.225  1.00 331.71 ? 860  SER B O   1 
ATOM   18903 C  CB  . SER C 1 860  ? 86.618  -8.963  55.720  1.00 333.33 ? 860  SER B CB  1 
ATOM   18904 O  OG  . SER C 1 860  ? 87.656  -9.487  56.532  1.00 340.80 ? 860  SER B OG  1 
ATOM   18905 N  N   . ALA C 1 861  ? 86.209  -12.408 55.721  1.00 237.81 ? 861  ALA B N   1 
ATOM   18906 C  CA  . ALA C 1 861  ? 86.257  -13.565 56.612  1.00 238.28 ? 861  ALA B CA  1 
ATOM   18907 C  C   . ALA C 1 861  ? 87.257  -13.377 57.758  1.00 241.17 ? 861  ALA B C   1 
ATOM   18908 O  O   . ALA C 1 861  ? 88.464  -13.489 57.552  1.00 244.18 ? 861  ALA B O   1 
ATOM   18909 C  CB  . ALA C 1 861  ? 86.608  -14.806 55.825  1.00 240.61 ? 861  ALA B CB  1 
ATOM   18910 N  N   . VAL C 1 862  ? 86.756  -13.107 58.962  1.00 286.90 ? 862  VAL B N   1 
ATOM   18911 C  CA  . VAL C 1 862  ? 87.614  -12.968 60.143  1.00 291.96 ? 862  VAL B CA  1 
ATOM   18912 C  C   . VAL C 1 862  ? 87.798  -14.292 60.914  1.00 294.59 ? 862  VAL B C   1 
ATOM   18913 O  O   . VAL C 1 862  ? 86.831  -14.889 61.396  1.00 293.24 ? 862  VAL B O   1 
ATOM   18914 C  CB  . VAL C 1 862  ? 87.102  -11.847 61.094  1.00 290.75 ? 862  VAL B CB  1 
ATOM   18915 C  CG1 . VAL C 1 862  ? 87.936  -11.791 62.370  1.00 296.35 ? 862  VAL B CG1 1 
ATOM   18916 C  CG2 . VAL C 1 862  ? 87.108  -10.494 60.383  1.00 287.70 ? 862  VAL B CG2 1 
ATOM   18917 N  N   . GLU C 1 863  ? 89.052  -14.732 61.011  1.00 271.82 ? 863  GLU B N   1 
ATOM   18918 C  CA  . GLU C 1 863  ? 89.440  -15.947 61.740  1.00 273.41 ? 863  GLU B CA  1 
ATOM   18919 C  C   . GLU C 1 863  ? 88.293  -16.884 62.128  1.00 265.91 ? 863  GLU B C   1 
ATOM   18920 O  O   . GLU C 1 863  ? 87.945  -17.809 61.396  1.00 263.16 ? 863  GLU B O   1 
ATOM   18921 C  CB  . GLU C 1 863  ? 90.245  -15.591 63.005  1.00 284.31 ? 863  GLU B CB  1 
ATOM   18922 C  CG  . GLU C 1 863  ? 91.776  -15.563 62.849  1.00 301.83 ? 863  GLU B CG  1 
ATOM   18923 C  CD  . GLU C 1 863  ? 92.403  -16.954 62.776  1.00 311.31 ? 863  GLU B CD  1 
ATOM   18924 O  OE1 . GLU C 1 863  ? 91.831  -17.844 62.109  1.00 309.60 ? 863  GLU B OE1 1 
ATOM   18925 O  OE2 . GLU C 1 863  ? 93.478  -17.155 63.383  1.00 318.53 ? 863  GLU B OE2 1 
ATOM   18926 N  N   . GLY C 1 864  ? 87.727  -16.633 63.301  1.00 224.16 ? 864  GLY B N   1 
ATOM   18927 C  CA  . GLY C 1 864  ? 86.879  -17.599 63.963  1.00 222.32 ? 864  GLY B CA  1 
ATOM   18928 C  C   . GLY C 1 864  ? 85.429  -17.563 63.562  1.00 212.70 ? 864  GLY B C   1 
ATOM   18929 O  O   . GLY C 1 864  ? 84.616  -18.328 64.070  1.00 211.89 ? 864  GLY B O   1 
ATOM   18930 N  N   . ILE C 1 865  ? 85.085  -16.662 62.662  1.00 227.75 ? 865  ILE B N   1 
ATOM   18931 C  CA  . ILE C 1 865  ? 83.733  -16.667 62.149  1.00 218.05 ? 865  ILE B CA  1 
ATOM   18932 C  C   . ILE C 1 865  ? 83.632  -17.613 60.942  1.00 218.10 ? 865  ILE B C   1 
ATOM   18933 O  O   . ILE C 1 865  ? 84.605  -17.797 60.205  1.00 220.01 ? 865  ILE B O   1 
ATOM   18934 C  CB  . ILE C 1 865  ? 83.273  -15.252 61.817  1.00 210.29 ? 865  ILE B CB  1 
ATOM   18935 C  CG1 . ILE C 1 865  ? 83.959  -14.260 62.756  1.00 210.79 ? 865  ILE B CG1 1 
ATOM   18936 C  CG2 . ILE C 1 865  ? 81.766  -15.154 61.941  1.00 203.60 ? 865  ILE B CG2 1 
ATOM   18937 C  CD1 . ILE C 1 865  ? 83.398  -12.861 62.682  1.00 205.94 ? 865  ILE B CD1 1 
ATOM   18938 N  N   . CYS C 1 866  ? 82.463  -18.232 60.775  1.00 229.74 ? 866  CYS B N   1 
ATOM   18939 C  CA  . CYS C 1 866  ? 82.215  -19.194 59.703  1.00 234.56 ? 866  CYS B CA  1 
ATOM   18940 C  C   . CYS C 1 866  ? 81.552  -18.546 58.507  1.00 238.10 ? 866  CYS B C   1 
ATOM   18941 O  O   . CYS C 1 866  ? 80.873  -17.534 58.644  1.00 230.38 ? 866  CYS B O   1 
ATOM   18942 C  CB  . CYS C 1 866  ? 81.320  -20.317 60.204  1.00 231.75 ? 866  CYS B CB  1 
ATOM   18943 S  SG  . CYS C 1 866  ? 82.170  -21.869 60.387  1.00 241.21 ? 866  CYS B SG  1 
ATOM   18944 N  N   . THR C 1 867  ? 81.735  -19.139 57.334  1.00 278.67 ? 867  THR B N   1 
ATOM   18945 C  CA  . THR C 1 867  ? 81.120  -18.595 56.134  1.00 284.99 ? 867  THR B CA  1 
ATOM   18946 C  C   . THR C 1 867  ? 81.169  -19.549 54.957  1.00 297.90 ? 867  THR B C   1 
ATOM   18947 O  O   . THR C 1 867  ? 81.577  -20.705 55.081  1.00 302.00 ? 867  THR B O   1 
ATOM   18948 C  CB  . THR C 1 867  ? 81.753  -17.251 55.719  1.00 273.65 ? 867  THR B CB  1 
ATOM   18949 O  OG1 . THR C 1 867  ? 82.813  -16.922 56.624  1.00 277.56 ? 867  THR B OG1 1 
ATOM   18950 C  CG2 . THR C 1 867  ? 80.713  -16.140 55.744  1.00 267.06 ? 867  THR B CG2 1 
ATOM   18951 N  N   . SER C 1 868  ? 80.748  -19.039 53.808  1.00 256.31 ? 868  SER B N   1 
ATOM   18952 C  CA  . SER C 1 868  ? 80.518  -19.869 52.640  1.00 269.16 ? 868  SER B CA  1 
ATOM   18953 C  C   . SER C 1 868  ? 81.617  -19.744 51.571  1.00 286.06 ? 868  SER B C   1 
ATOM   18954 O  O   . SER C 1 868  ? 81.725  -20.595 50.685  1.00 287.23 ? 868  SER B O   1 
ATOM   18955 C  CB  . SER C 1 868  ? 79.134  -19.554 52.074  1.00 263.56 ? 868  SER B CB  1 
ATOM   18956 O  OG  . SER C 1 868  ? 78.174  -19.537 53.122  1.00 261.09 ? 868  SER B OG  1 
ATOM   18957 N  N   . GLU C 1 869  ? 82.423  -18.686 51.659  1.00 319.96 ? 869  GLU B N   1 
ATOM   18958 C  CA  . GLU C 1 869  ? 83.624  -18.545 50.830  1.00 336.30 ? 869  GLU B CA  1 
ATOM   18959 C  C   . GLU C 1 869  ? 84.716  -19.454 51.411  1.00 345.55 ? 869  GLU B C   1 
ATOM   18960 O  O   . GLU C 1 869  ? 84.711  -19.729 52.612  1.00 346.41 ? 869  GLU B O   1 
ATOM   18961 C  CB  . GLU C 1 869  ? 84.077  -17.076 50.804  1.00 337.93 ? 869  GLU B CB  1 
ATOM   18962 C  CG  . GLU C 1 869  ? 85.103  -16.712 49.730  1.00 342.17 ? 869  GLU B CG  1 
ATOM   18963 C  CD  . GLU C 1 869  ? 86.532  -16.754 50.237  1.00 346.85 ? 869  GLU B CD  1 
ATOM   18964 O  OE1 . GLU C 1 869  ? 86.726  -16.910 51.458  1.00 347.63 ? 869  GLU B OE1 1 
ATOM   18965 O  OE2 . GLU C 1 869  ? 87.463  -16.628 49.416  1.00 348.05 ? 869  GLU B OE2 1 
ATOM   18966 N  N   . SER C 1 870  ? 85.637  -19.934 50.574  1.00 270.79 ? 870  SER B N   1 
ATOM   18967 C  CA  . SER C 1 870  ? 86.680  -20.856 51.042  1.00 281.24 ? 870  SER B CA  1 
ATOM   18968 C  C   . SER C 1 870  ? 87.585  -20.199 52.081  1.00 286.34 ? 870  SER B C   1 
ATOM   18969 O  O   . SER C 1 870  ? 88.200  -19.162 51.824  1.00 288.06 ? 870  SER B O   1 
ATOM   18970 C  CB  . SER C 1 870  ? 87.515  -21.412 49.879  1.00 287.63 ? 870  SER B CB  1 
ATOM   18971 O  OG  . SER C 1 870  ? 88.587  -20.549 49.542  1.00 291.62 ? 870  SER B OG  1 
ATOM   18972 N  N   . LYS C 1 882  ? 83.864  -12.937 48.395  1.00 279.61 ? 882  LYS B N   1 
ATOM   18973 C  CA  . LYS C 1 882  ? 83.589  -13.189 46.978  1.00 279.58 ? 882  LYS B CA  1 
ATOM   18974 C  C   . LYS C 1 882  ? 82.810  -12.043 46.312  1.00 271.90 ? 882  LYS B C   1 
ATOM   18975 O  O   . LYS C 1 882  ? 82.104  -11.297 46.988  1.00 267.51 ? 882  LYS B O   1 
ATOM   18976 C  CB  . LYS C 1 882  ? 82.850  -14.524 46.798  1.00 280.62 ? 882  LYS B CB  1 
ATOM   18977 C  CG  . LYS C 1 882  ? 81.421  -14.550 47.329  1.00 276.80 ? 882  LYS B CG  1 
ATOM   18978 C  CD  . LYS C 1 882  ? 80.804  -15.941 47.207  1.00 277.59 ? 882  LYS B CD  1 
ATOM   18979 C  CE  . LYS C 1 882  ? 81.585  -16.967 48.021  1.00 283.41 ? 882  LYS B CE  1 
ATOM   18980 N  NZ  . LYS C 1 882  ? 81.083  -18.361 47.844  1.00 283.14 ? 882  LYS B NZ  1 
ATOM   18981 N  N   . CYS C 1 883  ? 82.942  -11.909 44.990  1.00 281.45 ? 883  CYS B N   1 
ATOM   18982 C  CA  . CYS C 1 883  ? 82.299  -10.818 44.244  1.00 275.08 ? 883  CYS B CA  1 
ATOM   18983 C  C   . CYS C 1 883  ? 81.006  -11.235 43.533  1.00 267.37 ? 883  CYS B C   1 
ATOM   18984 O  O   . CYS C 1 883  ? 81.029  -11.655 42.374  1.00 267.97 ? 883  CYS B O   1 
ATOM   18985 C  CB  . CYS C 1 883  ? 83.275  -10.211 43.226  1.00 277.99 ? 883  CYS B CB  1 
ATOM   18986 S  SG  . CYS C 1 883  ? 82.665  -8.736  42.353  1.00 327.10 ? 883  CYS B SG  1 
ATOM   18987 N  N   . VAL C 1 884  ? 79.883  -11.100 44.230  1.00 277.53 ? 884  VAL B N   1 
ATOM   18988 C  CA  . VAL C 1 884  ? 78.571  -11.418 43.675  1.00 271.21 ? 884  VAL B CA  1 
ATOM   18989 C  C   . VAL C 1 884  ? 77.870  -10.165 43.146  1.00 268.18 ? 884  VAL B C   1 
ATOM   18990 O  O   . VAL C 1 884  ? 76.879  -9.713  43.726  1.00 264.15 ? 884  VAL B O   1 
ATOM   18991 C  CB  . VAL C 1 884  ? 77.682  -12.065 44.747  1.00 233.33 ? 884  VAL B CB  1 
ATOM   18992 C  CG1 . VAL C 1 884  ? 78.115  -13.495 45.001  1.00 236.76 ? 884  VAL B CG1 1 
ATOM   18993 C  CG2 . VAL C 1 884  ? 77.755  -11.263 46.036  1.00 233.07 ? 884  VAL B CG2 1 
ATOM   18994 N  N   . ARG C 1 885  ? 78.372  -9.610  42.042  1.00 265.63 ? 885  ARG B N   1 
ATOM   18995 C  CA  . ARG C 1 885  ? 77.892  -8.303  41.580  1.00 261.52 ? 885  ARG B CA  1 
ATOM   18996 C  C   . ARG C 1 885  ? 76.409  -8.275  41.253  1.00 254.83 ? 885  ARG B C   1 
ATOM   18997 O  O   . ARG C 1 885  ? 75.882  -9.161  40.591  1.00 253.37 ? 885  ARG B O   1 
ATOM   18998 C  CB  . ARG C 1 885  ? 78.746  -7.698  40.439  1.00 263.73 ? 885  ARG B CB  1 
ATOM   18999 C  CG  . ARG C 1 885  ? 78.794  -8.451  39.108  1.00 264.53 ? 885  ARG B CG  1 
ATOM   19000 C  CD  . ARG C 1 885  ? 79.492  -7.609  38.001  1.00 266.32 ? 885  ARG B CD  1 
ATOM   19001 N  NE  . ARG C 1 885  ? 80.782  -7.056  38.426  1.00 271.15 ? 885  ARG B NE  1 
ATOM   19002 C  CZ  . ARG C 1 885  ? 81.535  -6.222  37.707  1.00 273.84 ? 885  ARG B CZ  1 
ATOM   19003 N  NH1 . ARG C 1 885  ? 81.142  -5.829  36.505  1.00 272.32 ? 885  ARG B NH1 1 
ATOM   19004 N  NH2 . ARG C 1 885  ? 82.688  -5.778  38.196  1.00 277.84 ? 885  ARG B NH2 1 
ATOM   19005 N  N   . GLN C 1 886  ? 75.751  -7.232  41.739  1.00 225.79 ? 886  GLN B N   1 
ATOM   19006 C  CA  . GLN C 1 886  ? 74.316  -7.082  41.590  1.00 222.22 ? 886  GLN B CA  1 
ATOM   19007 C  C   . GLN C 1 886  ? 74.017  -5.700  40.987  1.00 215.27 ? 886  GLN B C   1 
ATOM   19008 O  O   . GLN C 1 886  ? 74.933  -4.942  40.659  1.00 217.64 ? 886  GLN B O   1 
ATOM   19009 C  CB  . GLN C 1 886  ? 73.657  -7.243  42.956  1.00 226.69 ? 886  GLN B CB  1 
ATOM   19010 C  CG  . GLN C 1 886  ? 72.201  -7.603  42.960  1.00 229.06 ? 886  GLN B CG  1 
ATOM   19011 C  CD  . GLN C 1 886  ? 72.002  -9.080  43.119  1.00 235.03 ? 886  GLN B CD  1 
ATOM   19012 O  OE1 . GLN C 1 886  ? 70.881  -9.546  43.293  1.00 235.03 ? 886  GLN B OE1 1 
ATOM   19013 N  NE2 . GLN C 1 886  ? 73.096  -9.834  43.068  1.00 239.68 ? 886  GLN B NE2 1 
ATOM   19014 N  N   . LYS C 1 887  ? 72.739  -5.373  40.832  1.00 236.65 ? 887  LYS B N   1 
ATOM   19015 C  CA  . LYS C 1 887  ? 72.360  -4.142  40.156  1.00 232.35 ? 887  LYS B CA  1 
ATOM   19016 C  C   . LYS C 1 887  ? 71.278  -3.428  40.944  1.00 225.46 ? 887  LYS B C   1 
ATOM   19017 O  O   . LYS C 1 887  ? 70.293  -4.031  41.376  1.00 219.85 ? 887  LYS B O   1 
ATOM   19018 C  CB  . LYS C 1 887  ? 71.871  -4.434  38.731  1.00 231.78 ? 887  LYS B CB  1 
ATOM   19019 C  CG  . LYS C 1 887  ? 72.636  -5.539  37.982  1.00 236.31 ? 887  LYS B CG  1 
ATOM   19020 C  CD  . LYS C 1 887  ? 72.012  -6.924  38.218  1.00 236.90 ? 887  LYS B CD  1 
ATOM   19021 C  CE  . LYS C 1 887  ? 72.728  -8.044  37.459  1.00 240.59 ? 887  LYS B CE  1 
ATOM   19022 N  NZ  . LYS C 1 887  ? 72.218  -8.252  36.075  1.00 238.74 ? 887  LYS B NZ  1 
ATOM   19023 N  N   . VAL C 1 888  ? 71.471  -2.134  41.130  1.00 200.10 ? 888  VAL B N   1 
ATOM   19024 C  CA  . VAL C 1 888  ? 70.529  -1.346  41.892  1.00 196.54 ? 888  VAL B CA  1 
ATOM   19025 C  C   . VAL C 1 888  ? 69.748  -0.426  40.993  1.00 196.52 ? 888  VAL B C   1 
ATOM   19026 O  O   . VAL C 1 888  ? 70.327  0.404   40.298  1.00 200.25 ? 888  VAL B O   1 
ATOM   19027 C  CB  . VAL C 1 888  ? 71.255  -0.471  42.905  1.00 194.20 ? 888  VAL B CB  1 
ATOM   19028 C  CG1 . VAL C 1 888  ? 71.629  -1.296  44.119  1.00 194.76 ? 888  VAL B CG1 1 
ATOM   19029 C  CG2 . VAL C 1 888  ? 72.485  0.156   42.260  1.00 195.77 ? 888  VAL B CG2 1 
ATOM   19030 N  N   . GLU C 1 889  ? 68.429  -0.563  41.008  1.00 201.89 ? 889  GLU B N   1 
ATOM   19031 C  CA  . GLU C 1 889  ? 67.594  0.399   40.315  1.00 203.86 ? 889  GLU B CA  1 
ATOM   19032 C  C   . GLU C 1 889  ? 67.867  1.760   40.940  1.00 200.60 ? 889  GLU B C   1 
ATOM   19033 O  O   . GLU C 1 889  ? 68.072  1.869   42.154  1.00 197.64 ? 889  GLU B O   1 
ATOM   19034 C  CB  . GLU C 1 889  ? 66.112  0.024   40.399  1.00 211.47 ? 889  GLU B CB  1 
ATOM   19035 C  CG  . GLU C 1 889  ? 65.610  -0.310  41.793  1.00 222.16 ? 889  GLU B CG  1 
ATOM   19036 C  CD  . GLU C 1 889  ? 65.994  -1.706  42.245  1.00 233.63 ? 889  GLU B CD  1 
ATOM   19037 O  OE1 . GLU C 1 889  ? 66.624  -2.450  41.462  1.00 238.97 ? 889  GLU B OE1 1 
ATOM   19038 O  OE2 . GLU C 1 889  ? 65.658  -2.064  43.390  1.00 236.36 ? 889  GLU B OE2 1 
ATOM   19039 N  N   . GLY C 1 890  ? 67.888  2.791   40.104  1.00 242.60 ? 890  GLY B N   1 
ATOM   19040 C  CA  . GLY C 1 890  ? 68.296  4.115   40.532  1.00 239.77 ? 890  GLY B CA  1 
ATOM   19041 C  C   . GLY C 1 890  ? 67.492  4.697   41.674  1.00 229.53 ? 890  GLY B C   1 
ATOM   19042 O  O   . GLY C 1 890  ? 66.278  4.531   41.745  1.00 225.78 ? 890  GLY B O   1 
ATOM   19043 N  N   . SER C 1 891  ? 68.171  5.384   42.581  1.00 240.66 ? 891  SER B N   1 
ATOM   19044 C  CA  . SER C 1 891  ? 67.457  6.110   43.607  1.00 233.47 ? 891  SER B CA  1 
ATOM   19045 C  C   . SER C 1 891  ? 66.584  5.161   44.422  1.00 230.39 ? 891  SER B C   1 
ATOM   19046 O  O   . SER C 1 891  ? 65.390  5.402   44.591  1.00 228.33 ? 891  SER B O   1 
ATOM   19047 C  CB  . SER C 1 891  ? 66.570  7.161   42.943  1.00 227.34 ? 891  SER B CB  1 
ATOM   19048 O  OG  . SER C 1 891  ? 67.045  7.472   41.646  1.00 228.86 ? 891  SER B OG  1 
ATOM   19049 N  N   . SER C 1 892  ? 67.174  4.077   44.912  1.00 198.49 ? 892  SER B N   1 
ATOM   19050 C  CA  . SER C 1 892  ? 66.453  3.146   45.777  1.00 196.11 ? 892  SER B CA  1 
ATOM   19051 C  C   . SER C 1 892  ? 67.414  2.309   46.609  1.00 198.89 ? 892  SER B C   1 
ATOM   19052 O  O   . SER C 1 892  ? 68.379  2.834   47.170  1.00 199.19 ? 892  SER B O   1 
ATOM   19053 C  CB  . SER C 1 892  ? 65.513  2.246   44.968  1.00 194.33 ? 892  SER B CB  1 
ATOM   19054 O  OG  . SER C 1 892  ? 64.384  2.967   44.498  1.00 191.14 ? 892  SER B OG  1 
ATOM   19055 N  N   . SER C 1 893  ? 67.152  1.009   46.694  1.00 170.82 ? 893  SER B N   1 
ATOM   19056 C  CA  . SER C 1 893  ? 68.014  0.142   47.485  1.00 174.46 ? 893  SER B CA  1 
ATOM   19057 C  C   . SER C 1 893  ? 67.812  -1.363  47.255  1.00 176.91 ? 893  SER B C   1 
ATOM   19058 O  O   . SER C 1 893  ? 66.692  -1.854  47.192  1.00 175.14 ? 893  SER B O   1 
ATOM   19059 C  CB  . SER C 1 893  ? 67.864  0.468   48.969  1.00 173.48 ? 893  SER B CB  1 
ATOM   19060 O  OG  . SER C 1 893  ? 68.977  -0.018  49.692  1.00 175.86 ? 893  SER B OG  1 
ATOM   19061 N  N   . HIS C 1 894  ? 68.919  -2.090  47.133  1.00 159.65 ? 894  HIS B N   1 
ATOM   19062 C  CA  . HIS C 1 894  ? 68.891  -3.544  47.000  1.00 170.29 ? 894  HIS B CA  1 
ATOM   19063 C  C   . HIS C 1 894  ? 69.374  -4.178  48.304  1.00 156.41 ? 894  HIS B C   1 
ATOM   19064 O  O   . HIS C 1 894  ? 70.554  -4.090  48.667  1.00 156.87 ? 894  HIS B O   1 
ATOM   19065 C  CB  . HIS C 1 894  ? 69.753  -4.006  45.816  1.00 210.31 ? 894  HIS B CB  1 
ATOM   19066 C  CG  . HIS C 1 894  ? 69.154  -5.135  45.039  1.00 257.47 ? 894  HIS B CG  1 
ATOM   19067 N  ND1 . HIS C 1 894  ? 69.802  -6.336  44.848  1.00 287.05 ? 894  HIS B ND1 1 
ATOM   19068 C  CD2 . HIS C 1 894  ? 67.960  -5.248  44.414  1.00 275.11 ? 894  HIS B CD2 1 
ATOM   19069 C  CE1 . HIS C 1 894  ? 69.034  -7.136  44.133  1.00 308.29 ? 894  HIS B CE1 1 
ATOM   19070 N  NE2 . HIS C 1 894  ? 67.910  -6.500  43.858  1.00 292.84 ? 894  HIS B NE2 1 
ATOM   19071 N  N   . LEU C 1 895  ? 68.440  -4.792  49.020  1.00 223.81 ? 895  LEU B N   1 
ATOM   19072 C  CA  . LEU C 1 895  ? 68.758  -5.499  50.246  1.00 219.85 ? 895  LEU B CA  1 
ATOM   19073 C  C   . LEU C 1 895  ? 69.985  -6.355  50.028  1.00 214.55 ? 895  LEU B C   1 
ATOM   19074 O  O   . LEU C 1 895  ? 70.298  -6.719  48.903  1.00 215.16 ? 895  LEU B O   1 
ATOM   19075 C  CB  . LEU C 1 895  ? 67.592  -6.392  50.628  1.00 220.70 ? 895  LEU B CB  1 
ATOM   19076 C  CG  . LEU C 1 895  ? 66.791  -5.912  51.823  1.00 221.59 ? 895  LEU B CG  1 
ATOM   19077 C  CD1 . LEU C 1 895  ? 65.317  -6.160  51.588  1.00 218.79 ? 895  LEU B CD1 1 
ATOM   19078 C  CD2 . LEU C 1 895  ? 67.286  -6.634  53.061  1.00 224.27 ? 895  LEU B CD2 1 
ATOM   19079 N  N   . VAL C 1 896  ? 70.685  -6.681  51.101  1.00 175.69 ? 896  VAL B N   1 
ATOM   19080 C  CA  . VAL C 1 896  ? 71.828  -7.573  50.999  1.00 171.07 ? 896  VAL B CA  1 
ATOM   19081 C  C   . VAL C 1 896  ? 71.676  -8.643  52.062  1.00 170.67 ? 896  VAL B C   1 
ATOM   19082 O  O   . VAL C 1 896  ? 70.779  -8.554  52.899  1.00 169.46 ? 896  VAL B O   1 
ATOM   19083 C  CB  . VAL C 1 896  ? 73.167  -6.821  51.219  1.00 169.11 ? 896  VAL B CB  1 
ATOM   19084 C  CG1 . VAL C 1 896  ? 74.344  -7.700  50.797  1.00 172.93 ? 896  VAL B CG1 1 
ATOM   19085 C  CG2 . VAL C 1 896  ? 73.184  -5.478  50.473  1.00 164.50 ? 896  VAL B CG2 1 
ATOM   19086 N  N   . THR C 1 897  ? 72.521  -9.668  52.019  1.00 201.04 ? 897  THR B N   1 
ATOM   19087 C  CA  . THR C 1 897  ? 72.619  -10.603 53.138  1.00 199.52 ? 897  THR B CA  1 
ATOM   19088 C  C   . THR C 1 897  ? 73.866  -11.487 53.089  1.00 205.09 ? 897  THR B C   1 
ATOM   19089 O  O   . THR C 1 897  ? 74.437  -11.729 52.026  1.00 207.27 ? 897  THR B O   1 
ATOM   19090 C  CB  . THR C 1 897  ? 71.379  -11.534 53.290  1.00 194.01 ? 897  THR B CB  1 
ATOM   19091 O  OG1 . THR C 1 897  ? 71.733  -12.865 52.889  1.00 196.78 ? 897  THR B OG1 1 
ATOM   19092 C  CG2 . THR C 1 897  ? 70.172  -11.044 52.484  1.00 188.69 ? 897  THR B CG2 1 
ATOM   19093 N  N   . PHE C 1 898  ? 74.266  -11.952 54.271  1.00 196.39 ? 898  PHE B N   1 
ATOM   19094 C  CA  . PHE C 1 898  ? 75.366  -12.888 54.472  1.00 199.86 ? 898  PHE B CA  1 
ATOM   19095 C  C   . PHE C 1 898  ? 75.060  -13.663 55.744  1.00 200.22 ? 898  PHE B C   1 
ATOM   19096 O  O   . PHE C 1 898  ? 74.716  -13.069 56.772  1.00 197.17 ? 898  PHE B O   1 
ATOM   19097 C  CB  . PHE C 1 898  ? 76.683  -12.153 54.724  1.00 203.03 ? 898  PHE B CB  1 
ATOM   19098 C  CG  . PHE C 1 898  ? 77.164  -11.330 53.575  1.00 201.73 ? 898  PHE B CG  1 
ATOM   19099 C  CD1 . PHE C 1 898  ? 78.359  -11.640 52.952  1.00 204.89 ? 898  PHE B CD1 1 
ATOM   19100 C  CD2 . PHE C 1 898  ? 76.443  -10.229 53.141  1.00 197.49 ? 898  PHE B CD2 1 
ATOM   19101 C  CE1 . PHE C 1 898  ? 78.816  -10.881 51.908  1.00 205.20 ? 898  PHE B CE1 1 
ATOM   19102 C  CE2 . PHE C 1 898  ? 76.884  -9.472  52.092  1.00 197.49 ? 898  PHE B CE2 1 
ATOM   19103 C  CZ  . PHE C 1 898  ? 78.074  -9.791  51.472  1.00 201.61 ? 898  PHE B CZ  1 
ATOM   19104 N  N   . THR C 1 899  ? 75.212  -14.977 55.708  1.00 171.00 ? 899  THR B N   1 
ATOM   19105 C  CA  . THR C 1 899  ? 75.061  -15.743 56.936  1.00 170.03 ? 899  THR B CA  1 
ATOM   19106 C  C   . THR C 1 899  ? 76.406  -16.234 57.468  1.00 172.08 ? 899  THR B C   1 
ATOM   19107 O  O   . THR C 1 899  ? 77.303  -16.592 56.694  1.00 173.41 ? 899  THR B O   1 
ATOM   19108 C  CB  . THR C 1 899  ? 74.105  -16.914 56.761  1.00 171.00 ? 899  THR B CB  1 
ATOM   19109 O  OG1 . THR C 1 899  ? 74.657  -17.838 55.815  1.00 175.10 ? 899  THR B OG1 1 
ATOM   19110 C  CG2 . THR C 1 899  ? 72.765  -16.406 56.263  1.00 161.78 ? 899  THR B CG2 1 
ATOM   19111 N  N   . VAL C 1 900  ? 76.525  -16.228 58.799  1.00 198.59 ? 900  VAL B N   1 
ATOM   19112 C  CA  . VAL C 1 900  ? 77.742  -16.602 59.516  1.00 202.65 ? 900  VAL B CA  1 
ATOM   19113 C  C   . VAL C 1 900  ? 77.391  -17.326 60.812  1.00 201.08 ? 900  VAL B C   1 
ATOM   19114 O  O   . VAL C 1 900  ? 76.228  -17.396 61.222  1.00 197.60 ? 900  VAL B O   1 
ATOM   19115 C  CB  . VAL C 1 900  ? 78.607  -15.365 59.873  1.00 187.79 ? 900  VAL B CB  1 
ATOM   19116 C  CG1 . VAL C 1 900  ? 79.621  -15.062 58.786  1.00 190.80 ? 900  VAL B CG1 1 
ATOM   19117 C  CG2 . VAL C 1 900  ? 77.732  -14.160 60.132  1.00 183.15 ? 900  VAL B CG2 1 
ATOM   19118 N  N   . LEU C 1 901  ? 78.419  -17.852 61.459  1.00 177.51 ? 901  LEU B N   1 
ATOM   19119 C  CA  . LEU C 1 901  ? 78.255  -18.601 62.697  1.00 184.11 ? 901  LEU B CA  1 
ATOM   19120 C  C   . LEU C 1 901  ? 79.591  -18.684 63.449  1.00 194.77 ? 901  LEU B C   1 
ATOM   19121 O  O   . LEU C 1 901  ? 80.498  -19.394 63.024  1.00 201.32 ? 901  LEU B O   1 
ATOM   19122 C  CB  . LEU C 1 901  ? 77.701  -19.990 62.378  1.00 182.10 ? 901  LEU B CB  1 
ATOM   19123 C  CG  . LEU C 1 901  ? 77.871  -21.139 63.372  1.00 186.17 ? 901  LEU B CG  1 
ATOM   19124 C  CD1 . LEU C 1 901  ? 76.550  -21.851 63.589  1.00 181.62 ? 901  LEU B CD1 1 
ATOM   19125 C  CD2 . LEU C 1 901  ? 78.940  -22.114 62.885  1.00 191.73 ? 901  LEU B CD2 1 
ATOM   19126 N  N   . PRO C 1 902  ? 79.717  -17.934 64.559  1.00 177.18 ? 902  PRO B N   1 
ATOM   19127 C  CA  . PRO C 1 902  ? 80.939  -17.814 65.357  1.00 183.41 ? 902  PRO B CA  1 
ATOM   19128 C  C   . PRO C 1 902  ? 81.111  -18.930 66.381  1.00 189.85 ? 902  PRO B C   1 
ATOM   19129 O  O   . PRO C 1 902  ? 80.129  -19.470 66.900  1.00 187.48 ? 902  PRO B O   1 
ATOM   19130 C  CB  . PRO C 1 902  ? 80.743  -16.488 66.105  1.00 182.74 ? 902  PRO B CB  1 
ATOM   19131 C  CG  . PRO C 1 902  ? 79.442  -15.912 65.627  1.00 169.81 ? 902  PRO B CG  1 
ATOM   19132 C  CD  . PRO C 1 902  ? 78.663  -17.053 65.073  1.00 168.88 ? 902  PRO B CD  1 
ATOM   19133 N  N   . LEU C 1 903  ? 82.370  -19.248 66.672  1.00 217.31 ? 903  LEU B N   1 
ATOM   19134 C  CA  . LEU C 1 903  ? 82.737  -20.230 67.684  1.00 223.83 ? 903  LEU B CA  1 
ATOM   19135 C  C   . LEU C 1 903  ? 83.597  -19.530 68.716  1.00 229.44 ? 903  LEU B C   1 
ATOM   19136 O  O   . LEU C 1 903  ? 83.858  -20.060 69.804  1.00 233.72 ? 903  LEU B O   1 
ATOM   19137 C  CB  . LEU C 1 903  ? 83.543  -21.362 67.060  1.00 227.20 ? 903  LEU B CB  1 
ATOM   19138 C  CG  . LEU C 1 903  ? 82.999  -21.874 65.734  1.00 223.85 ? 903  LEU B CG  1 
ATOM   19139 C  CD1 . LEU C 1 903  ? 81.497  -22.005 65.859  1.00 217.64 ? 903  LEU B CD1 1 
ATOM   19140 C  CD2 . LEU C 1 903  ? 83.374  -20.936 64.597  1.00 221.84 ? 903  LEU B CD2 1 
ATOM   19141 N  N   . GLU C 1 904  ? 84.050  -18.337 68.346  1.00 229.76 ? 904  GLU B N   1 
ATOM   19142 C  CA  . GLU C 1 904  ? 84.855  -17.514 69.227  1.00 237.79 ? 904  GLU B CA  1 
ATOM   19143 C  C   . GLU C 1 904  ? 84.002  -16.443 69.894  1.00 231.23 ? 904  GLU B C   1 
ATOM   19144 O  O   . GLU C 1 904  ? 83.549  -15.491 69.251  1.00 225.02 ? 904  GLU B O   1 
ATOM   19145 C  CB  . GLU C 1 904  ? 86.038  -16.912 68.468  1.00 246.73 ? 904  GLU B CB  1 
ATOM   19146 C  CG  . GLU C 1 904  ? 86.857  -17.978 67.754  1.00 256.63 ? 904  GLU B CG  1 
ATOM   19147 C  CD  . GLU C 1 904  ? 88.347  -17.690 67.741  1.00 269.28 ? 904  GLU B CD  1 
ATOM   19148 O  OE1 . GLU C 1 904  ? 88.752  -16.554 68.086  1.00 271.79 ? 904  GLU B OE1 1 
ATOM   19149 O  OE2 . GLU C 1 904  ? 89.112  -18.612 67.382  1.00 275.57 ? 904  GLU B OE2 1 
ATOM   19150 N  N   . ILE C 1 905  ? 83.804  -16.639 71.199  1.00 211.03 ? 905  ILE B N   1 
ATOM   19151 C  CA  . ILE C 1 905  ? 82.971  -15.800 72.061  1.00 199.76 ? 905  ILE B CA  1 
ATOM   19152 C  C   . ILE C 1 905  ? 83.628  -14.466 72.340  1.00 195.38 ? 905  ILE B C   1 
ATOM   19153 O  O   . ILE C 1 905  ? 84.729  -14.414 72.886  1.00 192.47 ? 905  ILE B O   1 
ATOM   19154 C  CB  . ILE C 1 905  ? 82.690  -16.486 73.425  1.00 186.69 ? 905  ILE B CB  1 
ATOM   19155 C  CG1 . ILE C 1 905  ? 82.326  -17.955 73.214  1.00 185.84 ? 905  ILE B CG1 1 
ATOM   19156 C  CG2 . ILE C 1 905  ? 81.606  -15.744 74.189  1.00 183.20 ? 905  ILE B CG2 1 
ATOM   19157 C  CD1 . ILE C 1 905  ? 81.536  -18.558 74.335  1.00 188.60 ? 905  ILE B CD1 1 
ATOM   19158 N  N   . GLY C 1 906  ? 82.932  -13.392 71.984  1.00 224.97 ? 906  GLY B N   1 
ATOM   19159 C  CA  . GLY C 1 906  ? 83.479  -12.057 72.087  1.00 231.84 ? 906  GLY B CA  1 
ATOM   19160 C  C   . GLY C 1 906  ? 84.093  -11.608 70.774  1.00 234.85 ? 906  GLY B C   1 
ATOM   19161 O  O   . GLY C 1 906  ? 84.186  -10.411 70.529  1.00 232.10 ? 906  GLY B O   1 
ATOM   19162 N  N   . LEU C 1 907  ? 84.491  -12.558 69.922  1.00 214.34 ? 907  LEU B N   1 
ATOM   19163 C  CA  . LEU C 1 907  ? 85.204  -12.221 68.683  1.00 218.11 ? 907  LEU B CA  1 
ATOM   19164 C  C   . LEU C 1 907  ? 84.413  -11.251 67.824  1.00 214.64 ? 907  LEU B C   1 
ATOM   19165 O  O   . LEU C 1 907  ? 83.245  -11.484 67.519  1.00 208.99 ? 907  LEU B O   1 
ATOM   19166 C  CB  . LEU C 1 907  ? 85.588  -13.458 67.863  1.00 222.29 ? 907  LEU B CB  1 
ATOM   19167 C  CG  . LEU C 1 907  ? 86.229  -13.089 66.510  1.00 228.37 ? 907  LEU B CG  1 
ATOM   19168 C  CD1 . LEU C 1 907  ? 87.413  -12.147 66.679  1.00 234.02 ? 907  LEU B CD1 1 
ATOM   19169 C  CD2 . LEU C 1 907  ? 86.646  -14.316 65.725  1.00 234.35 ? 907  LEU B CD2 1 
ATOM   19170 N  N   . HIS C 1 908  ? 85.077  -10.171 67.427  1.00 218.45 ? 908  HIS B N   1 
ATOM   19171 C  CA  . HIS C 1 908  ? 84.422  -9.033  66.800  1.00 216.91 ? 908  HIS B CA  1 
ATOM   19172 C  C   . HIS C 1 908  ? 84.934  -8.783  65.385  1.00 217.07 ? 908  HIS B C   1 
ATOM   19173 O  O   . HIS C 1 908  ? 85.543  -9.659  64.770  1.00 221.80 ? 908  HIS B O   1 
ATOM   19174 C  CB  . HIS C 1 908  ? 84.689  -7.759  67.612  1.00 219.39 ? 908  HIS B CB  1 
ATOM   19175 C  CG  . HIS C 1 908  ? 84.938  -7.982  69.076  1.00 218.97 ? 908  HIS B CG  1 
ATOM   19176 N  ND1 . HIS C 1 908  ? 86.011  -8.706  69.557  1.00 222.11 ? 908  HIS B ND1 1 
ATOM   19177 C  CD2 . HIS C 1 908  ? 84.286  -7.513  70.167  1.00 214.77 ? 908  HIS B CD2 1 
ATOM   19178 C  CE1 . HIS C 1 908  ? 85.987  -8.700  70.874  1.00 222.65 ? 908  HIS B CE1 1 
ATOM   19179 N  NE2 . HIS C 1 908  ? 84.948  -7.984  71.271  1.00 217.99 ? 908  HIS B NE2 1 
ATOM   19180 N  N   . ASN C 1 909  ? 84.679  -7.570  64.890  1.00 223.22 ? 909  ASN B N   1 
ATOM   19181 C  CA  . ASN C 1 909  ? 85.240  -7.069  63.633  1.00 222.35 ? 909  ASN B CA  1 
ATOM   19182 C  C   . ASN C 1 909  ? 84.891  -7.844  62.365  1.00 215.62 ? 909  ASN B C   1 
ATOM   19183 O  O   . ASN C 1 909  ? 85.211  -9.024  62.234  1.00 215.80 ? 909  ASN B O   1 
ATOM   19184 C  CB  . ASN C 1 909  ? 86.763  -6.921  63.722  1.00 233.50 ? 909  ASN B CB  1 
ATOM   19185 C  CG  . ASN C 1 909  ? 87.411  -6.736  62.357  1.00 239.68 ? 909  ASN B CG  1 
ATOM   19186 O  OD1 . ASN C 1 909  ? 88.397  -7.398  62.020  1.00 245.99 ? 909  ASN B OD1 1 
ATOM   19187 N  ND2 . ASN C 1 909  ? 86.849  -5.842  61.561  1.00 237.17 ? 909  ASN B ND2 1 
ATOM   19188 N  N   . ILE C 1 910  ? 84.258  -7.151  61.424  1.00 185.51 ? 910  ILE B N   1 
ATOM   19189 C  CA  . ILE C 1 910  ? 84.015  -7.661  60.082  1.00 177.53 ? 910  ILE B CA  1 
ATOM   19190 C  C   . ILE C 1 910  ? 84.020  -6.432  59.179  1.00 176.88 ? 910  ILE B C   1 
ATOM   19191 O  O   . ILE C 1 910  ? 83.214  -5.518  59.355  1.00 177.95 ? 910  ILE B O   1 
ATOM   19192 C  CB  . ILE C 1 910  ? 82.672  -8.429  59.992  1.00 165.11 ? 910  ILE B CB  1 
ATOM   19193 C  CG1 . ILE C 1 910  ? 82.831  -9.831  60.568  1.00 162.92 ? 910  ILE B CG1 1 
ATOM   19194 C  CG2 . ILE C 1 910  ? 82.186  -8.545  58.561  1.00 160.06 ? 910  ILE B CG2 1 
ATOM   19195 C  CD1 . ILE C 1 910  ? 81.533  -10.564 60.714  1.00 156.34 ? 910  ILE B CD1 1 
ATOM   19196 N  N   . ASN C 1 911  ? 84.967  -6.386  58.245  1.00 218.70 ? 911  ASN B N   1 
ATOM   19197 C  CA  . ASN C 1 911  ? 85.066  -5.269  57.300  1.00 212.81 ? 911  ASN B CA  1 
ATOM   19198 C  C   . ASN C 1 911  ? 84.256  -5.531  56.009  1.00 209.76 ? 911  ASN B C   1 
ATOM   19199 O  O   . ASN C 1 911  ? 84.560  -6.455  55.240  1.00 209.47 ? 911  ASN B O   1 
ATOM   19200 C  CB  . ASN C 1 911  ? 86.536  -4.961  56.961  1.00 214.88 ? 911  ASN B CB  1 
ATOM   19201 C  CG  . ASN C 1 911  ? 87.414  -4.750  58.202  1.00 215.44 ? 911  ASN B CG  1 
ATOM   19202 O  OD1 . ASN C 1 911  ? 87.510  -5.617  59.074  1.00 218.84 ? 911  ASN B OD1 1 
ATOM   19203 N  ND2 . ASN C 1 911  ? 88.078  -3.600  58.264  1.00 216.59 ? 911  ASN B ND2 1 
ATOM   19204 N  N   . PHE C 1 912  ? 83.223  -4.721  55.781  1.00 198.78 ? 912  PHE B N   1 
ATOM   19205 C  CA  . PHE C 1 912  ? 82.388  -4.853  54.584  1.00 193.96 ? 912  PHE B CA  1 
ATOM   19206 C  C   . PHE C 1 912  ? 82.846  -3.920  53.449  1.00 197.59 ? 912  PHE B C   1 
ATOM   19207 O  O   . PHE C 1 912  ? 83.295  -2.799  53.709  1.00 200.09 ? 912  PHE B O   1 
ATOM   19208 C  CB  . PHE C 1 912  ? 80.904  -4.626  54.922  1.00 184.04 ? 912  PHE B CB  1 
ATOM   19209 C  CG  . PHE C 1 912  ? 80.263  -5.777  55.651  1.00 177.63 ? 912  PHE B CG  1 
ATOM   19210 C  CD1 . PHE C 1 912  ? 79.815  -6.887  54.963  1.00 174.70 ? 912  PHE B CD1 1 
ATOM   19211 C  CD2 . PHE C 1 912  ? 80.108  -5.749  57.023  1.00 175.85 ? 912  PHE B CD2 1 
ATOM   19212 C  CE1 . PHE C 1 912  ? 79.231  -7.941  55.632  1.00 171.78 ? 912  PHE B CE1 1 
ATOM   19213 C  CE2 . PHE C 1 912  ? 79.521  -6.808  57.696  1.00 172.98 ? 912  PHE B CE2 1 
ATOM   19214 C  CZ  . PHE C 1 912  ? 79.085  -7.900  57.000  1.00 170.51 ? 912  PHE B CZ  1 
ATOM   19215 N  N   . SER C 1 913  ? 82.706  -4.387  52.200  1.00 210.19 ? 913  SER B N   1 
ATOM   19216 C  CA  . SER C 1 913  ? 83.197  -3.681  51.003  1.00 213.93 ? 913  SER B CA  1 
ATOM   19217 C  C   . SER C 1 913  ? 82.237  -3.807  49.802  1.00 215.32 ? 913  SER B C   1 
ATOM   19218 O  O   . SER C 1 913  ? 81.757  -4.901  49.502  1.00 213.15 ? 913  SER B O   1 
ATOM   19219 C  CB  . SER C 1 913  ? 84.592  -4.207  50.625  1.00 218.61 ? 913  SER B CB  1 
ATOM   19220 O  OG  . SER C 1 913  ? 85.111  -3.588  49.462  1.00 218.47 ? 913  SER B OG  1 
ATOM   19221 N  N   . LEU C 1 914  ? 81.953  -2.687  49.133  1.00 198.55 ? 914  LEU B N   1 
ATOM   19222 C  CA  . LEU C 1 914  ? 81.151  -2.698  47.906  1.00 199.36 ? 914  LEU B CA  1 
ATOM   19223 C  C   . LEU C 1 914  ? 81.920  -2.073  46.744  1.00 210.18 ? 914  LEU B C   1 
ATOM   19224 O  O   . LEU C 1 914  ? 82.871  -1.324  46.952  1.00 214.96 ? 914  LEU B O   1 
ATOM   19225 C  CB  . LEU C 1 914  ? 79.777  -2.026  48.104  1.00 186.78 ? 914  LEU B CB  1 
ATOM   19226 C  CG  . LEU C 1 914  ? 79.625  -0.580  48.604  1.00 178.36 ? 914  LEU B CG  1 
ATOM   19227 C  CD1 . LEU C 1 914  ? 80.263  0.427   47.649  1.00 177.71 ? 914  LEU B CD1 1 
ATOM   19228 C  CD2 . LEU C 1 914  ? 78.154  -0.216  48.862  1.00 170.67 ? 914  LEU B CD2 1 
ATOM   19229 N  N   . GLU C 1 915  ? 81.513  -2.391  45.521  1.00 239.18 ? 915  GLU B N   1 
ATOM   19230 C  CA  . GLU C 1 915  ? 82.271  -1.960  44.357  1.00 248.93 ? 915  GLU B CA  1 
ATOM   19231 C  C   . GLU C 1 915  ? 81.376  -1.425  43.254  1.00 249.10 ? 915  GLU B C   1 
ATOM   19232 O  O   . GLU C 1 915  ? 80.373  -2.038  42.901  1.00 244.21 ? 915  GLU B O   1 
ATOM   19233 C  CB  . GLU C 1 915  ? 83.158  -3.096  43.831  1.00 255.51 ? 915  GLU B CB  1 
ATOM   19234 C  CG  . GLU C 1 915  ? 84.511  -3.209  44.539  1.00 264.70 ? 915  GLU B CG  1 
ATOM   19235 C  CD  . GLU C 1 915  ? 84.722  -4.546  45.244  1.00 269.70 ? 915  GLU B CD  1 
ATOM   19236 O  OE1 . GLU C 1 915  ? 84.177  -5.569  44.779  1.00 268.49 ? 915  GLU B OE1 1 
ATOM   19237 O  OE2 . GLU C 1 915  ? 85.440  -4.578  46.265  1.00 274.70 ? 915  GLU B OE2 1 
ATOM   19238 N  N   . THR C 1 916  ? 81.760  -0.273  42.717  1.00 254.64 ? 916  THR B N   1 
ATOM   19239 C  CA  . THR C 1 916  ? 81.013  0.389   41.661  1.00 258.28 ? 916  THR B CA  1 
ATOM   19240 C  C   . THR C 1 916  ? 81.980  1.001   40.667  1.00 270.51 ? 916  THR B C   1 
ATOM   19241 O  O   . THR C 1 916  ? 83.144  1.246   40.988  1.00 275.13 ? 916  THR B O   1 
ATOM   19242 C  CB  . THR C 1 916  ? 80.120  1.508   42.218  1.00 251.94 ? 916  THR B CB  1 
ATOM   19243 O  OG1 . THR C 1 916  ? 79.209  0.958   43.174  1.00 248.08 ? 916  THR B OG1 1 
ATOM   19244 C  CG2 . THR C 1 916  ? 79.333  2.180   41.096  1.00 247.46 ? 916  THR B CG2 1 
ATOM   19245 N  N   . TRP C 1 917  ? 81.483  1.249   39.462  1.00 312.80 ? 917  TRP B N   1 
ATOM   19246 C  CA  . TRP C 1 917  ? 82.292  1.790   38.388  1.00 323.33 ? 917  TRP B CA  1 
ATOM   19247 C  C   . TRP C 1 917  ? 83.271  2.825   38.911  1.00 330.44 ? 917  TRP B C   1 
ATOM   19248 O  O   . TRP C 1 917  ? 84.481  2.692   38.733  1.00 333.86 ? 917  TRP B O   1 
ATOM   19249 C  CB  . TRP C 1 917  ? 81.395  2.423   37.331  1.00 324.19 ? 917  TRP B CB  1 
ATOM   19250 C  CG  . TRP C 1 917  ? 81.932  2.285   35.953  1.00 328.78 ? 917  TRP B CG  1 
ATOM   19251 C  CD1 . TRP C 1 917  ? 82.468  3.269   35.177  1.00 325.36 ? 917  TRP B CD1 1 
ATOM   19252 C  CD2 . TRP C 1 917  ? 81.999  1.082   35.180  1.00 330.66 ? 917  TRP B CD2 1 
ATOM   19253 N  NE1 . TRP C 1 917  ? 82.858  2.755   33.963  1.00 323.46 ? 917  TRP B NE1 1 
ATOM   19254 C  CE2 . TRP C 1 917  ? 82.581  1.412   33.941  1.00 326.52 ? 917  TRP B CE2 1 
ATOM   19255 C  CE3 . TRP C 1 917  ? 81.620  -0.244  35.416  1.00 335.64 ? 917  TRP B CE3 1 
ATOM   19256 C  CZ2 . TRP C 1 917  ? 82.795  0.466   32.938  1.00 327.03 ? 917  TRP B CZ2 1 
ATOM   19257 C  CZ3 . TRP C 1 917  ? 81.833  -1.181  34.420  1.00 334.33 ? 917  TRP B CZ3 1 
ATOM   19258 C  CH2 . TRP C 1 917  ? 82.414  -0.822  33.197  1.00 330.96 ? 917  TRP B CH2 1 
ATOM   19259 N  N   . PHE C 1 918  ? 82.746  3.852   39.570  1.00 262.67 ? 918  PHE B N   1 
ATOM   19260 C  CA  . PHE C 1 918  ? 83.595  4.941   40.040  1.00 268.70 ? 918  PHE B CA  1 
ATOM   19261 C  C   . PHE C 1 918  ? 83.940  4.905   41.529  1.00 263.78 ? 918  PHE B C   1 
ATOM   19262 O  O   . PHE C 1 918  ? 84.348  5.916   42.098  1.00 265.22 ? 918  PHE B O   1 
ATOM   19263 C  CB  . PHE C 1 918  ? 83.043  6.316   39.617  1.00 273.04 ? 918  PHE B CB  1 
ATOM   19264 C  CG  . PHE C 1 918  ? 81.637  6.614   40.094  1.00 272.51 ? 918  PHE B CG  1 
ATOM   19265 C  CD1 . PHE C 1 918  ? 81.421  7.310   41.276  1.00 274.14 ? 918  PHE B CD1 1 
ATOM   19266 C  CD2 . PHE C 1 918  ? 80.535  6.254   39.329  1.00 270.20 ? 918  PHE B CD2 1 
ATOM   19267 C  CE1 . PHE C 1 918  ? 80.132  7.612   41.703  1.00 270.31 ? 918  PHE B CE1 1 
ATOM   19268 C  CE2 . PHE C 1 918  ? 79.243  6.553   39.750  1.00 266.29 ? 918  PHE B CE2 1 
ATOM   19269 C  CZ  . PHE C 1 918  ? 79.043  7.232   40.937  1.00 266.30 ? 918  PHE B CZ  1 
ATOM   19270 N  N   . GLY C 1 919  ? 83.810  3.743   42.158  1.00 286.42 ? 919  GLY B N   1 
ATOM   19271 C  CA  . GLY C 1 919  ? 84.092  3.667   43.578  1.00 280.52 ? 919  GLY B CA  1 
ATOM   19272 C  C   . GLY C 1 919  ? 84.253  2.288   44.182  1.00 276.43 ? 919  GLY B C   1 
ATOM   19273 O  O   . GLY C 1 919  ? 83.873  1.277   43.591  1.00 273.82 ? 919  GLY B O   1 
ATOM   19274 N  N   . LYS C 1 920  ? 84.826  2.271   45.381  1.00 270.25 ? 920  LYS B N   1 
ATOM   19275 C  CA  . LYS C 1 920  ? 85.003  1.059   46.172  1.00 265.77 ? 920  LYS B CA  1 
ATOM   19276 C  C   . LYS C 1 920  ? 85.164  1.495   47.628  1.00 260.55 ? 920  LYS B C   1 
ATOM   19277 O  O   . LYS C 1 920  ? 86.079  2.251   47.956  1.00 265.50 ? 920  LYS B O   1 
ATOM   19278 C  CB  . LYS C 1 920  ? 86.226  0.277   45.682  1.00 269.39 ? 920  LYS B CB  1 
ATOM   19279 C  CG  . LYS C 1 920  ? 86.454  -1.069  46.363  1.00 269.75 ? 920  LYS B CG  1 
ATOM   19280 C  CD  . LYS C 1 920  ? 87.446  -1.924  45.573  1.00 272.13 ? 920  LYS B CD  1 
ATOM   19281 C  CE  . LYS C 1 920  ? 87.800  -3.212  46.306  1.00 272.93 ? 920  LYS B CE  1 
ATOM   19282 N  NZ  . LYS C 1 920  ? 88.351  -4.248  45.387  1.00 275.49 ? 920  LYS B NZ  1 
ATOM   19283 N  N   . GLU C 1 921  ? 84.267  1.021   48.493  1.00 287.48 ? 921  GLU B N   1 
ATOM   19284 C  CA  . GLU C 1 921  ? 84.141  1.538   49.862  1.00 280.41 ? 921  GLU B CA  1 
ATOM   19285 C  C   . GLU C 1 921  ? 84.186  0.414   50.916  1.00 273.40 ? 921  GLU B C   1 
ATOM   19286 O  O   . GLU C 1 921  ? 83.747  -0.706  50.648  1.00 270.95 ? 921  GLU B O   1 
ATOM   19287 C  CB  . GLU C 1 921  ? 82.830  2.331   49.983  1.00 278.16 ? 921  GLU B CB  1 
ATOM   19288 C  CG  . GLU C 1 921  ? 82.764  3.318   51.138  1.00 281.68 ? 921  GLU B CG  1 
ATOM   19289 C  CD  . GLU C 1 921  ? 82.999  4.754   50.703  1.00 285.55 ? 921  GLU B CD  1 
ATOM   19290 O  OE1 . GLU C 1 921  ? 83.576  4.972   49.618  1.00 289.38 ? 921  GLU B OE1 1 
ATOM   19291 O  OE2 . GLU C 1 921  ? 82.608  5.669   51.457  1.00 284.81 ? 921  GLU B OE2 1 
ATOM   19292 N  N   . ILE C 1 922  ? 84.714  0.715   52.105  1.00 220.39 ? 922  ILE B N   1 
ATOM   19293 C  CA  . ILE C 1 922  ? 84.836  -0.277  53.180  1.00 213.23 ? 922  ILE B CA  1 
ATOM   19294 C  C   . ILE C 1 922  ? 84.247  0.191   54.502  1.00 204.38 ? 922  ILE B C   1 
ATOM   19295 O  O   . ILE C 1 922  ? 84.827  1.031   55.189  1.00 204.86 ? 922  ILE B O   1 
ATOM   19296 C  CB  . ILE C 1 922  ? 86.307  -0.683  53.446  1.00 216.59 ? 922  ILE B CB  1 
ATOM   19297 C  CG1 . ILE C 1 922  ? 86.773  -1.706  52.416  1.00 216.77 ? 922  ILE B CG1 1 
ATOM   19298 C  CG2 . ILE C 1 922  ? 86.447  -1.303  54.820  1.00 218.89 ? 922  ILE B CG2 1 
ATOM   19299 C  CD1 . ILE C 1 922  ? 88.016  -2.463  52.823  1.00 221.04 ? 922  ILE B CD1 1 
ATOM   19300 N  N   . LEU C 1 923  ? 83.098  -0.365  54.863  1.00 230.83 ? 923  LEU B N   1 
ATOM   19301 C  CA  . LEU C 1 923  ? 82.511  -0.103  56.169  1.00 227.63 ? 923  LEU B CA  1 
ATOM   19302 C  C   . LEU C 1 923  ? 82.854  -1.234  57.127  1.00 229.98 ? 923  LEU B C   1 
ATOM   19303 O  O   . LEU C 1 923  ? 82.521  -2.393  56.863  1.00 231.29 ? 923  LEU B O   1 
ATOM   19304 C  CB  . LEU C 1 923  ? 80.998  0.039   56.047  1.00 220.11 ? 923  LEU B CB  1 
ATOM   19305 C  CG  . LEU C 1 923  ? 80.153  -0.477  57.211  1.00 217.23 ? 923  LEU B CG  1 
ATOM   19306 C  CD1 . LEU C 1 923  ? 80.448  0.277   58.497  1.00 219.28 ? 923  LEU B CD1 1 
ATOM   19307 C  CD2 . LEU C 1 923  ? 78.689  -0.364  56.852  1.00 211.02 ? 923  LEU B CD2 1 
ATOM   19308 N  N   . VAL C 1 924  ? 83.517  -0.905  58.237  1.00 185.59 ? 924  VAL B N   1 
ATOM   19309 C  CA  . VAL C 1 924  ? 83.872  -1.934  59.209  1.00 185.55 ? 924  VAL B CA  1 
ATOM   19310 C  C   . VAL C 1 924  ? 82.891  -2.059  60.368  1.00 177.30 ? 924  VAL B C   1 
ATOM   19311 O  O   . VAL C 1 924  ? 82.391  -1.071  60.903  1.00 172.42 ? 924  VAL B O   1 
ATOM   19312 C  CB  . VAL C 1 924  ? 85.290  -1.776  59.760  1.00 190.98 ? 924  VAL B CB  1 
ATOM   19313 C  CG1 . VAL C 1 924  ? 85.827  -3.139  60.101  1.00 195.08 ? 924  VAL B CG1 1 
ATOM   19314 C  CG2 . VAL C 1 924  ? 86.190  -1.102  58.748  1.00 193.75 ? 924  VAL B CG2 1 
ATOM   19315 N  N   . LYS C 1 925  ? 82.652  -3.304  60.755  1.00 172.78 ? 925  LYS B N   1 
ATOM   19316 C  CA  . LYS C 1 925  ? 81.673  -3.637  61.774  1.00 166.32 ? 925  LYS B CA  1 
ATOM   19317 C  C   . LYS C 1 925  ? 82.243  -4.583  62.837  1.00 168.08 ? 925  LYS B C   1 
ATOM   19318 O  O   . LYS C 1 925  ? 83.365  -5.077  62.720  1.00 177.01 ? 925  LYS B O   1 
ATOM   19319 C  CB  . LYS C 1 925  ? 80.462  -4.294  61.122  1.00 159.15 ? 925  LYS B CB  1 
ATOM   19320 C  CG  . LYS C 1 925  ? 79.141  -3.662  61.477  1.00 151.76 ? 925  LYS B CG  1 
ATOM   19321 C  CD  . LYS C 1 925  ? 78.921  -2.384  60.715  1.00 149.11 ? 925  LYS B CD  1 
ATOM   19322 C  CE  . LYS C 1 925  ? 77.486  -1.922  60.871  1.00 144.77 ? 925  LYS B CE  1 
ATOM   19323 N  NZ  . LYS C 1 925  ? 77.371  -0.441  60.732  1.00 143.51 ? 925  LYS B NZ  1 
ATOM   19324 N  N   . THR C 1 926  ? 81.445  -4.859  63.864  1.00 178.58 ? 926  THR B N   1 
ATOM   19325 C  CA  . THR C 1 926  ? 81.915  -5.634  65.002  1.00 176.24 ? 926  THR B CA  1 
ATOM   19326 C  C   . THR C 1 926  ? 80.781  -6.402  65.680  1.00 171.23 ? 926  THR B C   1 
ATOM   19327 O  O   . THR C 1 926  ? 79.767  -5.822  66.067  1.00 167.18 ? 926  THR B O   1 
ATOM   19328 C  CB  . THR C 1 926  ? 82.559  -4.691  65.992  1.00 206.84 ? 926  THR B CB  1 
ATOM   19329 O  OG1 . THR C 1 926  ? 81.922  -3.410  65.874  1.00 203.57 ? 926  THR B OG1 1 
ATOM   19330 C  CG2 . THR C 1 926  ? 84.033  -4.538  65.663  1.00 209.02 ? 926  THR B CG2 1 
ATOM   19331 N  N   . LEU C 1 927  ? 80.972  -7.708  65.833  1.00 148.73 ? 927  LEU B N   1 
ATOM   19332 C  CA  . LEU C 1 927  ? 79.903  -8.606  66.255  1.00 150.39 ? 927  LEU B CA  1 
ATOM   19333 C  C   . LEU C 1 927  ? 80.118  -9.092  67.676  1.00 153.93 ? 927  LEU B C   1 
ATOM   19334 O  O   . LEU C 1 927  ? 81.185  -9.610  67.992  1.00 155.89 ? 927  LEU B O   1 
ATOM   19335 C  CB  . LEU C 1 927  ? 79.877  -9.818  65.320  1.00 150.55 ? 927  LEU B CB  1 
ATOM   19336 C  CG  . LEU C 1 927  ? 78.868  -10.979 65.409  1.00 152.06 ? 927  LEU B CG  1 
ATOM   19337 C  CD1 . LEU C 1 927  ? 79.414  -12.205 64.677  1.00 152.95 ? 927  LEU B CD1 1 
ATOM   19338 C  CD2 . LEU C 1 927  ? 78.512  -11.357 66.833  1.00 155.12 ? 927  LEU B CD2 1 
ATOM   19339 N  N   . ARG C 1 928  ? 79.097  -8.962  68.523  1.00 204.40 ? 928  ARG B N   1 
ATOM   19340 C  CA  . ARG C 1 928  ? 79.179  -9.409  69.923  1.00 206.62 ? 928  ARG B CA  1 
ATOM   19341 C  C   . ARG C 1 928  ? 78.760  -10.884 70.121  1.00 208.20 ? 928  ARG B C   1 
ATOM   19342 O  O   . ARG C 1 928  ? 77.588  -11.227 69.964  1.00 204.89 ? 928  ARG B O   1 
ATOM   19343 C  CB  . ARG C 1 928  ? 78.367  -8.462  70.840  1.00 204.68 ? 928  ARG B CB  1 
ATOM   19344 C  CG  . ARG C 1 928  ? 79.065  -7.113  71.204  1.00 210.64 ? 928  ARG B CG  1 
ATOM   19345 C  CD  . ARG C 1 928  ? 78.076  -5.938  71.417  1.00 213.53 ? 928  ARG B CD  1 
ATOM   19346 N  NE  . ARG C 1 928  ? 77.455  -5.490  70.163  1.00 217.55 ? 928  ARG B NE  1 
ATOM   19347 C  CZ  . ARG C 1 928  ? 77.773  -4.374  69.505  1.00 220.22 ? 928  ARG B CZ  1 
ATOM   19348 N  NH1 . ARG C 1 928  ? 78.701  -3.555  69.981  1.00 224.48 ? 928  ARG B NH1 1 
ATOM   19349 N  NH2 . ARG C 1 928  ? 77.154  -4.068  68.368  1.00 214.52 ? 928  ARG B NH2 1 
ATOM   19350 N  N   . VAL C 1 929  ? 79.715  -11.744 70.478  1.00 165.04 ? 929  VAL B N   1 
ATOM   19351 C  CA  . VAL C 1 929  ? 79.446  -13.181 70.656  1.00 165.86 ? 929  VAL B CA  1 
ATOM   19352 C  C   . VAL C 1 929  ? 79.365  -13.599 72.152  1.00 169.54 ? 929  VAL B C   1 
ATOM   19353 O  O   . VAL C 1 929  ? 80.245  -13.257 72.946  1.00 171.12 ? 929  VAL B O   1 
ATOM   19354 C  CB  . VAL C 1 929  ? 80.485  -14.041 69.863  1.00 172.12 ? 929  VAL B CB  1 
ATOM   19355 C  CG1 . VAL C 1 929  ? 80.007  -15.474 69.668  1.00 171.68 ? 929  VAL B CG1 1 
ATOM   19356 C  CG2 . VAL C 1 929  ? 80.754  -13.410 68.513  1.00 169.07 ? 929  VAL B CG2 1 
ATOM   19357 N  N   . VAL C 1 930  ? 78.315  -14.348 72.513  1.00 189.15 ? 930  VAL B N   1 
ATOM   19358 C  CA  . VAL C 1 930  ? 77.958  -14.666 73.908  1.00 193.48 ? 930  VAL B CA  1 
ATOM   19359 C  C   . VAL C 1 930  ? 77.830  -16.167 74.133  1.00 200.01 ? 930  VAL B C   1 
ATOM   19360 O  O   . VAL C 1 930  ? 77.827  -16.925 73.180  1.00 203.02 ? 930  VAL B O   1 
ATOM   19361 C  CB  . VAL C 1 930  ? 76.566  -14.095 74.256  1.00 190.46 ? 930  VAL B CB  1 
ATOM   19362 C  CG1 . VAL C 1 930  ? 76.377  -13.939 75.780  1.00 192.20 ? 930  VAL B CG1 1 
ATOM   19363 C  CG2 . VAL C 1 930  ? 76.331  -12.786 73.529  1.00 187.98 ? 930  VAL B CG2 1 
ATOM   19364 N  N   . PRO C 1 931  ? 77.750  -16.603 75.402  1.00 181.72 ? 931  PRO B N   1 
ATOM   19365 C  CA  . PRO C 1 931  ? 77.300  -17.949 75.780  1.00 184.41 ? 931  PRO B CA  1 
ATOM   19366 C  C   . PRO C 1 931  ? 75.969  -17.934 76.536  1.00 180.08 ? 931  PRO B C   1 
ATOM   19367 O  O   . PRO C 1 931  ? 75.198  -16.988 76.382  1.00 181.74 ? 931  PRO B O   1 
ATOM   19368 C  CB  . PRO C 1 931  ? 78.415  -18.452 76.708  1.00 181.46 ? 931  PRO B CB  1 
ATOM   19369 C  CG  . PRO C 1 931  ? 79.459  -17.355 76.716  1.00 178.17 ? 931  PRO B CG  1 
ATOM   19370 C  CD  . PRO C 1 931  ? 78.719  -16.108 76.377  1.00 177.36 ? 931  PRO B CD  1 
ATOM   19371 N  N   . GLU C 1 932  ? 75.727  -18.956 77.358  1.00 187.33 ? 932  GLU B N   1 
ATOM   19372 C  CA  . GLU C 1 932  ? 74.375  -19.313 77.802  1.00 188.62 ? 932  GLU B CA  1 
ATOM   19373 C  C   . GLU C 1 932  ? 74.234  -19.560 79.314  1.00 182.39 ? 932  GLU B C   1 
ATOM   19374 O  O   . GLU C 1 932  ? 74.553  -20.650 79.781  1.00 178.29 ? 932  GLU B O   1 
ATOM   19375 C  CB  . GLU C 1 932  ? 73.963  -20.605 77.083  1.00 193.85 ? 932  GLU B CB  1 
ATOM   19376 C  CG  . GLU C 1 932  ? 74.599  -20.802 75.700  1.00 198.02 ? 932  GLU B CG  1 
ATOM   19377 C  CD  . GLU C 1 932  ? 76.061  -21.243 75.739  1.00 197.16 ? 932  GLU B CD  1 
ATOM   19378 O  OE1 . GLU C 1 932  ? 76.796  -20.845 76.660  1.00 193.86 ? 932  GLU B OE1 1 
ATOM   19379 O  OE2 . GLU C 1 932  ? 76.484  -21.982 74.827  1.00 199.90 ? 932  GLU B OE2 1 
ATOM   19380 N  N   . GLY C 1 933  ? 73.728  -18.586 80.074  1.00 182.78 ? 933  GLY B N   1 
ATOM   19381 C  CA  . GLY C 1 933  ? 73.566  -18.744 81.523  1.00 181.50 ? 933  GLY B CA  1 
ATOM   19382 C  C   . GLY C 1 933  ? 74.493  -17.939 82.441  1.00 176.90 ? 933  GLY B C   1 
ATOM   19383 O  O   . GLY C 1 933  ? 75.188  -18.495 83.294  1.00 172.89 ? 933  GLY B O   1 
ATOM   19384 N  N   . VAL C 1 934  ? 74.492  -16.620 82.274  1.00 192.35 ? 934  VAL B N   1 
ATOM   19385 C  CA  . VAL C 1 934  ? 75.346  -15.715 83.048  1.00 195.33 ? 934  VAL B CA  1 
ATOM   19386 C  C   . VAL C 1 934  ? 74.978  -15.642 84.526  1.00 190.70 ? 934  VAL B C   1 
ATOM   19387 O  O   . VAL C 1 934  ? 73.916  -15.132 84.877  1.00 188.63 ? 934  VAL B O   1 
ATOM   19388 C  CB  . VAL C 1 934  ? 75.297  -14.272 82.467  1.00 202.55 ? 934  VAL B CB  1 
ATOM   19389 C  CG1 . VAL C 1 934  ? 76.046  -13.280 83.361  1.00 164.88 ? 934  VAL B CG1 1 
ATOM   19390 C  CG2 . VAL C 1 934  ? 75.849  -14.247 81.054  1.00 208.96 ? 934  VAL B CG2 1 
ATOM   19391 N  N   . LYS C 1 935  ? 75.866  -16.149 85.380  1.00 181.66 ? 935  LYS B N   1 
ATOM   19392 C  CA  . LYS C 1 935  ? 75.772  -15.957 86.831  1.00 180.55 ? 935  LYS B CA  1 
ATOM   19393 C  C   . LYS C 1 935  ? 77.105  -15.359 87.339  1.00 181.65 ? 935  LYS B C   1 
ATOM   19394 O  O   . LYS C 1 935  ? 78.180  -15.772 86.898  1.00 180.61 ? 935  LYS B O   1 
ATOM   19395 C  CB  . LYS C 1 935  ? 75.450  -17.295 87.519  1.00 181.76 ? 935  LYS B CB  1 
ATOM   19396 C  CG  . LYS C 1 935  ? 74.147  -17.339 88.346  1.00 151.24 ? 935  LYS B CG  1 
ATOM   19397 C  CD  . LYS C 1 935  ? 73.047  -16.441 87.797  1.00 159.80 ? 935  LYS B CD  1 
ATOM   19398 C  CE  . LYS C 1 935  ? 72.088  -15.937 88.891  1.00 161.56 ? 935  LYS B CE  1 
ATOM   19399 N  NZ  . LYS C 1 935  ? 70.921  -16.824 89.187  1.00 166.12 ? 935  LYS B NZ  1 
ATOM   19400 N  N   . ARG C 1 936  ? 77.058  -14.373 88.233  1.00 164.63 ? 936  ARG B N   1 
ATOM   19401 C  CA  . ARG C 1 936  ? 78.318  -13.864 88.773  1.00 164.45 ? 936  ARG B CA  1 
ATOM   19402 C  C   . ARG C 1 936  ? 78.374  -13.898 90.287  1.00 164.34 ? 936  ARG B C   1 
ATOM   19403 O  O   . ARG C 1 936  ? 77.499  -13.355 90.965  1.00 166.64 ? 936  ARG B O   1 
ATOM   19404 C  CB  . ARG C 1 936  ? 78.646  -12.470 88.241  1.00 163.94 ? 936  ARG B CB  1 
ATOM   19405 C  CG  . ARG C 1 936  ? 77.881  -11.335 88.870  1.00 164.30 ? 936  ARG B CG  1 
ATOM   19406 C  CD  . ARG C 1 936  ? 77.826  -10.152 87.917  1.00 169.60 ? 936  ARG B CD  1 
ATOM   19407 N  NE  . ARG C 1 936  ? 78.390  -8.927  88.482  1.00 171.81 ? 936  ARG B NE  1 
ATOM   19408 C  CZ  . ARG C 1 936  ? 78.528  -7.791  87.803  1.00 175.41 ? 936  ARG B CZ  1 
ATOM   19409 N  NH1 . ARG C 1 936  ? 78.139  -7.730  86.535  1.00 178.03 ? 936  ARG B NH1 1 
ATOM   19410 N  NH2 . ARG C 1 936  ? 79.052  -6.716  88.388  1.00 174.40 ? 936  ARG B NH2 1 
ATOM   19411 N  N   . GLU C 1 937  ? 79.431  -14.544 90.789  1.00 215.86 ? 937  GLU B N   1 
ATOM   19412 C  CA  . GLU C 1 937  ? 79.675  -14.778 92.219  1.00 222.24 ? 937  GLU B CA  1 
ATOM   19413 C  C   . GLU C 1 937  ? 81.003  -14.156 92.676  1.00 224.78 ? 937  GLU B C   1 
ATOM   19414 O  O   . GLU C 1 937  ? 82.087  -14.688 92.396  1.00 219.29 ? 937  GLU B O   1 
ATOM   19415 C  CB  . GLU C 1 937  ? 79.665  -16.279 92.509  1.00 235.10 ? 937  GLU B CB  1 
ATOM   19416 C  CG  . GLU C 1 937  ? 80.804  -17.063 91.852  1.00 285.46 ? 937  GLU B CG  1 
ATOM   19417 C  CD  . GLU C 1 937  ? 80.549  -18.565 91.804  1.00 298.31 ? 937  GLU B CD  1 
ATOM   19418 O  OE1 . GLU C 1 937  ? 79.597  -18.984 91.106  1.00 300.23 ? 937  GLU B OE1 1 
ATOM   19419 O  OE2 . GLU C 1 937  ? 81.305  -19.327 92.453  1.00 297.45 ? 937  GLU B OE2 1 
ATOM   19420 N  N   . SER C 1 938  ? 80.897  -13.049 93.415  1.00 146.94 ? 938  SER B N   1 
ATOM   19421 C  CA  . SER C 1 938  ? 82.025  -12.141 93.665  1.00 149.49 ? 938  SER B CA  1 
ATOM   19422 C  C   . SER C 1 938  ? 82.570  -12.107 95.100  1.00 158.18 ? 938  SER B C   1 
ATOM   19423 O  O   . SER C 1 938  ? 83.518  -11.362 95.384  1.00 164.60 ? 938  SER B O   1 
ATOM   19424 C  CB  . SER C 1 938  ? 81.616  -10.721 93.258  1.00 127.18 ? 938  SER B CB  1 
ATOM   19425 O  OG  . SER C 1 938  ? 80.282  -10.470 93.633  1.00 126.10 ? 938  SER B OG  1 
ATOM   19426 N  N   . TYR C 1 939  ? 81.988  -12.928 95.982  1.00 245.87 ? 939  TYR B N   1 
ATOM   19427 C  CA  . TYR C 1 939  ? 82.146  -12.797 97.448  1.00 253.56 ? 939  TYR B CA  1 
ATOM   19428 C  C   . TYR C 1 939  ? 83.567  -12.775 98.017  1.00 240.19 ? 939  TYR B C   1 
ATOM   19429 O  O   . TYR C 1 939  ? 83.768  -12.466 99.198  1.00 231.03 ? 939  TYR B O   1 
ATOM   19430 C  CB  . TYR C 1 939  ? 81.301  -13.836 98.195  1.00 283.99 ? 939  TYR B CB  1 
ATOM   19431 C  CG  . TYR C 1 939  ? 81.711  -15.268 97.970  1.00 301.76 ? 939  TYR B CG  1 
ATOM   19432 C  CD1 . TYR C 1 939  ? 82.687  -15.865 98.754  1.00 306.56 ? 939  TYR B CD1 1 
ATOM   19433 C  CD2 . TYR C 1 939  ? 81.111  -16.027 96.981  1.00 310.27 ? 939  TYR B CD2 1 
ATOM   19434 C  CE1 . TYR C 1 939  ? 83.055  -17.174 98.551  1.00 310.02 ? 939  TYR B CE1 1 
ATOM   19435 C  CE2 . TYR C 1 939  ? 81.470  -17.332 96.771  1.00 313.81 ? 939  TYR B CE2 1 
ATOM   19436 C  CZ  . TYR C 1 939  ? 82.442  -17.904 97.556  1.00 313.46 ? 939  TYR B CZ  1 
ATOM   19437 O  OH  . TYR C 1 939  ? 82.796  -19.214 97.339  1.00 315.79 ? 939  TYR B OH  1 
ATOM   19438 N  N   . SER C 1 940  ? 84.539  -13.122 97.186  1.00 203.50 ? 940  SER B N   1 
ATOM   19439 C  CA  . SER C 1 940  ? 85.930  -12.888 97.518  1.00 196.90 ? 940  SER B CA  1 
ATOM   19440 C  C   . SER C 1 940  ? 86.149  -11.383 97.669  1.00 185.56 ? 940  SER B C   1 
ATOM   19441 O  O   . SER C 1 940  ? 85.826  -10.598 96.773  1.00 185.78 ? 940  SER B O   1 
ATOM   19442 C  CB  . SER C 1 940  ? 86.809  -13.427 96.404  1.00 201.27 ? 940  SER B CB  1 
ATOM   19443 O  OG  . SER C 1 940  ? 86.470  -12.808 95.176  1.00 202.86 ? 940  SER B OG  1 
ATOM   19444 N  N   . GLY C 1 941  ? 86.689  -10.993 98.815  1.00 199.11 ? 941  GLY B N   1 
ATOM   19445 C  CA  . GLY C 1 941  ? 86.955  -9.603  99.112  1.00 189.48 ? 941  GLY B CA  1 
ATOM   19446 C  C   . GLY C 1 941  ? 87.779  -9.544  100.380 1.00 181.83 ? 941  GLY B C   1 
ATOM   19447 O  O   . GLY C 1 941  ? 87.592  -10.377 101.271 1.00 180.21 ? 941  GLY B O   1 
ATOM   19448 N  N   . VAL C 1 942  ? 88.691  -8.577  100.458 1.00 179.15 ? 942  VAL B N   1 
ATOM   19449 C  CA  . VAL C 1 942  ? 89.531  -8.395  101.636 1.00 169.94 ? 942  VAL B CA  1 
ATOM   19450 C  C   . VAL C 1 942  ? 89.534  -6.930  102.070 1.00 164.22 ? 942  VAL B C   1 
ATOM   19451 O  O   . VAL C 1 942  ? 89.113  -6.047  101.312 1.00 166.59 ? 942  VAL B O   1 
ATOM   19452 C  CB  . VAL C 1 942  ? 90.989  -8.774  101.341 1.00 168.71 ? 942  VAL B CB  1 
ATOM   19453 C  CG1 . VAL C 1 942  ? 91.681  -9.203  102.610 1.00 168.30 ? 942  VAL B CG1 1 
ATOM   19454 C  CG2 . VAL C 1 942  ? 91.054  -9.870  100.303 1.00 171.15 ? 942  VAL B CG2 1 
ATOM   19455 N  N   . THR C 1 943  ? 89.987  -6.668  103.292 1.00 105.98 ? 943  THR B N   1 
ATOM   19456 C  CA  . THR C 1 943  ? 90.491  -5.343  103.593 1.00 101.17 ? 943  THR B CA  1 
ATOM   19457 C  C   . THR C 1 943  ? 91.974  -5.520  103.833 1.00 101.23 ? 943  THR B C   1 
ATOM   19458 O  O   . THR C 1 943  ? 92.383  -6.371  104.607 1.00 102.17 ? 943  THR B O   1 
ATOM   19459 C  CB  . THR C 1 943  ? 89.816  -4.663  104.811 1.00 105.66 ? 943  THR B CB  1 
ATOM   19460 O  OG1 . THR C 1 943  ? 88.403  -4.903  104.802 1.00 105.53 ? 943  THR B OG1 1 
ATOM   19461 C  CG2 . THR C 1 943  ? 90.064  -3.148  104.769 1.00 101.95 ? 943  THR B CG2 1 
ATOM   19462 N  N   . LEU C 1 944  ? 92.789  -4.771  103.115 1.00 164.91 ? 944  LEU B N   1 
ATOM   19463 C  CA  . LEU C 1 944  ? 94.184  -4.718  103.477 1.00 163.14 ? 944  LEU B CA  1 
ATOM   19464 C  C   . LEU C 1 944  ? 94.309  -3.813  104.699 1.00 165.67 ? 944  LEU B C   1 
ATOM   19465 O  O   . LEU C 1 944  ? 93.886  -2.647  104.663 1.00 166.43 ? 944  LEU B O   1 
ATOM   19466 C  CB  . LEU C 1 944  ? 95.052  -4.241  102.312 1.00 162.24 ? 944  LEU B CB  1 
ATOM   19467 C  CG  . LEU C 1 944  ? 95.302  -5.370  101.320 1.00 161.97 ? 944  LEU B CG  1 
ATOM   19468 C  CD1 . LEU C 1 944  ? 96.517  -5.126  100.438 1.00 163.22 ? 944  LEU B CD1 1 
ATOM   19469 C  CD2 . LEU C 1 944  ? 95.490  -6.632  102.118 1.00 160.07 ? 944  LEU B CD2 1 
ATOM   19470 N  N   . ASP C 1 945  ? 94.854  -4.375  105.788 1.00 145.51 ? 945  ASP B N   1 
ATOM   19471 C  CA  . ASP C 1 945  ? 95.083  -3.656  107.053 1.00 143.34 ? 945  ASP B CA  1 
ATOM   19472 C  C   . ASP C 1 945  ? 96.435  -4.038  107.574 1.00 141.51 ? 945  ASP B C   1 
ATOM   19473 O  O   . ASP C 1 945  ? 96.575  -5.026  108.283 1.00 142.36 ? 945  ASP B O   1 
ATOM   19474 C  CB  . ASP C 1 945  ? 94.058  -4.026  108.119 1.00 142.75 ? 945  ASP B CB  1 
ATOM   19475 C  CG  . ASP C 1 945  ? 93.874  -2.931  109.138 1.00 140.66 ? 945  ASP B CG  1 
ATOM   19476 O  OD1 . ASP C 1 945  ? 94.590  -1.902  109.027 1.00 141.08 ? 945  ASP B OD1 1 
ATOM   19477 O  OD2 . ASP C 1 945  ? 93.002  -3.106  110.024 1.00 137.57 ? 945  ASP B OD2 1 
ATOM   19478 N  N   . PRO C 1 946  ? 97.439  -3.230  107.260 1.00 107.09 ? 946  PRO B N   1 
ATOM   19479 C  CA  . PRO C 1 946  ? 98.774  -3.693  107.613 1.00 109.37 ? 946  PRO B CA  1 
ATOM   19480 C  C   . PRO C 1 946  ? 98.999  -3.488  109.123 1.00 108.95 ? 946  PRO B C   1 
ATOM   19481 O  O   . PRO C 1 946  ? 99.679  -4.289  109.784 1.00 109.00 ? 946  PRO B O   1 
ATOM   19482 C  CB  . PRO C 1 946  ? 99.684  -2.750  106.813 1.00 110.27 ? 946  PRO B CB  1 
ATOM   19483 C  CG  . PRO C 1 946  ? 98.794  -1.660  106.248 1.00 108.92 ? 946  PRO B CG  1 
ATOM   19484 C  CD  . PRO C 1 946  ? 97.442  -1.808  106.892 1.00 111.40 ? 946  PRO B CD  1 
ATOM   19485 N  N   . ARG C 1 947  ? 98.417  -2.403  109.646 1.00 140.23 ? 947  ARG B N   1 
ATOM   19486 C  CA  . ARG C 1 947  ? 98.587  -1.986  111.037 1.00 139.40 ? 947  ARG B CA  1 
ATOM   19487 C  C   . ARG C 1 947  ? 97.535  -2.579  111.956 1.00 136.79 ? 947  ARG B C   1 
ATOM   19488 O  O   . ARG C 1 947  ? 97.187  -1.976  112.964 1.00 138.16 ? 947  ARG B O   1 
ATOM   19489 C  CB  . ARG C 1 947  ? 98.520  -0.468  111.139 1.00 140.22 ? 947  ARG B CB  1 
ATOM   19490 C  CG  . ARG C 1 947  ? 99.354  0.258   110.139 1.00 142.65 ? 947  ARG B CG  1 
ATOM   19491 C  CD  . ARG C 1 947  ? 100.697 0.662   110.721 1.00 143.52 ? 947  ARG B CD  1 
ATOM   19492 N  NE  . ARG C 1 947  ? 100.716 2.075   111.112 1.00 143.56 ? 947  ARG B NE  1 
ATOM   19493 C  CZ  . ARG C 1 947  ? 101.590 2.973   110.648 1.00 148.03 ? 947  ARG B CZ  1 
ATOM   19494 N  NH1 . ARG C 1 947  ? 102.527 2.609   109.769 1.00 150.40 ? 947  ARG B NH1 1 
ATOM   19495 N  NH2 . ARG C 1 947  ? 101.537 4.239   111.061 1.00 149.29 ? 947  ARG B NH2 1 
ATOM   19496 N  N   . GLY C 1 948  ? 97.000  -3.737  111.600 1.00 107.68 ? 948  GLY B N   1 
ATOM   19497 C  CA  . GLY C 1 948  ? 95.992  -4.373  112.432 1.00 104.76 ? 948  GLY B CA  1 
ATOM   19498 C  C   . GLY C 1 948  ? 94.834  -3.495  112.903 1.00 100.72 ? 948  GLY B C   1 
ATOM   19499 O  O   . GLY C 1 948  ? 93.846  -3.994  113.451 1.00 99.71  ? 948  GLY B O   1 
ATOM   19500 N  N   . ILE C 1 949  ? 94.961  -2.192  112.686 1.00 110.04 ? 949  ILE B N   1 
ATOM   19501 C  CA  . ILE C 1 949  ? 93.984  -1.187  113.099 1.00 102.68 ? 949  ILE B CA  1 
ATOM   19502 C  C   . ILE C 1 949  ? 92.535  -1.638  113.358 1.00 101.30 ? 949  ILE B C   1 
ATOM   19503 O  O   . ILE C 1 949  ? 91.879  -1.077  114.236 1.00 102.65 ? 949  ILE B O   1 
ATOM   19504 C  CB  . ILE C 1 949  ? 93.974  -0.014  112.072 1.00 104.67 ? 949  ILE B CB  1 
ATOM   19505 C  CG1 . ILE C 1 949  ? 95.418  0.424   111.753 1.00 113.77 ? 949  ILE B CG1 1 
ATOM   19506 C  CG2 . ILE C 1 949  ? 93.111  1.140   112.560 1.00 103.08 ? 949  ILE B CG2 1 
ATOM   19507 C  CD1 . ILE C 1 949  ? 95.594  1.886   111.229 1.00 113.06 ? 949  ILE B CD1 1 
ATOM   19508 N  N   . TYR C 1 950  ? 92.030  -2.630  112.616 1.00 154.24 ? 950  TYR B N   1 
ATOM   19509 C  CA  . TYR C 1 950  ? 90.601  -2.994  112.702 1.00 156.45 ? 950  TYR B CA  1 
ATOM   19510 C  C   . TYR C 1 950  ? 90.173  -4.257  113.495 1.00 156.76 ? 950  TYR B C   1 
ATOM   19511 O  O   . TYR C 1 950  ? 88.988  -4.410  113.834 1.00 159.26 ? 950  TYR B O   1 
ATOM   19512 C  CB  . TYR C 1 950  ? 89.929  -2.909  111.311 1.00 149.05 ? 950  TYR B CB  1 
ATOM   19513 C  CG  . TYR C 1 950  ? 89.464  -1.491  111.028 1.00 148.17 ? 950  TYR B CG  1 
ATOM   19514 C  CD1 . TYR C 1 950  ? 88.134  -1.120  111.222 1.00 144.91 ? 950  TYR B CD1 1 
ATOM   19515 C  CD2 . TYR C 1 950  ? 90.369  -0.506  110.628 1.00 148.65 ? 950  TYR B CD2 1 
ATOM   19516 C  CE1 . TYR C 1 950  ? 87.716  0.178   110.998 1.00 145.90 ? 950  TYR B CE1 1 
ATOM   19517 C  CE2 . TYR C 1 950  ? 89.957  0.797   110.402 1.00 150.57 ? 950  TYR B CE2 1 
ATOM   19518 C  CZ  . TYR C 1 950  ? 88.630  1.132   110.587 1.00 151.50 ? 950  TYR B CZ  1 
ATOM   19519 O  OH  . TYR C 1 950  ? 88.221  2.425   110.364 1.00 151.98 ? 950  TYR B OH  1 
ATOM   19520 N  N   . GLY C 1 951  ? 91.129  -5.129  113.818 1.00 112.05 ? 951  GLY B N   1 
ATOM   19521 C  CA  . GLY C 1 951  ? 90.831  -6.379  114.499 1.00 115.17 ? 951  GLY B CA  1 
ATOM   19522 C  C   . GLY C 1 951  ? 91.797  -7.499  114.131 1.00 119.49 ? 951  GLY B C   1 
ATOM   19523 O  O   . GLY C 1 951  ? 91.571  -8.655  114.483 1.00 120.76 ? 951  GLY B O   1 
ATOM   19524 N  N   . THR C 1 952  ? 92.830  -7.150  113.362 1.00 111.62 ? 952  THR B N   1 
ATOM   19525 C  CA  . THR C 1 952  ? 94.010  -7.995  113.027 1.00 111.32 ? 952  THR B CA  1 
ATOM   19526 C  C   . THR C 1 952  ? 94.842  -7.448  111.878 1.00 111.26 ? 952  THR B C   1 
ATOM   19527 O  O   . THR C 1 952  ? 94.399  -6.585  111.113 1.00 115.32 ? 952  THR B O   1 
ATOM   19528 C  CB  . THR C 1 952  ? 93.755  -9.509  112.671 1.00 111.01 ? 952  THR B CB  1 
ATOM   19529 O  OG1 . THR C 1 952  ? 94.867  -9.999  111.887 1.00 115.15 ? 952  THR B OG1 1 
ATOM   19530 C  CG2 . THR C 1 952  ? 92.450  -9.723  111.900 1.00 113.32 ? 952  THR B CG2 1 
ATOM   19531 N  N   . ILE C 1 953  ? 96.060  -7.960  111.762 1.00 145.03 ? 953  ILE B N   1 
ATOM   19532 C  CA  . ILE C 1 953  ? 96.893  -7.608  110.629 1.00 149.79 ? 953  ILE B CA  1 
ATOM   19533 C  C   . ILE C 1 953  ? 96.552  -8.431  109.374 1.00 160.60 ? 953  ILE B C   1 
ATOM   19534 O  O   . ILE C 1 953  ? 96.537  -9.669  109.428 1.00 163.65 ? 953  ILE B O   1 
ATOM   19535 C  CB  . ILE C 1 953  ? 98.374  -7.709  110.988 1.00 153.95 ? 953  ILE B CB  1 
ATOM   19536 C  CG1 . ILE C 1 953  ? 98.912  -9.106  110.719 1.00 155.31 ? 953  ILE B CG1 1 
ATOM   19537 C  CG2 . ILE C 1 953  ? 98.577  -7.340  112.441 1.00 156.36 ? 953  ILE B CG2 1 
ATOM   19538 C  CD1 . ILE C 1 953  ? 100.401 -9.132  110.706 1.00 156.33 ? 953  ILE B CD1 1 
ATOM   19539 N  N   . SER C 1 954  ? 96.271  -7.734  108.259 1.00 174.02 ? 954  SER B N   1 
ATOM   19540 C  CA  . SER C 1 954  ? 95.928  -8.370  106.971 1.00 169.47 ? 954  SER B CA  1 
ATOM   19541 C  C   . SER C 1 954  ? 96.882  -7.923  105.875 1.00 169.57 ? 954  SER B C   1 
ATOM   19542 O  O   . SER C 1 954  ? 96.889  -6.760  105.476 1.00 170.71 ? 954  SER B O   1 
ATOM   19543 C  CB  . SER C 1 954  ? 94.490  -8.055  106.548 1.00 163.41 ? 954  SER B CB  1 
ATOM   19544 O  OG  . SER C 1 954  ? 93.981  -9.079  105.712 1.00 162.39 ? 954  SER B OG  1 
ATOM   19545 N  N   . ARG C 1 955  ? 97.686  -8.859  105.393 1.00 152.93 ? 955  ARG B N   1 
ATOM   19546 C  CA  . ARG C 1 955  ? 98.676  -8.551  104.376 1.00 154.82 ? 955  ARG B CA  1 
ATOM   19547 C  C   . ARG C 1 955  ? 98.757  -9.648  103.317 1.00 159.83 ? 955  ARG B C   1 
ATOM   19548 O  O   . ARG C 1 955  ? 99.694  -9.657  102.510 1.00 164.07 ? 955  ARG B O   1 
ATOM   19549 C  CB  . ARG C 1 955  ? 100.059 -8.352  104.993 1.00 155.21 ? 955  ARG B CB  1 
ATOM   19550 C  CG  . ARG C 1 955  ? 100.237 -7.213  105.987 1.00 154.79 ? 955  ARG B CG  1 
ATOM   19551 C  CD  . ARG C 1 955  ? 101.650 -7.347  106.536 1.00 154.66 ? 955  ARG B CD  1 
ATOM   19552 N  NE  . ARG C 1 955  ? 101.965 -6.591  107.743 1.00 150.00 ? 955  ARG B NE  1 
ATOM   19553 C  CZ  . ARG C 1 955  ? 103.033 -6.840  108.505 1.00 149.63 ? 955  ARG B CZ  1 
ATOM   19554 N  NH1 . ARG C 1 955  ? 103.863 -7.831  108.187 1.00 151.78 ? 955  ARG B NH1 1 
ATOM   19555 N  NH2 . ARG C 1 955  ? 103.278 -6.113  109.592 1.00 153.24 ? 955  ARG B NH2 1 
ATOM   19556 N  N   . ARG C 1 956  ? 97.795  -10.575 103.340 1.00 125.16 ? 956  ARG B N   1 
ATOM   19557 C  CA  . ARG C 1 956  ? 97.679  -11.617 102.303 1.00 126.49 ? 956  ARG B CA  1 
ATOM   19558 C  C   . ARG C 1 956  ? 96.351  -12.406 102.386 1.00 131.57 ? 956  ARG B C   1 
ATOM   19559 O  O   . ARG C 1 956  ? 96.107  -13.151 103.364 1.00 129.67 ? 956  ARG B O   1 
ATOM   19560 C  CB  . ARG C 1 956  ? 98.885  -12.580 102.342 1.00 125.80 ? 956  ARG B CB  1 
ATOM   19561 C  CG  . ARG C 1 956  ? 99.434  -12.970 100.969 1.00 128.97 ? 956  ARG B CG  1 
ATOM   19562 C  CD  . ARG C 1 956  ? 100.616 -13.908 101.059 1.00 133.92 ? 956  ARG B CD  1 
ATOM   19563 N  NE  . ARG C 1 956  ? 100.193 -15.300 101.018 1.00 136.56 ? 956  ARG B NE  1 
ATOM   19564 C  CZ  . ARG C 1 956  ? 100.950 -16.289 100.569 1.00 140.71 ? 956  ARG B CZ  1 
ATOM   19565 N  NH1 . ARG C 1 956  ? 102.168 -16.034 100.115 1.00 142.94 ? 956  ARG B NH1 1 
ATOM   19566 N  NH2 . ARG C 1 956  ? 100.484 -17.529 100.574 1.00 141.37 ? 956  ARG B NH2 1 
ATOM   19567 N  N   . LYS C 1 957  ? 95.496  -12.210 101.372 1.00 143.70 ? 957  LYS B N   1 
ATOM   19568 C  CA  . LYS C 1 957  ? 94.299  -13.031 101.177 1.00 144.80 ? 957  LYS B CA  1 
ATOM   19569 C  C   . LYS C 1 957  ? 94.406  -13.707 99.824  1.00 144.37 ? 957  LYS B C   1 
ATOM   19570 O  O   . LYS C 1 957  ? 95.055  -13.187 98.914  1.00 142.31 ? 957  LYS B O   1 
ATOM   19571 C  CB  . LYS C 1 957  ? 92.996  -12.227 101.286 1.00 144.74 ? 957  LYS B CB  1 
ATOM   19572 C  CG  . LYS C 1 957  ? 91.749  -13.086 101.062 1.00 149.48 ? 957  LYS B CG  1 
ATOM   19573 C  CD  . LYS C 1 957  ? 90.588  -12.752 101.995 1.00 152.06 ? 957  LYS B CD  1 
ATOM   19574 C  CE  . LYS C 1 957  ? 89.936  -14.025 102.599 1.00 156.09 ? 957  LYS B CE  1 
ATOM   19575 N  NZ  . LYS C 1 957  ? 89.597  -15.126 101.640 1.00 160.26 ? 957  LYS B NZ  1 
ATOM   19576 N  N   . GLU C 1 958  ? 93.771  -14.869 99.707  1.00 150.32 ? 958  GLU B N   1 
ATOM   19577 C  CA  . GLU C 1 958  ? 93.948  -15.726 98.553  1.00 157.48 ? 958  GLU B CA  1 
ATOM   19578 C  C   . GLU C 1 958  ? 92.611  -16.081 97.909  1.00 158.72 ? 958  GLU B C   1 
ATOM   19579 O  O   . GLU C 1 958  ? 91.806  -16.824 98.479  1.00 158.71 ? 958  GLU B O   1 
ATOM   19580 C  CB  . GLU C 1 958  ? 94.688  -16.988 98.979  1.00 164.44 ? 958  GLU B CB  1 
ATOM   19581 C  CG  . GLU C 1 958  ? 95.064  -17.916 97.850  1.00 173.29 ? 958  GLU B CG  1 
ATOM   19582 C  CD  . GLU C 1 958  ? 95.815  -19.144 98.341  1.00 180.53 ? 958  GLU B CD  1 
ATOM   19583 O  OE1 . GLU C 1 958  ? 96.799  -18.981 99.105  1.00 182.84 ? 958  GLU B OE1 1 
ATOM   19584 O  OE2 . GLU C 1 958  ? 95.423  -20.271 97.963  1.00 183.00 ? 958  GLU B OE2 1 
ATOM   19585 N  N   . PHE C 1 959  ? 92.380  -15.513 96.727  1.00 169.62 ? 959  PHE B N   1 
ATOM   19586 C  CA  . PHE C 1 959  ? 91.259  -15.883 95.875  1.00 171.50 ? 959  PHE B CA  1 
ATOM   19587 C  C   . PHE C 1 959  ? 91.743  -16.916 94.877  1.00 178.70 ? 959  PHE B C   1 
ATOM   19588 O  O   . PHE C 1 959  ? 92.551  -16.602 94.002  1.00 181.55 ? 959  PHE B O   1 
ATOM   19589 C  CB  . PHE C 1 959  ? 90.782  -14.671 95.102  1.00 165.27 ? 959  PHE B CB  1 
ATOM   19590 C  CG  . PHE C 1 959  ? 90.805  -13.423 95.892  1.00 159.48 ? 959  PHE B CG  1 
ATOM   19591 C  CD1 . PHE C 1 959  ? 89.673  -12.995 96.540  1.00 157.46 ? 959  PHE B CD1 1 
ATOM   19592 C  CD2 . PHE C 1 959  ? 91.964  -12.686 96.007  1.00 157.01 ? 959  PHE B CD2 1 
ATOM   19593 C  CE1 . PHE C 1 959  ? 89.678  -11.850 97.275  1.00 154.73 ? 959  PHE B CE1 1 
ATOM   19594 C  CE2 . PHE C 1 959  ? 91.978  -11.537 96.750  1.00 154.60 ? 959  PHE B CE2 1 
ATOM   19595 C  CZ  . PHE C 1 959  ? 90.831  -11.119 97.385  1.00 153.43 ? 959  PHE B CZ  1 
ATOM   19596 N  N   . PRO C 1 960  ? 91.253  -18.156 94.998  1.00 172.76 ? 960  PRO B N   1 
ATOM   19597 C  CA  . PRO C 1 960  ? 91.722  -19.255 94.147  1.00 180.30 ? 960  PRO B CA  1 
ATOM   19598 C  C   . PRO C 1 960  ? 90.854  -19.474 92.909  1.00 189.70 ? 960  PRO B C   1 
ATOM   19599 O  O   . PRO C 1 960  ? 90.035  -18.629 92.541  1.00 189.35 ? 960  PRO B O   1 
ATOM   19600 C  CB  . PRO C 1 960  ? 91.610  -20.483 95.069  1.00 179.53 ? 960  PRO B CB  1 
ATOM   19601 C  CG  . PRO C 1 960  ? 91.090  -19.960 96.408  1.00 164.25 ? 960  PRO B CG  1 
ATOM   19602 C  CD  . PRO C 1 960  ? 90.430  -18.654 96.106  1.00 166.10 ? 960  PRO B CD  1 
ATOM   19603 N  N   . TYR C 1 961  ? 91.049  -20.631 92.282  1.00 227.22 ? 961  TYR B N   1 
ATOM   19604 C  CA  . TYR C 1 961  ? 90.187  -21.110 91.215  1.00 235.98 ? 961  TYR B CA  1 
ATOM   19605 C  C   . TYR C 1 961  ? 89.062  -21.960 91.772  1.00 238.96 ? 961  TYR B C   1 
ATOM   19606 O  O   . TYR C 1 961  ? 89.305  -22.904 92.528  1.00 240.44 ? 961  TYR B O   1 
ATOM   19607 C  CB  . TYR C 1 961  ? 90.994  -21.960 90.245  1.00 242.70 ? 961  TYR B CB  1 
ATOM   19608 C  CG  . TYR C 1 961  ? 91.032  -21.360 88.885  1.00 247.82 ? 961  TYR B CG  1 
ATOM   19609 C  CD1 . TYR C 1 961  ? 90.271  -21.883 87.854  1.00 251.35 ? 961  TYR B CD1 1 
ATOM   19610 C  CD2 . TYR C 1 961  ? 91.799  -20.239 88.636  1.00 248.76 ? 961  TYR B CD2 1 
ATOM   19611 C  CE1 . TYR C 1 961  ? 90.295  -21.317 86.599  1.00 253.95 ? 961  TYR B CE1 1 
ATOM   19612 C  CE2 . TYR C 1 961  ? 91.831  -19.666 87.393  1.00 252.07 ? 961  TYR B CE2 1 
ATOM   19613 C  CZ  . TYR C 1 961  ? 91.078  -20.206 86.375  1.00 255.01 ? 961  TYR B CZ  1 
ATOM   19614 O  OH  . TYR C 1 961  ? 91.105  -19.624 85.131  1.00 258.51 ? 961  TYR B OH  1 
ATOM   19615 N  N   . ARG C 1 962  ? 87.831  -21.634 91.398  1.00 228.09 ? 962  ARG B N   1 
ATOM   19616 C  CA  . ARG C 1 962  ? 86.698  -22.475 91.767  1.00 232.86 ? 962  ARG B CA  1 
ATOM   19617 C  C   . ARG C 1 962  ? 85.736  -22.626 90.601  1.00 231.51 ? 962  ARG B C   1 
ATOM   19618 O  O   . ARG C 1 962  ? 84.715  -21.943 90.533  1.00 228.34 ? 962  ARG B O   1 
ATOM   19619 C  CB  . ARG C 1 962  ? 85.959  -21.949 93.007  1.00 239.73 ? 962  ARG B CB  1 
ATOM   19620 C  CG  . ARG C 1 962  ? 84.567  -22.576 93.216  1.00 250.16 ? 962  ARG B CG  1 
ATOM   19621 C  CD  . ARG C 1 962  ? 84.412  -23.276 94.562  1.00 256.83 ? 962  ARG B CD  1 
ATOM   19622 N  NE  . ARG C 1 962  ? 83.478  -22.564 95.427  1.00 260.60 ? 962  ARG B NE  1 
ATOM   19623 C  CZ  . ARG C 1 962  ? 82.980  -23.053 96.559  1.00 263.29 ? 962  ARG B CZ  1 
ATOM   19624 N  NH1 . ARG C 1 962  ? 83.317  -24.272 96.971  1.00 265.47 ? 962  ARG B NH1 1 
ATOM   19625 N  NH2 . ARG C 1 962  ? 82.137  -22.321 97.276  1.00 262.37 ? 962  ARG B NH2 1 
ATOM   19626 N  N   . ILE C 1 963  ? 86.072  -23.527 89.683  1.00 207.92 ? 963  ILE B N   1 
ATOM   19627 C  CA  . ILE C 1 963  ? 85.232  -23.783 88.526  1.00 203.08 ? 963  ILE B CA  1 
ATOM   19628 C  C   . ILE C 1 963  ? 83.957  -24.503 88.951  1.00 203.62 ? 963  ILE B C   1 
ATOM   19629 O  O   . ILE C 1 963  ? 84.002  -25.666 89.378  1.00 204.10 ? 963  ILE B O   1 
ATOM   19630 C  CB  . ILE C 1 963  ? 85.966  -24.642 87.482  1.00 195.89 ? 963  ILE B CB  1 
ATOM   19631 C  CG1 . ILE C 1 963  ? 87.474  -24.377 87.517  1.00 190.25 ? 963  ILE B CG1 1 
ATOM   19632 C  CG2 . ILE C 1 963  ? 85.416  -24.370 86.098  1.00 197.50 ? 963  ILE B CG2 1 
ATOM   19633 C  CD1 . ILE C 1 963  ? 88.288  -25.341 86.659  1.00 190.72 ? 963  ILE B CD1 1 
ATOM   19634 N  N   . PRO C 1 964  ? 82.810  -23.817 88.832  1.00 181.68 ? 964  PRO B N   1 
ATOM   19635 C  CA  . PRO C 1 964  ? 81.528  -24.440 89.179  1.00 184.52 ? 964  PRO B CA  1 
ATOM   19636 C  C   . PRO C 1 964  ? 81.326  -25.663 88.286  1.00 191.89 ? 964  PRO B C   1 
ATOM   19637 O  O   . PRO C 1 964  ? 81.603  -25.564 87.092  1.00 194.10 ? 964  PRO B O   1 
ATOM   19638 C  CB  . PRO C 1 964  ? 80.497  -23.358 88.818  1.00 183.91 ? 964  PRO B CB  1 
ATOM   19639 C  CG  . PRO C 1 964  ? 81.271  -22.094 88.626  1.00 178.44 ? 964  PRO B CG  1 
ATOM   19640 C  CD  . PRO C 1 964  ? 82.644  -22.494 88.208  1.00 178.91 ? 964  PRO B CD  1 
ATOM   19641 N  N   . LEU C 1 965  ? 80.861  -26.789 88.818  1.00 221.06 ? 965  LEU B N   1 
ATOM   19642 C  CA  . LEU C 1 965  ? 80.665  -27.969 87.965  1.00 230.59 ? 965  LEU B CA  1 
ATOM   19643 C  C   . LEU C 1 965  ? 79.501  -27.836 86.955  1.00 235.80 ? 965  LEU B C   1 
ATOM   19644 O  O   . LEU C 1 965  ? 79.106  -28.813 86.309  1.00 240.19 ? 965  LEU B O   1 
ATOM   19645 C  CB  . LEU C 1 965  ? 80.550  -29.249 88.798  1.00 233.85 ? 965  LEU B CB  1 
ATOM   19646 C  CG  . LEU C 1 965  ? 81.752  -29.618 89.673  1.00 246.74 ? 965  LEU B CG  1 
ATOM   19647 C  CD1 . LEU C 1 965  ? 81.568  -31.014 90.261  1.00 248.77 ? 965  LEU B CD1 1 
ATOM   19648 C  CD2 . LEU C 1 965  ? 83.075  -29.537 88.911  1.00 248.10 ? 965  LEU B CD2 1 
ATOM   19649 N  N   . ASP C 1 966  ? 78.964  -26.624 86.829  1.00 223.08 ? 966  ASP B N   1 
ATOM   19650 C  CA  . ASP C 1 966  ? 77.932  -26.314 85.845  1.00 223.00 ? 966  ASP B CA  1 
ATOM   19651 C  C   . ASP C 1 966  ? 78.475  -25.424 84.738  1.00 215.52 ? 966  ASP B C   1 
ATOM   19652 O  O   . ASP C 1 966  ? 77.700  -24.855 83.974  1.00 217.02 ? 966  ASP B O   1 
ATOM   19653 C  CB  . ASP C 1 966  ? 76.766  -25.574 86.503  1.00 225.32 ? 966  ASP B CB  1 
ATOM   19654 C  CG  . ASP C 1 966  ? 75.640  -26.495 86.915  1.00 228.92 ? 966  ASP B CG  1 
ATOM   19655 O  OD1 . ASP C 1 966  ? 75.719  -27.709 86.633  1.00 231.84 ? 966  ASP B OD1 1 
ATOM   19656 O  OD2 . ASP C 1 966  ? 74.672  -25.996 87.522  1.00 228.02 ? 966  ASP B OD2 1 
ATOM   19657 N  N   . LEU C 1 967  ? 79.792  -25.267 84.661  1.00 187.05 ? 967  LEU B N   1 
ATOM   19658 C  CA  . LEU C 1 967  ? 80.360  -24.333 83.692  1.00 181.66 ? 967  LEU B CA  1 
ATOM   19659 C  C   . LEU C 1 967  ? 79.904  -24.680 82.269  1.00 180.73 ? 967  LEU B C   1 
ATOM   19660 O  O   . LEU C 1 967  ? 79.746  -25.859 81.929  1.00 183.87 ? 967  LEU B O   1 
ATOM   19661 C  CB  . LEU C 1 967  ? 81.889  -24.310 83.772  1.00 180.15 ? 967  LEU B CB  1 
ATOM   19662 C  CG  . LEU C 1 967  ? 82.573  -23.540 82.640  1.00 182.18 ? 967  LEU B CG  1 
ATOM   19663 C  CD1 . LEU C 1 967  ? 82.122  -22.085 82.582  1.00 181.99 ? 967  LEU B CD1 1 
ATOM   19664 C  CD2 . LEU C 1 967  ? 84.079  -23.644 82.749  1.00 180.93 ? 967  LEU B CD2 1 
ATOM   19665 N  N   . VAL C 1 968  ? 79.679  -23.660 81.442  1.00 185.00 ? 968  VAL B N   1 
ATOM   19666 C  CA  . VAL C 1 968  ? 79.336  -23.874 80.034  1.00 183.13 ? 968  VAL B CA  1 
ATOM   19667 C  C   . VAL C 1 968  ? 80.607  -24.072 79.193  1.00 183.52 ? 968  VAL B C   1 
ATOM   19668 O  O   . VAL C 1 968  ? 81.276  -23.107 78.836  1.00 180.96 ? 968  VAL B O   1 
ATOM   19669 C  CB  . VAL C 1 968  ? 78.539  -22.697 79.516  1.00 179.72 ? 968  VAL B CB  1 
ATOM   19670 C  CG1 . VAL C 1 968  ? 77.230  -22.619 80.243  1.00 177.25 ? 968  VAL B CG1 1 
ATOM   19671 C  CG2 . VAL C 1 968  ? 79.305  -21.422 79.754  1.00 177.19 ? 968  VAL B CG2 1 
ATOM   19672 N  N   . PRO C 1 969  ? 80.924  -25.329 78.850  1.00 214.04 ? 969  PRO B N   1 
ATOM   19673 C  CA  . PRO C 1 969  ? 82.300  -25.726 78.509  1.00 216.95 ? 969  PRO B CA  1 
ATOM   19674 C  C   . PRO C 1 969  ? 83.038  -24.781 77.559  1.00 222.12 ? 969  PRO B C   1 
ATOM   19675 O  O   . PRO C 1 969  ? 82.419  -24.042 76.796  1.00 223.47 ? 969  PRO B O   1 
ATOM   19676 C  CB  . PRO C 1 969  ? 82.123  -27.109 77.885  1.00 219.59 ? 969  PRO B CB  1 
ATOM   19677 C  CG  . PRO C 1 969  ? 80.843  -27.616 78.469  1.00 218.75 ? 969  PRO B CG  1 
ATOM   19678 C  CD  . PRO C 1 969  ? 79.959  -26.409 78.595  1.00 216.54 ? 969  PRO B CD  1 
ATOM   19679 N  N   . LYS C 1 970  ? 84.365  -24.807 77.641  1.00 223.50 ? 970  LYS B N   1 
ATOM   19680 C  CA  . LYS C 1 970  ? 85.224  -23.988 76.792  1.00 231.58 ? 970  LYS B CA  1 
ATOM   19681 C  C   . LYS C 1 970  ? 84.989  -22.478 76.887  1.00 232.71 ? 970  LYS B C   1 
ATOM   19682 O  O   . LYS C 1 970  ? 85.383  -21.742 75.990  1.00 233.00 ? 970  LYS B O   1 
ATOM   19683 C  CB  . LYS C 1 970  ? 85.123  -24.425 75.328  1.00 241.38 ? 970  LYS B CB  1 
ATOM   19684 C  CG  . LYS C 1 970  ? 86.137  -25.481 74.890  1.00 250.65 ? 970  LYS B CG  1 
ATOM   19685 C  CD  . LYS C 1 970  ? 86.110  -25.657 73.360  1.00 260.33 ? 970  LYS B CD  1 
ATOM   19686 C  CE  . LYS C 1 970  ? 87.111  -26.709 72.873  1.00 266.08 ? 970  LYS B CE  1 
ATOM   19687 N  NZ  . LYS C 1 970  ? 87.266  -26.722 71.389  1.00 270.50 ? 970  LYS B NZ  1 
ATOM   19688 N  N   . THR C 1 971  ? 84.347  -22.015 77.956  1.00 211.05 ? 971  THR B N   1 
ATOM   19689 C  CA  . THR C 1 971  ? 84.247  -20.577 78.212  1.00 212.17 ? 971  THR B CA  1 
ATOM   19690 C  C   . THR C 1 971  ? 85.036  -20.197 79.438  1.00 208.39 ? 971  THR B C   1 
ATOM   19691 O  O   . THR C 1 971  ? 84.787  -20.708 80.529  1.00 209.01 ? 971  THR B O   1 
ATOM   19692 C  CB  . THR C 1 971  ? 82.818  -20.132 78.480  1.00 214.46 ? 971  THR B CB  1 
ATOM   19693 O  OG1 . THR C 1 971  ? 82.477  -20.409 79.845  1.00 210.86 ? 971  THR B OG1 1 
ATOM   19694 C  CG2 . THR C 1 971  ? 81.879  -20.850 77.557  1.00 220.22 ? 971  THR B CG2 1 
ATOM   19695 N  N   . GLU C 1 972  ? 85.963  -19.270 79.264  1.00 266.15 ? 972  GLU B N   1 
ATOM   19696 C  CA  . GLU C 1 972  ? 86.841  -18.861 80.346  1.00 260.96 ? 972  GLU B CA  1 
ATOM   19697 C  C   . GLU C 1 972  ? 86.123  -18.131 81.497  1.00 249.06 ? 972  GLU B C   1 
ATOM   19698 O  O   . GLU C 1 972  ? 85.142  -17.409 81.268  1.00 245.28 ? 972  GLU B O   1 
ATOM   19699 C  CB  . GLU C 1 972  ? 87.957  -18.002 79.769  1.00 269.51 ? 972  GLU B CB  1 
ATOM   19700 C  CG  . GLU C 1 972  ? 87.636  -17.460 78.386  1.00 279.70 ? 972  GLU B CG  1 
ATOM   19701 C  CD  . GLU C 1 972  ? 88.857  -16.895 77.699  1.00 286.38 ? 972  GLU B CD  1 
ATOM   19702 O  OE1 . GLU C 1 972  ? 89.845  -16.600 78.402  1.00 286.15 ? 972  GLU B OE1 1 
ATOM   19703 O  OE2 . GLU C 1 972  ? 88.833  -16.747 76.460  1.00 291.08 ? 972  GLU B OE2 1 
ATOM   19704 N  N   . ILE C 1 973  ? 86.624  -18.346 82.724  1.00 164.05 ? 973  ILE B N   1 
ATOM   19705 C  CA  . ILE C 1 973  ? 86.143  -17.674 83.944  1.00 154.41 ? 973  ILE B CA  1 
ATOM   19706 C  C   . ILE C 1 973  ? 86.829  -16.307 84.137  1.00 156.79 ? 973  ILE B C   1 
ATOM   19707 O  O   . ILE C 1 973  ? 88.001  -16.221 84.539  1.00 158.43 ? 973  ILE B O   1 
ATOM   19708 C  CB  . ILE C 1 973  ? 86.301  -18.545 85.242  1.00 140.90 ? 973  ILE B CB  1 
ATOM   19709 C  CG1 . ILE C 1 973  ? 86.409  -20.046 84.948  1.00 139.66 ? 973  ILE B CG1 1 
ATOM   19710 C  CG2 . ILE C 1 973  ? 85.141  -18.310 86.139  1.00 135.23 ? 973  ILE B CG2 1 
ATOM   19711 C  CD1 . ILE C 1 973  ? 86.080  -20.937 86.139  1.00 137.59 ? 973  ILE B CD1 1 
ATOM   19712 N  N   . LYS C 1 974  ? 86.083  -15.246 83.846  1.00 199.59 ? 974  LYS B N   1 
ATOM   19713 C  CA  . LYS C 1 974  ? 86.622  -13.897 83.828  1.00 196.77 ? 974  LYS B CA  1 
ATOM   19714 C  C   . LYS C 1 974  ? 86.387  -13.198 85.148  1.00 187.94 ? 974  LYS B C   1 
ATOM   19715 O  O   . LYS C 1 974  ? 85.265  -13.199 85.648  1.00 186.85 ? 974  LYS B O   1 
ATOM   19716 C  CB  . LYS C 1 974  ? 85.950  -13.111 82.713  1.00 202.37 ? 974  LYS B CB  1 
ATOM   19717 C  CG  . LYS C 1 974  ? 85.859  -11.618 82.943  1.00 207.34 ? 974  LYS B CG  1 
ATOM   19718 C  CD  . LYS C 1 974  ? 85.206  -10.966 81.733  1.00 216.24 ? 974  LYS B CD  1 
ATOM   19719 C  CE  . LYS C 1 974  ? 85.100  -9.464  81.883  1.00 218.97 ? 974  LYS B CE  1 
ATOM   19720 N  NZ  . LYS C 1 974  ? 84.372  -8.893  80.714  1.00 221.85 ? 974  LYS B NZ  1 
ATOM   19721 N  N   . ARG C 1 975  ? 87.432  -12.586 85.706  1.00 147.35 ? 975  ARG B N   1 
ATOM   19722 C  CA  . ARG C 1 975  ? 87.313  -11.947 87.021  1.00 139.66 ? 975  ARG B CA  1 
ATOM   19723 C  C   . ARG C 1 975  ? 88.077  -10.638 87.210  1.00 133.75 ? 975  ARG B C   1 
ATOM   19724 O  O   . ARG C 1 975  ? 89.173  -10.454 86.698  1.00 135.18 ? 975  ARG B O   1 
ATOM   19725 C  CB  . ARG C 1 975  ? 87.705  -12.939 88.093  1.00 136.44 ? 975  ARG B CB  1 
ATOM   19726 C  CG  . ARG C 1 975  ? 88.871  -13.784 87.705  1.00 135.79 ? 975  ARG B CG  1 
ATOM   19727 C  CD  . ARG C 1 975  ? 88.739  -15.124 88.382  1.00 134.32 ? 975  ARG B CD  1 
ATOM   19728 N  NE  . ARG C 1 975  ? 90.037  -15.673 88.765  1.00 134.38 ? 975  ARG B NE  1 
ATOM   19729 C  CZ  . ARG C 1 975  ? 90.240  -16.513 89.792  1.00 132.10 ? 975  ARG B CZ  1 
ATOM   19730 N  NH1 . ARG C 1 975  ? 89.231  -16.916 90.577  1.00 129.20 ? 975  ARG B NH1 1 
ATOM   19731 N  NH2 . ARG C 1 975  ? 91.469  -16.957 90.052  1.00 132.82 ? 975  ARG B NH2 1 
ATOM   19732 N  N   . ILE C 1 976  ? 87.464  -9.738  87.970  1.00 137.15 ? 976  ILE B N   1 
ATOM   19733 C  CA  . ILE C 1 976  ? 88.040  -8.431  88.233  1.00 132.19 ? 976  ILE B CA  1 
ATOM   19734 C  C   . ILE C 1 976  ? 88.521  -8.364  89.658  1.00 127.47 ? 976  ILE B C   1 
ATOM   19735 O  O   . ILE C 1 976  ? 88.131  -9.189  90.479  1.00 128.37 ? 976  ILE B O   1 
ATOM   19736 C  CB  . ILE C 1 976  ? 87.029  -7.296  88.054  1.00 131.95 ? 976  ILE B CB  1 
ATOM   19737 C  CG1 . ILE C 1 976  ? 85.882  -7.776  87.176  1.00 137.72 ? 976  ILE B CG1 1 
ATOM   19738 C  CG2 . ILE C 1 976  ? 87.747  -6.040  87.541  1.00 130.63 ? 976  ILE B CG2 1 
ATOM   19739 C  CD1 . ILE C 1 976  ? 84.671  -6.864  87.121  1.00 141.18 ? 976  ILE B CD1 1 
ATOM   19740 N  N   . LEU C 1 977  ? 89.306  -7.322  89.951  1.00 142.42 ? 977  LEU B N   1 
ATOM   19741 C  CA  . LEU C 1 977  ? 90.162  -7.216  91.137  1.00 134.23 ? 977  LEU B CA  1 
ATOM   19742 C  C   . LEU C 1 977  ? 90.357  -5.746  91.461  1.00 132.58 ? 977  LEU B C   1 
ATOM   19743 O  O   . LEU C 1 977  ? 91.316  -5.129  90.994  1.00 135.01 ? 977  LEU B O   1 
ATOM   19744 C  CB  . LEU C 1 977  ? 91.500  -7.809  90.764  1.00 133.47 ? 977  LEU B CB  1 
ATOM   19745 C  CG  . LEU C 1 977  ? 92.654  -7.953  91.712  1.00 133.58 ? 977  LEU B CG  1 
ATOM   19746 C  CD1 . LEU C 1 977  ? 92.633  -9.356  92.224  1.00 132.52 ? 977  LEU B CD1 1 
ATOM   19747 C  CD2 . LEU C 1 977  ? 93.893  -7.709  90.884  1.00 138.21 ? 977  LEU B CD2 1 
ATOM   19748 N  N   . SER C 1 978  ? 89.443  -5.184  92.248  1.00 148.03 ? 978  SER B N   1 
ATOM   19749 C  CA  . SER C 1 978  ? 89.428  -3.743  92.493  1.00 152.82 ? 978  SER B CA  1 
ATOM   19750 C  C   . SER C 1 978  ? 90.134  -3.347  93.785  1.00 160.11 ? 978  SER B C   1 
ATOM   19751 O  O   . SER C 1 978  ? 89.639  -3.626  94.883  1.00 163.49 ? 978  SER B O   1 
ATOM   19752 C  CB  . SER C 1 978  ? 87.998  -3.226  92.539  1.00 151.62 ? 978  SER B CB  1 
ATOM   19753 O  OG  . SER C 1 978  ? 88.003  -1.817  92.639  1.00 143.69 ? 978  SER B OG  1 
ATOM   19754 N  N   . VAL C 1 979  ? 91.274  -2.674  93.656  1.00 123.56 ? 979  VAL B N   1 
ATOM   19755 C  CA  . VAL C 1 979  ? 92.081  -2.340  94.821  1.00 118.97 ? 979  VAL B CA  1 
ATOM   19756 C  C   . VAL C 1 979  ? 92.174  -0.829  95.002  1.00 118.12 ? 979  VAL B C   1 
ATOM   19757 O  O   . VAL C 1 979  ? 92.773  -0.136  94.176  1.00 121.86 ? 979  VAL B O   1 
ATOM   19758 C  CB  . VAL C 1 979  ? 93.526  -2.887  94.698  1.00 117.45 ? 979  VAL B CB  1 
ATOM   19759 C  CG1 . VAL C 1 979  ? 94.082  -3.145  96.052  1.00 114.25 ? 979  VAL B CG1 1 
ATOM   19760 C  CG2 . VAL C 1 979  ? 93.567  -4.165  93.917  1.00 118.86 ? 979  VAL B CG2 1 
ATOM   19761 N  N   . LYS C 1 980  ? 91.604  -0.317  96.087  1.00 181.00 ? 980  LYS B N   1 
ATOM   19762 C  CA  . LYS C 1 980  ? 91.661  1.121   96.339  1.00 182.66 ? 980  LYS B CA  1 
ATOM   19763 C  C   . LYS C 1 980  ? 91.850  1.503   97.815  1.00 179.93 ? 980  LYS B C   1 
ATOM   19764 O  O   . LYS C 1 980  ? 91.262  0.890   98.703  1.00 179.72 ? 980  LYS B O   1 
ATOM   19765 C  CB  . LYS C 1 980  ? 90.418  1.810   95.779  1.00 184.30 ? 980  LYS B CB  1 
ATOM   19766 C  CG  . LYS C 1 980  ? 89.238  0.879   95.555  1.00 185.16 ? 980  LYS B CG  1 
ATOM   19767 C  CD  . LYS C 1 980  ? 89.290  0.305   94.156  1.00 185.93 ? 980  LYS B CD  1 
ATOM   19768 C  CE  . LYS C 1 980  ? 89.299  1.434   93.139  1.00 184.31 ? 980  LYS B CE  1 
ATOM   19769 N  NZ  . LYS C 1 980  ? 89.487  0.986   91.730  1.00 185.39 ? 980  LYS B NZ  1 
ATOM   19770 N  N   . GLY C 1 981  ? 92.676  2.520   98.066  1.00 133.61 ? 981  GLY B N   1 
ATOM   19771 C  CA  . GLY C 1 981  ? 92.847  3.060   99.404  1.00 129.74 ? 981  GLY B CA  1 
ATOM   19772 C  C   . GLY C 1 981  ? 91.577  3.700   99.936  1.00 126.64 ? 981  GLY B C   1 
ATOM   19773 O  O   . GLY C 1 981  ? 90.871  4.390   99.207  1.00 128.00 ? 981  GLY B O   1 
ATOM   19774 N  N   . LEU C 1 982  ? 91.282  3.464   101.208 1.00 107.31 ? 982  LEU B N   1 
ATOM   19775 C  CA  . LEU C 1 982  ? 90.108  4.042   101.858 1.00 105.29 ? 982  LEU B CA  1 
ATOM   19776 C  C   . LEU C 1 982  ? 88.864  3.156   101.833 1.00 108.54 ? 982  LEU B C   1 
ATOM   19777 O  O   . LEU C 1 982  ? 88.616  2.457   100.849 1.00 109.25 ? 982  LEU B O   1 
ATOM   19778 C  CB  . LEU C 1 982  ? 89.764  5.365   101.216 1.00 102.95 ? 982  LEU B CB  1 
ATOM   19779 C  CG  . LEU C 1 982  ? 90.713  6.528   101.483 1.00 113.93 ? 982  LEU B CG  1 
ATOM   19780 C  CD1 . LEU C 1 982  ? 90.085  7.436   102.537 1.00 101.05 ? 982  LEU B CD1 1 
ATOM   19781 C  CD2 . LEU C 1 982  ? 92.110  6.072   101.864 1.00 113.46 ? 982  LEU B CD2 1 
ATOM   19782 N  N   . LEU C 1 983  ? 88.090  3.197   102.924 1.00 153.09 ? 983  LEU B N   1 
ATOM   19783 C  CA  . LEU C 1 983  ? 86.837  2.442   103.051 1.00 154.78 ? 983  LEU B CA  1 
ATOM   19784 C  C   . LEU C 1 983  ? 85.780  3.218   102.341 1.00 162.69 ? 983  LEU B C   1 
ATOM   19785 O  O   . LEU C 1 983  ? 84.588  2.923   102.427 1.00 162.09 ? 983  LEU B O   1 
ATOM   19786 C  CB  . LEU C 1 983  ? 86.399  2.320   104.506 1.00 149.59 ? 983  LEU B CB  1 
ATOM   19787 C  CG  . LEU C 1 983  ? 87.162  1.474   105.532 1.00 147.87 ? 983  LEU B CG  1 
ATOM   19788 C  CD1 . LEU C 1 983  ? 88.412  0.790   104.983 1.00 147.23 ? 983  LEU B CD1 1 
ATOM   19789 C  CD2 . LEU C 1 983  ? 87.526  2.363   106.682 1.00 148.53 ? 983  LEU B CD2 1 
ATOM   19790 N  N   . VAL C 1 984  ? 86.244  4.253   101.669 1.00 130.32 ? 984  VAL B N   1 
ATOM   19791 C  CA  . VAL C 1 984  ? 85.379  5.142   100.951 1.00 131.88 ? 984  VAL B CA  1 
ATOM   19792 C  C   . VAL C 1 984  ? 86.057  5.439   99.601  1.00 144.07 ? 984  VAL B C   1 
ATOM   19793 O  O   . VAL C 1 984  ? 85.764  6.431   98.948  1.00 143.39 ? 984  VAL B O   1 
ATOM   19794 C  CB  . VAL C 1 984  ? 85.101  6.391   101.816 1.00 131.43 ? 984  VAL B CB  1 
ATOM   19795 C  CG1 . VAL C 1 984  ? 86.375  7.213   101.999 1.00 131.29 ? 984  VAL B CG1 1 
ATOM   19796 C  CG2 . VAL C 1 984  ? 83.931  7.205   101.257 1.00 129.82 ? 984  VAL B CG2 1 
ATOM   19797 N  N   . GLY C 1 985  ? 86.959  4.542   99.193  1.00 194.54 ? 985  GLY B N   1 
ATOM   19798 C  CA  . GLY C 1 985  ? 87.653  4.624   97.912  1.00 195.17 ? 985  GLY B CA  1 
ATOM   19799 C  C   . GLY C 1 985  ? 86.988  3.962   96.702  1.00 196.53 ? 985  GLY B C   1 
ATOM   19800 O  O   . GLY C 1 985  ? 87.272  4.313   95.554  1.00 201.48 ? 985  GLY B O   1 
ATOM   19801 N  N   . GLU C 1 986  ? 86.118  2.989   96.946  1.00 136.18 ? 986  GLU B N   1 
ATOM   19802 C  CA  . GLU C 1 986  ? 85.363  2.347   95.875  1.00 136.60 ? 986  GLU B CA  1 
ATOM   19803 C  C   . GLU C 1 986  ? 84.213  3.250   95.528  1.00 134.61 ? 986  GLU B C   1 
ATOM   19804 O  O   . GLU C 1 986  ? 83.831  3.381   94.380  1.00 138.74 ? 986  GLU B O   1 
ATOM   19805 C  CB  . GLU C 1 986  ? 84.831  0.989   96.335  1.00 138.23 ? 986  GLU B CB  1 
ATOM   19806 C  CG  . GLU C 1 986  ? 84.601  -0.024  95.216  1.00 143.36 ? 986  GLU B CG  1 
ATOM   19807 C  CD  . GLU C 1 986  ? 85.837  -0.254  94.344  1.00 148.33 ? 986  GLU B CD  1 
ATOM   19808 O  OE1 . GLU C 1 986  ? 86.136  -1.425  94.013  1.00 150.23 ? 986  GLU B OE1 1 
ATOM   19809 O  OE2 . GLU C 1 986  ? 86.507  0.739   93.994  1.00 150.18 ? 986  GLU B OE2 1 
ATOM   19810 N  N   . ILE C 1 987  ? 83.669  3.878   96.555  1.00 127.93 ? 987  ILE B N   1 
ATOM   19811 C  CA  . ILE C 1 987  ? 82.674  4.915   96.388  1.00 125.86 ? 987  ILE B CA  1 
ATOM   19812 C  C   . ILE C 1 987  ? 83.296  6.184   95.761  1.00 129.17 ? 987  ILE B C   1 
ATOM   19813 O  O   . ILE C 1 987  ? 82.585  6.971   95.138  1.00 130.17 ? 987  ILE B O   1 
ATOM   19814 C  CB  . ILE C 1 987  ? 81.949  5.190   97.731  1.00 121.39 ? 987  ILE B CB  1 
ATOM   19815 C  CG1 . ILE C 1 987  ? 81.254  3.921   98.211  1.00 127.13 ? 987  ILE B CG1 1 
ATOM   19816 C  CG2 . ILE C 1 987  ? 80.911  6.305   97.619  1.00 115.64 ? 987  ILE B CG2 1 
ATOM   19817 C  CD1 . ILE C 1 987  ? 80.759  4.028   99.641  1.00 129.60 ? 987  ILE B CD1 1 
ATOM   19818 N  N   . LEU C 1 988  ? 84.612  6.374   95.896  1.00 111.47 ? 988  LEU B N   1 
ATOM   19819 C  CA  . LEU C 1 988  ? 85.296  7.498   95.225  1.00 113.01 ? 988  LEU B CA  1 
ATOM   19820 C  C   . LEU C 1 988  ? 85.552  7.217   93.735  1.00 117.65 ? 988  LEU B C   1 
ATOM   19821 O  O   . LEU C 1 988  ? 85.235  8.058   92.896  1.00 120.83 ? 988  LEU B O   1 
ATOM   19822 C  CB  . LEU C 1 988  ? 86.617  7.895   95.930  1.00 112.93 ? 988  LEU B CB  1 
ATOM   19823 C  CG  . LEU C 1 988  ? 86.664  9.111   96.875  1.00 110.61 ? 988  LEU B CG  1 
ATOM   19824 C  CD1 . LEU C 1 988  ? 88.106  9.500   97.236  1.00 111.35 ? 988  LEU B CD1 1 
ATOM   19825 C  CD2 . LEU C 1 988  ? 85.923  10.274  96.262  1.00 107.84 ? 988  LEU B CD2 1 
ATOM   19826 N  N   . SER C 1 989  ? 86.093  6.032   93.418  1.00 136.43 ? 989  SER B N   1 
ATOM   19827 C  CA  . SER C 1 989  ? 86.426  5.634   92.034  1.00 138.36 ? 989  SER B CA  1 
ATOM   19828 C  C   . SER C 1 989  ? 85.212  5.566   91.085  1.00 136.82 ? 989  SER B C   1 
ATOM   19829 O  O   . SER C 1 989  ? 85.291  5.976   89.921  1.00 137.21 ? 989  SER B O   1 
ATOM   19830 C  CB  . SER C 1 989  ? 87.198  4.300   92.018  1.00 142.92 ? 989  SER B CB  1 
ATOM   19831 O  OG  . SER C 1 989  ? 87.725  4.015   90.730  1.00 148.33 ? 989  SER B OG  1 
ATOM   19832 N  N   . ALA C 1 990  ? 84.101  5.037   91.589  1.00 176.82 ? 990  ALA B N   1 
ATOM   19833 C  CA  . ALA C 1 990  ? 82.852  5.041   90.849  1.00 178.83 ? 990  ALA B CA  1 
ATOM   19834 C  C   . ALA C 1 990  ? 82.638  6.428   90.245  1.00 178.26 ? 990  ALA B C   1 
ATOM   19835 O  O   . ALA C 1 990  ? 82.671  6.614   89.028  1.00 183.36 ? 990  ALA B O   1 
ATOM   19836 C  CB  . ALA C 1 990  ? 81.699  4.672   91.769  1.00 177.94 ? 990  ALA B CB  1 
ATOM   19837 N  N   . VAL C 1 991  ? 82.442  7.406   91.109  1.00 121.94 ? 991  VAL B N   1 
ATOM   19838 C  CA  . VAL C 1 991  ? 82.076  8.743   90.676  1.00 122.64 ? 991  VAL B CA  1 
ATOM   19839 C  C   . VAL C 1 991  ? 83.203  9.537   89.984  1.00 125.76 ? 991  VAL B C   1 
ATOM   19840 O  O   . VAL C 1 991  ? 82.964  10.628  89.486  1.00 127.27 ? 991  VAL B O   1 
ATOM   19841 C  CB  . VAL C 1 991  ? 81.423  9.498   91.874  1.00 96.17  ? 991  VAL B CB  1 
ATOM   19842 C  CG1 . VAL C 1 991  ? 81.278  10.998  91.647  1.00 95.09  ? 991  VAL B CG1 1 
ATOM   19843 C  CG2 . VAL C 1 991  ? 80.078  8.862   92.180  1.00 96.79  ? 991  VAL B CG2 1 
ATOM   19844 N  N   . LEU C 1 992  ? 84.416  8.990   89.905  1.00 142.10 ? 992  LEU B N   1 
ATOM   19845 C  CA  . LEU C 1 992  ? 85.533  9.775   89.344  1.00 148.65 ? 992  LEU B CA  1 
ATOM   19846 C  C   . LEU C 1 992  ? 86.460  9.020   88.407  1.00 167.40 ? 992  LEU B C   1 
ATOM   19847 O  O   . LEU C 1 992  ? 87.685  9.049   88.565  1.00 173.02 ? 992  LEU B O   1 
ATOM   19848 C  CB  . LEU C 1 992  ? 86.371  10.451  90.441  1.00 138.86 ? 992  LEU B CB  1 
ATOM   19849 C  CG  . LEU C 1 992  ? 85.722  11.464  91.393  1.00 130.82 ? 992  LEU B CG  1 
ATOM   19850 C  CD1 . LEU C 1 992  ? 86.699  11.845  92.480  1.00 126.65 ? 992  LEU B CD1 1 
ATOM   19851 C  CD2 . LEU C 1 992  ? 85.218  12.722  90.676  1.00 131.05 ? 992  LEU B CD2 1 
ATOM   19852 N  N   . SER C 1 993  ? 85.878  8.368   87.414  1.00 202.25 ? 993  SER B N   1 
ATOM   19853 C  CA  . SER C 1 993  ? 86.656  7.563   86.496  1.00 213.81 ? 993  SER B CA  1 
ATOM   19854 C  C   . SER C 1 993  ? 85.803  7.324   85.281  1.00 225.55 ? 993  SER B C   1 
ATOM   19855 O  O   . SER C 1 993  ? 86.313  7.243   84.171  1.00 230.18 ? 993  SER B O   1 
ATOM   19856 C  CB  . SER C 1 993  ? 87.032  6.234   87.143  1.00 213.26 ? 993  SER B CB  1 
ATOM   19857 O  OG  . SER C 1 993  ? 87.846  6.443   88.287  1.00 210.63 ? 993  SER B OG  1 
ATOM   19858 N  N   . GLN C 1 994  ? 84.501  7.172   85.509  1.00 179.26 ? 994  GLN B N   1 
ATOM   19859 C  CA  . GLN C 1 994  ? 83.517  7.376   84.458  1.00 189.11 ? 994  GLN B CA  1 
ATOM   19860 C  C   . GLN C 1 994  ? 83.047  8.804   84.648  1.00 188.60 ? 994  GLN B C   1 
ATOM   19861 O  O   . GLN C 1 994  ? 83.293  9.405   85.695  1.00 183.04 ? 994  GLN B O   1 
ATOM   19862 C  CB  . GLN C 1 994  ? 82.330  6.397   84.558  1.00 194.53 ? 994  GLN B CB  1 
ATOM   19863 C  CG  . GLN C 1 994  ? 81.458  6.575   85.806  1.00 195.16 ? 994  GLN B CG  1 
ATOM   19864 C  CD  . GLN C 1 994  ? 79.962  6.443   85.539  1.00 198.60 ? 994  GLN B CD  1 
ATOM   19865 O  OE1 . GLN C 1 994  ? 79.539  5.979   84.482  1.00 203.12 ? 994  GLN B OE1 1 
ATOM   19866 N  NE2 . GLN C 1 994  ? 79.156  6.850   86.510  1.00 195.51 ? 994  GLN B NE2 1 
ATOM   19867 N  N   . GLU C 1 995  ? 82.417  9.366   83.632  1.00 192.82 ? 995  GLU B N   1 
ATOM   19868 C  CA  . GLU C 1 995  ? 81.713  10.609  83.820  1.00 196.46 ? 995  GLU B CA  1 
ATOM   19869 C  C   . GLU C 1 995  ? 80.250  10.243  83.890  1.00 196.98 ? 995  GLU B C   1 
ATOM   19870 O  O   . GLU C 1 995  ? 79.904  9.061   83.884  1.00 196.86 ? 995  GLU B O   1 
ATOM   19871 C  CB  . GLU C 1 995  ? 81.990  11.584  82.677  1.00 203.03 ? 995  GLU B CB  1 
ATOM   19872 C  CG  . GLU C 1 995  ? 83.048  12.639  82.997  1.00 205.49 ? 995  GLU B CG  1 
ATOM   19873 C  CD  . GLU C 1 995  ? 84.248  12.599  82.057  1.00 210.55 ? 995  GLU B CD  1 
ATOM   19874 O  OE1 . GLU C 1 995  ? 84.314  11.688  81.200  1.00 214.12 ? 995  GLU B OE1 1 
ATOM   19875 O  OE2 . GLU C 1 995  ? 85.125  13.485  82.179  1.00 210.68 ? 995  GLU B OE2 1 
ATOM   19876 N  N   . GLY C 1 996  ? 79.398  11.254  83.972  1.00 222.53 ? 996  GLY B N   1 
ATOM   19877 C  CA  . GLY C 1 996  ? 77.968  11.034  83.986  1.00 225.37 ? 996  GLY B CA  1 
ATOM   19878 C  C   . GLY C 1 996  ? 77.505  10.203  85.163  1.00 225.19 ? 996  GLY B C   1 
ATOM   19879 O  O   . GLY C 1 996  ? 78.011  9.106   85.417  1.00 225.82 ? 996  GLY B O   1 
ATOM   19880 N  N   . ILE C 1 997  ? 76.521  10.733  85.878  1.00 231.13 ? 997  ILE B N   1 
ATOM   19881 C  CA  . ILE C 1 997  ? 75.918  10.040  87.006  1.00 229.91 ? 997  ILE B CA  1 
ATOM   19882 C  C   . ILE C 1 997  ? 75.476  8.635   86.569  1.00 235.59 ? 997  ILE B C   1 
ATOM   19883 O  O   . ILE C 1 997  ? 75.226  8.409   85.389  1.00 239.24 ? 997  ILE B O   1 
ATOM   19884 C  CB  . ILE C 1 997  ? 74.737  10.858  87.538  1.00 224.60 ? 997  ILE B CB  1 
ATOM   19885 C  CG1 . ILE C 1 997  ? 73.561  10.782  86.572  1.00 226.30 ? 997  ILE B CG1 1 
ATOM   19886 C  CG2 . ILE C 1 997  ? 75.146  12.319  87.704  1.00 222.90 ? 997  ILE B CG2 1 
ATOM   19887 C  CD1 . ILE C 1 997  ? 72.494  11.805  86.848  1.00 224.74 ? 997  ILE B CD1 1 
ATOM   19888 N  N   . ASN C 1 998  ? 75.386  7.691   87.502  1.00 223.30 ? 998  ASN B N   1 
ATOM   19889 C  CA  . ASN C 1 998  ? 75.180  6.290   87.126  1.00 226.51 ? 998  ASN B CA  1 
ATOM   19890 C  C   . ASN C 1 998  ? 74.710  5.386   88.274  1.00 219.20 ? 998  ASN B C   1 
ATOM   19891 O  O   . ASN C 1 998  ? 75.227  5.484   89.382  1.00 219.50 ? 998  ASN B O   1 
ATOM   19892 C  CB  . ASN C 1 998  ? 76.475  5.742   86.509  1.00 235.58 ? 998  ASN B CB  1 
ATOM   19893 C  CG  . ASN C 1 998  ? 76.662  4.253   86.743  1.00 242.86 ? 998  ASN B CG  1 
ATOM   19894 O  OD1 . ASN C 1 998  ? 75.811  3.442   86.386  1.00 247.18 ? 998  ASN B OD1 1 
ATOM   19895 N  ND2 . ASN C 1 998  ? 77.795  3.886   87.331  1.00 244.35 ? 998  ASN B ND2 1 
ATOM   19896 N  N   . ILE C 1 999  ? 73.735  4.510   88.004  1.00 211.99 ? 999  ILE B N   1 
ATOM   19897 C  CA  . ILE C 1 999  ? 73.217  3.555   89.005  1.00 201.66 ? 999  ILE B CA  1 
ATOM   19898 C  C   . ILE C 1 999  ? 74.252  2.486   89.332  1.00 192.98 ? 999  ILE B C   1 
ATOM   19899 O  O   . ILE C 1 999  ? 74.969  2.008   88.449  1.00 191.64 ? 999  ILE B O   1 
ATOM   19900 C  CB  . ILE C 1 999  ? 71.922  2.844   88.542  1.00 314.61 ? 999  ILE B CB  1 
ATOM   19901 C  CG1 . ILE C 1 999  ? 70.884  3.865   88.077  1.00 314.96 ? 999  ILE B CG1 1 
ATOM   19902 C  CG2 . ILE C 1 999  ? 71.355  1.976   89.665  1.00 313.15 ? 999  ILE B CG2 1 
ATOM   19903 C  CD1 . ILE C 1 999  ? 70.451  4.813   89.157  1.00 311.97 ? 999  ILE B CD1 1 
ATOM   19904 N  N   . LEU C 1 1000 ? 74.330  2.102   90.598  1.00 199.77 ? 1000 LEU B N   1 
ATOM   19905 C  CA  . LEU C 1 1000 ? 75.420  1.232   91.023  1.00 192.04 ? 1000 LEU B CA  1 
ATOM   19906 C  C   . LEU C 1 1000 ? 75.042  -0.228  91.117  1.00 191.07 ? 1000 LEU B C   1 
ATOM   19907 O  O   . LEU C 1 1000 ? 75.732  -1.029  91.742  1.00 190.94 ? 1000 LEU B O   1 
ATOM   19908 C  CB  . LEU C 1 1000 ? 76.031  1.721   92.328  1.00 182.15 ? 1000 LEU B CB  1 
ATOM   19909 C  CG  . LEU C 1 1000 ? 77.041  2.844   92.081  1.00 171.68 ? 1000 LEU B CG  1 
ATOM   19910 C  CD1 . LEU C 1 1000 ? 77.634  3.276   93.383  1.00 166.79 ? 1000 LEU B CD1 1 
ATOM   19911 C  CD2 . LEU C 1 1000 ? 78.138  2.399   91.128  1.00 170.88 ? 1000 LEU B CD2 1 
ATOM   19912 N  N   . THR C 1 1001 ? 73.950  -0.578  90.471  1.00 201.03 ? 1001 THR B N   1 
ATOM   19913 C  CA  . THR C 1 1001 ? 73.563  -1.962  90.426  1.00 202.10 ? 1001 THR B CA  1 
ATOM   19914 C  C   . THR C 1 1001 ? 73.182  -2.258  89.000  1.00 209.34 ? 1001 THR B C   1 
ATOM   19915 O  O   . THR C 1 1001 ? 73.306  -1.396  88.140  1.00 212.05 ? 1001 THR B O   1 
ATOM   19916 C  CB  . THR C 1 1001 ? 72.372  -2.184  91.325  1.00 193.66 ? 1001 THR B CB  1 
ATOM   19917 O  OG1 . THR C 1 1001 ? 72.258  -1.068  92.218  1.00 185.55 ? 1001 THR B OG1 1 
ATOM   19918 C  CG2 . THR C 1 1001 ? 72.551  -3.462  92.111  1.00 193.83 ? 1001 THR B CG2 1 
ATOM   19919 N  N   . HIS C 1 1002 ? 72.737  -3.476  88.737  1.00 183.42 ? 1002 HIS B N   1 
ATOM   19920 C  CA  . HIS C 1 1002 ? 72.177  -3.781  87.438  1.00 190.43 ? 1002 HIS B CA  1 
ATOM   19921 C  C   . HIS C 1 1002 ? 70.676  -3.496  87.434  1.00 165.15 ? 1002 HIS B C   1 
ATOM   19922 O  O   . HIS C 1 1002 ? 70.005  -3.670  86.424  1.00 168.77 ? 1002 HIS B O   1 
ATOM   19923 C  CB  . HIS C 1 1002 ? 72.472  -5.226  87.053  1.00 201.72 ? 1002 HIS B CB  1 
ATOM   19924 C  CG  . HIS C 1 1002 ? 73.908  -5.480  86.699  1.00 210.38 ? 1002 HIS B CG  1 
ATOM   19925 N  ND1 . HIS C 1 1002 ? 74.851  -5.837  87.636  1.00 211.96 ? 1002 HIS B ND1 1 
ATOM   19926 C  CD2 . HIS C 1 1002 ? 74.557  -5.436  85.511  1.00 216.08 ? 1002 HIS B CD2 1 
ATOM   19927 C  CE1 . HIS C 1 1002 ? 76.021  -6.000  87.042  1.00 214.73 ? 1002 HIS B CE1 1 
ATOM   19928 N  NE2 . HIS C 1 1002 ? 75.870  -5.764  85.754  1.00 217.15 ? 1002 HIS B NE2 1 
ATOM   19929 N  N   . LEU C 1 1003 ? 70.162  -3.023  88.563  1.00 151.10 ? 1003 LEU B N   1 
ATOM   19930 C  CA  . LEU C 1 1003 ? 68.732  -2.699  88.706  1.00 146.08 ? 1003 LEU B CA  1 
ATOM   19931 C  C   . LEU C 1 1003 ? 68.097  -1.717  87.679  1.00 149.17 ? 1003 LEU B C   1 
ATOM   19932 O  O   . LEU C 1 1003 ? 68.620  -0.635  87.422  1.00 151.41 ? 1003 LEU B O   1 
ATOM   19933 C  CB  . LEU C 1 1003 ? 68.430  -2.279  90.152  1.00 134.34 ? 1003 LEU B CB  1 
ATOM   19934 C  CG  . LEU C 1 1003 ? 68.403  -3.521  91.024  1.00 127.49 ? 1003 LEU B CG  1 
ATOM   19935 C  CD1 . LEU C 1 1003 ? 67.133  -3.564  91.822  1.00 122.07 ? 1003 LEU B CD1 1 
ATOM   19936 C  CD2 . LEU C 1 1003 ? 68.514  -4.765  90.148  1.00 129.66 ? 1003 LEU B CD2 1 
ATOM   19937 N  N   . PRO C 1 1004 ? 66.941  -2.109  87.127  1.00 179.90 ? 1004 PRO B N   1 
ATOM   19938 C  CA  . PRO C 1 1004 ? 66.080  -1.479  86.122  1.00 178.85 ? 1004 PRO B CA  1 
ATOM   19939 C  C   . PRO C 1 1004 ? 65.656  -0.059  86.454  1.00 174.95 ? 1004 PRO B C   1 
ATOM   19940 O  O   . PRO C 1 1004 ? 65.197  0.196   87.567  1.00 172.10 ? 1004 PRO B O   1 
ATOM   19941 C  CB  . PRO C 1 1004 ? 64.834  -2.365  86.155  1.00 183.40 ? 1004 PRO B CB  1 
ATOM   19942 C  CG  . PRO C 1 1004 ? 64.942  -3.164  87.423  1.00 180.16 ? 1004 PRO B CG  1 
ATOM   19943 C  CD  . PRO C 1 1004 ? 66.387  -3.404  87.543  1.00 179.11 ? 1004 PRO B CD  1 
ATOM   19944 N  N   . LYS C 1 1005 ? 65.747  0.829   85.468  1.00 151.17 ? 1005 LYS B N   1 
ATOM   19945 C  CA  . LYS C 1 1005 ? 65.527  2.261   85.676  1.00 153.11 ? 1005 LYS B CA  1 
ATOM   19946 C  C   . LYS C 1 1005 ? 64.063  2.652   85.950  1.00 152.52 ? 1005 LYS B C   1 
ATOM   19947 O  O   . LYS C 1 1005 ? 63.739  3.833   86.154  1.00 148.62 ? 1005 LYS B O   1 
ATOM   19948 C  CB  . LYS C 1 1005 ? 66.083  3.048   84.485  1.00 160.27 ? 1005 LYS B CB  1 
ATOM   19949 C  CG  . LYS C 1 1005 ? 67.595  2.921   84.291  1.00 168.09 ? 1005 LYS B CG  1 
ATOM   19950 C  CD  . LYS C 1 1005 ? 68.365  3.835   85.243  1.00 171.23 ? 1005 LYS B CD  1 
ATOM   19951 C  CE  . LYS C 1 1005 ? 67.862  5.278   85.168  1.00 174.40 ? 1005 LYS B CE  1 
ATOM   19952 N  NZ  . LYS C 1 1005 ? 68.599  6.180   86.110  1.00 172.63 ? 1005 LYS B NZ  1 
ATOM   19953 N  N   . GLY C 1 1006 ? 63.194  1.649   85.991  1.00 167.24 ? 1006 GLY B N   1 
ATOM   19954 C  CA  . GLY C 1 1006 ? 61.756  1.871   85.983  1.00 170.28 ? 1006 GLY B CA  1 
ATOM   19955 C  C   . GLY C 1 1006 ? 61.205  2.929   86.921  1.00 163.57 ? 1006 GLY B C   1 
ATOM   19956 O  O   . GLY C 1 1006 ? 60.603  3.920   86.489  1.00 161.18 ? 1006 GLY B O   1 
ATOM   19957 N  N   . SER C 1 1007 ? 61.417  2.704   88.213  1.00 178.53 ? 1007 SER B N   1 
ATOM   19958 C  CA  . SER C 1 1007 ? 60.852  3.533   89.275  1.00 173.45 ? 1007 SER B CA  1 
ATOM   19959 C  C   . SER C 1 1007 ? 61.278  4.979   89.171  1.00 166.76 ? 1007 SER B C   1 
ATOM   19960 O  O   . SER C 1 1007 ? 61.946  5.381   88.211  1.00 163.96 ? 1007 SER B O   1 
ATOM   19961 C  CB  . SER C 1 1007 ? 61.271  2.994   90.654  1.00 173.39 ? 1007 SER B CB  1 
ATOM   19962 O  OG  . SER C 1 1007 ? 60.820  3.831   91.706  1.00 172.64 ? 1007 SER B OG  1 
ATOM   19963 N  N   . ALA C 1 1008 ? 60.858  5.755   90.165  1.00 146.15 ? 1008 ALA B N   1 
ATOM   19964 C  CA  . ALA C 1 1008 ? 61.444  7.054   90.425  1.00 144.65 ? 1008 ALA B CA  1 
ATOM   19965 C  C   . ALA C 1 1008 ? 62.696  6.823   91.264  1.00 140.75 ? 1008 ALA B C   1 
ATOM   19966 O  O   . ALA C 1 1008 ? 63.793  7.258   90.915  1.00 140.56 ? 1008 ALA B O   1 
ATOM   19967 C  CB  . ALA C 1 1008 ? 60.455  7.936   91.172  1.00 145.35 ? 1008 ALA B CB  1 
ATOM   19968 N  N   . GLU C 1 1009 ? 62.506  6.112   92.366  1.00 149.50 ? 1009 GLU B N   1 
ATOM   19969 C  CA  . GLU C 1 1009 ? 63.591  5.669   93.209  1.00 146.82 ? 1009 GLU B CA  1 
ATOM   19970 C  C   . GLU C 1 1009 ? 64.865  5.603   92.399  1.00 145.24 ? 1009 GLU B C   1 
ATOM   19971 O  O   . GLU C 1 1009 ? 65.834  6.297   92.689  1.00 144.23 ? 1009 GLU B O   1 
ATOM   19972 C  CB  . GLU C 1 1009 ? 63.271  4.267   93.740  1.00 146.05 ? 1009 GLU B CB  1 
ATOM   19973 C  CG  . GLU C 1 1009 ? 64.076  3.878   94.980  1.00 139.83 ? 1009 GLU B CG  1 
ATOM   19974 C  CD  . GLU C 1 1009 ? 63.716  2.531   95.544  1.00 138.10 ? 1009 GLU B CD  1 
ATOM   19975 O  OE1 . GLU C 1 1009 ? 62.814  1.863   94.996  1.00 138.60 ? 1009 GLU B OE1 1 
ATOM   19976 O  OE2 . GLU C 1 1009 ? 64.352  2.150   96.542  1.00 136.62 ? 1009 GLU B OE2 1 
ATOM   19977 N  N   . ALA C 1 1010 ? 64.848  4.766   91.372  1.00 166.49 ? 1010 ALA B N   1 
ATOM   19978 C  CA  . ALA C 1 1010 ? 66.038  4.520   90.580  1.00 169.88 ? 1010 ALA B CA  1 
ATOM   19979 C  C   . ALA C 1 1010 ? 66.601  5.808   89.996  1.00 166.88 ? 1010 ALA B C   1 
ATOM   19980 O  O   . ALA C 1 1010 ? 67.811  6.006   89.961  1.00 162.36 ? 1010 ALA B O   1 
ATOM   19981 C  CB  . ALA C 1 1010 ? 65.730  3.535   89.486  1.00 177.00 ? 1010 ALA B CB  1 
ATOM   19982 N  N   . GLU C 1 1011 ? 65.721  6.685   89.534  1.00 211.70 ? 1011 GLU B N   1 
ATOM   19983 C  CA  . GLU C 1 1011 ? 66.157  7.966   88.997  1.00 214.06 ? 1011 GLU B CA  1 
ATOM   19984 C  C   . GLU C 1 1011 ? 66.727  8.864   90.100  1.00 210.60 ? 1011 GLU B C   1 
ATOM   19985 O  O   . GLU C 1 1011 ? 67.402  9.856   89.805  1.00 210.76 ? 1011 GLU B O   1 
ATOM   19986 C  CB  . GLU C 1 1011 ? 65.016  8.672   88.251  1.00 218.22 ? 1011 GLU B CB  1 
ATOM   19987 C  CG  . GLU C 1 1011 ? 65.411  9.312   86.905  1.00 221.10 ? 1011 GLU B CG  1 
ATOM   19988 C  CD  . GLU C 1 1011 ? 65.519  8.306   85.762  1.00 225.86 ? 1011 GLU B CD  1 
ATOM   19989 O  OE1 . GLU C 1 1011 ? 64.634  7.435   85.632  1.00 228.83 ? 1011 GLU B OE1 1 
ATOM   19990 O  OE2 . GLU C 1 1011 ? 66.490  8.392   84.984  1.00 227.13 ? 1011 GLU B OE2 1 
ATOM   19991 N  N   . LEU C 1 1012 ? 66.444  8.525   91.363  1.00 114.73 ? 1012 LEU B N   1 
ATOM   19992 C  CA  . LEU C 1 1012 ? 67.077  9.194   92.522  1.00 107.59 ? 1012 LEU B CA  1 
ATOM   19993 C  C   . LEU C 1 1012 ? 68.399  8.528   92.872  1.00 109.72 ? 1012 LEU B C   1 
ATOM   19994 O  O   . LEU C 1 1012 ? 69.349  9.188   93.266  1.00 109.93 ? 1012 LEU B O   1 
ATOM   19995 C  CB  . LEU C 1 1012 ? 66.140  9.197   93.731  1.00 99.90  ? 1012 LEU B CB  1 
ATOM   19996 C  CG  . LEU C 1 1012 ? 65.081  10.308  93.749  1.00 97.24  ? 1012 LEU B CG  1 
ATOM   19997 C  CD1 . LEU C 1 1012 ? 63.797  9.901   94.471  1.00 95.90  ? 1012 LEU B CD1 1 
ATOM   19998 C  CD2 . LEU C 1 1012 ? 65.694  11.581  94.317  1.00 94.96  ? 1012 LEU B CD2 1 
ATOM   19999 N  N   . MET C 1 1013 ? 68.467  7.214   92.691  1.00 171.44 ? 1013 MET B N   1 
ATOM   20000 C  CA  . MET C 1 1013 ? 69.677  6.485   93.049  1.00 171.11 ? 1013 MET B CA  1 
ATOM   20001 C  C   . MET C 1 1013 ? 70.853  6.881   92.176  1.00 174.90 ? 1013 MET B C   1 
ATOM   20002 O  O   . MET C 1 1013 ? 71.935  6.301   92.283  1.00 176.56 ? 1013 MET B O   1 
ATOM   20003 C  CB  . MET C 1 1013 ? 69.474  4.978   92.978  1.00 171.56 ? 1013 MET B CB  1 
ATOM   20004 C  CG  . MET C 1 1013 ? 70.200  4.289   94.072  1.00 170.87 ? 1013 MET B CG  1 
ATOM   20005 S  SD  . MET C 1 1013 ? 69.686  5.159   95.555  1.00 189.28 ? 1013 MET B SD  1 
ATOM   20006 C  CE  . MET C 1 1013 ? 67.980  4.625   95.733  1.00 168.88 ? 1013 MET B CE  1 
ATOM   20007 N  N   . SER C 1 1014 ? 70.622  7.862   91.308  1.00 146.51 ? 1014 SER B N   1 
ATOM   20008 C  CA  . SER C 1 1014 ? 71.652  8.407   90.437  1.00 146.90 ? 1014 SER B CA  1 
ATOM   20009 C  C   . SER C 1 1014 ? 72.394  9.525   91.156  1.00 139.06 ? 1014 SER B C   1 
ATOM   20010 O  O   . SER C 1 1014 ? 73.614  9.669   91.014  1.00 135.87 ? 1014 SER B O   1 
ATOM   20011 C  CB  . SER C 1 1014 ? 71.037  8.933   89.115  1.00 155.31 ? 1014 SER B CB  1 
ATOM   20012 O  OG  . SER C 1 1014 ? 70.286  10.137  89.288  1.00 157.32 ? 1014 SER B OG  1 
ATOM   20013 N  N   . VAL C 1 1015 ? 71.649  10.314  91.927  1.00 140.41 ? 1015 VAL B N   1 
ATOM   20014 C  CA  . VAL C 1 1015 ? 72.215  11.493  92.578  1.00 139.77 ? 1015 VAL B CA  1 
ATOM   20015 C  C   . VAL C 1 1015 ? 73.091  11.141  93.769  1.00 138.93 ? 1015 VAL B C   1 
ATOM   20016 O  O   . VAL C 1 1015 ? 74.028  11.875  94.119  1.00 141.02 ? 1015 VAL B O   1 
ATOM   20017 C  CB  . VAL C 1 1015 ? 71.124  12.493  93.035  1.00 145.81 ? 1015 VAL B CB  1 
ATOM   20018 C  CG1 . VAL C 1 1015 ? 69.785  11.801  93.204  1.00 145.71 ? 1015 VAL B CG1 1 
ATOM   20019 C  CG2 . VAL C 1 1015 ? 71.567  13.215  94.321  1.00 144.56 ? 1015 VAL B CG2 1 
ATOM   20020 N  N   . VAL C 1 1016 ? 72.787  10.006  94.382  1.00 112.89 ? 1016 VAL B N   1 
ATOM   20021 C  CA  . VAL C 1 1016 ? 73.497  9.564   95.573  1.00 103.89 ? 1016 VAL B CA  1 
ATOM   20022 C  C   . VAL C 1 1016 ? 74.998  9.377   95.381  1.00 98.01  ? 1016 VAL B C   1 
ATOM   20023 O  O   . VAL C 1 1016 ? 75.733  10.249  95.792  1.00 93.20  ? 1016 VAL B O   1 
ATOM   20024 C  CB  . VAL C 1 1016 ? 72.824  8.340   96.205  1.00 101.82 ? 1016 VAL B CB  1 
ATOM   20025 C  CG1 . VAL C 1 1016 ? 73.822  7.515   97.010  1.00 100.10 ? 1016 VAL B CG1 1 
ATOM   20026 C  CG2 . VAL C 1 1016 ? 71.656  8.786   97.057  1.00 101.10 ? 1016 VAL B CG2 1 
ATOM   20027 N  N   . PRO C 1 1017 ? 75.460  8.278   94.738  1.00 108.39 ? 1017 PRO B N   1 
ATOM   20028 C  CA  . PRO C 1 1017 ? 76.922  8.115   94.700  1.00 109.89 ? 1017 PRO B CA  1 
ATOM   20029 C  C   . PRO C 1 1017 ? 77.770  9.384   94.502  1.00 111.03 ? 1017 PRO B C   1 
ATOM   20030 O  O   . PRO C 1 1017 ? 78.907  9.356   94.961  1.00 108.95 ? 1017 PRO B O   1 
ATOM   20031 C  CB  . PRO C 1 1017 ? 77.136  7.130   93.545  1.00 111.11 ? 1017 PRO B CB  1 
ATOM   20032 C  CG  . PRO C 1 1017 ? 75.938  6.284   93.601  1.00 111.47 ? 1017 PRO B CG  1 
ATOM   20033 C  CD  . PRO C 1 1017 ? 74.786  7.166   94.035  1.00 110.62 ? 1017 PRO B CD  1 
ATOM   20034 N  N   . VAL C 1 1018 ? 77.282  10.450  93.862  1.00 109.30 ? 1018 VAL B N   1 
ATOM   20035 C  CA  . VAL C 1 1018 ? 78.044  11.706  93.898  1.00 116.12 ? 1018 VAL B CA  1 
ATOM   20036 C  C   . VAL C 1 1018 ? 77.834  12.391  95.234  1.00 116.87 ? 1018 VAL B C   1 
ATOM   20037 O  O   . VAL C 1 1018 ? 78.782  12.530  96.006  1.00 115.49 ? 1018 VAL B O   1 
ATOM   20038 C  CB  . VAL C 1 1018 ? 77.663  12.674  92.809  1.00 122.18 ? 1018 VAL B CB  1 
ATOM   20039 C  CG1 . VAL C 1 1018 ? 78.711  13.785  92.712  1.00 123.92 ? 1018 VAL B CG1 1 
ATOM   20040 C  CG2 . VAL C 1 1018 ? 77.554  11.916  91.509  1.00 126.09 ? 1018 VAL B CG2 1 
ATOM   20041 N  N   . PHE C 1 1019 ? 76.596  12.791  95.533  1.00 147.38 ? 1019 PHE B N   1 
ATOM   20042 C  CA  . PHE C 1 1019 ? 76.342  13.566  96.759  1.00 144.71 ? 1019 PHE B CA  1 
ATOM   20043 C  C   . PHE C 1 1019 ? 77.237  13.196  97.938  1.00 139.63 ? 1019 PHE B C   1 
ATOM   20044 O  O   . PHE C 1 1019 ? 77.958  14.050  98.466  1.00 138.80 ? 1019 PHE B O   1 
ATOM   20045 C  CB  . PHE C 1 1019 ? 74.888  13.470  97.221  1.00 145.87 ? 1019 PHE B CB  1 
ATOM   20046 C  CG  . PHE C 1 1019 ? 74.696  13.879  98.658  1.00 142.25 ? 1019 PHE B CG  1 
ATOM   20047 C  CD1 . PHE C 1 1019 ? 75.052  15.152  99.083  1.00 139.58 ? 1019 PHE B CD1 1 
ATOM   20048 C  CD2 . PHE C 1 1019 ? 74.182  12.991  99.579  1.00 139.95 ? 1019 PHE B CD2 1 
ATOM   20049 C  CE1 . PHE C 1 1019 ? 74.890  15.524  100.384 1.00 137.31 ? 1019 PHE B CE1 1 
ATOM   20050 C  CE2 . PHE C 1 1019 ? 74.018  13.363  100.881 1.00 137.95 ? 1019 PHE B CE2 1 
ATOM   20051 C  CZ  . PHE C 1 1019 ? 74.369  14.627  101.283 1.00 137.38 ? 1019 PHE B CZ  1 
ATOM   20052 N  N   . TYR C 1 1020 ? 77.174  11.934  98.359  1.00 105.52 ? 1020 TYR B N   1 
ATOM   20053 C  CA  . TYR C 1 1020 ? 78.040  11.469  99.431  1.00 102.22 ? 1020 TYR B CA  1 
ATOM   20054 C  C   . TYR C 1 1020 ? 79.490  11.774  99.111  1.00 100.06 ? 1020 TYR B C   1 
ATOM   20055 O  O   . TYR C 1 1020 ? 80.220  12.302  99.957  1.00 99.45  ? 1020 TYR B O   1 
ATOM   20056 C  CB  . TYR C 1 1020 ? 77.850  9.990   99.694  1.00 104.12 ? 1020 TYR B CB  1 
ATOM   20057 C  CG  . TYR C 1 1020 ? 76.519  9.750   100.307 1.00 107.53 ? 1020 TYR B CG  1 
ATOM   20058 C  CD1 . TYR C 1 1020 ? 75.744  10.814  100.731 1.00 109.70 ? 1020 TYR B CD1 1 
ATOM   20059 C  CD2 . TYR C 1 1020 ? 76.024  8.472   100.460 1.00 111.20 ? 1020 TYR B CD2 1 
ATOM   20060 C  CE1 . TYR C 1 1020 ? 74.511  10.619  101.294 1.00 112.98 ? 1020 TYR B CE1 1 
ATOM   20061 C  CE2 . TYR C 1 1020 ? 74.779  8.257   101.018 1.00 113.95 ? 1020 TYR B CE2 1 
ATOM   20062 C  CZ  . TYR C 1 1020 ? 74.022  9.340   101.440 1.00 116.07 ? 1020 TYR B CZ  1 
ATOM   20063 O  OH  . TYR C 1 1020 ? 72.773  9.132   102.006 1.00 119.67 ? 1020 TYR B OH  1 
ATOM   20064 N  N   . VAL C 1 1021 ? 79.907  11.467  97.889  1.00 89.07  ? 1021 VAL B N   1 
ATOM   20065 C  CA  . VAL C 1 1021 ? 81.277  11.744  97.474  1.00 88.74  ? 1021 VAL B CA  1 
ATOM   20066 C  C   . VAL C 1 1021 ? 81.626  13.261  97.477  1.00 86.81  ? 1021 VAL B C   1 
ATOM   20067 O  O   . VAL C 1 1021 ? 82.786  13.639  97.560  1.00 84.82  ? 1021 VAL B O   1 
ATOM   20068 C  CB  . VAL C 1 1021 ? 81.614  10.964  96.169  1.00 81.33  ? 1021 VAL B CB  1 
ATOM   20069 C  CG1 . VAL C 1 1021 ? 82.924  11.413  95.560  1.00 80.66  ? 1021 VAL B CG1 1 
ATOM   20070 C  CG2 . VAL C 1 1021 ? 81.677  9.493   96.483  1.00 82.29  ? 1021 VAL B CG2 1 
ATOM   20071 N  N   . PHE C 1 1022 ? 80.629  14.132  97.445  1.00 109.15 ? 1022 PHE B N   1 
ATOM   20072 C  CA  . PHE C 1 1022 ? 80.926  15.551  97.522  1.00 113.08 ? 1022 PHE B CA  1 
ATOM   20073 C  C   . PHE C 1 1022 ? 80.955  15.936  98.973  1.00 113.93 ? 1022 PHE B C   1 
ATOM   20074 O  O   . PHE C 1 1022 ? 81.762  16.747  99.413  1.00 115.97 ? 1022 PHE B O   1 
ATOM   20075 C  CB  . PHE C 1 1022 ? 79.847  16.347  96.836  1.00 115.42 ? 1022 PHE B CB  1 
ATOM   20076 C  CG  . PHE C 1 1022 ? 80.143  17.800  96.749  1.00 114.63 ? 1022 PHE B CG  1 
ATOM   20077 C  CD1 . PHE C 1 1022 ? 81.101  18.274  95.858  1.00 115.03 ? 1022 PHE B CD1 1 
ATOM   20078 C  CD2 . PHE C 1 1022 ? 79.453  18.695  97.541  1.00 113.89 ? 1022 PHE B CD2 1 
ATOM   20079 C  CE1 . PHE C 1 1022 ? 81.367  19.619  95.765  1.00 116.13 ? 1022 PHE B CE1 1 
ATOM   20080 C  CE2 . PHE C 1 1022 ? 79.706  20.033  97.464  1.00 115.36 ? 1022 PHE B CE2 1 
ATOM   20081 C  CZ  . PHE C 1 1022 ? 80.665  20.508  96.573  1.00 116.23 ? 1022 PHE B CZ  1 
ATOM   20082 N  N   . HIS C 1 1023 ? 80.043  15.342  99.721  1.00 115.14 ? 1023 HIS B N   1 
ATOM   20083 C  CA  . HIS C 1 1023 ? 79.938  15.579  101.147 1.00 114.42 ? 1023 HIS B CA  1 
ATOM   20084 C  C   . HIS C 1 1023 ? 81.189  15.103  101.845 1.00 111.01 ? 1023 HIS B C   1 
ATOM   20085 O  O   . HIS C 1 1023 ? 81.754  15.804  102.680 1.00 112.13 ? 1023 HIS B O   1 
ATOM   20086 C  CB  . HIS C 1 1023 ? 78.744  14.816  101.657 1.00 115.45 ? 1023 HIS B CB  1 
ATOM   20087 C  CG  . HIS C 1 1023 ? 78.544  14.929  103.123 1.00 117.01 ? 1023 HIS B CG  1 
ATOM   20088 N  ND1 . HIS C 1 1023 ? 78.843  13.902  103.994 1.00 118.85 ? 1023 HIS B ND1 1 
ATOM   20089 C  CD2 . HIS C 1 1023 ? 78.052  15.938  103.878 1.00 117.82 ? 1023 HIS B CD2 1 
ATOM   20090 C  CE1 . HIS C 1 1023 ? 78.531  14.271  105.222 1.00 120.69 ? 1023 HIS B CE1 1 
ATOM   20091 N  NE2 . HIS C 1 1023 ? 78.050  15.503  105.179 1.00 120.70 ? 1023 HIS B NE2 1 
ATOM   20092 N  N   . TYR C 1 1024 ? 81.612  13.899  101.482 1.00 87.57  ? 1024 TYR B N   1 
ATOM   20093 C  CA  . TYR C 1 1024 ? 82.945  13.437  101.803 1.00 87.22  ? 1024 TYR B CA  1 
ATOM   20094 C  C   . TYR C 1 1024 ? 84.017  14.404  101.317 1.00 88.58  ? 1024 TYR B C   1 
ATOM   20095 O  O   . TYR C 1 1024 ? 84.698  15.032  102.105 1.00 88.59  ? 1024 TYR B O   1 
ATOM   20096 C  CB  . TYR C 1 1024 ? 83.227  12.063  101.215 1.00 89.38  ? 1024 TYR B CB  1 
ATOM   20097 C  CG  . TYR C 1 1024 ? 84.626  11.622  101.527 1.00 93.86  ? 1024 TYR B CG  1 
ATOM   20098 C  CD1 . TYR C 1 1024 ? 84.864  10.457  102.247 1.00 98.40  ? 1024 TYR B CD1 1 
ATOM   20099 C  CD2 . TYR C 1 1024 ? 85.721  12.403  101.143 1.00 95.73  ? 1024 TYR B CD2 1 
ATOM   20100 C  CE1 . TYR C 1 1024 ? 86.159  10.073  102.560 1.00 102.26 ? 1024 TYR B CE1 1 
ATOM   20101 C  CE2 . TYR C 1 1024 ? 87.003  12.031  101.452 1.00 99.50  ? 1024 TYR B CE2 1 
ATOM   20102 C  CZ  . TYR C 1 1024 ? 87.225  10.864  102.159 1.00 105.03 ? 1024 TYR B CZ  1 
ATOM   20103 O  OH  . TYR C 1 1024 ? 88.522  10.497  102.463 1.00 111.08 ? 1024 TYR B OH  1 
ATOM   20104 N  N   . LEU C 1 1025 ? 84.212  14.513  100.024 1.00 123.61 ? 1025 LEU B N   1 
ATOM   20105 C  CA  . LEU C 1 1025 ? 85.276  15.383  99.578  1.00 126.04 ? 1025 LEU B CA  1 
ATOM   20106 C  C   . LEU C 1 1025 ? 85.246  16.768  100.244 1.00 126.04 ? 1025 LEU B C   1 
ATOM   20107 O  O   . LEU C 1 1025 ? 86.289  17.319  100.559 1.00 124.79 ? 1025 LEU B O   1 
ATOM   20108 C  CB  . LEU C 1 1025 ? 85.212  15.524  98.069  1.00 126.89 ? 1025 LEU B CB  1 
ATOM   20109 C  CG  . LEU C 1 1025 ? 85.664  14.295  97.288  1.00 127.93 ? 1025 LEU B CG  1 
ATOM   20110 C  CD1 . LEU C 1 1025 ? 85.444  14.556  95.813  1.00 130.21 ? 1025 LEU B CD1 1 
ATOM   20111 C  CD2 . LEU C 1 1025 ? 87.121  13.986  97.592  1.00 128.35 ? 1025 LEU B CD2 1 
ATOM   20112 N  N   . GLU C 1 1026 ? 84.055  17.318  100.467 1.00 126.05 ? 1026 GLU B N   1 
ATOM   20113 C  CA  . GLU C 1 1026 ? 83.913  18.719  100.884 1.00 132.28 ? 1026 GLU B CA  1 
ATOM   20114 C  C   . GLU C 1 1026 ? 84.000  18.873  102.384 1.00 136.53 ? 1026 GLU B C   1 
ATOM   20115 O  O   . GLU C 1 1026 ? 84.930  19.495  102.926 1.00 140.70 ? 1026 GLU B O   1 
ATOM   20116 C  CB  . GLU C 1 1026 ? 82.562  19.283  100.413 1.00 134.80 ? 1026 GLU B CB  1 
ATOM   20117 C  CG  . GLU C 1 1026 ? 82.172  20.645  100.993 1.00 139.13 ? 1026 GLU B CG  1 
ATOM   20118 C  CD  . GLU C 1 1026 ? 82.958  21.807  100.394 1.00 142.96 ? 1026 GLU B CD  1 
ATOM   20119 O  OE1 . GLU C 1 1026 ? 83.998  21.554  99.758  1.00 143.58 ? 1026 GLU B OE1 1 
ATOM   20120 O  OE2 . GLU C 1 1026 ? 82.540  22.977  100.550 1.00 144.23 ? 1026 GLU B OE2 1 
ATOM   20121 N  N   . THR C 1 1027 ? 82.999  18.304  103.045 1.00 127.35 ? 1027 THR B N   1 
ATOM   20122 C  CA  . THR C 1 1027 ? 82.848  18.472  104.469 1.00 127.68 ? 1027 THR B CA  1 
ATOM   20123 C  C   . THR C 1 1027 ? 84.127  18.030  105.133 1.00 129.45 ? 1027 THR B C   1 
ATOM   20124 O  O   . THR C 1 1027 ? 84.704  18.779  105.917 1.00 132.46 ? 1027 THR B O   1 
ATOM   20125 C  CB  . THR C 1 1027 ? 81.668  17.684  104.980 1.00 125.86 ? 1027 THR B CB  1 
ATOM   20126 O  OG1 . THR C 1 1027 ? 80.655  18.605  105.396 1.00 127.38 ? 1027 THR B OG1 1 
ATOM   20127 C  CG2 . THR C 1 1027 ? 82.087  16.840  106.149 1.00 125.87 ? 1027 THR B CG2 1 
ATOM   20128 N  N   . GLY C 1 1028 ? 84.593  16.837  104.775 1.00 91.82  ? 1028 GLY B N   1 
ATOM   20129 C  CA  . GLY C 1 1028 ? 85.929  16.400  105.143 1.00 95.38  ? 1028 GLY B CA  1 
ATOM   20130 C  C   . GLY C 1 1028 ? 87.084  17.014  104.343 1.00 97.60  ? 1028 GLY B C   1 
ATOM   20131 O  O   . GLY C 1 1028 ? 88.079  16.336  104.105 1.00 96.65  ? 1028 GLY B O   1 
ATOM   20132 N  N   . ASN C 1 1029 ? 86.995  18.287  103.967 1.00 128.21 ? 1029 ASN B N   1 
ATOM   20133 C  CA  . ASN C 1 1029 ? 87.913  18.799  102.958 1.00 134.55 ? 1029 ASN B CA  1 
ATOM   20134 C  C   . ASN C 1 1029 ? 88.995  17.786  102.532 1.00 132.56 ? 1029 ASN B C   1 
ATOM   20135 O  O   . ASN C 1 1029 ? 89.889  17.392  103.295 1.00 131.41 ? 1029 ASN B O   1 
ATOM   20136 C  CB  . ASN C 1 1029 ? 88.497  20.160  103.338 1.00 144.49 ? 1029 ASN B CB  1 
ATOM   20137 C  CG  . ASN C 1 1029 ? 89.968  20.080  103.715 1.00 154.87 ? 1029 ASN B CG  1 
ATOM   20138 O  OD1 . ASN C 1 1029 ? 90.816  20.795  103.163 1.00 159.42 ? 1029 ASN B OD1 1 
ATOM   20139 N  ND2 . ASN C 1 1029 ? 90.281  19.200  104.666 1.00 157.57 ? 1029 ASN B ND2 1 
ATOM   20140 N  N   . HIS C 1 1030 ? 88.870  17.353  101.284 1.00 148.36 ? 1030 HIS B N   1 
ATOM   20141 C  CA  . HIS C 1 1030 ? 89.755  16.353  100.690 1.00 147.47 ? 1030 HIS B CA  1 
ATOM   20142 C  C   . HIS C 1 1030 ? 89.933  16.631  99.204  1.00 145.61 ? 1030 HIS B C   1 
ATOM   20143 O  O   . HIS C 1 1030 ? 90.436  15.806  98.434  1.00 144.53 ? 1030 HIS B O   1 
ATOM   20144 C  CB  . HIS C 1 1030 ? 89.165  14.965  100.855 1.00 144.53 ? 1030 HIS B CB  1 
ATOM   20145 C  CG  . HIS C 1 1030 ? 89.205  14.467  102.255 1.00 142.69 ? 1030 HIS B CG  1 
ATOM   20146 N  ND1 . HIS C 1 1030 ? 90.358  14.473  103.005 1.00 142.51 ? 1030 HIS B ND1 1 
ATOM   20147 C  CD2 . HIS C 1 1030 ? 88.235  13.950  103.039 1.00 141.49 ? 1030 HIS B CD2 1 
ATOM   20148 C  CE1 . HIS C 1 1030 ? 90.094  13.977  104.196 1.00 142.28 ? 1030 HIS B CE1 1 
ATOM   20149 N  NE2 . HIS C 1 1030 ? 88.814  13.652  104.242 1.00 141.17 ? 1030 HIS B NE2 1 
ATOM   20150 N  N   . TRP C 1 1031 ? 89.511  17.818  98.813  1.00 169.59 ? 1031 TRP B N   1 
ATOM   20151 C  CA  . TRP C 1 1031 ? 89.711  18.261  97.463  1.00 166.24 ? 1031 TRP B CA  1 
ATOM   20152 C  C   . TRP C 1 1031 ? 91.153  18.004  97.003  1.00 167.90 ? 1031 TRP B C   1 
ATOM   20153 O  O   . TRP C 1 1031 ? 91.401  17.777  95.821  1.00 171.65 ? 1031 TRP B O   1 
ATOM   20154 C  CB  . TRP C 1 1031 ? 89.328  19.735  97.357  1.00 164.06 ? 1031 TRP B CB  1 
ATOM   20155 C  CG  . TRP C 1 1031 ? 87.857  19.933  97.482  1.00 160.37 ? 1031 TRP B CG  1 
ATOM   20156 C  CD1 . TRP C 1 1031 ? 87.213  20.848  98.253  1.00 160.12 ? 1031 TRP B CD1 1 
ATOM   20157 C  CD2 . TRP C 1 1031 ? 86.840  19.175  96.822  1.00 159.35 ? 1031 TRP B CD2 1 
ATOM   20158 N  NE1 . TRP C 1 1031 ? 85.856  20.716  98.104  1.00 159.39 ? 1031 TRP B NE1 1 
ATOM   20159 C  CE2 . TRP C 1 1031 ? 85.603  19.694  97.226  1.00 159.87 ? 1031 TRP B CE2 1 
ATOM   20160 C  CE3 . TRP C 1 1031 ? 86.859  18.111  95.916  1.00 160.16 ? 1031 TRP B CE3 1 
ATOM   20161 C  CZ2 . TRP C 1 1031 ? 84.390  19.182  96.759  1.00 161.82 ? 1031 TRP B CZ2 1 
ATOM   20162 C  CZ3 . TRP C 1 1031 ? 85.656  17.608  95.453  1.00 162.70 ? 1031 TRP B CZ3 1 
ATOM   20163 C  CH2 . TRP C 1 1031 ? 84.441  18.139  95.876  1.00 163.28 ? 1031 TRP B CH2 1 
ATOM   20164 N  N   . ASN C 1 1032 ? 92.106  18.007  97.926  1.00 179.38 ? 1032 ASN B N   1 
ATOM   20165 C  CA  . ASN C 1 1032 ? 93.506  17.891  97.528  1.00 181.90 ? 1032 ASN B CA  1 
ATOM   20166 C  C   . ASN C 1 1032 ? 93.890  16.509  97.021  1.00 179.78 ? 1032 ASN B C   1 
ATOM   20167 O  O   . ASN C 1 1032 ? 95.068  16.269  96.739  1.00 180.24 ? 1032 ASN B O   1 
ATOM   20168 C  CB  . ASN C 1 1032 ? 94.418  18.260  98.678  1.00 185.12 ? 1032 ASN B CB  1 
ATOM   20169 C  CG  . ASN C 1 1032 ? 94.266  17.318  99.845  1.00 184.50 ? 1032 ASN B CG  1 
ATOM   20170 O  OD1 . ASN C 1 1032 ? 93.160  17.102  100.348 1.00 181.86 ? 1032 ASN B OD1 1 
ATOM   20171 N  ND2 . ASN C 1 1032 ? 95.377  16.744  100.286 1.00 186.21 ? 1032 ASN B ND2 1 
ATOM   20172 N  N   . ILE C 1 1033 ? 92.909  15.603  96.921  1.00 126.34 ? 1033 ILE B N   1 
ATOM   20173 C  CA  . ILE C 1 1033 ? 93.141  14.287  96.302  1.00 125.84 ? 1033 ILE B CA  1 
ATOM   20174 C  C   . ILE C 1 1033 ? 93.696  14.399  94.878  1.00 128.84 ? 1033 ILE B C   1 
ATOM   20175 O  O   . ILE C 1 1033 ? 94.417  13.501  94.412  1.00 131.09 ? 1033 ILE B O   1 
ATOM   20176 C  CB  . ILE C 1 1033 ? 91.861  13.450  96.064  1.00 122.63 ? 1033 ILE B CB  1 
ATOM   20177 C  CG1 . ILE C 1 1033 ? 90.852  13.518  97.187  1.00 120.93 ? 1033 ILE B CG1 1 
ATOM   20178 C  CG2 . ILE C 1 1033 ? 92.240  12.003  95.815  1.00 123.52 ? 1033 ILE B CG2 1 
ATOM   20179 C  CD1 . ILE C 1 1033 ? 89.831  12.415  97.033  1.00 120.24 ? 1033 ILE B CD1 1 
ATOM   20180 N  N   . PHE C 1 1034 ? 93.301  15.479  94.188  1.00 170.32 ? 1034 PHE B N   1 
ATOM   20181 C  CA  . PHE C 1 1034 ? 93.535  15.679  92.753  1.00 173.84 ? 1034 PHE B CA  1 
ATOM   20182 C  C   . PHE C 1 1034 ? 94.860  16.348  92.432  1.00 181.52 ? 1034 PHE B C   1 
ATOM   20183 O  O   . PHE C 1 1034 ? 95.257  17.311  93.087  1.00 181.04 ? 1034 PHE B O   1 
ATOM   20184 C  CB  . PHE C 1 1034 ? 92.420  16.528  92.154  1.00 168.25 ? 1034 PHE B CB  1 
ATOM   20185 C  CG  . PHE C 1 1034 ? 91.054  16.000  92.427  1.00 162.44 ? 1034 PHE B CG  1 
ATOM   20186 C  CD1 . PHE C 1 1034 ? 90.720  14.711  92.066  1.00 161.49 ? 1034 PHE B CD1 1 
ATOM   20187 C  CD2 . PHE C 1 1034 ? 90.100  16.790  93.041  1.00 158.37 ? 1034 PHE B CD2 1 
ATOM   20188 C  CE1 . PHE C 1 1034 ? 89.461  14.217  92.318  1.00 158.83 ? 1034 PHE B CE1 1 
ATOM   20189 C  CE2 . PHE C 1 1034 ? 88.839  16.302  93.296  1.00 154.89 ? 1034 PHE B CE2 1 
ATOM   20190 C  CZ  . PHE C 1 1034 ? 88.516  15.017  92.935  1.00 155.22 ? 1034 PHE B CZ  1 
ATOM   20191 N  N   . HIS C 1 1035 ? 95.525  15.848  91.397  1.00 163.19 ? 1035 HIS B N   1 
ATOM   20192 C  CA  . HIS C 1 1035 ? 96.771  16.433  90.935  1.00 174.95 ? 1035 HIS B CA  1 
ATOM   20193 C  C   . HIS C 1 1035 ? 96.427  17.566  89.988  1.00 179.79 ? 1035 HIS B C   1 
ATOM   20194 O  O   . HIS C 1 1035 ? 97.262  18.410  89.687  1.00 183.00 ? 1035 HIS B O   1 
ATOM   20195 C  CB  . HIS C 1 1035 ? 97.600  15.381  90.211  1.00 186.03 ? 1035 HIS B CB  1 
ATOM   20196 C  CG  . HIS C 1 1035 ? 97.606  14.052  90.895  1.00 193.33 ? 1035 HIS B CG  1 
ATOM   20197 N  ND1 . HIS C 1 1035 ? 98.720  13.545  91.523  1.00 196.86 ? 1035 HIS B ND1 1 
ATOM   20198 C  CD2 . HIS C 1 1035 ? 96.624  13.134  91.061  1.00 195.37 ? 1035 HIS B CD2 1 
ATOM   20199 C  CE1 . HIS C 1 1035 ? 98.428  12.363  92.042  1.00 197.52 ? 1035 HIS B CE1 1 
ATOM   20200 N  NE2 . HIS C 1 1035 ? 97.164  12.092  91.776  1.00 196.94 ? 1035 HIS B NE2 1 
ATOM   20201 N  N   . SER C 1 1036 ? 95.178  17.577  89.533  1.00 202.94 ? 1036 SER B N   1 
ATOM   20202 C  CA  . SER C 1 1036 ? 94.682  18.563  88.573  1.00 204.27 ? 1036 SER B CA  1 
ATOM   20203 C  C   . SER C 1 1036 ? 94.365  19.886  89.243  1.00 200.92 ? 1036 SER B C   1 
ATOM   20204 O  O   . SER C 1 1036 ? 94.784  20.138  90.370  1.00 198.06 ? 1036 SER B O   1 
ATOM   20205 C  CB  . SER C 1 1036 ? 93.403  18.044  87.915  1.00 206.46 ? 1036 SER B CB  1 
ATOM   20206 O  OG  . SER C 1 1036 ? 92.290  18.180  88.786  1.00 204.51 ? 1036 SER B OG  1 
ATOM   20207 N  N   . ASP C 1 1037 ? 93.629  20.743  88.549  1.00 229.30 ? 1037 ASP B N   1 
ATOM   20208 C  CA  . ASP C 1 1037 ? 92.960  21.794  89.276  1.00 224.78 ? 1037 ASP B CA  1 
ATOM   20209 C  C   . ASP C 1 1037 ? 91.758  21.160  89.910  1.00 215.19 ? 1037 ASP B C   1 
ATOM   20210 O  O   . ASP C 1 1037 ? 90.985  20.464  89.257  1.00 215.62 ? 1037 ASP B O   1 
ATOM   20211 C  CB  . ASP C 1 1037 ? 92.507  22.953  88.413  1.00 228.85 ? 1037 ASP B CB  1 
ATOM   20212 C  CG  . ASP C 1 1037 ? 91.803  24.032  89.234  1.00 226.12 ? 1037 ASP B CG  1 
ATOM   20213 O  OD1 . ASP C 1 1037 ? 91.425  23.765  90.401  1.00 219.98 ? 1037 ASP B OD1 1 
ATOM   20214 O  OD2 . ASP C 1 1037 ? 91.636  25.156  88.716  1.00 228.52 ? 1037 ASP B OD2 1 
ATOM   20215 N  N   . PRO C 1 1038 ? 91.604  21.397  91.201  1.00 168.18 ? 1038 PRO B N   1 
ATOM   20216 C  CA  . PRO C 1 1038 ? 90.537  20.761  91.964  1.00 163.26 ? 1038 PRO B CA  1 
ATOM   20217 C  C   . PRO C 1 1038 ? 89.236  21.566  91.932  1.00 161.24 ? 1038 PRO B C   1 
ATOM   20218 O  O   . PRO C 1 1038 ? 88.140  20.998  91.869  1.00 161.01 ? 1038 PRO B O   1 
ATOM   20219 C  CB  . PRO C 1 1038 ? 91.125  20.711  93.382  1.00 161.88 ? 1038 PRO B CB  1 
ATOM   20220 C  CG  . PRO C 1 1038 ? 92.608  21.037  93.215  1.00 165.63 ? 1038 PRO B CG  1 
ATOM   20221 C  CD  . PRO C 1 1038 ? 92.643  21.963  92.069  1.00 167.82 ? 1038 PRO B CD  1 
ATOM   20222 N  N   . LEU C 1 1039 ? 89.356  22.885  91.956  1.00 195.25 ? 1039 LEU B N   1 
ATOM   20223 C  CA  . LEU C 1 1039 ? 88.177  23.713  92.117  1.00 193.33 ? 1039 LEU B CA  1 
ATOM   20224 C  C   . LEU C 1 1039 ? 87.206  23.487  90.967  1.00 190.89 ? 1039 LEU B C   1 
ATOM   20225 O  O   . LEU C 1 1039 ? 85.993  23.529  91.147  1.00 188.31 ? 1039 LEU B O   1 
ATOM   20226 C  CB  . LEU C 1 1039 ? 88.576  25.180  92.240  1.00 195.04 ? 1039 LEU B CB  1 
ATOM   20227 C  CG  . LEU C 1 1039 ? 87.523  26.127  92.823  1.00 196.65 ? 1039 LEU B CG  1 
ATOM   20228 C  CD1 . LEU C 1 1039 ? 86.624  25.423  93.826  1.00 193.63 ? 1039 LEU B CD1 1 
ATOM   20229 C  CD2 . LEU C 1 1039 ? 88.206  27.327  93.456  1.00 199.57 ? 1039 LEU B CD2 1 
ATOM   20230 N  N   . ILE C 1 1040 ? 87.753  23.227  89.788  1.00 169.34 ? 1040 ILE B N   1 
ATOM   20231 C  CA  . ILE C 1 1040 ? 86.945  22.943  88.615  1.00 169.29 ? 1040 ILE B CA  1 
ATOM   20232 C  C   . ILE C 1 1040 ? 86.431  21.519  88.731  1.00 169.79 ? 1040 ILE B C   1 
ATOM   20233 O  O   . ILE C 1 1040 ? 85.343  21.193  88.268  1.00 170.72 ? 1040 ILE B O   1 
ATOM   20234 C  CB  . ILE C 1 1040 ? 87.775  23.087  87.311  1.00 169.69 ? 1040 ILE B CB  1 
ATOM   20235 C  CG1 . ILE C 1 1040 ? 86.969  23.772  86.195  1.00 174.13 ? 1040 ILE B CG1 1 
ATOM   20236 C  CG2 . ILE C 1 1040 ? 88.320  21.742  86.850  1.00 167.40 ? 1040 ILE B CG2 1 
ATOM   20237 C  CD1 . ILE C 1 1040 ? 85.466  23.720  86.383  1.00 192.78 ? 1040 ILE B CD1 1 
ATOM   20238 N  N   . GLU C 1 1041 ? 87.235  20.668  89.353  1.00 155.42 ? 1041 GLU B N   1 
ATOM   20239 C  CA  . GLU C 1 1041 ? 86.834  19.299  89.572  1.00 157.57 ? 1041 GLU B CA  1 
ATOM   20240 C  C   . GLU C 1 1041 ? 85.593  19.368  90.443  1.00 156.98 ? 1041 GLU B C   1 
ATOM   20241 O  O   . GLU C 1 1041 ? 84.702  18.523  90.338  1.00 154.51 ? 1041 GLU B O   1 
ATOM   20242 C  CB  . GLU C 1 1041 ? 87.948  18.524  90.268  1.00 160.24 ? 1041 GLU B CB  1 
ATOM   20243 C  CG  . GLU C 1 1041 ? 88.059  17.079  89.833  1.00 165.44 ? 1041 GLU B CG  1 
ATOM   20244 C  CD  . GLU C 1 1041 ? 88.940  16.909  88.614  1.00 174.93 ? 1041 GLU B CD  1 
ATOM   20245 O  OE1 . GLU C 1 1041 ? 89.897  17.693  88.478  1.00 176.93 ? 1041 GLU B OE1 1 
ATOM   20246 O  OE2 . GLU C 1 1041 ? 88.686  15.995  87.798  1.00 180.66 ? 1041 GLU B OE2 1 
ATOM   20247 N  N   . LYS C 1 1042 ? 85.536  20.402  91.286  1.00 152.01 ? 1042 LYS B N   1 
ATOM   20248 C  CA  . LYS C 1 1042 ? 84.404  20.617  92.197  1.00 155.60 ? 1042 LYS B CA  1 
ATOM   20249 C  C   . LYS C 1 1042 ? 83.139  20.902  91.410  1.00 162.28 ? 1042 LYS B C   1 
ATOM   20250 O  O   . LYS C 1 1042 ? 82.088  20.283  91.617  1.00 163.41 ? 1042 LYS B O   1 
ATOM   20251 C  CB  . LYS C 1 1042 ? 84.666  21.792  93.155  1.00 155.96 ? 1042 LYS B CB  1 
ATOM   20252 C  CG  . LYS C 1 1042 ? 83.420  22.237  93.949  1.00 158.86 ? 1042 LYS B CG  1 
ATOM   20253 C  CD  . LYS C 1 1042 ? 83.682  23.428  94.889  1.00 161.33 ? 1042 LYS B CD  1 
ATOM   20254 C  CE  . LYS C 1 1042 ? 83.814  22.991  96.347  1.00 159.48 ? 1042 LYS B CE  1 
ATOM   20255 N  NZ  . LYS C 1 1042 ? 83.871  24.147  97.282  1.00 160.71 ? 1042 LYS B NZ  1 
ATOM   20256 N  N   . GLN C 1 1043 ? 83.255  21.865  90.505  1.00 170.29 ? 1043 GLN B N   1 
ATOM   20257 C  CA  . GLN C 1 1043 ? 82.150  22.260  89.652  1.00 174.43 ? 1043 GLN B CA  1 
ATOM   20258 C  C   . GLN C 1 1043 ? 81.494  21.052  89.038  1.00 170.01 ? 1043 GLN B C   1 
ATOM   20259 O  O   . GLN C 1 1043 ? 80.274  20.882  89.129  1.00 169.94 ? 1043 GLN B O   1 
ATOM   20260 C  CB  . GLN C 1 1043 ? 82.668  23.178  88.549  1.00 182.50 ? 1043 GLN B CB  1 
ATOM   20261 C  CG  . GLN C 1 1043 ? 83.091  24.500  89.091  1.00 188.32 ? 1043 GLN B CG  1 
ATOM   20262 C  CD  . GLN C 1 1043 ? 82.158  24.919  90.200  1.00 190.74 ? 1043 GLN B CD  1 
ATOM   20263 O  OE1 . GLN C 1 1043 ? 80.938  24.744  90.092  1.00 191.68 ? 1043 GLN B OE1 1 
ATOM   20264 N  NE2 . GLN C 1 1043 ? 82.718  25.449  91.289  1.00 189.94 ? 1043 GLN B NE2 1 
ATOM   20265 N  N   . LYS C 1 1044 ? 82.330  20.219  88.415  1.00 150.20 ? 1044 LYS B N   1 
ATOM   20266 C  CA  . LYS C 1 1044 ? 81.875  19.045  87.669  1.00 148.70 ? 1044 LYS B CA  1 
ATOM   20267 C  C   . LYS C 1 1044 ? 80.985  18.169  88.544  1.00 145.85 ? 1044 LYS B C   1 
ATOM   20268 O  O   . LYS C 1 1044 ? 79.995  17.599  88.078  1.00 147.47 ? 1044 LYS B O   1 
ATOM   20269 C  CB  . LYS C 1 1044 ? 83.065  18.251  87.081  1.00 148.94 ? 1044 LYS B CB  1 
ATOM   20270 C  CG  . LYS C 1 1044 ? 83.756  18.914  85.867  1.00 185.99 ? 1044 LYS B CG  1 
ATOM   20271 C  CD  . LYS C 1 1044 ? 84.970  18.129  85.346  1.00 183.97 ? 1044 LYS B CD  1 
ATOM   20272 C  CE  . LYS C 1 1044 ? 84.561  16.892  84.562  1.00 184.45 ? 1044 LYS B CE  1 
ATOM   20273 N  NZ  . LYS C 1 1044 ? 85.750  16.109  84.137  1.00 184.39 ? 1044 LYS B NZ  1 
ATOM   20274 N  N   . LEU C 1 1045 ? 81.323  18.081  89.822  1.00 169.54 ? 1045 LEU B N   1 
ATOM   20275 C  CA  . LEU C 1 1045 ? 80.539  17.258  90.720  1.00 163.99 ? 1045 LEU B CA  1 
ATOM   20276 C  C   . LEU C 1 1045 ? 79.291  18.024  91.086  1.00 162.65 ? 1045 LEU B C   1 
ATOM   20277 O  O   . LEU C 1 1045 ? 78.223  17.444  91.258  1.00 161.58 ? 1045 LEU B O   1 
ATOM   20278 C  CB  . LEU C 1 1045 ? 81.356  16.913  91.948  1.00 158.67 ? 1045 LEU B CB  1 
ATOM   20279 C  CG  . LEU C 1 1045 ? 82.770  16.467  91.575  1.00 155.37 ? 1045 LEU B CG  1 
ATOM   20280 C  CD1 . LEU C 1 1045 ? 83.335  15.680  92.719  1.00 154.45 ? 1045 LEU B CD1 1 
ATOM   20281 C  CD2 . LEU C 1 1045 ? 82.801  15.632  90.309  1.00 153.85 ? 1045 LEU B CD2 1 
ATOM   20282 N  N   . LYS C 1 1046 ? 79.433  19.340  91.178  1.00 147.26 ? 1046 LYS B N   1 
ATOM   20283 C  CA  . LYS C 1 1046 ? 78.303  20.196  91.467  1.00 151.19 ? 1046 LYS B CA  1 
ATOM   20284 C  C   . LYS C 1 1046 ? 77.254  19.964  90.399  1.00 156.70 ? 1046 LYS B C   1 
ATOM   20285 O  O   . LYS C 1 1046 ? 76.125  19.542  90.672  1.00 158.20 ? 1046 LYS B O   1 
ATOM   20286 C  CB  . LYS C 1 1046 ? 78.736  21.665  91.491  1.00 153.01 ? 1046 LYS B CB  1 
ATOM   20287 C  CG  . LYS C 1 1046 ? 79.542  22.097  92.723  1.00 153.03 ? 1046 LYS B CG  1 
ATOM   20288 C  CD  . LYS C 1 1046 ? 79.456  23.621  92.857  1.00 157.91 ? 1046 LYS B CD  1 
ATOM   20289 C  CE  . LYS C 1 1046 ? 80.517  24.268  93.751  1.00 159.63 ? 1046 LYS B CE  1 
ATOM   20290 N  NZ  . LYS C 1 1046 ? 80.405  25.771  93.768  1.00 162.30 ? 1046 LYS B NZ  1 
ATOM   20291 N  N   . LYS C 1 1047 ? 77.647  20.228  89.163  1.00 134.41 ? 1047 LYS B N   1 
ATOM   20292 C  CA  . LYS C 1 1047 ? 76.778  19.926  88.041  1.00 137.26 ? 1047 LYS B CA  1 
ATOM   20293 C  C   . LYS C 1 1047 ? 76.213  18.537  88.271  1.00 130.09 ? 1047 LYS B C   1 
ATOM   20294 O  O   . LYS C 1 1047 ? 75.018  18.392  88.536  1.00 127.96 ? 1047 LYS B O   1 
ATOM   20295 C  CB  . LYS C 1 1047 ? 77.543  19.977  86.708  1.00 146.86 ? 1047 LYS B CB  1 
ATOM   20296 C  CG  . LYS C 1 1047 ? 76.664  20.048  85.437  1.00 157.79 ? 1047 LYS B CG  1 
ATOM   20297 C  CD  . LYS C 1 1047 ? 77.422  20.638  84.244  1.00 168.54 ? 1047 LYS B CD  1 
ATOM   20298 C  CE  . LYS C 1 1047 ? 76.480  20.898  83.102  1.00 177.54 ? 1047 LYS B CE  1 
ATOM   20299 N  NZ  . LYS C 1 1047 ? 75.719  19.685  82.744  1.00 180.65 ? 1047 LYS B NZ  1 
ATOM   20300 N  N   . LYS C 1 1048 ? 77.075  17.526  88.198  1.00 124.58 ? 1048 LYS B N   1 
ATOM   20301 C  CA  . LYS C 1 1048 ? 76.603  16.153  88.162  1.00 119.12 ? 1048 LYS B CA  1 
ATOM   20302 C  C   . LYS C 1 1048 ? 75.483  15.972  89.118  1.00 113.92 ? 1048 LYS B C   1 
ATOM   20303 O  O   . LYS C 1 1048 ? 74.660  15.074  88.952  1.00 112.91 ? 1048 LYS B O   1 
ATOM   20304 C  CB  . LYS C 1 1048 ? 77.690  15.186  88.548  1.00 115.43 ? 1048 LYS B CB  1 
ATOM   20305 C  CG  . LYS C 1 1048 ? 78.613  14.929  87.458  1.00 116.32 ? 1048 LYS B CG  1 
ATOM   20306 C  CD  . LYS C 1 1048 ? 78.974  13.519  87.466  1.00 116.90 ? 1048 LYS B CD  1 
ATOM   20307 C  CE  . LYS C 1 1048 ? 80.432  13.433  87.215  1.00 117.27 ? 1048 LYS B CE  1 
ATOM   20308 N  NZ  . LYS C 1 1048 ? 80.792  12.017  87.209  1.00 117.86 ? 1048 LYS B NZ  1 
ATOM   20309 N  N   . LEU C 1 1049 ? 75.498  16.820  90.142  1.00 146.01 ? 1049 LEU B N   1 
ATOM   20310 C  CA  . LEU C 1 1049 ? 74.485  16.828  91.180  1.00 144.03 ? 1049 LEU B CA  1 
ATOM   20311 C  C   . LEU C 1 1049 ? 73.225  17.562  90.704  1.00 148.37 ? 1049 LEU B C   1 
ATOM   20312 O  O   . LEU C 1 1049 ? 72.195  16.935  90.462  1.00 151.37 ? 1049 LEU B O   1 
ATOM   20313 C  CB  . LEU C 1 1049 ? 75.053  17.399  92.503  1.00 137.25 ? 1049 LEU B CB  1 
ATOM   20314 C  CG  . LEU C 1 1049 ? 74.860  16.591  93.817  1.00 131.09 ? 1049 LEU B CG  1 
ATOM   20315 C  CD1 . LEU C 1 1049 ? 75.511  15.211  93.780  1.00 126.28 ? 1049 LEU B CD1 1 
ATOM   20316 C  CD2 . LEU C 1 1049 ? 75.339  17.361  95.047  1.00 129.37 ? 1049 LEU B CD2 1 
ATOM   20317 N  N   . LYS C 1 1050 ? 73.284  18.868  90.516  1.00 160.13 ? 1050 LYS B N   1 
ATOM   20318 C  CA  . LYS C 1 1050 ? 72.074  19.498  90.033  1.00 162.82 ? 1050 LYS B CA  1 
ATOM   20319 C  C   . LYS C 1 1050 ? 71.457  18.690  88.884  1.00 168.80 ? 1050 LYS B C   1 
ATOM   20320 O  O   . LYS C 1 1050 ? 70.289  18.350  88.944  1.00 168.49 ? 1050 LYS B O   1 
ATOM   20321 C  CB  . LYS C 1 1050 ? 72.295  20.944  89.617  1.00 162.63 ? 1050 LYS B CB  1 
ATOM   20322 C  CG  . LYS C 1 1050 ? 71.031  21.586  89.099  1.00 163.34 ? 1050 LYS B CG  1 
ATOM   20323 C  CD  . LYS C 1 1050 ? 71.111  23.079  89.153  1.00 164.35 ? 1050 LYS B CD  1 
ATOM   20324 C  CE  . LYS C 1 1050 ? 69.722  23.648  89.117  1.00 168.10 ? 1050 LYS B CE  1 
ATOM   20325 N  NZ  . LYS C 1 1050 ? 69.734  25.047  89.585  1.00 170.94 ? 1050 LYS B NZ  1 
ATOM   20326 N  N   . GLU C 1 1051 ? 72.220  18.351  87.850  1.00 209.36 ? 1051 GLU B N   1 
ATOM   20327 C  CA  . GLU C 1 1051 ? 71.598  17.680  86.699  1.00 219.73 ? 1051 GLU B CA  1 
ATOM   20328 C  C   . GLU C 1 1051 ? 70.952  16.337  87.054  1.00 218.70 ? 1051 GLU B C   1 
ATOM   20329 O  O   . GLU C 1 1051 ? 69.867  16.009  86.571  1.00 220.75 ? 1051 GLU B O   1 
ATOM   20330 C  CB  . GLU C 1 1051 ? 72.591  17.497  85.559  1.00 230.46 ? 1051 GLU B CB  1 
ATOM   20331 C  CG  . GLU C 1 1051 ? 73.424  16.245  85.681  1.00 238.41 ? 1051 GLU B CG  1 
ATOM   20332 C  CD  . GLU C 1 1051 ? 74.520  16.197  84.650  1.00 246.73 ? 1051 GLU B CD  1 
ATOM   20333 O  OE1 . GLU C 1 1051 ? 74.812  17.262  84.059  1.00 249.48 ? 1051 GLU B OE1 1 
ATOM   20334 O  OE2 . GLU C 1 1051 ? 75.084  15.101  84.432  1.00 249.85 ? 1051 GLU B OE2 1 
ATOM   20335 N  N   . GLY C 1 1052 ? 71.626  15.553  87.884  1.00 135.61 ? 1052 GLY B N   1 
ATOM   20336 C  CA  . GLY C 1 1052 ? 71.047  14.315  88.353  1.00 136.85 ? 1052 GLY B CA  1 
ATOM   20337 C  C   . GLY C 1 1052 ? 69.776  14.687  89.074  1.00 135.08 ? 1052 GLY B C   1 
ATOM   20338 O  O   . GLY C 1 1052 ? 68.811  13.934  89.095  1.00 136.31 ? 1052 GLY B O   1 
ATOM   20339 N  N   . MET C 1 1053 ? 69.783  15.882  89.651  1.00 191.79 ? 1053 MET B N   1 
ATOM   20340 C  CA  . MET C 1 1053 ? 68.675  16.358  90.457  1.00 192.18 ? 1053 MET B CA  1 
ATOM   20341 C  C   . MET C 1 1053 ? 67.450  16.571  89.604  1.00 193.79 ? 1053 MET B C   1 
ATOM   20342 O  O   . MET C 1 1053 ? 66.334  16.257  90.006  1.00 194.03 ? 1053 MET B O   1 
ATOM   20343 C  CB  . MET C 1 1053 ? 69.042  17.671  91.153  1.00 194.72 ? 1053 MET B CB  1 
ATOM   20344 C  CG  . MET C 1 1053 ? 68.098  18.022  92.276  1.00 194.23 ? 1053 MET B CG  1 
ATOM   20345 S  SD  . MET C 1 1053 ? 67.292  16.509  92.857  1.00 303.00 ? 1053 MET B SD  1 
ATOM   20346 C  CE  . MET C 1 1053 ? 67.567  16.579  94.639  1.00 130.37 ? 1053 MET B CE  1 
ATOM   20347 N  N   . LEU C 1 1054 ? 67.649  17.128  88.421  1.00 185.81 ? 1054 LEU B N   1 
ATOM   20348 C  CA  . LEU C 1 1054 ? 66.504  17.380  87.576  1.00 188.77 ? 1054 LEU B CA  1 
ATOM   20349 C  C   . LEU C 1 1054 ? 65.983  16.017  87.168  1.00 186.91 ? 1054 LEU B C   1 
ATOM   20350 O  O   . LEU C 1 1054 ? 64.782  15.823  87.016  1.00 187.00 ? 1054 LEU B O   1 
ATOM   20351 C  CB  . LEU C 1 1054 ? 66.874  18.233  86.358  1.00 195.37 ? 1054 LEU B CB  1 
ATOM   20352 C  CG  . LEU C 1 1054 ? 67.579  19.572  86.634  1.00 198.93 ? 1054 LEU B CG  1 
ATOM   20353 C  CD1 . LEU C 1 1054 ? 67.916  20.295  85.332  1.00 202.51 ? 1054 LEU B CD1 1 
ATOM   20354 C  CD2 . LEU C 1 1054 ? 66.789  20.496  87.583  1.00 200.35 ? 1054 LEU B CD2 1 
ATOM   20355 N  N   . SER C 1 1055 ? 66.898  15.059  87.060  1.00 169.10 ? 1055 SER B N   1 
ATOM   20356 C  CA  . SER C 1 1055 ? 66.592  13.788  86.421  1.00 168.94 ? 1055 SER B CA  1 
ATOM   20357 C  C   . SER C 1 1055 ? 65.273  13.187  86.889  1.00 163.13 ? 1055 SER B C   1 
ATOM   20358 O  O   . SER C 1 1055 ? 64.719  12.297  86.238  1.00 166.38 ? 1055 SER B O   1 
ATOM   20359 C  CB  . SER C 1 1055 ? 67.720  12.771  86.627  1.00 173.48 ? 1055 SER B CB  1 
ATOM   20360 O  OG  . SER C 1 1055 ? 67.432  11.564  85.929  1.00 177.86 ? 1055 SER B OG  1 
ATOM   20361 N  N   . ILE C 1 1056 ? 64.773  13.687  88.010  1.00 170.16 ? 1056 ILE B N   1 
ATOM   20362 C  CA  . ILE C 1 1056 ? 63.605  13.121  88.656  1.00 169.61 ? 1056 ILE B CA  1 
ATOM   20363 C  C   . ILE C 1 1056 ? 62.352  13.951  88.429  1.00 168.78 ? 1056 ILE B C   1 
ATOM   20364 O  O   . ILE C 1 1056 ? 61.250  13.416  88.380  1.00 169.39 ? 1056 ILE B O   1 
ATOM   20365 C  CB  . ILE C 1 1056 ? 63.886  12.966  90.155  1.00 155.84 ? 1056 ILE B CB  1 
ATOM   20366 C  CG1 . ILE C 1 1056 ? 62.669  13.373  90.997  1.00 152.08 ? 1056 ILE B CG1 1 
ATOM   20367 C  CG2 . ILE C 1 1056 ? 65.121  13.783  90.528  1.00 151.70 ? 1056 ILE B CG2 1 
ATOM   20368 C  CD1 . ILE C 1 1056 ? 62.993  14.327  92.167  1.00 149.49 ? 1056 ILE B CD1 1 
ATOM   20369 N  N   . MET C 1 1057 ? 62.532  15.254  88.266  1.00 195.96 ? 1057 MET B N   1 
ATOM   20370 C  CA  . MET C 1 1057 ? 61.405  16.166  88.169  1.00 203.48 ? 1057 MET B CA  1 
ATOM   20371 C  C   . MET C 1 1057 ? 60.213  15.473  87.577  1.00 209.15 ? 1057 MET B C   1 
ATOM   20372 O  O   . MET C 1 1057 ? 59.090  15.606  88.045  1.00 209.33 ? 1057 MET B O   1 
ATOM   20373 C  CB  . MET C 1 1057 ? 61.759  17.366  87.298  1.00 210.57 ? 1057 MET B CB  1 
ATOM   20374 C  CG  . MET C 1 1057 ? 61.231  18.667  87.869  1.00 213.90 ? 1057 MET B CG  1 
ATOM   20375 S  SD  . MET C 1 1057 ? 61.758  18.909  89.595  1.00 244.53 ? 1057 MET B SD  1 
ATOM   20376 C  CE  . MET C 1 1057 ? 63.303  19.796  89.392  1.00 274.12 ? 1057 MET B CE  1 
ATOM   20377 N  N   . SER C 1 1058 ? 60.488  14.711  86.538  1.00 190.20 ? 1058 SER B N   1 
ATOM   20378 C  CA  . SER C 1 1058 ? 59.458  14.038  85.779  1.00 189.64 ? 1058 SER B CA  1 
ATOM   20379 C  C   . SER C 1 1058 ? 58.477  13.269  86.652  1.00 186.42 ? 1058 SER B C   1 
ATOM   20380 O  O   . SER C 1 1058 ? 57.301  13.140  86.306  1.00 187.40 ? 1058 SER B O   1 
ATOM   20381 C  CB  . SER C 1 1058 ? 60.116  13.112  84.757  1.00 188.64 ? 1058 SER B CB  1 
ATOM   20382 O  OG  . SER C 1 1058 ? 61.064  13.835  83.975  1.00 186.89 ? 1058 SER B OG  1 
ATOM   20383 N  N   . TYR C 1 1059 ? 58.958  12.767  87.783  1.00 172.73 ? 1059 TYR B N   1 
ATOM   20384 C  CA  . TYR C 1 1059 ? 58.129  11.936  88.653  1.00 172.45 ? 1059 TYR B CA  1 
ATOM   20385 C  C   . TYR C 1 1059 ? 57.416  12.791  89.668  1.00 177.48 ? 1059 TYR B C   1 
ATOM   20386 O  O   . TYR C 1 1059 ? 56.555  12.320  90.412  1.00 179.48 ? 1059 TYR B O   1 
ATOM   20387 C  CB  . TYR C 1 1059 ? 58.974  10.889  89.366  1.00 165.52 ? 1059 TYR B CB  1 
ATOM   20388 C  CG  . TYR C 1 1059 ? 59.722  9.986   88.421  1.00 163.85 ? 1059 TYR B CG  1 
ATOM   20389 C  CD1 . TYR C 1 1059 ? 60.740  10.482  87.608  1.00 165.45 ? 1059 TYR B CD1 1 
ATOM   20390 C  CD2 . TYR C 1 1059 ? 59.415  8.638   88.335  1.00 166.81 ? 1059 TYR B CD2 1 
ATOM   20391 C  CE1 . TYR C 1 1059 ? 61.435  9.648   86.725  1.00 170.32 ? 1059 TYR B CE1 1 
ATOM   20392 C  CE2 . TYR C 1 1059 ? 60.099  7.793   87.466  1.00 172.78 ? 1059 TYR B CE2 1 
ATOM   20393 C  CZ  . TYR C 1 1059 ? 61.107  8.296   86.663  1.00 174.31 ? 1059 TYR B CZ  1 
ATOM   20394 O  OH  . TYR C 1 1059 ? 61.765  7.423   85.814  1.00 176.53 ? 1059 TYR B OH  1 
ATOM   20395 N  N   . ARG C 1 1060 ? 57.788  14.061  89.698  1.00 173.19 ? 1060 ARG B N   1 
ATOM   20396 C  CA  . ARG C 1 1060 ? 57.181  14.983  90.630  1.00 176.63 ? 1060 ARG B CA  1 
ATOM   20397 C  C   . ARG C 1 1060 ? 55.800  15.407  90.194  1.00 181.15 ? 1060 ARG B C   1 
ATOM   20398 O  O   . ARG C 1 1060 ? 55.656  16.108  89.196  1.00 182.99 ? 1060 ARG B O   1 
ATOM   20399 C  CB  . ARG C 1 1060 ? 58.011  16.239  90.736  1.00 178.56 ? 1060 ARG B CB  1 
ATOM   20400 C  CG  . ARG C 1 1060 ? 57.283  17.285  91.522  1.00 173.22 ? 1060 ARG B CG  1 
ATOM   20401 C  CD  . ARG C 1 1060 ? 58.164  18.441  91.820  1.00 174.13 ? 1060 ARG B CD  1 
ATOM   20402 N  NE  . ARG C 1 1060 ? 57.458  19.677  91.557  1.00 180.44 ? 1060 ARG B NE  1 
ATOM   20403 C  CZ  . ARG C 1 1060 ? 57.982  20.872  91.774  1.00 183.17 ? 1060 ARG B CZ  1 
ATOM   20404 N  NH1 . ARG C 1 1060 ? 59.215  20.977  92.261  1.00 184.24 ? 1060 ARG B NH1 1 
ATOM   20405 N  NH2 . ARG C 1 1060 ? 57.272  21.955  91.505  1.00 183.96 ? 1060 ARG B NH2 1 
ATOM   20406 N  N   . ASN C 1 1061 ? 54.785  15.038  90.961  1.00 147.32 ? 1061 ASN B N   1 
ATOM   20407 C  CA  . ASN C 1 1061 ? 53.432  15.449  90.607  1.00 155.46 ? 1061 ASN B CA  1 
ATOM   20408 C  C   . ASN C 1 1061 ? 53.125  16.934  90.787  1.00 158.78 ? 1061 ASN B C   1 
ATOM   20409 O  O   . ASN C 1 1061 ? 54.014  17.788  90.872  1.00 157.27 ? 1061 ASN B O   1 
ATOM   20410 C  CB  . ASN C 1 1061 ? 52.364  14.589  91.306  1.00 160.40 ? 1061 ASN B CB  1 
ATOM   20411 C  CG  . ASN C 1 1061 ? 51.967  13.353  90.488  1.00 167.04 ? 1061 ASN B CG  1 
ATOM   20412 O  OD1 . ASN C 1 1061 ? 52.828  12.572  90.089  1.00 167.60 ? 1061 ASN B OD1 1 
ATOM   20413 N  ND2 . ASN C 1 1061 ? 50.661  13.172  90.246  1.00 171.89 ? 1061 ASN B ND2 1 
ATOM   20414 N  N   . ALA C 1 1062 ? 51.831  17.212  90.834  1.00 182.95 ? 1062 ALA B N   1 
ATOM   20415 C  CA  . ALA C 1 1062 ? 51.314  18.561  90.738  1.00 185.89 ? 1062 ALA B CA  1 
ATOM   20416 C  C   . ALA C 1 1062 ? 51.425  19.300  92.049  1.00 184.51 ? 1062 ALA B C   1 
ATOM   20417 O  O   . ALA C 1 1062 ? 52.061  20.351  92.128  1.00 185.90 ? 1062 ALA B O   1 
ATOM   20418 C  CB  . ALA C 1 1062 ? 49.862  18.516  90.294  1.00 190.28 ? 1062 ALA B CB  1 
ATOM   20419 N  N   . ASP C 1 1063 ? 50.780  18.725  93.064  1.00 219.55 ? 1063 ASP B N   1 
ATOM   20420 C  CA  . ASP C 1 1063 ? 50.644  19.292  94.403  1.00 217.51 ? 1063 ASP B CA  1 
ATOM   20421 C  C   . ASP C 1 1063 ? 51.965  19.235  95.144  1.00 209.81 ? 1063 ASP B C   1 
ATOM   20422 O  O   . ASP C 1 1063 ? 52.027  19.449  96.352  1.00 207.71 ? 1063 ASP B O   1 
ATOM   20423 C  CB  . ASP C 1 1063 ? 49.611  18.485  95.174  1.00 220.66 ? 1063 ASP B CB  1 
ATOM   20424 C  CG  . ASP C 1 1063 ? 49.933  17.012  95.177  1.00 221.68 ? 1063 ASP B CG  1 
ATOM   20425 O  OD1 . ASP C 1 1063 ? 51.122  16.669  95.002  1.00 220.18 ? 1063 ASP B OD1 1 
ATOM   20426 O  OD2 . ASP C 1 1063 ? 49.005  16.199  95.347  1.00 224.43 ? 1063 ASP B OD2 1 
ATOM   20427 N  N   . TYR C 1 1064 ? 53.012  18.918  94.397  1.00 181.51 ? 1064 TYR B N   1 
ATOM   20428 C  CA  . TYR C 1 1064 ? 54.363  18.899  94.912  1.00 176.43 ? 1064 TYR B CA  1 
ATOM   20429 C  C   . TYR C 1 1064 ? 54.659  17.559  95.542  1.00 175.45 ? 1064 TYR B C   1 
ATOM   20430 O  O   . TYR C 1 1064 ? 55.772  17.313  95.993  1.00 176.93 ? 1064 TYR B O   1 
ATOM   20431 C  CB  . TYR C 1 1064 ? 54.603  20.077  95.863  1.00 173.42 ? 1064 TYR B CB  1 
ATOM   20432 C  CG  . TYR C 1 1064 ? 54.578  21.425  95.149  1.00 174.58 ? 1064 TYR B CG  1 
ATOM   20433 C  CD1 . TYR C 1 1064 ? 55.694  21.886  94.446  1.00 173.00 ? 1064 TYR B CD1 1 
ATOM   20434 C  CD2 . TYR C 1 1064 ? 53.435  22.228  95.149  1.00 177.74 ? 1064 TYR B CD2 1 
ATOM   20435 C  CE1 . TYR C 1 1064 ? 55.679  23.127  93.773  1.00 176.06 ? 1064 TYR B CE1 1 
ATOM   20436 C  CE2 . TYR C 1 1064 ? 53.411  23.472  94.477  1.00 181.06 ? 1064 TYR B CE2 1 
ATOM   20437 C  CZ  . TYR C 1 1064 ? 54.536  23.913  93.794  1.00 179.38 ? 1064 TYR B CZ  1 
ATOM   20438 O  OH  . TYR C 1 1064 ? 54.521  25.133  93.138  1.00 181.45 ? 1064 TYR B OH  1 
ATOM   20439 N  N   . SER C 1 1065 ? 53.661  16.684  95.538  1.00 184.16 ? 1065 SER B N   1 
ATOM   20440 C  CA  . SER C 1 1065 ? 53.885  15.300  95.915  1.00 180.20 ? 1065 SER B CA  1 
ATOM   20441 C  C   . SER C 1 1065 ? 54.652  14.598  94.800  1.00 177.43 ? 1065 SER B C   1 
ATOM   20442 O  O   . SER C 1 1065 ? 54.343  14.773  93.624  1.00 179.16 ? 1065 SER B O   1 
ATOM   20443 C  CB  . SER C 1 1065 ? 52.559  14.585  96.135  1.00 182.79 ? 1065 SER B CB  1 
ATOM   20444 O  OG  . SER C 1 1065 ? 51.965  14.265  94.887  1.00 186.47 ? 1065 SER B OG  1 
ATOM   20445 N  N   . TYR C 1 1066 ? 55.655  13.811  95.171  1.00 149.89 ? 1066 TYR B N   1 
ATOM   20446 C  CA  . TYR C 1 1066 ? 56.428  13.051  94.202  1.00 149.84 ? 1066 TYR B CA  1 
ATOM   20447 C  C   . TYR C 1 1066 ? 55.662  11.766  93.881  1.00 151.97 ? 1066 TYR B C   1 
ATOM   20448 O  O   . TYR C 1 1066 ? 54.585  11.553  94.433  1.00 153.87 ? 1066 TYR B O   1 
ATOM   20449 C  CB  . TYR C 1 1066 ? 57.839  12.815  94.752  1.00 145.07 ? 1066 TYR B CB  1 
ATOM   20450 C  CG  . TYR C 1 1066 ? 58.603  14.120  94.798  1.00 144.44 ? 1066 TYR B CG  1 
ATOM   20451 C  CD1 . TYR C 1 1066 ? 57.972  15.289  95.228  1.00 145.25 ? 1066 TYR B CD1 1 
ATOM   20452 C  CD2 . TYR C 1 1066 ? 59.927  14.208  94.382  1.00 144.00 ? 1066 TYR B CD2 1 
ATOM   20453 C  CE1 . TYR C 1 1066 ? 58.639  16.522  95.257  1.00 147.41 ? 1066 TYR B CE1 1 
ATOM   20454 C  CE2 . TYR C 1 1066 ? 60.611  15.443  94.407  1.00 145.71 ? 1066 TYR B CE2 1 
ATOM   20455 C  CZ  . TYR C 1 1066 ? 59.958  16.601  94.847  1.00 148.14 ? 1066 TYR B CZ  1 
ATOM   20456 O  OH  . TYR C 1 1066 ? 60.612  17.828  94.878  1.00 150.25 ? 1066 TYR B OH  1 
ATOM   20457 N  N   . SER C 1 1067 ? 56.170  10.924  92.983  1.00 161.44 ? 1067 SER B N   1 
ATOM   20458 C  CA  . SER C 1 1067 ? 55.488  9.654   92.708  1.00 162.87 ? 1067 SER B CA  1 
ATOM   20459 C  C   . SER C 1 1067 ? 56.371  8.536   92.129  1.00 163.56 ? 1067 SER B C   1 
ATOM   20460 O  O   . SER C 1 1067 ? 57.320  8.791   91.385  1.00 163.51 ? 1067 SER B O   1 
ATOM   20461 C  CB  . SER C 1 1067 ? 54.258  9.875   91.825  1.00 165.32 ? 1067 SER B CB  1 
ATOM   20462 O  OG  . SER C 1 1067 ? 53.551  8.656   91.653  1.00 167.28 ? 1067 SER B OG  1 
ATOM   20463 N  N   . VAL C 1 1068 ? 56.026  7.297   92.480  1.00 165.39 ? 1068 VAL B N   1 
ATOM   20464 C  CA  . VAL C 1 1068 ? 56.785  6.101   92.102  1.00 166.60 ? 1068 VAL B CA  1 
ATOM   20465 C  C   . VAL C 1 1068 ? 57.249  6.005   90.640  1.00 172.69 ? 1068 VAL B C   1 
ATOM   20466 O  O   . VAL C 1 1068 ? 58.419  6.255   90.360  1.00 172.95 ? 1068 VAL B O   1 
ATOM   20467 C  CB  . VAL C 1 1068 ? 55.987  4.849   92.392  1.00 167.04 ? 1068 VAL B CB  1 
ATOM   20468 C  CG1 . VAL C 1 1068 ? 54.608  4.926   91.694  1.00 172.48 ? 1068 VAL B CG1 1 
ATOM   20469 C  CG2 . VAL C 1 1068 ? 56.783  3.633   91.948  1.00 166.10 ? 1068 VAL B CG2 1 
ATOM   20470 N  N   . TRP C 1 1069 ? 56.361  5.567   89.734  1.00 162.21 ? 1069 TRP B N   1 
ATOM   20471 C  CA  . TRP C 1 1069 ? 56.598  5.661   88.283  1.00 165.34 ? 1069 TRP B CA  1 
ATOM   20472 C  C   . TRP C 1 1069 ? 55.686  6.713   87.657  1.00 167.79 ? 1069 TRP B C   1 
ATOM   20473 O  O   . TRP C 1 1069 ? 54.543  6.905   88.102  1.00 167.76 ? 1069 TRP B O   1 
ATOM   20474 C  CB  . TRP C 1 1069 ? 56.365  4.345   87.548  1.00 166.74 ? 1069 TRP B CB  1 
ATOM   20475 C  CG  . TRP C 1 1069 ? 56.715  3.149   88.314  1.00 162.96 ? 1069 TRP B CG  1 
ATOM   20476 C  CD1 . TRP C 1 1069 ? 57.928  2.535   88.369  1.00 160.73 ? 1069 TRP B CD1 1 
ATOM   20477 C  CD2 . TRP C 1 1069 ? 55.834  2.382   89.132  1.00 159.38 ? 1069 TRP B CD2 1 
ATOM   20478 N  NE1 . TRP C 1 1069 ? 57.858  1.428   89.177  1.00 158.92 ? 1069 TRP B NE1 1 
ATOM   20479 C  CE2 . TRP C 1 1069 ? 56.583  1.312   89.659  1.00 159.66 ? 1069 TRP B CE2 1 
ATOM   20480 C  CE3 . TRP C 1 1069 ? 54.484  2.496   89.470  1.00 157.67 ? 1069 TRP B CE3 1 
ATOM   20481 C  CZ2 . TRP C 1 1069 ? 56.029  0.361   90.510  1.00 161.21 ? 1069 TRP B CZ2 1 
ATOM   20482 C  CZ3 . TRP C 1 1069 ? 53.936  1.556   90.311  1.00 160.16 ? 1069 TRP B CZ3 1 
ATOM   20483 C  CH2 . TRP C 1 1069 ? 54.706  0.500   90.824  1.00 162.38 ? 1069 TRP B CH2 1 
ATOM   20484 N  N   . LYS C 1 1070 ? 56.187  7.343   86.591  1.00 142.16 ? 1070 LYS B N   1 
ATOM   20485 C  CA  . LYS C 1 1070 ? 55.650  8.610   86.092  1.00 141.43 ? 1070 LYS B CA  1 
ATOM   20486 C  C   . LYS C 1 1070 ? 54.143  8.719   86.193  1.00 144.61 ? 1070 LYS B C   1 
ATOM   20487 O  O   . LYS C 1 1070 ? 53.423  7.830   85.752  1.00 146.84 ? 1070 LYS B O   1 
ATOM   20488 C  CB  . LYS C 1 1070 ? 56.114  8.889   84.662  1.00 140.40 ? 1070 LYS B CB  1 
ATOM   20489 C  CG  . LYS C 1 1070 ? 57.361  9.751   84.615  1.00 137.21 ? 1070 LYS B CG  1 
ATOM   20490 C  CD  . LYS C 1 1070 ? 57.381  10.690  83.442  1.00 139.62 ? 1070 LYS B CD  1 
ATOM   20491 C  CE  . LYS C 1 1070 ? 57.919  10.017  82.207  1.00 141.15 ? 1070 LYS B CE  1 
ATOM   20492 N  NZ  . LYS C 1 1070 ? 58.149  11.053  81.173  1.00 143.59 ? 1070 LYS B NZ  1 
ATOM   20493 N  N   . GLY C 1 1071 ? 53.680  9.818   86.782  1.00 143.86 ? 1071 GLY B N   1 
ATOM   20494 C  CA  . GLY C 1 1071 ? 52.261  10.105  86.908  1.00 149.57 ? 1071 GLY B CA  1 
ATOM   20495 C  C   . GLY C 1 1071 ? 51.509  9.235   87.895  1.00 152.23 ? 1071 GLY B C   1 
ATOM   20496 O  O   . GLY C 1 1071 ? 50.435  9.625   88.367  1.00 157.90 ? 1071 GLY B O   1 
ATOM   20497 N  N   . GLY C 1 1072 ? 52.074  8.064   88.200  1.00 294.96 ? 1072 GLY B N   1 
ATOM   20498 C  CA  . GLY C 1 1072 ? 51.470  7.106   89.110  1.00 295.51 ? 1072 GLY B CA  1 
ATOM   20499 C  C   . GLY C 1 1072 ? 50.890  7.796   90.326  1.00 295.15 ? 1072 GLY B C   1 
ATOM   20500 O  O   . GLY C 1 1072 ? 51.340  8.882   90.694  1.00 293.63 ? 1072 GLY B O   1 
ATOM   20501 N  N   . SER C 1 1073 ? 49.884  7.185   90.945  1.00 196.61 ? 1073 SER B N   1 
ATOM   20502 C  CA  . SER C 1 1073 ? 49.234  7.814   92.083  1.00 195.43 ? 1073 SER B CA  1 
ATOM   20503 C  C   . SER C 1 1073 ? 50.333  8.159   93.062  1.00 189.10 ? 1073 SER B C   1 
ATOM   20504 O  O   . SER C 1 1073 ? 51.130  7.293   93.430  1.00 185.84 ? 1073 SER B O   1 
ATOM   20505 C  CB  . SER C 1 1073 ? 48.201  6.883   92.715  1.00 197.89 ? 1073 SER B CB  1 
ATOM   20506 O  OG  . SER C 1 1073 ? 48.706  5.565   92.834  1.00 198.90 ? 1073 SER B OG  1 
ATOM   20507 N  N   . ALA C 1 1074 ? 50.394  9.428   93.455  1.00 169.48 ? 1074 ALA B N   1 
ATOM   20508 C  CA  . ALA C 1 1074 ? 51.473  9.917   94.303  1.00 164.79 ? 1074 ALA B CA  1 
ATOM   20509 C  C   . ALA C 1 1074 ? 51.752  8.997   95.518  1.00 161.05 ? 1074 ALA B C   1 
ATOM   20510 O  O   . ALA C 1 1074 ? 50.866  8.714   96.327  1.00 163.08 ? 1074 ALA B O   1 
ATOM   20511 C  CB  . ALA C 1 1074 ? 51.171  11.343  94.740  1.00 166.92 ? 1074 ALA B CB  1 
ATOM   20512 N  N   . SER C 1 1075 ? 52.983  8.504   95.625  1.00 206.89 ? 1075 SER B N   1 
ATOM   20513 C  CA  . SER C 1 1075 ? 53.356  7.640   96.742  1.00 203.80 ? 1075 SER B CA  1 
ATOM   20514 C  C   . SER C 1 1075 ? 53.841  8.490   97.897  1.00 201.36 ? 1075 SER B C   1 
ATOM   20515 O  O   . SER C 1 1075 ? 54.709  9.338   97.714  1.00 198.06 ? 1075 SER B O   1 
ATOM   20516 C  CB  . SER C 1 1075 ? 54.466  6.674   96.327  1.00 203.56 ? 1075 SER B CB  1 
ATOM   20517 O  OG  . SER C 1 1075 ? 55.622  7.367   95.882  1.00 202.65 ? 1075 SER B OG  1 
ATOM   20518 N  N   . THR C 1 1076 ? 53.294  8.273   99.086  1.00 167.44 ? 1076 THR B N   1 
ATOM   20519 C  CA  . THR C 1 1076 ? 53.769  9.006   100.258 1.00 162.60 ? 1076 THR B CA  1 
ATOM   20520 C  C   . THR C 1 1076 ? 55.205  8.568   100.630 1.00 158.63 ? 1076 THR B C   1 
ATOM   20521 O  O   . THR C 1 1076 ? 56.043  9.391   101.030 1.00 157.36 ? 1076 THR B O   1 
ATOM   20522 C  CB  . THR C 1 1076 ? 52.788  8.848   101.450 1.00 161.11 ? 1076 THR B CB  1 
ATOM   20523 O  OG1 . THR C 1 1076 ? 52.884  9.982   102.327 1.00 162.64 ? 1076 THR B OG1 1 
ATOM   20524 C  CG2 . THR C 1 1076 ? 53.063  7.568   102.216 1.00 157.73 ? 1076 THR B CG2 1 
ATOM   20525 N  N   . TRP C 1 1077 ? 55.465  7.268   100.460 1.00 166.89 ? 1077 TRP B N   1 
ATOM   20526 C  CA  . TRP C 1 1077 ? 56.767  6.619   100.678 1.00 164.59 ? 1077 TRP B CA  1 
ATOM   20527 C  C   . TRP C 1 1077 ? 57.909  7.320   99.925  1.00 158.86 ? 1077 TRP B C   1 
ATOM   20528 O  O   . TRP C 1 1077 ? 58.821  7.881   100.536 1.00 153.49 ? 1077 TRP B O   1 
ATOM   20529 C  CB  . TRP C 1 1077 ? 56.653  5.154   100.224 1.00 167.76 ? 1077 TRP B CB  1 
ATOM   20530 C  CG  . TRP C 1 1077 ? 57.827  4.259   100.474 1.00 170.17 ? 1077 TRP B CG  1 
ATOM   20531 C  CD1 . TRP C 1 1077 ? 58.004  3.437   101.543 1.00 172.09 ? 1077 TRP B CD1 1 
ATOM   20532 C  CD2 . TRP C 1 1077 ? 58.962  4.048   99.612  1.00 171.94 ? 1077 TRP B CD2 1 
ATOM   20533 N  NE1 . TRP C 1 1077 ? 59.183  2.747   101.416 1.00 172.87 ? 1077 TRP B NE1 1 
ATOM   20534 C  CE2 . TRP C 1 1077 ? 59.788  3.103   100.238 1.00 172.55 ? 1077 TRP B CE2 1 
ATOM   20535 C  CE3 . TRP C 1 1077 ? 59.365  4.579   98.383  1.00 173.20 ? 1077 TRP B CE3 1 
ATOM   20536 C  CZ2 . TRP C 1 1077 ? 60.992  2.675   99.672  1.00 171.16 ? 1077 TRP B CZ2 1 
ATOM   20537 C  CZ3 . TRP C 1 1077 ? 60.565  4.152   97.827  1.00 173.33 ? 1077 TRP B CZ3 1 
ATOM   20538 C  CH2 . TRP C 1 1077 ? 61.358  3.213   98.467  1.00 171.21 ? 1077 TRP B CH2 1 
ATOM   20539 N  N   . LEU C 1 1078 ? 57.846  7.289   98.595  1.00 159.01 ? 1078 LEU B N   1 
ATOM   20540 C  CA  . LEU C 1 1078 ? 58.837  7.959   97.760  1.00 156.47 ? 1078 LEU B CA  1 
ATOM   20541 C  C   . LEU C 1 1078 ? 58.818  9.470   97.996  1.00 157.80 ? 1078 LEU B C   1 
ATOM   20542 O  O   . LEU C 1 1078 ? 59.868  10.116  97.999  1.00 157.74 ? 1078 LEU B O   1 
ATOM   20543 C  CB  . LEU C 1 1078 ? 58.612  7.626   96.279  1.00 153.82 ? 1078 LEU B CB  1 
ATOM   20544 C  CG  . LEU C 1 1078 ? 59.810  7.916   95.372  1.00 147.78 ? 1078 LEU B CG  1 
ATOM   20545 C  CD1 . LEU C 1 1078 ? 59.874  6.984   94.182  1.00 146.04 ? 1078 LEU B CD1 1 
ATOM   20546 C  CD2 . LEU C 1 1078 ? 59.765  9.351   94.924  1.00 147.63 ? 1078 LEU B CD2 1 
ATOM   20547 N  N   . THR C 1 1079 ? 57.628  10.022  98.224  1.00 164.69 ? 1079 THR B N   1 
ATOM   20548 C  CA  . THR C 1 1079 ? 57.481  11.458  98.449  1.00 165.15 ? 1079 THR B CA  1 
ATOM   20549 C  C   . THR C 1 1079 ? 58.462  11.909  99.504  1.00 161.93 ? 1079 THR B C   1 
ATOM   20550 O  O   . THR C 1 1079 ? 58.963  13.031  99.457  1.00 162.14 ? 1079 THR B O   1 
ATOM   20551 C  CB  . THR C 1 1079 ? 56.058  11.828  98.897  1.00 177.43 ? 1079 THR B CB  1 
ATOM   20552 O  OG1 . THR C 1 1079 ? 55.151  11.682  97.794  1.00 179.91 ? 1079 THR B OG1 1 
ATOM   20553 C  CG2 . THR C 1 1079 ? 56.009  13.269  99.394  1.00 176.18 ? 1079 THR B CG2 1 
ATOM   20554 N  N   . ALA C 1 1080 ? 58.732  11.036  100.464 1.00 115.18 ? 1080 ALA B N   1 
ATOM   20555 C  CA  . ALA C 1 1080 ? 59.776  11.336  101.425 1.00 110.37 ? 1080 ALA B CA  1 
ATOM   20556 C  C   . ALA C 1 1080 ? 61.148  10.924  100.914 1.00 106.95 ? 1080 ALA B C   1 
ATOM   20557 O  O   . ALA C 1 1080 ? 62.102  11.692  101.026 1.00 104.51 ? 1080 ALA B O   1 
ATOM   20558 C  CB  . ALA C 1 1080 ? 59.497  10.679  102.741 1.00 110.33 ? 1080 ALA B CB  1 
ATOM   20559 N  N   . PHE C 1 1081 ? 61.273  9.713   100.377 1.00 146.46 ? 1081 PHE B N   1 
ATOM   20560 C  CA  . PHE C 1 1081 ? 62.600  9.279   99.961  1.00 143.26 ? 1081 PHE B CA  1 
ATOM   20561 C  C   . PHE C 1 1081 ? 63.253  10.324  99.088  1.00 139.60 ? 1081 PHE B C   1 
ATOM   20562 O  O   . PHE C 1 1081 ? 64.464  10.488  99.113  1.00 134.97 ? 1081 PHE B O   1 
ATOM   20563 C  CB  . PHE C 1 1081 ? 62.595  7.952   99.226  1.00 146.75 ? 1081 PHE B CB  1 
ATOM   20564 C  CG  . PHE C 1 1081 ? 63.981  7.480   98.835  1.00 148.70 ? 1081 PHE B CG  1 
ATOM   20565 C  CD1 . PHE C 1 1081 ? 64.564  6.408   99.481  1.00 148.72 ? 1081 PHE B CD1 1 
ATOM   20566 C  CD2 . PHE C 1 1081 ? 64.706  8.110   97.833  1.00 152.50 ? 1081 PHE B CD2 1 
ATOM   20567 C  CE1 . PHE C 1 1081 ? 65.841  5.960   99.134  1.00 149.07 ? 1081 PHE B CE1 1 
ATOM   20568 C  CE2 . PHE C 1 1081 ? 65.979  7.664   97.485  1.00 153.06 ? 1081 PHE B CE2 1 
ATOM   20569 C  CZ  . PHE C 1 1081 ? 66.544  6.588   98.138  1.00 151.17 ? 1081 PHE B CZ  1 
ATOM   20570 N  N   . ALA C 1 1082 ? 62.465  11.022  98.288  1.00 190.95 ? 1082 ALA B N   1 
ATOM   20571 C  CA  . ALA C 1 1082 ? 63.037  12.172  97.614  1.00 191.86 ? 1082 ALA B CA  1 
ATOM   20572 C  C   . ALA C 1 1082 ? 63.316  13.226  98.680  1.00 190.12 ? 1082 ALA B C   1 
ATOM   20573 O  O   . ALA C 1 1082 ? 64.418  13.783  98.725  1.00 189.11 ? 1082 ALA B O   1 
ATOM   20574 C  CB  . ALA C 1 1082 ? 62.121  12.713  96.535  1.00 195.63 ? 1082 ALA B CB  1 
ATOM   20575 N  N   . LEU C 1 1083 ? 62.338  13.482  99.553  1.00 92.71  ? 1083 LEU B N   1 
ATOM   20576 C  CA  . LEU C 1 1083 ? 62.486  14.564  100.521 1.00 89.59  ? 1083 LEU B CA  1 
ATOM   20577 C  C   . LEU C 1 1083 ? 63.844  14.364  101.049 1.00 89.01  ? 1083 LEU B C   1 
ATOM   20578 O  O   . LEU C 1 1083 ? 64.726  15.175  100.838 1.00 90.61  ? 1083 LEU B O   1 
ATOM   20579 C  CB  . LEU C 1 1083 ? 61.453  14.454  101.632 1.00 86.74  ? 1083 LEU B CB  1 
ATOM   20580 C  CG  . LEU C 1 1083 ? 60.209  15.257  101.227 1.00 86.44  ? 1083 LEU B CG  1 
ATOM   20581 C  CD1 . LEU C 1 1083 ? 58.928  14.875  101.966 1.00 88.34  ? 1083 LEU B CD1 1 
ATOM   20582 C  CD2 . LEU C 1 1083 ? 60.495  16.742  101.357 1.00 89.03  ? 1083 LEU B CD2 1 
ATOM   20583 N  N   . ARG C 1 1084 ? 64.015  13.212  101.668 1.00 113.02 ? 1084 ARG B N   1 
ATOM   20584 C  CA  . ARG C 1 1084 ? 65.319  12.793  102.124 1.00 113.32 ? 1084 ARG B CA  1 
ATOM   20585 C  C   . ARG C 1 1084 ? 66.476  13.224  101.163 1.00 115.34 ? 1084 ARG B C   1 
ATOM   20586 O  O   . ARG C 1 1084 ? 67.207  14.181  101.461 1.00 115.34 ? 1084 ARG B O   1 
ATOM   20587 C  CB  . ARG C 1 1084 ? 65.316  11.287  102.472 1.00 114.75 ? 1084 ARG B CB  1 
ATOM   20588 C  CG  . ARG C 1 1084 ? 66.693  10.697  102.580 1.00 110.24 ? 1084 ARG B CG  1 
ATOM   20589 C  CD  . ARG C 1 1084 ? 66.820  9.649   103.623 1.00 111.73 ? 1084 ARG B CD  1 
ATOM   20590 N  NE  . ARG C 1 1084 ? 68.194  9.168   103.636 1.00 115.50 ? 1084 ARG B NE  1 
ATOM   20591 C  CZ  . ARG C 1 1084 ? 68.538  7.891   103.724 1.00 122.14 ? 1084 ARG B CZ  1 
ATOM   20592 N  NH1 . ARG C 1 1084 ? 67.602  6.960   103.839 1.00 127.14 ? 1084 ARG B NH1 1 
ATOM   20593 N  NH2 . ARG C 1 1084 ? 69.820  7.553   103.710 1.00 121.50 ? 1084 ARG B NH2 1 
ATOM   20594 N  N   . VAL C 1 1085 ? 66.648  12.570  100.015 1.00 121.76 ? 1085 VAL B N   1 
ATOM   20595 C  CA  . VAL C 1 1085 ? 67.840  12.876  99.212  1.00 124.28 ? 1085 VAL B CA  1 
ATOM   20596 C  C   . VAL C 1 1085 ? 67.715  14.236  98.532  1.00 124.73 ? 1085 VAL B C   1 
ATOM   20597 O  O   . VAL C 1 1085 ? 68.574  14.636  97.758  1.00 123.50 ? 1085 VAL B O   1 
ATOM   20598 C  CB  . VAL C 1 1085 ? 68.222  11.760  98.191  1.00 115.15 ? 1085 VAL B CB  1 
ATOM   20599 C  CG1 . VAL C 1 1085 ? 69.715  11.838  97.821  1.00 113.38 ? 1085 VAL B CG1 1 
ATOM   20600 C  CG2 . VAL C 1 1085 ? 67.885  10.370  98.737  1.00 112.88 ? 1085 VAL B CG2 1 
ATOM   20601 N  N   . LEU C 1 1086 ? 66.627  14.934  98.823  1.00 192.08 ? 1086 LEU B N   1 
ATOM   20602 C  CA  . LEU C 1 1086 ? 66.463  16.303  98.376  1.00 197.06 ? 1086 LEU B CA  1 
ATOM   20603 C  C   . LEU C 1 1086 ? 67.140  17.238  99.350  1.00 196.04 ? 1086 LEU B C   1 
ATOM   20604 O  O   . LEU C 1 1086 ? 67.903  18.128  98.956  1.00 197.25 ? 1086 LEU B O   1 
ATOM   20605 C  CB  . LEU C 1 1086 ? 64.987  16.649  98.300  1.00 202.07 ? 1086 LEU B CB  1 
ATOM   20606 C  CG  . LEU C 1 1086 ? 64.427  16.671  96.890  1.00 210.81 ? 1086 LEU B CG  1 
ATOM   20607 C  CD1 . LEU C 1 1086 ? 64.944  17.884  96.129  1.00 209.90 ? 1086 LEU B CD1 1 
ATOM   20608 C  CD2 . LEU C 1 1086 ? 64.790  15.381  96.181  1.00 211.70 ? 1086 LEU B CD2 1 
ATOM   20609 N  N   . GLY C 1 1087 ? 66.841  17.028  100.631 1.00 144.44 ? 1087 GLY B N   1 
ATOM   20610 C  CA  . GLY C 1 1087 ? 67.380  17.838  101.713 1.00 141.75 ? 1087 GLY B CA  1 
ATOM   20611 C  C   . GLY C 1 1087 ? 68.837  17.519  101.973 1.00 137.51 ? 1087 GLY B C   1 
ATOM   20612 O  O   . GLY C 1 1087 ? 69.562  18.332  102.545 1.00 138.66 ? 1087 GLY B O   1 
ATOM   20613 N  N   . GLN C 1 1088 ? 69.260  16.328  101.557 1.00 111.73 ? 1088 GLN B N   1 
ATOM   20614 C  CA  . GLN C 1 1088 ? 70.653  15.923  101.695 1.00 111.96 ? 1088 GLN B CA  1 
ATOM   20615 C  C   . GLN C 1 1088 ? 71.540  16.689  100.708 1.00 116.97 ? 1088 GLN B C   1 
ATOM   20616 O  O   . GLN C 1 1088 ? 72.599  17.213  101.060 1.00 116.67 ? 1088 GLN B O   1 
ATOM   20617 C  CB  . GLN C 1 1088 ? 70.808  14.423  101.449 1.00 110.88 ? 1088 GLN B CB  1 
ATOM   20618 C  CG  . GLN C 1 1088 ? 70.080  13.522  102.429 1.00 112.41 ? 1088 GLN B CG  1 
ATOM   20619 C  CD  . GLN C 1 1088 ? 70.579  12.076  102.372 1.00 112.94 ? 1088 GLN B CD  1 
ATOM   20620 O  OE1 . GLN C 1 1088 ? 69.831  11.125  102.647 1.00 112.01 ? 1088 GLN B OE1 1 
ATOM   20621 N  NE2 . GLN C 1 1088 ? 71.857  11.908  102.024 1.00 112.39 ? 1088 GLN B NE2 1 
ATOM   20622 N  N   . VAL C 1 1089 ? 71.103  16.750  99.460  1.00 159.34 ? 1089 VAL B N   1 
ATOM   20623 C  CA  . VAL C 1 1089 ? 71.845  17.483  98.452  1.00 160.38 ? 1089 VAL B CA  1 
ATOM   20624 C  C   . VAL C 1 1089 ? 71.597  18.982  98.633  1.00 163.14 ? 1089 VAL B C   1 
ATOM   20625 O  O   . VAL C 1 1089 ? 72.198  19.809  97.964  1.00 162.12 ? 1089 VAL B O   1 
ATOM   20626 C  CB  . VAL C 1 1089 ? 71.479  16.987  97.053  1.00 154.21 ? 1089 VAL B CB  1 
ATOM   20627 C  CG1 . VAL C 1 1089 ? 72.420  17.545  96.040  1.00 152.86 ? 1089 VAL B CG1 1 
ATOM   20628 C  CG2 . VAL C 1 1089 ? 71.538  15.457  97.029  1.00 154.34 ? 1089 VAL B CG2 1 
ATOM   20629 N  N   . ASN C 1 1090 ? 70.723  19.341  99.563  1.00 129.18 ? 1090 ASN B N   1 
ATOM   20630 C  CA  . ASN C 1 1090 ? 70.489  20.749  99.794  1.00 134.82 ? 1090 ASN B CA  1 
ATOM   20631 C  C   . ASN C 1 1090 ? 71.717  21.397  100.391 1.00 136.00 ? 1090 ASN B C   1 
ATOM   20632 O  O   . ASN C 1 1090 ? 71.853  22.618  100.406 1.00 136.94 ? 1090 ASN B O   1 
ATOM   20633 C  CB  . ASN C 1 1090 ? 69.296  20.980  100.703 1.00 137.92 ? 1090 ASN B CB  1 
ATOM   20634 C  CG  . ASN C 1 1090 ? 68.945  22.445  100.817 1.00 141.73 ? 1090 ASN B CG  1 
ATOM   20635 O  OD1 . ASN C 1 1090 ? 69.797  23.297  101.077 1.00 140.63 ? 1090 ASN B OD1 1 
ATOM   20636 N  ND2 . ASN C 1 1090 ? 67.683  22.752  100.600 1.00 146.36 ? 1090 ASN B ND2 1 
ATOM   20637 N  N   . LYS C 1 1091 ? 72.616  20.567  100.894 1.00 143.54 ? 1091 LYS B N   1 
ATOM   20638 C  CA  . LYS C 1 1091 ? 73.816  21.065  101.538 1.00 144.93 ? 1091 LYS B CA  1 
ATOM   20639 C  C   . LYS C 1 1091 ? 74.628  21.884  100.568 1.00 141.47 ? 1091 LYS B C   1 
ATOM   20640 O  O   . LYS C 1 1091 ? 75.110  22.957  100.910 1.00 142.75 ? 1091 LYS B O   1 
ATOM   20641 C  CB  . LYS C 1 1091 ? 74.671  19.914  102.072 1.00 152.08 ? 1091 LYS B CB  1 
ATOM   20642 C  CG  . LYS C 1 1091 ? 74.294  19.411  103.473 1.00 159.98 ? 1091 LYS B CG  1 
ATOM   20643 C  CD  . LYS C 1 1091 ? 75.544  18.937  104.200 1.00 165.93 ? 1091 LYS B CD  1 
ATOM   20644 C  CE  . LYS C 1 1091 ? 76.582  20.053  104.157 1.00 171.35 ? 1091 LYS B CE  1 
ATOM   20645 N  NZ  . LYS C 1 1091 ? 77.763  19.811  105.033 1.00 173.85 ? 1091 LYS B NZ  1 
ATOM   20646 N  N   . TYR C 1 1092 ? 74.761  21.385  99.347  1.00 145.21 ? 1092 TYR B N   1 
ATOM   20647 C  CA  . TYR C 1 1092 ? 75.685  21.992  98.399  1.00 144.61 ? 1092 TYR B CA  1 
ATOM   20648 C  C   . TYR C 1 1092 ? 75.026  22.469  97.107  1.00 152.25 ? 1092 TYR B C   1 
ATOM   20649 O  O   . TYR C 1 1092 ? 75.662  23.086  96.250  1.00 155.60 ? 1092 TYR B O   1 
ATOM   20650 C  CB  . TYR C 1 1092 ? 76.797  21.005  98.074  1.00 139.19 ? 1092 TYR B CB  1 
ATOM   20651 C  CG  . TYR C 1 1092 ? 77.327  20.238  99.261  1.00 135.78 ? 1092 TYR B CG  1 
ATOM   20652 C  CD1 . TYR C 1 1092 ? 78.153  20.843  100.195 1.00 135.89 ? 1092 TYR B CD1 1 
ATOM   20653 C  CD2 . TYR C 1 1092 ? 77.021  18.898  99.437  1.00 136.15 ? 1092 TYR B CD2 1 
ATOM   20654 C  CE1 . TYR C 1 1092 ? 78.657  20.140  101.273 1.00 136.78 ? 1092 TYR B CE1 1 
ATOM   20655 C  CE2 . TYR C 1 1092 ? 77.520  18.182  100.517 1.00 135.83 ? 1092 TYR B CE2 1 
ATOM   20656 C  CZ  . TYR C 1 1092 ? 78.340  18.811  101.430 1.00 136.43 ? 1092 TYR B CZ  1 
ATOM   20657 O  OH  . TYR C 1 1092 ? 78.844  18.109  102.499 1.00 136.28 ? 1092 TYR B OH  1 
ATOM   20658 N  N   . VAL C 1 1093 ? 73.749  22.168  96.962  1.00 183.20 ? 1093 VAL B N   1 
ATOM   20659 C  CA  . VAL C 1 1093 ? 73.013  22.585  95.786  1.00 184.73 ? 1093 VAL B CA  1 
ATOM   20660 C  C   . VAL C 1 1093 ? 71.669  23.052  96.296  1.00 183.08 ? 1093 VAL B C   1 
ATOM   20661 O  O   . VAL C 1 1093 ? 70.750  22.254  96.504  1.00 182.08 ? 1093 VAL B O   1 
ATOM   20662 C  CB  . VAL C 1 1093 ? 72.883  21.416  94.767  1.00 186.16 ? 1093 VAL B CB  1 
ATOM   20663 C  CG1 . VAL C 1 1093 ? 71.846  21.714  93.694  1.00 190.83 ? 1093 VAL B CG1 1 
ATOM   20664 C  CG2 . VAL C 1 1093 ? 74.246  21.109  94.148  1.00 184.51 ? 1093 VAL B CG2 1 
ATOM   20665 N  N   . GLU C 1 1094 ? 71.575  24.355  96.538  1.00 139.16 ? 1094 GLU B N   1 
ATOM   20666 C  CA  . GLU C 1 1094 ? 70.377  24.896  97.162  1.00 139.10 ? 1094 GLU B CA  1 
ATOM   20667 C  C   . GLU C 1 1094 ? 69.205  24.317  96.435  1.00 138.71 ? 1094 GLU B C   1 
ATOM   20668 O  O   . GLU C 1 1094 ? 69.201  24.265  95.219  1.00 143.04 ? 1094 GLU B O   1 
ATOM   20669 C  CB  . GLU C 1 1094 ? 70.276  26.419  97.067  1.00 144.27 ? 1094 GLU B CB  1 
ATOM   20670 C  CG  . GLU C 1 1094 ? 68.864  26.897  97.471  1.00 150.94 ? 1094 GLU B CG  1 
ATOM   20671 C  CD  . GLU C 1 1094 ? 68.713  28.408  97.598  1.00 158.61 ? 1094 GLU B CD  1 
ATOM   20672 O  OE1 . GLU C 1 1094 ? 69.586  29.160  97.085  1.00 160.87 ? 1094 GLU B OE1 1 
ATOM   20673 O  OE2 . GLU C 1 1094 ? 67.695  28.827  98.208  1.00 162.07 ? 1094 GLU B OE2 1 
ATOM   20674 N  N   . GLN C 1 1095 ? 68.206  23.869  97.167  1.00 120.84 ? 1095 GLN B N   1 
ATOM   20675 C  CA  . GLN C 1 1095 ? 67.022  23.394  96.508  1.00 122.96 ? 1095 GLN B CA  1 
ATOM   20676 C  C   . GLN C 1 1095 ? 65.907  24.408  96.624  1.00 130.73 ? 1095 GLN B C   1 
ATOM   20677 O  O   . GLN C 1 1095 ? 65.934  25.300  97.476  1.00 132.39 ? 1095 GLN B O   1 
ATOM   20678 C  CB  . GLN C 1 1095 ? 66.625  22.035  97.047  1.00 120.16 ? 1095 GLN B CB  1 
ATOM   20679 C  CG  . GLN C 1 1095 ? 67.683  20.982  96.780  1.00 122.89 ? 1095 GLN B CG  1 
ATOM   20680 C  CD  . GLN C 1 1095 ? 67.923  20.756  95.291  1.00 152.81 ? 1095 GLN B CD  1 
ATOM   20681 O  OE1 . GLN C 1 1095 ? 66.982  20.620  94.505  1.00 154.23 ? 1095 GLN B OE1 1 
ATOM   20682 N  NE2 . GLN C 1 1095 ? 69.191  20.707  94.898  1.00 151.80 ? 1095 GLN B NE2 1 
ATOM   20683 N  N   . ASN C 1 1096 ? 64.942  24.269  95.725  1.00 187.04 ? 1096 ASN B N   1 
ATOM   20684 C  CA  . ASN C 1 1096 ? 63.863  25.224  95.591  1.00 194.04 ? 1096 ASN B CA  1 
ATOM   20685 C  C   . ASN C 1 1096 ? 63.062  25.283  96.874  1.00 195.30 ? 1096 ASN B C   1 
ATOM   20686 O  O   . ASN C 1 1096 ? 62.408  24.310  97.238  1.00 194.35 ? 1096 ASN B O   1 
ATOM   20687 C  CB  . ASN C 1 1096 ? 62.974  24.841  94.400  1.00 200.01 ? 1096 ASN B CB  1 
ATOM   20688 C  CG  . ASN C 1 1096 ? 61.846  25.831  94.166  1.00 207.65 ? 1096 ASN B CG  1 
ATOM   20689 O  OD1 . ASN C 1 1096 ? 61.710  26.395  93.073  1.00 213.04 ? 1096 ASN B OD1 1 
ATOM   20690 N  ND2 . ASN C 1 1096 ? 61.029  26.049  95.195  1.00 208.13 ? 1096 ASN B ND2 1 
ATOM   20691 N  N   . GLN C 1 1097 ? 63.108  26.422  97.557  1.00 163.46 ? 1097 GLN B N   1 
ATOM   20692 C  CA  . GLN C 1 1097 ? 62.405  26.512  98.816  1.00 165.81 ? 1097 GLN B CA  1 
ATOM   20693 C  C   . GLN C 1 1097 ? 60.959  26.095  98.639  1.00 169.99 ? 1097 GLN B C   1 
ATOM   20694 O  O   . GLN C 1 1097 ? 60.641  24.921  98.759  1.00 167.99 ? 1097 GLN B O   1 
ATOM   20695 C  CB  . GLN C 1 1097 ? 62.506  27.885  99.493  1.00 165.74 ? 1097 GLN B CB  1 
ATOM   20696 C  CG  . GLN C 1 1097 ? 61.834  27.855  100.887 1.00 164.63 ? 1097 GLN B CG  1 
ATOM   20697 C  CD  . GLN C 1 1097 ? 62.379  28.854  101.915 1.00 166.38 ? 1097 GLN B CD  1 
ATOM   20698 O  OE1 . GLN C 1 1097 ? 63.019  29.846  101.570 1.00 166.81 ? 1097 GLN B OE1 1 
ATOM   20699 N  NE2 . GLN C 1 1097 ? 62.100  28.592  103.191 1.00 166.39 ? 1097 GLN B NE2 1 
ATOM   20700 N  N   . ASN C 1 1098 ? 60.084  27.039  98.332  1.00 172.00 ? 1098 ASN B N   1 
ATOM   20701 C  CA  . ASN C 1 1098 ? 58.659  26.747  98.377  1.00 176.70 ? 1098 ASN B CA  1 
ATOM   20702 C  C   . ASN C 1 1098 ? 58.276  25.384  97.800  1.00 161.16 ? 1098 ASN B C   1 
ATOM   20703 O  O   . ASN C 1 1098 ? 57.213  24.855  98.108  1.00 160.12 ? 1098 ASN B O   1 
ATOM   20704 C  CB  . ASN C 1 1098 ? 57.843  27.860  97.732  1.00 183.45 ? 1098 ASN B CB  1 
ATOM   20705 C  CG  . ASN C 1 1098 ? 56.365  27.546  97.704  1.00 189.89 ? 1098 ASN B CG  1 
ATOM   20706 O  OD1 . ASN C 1 1098 ? 55.818  27.202  96.656  1.00 192.69 ? 1098 ASN B OD1 1 
ATOM   20707 N  ND2 . ASN C 1 1098 ? 55.712  27.641  98.858  1.00 193.09 ? 1098 ASN B ND2 1 
ATOM   20708 N  N   . SER C 1 1099 ? 59.146  24.809  96.976  1.00 181.72 ? 1099 SER B N   1 
ATOM   20709 C  CA  . SER C 1 1099 ? 58.934  23.448  96.498  1.00 177.50 ? 1099 SER B CA  1 
ATOM   20710 C  C   . SER C 1 1099 ? 58.957  22.510  97.691  1.00 171.88 ? 1099 SER B C   1 
ATOM   20711 O  O   . SER C 1 1099 ? 57.935  21.931  98.074  1.00 173.99 ? 1099 SER B O   1 
ATOM   20712 C  CB  . SER C 1 1099 ? 60.026  23.045  95.497  1.00 174.22 ? 1099 SER B CB  1 
ATOM   20713 O  OG  . SER C 1 1099 ? 60.084  21.637  95.286  1.00 171.07 ? 1099 SER B OG  1 
ATOM   20714 N  N   . ILE C 1 1100 ? 60.140  22.379  98.281  1.00 163.95 ? 1100 ILE B N   1 
ATOM   20715 C  CA  . ILE C 1 1100 ? 60.352  21.492  99.411  1.00 156.54 ? 1100 ILE B CA  1 
ATOM   20716 C  C   . ILE C 1 1100 ? 59.267  21.720  100.443 1.00 159.60 ? 1100 ILE B C   1 
ATOM   20717 O  O   . ILE C 1 1100 ? 58.668  20.773  100.940 1.00 159.16 ? 1100 ILE B O   1 
ATOM   20718 C  CB  . ILE C 1 1100 ? 61.725  21.749  100.048 1.00 146.69 ? 1100 ILE B CB  1 
ATOM   20719 C  CG1 . ILE C 1 1100 ? 62.816  20.946  99.335  1.00 139.92 ? 1100 ILE B CG1 1 
ATOM   20720 C  CG2 . ILE C 1 1100 ? 61.691  21.405  101.506 1.00 144.41 ? 1100 ILE B CG2 1 
ATOM   20721 C  CD1 . ILE C 1 1100 ? 62.750  19.454  99.598  1.00 136.94 ? 1100 ILE B CD1 1 
ATOM   20722 N  N   . CYS C 1 1101 ? 59.006  22.987  100.745 1.00 153.58 ? 1101 CYS B N   1 
ATOM   20723 C  CA  . CYS C 1 1101 ? 57.952  23.349  101.692 1.00 155.65 ? 1101 CYS B CA  1 
ATOM   20724 C  C   . CYS C 1 1101 ? 56.706  22.513  101.439 1.00 155.74 ? 1101 CYS B C   1 
ATOM   20725 O  O   . CYS C 1 1101 ? 56.369  21.638  102.224 1.00 154.37 ? 1101 CYS B O   1 
ATOM   20726 C  CB  . CYS C 1 1101 ? 57.604  24.847  101.608 1.00 159.57 ? 1101 CYS B CB  1 
ATOM   20727 S  SG  . CYS C 1 1101 ? 58.542  25.960  102.721 1.00 184.17 ? 1101 CYS B SG  1 
ATOM   20728 N  N   . ASN C 1 1102 ? 56.029  22.771  100.331 1.00 158.26 ? 1102 ASN B N   1 
ATOM   20729 C  CA  . ASN C 1 1102 ? 54.800  22.066  100.054 1.00 158.83 ? 1102 ASN B CA  1 
ATOM   20730 C  C   . ASN C 1 1102 ? 55.022  20.580  100.084 1.00 156.04 ? 1102 ASN B C   1 
ATOM   20731 O  O   . ASN C 1 1102 ? 54.166  19.842  100.564 1.00 156.16 ? 1102 ASN B O   1 
ATOM   20732 C  CB  . ASN C 1 1102 ? 54.252  22.513  98.725  1.00 160.44 ? 1102 ASN B CB  1 
ATOM   20733 C  CG  . ASN C 1 1102 ? 53.777  23.926  98.782  1.00 162.88 ? 1102 ASN B CG  1 
ATOM   20734 O  OD1 . ASN C 1 1102 ? 52.962  24.266  99.637  1.00 165.62 ? 1102 ASN B OD1 1 
ATOM   20735 N  ND2 . ASN C 1 1102 ? 54.299  24.775  97.904  1.00 161.68 ? 1102 ASN B ND2 1 
ATOM   20736 N  N   . SER C 1 1103 ? 56.196  20.154  99.616  1.00 197.41 ? 1103 SER B N   1 
ATOM   20737 C  CA  . SER C 1 1103 ? 56.565  18.736  99.555  1.00 194.92 ? 1103 SER B CA  1 
ATOM   20738 C  C   . SER C 1 1103 ? 56.577  18.052  100.933 1.00 194.95 ? 1103 SER B C   1 
ATOM   20739 O  O   . SER C 1 1103 ? 56.251  16.866  101.050 1.00 194.17 ? 1103 SER B O   1 
ATOM   20740 C  CB  . SER C 1 1103 ? 57.906  18.561  98.832  1.00 192.29 ? 1103 SER B CB  1 
ATOM   20741 O  OG  . SER C 1 1103 ? 57.780  18.855  97.446  1.00 193.47 ? 1103 SER B OG  1 
ATOM   20742 N  N   . LEU C 1 1104 ? 56.962  18.802  101.966 1.00 146.06 ? 1104 LEU B N   1 
ATOM   20743 C  CA  . LEU C 1 1104 ? 56.806  18.357  103.352 1.00 146.29 ? 1104 LEU B CA  1 
ATOM   20744 C  C   . LEU C 1 1104 ? 55.312  18.445  103.714 1.00 153.50 ? 1104 LEU B C   1 
ATOM   20745 O  O   . LEU C 1 1104 ? 54.659  17.428  103.979 1.00 154.02 ? 1104 LEU B O   1 
ATOM   20746 C  CB  . LEU C 1 1104 ? 57.658  19.209  104.333 1.00 142.74 ? 1104 LEU B CB  1 
ATOM   20747 C  CG  . LEU C 1 1104 ? 59.200  19.127  104.437 1.00 137.69 ? 1104 LEU B CG  1 
ATOM   20748 C  CD1 . LEU C 1 1104 ? 59.765  20.293  105.232 1.00 136.64 ? 1104 LEU B CD1 1 
ATOM   20749 C  CD2 . LEU C 1 1104 ? 59.685  17.832  105.033 1.00 133.48 ? 1104 LEU B CD2 1 
ATOM   20750 N  N   . LEU C 1 1105 ? 54.782  19.672  103.675 1.00 140.25 ? 1105 LEU B N   1 
ATOM   20751 C  CA  . LEU C 1 1105 ? 53.391  19.988  104.029 1.00 145.32 ? 1105 LEU B CA  1 
ATOM   20752 C  C   . LEU C 1 1105 ? 52.349  19.150  103.296 1.00 147.21 ? 1105 LEU B C   1 
ATOM   20753 O  O   . LEU C 1 1105 ? 51.150  19.292  103.522 1.00 151.13 ? 1105 LEU B O   1 
ATOM   20754 C  CB  . LEU C 1 1105 ? 53.102  21.482  103.815 1.00 147.93 ? 1105 LEU B CB  1 
ATOM   20755 C  CG  . LEU C 1 1105 ? 53.597  22.487  104.867 1.00 149.42 ? 1105 LEU B CG  1 
ATOM   20756 C  CD1 . LEU C 1 1105 ? 54.114  23.745  104.188 1.00 151.78 ? 1105 LEU B CD1 1 
ATOM   20757 C  CD2 . LEU C 1 1105 ? 52.503  22.838  105.858 1.00 152.98 ? 1105 LEU B CD2 1 
ATOM   20758 N  N   . TRP C 1 1106 ? 52.796  18.287  102.402 1.00 157.97 ? 1106 TRP B N   1 
ATOM   20759 C  CA  . TRP C 1 1106 ? 51.861  17.370  101.791 1.00 160.05 ? 1106 TRP B CA  1 
ATOM   20760 C  C   . TRP C 1 1106 ? 51.641  16.190  102.730 1.00 158.42 ? 1106 TRP B C   1 
ATOM   20761 O  O   . TRP C 1 1106 ? 50.514  15.972  103.190 1.00 160.91 ? 1106 TRP B O   1 
ATOM   20762 C  CB  . TRP C 1 1106 ? 52.332  16.908  100.410 1.00 159.67 ? 1106 TRP B CB  1 
ATOM   20763 C  CG  . TRP C 1 1106 ? 51.398  15.941  99.800  1.00 159.72 ? 1106 TRP B CG  1 
ATOM   20764 C  CD1 . TRP C 1 1106 ? 50.093  16.154  99.478  1.00 160.91 ? 1106 TRP B CD1 1 
ATOM   20765 C  CD2 . TRP C 1 1106 ? 51.685  14.589  99.458  1.00 159.30 ? 1106 TRP B CD2 1 
ATOM   20766 N  NE1 . TRP C 1 1106 ? 49.549  15.012  98.954  1.00 161.19 ? 1106 TRP B NE1 1 
ATOM   20767 C  CE2 . TRP C 1 1106 ? 50.510  14.034  98.934  1.00 160.87 ? 1106 TRP B CE2 1 
ATOM   20768 C  CE3 . TRP C 1 1106 ? 52.825  13.790  99.547  1.00 159.21 ? 1106 TRP B CE3 1 
ATOM   20769 C  CZ2 . TRP C 1 1106 ? 50.443  12.715  98.493  1.00 163.46 ? 1106 TRP B CZ2 1 
ATOM   20770 C  CZ3 . TRP C 1 1106 ? 52.756  12.482  99.115  1.00 159.87 ? 1106 TRP B CZ3 1 
ATOM   20771 C  CH2 . TRP C 1 1106 ? 51.578  11.957  98.595  1.00 162.00 ? 1106 TRP B CH2 1 
ATOM   20772 N  N   . LEU C 1 1107 ? 52.713  15.454  103.045 1.00 165.35 ? 1107 LEU B N   1 
ATOM   20773 C  CA  . LEU C 1 1107 ? 52.588  14.221  103.835 1.00 165.48 ? 1107 LEU B CA  1 
ATOM   20774 C  C   . LEU C 1 1107 ? 51.839  14.535  105.108 1.00 173.09 ? 1107 LEU B C   1 
ATOM   20775 O  O   . LEU C 1 1107 ? 50.770  13.974  105.374 1.00 176.08 ? 1107 LEU B O   1 
ATOM   20776 C  CB  . LEU C 1 1107 ? 53.957  13.635  104.195 1.00 158.05 ? 1107 LEU B CB  1 
ATOM   20777 C  CG  . LEU C 1 1107 ? 54.987  13.442  103.085 1.00 152.45 ? 1107 LEU B CG  1 
ATOM   20778 C  CD1 . LEU C 1 1107 ? 55.973  14.590  103.127 1.00 150.88 ? 1107 LEU B CD1 1 
ATOM   20779 C  CD2 . LEU C 1 1107 ? 55.701  12.110  103.216 1.00 148.85 ? 1107 LEU B CD2 1 
ATOM   20780 N  N   . VAL C 1 1108 ? 52.415  15.462  105.869 1.00 159.47 ? 1108 VAL B N   1 
ATOM   20781 C  CA  . VAL C 1 1108 ? 51.870  15.914  107.139 1.00 162.61 ? 1108 VAL B CA  1 
ATOM   20782 C  C   . VAL C 1 1108 ? 50.383  16.216  107.083 1.00 169.41 ? 1108 VAL B C   1 
ATOM   20783 O  O   . VAL C 1 1108 ? 49.600  15.619  107.811 1.00 172.40 ? 1108 VAL B O   1 
ATOM   20784 C  CB  . VAL C 1 1108 ? 52.567  17.191  107.585 1.00 161.41 ? 1108 VAL B CB  1 
ATOM   20785 C  CG1 . VAL C 1 1108 ? 52.796  18.072  106.391 1.00 161.70 ? 1108 VAL B CG1 1 
ATOM   20786 C  CG2 . VAL C 1 1108 ? 51.722  17.915  108.609 1.00 164.73 ? 1108 VAL B CG2 1 
ATOM   20787 N  N   . GLU C 1 1109 ? 49.985  17.143  106.227 1.00 194.58 ? 1109 GLU B N   1 
ATOM   20788 C  CA  . GLU C 1 1109 ? 48.603  17.583  106.240 1.00 200.82 ? 1109 GLU B CA  1 
ATOM   20789 C  C   . GLU C 1 1109 ? 47.618  16.497  105.804 1.00 203.11 ? 1109 GLU B C   1 
ATOM   20790 O  O   . GLU C 1 1109 ? 46.461  16.514  106.210 1.00 207.02 ? 1109 GLU B O   1 
ATOM   20791 C  CB  . GLU C 1 1109 ? 48.450  18.855  105.414 1.00 203.17 ? 1109 GLU B CB  1 
ATOM   20792 C  CG  . GLU C 1 1109 ? 49.453  19.924  105.818 1.00 202.42 ? 1109 GLU B CG  1 
ATOM   20793 C  CD  . GLU C 1 1109 ? 49.071  21.299  105.315 1.00 204.29 ? 1109 GLU B CD  1 
ATOM   20794 O  OE1 . GLU C 1 1109 ? 49.949  22.189  105.252 1.00 202.58 ? 1109 GLU B OE1 1 
ATOM   20795 O  OE2 . GLU C 1 1109 ? 47.882  21.490  104.985 1.00 207.39 ? 1109 GLU B OE2 1 
ATOM   20796 N  N   . ASN C 1 1110 ? 48.085  15.533  105.016 1.00 199.33 ? 1110 ASN B N   1 
ATOM   20797 C  CA  . ASN C 1 1110 ? 47.185  14.566  104.402 1.00 200.49 ? 1110 ASN B CA  1 
ATOM   20798 C  C   . ASN C 1 1110 ? 47.382  13.124  104.863 1.00 197.68 ? 1110 ASN B C   1 
ATOM   20799 O  O   . ASN C 1 1110 ? 46.419  12.389  105.050 1.00 200.00 ? 1110 ASN B O   1 
ATOM   20800 C  CB  . ASN C 1 1110 ? 47.301  14.638  102.870 1.00 201.31 ? 1110 ASN B CB  1 
ATOM   20801 C  CG  . ASN C 1 1110 ? 46.924  16.015  102.297 1.00 204.50 ? 1110 ASN B CG  1 
ATOM   20802 O  OD1 . ASN C 1 1110 ? 47.766  16.713  101.716 1.00 203.81 ? 1110 ASN B OD1 1 
ATOM   20803 N  ND2 . ASN C 1 1110 ? 45.654  16.396  102.441 1.00 208.70 ? 1110 ASN B ND2 1 
ATOM   20804 N  N   . TYR C 1 1111 ? 48.627  12.717  105.041 1.00 215.87 ? 1111 TYR B N   1 
ATOM   20805 C  CA  . TYR C 1 1111 ? 48.906  11.305  105.255 1.00 214.01 ? 1111 TYR B CA  1 
ATOM   20806 C  C   . TYR C 1 1111 ? 49.470  10.930  106.622 1.00 213.74 ? 1111 TYR B C   1 
ATOM   20807 O  O   . TYR C 1 1111 ? 50.229  9.969   106.727 1.00 210.28 ? 1111 TYR B O   1 
ATOM   20808 C  CB  . TYR C 1 1111 ? 49.812  10.793  104.150 1.00 210.73 ? 1111 TYR B CB  1 
ATOM   20809 C  CG  . TYR C 1 1111 ? 49.125  10.861  102.829 1.00 212.56 ? 1111 TYR B CG  1 
ATOM   20810 C  CD1 . TYR C 1 1111 ? 48.473  9.755   102.310 1.00 214.27 ? 1111 TYR B CD1 1 
ATOM   20811 C  CD2 . TYR C 1 1111 ? 49.087  12.040  102.113 1.00 212.92 ? 1111 TYR B CD2 1 
ATOM   20812 C  CE1 . TYR C 1 1111 ? 47.819  9.814   101.093 1.00 216.69 ? 1111 TYR B CE1 1 
ATOM   20813 C  CE2 . TYR C 1 1111 ? 48.438  12.113  100.897 1.00 215.36 ? 1111 TYR B CE2 1 
ATOM   20814 C  CZ  . TYR C 1 1111 ? 47.805  10.997  100.386 1.00 217.48 ? 1111 TYR B CZ  1 
ATOM   20815 O  OH  . TYR C 1 1111 ? 47.156  11.067  99.170  1.00 220.35 ? 1111 TYR B OH  1 
ATOM   20816 N  N   . GLN C 1 1112 ? 49.088  11.673  107.662 1.00 190.98 ? 1112 GLN B N   1 
ATOM   20817 C  CA  . GLN C 1 1112 ? 49.531  11.390  109.036 1.00 191.52 ? 1112 GLN B CA  1 
ATOM   20818 C  C   . GLN C 1 1112 ? 48.370  11.092  109.982 1.00 201.18 ? 1112 GLN B C   1 
ATOM   20819 O  O   . GLN C 1 1112 ? 47.693  12.003  110.449 1.00 204.59 ? 1112 GLN B O   1 
ATOM   20820 C  CB  . GLN C 1 1112 ? 50.332  12.561  109.590 1.00 187.58 ? 1112 GLN B CB  1 
ATOM   20821 C  CG  . GLN C 1 1112 ? 50.629  12.463  111.061 1.00 186.15 ? 1112 GLN B CG  1 
ATOM   20822 C  CD  . GLN C 1 1112 ? 51.387  13.670  111.548 1.00 182.31 ? 1112 GLN B CD  1 
ATOM   20823 O  OE1 . GLN C 1 1112 ? 51.088  14.801  111.172 1.00 182.31 ? 1112 GLN B OE1 1 
ATOM   20824 N  NE2 . GLN C 1 1112 ? 52.382  13.440  112.385 1.00 179.70 ? 1112 GLN B NE2 1 
ATOM   20825 N  N   . LEU C 1 1113 ? 48.172  9.814   110.281 1.00 215.05 ? 1113 LEU B N   1 
ATOM   20826 C  CA  . LEU C 1 1113 ? 47.031  9.359   111.065 1.00 222.50 ? 1113 LEU B CA  1 
ATOM   20827 C  C   . LEU C 1 1113 ? 46.836  10.119  112.376 1.00 227.37 ? 1113 LEU B C   1 
ATOM   20828 O  O   . LEU C 1 1113 ? 47.706  10.884  112.804 1.00 224.45 ? 1113 LEU B O   1 
ATOM   20829 C  CB  . LEU C 1 1113 ? 47.156  7.857   111.327 1.00 222.23 ? 1113 LEU B CB  1 
ATOM   20830 C  CG  . LEU C 1 1113 ? 47.104  7.009   110.057 1.00 217.83 ? 1113 LEU B CG  1 
ATOM   20831 C  CD1 . LEU C 1 1113 ? 47.646  5.603   110.263 1.00 217.45 ? 1113 LEU B CD1 1 
ATOM   20832 C  CD2 . LEU C 1 1113 ? 45.678  6.962   109.532 1.00 221.15 ? 1113 LEU B CD2 1 
ATOM   20833 N  N   . ASP C 1 1114 ? 45.682  9.903   113.003 1.00 320.47 ? 1114 ASP B N   1 
ATOM   20834 C  CA  . ASP C 1 1114 ? 45.354  10.520  114.285 1.00 326.83 ? 1114 ASP B CA  1 
ATOM   20835 C  C   . ASP C 1 1114 ? 46.107  9.873   115.446 1.00 326.07 ? 1114 ASP B C   1 
ATOM   20836 O  O   . ASP C 1 1114 ? 45.545  9.648   116.517 1.00 331.68 ? 1114 ASP B O   1 
ATOM   20837 C  CB  . ASP C 1 1114 ? 43.844  10.461  114.530 1.00 337.22 ? 1114 ASP B CB  1 
ATOM   20838 C  CG  . ASP C 1 1114 ? 43.135  11.715  114.079 1.00 342.23 ? 1114 ASP B CG  1 
ATOM   20839 O  OD1 . ASP C 1 1114 ? 43.735  12.802  114.193 1.00 340.51 ? 1114 ASP B OD1 1 
ATOM   20840 O  OD2 . ASP C 1 1114 ? 41.981  11.616  113.615 1.00 347.29 ? 1114 ASP B OD2 1 
ATOM   20841 N  N   . ASN C 1 1115 ? 47.381  9.574   115.222 1.00 159.35 ? 1115 ASN B N   1 
ATOM   20842 C  CA  . ASN C 1 1115 ? 48.230  8.978   116.242 1.00 157.04 ? 1115 ASN B CA  1 
ATOM   20843 C  C   . ASN C 1 1115 ? 49.677  9.177   115.825 1.00 145.04 ? 1115 ASN B C   1 
ATOM   20844 O  O   . ASN C 1 1115 ? 50.595  8.516   116.313 1.00 142.41 ? 1115 ASN B O   1 
ATOM   20845 C  CB  . ASN C 1 1115 ? 47.848  7.507   116.554 1.00 162.21 ? 1115 ASN B CB  1 
ATOM   20846 C  CG  . ASN C 1 1115 ? 48.319  6.501   115.501 1.00 159.53 ? 1115 ASN B CG  1 
ATOM   20847 O  OD1 . ASN C 1 1115 ? 48.024  5.307   115.611 1.00 161.87 ? 1115 ASN B OD1 1 
ATOM   20848 N  ND2 . ASN C 1 1115 ? 49.050  6.964   114.502 1.00 154.63 ? 1115 ASN B ND2 1 
ATOM   20849 N  N   . GLY C 1 1116 ? 49.854  10.123  114.909 1.00 169.98 ? 1116 GLY B N   1 
ATOM   20850 C  CA  . GLY C 1 1116 ? 51.163  10.495  114.424 1.00 161.35 ? 1116 GLY B CA  1 
ATOM   20851 C  C   . GLY C 1 1116 ? 51.724  9.611   113.326 1.00 153.04 ? 1116 GLY B C   1 
ATOM   20852 O  O   . GLY C 1 1116 ? 52.696  9.986   112.675 1.00 148.52 ? 1116 GLY B O   1 
ATOM   20853 N  N   . SER C 1 1117 ? 51.137  8.435   113.114 1.00 203.62 ? 1117 SER B N   1 
ATOM   20854 C  CA  . SER C 1 1117 ? 51.651  7.515   112.091 1.00 199.71 ? 1117 SER B CA  1 
ATOM   20855 C  C   . SER C 1 1117 ? 51.266  7.950   110.673 1.00 198.59 ? 1117 SER B C   1 
ATOM   20856 O  O   . SER C 1 1117 ? 50.403  8.806   110.497 1.00 201.67 ? 1117 SER B O   1 
ATOM   20857 C  CB  . SER C 1 1117 ? 51.221  6.070   112.361 1.00 202.40 ? 1117 SER B CB  1 
ATOM   20858 O  OG  . SER C 1 1117 ? 49.940  5.819   111.826 1.00 205.04 ? 1117 SER B OG  1 
ATOM   20859 N  N   . PHE C 1 1118 ? 51.913  7.355   109.672 1.00 170.78 ? 1118 PHE B N   1 
ATOM   20860 C  CA  . PHE C 1 1118 ? 51.832  7.843   108.290 1.00 166.31 ? 1118 PHE B CA  1 
ATOM   20861 C  C   . PHE C 1 1118 ? 51.253  6.827   107.282 1.00 166.19 ? 1118 PHE B C   1 
ATOM   20862 O  O   . PHE C 1 1118 ? 51.901  5.829   106.976 1.00 165.94 ? 1118 PHE B O   1 
ATOM   20863 C  CB  . PHE C 1 1118 ? 53.220  8.327   107.835 1.00 161.87 ? 1118 PHE B CB  1 
ATOM   20864 C  CG  . PHE C 1 1118 ? 53.504  9.766   108.188 1.00 161.51 ? 1118 PHE B CG  1 
ATOM   20865 C  CD1 . PHE C 1 1118 ? 53.040  10.303  109.377 1.00 163.53 ? 1118 PHE B CD1 1 
ATOM   20866 C  CD2 . PHE C 1 1118 ? 54.221  10.587  107.333 1.00 161.30 ? 1118 PHE B CD2 1 
ATOM   20867 C  CE1 . PHE C 1 1118 ? 53.290  11.628  109.705 1.00 162.47 ? 1118 PHE B CE1 1 
ATOM   20868 C  CE2 . PHE C 1 1118 ? 54.474  11.919  107.660 1.00 160.71 ? 1118 PHE B CE2 1 
ATOM   20869 C  CZ  . PHE C 1 1118 ? 54.004  12.437  108.844 1.00 160.76 ? 1118 PHE B CZ  1 
ATOM   20870 N  N   . LYS C 1 1119 ? 50.043  7.086   106.767 1.00 184.18 ? 1119 LYS B N   1 
ATOM   20871 C  CA  . LYS C 1 1119 ? 49.390  6.165   105.823 1.00 185.28 ? 1119 LYS B CA  1 
ATOM   20872 C  C   . LYS C 1 1119 ? 49.957  6.327   104.419 1.00 180.75 ? 1119 LYS B C   1 
ATOM   20873 O  O   . LYS C 1 1119 ? 50.070  7.451   103.921 1.00 179.79 ? 1119 LYS B O   1 
ATOM   20874 C  CB  . LYS C 1 1119 ? 47.850  6.323   105.815 1.00 198.91 ? 1119 LYS B CB  1 
ATOM   20875 C  CG  . LYS C 1 1119 ? 47.305  7.705   105.394 1.00 206.54 ? 1119 LYS B CG  1 
ATOM   20876 C  CD  . LYS C 1 1119 ? 45.933  7.602   104.675 1.00 238.90 ? 1119 LYS B CD  1 
ATOM   20877 C  CE  . LYS C 1 1119 ? 44.730  7.520   105.619 1.00 242.98 ? 1119 LYS B CE  1 
ATOM   20878 N  NZ  . LYS C 1 1119 ? 44.088  8.845   105.863 1.00 242.86 ? 1119 LYS B NZ  1 
ATOM   20879 N  N   . GLU C 1 1120 ? 50.334  5.212   103.792 1.00 210.34 ? 1120 GLU B N   1 
ATOM   20880 C  CA  . GLU C 1 1120 ? 50.802  5.252   102.408 1.00 211.74 ? 1120 GLU B CA  1 
ATOM   20881 C  C   . GLU C 1 1120 ? 49.614  5.262   101.469 1.00 217.86 ? 1120 GLU B C   1 
ATOM   20882 O  O   . GLU C 1 1120 ? 48.707  4.437   101.602 1.00 221.46 ? 1120 GLU B O   1 
ATOM   20883 C  CB  . GLU C 1 1120 ? 51.726  4.080   102.075 1.00 211.48 ? 1120 GLU B CB  1 
ATOM   20884 C  CG  . GLU C 1 1120 ? 51.995  3.908   100.578 1.00 213.21 ? 1120 GLU B CG  1 
ATOM   20885 C  CD  . GLU C 1 1120 ? 52.759  5.071   99.958  1.00 210.72 ? 1120 GLU B CD  1 
ATOM   20886 O  OE1 . GLU C 1 1120 ? 53.940  4.879   99.611  1.00 207.90 ? 1120 GLU B OE1 1 
ATOM   20887 O  OE2 . GLU C 1 1120 ? 52.181  6.168   99.807  1.00 211.35 ? 1120 GLU B OE2 1 
ATOM   20888 N  N   . ASN C 1 1121 ? 49.634  6.198   100.522 1.00 206.10 ? 1121 ASN B N   1 
ATOM   20889 C  CA  . ASN C 1 1121 ? 48.513  6.431   99.615  1.00 209.96 ? 1121 ASN B CA  1 
ATOM   20890 C  C   . ASN C 1 1121 ? 48.330  5.352   98.559  1.00 214.71 ? 1121 ASN B C   1 
ATOM   20891 O  O   . ASN C 1 1121 ? 47.336  4.618   98.549  1.00 216.85 ? 1121 ASN B O   1 
ATOM   20892 C  CB  . ASN C 1 1121 ? 48.702  7.758   98.895  1.00 207.43 ? 1121 ASN B CB  1 
ATOM   20893 C  CG  . ASN C 1 1121 ? 47.518  8.107   98.038  1.00 206.76 ? 1121 ASN B CG  1 
ATOM   20894 O  OD1 . ASN C 1 1121 ? 46.378  7.982   98.475  1.00 208.39 ? 1121 ASN B OD1 1 
ATOM   20895 N  ND2 . ASN C 1 1121 ? 47.772  8.538   96.809  1.00 203.85 ? 1121 ASN B ND2 1 
ATOM   20896 N  N   . SER C 1 1122 ? 49.302  5.295   97.659  1.00 213.03 ? 1122 SER B N   1 
ATOM   20897 C  CA  . SER C 1 1122 ? 49.325  4.331   96.577  1.00 216.62 ? 1122 SER B CA  1 
ATOM   20898 C  C   . SER C 1 1122 ? 49.241  2.904   97.086  1.00 219.94 ? 1122 SER B C   1 
ATOM   20899 O  O   . SER C 1 1122 ? 49.268  2.651   98.283  1.00 220.19 ? 1122 SER B O   1 
ATOM   20900 C  CB  . SER C 1 1122 ? 50.625  4.502   95.792  1.00 212.14 ? 1122 SER B CB  1 
ATOM   20901 O  OG  . SER C 1 1122 ? 51.739  4.315   96.648  1.00 207.82 ? 1122 SER B OG  1 
ATOM   20902 N  N   . GLN C 1 1123 ? 49.148  1.964   96.164  1.00 247.87 ? 1123 GLN B N   1 
ATOM   20903 C  CA  . GLN C 1 1123 ? 49.153  0.575   96.549  1.00 251.16 ? 1123 GLN B CA  1 
ATOM   20904 C  C   . GLN C 1 1123 ? 50.583  0.097   96.742  1.00 242.15 ? 1123 GLN B C   1 
ATOM   20905 O  O   . GLN C 1 1123 ? 50.819  -1.062  97.063  1.00 243.26 ? 1123 GLN B O   1 
ATOM   20906 C  CB  . GLN C 1 1123 ? 48.432  -0.259  95.496  1.00 264.13 ? 1123 GLN B CB  1 
ATOM   20907 C  CG  . GLN C 1 1123 ? 47.048  0.277   95.148  1.00 276.21 ? 1123 GLN B CG  1 
ATOM   20908 C  CD  . GLN C 1 1123 ? 46.164  -0.759  94.475  1.00 289.67 ? 1123 GLN B CD  1 
ATOM   20909 O  OE1 . GLN C 1 1123 ? 46.206  -1.943  94.805  1.00 294.53 ? 1123 GLN B OE1 1 
ATOM   20910 N  NE2 . GLN C 1 1123 ? 45.352  -0.314  93.530  1.00 295.82 ? 1123 GLN B NE2 1 
ATOM   20911 N  N   . TYR C 1 1124 ? 51.542  0.994   96.574  1.00 175.84 ? 1124 TYR B N   1 
ATOM   20912 C  CA  . TYR C 1 1124 ? 52.936  0.577   96.561  1.00 166.47 ? 1124 TYR B CA  1 
ATOM   20913 C  C   . TYR C 1 1124 ? 53.396  -0.224  97.796  1.00 162.96 ? 1124 TYR B C   1 
ATOM   20914 O  O   . TYR C 1 1124 ? 53.309  0.246   98.932  1.00 159.87 ? 1124 TYR B O   1 
ATOM   20915 C  CB  . TYR C 1 1124 ? 53.838  1.782   96.321  1.00 159.09 ? 1124 TYR B CB  1 
ATOM   20916 C  CG  . TYR C 1 1124 ? 55.255  1.430   95.926  1.00 152.41 ? 1124 TYR B CG  1 
ATOM   20917 C  CD1 . TYR C 1 1124 ? 55.526  0.746   94.747  1.00 151.87 ? 1124 TYR B CD1 1 
ATOM   20918 C  CD2 . TYR C 1 1124 ? 56.327  1.804   96.725  1.00 147.61 ? 1124 TYR B CD2 1 
ATOM   20919 C  CE1 . TYR C 1 1124 ? 56.839  0.432   94.380  1.00 148.25 ? 1124 TYR B CE1 1 
ATOM   20920 C  CE2 . TYR C 1 1124 ? 57.640  1.499   96.372  1.00 143.66 ? 1124 TYR B CE2 1 
ATOM   20921 C  CZ  . TYR C 1 1124 ? 57.895  0.815   95.197  1.00 141.96 ? 1124 TYR B CZ  1 
ATOM   20922 O  OH  . TYR C 1 1124 ? 59.204  0.522   94.853  1.00 135.67 ? 1124 TYR B OH  1 
ATOM   20923 N  N   . GLN C 1 1125 ? 53.853  -1.453  97.542  1.00 193.08 ? 1125 GLN B N   1 
ATOM   20924 C  CA  . GLN C 1 1125 ? 54.518  -2.302  98.530  1.00 190.81 ? 1125 GLN B CA  1 
ATOM   20925 C  C   . GLN C 1 1125 ? 56.002  -2.224  98.211  1.00 182.23 ? 1125 GLN B C   1 
ATOM   20926 O  O   . GLN C 1 1125 ? 56.442  -2.778  97.217  1.00 178.86 ? 1125 GLN B O   1 
ATOM   20927 C  CB  . GLN C 1 1125 ? 54.086  -3.780  98.398  1.00 202.75 ? 1125 GLN B CB  1 
ATOM   20928 C  CG  . GLN C 1 1125 ? 52.571  -4.106  98.249  1.00 214.50 ? 1125 GLN B CG  1 
ATOM   20929 C  CD  . GLN C 1 1125 ? 51.774  -3.984  99.544  1.00 222.19 ? 1125 GLN B CD  1 
ATOM   20930 O  OE1 . GLN C 1 1125 ? 52.032  -3.095  100.352 1.00 221.00 ? 1125 GLN B OE1 1 
ATOM   20931 N  NE2 . GLN C 1 1125 ? 50.787  -4.867  99.732  1.00 228.69 ? 1125 GLN B NE2 1 
ATOM   20932 N  N   . PRO C 1 1126 ? 56.783  -1.528  99.036  1.00 148.74 ? 1126 PRO B N   1 
ATOM   20933 C  CA  . PRO C 1 1126 ? 58.211  -1.412  98.732  1.00 147.34 ? 1126 PRO B CA  1 
ATOM   20934 C  C   . PRO C 1 1126 ? 58.956  -2.632  99.240  1.00 150.56 ? 1126 PRO B C   1 
ATOM   20935 O  O   . PRO C 1 1126 ? 59.709  -3.251  98.495  1.00 153.28 ? 1126 PRO B O   1 
ATOM   20936 C  CB  . PRO C 1 1126 ? 58.645  -0.173  99.515  1.00 142.28 ? 1126 PRO B CB  1 
ATOM   20937 C  CG  . PRO C 1 1126 ? 57.377  0.398   100.115 1.00 143.86 ? 1126 PRO B CG  1 
ATOM   20938 C  CD  . PRO C 1 1126 ? 56.409  -0.735  100.206 1.00 147.66 ? 1126 PRO B CD  1 
ATOM   20939 N  N   . ILE C 1 1127 ? 58.723  -2.986  100.501 1.00 155.67 ? 1127 ILE B N   1 
ATOM   20940 C  CA  . ILE C 1 1127 ? 59.407  -4.119  101.139 1.00 158.73 ? 1127 ILE B CA  1 
ATOM   20941 C  C   . ILE C 1 1127 ? 58.464  -5.198  101.651 1.00 164.14 ? 1127 ILE B C   1 
ATOM   20942 O  O   . ILE C 1 1127 ? 57.374  -4.896  102.141 1.00 164.37 ? 1127 ILE B O   1 
ATOM   20943 C  CB  . ILE C 1 1127 ? 60.195  -3.671  102.362 1.00 162.68 ? 1127 ILE B CB  1 
ATOM   20944 C  CG1 . ILE C 1 1127 ? 59.552  -2.415  102.974 1.00 161.10 ? 1127 ILE B CG1 1 
ATOM   20945 C  CG2 . ILE C 1 1127 ? 61.654  -3.438  101.984 1.00 160.09 ? 1127 ILE B CG2 1 
ATOM   20946 C  CD1 . ILE C 1 1127 ? 58.089  -2.561  103.399 1.00 165.04 ? 1127 ILE B CD1 1 
ATOM   20947 N  N   . LYS C 1 1128 ? 58.893  -6.454  101.575 1.00 168.55 ? 1128 LYS B N   1 
ATOM   20948 C  CA  . LYS C 1 1128 ? 58.078  -7.540  102.109 1.00 175.63 ? 1128 LYS B CA  1 
ATOM   20949 C  C   . LYS C 1 1128 ? 58.358  -7.741  103.588 1.00 181.41 ? 1128 LYS B C   1 
ATOM   20950 O  O   . LYS C 1 1128 ? 59.423  -8.234  103.951 1.00 182.04 ? 1128 LYS B O   1 
ATOM   20951 C  CB  . LYS C 1 1128 ? 58.337  -8.849  101.362 1.00 176.68 ? 1128 LYS B CB  1 
ATOM   20952 C  CG  . LYS C 1 1128 ? 57.628  -10.069 101.977 1.00 180.89 ? 1128 LYS B CG  1 
ATOM   20953 C  CD  . LYS C 1 1128 ? 56.096  -10.074 101.777 1.00 183.06 ? 1128 LYS B CD  1 
ATOM   20954 C  CE  . LYS C 1 1128 ? 55.314  -9.781  103.068 1.00 183.22 ? 1128 LYS B CE  1 
ATOM   20955 N  NZ  . LYS C 1 1128 ? 53.976  -10.460 103.178 1.00 187.77 ? 1128 LYS B NZ  1 
ATOM   20956 N  N   . LEU C 1 1129 ? 57.406  -7.378  104.443 1.00 211.49 ? 1129 LEU B N   1 
ATOM   20957 C  CA  . LEU C 1 1129 ? 57.561  -7.621  105.881 1.00 217.11 ? 1129 LEU B CA  1 
ATOM   20958 C  C   . LEU C 1 1129 ? 57.038  -9.001  106.332 1.00 228.05 ? 1129 LEU B C   1 
ATOM   20959 O  O   . LEU C 1 1129 ? 55.999  -9.462  105.854 1.00 233.80 ? 1129 LEU B O   1 
ATOM   20960 C  CB  . LEU C 1 1129 ? 56.889  -6.509  106.693 1.00 213.01 ? 1129 LEU B CB  1 
ATOM   20961 C  CG  . LEU C 1 1129 ? 57.541  -5.127  106.647 1.00 205.82 ? 1129 LEU B CG  1 
ATOM   20962 C  CD1 . LEU C 1 1129 ? 57.094  -4.287  107.838 1.00 205.34 ? 1129 LEU B CD1 1 
ATOM   20963 C  CD2 . LEU C 1 1129 ? 59.057  -5.249  106.623 1.00 202.62 ? 1129 LEU B CD2 1 
ATOM   20964 N  N   . GLN C 1 1130 ? 57.749  -9.658  107.253 1.00 191.87 ? 1130 GLN B N   1 
ATOM   20965 C  CA  . GLN C 1 1130 ? 57.282  -10.932 107.805 1.00 197.45 ? 1130 GLN B CA  1 
ATOM   20966 C  C   . GLN C 1 1130 ? 56.164  -10.720 108.814 1.00 194.58 ? 1130 GLN B C   1 
ATOM   20967 O  O   . GLN C 1 1130 ? 55.952  -9.618  109.304 1.00 189.70 ? 1130 GLN B O   1 
ATOM   20968 C  CB  . GLN C 1 1130 ? 58.416  -11.682 108.486 1.00 205.37 ? 1130 GLN B CB  1 
ATOM   20969 C  CG  . GLN C 1 1130 ? 59.680  -11.781 107.682 1.00 207.01 ? 1130 GLN B CG  1 
ATOM   20970 C  CD  . GLN C 1 1130 ? 60.641  -12.779 108.282 1.00 213.33 ? 1130 GLN B CD  1 
ATOM   20971 O  OE1 . GLN C 1 1130 ? 60.263  -13.908 108.604 1.00 219.72 ? 1130 GLN B OE1 1 
ATOM   20972 N  NE2 . GLN C 1 1130 ? 61.895  -12.370 108.440 1.00 210.79 ? 1130 GLN B NE2 1 
ATOM   20973 N  N   . GLY C 1 1131 ? 55.449  -11.782 109.138 1.00 226.43 ? 1131 GLY B N   1 
ATOM   20974 C  CA  . GLY C 1 1131 ? 54.448  -11.680 110.173 1.00 231.00 ? 1131 GLY B CA  1 
ATOM   20975 C  C   . GLY C 1 1131 ? 53.031  -11.893 109.706 1.00 237.57 ? 1131 GLY B C   1 
ATOM   20976 O  O   . GLY C 1 1131 ? 52.720  -11.820 108.512 1.00 238.96 ? 1131 GLY B O   1 
ATOM   20977 N  N   . THR C 1 1132 ? 52.169  -12.164 110.677 1.00 268.05 ? 1132 THR B N   1 
ATOM   20978 C  CA  . THR C 1 1132 ? 50.769  -12.418 110.424 1.00 270.97 ? 1132 THR B CA  1 
ATOM   20979 C  C   . THR C 1 1132 ? 50.174  -11.246 109.669 1.00 265.71 ? 1132 THR B C   1 
ATOM   20980 O  O   . THR C 1 1132 ? 50.742  -10.158 109.650 1.00 259.17 ? 1132 THR B O   1 
ATOM   20981 C  CB  . THR C 1 1132 ? 50.006  -12.575 111.745 1.00 277.98 ? 1132 THR B CB  1 
ATOM   20982 O  OG1 . THR C 1 1132 ? 50.924  -12.924 112.788 1.00 278.86 ? 1132 THR B OG1 1 
ATOM   20983 C  CG2 . THR C 1 1132 ? 48.942  -13.651 111.623 1.00 285.69 ? 1132 THR B CG2 1 
ATOM   20984 N  N   . LEU C 1 1133 ? 49.025  -11.474 109.047 1.00 233.55 ? 1133 LEU B N   1 
ATOM   20985 C  CA  . LEU C 1 1133 ? 48.289  -10.403 108.395 1.00 234.03 ? 1133 LEU B CA  1 
ATOM   20986 C  C   . LEU C 1 1133 ? 48.001  -9.214  109.324 1.00 236.73 ? 1133 LEU B C   1 
ATOM   20987 O  O   . LEU C 1 1133 ? 48.064  -8.066  108.885 1.00 235.30 ? 1133 LEU B O   1 
ATOM   20988 C  CB  . LEU C 1 1133 ? 47.005  -10.945 107.771 1.00 237.07 ? 1133 LEU B CB  1 
ATOM   20989 C  CG  . LEU C 1 1133 ? 47.320  -11.797 106.541 1.00 234.05 ? 1133 LEU B CG  1 
ATOM   20990 C  CD1 . LEU C 1 1133 ? 48.007  -13.097 106.932 1.00 236.52 ? 1133 LEU B CD1 1 
ATOM   20991 C  CD2 . LEU C 1 1133 ? 46.076  -12.068 105.710 1.00 236.50 ? 1133 LEU B CD2 1 
ATOM   20992 N  N   . PRO C 1 1134 ? 47.680  -9.482  110.606 1.00 246.99 ? 1134 PRO B N   1 
ATOM   20993 C  CA  . PRO C 1 1134 ? 47.564  -8.396  111.585 1.00 247.26 ? 1134 PRO B CA  1 
ATOM   20994 C  C   . PRO C 1 1134 ? 48.931  -7.825  111.832 1.00 244.51 ? 1134 PRO B C   1 
ATOM   20995 O  O   . PRO C 1 1134 ? 49.148  -6.618  111.750 1.00 239.45 ? 1134 PRO B O   1 
ATOM   20996 C  CB  . PRO C 1 1134 ? 47.144  -9.114  112.868 1.00 252.92 ? 1134 PRO B CB  1 
ATOM   20997 C  CG  . PRO C 1 1134 ? 46.627  -10.417 112.451 1.00 258.05 ? 1134 PRO B CG  1 
ATOM   20998 C  CD  . PRO C 1 1134 ? 47.353  -10.786 111.201 1.00 253.88 ? 1134 PRO B CD  1 
ATOM   20999 N  N   . VAL C 1 1135 ? 49.852  -8.723  112.149 1.00 204.42 ? 1135 VAL B N   1 
ATOM   21000 C  CA  . VAL C 1 1135 ? 51.196  -8.328  112.497 1.00 198.50 ? 1135 VAL B CA  1 
ATOM   21001 C  C   . VAL C 1 1135 ? 51.775  -7.406  111.458 1.00 191.22 ? 1135 VAL B C   1 
ATOM   21002 O  O   . VAL C 1 1135 ? 52.242  -6.326  111.784 1.00 187.03 ? 1135 VAL B O   1 
ATOM   21003 C  CB  . VAL C 1 1135 ? 52.127  -9.523  112.568 1.00 199.28 ? 1135 VAL B CB  1 
ATOM   21004 C  CG1 . VAL C 1 1135 ? 53.546  -9.069  112.324 1.00 193.10 ? 1135 VAL B CG1 1 
ATOM   21005 C  CG2 . VAL C 1 1135 ? 52.005  -10.203 113.911 1.00 204.67 ? 1135 VAL B CG2 1 
ATOM   21006 N  N   . GLU C 1 1136 ? 51.754  -7.848  110.206 1.00 243.94 ? 1136 GLU B N   1 
ATOM   21007 C  CA  . GLU C 1 1136 ? 52.403  -7.129  109.111 1.00 237.31 ? 1136 GLU B CA  1 
ATOM   21008 C  C   . GLU C 1 1136 ? 51.886  -5.696  108.960 1.00 235.15 ? 1136 GLU B C   1 
ATOM   21009 O  O   . GLU C 1 1136 ? 52.633  -4.794  108.576 1.00 231.18 ? 1136 GLU B O   1 
ATOM   21010 C  CB  . GLU C 1 1136 ? 52.238  -7.906  107.791 1.00 236.12 ? 1136 GLU B CB  1 
ATOM   21011 C  CG  . GLU C 1 1136 ? 52.809  -7.212  106.550 1.00 230.50 ? 1136 GLU B CG  1 
ATOM   21012 C  CD  . GLU C 1 1136 ? 52.645  -8.035  105.272 1.00 230.47 ? 1136 GLU B CD  1 
ATOM   21013 O  OE1 . GLU C 1 1136 ? 51.878  -9.020  105.280 1.00 232.99 ? 1136 GLU B OE1 1 
ATOM   21014 O  OE2 . GLU C 1 1136 ? 53.288  -7.689  104.257 1.00 227.52 ? 1136 GLU B OE2 1 
ATOM   21015 N  N   . ALA C 1 1137 ? 50.606  -5.498  109.265 1.00 210.05 ? 1137 ALA B N   1 
ATOM   21016 C  CA  . ALA C 1 1137 ? 49.972  -4.195  109.123 1.00 208.96 ? 1137 ALA B CA  1 
ATOM   21017 C  C   . ALA C 1 1137 ? 50.601  -3.243  110.117 1.00 206.74 ? 1137 ALA B C   1 
ATOM   21018 O  O   . ALA C 1 1137 ? 51.046  -2.151  109.773 1.00 202.20 ? 1137 ALA B O   1 
ATOM   21019 C  CB  . ALA C 1 1137 ? 48.478  -4.315  109.379 1.00 214.87 ? 1137 ALA B CB  1 
ATOM   21020 N  N   . ARG C 1 1138 ? 50.632  -3.693  111.360 1.00 231.20 ? 1138 ARG B N   1 
ATOM   21021 C  CA  . ARG C 1 1138 ? 51.256  -2.971  112.447 1.00 230.12 ? 1138 ARG B CA  1 
ATOM   21022 C  C   . ARG C 1 1138 ? 52.745  -2.766  112.157 1.00 221.18 ? 1138 ARG B C   1 
ATOM   21023 O  O   . ARG C 1 1138 ? 53.306  -1.715  112.456 1.00 216.75 ? 1138 ARG B O   1 
ATOM   21024 C  CB  . ARG C 1 1138 ? 51.049  -3.758  113.739 1.00 240.47 ? 1138 ARG B CB  1 
ATOM   21025 C  CG  . ARG C 1 1138 ? 51.403  -3.014  115.003 1.00 244.29 ? 1138 ARG B CG  1 
ATOM   21026 C  CD  . ARG C 1 1138 ? 50.942  -3.781  116.249 1.00 254.52 ? 1138 ARG B CD  1 
ATOM   21027 N  NE  . ARG C 1 1138 ? 51.525  -3.243  117.481 1.00 259.28 ? 1138 ARG B NE  1 
ATOM   21028 C  CZ  . ARG C 1 1138 ? 51.154  -3.606  118.705 1.00 267.95 ? 1138 ARG B CZ  1 
ATOM   21029 N  NH1 . ARG C 1 1138 ? 50.192  -4.506  118.861 1.00 274.20 ? 1138 ARG B NH1 1 
ATOM   21030 N  NH2 . ARG C 1 1138 ? 51.738  -3.065  119.768 1.00 269.11 ? 1138 ARG B NH2 1 
ATOM   21031 N  N   . GLU C 1 1139 ? 53.370  -3.779  111.563 1.00 238.22 ? 1139 GLU B N   1 
ATOM   21032 C  CA  . GLU C 1 1139 ? 54.746  -3.689  111.076 1.00 229.20 ? 1139 GLU B CA  1 
ATOM   21033 C  C   . GLU C 1 1139 ? 54.864  -2.683  109.942 1.00 224.61 ? 1139 GLU B C   1 
ATOM   21034 O  O   . GLU C 1 1139 ? 55.607  -1.709  110.039 1.00 220.42 ? 1139 GLU B O   1 
ATOM   21035 C  CB  . GLU C 1 1139 ? 55.208  -5.048  110.555 1.00 227.74 ? 1139 GLU B CB  1 
ATOM   21036 C  CG  . GLU C 1 1139 ? 55.732  -5.987  111.613 1.00 228.22 ? 1139 GLU B CG  1 
ATOM   21037 C  CD  . GLU C 1 1139 ? 57.125  -5.617  112.069 1.00 224.27 ? 1139 GLU B CD  1 
ATOM   21038 O  OE1 . GLU C 1 1139 ? 58.074  -6.358  111.732 1.00 224.72 ? 1139 GLU B OE1 1 
ATOM   21039 O  OE2 . GLU C 1 1139 ? 57.266  -4.585  112.761 1.00 222.33 ? 1139 GLU B OE2 1 
ATOM   21040 N  N   . ASN C 1 1140 ? 54.130  -2.935  108.862 1.00 246.47 ? 1140 ASN B N   1 
ATOM   21041 C  CA  . ASN C 1 1140 ? 54.151  -2.070  107.690 1.00 242.56 ? 1140 ASN B CA  1 
ATOM   21042 C  C   . ASN C 1 1140 ? 53.913  -0.608  108.073 1.00 235.45 ? 1140 ASN B C   1 
ATOM   21043 O  O   . ASN C 1 1140 ? 54.581  0.282   107.554 1.00 230.11 ? 1140 ASN B O   1 
ATOM   21044 C  CB  . ASN C 1 1140 ? 53.131  -2.545  106.647 1.00 250.80 ? 1140 ASN B CB  1 
ATOM   21045 C  CG  . ASN C 1 1140 ? 53.436  -2.035  105.243 1.00 253.96 ? 1140 ASN B CG  1 
ATOM   21046 O  OD1 . ASN C 1 1140 ? 52.566  -2.027  104.377 1.00 259.05 ? 1140 ASN B OD1 1 
ATOM   21047 N  ND2 . ASN C 1 1140 ? 54.673  -1.613  105.015 1.00 251.73 ? 1140 ASN B ND2 1 
ATOM   21048 N  N   . SER C 1 1141 ? 52.982  -0.368  108.998 1.00 234.88 ? 1141 SER B N   1 
ATOM   21049 C  CA  . SER C 1 1141 ? 52.703  0.987   109.489 1.00 231.45 ? 1141 SER B CA  1 
ATOM   21050 C  C   . SER C 1 1141 ? 53.940  1.643   110.076 1.00 223.62 ? 1141 SER B C   1 
ATOM   21051 O  O   . SER C 1 1141 ? 54.273  2.784   109.755 1.00 218.53 ? 1141 SER B O   1 
ATOM   21052 C  CB  . SER C 1 1141 ? 51.611  0.968   110.561 1.00 237.61 ? 1141 SER B CB  1 
ATOM   21053 O  OG  . SER C 1 1141 ? 51.707  2.117   111.393 1.00 238.12 ? 1141 SER B OG  1 
ATOM   21054 N  N   . LEU C 1 1142 ? 54.610  0.915   110.956 1.00 188.85 ? 1142 LEU B N   1 
ATOM   21055 C  CA  . LEU C 1 1142 ? 55.814  1.425   111.580 1.00 181.86 ? 1142 LEU B CA  1 
ATOM   21056 C  C   . LEU C 1 1142 ? 56.795  1.834   110.483 1.00 176.42 ? 1142 LEU B C   1 
ATOM   21057 O  O   . LEU C 1 1142 ? 57.225  2.988   110.423 1.00 172.99 ? 1142 LEU B O   1 
ATOM   21058 C  CB  . LEU C 1 1142 ? 56.441  0.360   112.487 1.00 180.78 ? 1142 LEU B CB  1 
ATOM   21059 C  CG  . LEU C 1 1142 ? 57.223  0.860   113.703 1.00 176.42 ? 1142 LEU B CG  1 
ATOM   21060 C  CD1 . LEU C 1 1142 ? 57.706  -0.325  114.519 1.00 178.53 ? 1142 LEU B CD1 1 
ATOM   21061 C  CD2 . LEU C 1 1142 ? 58.379  1.745   113.283 1.00 168.90 ? 1142 LEU B CD2 1 
ATOM   21062 N  N   . TYR C 1 1143 ? 57.116  0.891   109.596 1.00 176.91 ? 1143 TYR B N   1 
ATOM   21063 C  CA  . TYR C 1 1143 ? 58.184  1.097   108.623 1.00 171.23 ? 1143 TYR B CA  1 
ATOM   21064 C  C   . TYR C 1 1143 ? 58.020  2.435   107.950 1.00 166.29 ? 1143 TYR B C   1 
ATOM   21065 O  O   . TYR C 1 1143 ? 58.934  3.254   107.971 1.00 161.66 ? 1143 TYR B O   1 
ATOM   21066 C  CB  . TYR C 1 1143 ? 58.235  -0.025  107.584 1.00 170.21 ? 1143 TYR B CB  1 
ATOM   21067 C  CG  . TYR C 1 1143 ? 59.358  0.120   106.569 1.00 165.84 ? 1143 TYR B CG  1 
ATOM   21068 C  CD1 . TYR C 1 1143 ? 60.611  -0.458  106.786 1.00 163.77 ? 1143 TYR B CD1 1 
ATOM   21069 C  CD2 . TYR C 1 1143 ? 59.163  0.831   105.383 1.00 164.06 ? 1143 TYR B CD2 1 
ATOM   21070 C  CE1 . TYR C 1 1143 ? 61.642  -0.324  105.847 1.00 161.74 ? 1143 TYR B CE1 1 
ATOM   21071 C  CE2 . TYR C 1 1143 ? 60.187  0.972   104.437 1.00 160.67 ? 1143 TYR B CE2 1 
ATOM   21072 C  CZ  . TYR C 1 1143 ? 61.427  0.388   104.671 1.00 159.68 ? 1143 TYR B CZ  1 
ATOM   21073 O  OH  . TYR C 1 1143 ? 62.446  0.523   103.735 1.00 156.94 ? 1143 TYR B OH  1 
ATOM   21074 N  N   . LEU C 1 1144 ? 56.843  2.659   107.373 1.00 246.79 ? 1144 LEU B N   1 
ATOM   21075 C  CA  . LEU C 1 1144 ? 56.553  3.932   106.726 1.00 245.27 ? 1144 LEU B CA  1 
ATOM   21076 C  C   . LEU C 1 1144 ? 56.852  5.040   107.732 1.00 245.69 ? 1144 LEU B C   1 
ATOM   21077 O  O   . LEU C 1 1144 ? 57.742  5.859   107.509 1.00 243.04 ? 1144 LEU B O   1 
ATOM   21078 C  CB  . LEU C 1 1144 ? 55.093  4.007   106.231 1.00 245.46 ? 1144 LEU B CB  1 
ATOM   21079 C  CG  . LEU C 1 1144 ? 54.749  4.811   104.959 1.00 240.57 ? 1144 LEU B CG  1 
ATOM   21080 C  CD1 . LEU C 1 1144 ? 55.278  4.146   103.694 1.00 239.25 ? 1144 LEU B CD1 1 
ATOM   21081 C  CD2 . LEU C 1 1144 ? 53.260  5.037   104.811 1.00 242.44 ? 1144 LEU B CD2 1 
ATOM   21082 N  N   . THR C 1 1145 ? 56.150  5.031   108.863 1.00 176.05 ? 1145 THR B N   1 
ATOM   21083 C  CA  . THR C 1 1145 ? 56.271  6.121   109.828 1.00 175.24 ? 1145 THR B CA  1 
ATOM   21084 C  C   . THR C 1 1145 ? 57.715  6.294   110.315 1.00 173.13 ? 1145 THR B C   1 
ATOM   21085 O  O   . THR C 1 1145 ? 58.063  7.330   110.886 1.00 171.96 ? 1145 THR B O   1 
ATOM   21086 C  CB  . THR C 1 1145 ? 55.312  5.961   111.029 1.00 183.84 ? 1145 THR B CB  1 
ATOM   21087 O  OG1 . THR C 1 1145 ? 54.073  5.377   110.598 1.00 185.42 ? 1145 THR B OG1 1 
ATOM   21088 C  CG2 . THR C 1 1145 ? 55.043  7.320   111.668 1.00 184.71 ? 1145 THR B CG2 1 
ATOM   21089 N  N   . ALA C 1 1146 ? 58.547  5.279   110.087 1.00 138.31 ? 1146 ALA B N   1 
ATOM   21090 C  CA  . ALA C 1 1146 ? 59.967  5.369   110.399 1.00 140.39 ? 1146 ALA B CA  1 
ATOM   21091 C  C   . ALA C 1 1146 ? 60.683  6.149   109.309 1.00 137.96 ? 1146 ALA B C   1 
ATOM   21092 O  O   . ALA C 1 1146 ? 61.442  7.086   109.585 1.00 134.77 ? 1146 ALA B O   1 
ATOM   21093 C  CB  . ALA C 1 1146 ? 60.552  3.988   110.506 1.00 142.09 ? 1146 ALA B CB  1 
ATOM   21094 N  N   . PHE C 1 1147 ? 60.401  5.740   108.069 1.00 194.23 ? 1147 PHE B N   1 
ATOM   21095 C  CA  . PHE C 1 1147 ? 60.974  6.286   106.829 1.00 190.39 ? 1147 PHE B CA  1 
ATOM   21096 C  C   . PHE C 1 1147 ? 60.609  7.743   106.558 1.00 187.66 ? 1147 PHE B C   1 
ATOM   21097 O  O   . PHE C 1 1147 ? 61.464  8.566   106.215 1.00 186.45 ? 1147 PHE B O   1 
ATOM   21098 C  CB  . PHE C 1 1147 ? 60.490  5.457   105.639 1.00 190.25 ? 1147 PHE B CB  1 
ATOM   21099 C  CG  . PHE C 1 1147 ? 61.465  5.401   104.517 1.00 187.66 ? 1147 PHE B CG  1 
ATOM   21100 C  CD1 . PHE C 1 1147 ? 61.849  4.185   103.978 1.00 185.63 ? 1147 PHE B CD1 1 
ATOM   21101 C  CD2 . PHE C 1 1147 ? 62.025  6.563   104.022 1.00 186.86 ? 1147 PHE B CD2 1 
ATOM   21102 C  CE1 . PHE C 1 1147 ? 62.764  4.130   102.959 1.00 184.10 ? 1147 PHE B CE1 1 
ATOM   21103 C  CE2 . PHE C 1 1147 ? 62.941  6.518   103.005 1.00 185.79 ? 1147 PHE B CE2 1 
ATOM   21104 C  CZ  . PHE C 1 1147 ? 63.312  5.298   102.472 1.00 184.35 ? 1147 PHE B CZ  1 
ATOM   21105 N  N   . THR C 1 1148 ? 59.319  8.038   106.667 1.00 133.13 ? 1148 THR B N   1 
ATOM   21106 C  CA  . THR C 1 1148 ? 58.834  9.399   106.504 1.00 135.31 ? 1148 THR B CA  1 
ATOM   21107 C  C   . THR C 1 1148 ? 59.500  10.382  107.461 1.00 127.77 ? 1148 THR B C   1 
ATOM   21108 O  O   . THR C 1 1148 ? 59.774  11.525  107.093 1.00 126.97 ? 1148 THR B O   1 
ATOM   21109 C  CB  . THR C 1 1148 ? 57.289  9.507   106.654 1.00 130.13 ? 1148 THR B CB  1 
ATOM   21110 O  OG1 . THR C 1 1148 ? 56.968  10.683  107.404 1.00 132.54 ? 1148 THR B OG1 1 
ATOM   21111 C  CG2 . THR C 1 1148 ? 56.717  8.309   107.359 1.00 129.64 ? 1148 THR B CG2 1 
ATOM   21112 N  N   . VAL C 1 1149 ? 59.761  9.935   108.684 1.00 149.55 ? 1149 VAL B N   1 
ATOM   21113 C  CA  . VAL C 1 1149 ? 60.417  10.776  109.665 1.00 149.16 ? 1149 VAL B CA  1 
ATOM   21114 C  C   . VAL C 1 1149 ? 61.772  11.100  109.126 1.00 144.58 ? 1149 VAL B C   1 
ATOM   21115 O  O   . VAL C 1 1149 ? 62.156  12.265  109.055 1.00 143.28 ? 1149 VAL B O   1 
ATOM   21116 C  CB  . VAL C 1 1149 ? 60.650  10.027  110.976 1.00 135.44 ? 1149 VAL B CB  1 
ATOM   21117 C  CG1 . VAL C 1 1149 ? 61.595  10.807  111.867 1.00 135.71 ? 1149 VAL B CG1 1 
ATOM   21118 C  CG2 . VAL C 1 1149 ? 59.328  9.760   111.685 1.00 136.29 ? 1149 VAL B CG2 1 
ATOM   21119 N  N   . ILE C 1 1150 ? 62.492  10.050  108.740 1.00 122.70 ? 1150 ILE B N   1 
ATOM   21120 C  CA  . ILE C 1 1150 ? 63.878  10.187  108.324 1.00 116.33 ? 1150 ILE B CA  1 
ATOM   21121 C  C   . ILE C 1 1150 ? 63.920  11.276  107.283 1.00 113.56 ? 1150 ILE B C   1 
ATOM   21122 O  O   . ILE C 1 1150 ? 64.637  12.286  107.399 1.00 113.35 ? 1150 ILE B O   1 
ATOM   21123 C  CB  . ILE C 1 1150 ? 64.368  8.911   107.672 1.00 112.12 ? 1150 ILE B CB  1 
ATOM   21124 C  CG1 . ILE C 1 1150 ? 63.841  7.713   108.445 1.00 116.13 ? 1150 ILE B CG1 1 
ATOM   21125 C  CG2 . ILE C 1 1150 ? 65.886  8.901   107.587 1.00 105.87 ? 1150 ILE B CG2 1 
ATOM   21126 C  CD1 . ILE C 1 1150 ? 64.490  6.418   108.045 1.00 117.47 ? 1150 ILE B CD1 1 
ATOM   21127 N  N   . GLY C 1 1151 ? 63.113  11.045  106.259 1.00 238.82 ? 1151 GLY B N   1 
ATOM   21128 C  CA  . GLY C 1 1151 ? 62.871  12.037  105.247 1.00 240.65 ? 1151 GLY B CA  1 
ATOM   21129 C  C   . GLY C 1 1151 ? 62.667  13.390  105.899 1.00 242.34 ? 1151 GLY B C   1 
ATOM   21130 O  O   . GLY C 1 1151 ? 63.564  14.244  105.851 1.00 241.83 ? 1151 GLY B O   1 
ATOM   21131 N  N   . ILE C 1 1152 ? 61.513  13.579  106.543 1.00 105.30 ? 1152 ILE B N   1 
ATOM   21132 C  CA  . ILE C 1 1152 ? 61.122  14.911  106.969 1.00 108.55 ? 1152 ILE B CA  1 
ATOM   21133 C  C   . ILE C 1 1152 ? 62.330  15.470  107.621 1.00 111.29 ? 1152 ILE B C   1 
ATOM   21134 O  O   . ILE C 1 1152 ? 62.786  16.557  107.302 1.00 112.33 ? 1152 ILE B O   1 
ATOM   21135 C  CB  . ILE C 1 1152 ? 59.995  14.914  108.015 1.00 106.72 ? 1152 ILE B CB  1 
ATOM   21136 C  CG1 . ILE C 1 1152 ? 58.850  13.975  107.589 1.00 103.17 ? 1152 ILE B CG1 1 
ATOM   21137 C  CG2 . ILE C 1 1152 ? 59.527  16.376  108.247 1.00 92.22  ? 1152 ILE B CG2 1 
ATOM   21138 C  CD1 . ILE C 1 1152 ? 58.277  13.129  108.697 1.00 100.68 ? 1152 ILE B CD1 1 
ATOM   21139 N  N   . ARG C 1 1153 ? 62.866  14.678  108.530 1.00 183.21 ? 1153 ARG B N   1 
ATOM   21140 C  CA  . ARG C 1 1153 ? 64.067  15.079  109.191 1.00 185.28 ? 1153 ARG B CA  1 
ATOM   21141 C  C   . ARG C 1 1153 ? 65.030  15.571  108.121 1.00 180.79 ? 1153 ARG B C   1 
ATOM   21142 O  O   . ARG C 1 1153 ? 65.175  16.777  107.953 1.00 182.35 ? 1153 ARG B O   1 
ATOM   21143 C  CB  . ARG C 1 1153 ? 64.636  13.947  110.046 1.00 191.69 ? 1153 ARG B CB  1 
ATOM   21144 C  CG  . ARG C 1 1153 ? 63.775  13.605  111.283 1.00 200.54 ? 1153 ARG B CG  1 
ATOM   21145 C  CD  . ARG C 1 1153 ? 63.928  14.646  112.405 1.00 206.53 ? 1153 ARG B CD  1 
ATOM   21146 N  NE  . ARG C 1 1153 ? 63.152  14.321  113.603 1.00 210.79 ? 1153 ARG B NE  1 
ATOM   21147 C  CZ  . ARG C 1 1153 ? 63.037  15.116  114.666 1.00 213.43 ? 1153 ARG B CZ  1 
ATOM   21148 N  NH1 . ARG C 1 1153 ? 63.647  16.294  114.697 1.00 211.55 ? 1153 ARG B NH1 1 
ATOM   21149 N  NH2 . ARG C 1 1153 ? 62.304  14.734  115.700 1.00 218.83 ? 1153 ARG B NH2 1 
ATOM   21150 N  N   . LYS C 1 1154 ? 65.643  14.672  107.365 1.00 121.08 ? 1154 LYS B N   1 
ATOM   21151 C  CA  . LYS C 1 1154 ? 66.785  15.074  106.549 1.00 119.15 ? 1154 LYS B CA  1 
ATOM   21152 C  C   . LYS C 1 1154 ? 66.665  16.496  105.943 1.00 122.69 ? 1154 LYS B C   1 
ATOM   21153 O  O   . LYS C 1 1154 ? 67.594  17.312  105.991 1.00 121.08 ? 1154 LYS B O   1 
ATOM   21154 C  CB  . LYS C 1 1154 ? 67.004  14.035  105.459 1.00 116.74 ? 1154 LYS B CB  1 
ATOM   21155 C  CG  . LYS C 1 1154 ? 67.630  12.753  105.928 1.00 115.20 ? 1154 LYS B CG  1 
ATOM   21156 C  CD  . LYS C 1 1154 ? 69.127  12.943  105.990 1.00 114.99 ? 1154 LYS B CD  1 
ATOM   21157 C  CE  . LYS C 1 1154 ? 69.883  11.635  105.859 1.00 115.56 ? 1154 LYS B CE  1 
ATOM   21158 N  NZ  . LYS C 1 1154 ? 71.355  11.894  105.771 1.00 115.37 ? 1154 LYS B NZ  1 
ATOM   21159 N  N   . ALA C 1 1155 ? 65.495  16.779  105.391 1.00 182.76 ? 1155 ALA B N   1 
ATOM   21160 C  CA  . ALA C 1 1155 ? 65.262  18.005  104.649 1.00 187.04 ? 1155 ALA B CA  1 
ATOM   21161 C  C   . ALA C 1 1155 ? 64.818  19.129  105.551 1.00 194.66 ? 1155 ALA B C   1 
ATOM   21162 O  O   . ALA C 1 1155 ? 64.854  20.291  105.166 1.00 197.54 ? 1155 ALA B O   1 
ATOM   21163 C  CB  . ALA C 1 1155 ? 64.204  17.770  103.595 1.00 185.56 ? 1155 ALA B CB  1 
ATOM   21164 N  N   . PHE C 1 1156 ? 64.382  18.776  106.752 1.00 164.95 ? 1156 PHE B N   1 
ATOM   21165 C  CA  . PHE C 1 1156 ? 63.626  19.705  107.597 1.00 170.01 ? 1156 PHE B CA  1 
ATOM   21166 C  C   . PHE C 1 1156 ? 64.150  21.144  107.547 1.00 169.25 ? 1156 PHE B C   1 
ATOM   21167 O  O   . PHE C 1 1156 ? 63.377  22.109  107.533 1.00 171.34 ? 1156 PHE B O   1 
ATOM   21168 C  CB  . PHE C 1 1156 ? 63.550  19.212  109.060 1.00 172.44 ? 1156 PHE B CB  1 
ATOM   21169 C  CG  . PHE C 1 1156 ? 62.909  20.198  109.985 1.00 176.41 ? 1156 PHE B CG  1 
ATOM   21170 C  CD1 . PHE C 1 1156 ? 61.540  20.199  110.180 1.00 179.12 ? 1156 PHE B CD1 1 
ATOM   21171 C  CD2 . PHE C 1 1156 ? 63.671  21.152  110.625 1.00 177.90 ? 1156 PHE B CD2 1 
ATOM   21172 C  CE1 . PHE C 1 1156 ? 60.954  21.127  111.009 1.00 181.94 ? 1156 PHE B CE1 1 
ATOM   21173 C  CE2 . PHE C 1 1156 ? 63.084  22.074  111.453 1.00 181.00 ? 1156 PHE B CE2 1 
ATOM   21174 C  CZ  . PHE C 1 1156 ? 61.728  22.062  111.645 1.00 183.56 ? 1156 PHE B CZ  1 
ATOM   21175 N  N   . ASP C 1 1157 ? 65.461  21.293  107.489 1.00 178.51 ? 1157 ASP B N   1 
ATOM   21176 C  CA  . ASP C 1 1157 ? 66.042  22.593  107.749 1.00 180.06 ? 1157 ASP B CA  1 
ATOM   21177 C  C   . ASP C 1 1157 ? 65.768  23.679  106.724 1.00 180.73 ? 1157 ASP B C   1 
ATOM   21178 O  O   . ASP C 1 1157 ? 65.949  24.852  107.025 1.00 181.18 ? 1157 ASP B O   1 
ATOM   21179 C  CB  . ASP C 1 1157 ? 67.521  22.427  108.024 1.00 182.95 ? 1157 ASP B CB  1 
ATOM   21180 C  CG  . ASP C 1 1157 ? 67.761  21.466  109.152 1.00 190.44 ? 1157 ASP B CG  1 
ATOM   21181 O  OD1 . ASP C 1 1157 ? 66.760  21.012  109.755 1.00 194.50 ? 1157 ASP B OD1 1 
ATOM   21182 O  OD2 . ASP C 1 1157 ? 68.933  21.163  109.438 1.00 190.95 ? 1157 ASP B OD2 1 
ATOM   21183 N  N   . ILE C 1 1158 ? 65.326  23.303  105.526 1.00 152.50 ? 1158 ILE B N   1 
ATOM   21184 C  CA  . ILE C 1 1158 ? 65.016  24.295  104.488 1.00 149.23 ? 1158 ILE B CA  1 
ATOM   21185 C  C   . ILE C 1 1158 ? 63.588  24.769  104.601 1.00 155.25 ? 1158 ILE B C   1 
ATOM   21186 O  O   . ILE C 1 1158 ? 63.229  25.826  104.084 1.00 159.64 ? 1158 ILE B O   1 
ATOM   21187 C  CB  . ILE C 1 1158 ? 65.253  23.790  103.038 1.00 141.62 ? 1158 ILE B CB  1 
ATOM   21188 C  CG1 . ILE C 1 1158 ? 65.624  22.303  103.022 1.00 133.17 ? 1158 ILE B CG1 1 
ATOM   21189 C  CG2 . ILE C 1 1158 ? 66.311  24.663  102.343 1.00 139.88 ? 1158 ILE B CG2 1 
ATOM   21190 C  CD1 . ILE C 1 1158 ? 65.376  21.573  101.694 1.00 130.62 ? 1158 ILE B CD1 1 
ATOM   21191 N  N   . CYS C 1 1159 ? 62.766  23.984  105.276 1.00 215.26 ? 1159 CYS B N   1 
ATOM   21192 C  CA  . CYS C 1 1159 ? 61.443  24.471  105.591 1.00 219.60 ? 1159 CYS B CA  1 
ATOM   21193 C  C   . CYS C 1 1159 ? 61.144  24.278  107.061 1.00 223.86 ? 1159 CYS B C   1 
ATOM   21194 O  O   . CYS C 1 1159 ? 60.151  23.647  107.417 1.00 227.43 ? 1159 CYS B O   1 
ATOM   21195 C  CB  . CYS C 1 1159 ? 60.382  23.820  104.712 1.00 216.75 ? 1159 CYS B CB  1 
ATOM   21196 S  SG  . CYS C 1 1159 ? 58.961  24.898  104.418 1.00 281.68 ? 1159 CYS B SG  1 
ATOM   21197 N  N   . PRO C 1 1160 ? 62.015  24.827  107.922 1.00 169.30 ? 1160 PRO B N   1 
ATOM   21198 C  CA  . PRO C 1 1160 ? 61.736  24.891  109.353 1.00 168.66 ? 1160 PRO B CA  1 
ATOM   21199 C  C   . PRO C 1 1160 ? 60.367  25.518  109.540 1.00 171.82 ? 1160 PRO B C   1 
ATOM   21200 O  O   . PRO C 1 1160 ? 60.146  26.682  109.183 1.00 172.17 ? 1160 PRO B O   1 
ATOM   21201 C  CB  . PRO C 1 1160 ? 62.822  25.835  109.876 1.00 171.46 ? 1160 PRO B CB  1 
ATOM   21202 C  CG  . PRO C 1 1160 ? 63.352  26.541  108.660 1.00 171.80 ? 1160 PRO B CG  1 
ATOM   21203 C  CD  . PRO C 1 1160 ? 63.276  25.506  107.598 1.00 168.90 ? 1160 PRO B CD  1 
ATOM   21204 N  N   . LEU C 1 1161 ? 59.448  24.747  110.101 1.00 157.48 ? 1161 LEU B N   1 
ATOM   21205 C  CA  . LEU C 1 1161 ? 58.071  25.177  110.117 1.00 161.31 ? 1161 LEU B CA  1 
ATOM   21206 C  C   . LEU C 1 1161 ? 57.388  24.715  111.375 1.00 165.20 ? 1161 LEU B C   1 
ATOM   21207 O  O   . LEU C 1 1161 ? 57.464  23.543  111.764 1.00 164.81 ? 1161 LEU B O   1 
ATOM   21208 C  CB  . LEU C 1 1161 ? 57.350  24.642  108.873 1.00 157.38 ? 1161 LEU B CB  1 
ATOM   21209 C  CG  . LEU C 1 1161 ? 56.000  25.154  108.316 1.00 157.02 ? 1161 LEU B CG  1 
ATOM   21210 C  CD1 . LEU C 1 1161 ? 55.330  26.239  109.175 1.00 152.87 ? 1161 LEU B CD1 1 
ATOM   21211 C  CD2 . LEU C 1 1161 ? 56.134  25.585  106.833 1.00 153.54 ? 1161 LEU B CD2 1 
ATOM   21212 N  N   . VAL C 1 1162 ? 56.743  25.681  112.014 1.00 169.22 ? 1162 VAL B N   1 
ATOM   21213 C  CA  . VAL C 1 1162 ? 55.889  25.411  113.136 1.00 173.55 ? 1162 VAL B CA  1 
ATOM   21214 C  C   . VAL C 1 1162 ? 55.130  24.159  112.760 1.00 173.04 ? 1162 VAL B C   1 
ATOM   21215 O  O   . VAL C 1 1162 ? 55.495  23.050  113.149 1.00 169.43 ? 1162 VAL B O   1 
ATOM   21216 C  CB  . VAL C 1 1162 ? 54.901  26.600  113.393 1.00 182.70 ? 1162 VAL B CB  1 
ATOM   21217 C  CG1 . VAL C 1 1162 ? 55.594  27.735  114.155 1.00 184.24 ? 1162 VAL B CG1 1 
ATOM   21218 C  CG2 . VAL C 1 1162 ? 54.302  27.119  112.083 1.00 186.31 ? 1162 VAL B CG2 1 
ATOM   21219 N  N   . LYS C 1 1163 ? 54.123  24.347  111.924 1.00 149.84 ? 1163 LYS B N   1 
ATOM   21220 C  CA  . LYS C 1 1163 ? 53.142  23.320  111.680 1.00 151.63 ? 1163 LYS B CA  1 
ATOM   21221 C  C   . LYS C 1 1163 ? 53.780  21.945  111.388 1.00 148.08 ? 1163 LYS B C   1 
ATOM   21222 O  O   . LYS C 1 1163 ? 53.140  20.910  111.594 1.00 148.33 ? 1163 LYS B O   1 
ATOM   21223 C  CB  . LYS C 1 1163 ? 52.183  23.785  110.572 1.00 153.04 ? 1163 LYS B CB  1 
ATOM   21224 C  CG  . LYS C 1 1163 ? 50.733  23.304  110.729 1.00 154.91 ? 1163 LYS B CG  1 
ATOM   21225 C  CD  . LYS C 1 1163 ? 49.876  23.559  109.469 1.00 155.85 ? 1163 LYS B CD  1 
ATOM   21226 C  CE  . LYS C 1 1163 ? 48.577  22.729  109.501 1.00 157.74 ? 1163 LYS B CE  1 
ATOM   21227 N  NZ  . LYS C 1 1163 ? 47.753  22.787  108.250 1.00 158.43 ? 1163 LYS B NZ  1 
ATOM   21228 N  N   . ILE C 1 1164 ? 55.034  21.917  110.933 1.00 211.09 ? 1164 ILE B N   1 
ATOM   21229 C  CA  . ILE C 1 1164 ? 55.663  20.628  110.626 1.00 209.95 ? 1164 ILE B CA  1 
ATOM   21230 C  C   . ILE C 1 1164 ? 56.566  20.152  111.737 1.00 209.57 ? 1164 ILE B C   1 
ATOM   21231 O  O   . ILE C 1 1164 ? 56.925  18.977  111.805 1.00 207.72 ? 1164 ILE B O   1 
ATOM   21232 C  CB  . ILE C 1 1164 ? 56.471  20.613  109.310 1.00 184.04 ? 1164 ILE B CB  1 
ATOM   21233 C  CG1 . ILE C 1 1164 ? 57.971  20.783  109.581 1.00 180.71 ? 1164 ILE B CG1 1 
ATOM   21234 C  CG2 . ILE C 1 1164 ? 55.906  21.610  108.287 1.00 185.42 ? 1164 ILE B CG2 1 
ATOM   21235 C  CD1 . ILE C 1 1164 ? 58.839  20.265  108.440 1.00 178.82 ? 1164 ILE B CD1 1 
ATOM   21236 N  N   . ASP C 1 1165 ? 56.957  21.067  112.606 1.00 195.32 ? 1165 ASP B N   1 
ATOM   21237 C  CA  . ASP C 1 1165 ? 57.664  20.639  113.795 1.00 197.38 ? 1165 ASP B CA  1 
ATOM   21238 C  C   . ASP C 1 1165 ? 56.711  19.801  114.628 1.00 199.77 ? 1165 ASP B C   1 
ATOM   21239 O  O   . ASP C 1 1165 ? 57.047  18.703  115.074 1.00 198.96 ? 1165 ASP B O   1 
ATOM   21240 C  CB  . ASP C 1 1165 ? 58.158  21.826  114.614 1.00 201.42 ? 1165 ASP B CB  1 
ATOM   21241 C  CG  . ASP C 1 1165 ? 58.873  21.391  115.878 1.00 203.73 ? 1165 ASP B CG  1 
ATOM   21242 O  OD1 . ASP C 1 1165 ? 59.544  20.333  115.858 1.00 201.00 ? 1165 ASP B OD1 1 
ATOM   21243 O  OD2 . ASP C 1 1165 ? 58.760  22.106  116.892 1.00 208.17 ? 1165 ASP B OD2 1 
ATOM   21244 N  N   . THR C 1 1166 ? 55.517  20.341  114.830 1.00 198.26 ? 1166 THR B N   1 
ATOM   21245 C  CA  . THR C 1 1166 ? 54.464  19.632  115.524 1.00 201.38 ? 1166 THR B CA  1 
ATOM   21246 C  C   . THR C 1 1166 ? 54.408  18.231  114.977 1.00 198.49 ? 1166 THR B C   1 
ATOM   21247 O  O   . THR C 1 1166 ? 54.808  17.280  115.644 1.00 200.40 ? 1166 THR B O   1 
ATOM   21248 C  CB  . THR C 1 1166 ? 53.101  20.291  115.271 1.00 204.27 ? 1166 THR B CB  1 
ATOM   21249 O  OG1 . THR C 1 1166 ? 53.075  21.575  115.898 1.00 207.81 ? 1166 THR B OG1 1 
ATOM   21250 C  CG2 . THR C 1 1166 ? 51.966  19.436  115.827 1.00 207.54 ? 1166 THR B CG2 1 
ATOM   21251 N  N   . ALA C 1 1167 ? 53.927  18.112  113.744 1.00 269.37 ? 1167 ALA B N   1 
ATOM   21252 C  CA  . ALA C 1 1167 ? 53.757  16.812  113.127 1.00 264.12 ? 1167 ALA B CA  1 
ATOM   21253 C  C   . ALA C 1 1167 ? 55.002  15.980  113.380 1.00 257.02 ? 1167 ALA B C   1 
ATOM   21254 O  O   . ALA C 1 1167 ? 54.911  14.770  113.580 1.00 256.33 ? 1167 ALA B O   1 
ATOM   21255 C  CB  . ALA C 1 1167 ? 53.506  16.954  111.647 1.00 261.97 ? 1167 ALA B CB  1 
ATOM   21256 N  N   . LEU C 1 1168 ? 56.163  16.628  113.404 1.00 137.84 ? 1168 LEU B N   1 
ATOM   21257 C  CA  . LEU C 1 1168 ? 57.401  15.890  113.574 1.00 134.50 ? 1168 LEU B CA  1 
ATOM   21258 C  C   . LEU C 1 1168 ? 57.436  15.085  114.877 1.00 142.75 ? 1168 LEU B C   1 
ATOM   21259 O  O   . LEU C 1 1168 ? 57.914  13.949  114.902 1.00 143.99 ? 1168 LEU B O   1 
ATOM   21260 C  CB  . LEU C 1 1168 ? 58.595  16.820  113.466 1.00 127.70 ? 1168 LEU B CB  1 
ATOM   21261 C  CG  . LEU C 1 1168 ? 59.599  16.224  112.483 1.00 122.30 ? 1168 LEU B CG  1 
ATOM   21262 C  CD1 . LEU C 1 1168 ? 60.575  17.275  111.960 1.00 120.27 ? 1168 LEU B CD1 1 
ATOM   21263 C  CD2 . LEU C 1 1168 ? 60.313  15.028  113.098 1.00 120.06 ? 1168 LEU B CD2 1 
ATOM   21264 N  N   . ILE C 1 1169 ? 56.912  15.676  115.948 1.00 152.38 ? 1169 ILE B N   1 
ATOM   21265 C  CA  . ILE C 1 1169 ? 56.860  15.032  117.257 1.00 153.65 ? 1169 ILE B CA  1 
ATOM   21266 C  C   . ILE C 1 1169 ? 55.785  13.963  117.315 1.00 156.41 ? 1169 ILE B C   1 
ATOM   21267 O  O   . ILE C 1 1169 ? 56.056  12.824  117.678 1.00 156.68 ? 1169 ILE B O   1 
ATOM   21268 C  CB  . ILE C 1 1169 ? 56.577  16.053  118.356 1.00 155.61 ? 1169 ILE B CB  1 
ATOM   21269 C  CG1 . ILE C 1 1169 ? 57.795  16.957  118.552 1.00 151.65 ? 1169 ILE B CG1 1 
ATOM   21270 C  CG2 . ILE C 1 1169 ? 56.218  15.351  119.643 1.00 160.47 ? 1169 ILE B CG2 1 
ATOM   21271 C  CD1 . ILE C 1 1169 ? 57.516  18.422  118.285 1.00 151.17 ? 1169 ILE B CD1 1 
ATOM   21272 N  N   . LYS C 1 1170 ? 54.563  14.344  116.953 1.00 175.71 ? 1170 LYS B N   1 
ATOM   21273 C  CA  . LYS C 1 1170 ? 53.454  13.403  116.873 1.00 180.88 ? 1170 LYS B CA  1 
ATOM   21274 C  C   . LYS C 1 1170 ? 53.962  12.119  116.245 1.00 174.79 ? 1170 LYS B C   1 
ATOM   21275 O  O   . LYS C 1 1170 ? 53.464  11.032  116.538 1.00 175.42 ? 1170 LYS B O   1 
ATOM   21276 C  CB  . LYS C 1 1170 ? 52.324  13.964  116.009 1.00 187.34 ? 1170 LYS B CB  1 
ATOM   21277 C  CG  . LYS C 1 1170 ? 51.614  15.187  116.574 1.00 197.48 ? 1170 LYS B CG  1 
ATOM   21278 C  CD  . LYS C 1 1170 ? 50.894  14.873  117.878 1.00 209.82 ? 1170 LYS B CD  1 
ATOM   21279 C  CE  . LYS C 1 1170 ? 49.796  13.834  117.687 1.00 217.54 ? 1170 LYS B CE  1 
ATOM   21280 N  NZ  . LYS C 1 1170 ? 49.070  13.543  118.956 1.00 224.73 ? 1170 LYS B NZ  1 
ATOM   21281 N  N   . ALA C 1 1171 ? 54.956  12.260  115.372 1.00 186.59 ? 1171 ALA B N   1 
ATOM   21282 C  CA  . ALA C 1 1171 ? 55.574  11.126  114.698 1.00 185.54 ? 1171 ALA B CA  1 
ATOM   21283 C  C   . ALA C 1 1171 ? 56.526  10.407  115.634 1.00 186.79 ? 1171 ALA B C   1 
ATOM   21284 O  O   . ALA C 1 1171 ? 56.331  9.237   115.962 1.00 188.81 ? 1171 ALA B O   1 
ATOM   21285 C  CB  . ALA C 1 1171 ? 56.316  11.593  113.464 1.00 182.16 ? 1171 ALA B CB  1 
ATOM   21286 N  N   . ASP C 1 1172 ? 57.561  11.112  116.067 1.00 191.73 ? 1172 ASP B N   1 
ATOM   21287 C  CA  . ASP C 1 1172 ? 58.508  10.521  116.992 1.00 193.38 ? 1172 ASP B CA  1 
ATOM   21288 C  C   . ASP C 1 1172 ? 57.739  9.771   118.086 1.00 198.46 ? 1172 ASP B C   1 
ATOM   21289 O  O   . ASP C 1 1172 ? 58.036  8.619   118.397 1.00 198.23 ? 1172 ASP B O   1 
ATOM   21290 C  CB  . ASP C 1 1172 ? 59.432  11.598  117.581 1.00 195.17 ? 1172 ASP B CB  1 
ATOM   21291 C  CG  . ASP C 1 1172 ? 60.623  11.933  116.668 1.00 193.27 ? 1172 ASP B CG  1 
ATOM   21292 O  OD1 . ASP C 1 1172 ? 60.579  11.623  115.463 1.00 190.56 ? 1172 ASP B OD1 1 
ATOM   21293 O  OD2 . ASP C 1 1172 ? 61.616  12.511  117.159 1.00 194.89 ? 1172 ASP B OD2 1 
ATOM   21294 N  N   . ASN C 1 1173 ? 56.720  10.419  118.636 1.00 202.23 ? 1173 ASN B N   1 
ATOM   21295 C  CA  . ASN C 1 1173 ? 55.899  9.800   119.664 1.00 209.20 ? 1173 ASN B CA  1 
ATOM   21296 C  C   . ASN C 1 1173 ? 55.459  8.413   119.275 1.00 207.76 ? 1173 ASN B C   1 
ATOM   21297 O  O   . ASN C 1 1173 ? 55.852  7.445   119.911 1.00 210.00 ? 1173 ASN B O   1 
ATOM   21298 C  CB  . ASN C 1 1173 ? 54.664  10.643  119.960 1.00 217.78 ? 1173 ASN B CB  1 
ATOM   21299 C  CG  . ASN C 1 1173 ? 54.964  11.810  120.868 1.00 225.72 ? 1173 ASN B CG  1 
ATOM   21300 O  OD1 . ASN C 1 1173 ? 54.269  12.031  121.861 1.00 233.45 ? 1173 ASN B OD1 1 
ATOM   21301 N  ND2 . ASN C 1 1173 ? 56.010  12.563  120.541 1.00 223.23 ? 1173 ASN B ND2 1 
ATOM   21302 N  N   . PHE C 1 1174 ? 54.643  8.323   118.228 1.00 194.45 ? 1174 PHE B N   1 
ATOM   21303 C  CA  . PHE C 1 1174 ? 54.163  7.032   117.759 1.00 193.88 ? 1174 PHE B CA  1 
ATOM   21304 C  C   . PHE C 1 1174 ? 55.333  6.082   117.857 1.00 189.79 ? 1174 PHE B C   1 
ATOM   21305 O  O   . PHE C 1 1174 ? 55.186  4.957   118.331 1.00 193.59 ? 1174 PHE B O   1 
ATOM   21306 C  CB  . PHE C 1 1174 ? 53.644  7.119   116.309 1.00 190.41 ? 1174 PHE B CB  1 
ATOM   21307 C  CG  . PHE C 1 1174 ? 53.273  5.775   115.682 1.00 189.08 ? 1174 PHE B CG  1 
ATOM   21308 C  CD1 . PHE C 1 1174 ? 51.952  5.351   115.632 1.00 192.74 ? 1174 PHE B CD1 1 
ATOM   21309 C  CD2 . PHE C 1 1174 ? 54.245  4.961   115.107 1.00 185.41 ? 1174 PHE B CD2 1 
ATOM   21310 C  CE1 . PHE C 1 1174 ? 51.618  4.137   115.049 1.00 193.76 ? 1174 PHE B CE1 1 
ATOM   21311 C  CE2 . PHE C 1 1174 ? 53.911  3.750   114.523 1.00 185.92 ? 1174 PHE B CE2 1 
ATOM   21312 C  CZ  . PHE C 1 1174 ? 52.597  3.341   114.495 1.00 190.19 ? 1174 PHE B CZ  1 
ATOM   21313 N  N   . LEU C 1 1175 ? 56.510  6.558   117.462 1.00 186.95 ? 1175 LEU B N   1 
ATOM   21314 C  CA  . LEU C 1 1175 ? 57.670  5.687   117.381 1.00 184.76 ? 1175 LEU B CA  1 
ATOM   21315 C  C   . LEU C 1 1175 ? 58.072  5.098   118.727 1.00 187.84 ? 1175 LEU B C   1 
ATOM   21316 O  O   . LEU C 1 1175 ? 58.081  3.878   118.897 1.00 188.51 ? 1175 LEU B O   1 
ATOM   21317 C  CB  . LEU C 1 1175 ? 58.840  6.387   116.714 1.00 180.44 ? 1175 LEU B CB  1 
ATOM   21318 C  CG  . LEU C 1 1175 ? 58.829  6.212   115.203 1.00 176.77 ? 1175 LEU B CG  1 
ATOM   21319 C  CD1 . LEU C 1 1175 ? 60.171  6.600   114.651 1.00 172.15 ? 1175 LEU B CD1 1 
ATOM   21320 C  CD2 . LEU C 1 1175 ? 58.510  4.778   114.845 1.00 177.64 ? 1175 LEU B CD2 1 
ATOM   21321 N  N   . LEU C 1 1176 ? 58.395  5.946   119.691 1.00 190.13 ? 1176 LEU B N   1 
ATOM   21322 C  CA  . LEU C 1 1176 ? 58.667  5.445   121.030 1.00 194.70 ? 1176 LEU B CA  1 
ATOM   21323 C  C   . LEU C 1 1176 ? 57.517  4.542   121.463 1.00 204.71 ? 1176 LEU B C   1 
ATOM   21324 O  O   . LEU C 1 1176 ? 57.689  3.329   121.635 1.00 208.32 ? 1176 LEU B O   1 
ATOM   21325 C  CB  . LEU C 1 1176 ? 58.775  6.626   121.974 1.00 192.07 ? 1176 LEU B CB  1 
ATOM   21326 C  CG  . LEU C 1 1176 ? 59.574  7.665   121.199 1.00 183.39 ? 1176 LEU B CG  1 
ATOM   21327 C  CD1 . LEU C 1 1176 ? 59.369  9.050   121.759 1.00 183.96 ? 1176 LEU B CD1 1 
ATOM   21328 C  CD2 . LEU C 1 1176 ? 61.032  7.249   121.201 1.00 180.74 ? 1176 LEU B CD2 1 
ATOM   21329 N  N   . GLU C 1 1177 ? 56.335  5.153   121.578 1.00 229.39 ? 1177 GLU B N   1 
ATOM   21330 C  CA  . GLU C 1 1177 ? 55.141  4.520   122.135 1.00 237.71 ? 1177 GLU B CA  1 
ATOM   21331 C  C   . GLU C 1 1177 ? 54.678  3.284   121.384 1.00 237.96 ? 1177 GLU B C   1 
ATOM   21332 O  O   . GLU C 1 1177 ? 53.578  2.807   121.631 1.00 244.49 ? 1177 GLU B O   1 
ATOM   21333 C  CB  . GLU C 1 1177 ? 53.973  5.523   122.216 1.00 244.17 ? 1177 GLU B CB  1 
ATOM   21334 C  CG  . GLU C 1 1177 ? 53.896  6.347   123.510 1.00 252.75 ? 1177 GLU B CG  1 
ATOM   21335 C  CD  . GLU C 1 1177 ? 52.528  6.992   123.747 1.00 261.91 ? 1177 GLU B CD  1 
ATOM   21336 O  OE1 . GLU C 1 1177 ? 52.090  7.071   124.916 1.00 269.36 ? 1177 GLU B OE1 1 
ATOM   21337 O  OE2 . GLU C 1 1177 ? 51.887  7.416   122.766 1.00 261.53 ? 1177 GLU B OE2 1 
ATOM   21338 N  N   . ASN C 1 1178 ? 55.499  2.762   120.479 1.00 191.82 ? 1178 ASN B N   1 
ATOM   21339 C  CA  . ASN C 1 1178 ? 55.077  1.618   119.676 1.00 189.13 ? 1178 ASN B CA  1 
ATOM   21340 C  C   . ASN C 1 1178 ? 56.203  0.732   119.110 1.00 183.88 ? 1178 ASN B C   1 
ATOM   21341 O  O   . ASN C 1 1178 ? 55.918  -0.255  118.437 1.00 184.30 ? 1178 ASN B O   1 
ATOM   21342 C  CB  . ASN C 1 1178 ? 54.131  2.066   118.537 1.00 185.30 ? 1178 ASN B CB  1 
ATOM   21343 C  CG  . ASN C 1 1178 ? 52.630  1.861   118.860 1.00 188.39 ? 1178 ASN B CG  1 
ATOM   21344 O  OD1 . ASN C 1 1178 ? 52.093  0.751   118.751 1.00 190.47 ? 1178 ASN B OD1 1 
ATOM   21345 N  ND2 . ASN C 1 1178 ? 51.949  2.951   119.210 1.00 189.42 ? 1178 ASN B ND2 1 
ATOM   21346 N  N   . THR C 1 1179 ? 57.467  1.057   119.363 1.00 202.34 ? 1179 THR B N   1 
ATOM   21347 C  CA  . THR C 1 1179 ? 58.536  0.216   118.812 1.00 197.67 ? 1179 THR B CA  1 
ATOM   21348 C  C   . THR C 1 1179 ? 58.801  -1.048  119.612 1.00 199.44 ? 1179 THR B C   1 
ATOM   21349 O  O   . THR C 1 1179 ? 58.885  -2.148  119.064 1.00 198.03 ? 1179 THR B O   1 
ATOM   21350 C  CB  . THR C 1 1179 ? 59.911  0.918   118.786 1.00 180.01 ? 1179 THR B CB  1 
ATOM   21351 O  OG1 . THR C 1 1179 ? 59.762  2.289   118.423 1.00 177.82 ? 1179 THR B OG1 1 
ATOM   21352 C  CG2 . THR C 1 1179 ? 60.866  0.211   117.814 1.00 168.78 ? 1179 THR B CG2 1 
ATOM   21353 N  N   . LEU C 1 1180 ? 58.947  -0.870  120.920 1.00 265.26 ? 1180 LEU B N   1 
ATOM   21354 C  CA  . LEU C 1 1180 ? 59.813  -1.741  121.712 1.00 268.11 ? 1180 LEU B CA  1 
ATOM   21355 C  C   . LEU C 1 1180 ? 59.429  -3.193  121.927 1.00 277.84 ? 1180 LEU B C   1 
ATOM   21356 O  O   . LEU C 1 1180 ? 60.306  -4.044  122.032 1.00 279.27 ? 1180 LEU B O   1 
ATOM   21357 C  CB  . LEU C 1 1180 ? 60.222  -1.067  123.017 1.00 266.61 ? 1180 LEU B CB  1 
ATOM   21358 C  CG  . LEU C 1 1180 ? 61.506  -0.282  122.745 1.00 257.77 ? 1180 LEU B CG  1 
ATOM   21359 C  CD1 . LEU C 1 1180 ? 62.082  0.317   124.005 1.00 258.48 ? 1180 LEU B CD1 1 
ATOM   21360 C  CD2 . LEU C 1 1180 ? 62.525  -1.197  122.075 1.00 254.24 ? 1180 LEU B CD2 1 
ATOM   21361 N  N   . PRO C 1 1181 ? 58.136  -3.490  122.032 1.00 204.07 ? 1181 PRO B N   1 
ATOM   21362 C  CA  . PRO C 1 1181 ? 57.897  -4.923  121.873 1.00 205.95 ? 1181 PRO B CA  1 
ATOM   21363 C  C   . PRO C 1 1181 ? 58.307  -5.315  120.453 1.00 200.82 ? 1181 PRO B C   1 
ATOM   21364 O  O   . PRO C 1 1181 ? 57.453  -5.574  119.607 1.00 199.48 ? 1181 PRO B O   1 
ATOM   21365 C  CB  . PRO C 1 1181 ? 56.390  -5.041  122.076 1.00 208.32 ? 1181 PRO B CB  1 
ATOM   21366 C  CG  . PRO C 1 1181 ? 56.069  -3.911  123.013 1.00 209.74 ? 1181 PRO B CG  1 
ATOM   21367 C  CD  . PRO C 1 1181 ? 56.985  -2.786  122.621 1.00 205.07 ? 1181 PRO B CD  1 
ATOM   21368 N  N   . ALA C 1 1182 ? 59.617  -5.353  120.215 1.00 213.41 ? 1182 ALA B N   1 
ATOM   21369 C  CA  . ALA C 1 1182 ? 60.203  -5.471  118.880 1.00 206.58 ? 1182 ALA B CA  1 
ATOM   21370 C  C   . ALA C 1 1182 ? 59.714  -6.676  118.089 1.00 210.39 ? 1182 ALA B C   1 
ATOM   21371 O  O   . ALA C 1 1182 ? 59.848  -7.808  118.545 1.00 215.84 ? 1182 ALA B O   1 
ATOM   21372 C  CB  . ALA C 1 1182 ? 61.722  -5.504  118.984 1.00 199.88 ? 1182 ALA B CB  1 
ATOM   21373 N  N   . GLN C 1 1183 ? 59.169  -6.413  116.898 1.00 196.49 ? 1183 GLN B N   1 
ATOM   21374 C  CA  . GLN C 1 1183 ? 58.691  -7.450  115.983 1.00 194.65 ? 1183 GLN B CA  1 
ATOM   21375 C  C   . GLN C 1 1183 ? 59.800  -7.994  115.075 1.00 186.92 ? 1183 GLN B C   1 
ATOM   21376 O  O   . GLN C 1 1183 ? 59.826  -9.188  114.755 1.00 189.32 ? 1183 GLN B O   1 
ATOM   21377 C  CB  . GLN C 1 1183 ? 57.555  -6.907  115.126 1.00 196.07 ? 1183 GLN B CB  1 
ATOM   21378 C  CG  . GLN C 1 1183 ? 56.803  -7.990  114.373 1.00 201.87 ? 1183 GLN B CG  1 
ATOM   21379 C  CD  . GLN C 1 1183 ? 56.034  -8.905  115.307 1.00 210.16 ? 1183 GLN B CD  1 
ATOM   21380 O  OE1 . GLN C 1 1183 ? 55.907  -8.613  116.496 1.00 213.04 ? 1183 GLN B OE1 1 
ATOM   21381 N  NE2 . GLN C 1 1183 ? 55.514  -10.013 114.777 1.00 213.45 ? 1183 GLN B NE2 1 
ATOM   21382 N  N   . SER C 1 1184 ? 60.712  -7.109  114.672 1.00 179.43 ? 1184 SER B N   1 
ATOM   21383 C  CA  . SER C 1 1184 ? 61.873  -7.487  113.859 1.00 174.74 ? 1184 SER B CA  1 
ATOM   21384 C  C   . SER C 1 1184 ? 63.051  -6.501  113.891 1.00 169.26 ? 1184 SER B C   1 
ATOM   21385 O  O   . SER C 1 1184 ? 62.858  -5.288  113.988 1.00 166.29 ? 1184 SER B O   1 
ATOM   21386 C  CB  . SER C 1 1184 ? 61.476  -7.711  112.408 1.00 174.37 ? 1184 SER B CB  1 
ATOM   21387 O  OG  . SER C 1 1184 ? 62.645  -7.807  111.614 1.00 171.15 ? 1184 SER B OG  1 
ATOM   21388 N  N   . THR C 1 1185 ? 64.263  -7.047  113.773 1.00 169.14 ? 1185 THR B N   1 
ATOM   21389 C  CA  . THR C 1 1185 ? 65.505  -6.274  113.785 1.00 164.37 ? 1185 THR B CA  1 
ATOM   21390 C  C   . THR C 1 1185 ? 65.436  -5.150  112.770 1.00 159.52 ? 1185 THR B C   1 
ATOM   21391 O  O   . THR C 1 1185 ? 65.777  -3.994  113.066 1.00 154.71 ? 1185 THR B O   1 
ATOM   21392 C  CB  . THR C 1 1185 ? 66.718  -7.157  113.393 1.00 163.46 ? 1185 THR B CB  1 
ATOM   21393 O  OG1 . THR C 1 1185 ? 66.818  -8.266  114.291 1.00 167.07 ? 1185 THR B OG1 1 
ATOM   21394 C  CG2 . THR C 1 1185 ? 68.027  -6.352  113.406 1.00 159.36 ? 1185 THR B CG2 1 
ATOM   21395 N  N   . PHE C 1 1186 ? 65.014  -5.510  111.559 1.00 204.91 ? 1186 PHE B N   1 
ATOM   21396 C  CA  . PHE C 1 1186 ? 64.821  -4.540  110.497 1.00 200.60 ? 1186 PHE B CA  1 
ATOM   21397 C  C   . PHE C 1 1186 ? 63.918  -3.467  111.095 1.00 202.49 ? 1186 PHE B C   1 
ATOM   21398 O  O   . PHE C 1 1186 ? 64.341  -2.322  111.220 1.00 201.33 ? 1186 PHE B O   1 
ATOM   21399 C  CB  . PHE C 1 1186 ? 64.212  -5.211  109.247 1.00 197.25 ? 1186 PHE B CB  1 
ATOM   21400 C  CG  . PHE C 1 1186 ? 63.976  -4.278  108.066 1.00 191.60 ? 1186 PHE B CG  1 
ATOM   21401 C  CD1 . PHE C 1 1186 ? 65.024  -3.855  107.261 1.00 187.84 ? 1186 PHE B CD1 1 
ATOM   21402 C  CD2 . PHE C 1 1186 ? 62.685  -3.871  107.738 1.00 191.45 ? 1186 PHE B CD2 1 
ATOM   21403 C  CE1 . PHE C 1 1186 ? 64.785  -3.012  106.179 1.00 184.24 ? 1186 PHE B CE1 1 
ATOM   21404 C  CE2 . PHE C 1 1186 ? 62.446  -3.038  106.658 1.00 188.41 ? 1186 PHE B CE2 1 
ATOM   21405 C  CZ  . PHE C 1 1186 ? 63.495  -2.607  105.880 1.00 184.84 ? 1186 PHE B CZ  1 
ATOM   21406 N  N   . THR C 1 1187 ? 62.718  -3.843  111.545 1.00 135.11 ? 1187 THR B N   1 
ATOM   21407 C  CA  . THR C 1 1187 ? 61.738  -2.850  111.999 1.00 133.28 ? 1187 THR B CA  1 
ATOM   21408 C  C   . THR C 1 1187 ? 62.372  -1.868  112.963 1.00 131.34 ? 1187 THR B C   1 
ATOM   21409 O  O   . THR C 1 1187 ? 62.276  -0.641  112.815 1.00 128.63 ? 1187 THR B O   1 
ATOM   21410 C  CB  . THR C 1 1187 ? 60.562  -3.485  112.743 1.00 136.56 ? 1187 THR B CB  1 
ATOM   21411 O  OG1 . THR C 1 1187 ? 60.065  -4.604  112.003 1.00 136.97 ? 1187 THR B OG1 1 
ATOM   21412 C  CG2 . THR C 1 1187 ? 59.451  -2.447  112.940 1.00 137.01 ? 1187 THR B CG2 1 
ATOM   21413 N  N   . LEU C 1 1188 ? 63.017  -2.449  113.963 1.00 173.00 ? 1188 LEU B N   1 
ATOM   21414 C  CA  . LEU C 1 1188 ? 63.706  -1.717  115.001 1.00 172.79 ? 1188 LEU B CA  1 
ATOM   21415 C  C   . LEU C 1 1188 ? 64.644  -0.721  114.366 1.00 168.01 ? 1188 LEU B C   1 
ATOM   21416 O  O   . LEU C 1 1188 ? 64.566  0.481   114.616 1.00 166.96 ? 1188 LEU B O   1 
ATOM   21417 C  CB  . LEU C 1 1188 ? 64.533  -2.705  115.809 1.00 175.43 ? 1188 LEU B CB  1 
ATOM   21418 C  CG  . LEU C 1 1188 ? 64.382  -2.599  117.312 1.00 174.48 ? 1188 LEU B CG  1 
ATOM   21419 C  CD1 . LEU C 1 1188 ? 62.941  -2.284  117.654 1.00 175.33 ? 1188 LEU B CD1 1 
ATOM   21420 C  CD2 . LEU C 1 1188 ? 64.824  -3.906  117.931 1.00 175.93 ? 1188 LEU B CD2 1 
ATOM   21421 N  N   . ALA C 1 1189 ? 65.511  -1.255  113.513 1.00 162.05 ? 1189 ALA B N   1 
ATOM   21422 C  CA  . ALA C 1 1189 ? 66.653  -0.537  112.974 1.00 161.46 ? 1189 ALA B CA  1 
ATOM   21423 C  C   . ALA C 1 1189 ? 66.318  0.857   112.453 1.00 157.12 ? 1189 ALA B C   1 
ATOM   21424 O  O   . ALA C 1 1189 ? 67.020  1.825   112.751 1.00 153.78 ? 1189 ALA B O   1 
ATOM   21425 C  CB  . ALA C 1 1189 ? 67.329  -1.369  111.894 1.00 160.45 ? 1189 ALA B CB  1 
ATOM   21426 N  N   . ILE C 1 1190 ? 65.258  0.966   111.662 1.00 184.25 ? 1190 ILE B N   1 
ATOM   21427 C  CA  . ILE C 1 1190 ? 64.877  2.268   111.134 1.00 183.24 ? 1190 ILE B CA  1 
ATOM   21428 C  C   . ILE C 1 1190 ? 64.248  3.086   112.261 1.00 184.77 ? 1190 ILE B C   1 
ATOM   21429 O  O   . ILE C 1 1190 ? 64.537  4.278   112.404 1.00 182.51 ? 1190 ILE B O   1 
ATOM   21430 C  CB  . ILE C 1 1190 ? 63.945  2.170   109.886 1.00 181.20 ? 1190 ILE B CB  1 
ATOM   21431 C  CG1 . ILE C 1 1190 ? 64.672  1.476   108.735 1.00 179.69 ? 1190 ILE B CG1 1 
ATOM   21432 C  CG2 . ILE C 1 1190 ? 63.527  3.545   109.411 1.00 178.71 ? 1190 ILE B CG2 1 
ATOM   21433 C  CD1 . ILE C 1 1190 ? 63.841  1.306   107.487 1.00 179.28 ? 1190 ILE B CD1 1 
ATOM   21434 N  N   . SER C 1 1191 ? 63.426  2.446   113.092 1.00 144.52 ? 1191 SER B N   1 
ATOM   21435 C  CA  . SER C 1 1191 ? 62.792  3.174   114.182 1.00 144.46 ? 1191 SER B CA  1 
ATOM   21436 C  C   . SER C 1 1191 ? 63.888  3.811   115.021 1.00 142.66 ? 1191 SER B C   1 
ATOM   21437 O  O   . SER C 1 1191 ? 63.724  4.889   115.603 1.00 141.05 ? 1191 SER B O   1 
ATOM   21438 C  CB  . SER C 1 1191 ? 61.948  2.255   115.043 1.00 148.38 ? 1191 SER B CB  1 
ATOM   21439 O  OG  . SER C 1 1191 ? 61.180  3.041   115.934 1.00 150.68 ? 1191 SER B OG  1 
ATOM   21440 N  N   . ALA C 1 1192 ? 65.019  3.116   115.053 1.00 114.91 ? 1192 ALA B N   1 
ATOM   21441 C  CA  . ALA C 1 1192 ? 66.220  3.555   115.750 1.00 113.13 ? 1192 ALA B CA  1 
ATOM   21442 C  C   . ALA C 1 1192 ? 66.777  4.798   115.109 1.00 113.67 ? 1192 ALA B C   1 
ATOM   21443 O  O   . ALA C 1 1192 ? 66.673  5.910   115.629 1.00 115.71 ? 1192 ALA B O   1 
ATOM   21444 C  CB  . ALA C 1 1192 ? 67.287  2.452   115.682 1.00 110.57 ? 1192 ALA B CB  1 
ATOM   21445 N  N   . TYR C 1 1193 ? 67.401  4.571   113.966 1.00 142.06 ? 1193 TYR B N   1 
ATOM   21446 C  CA  . TYR C 1 1193 ? 68.108  5.609   113.271 1.00 138.51 ? 1193 TYR B CA  1 
ATOM   21447 C  C   . TYR C 1 1193 ? 67.254  6.879   113.156 1.00 137.96 ? 1193 TYR B C   1 
ATOM   21448 O  O   . TYR C 1 1193 ? 67.785  7.978   113.077 1.00 138.56 ? 1193 TYR B O   1 
ATOM   21449 C  CB  . TYR C 1 1193 ? 68.570  5.078   111.915 1.00 136.05 ? 1193 TYR B CB  1 
ATOM   21450 C  CG  . TYR C 1 1193 ? 69.223  6.129   111.071 1.00 132.61 ? 1193 TYR B CG  1 
ATOM   21451 C  CD1 . TYR C 1 1193 ? 70.525  6.516   111.305 1.00 133.75 ? 1193 TYR B CD1 1 
ATOM   21452 C  CD2 . TYR C 1 1193 ? 68.526  6.762   110.052 1.00 128.80 ? 1193 TYR B CD2 1 
ATOM   21453 C  CE1 . TYR C 1 1193 ? 71.124  7.500   110.538 1.00 131.52 ? 1193 TYR B CE1 1 
ATOM   21454 C  CE2 . TYR C 1 1193 ? 69.117  7.748   109.281 1.00 126.76 ? 1193 TYR B CE2 1 
ATOM   21455 C  CZ  . TYR C 1 1193 ? 70.418  8.109   109.532 1.00 127.13 ? 1193 TYR B CZ  1 
ATOM   21456 O  OH  . TYR C 1 1193 ? 71.017  9.086   108.780 1.00 122.80 ? 1193 TYR B OH  1 
ATOM   21457 N  N   . ALA C 1 1194 ? 65.934  6.725   113.198 1.00 189.95 ? 1194 ALA B N   1 
ATOM   21458 C  CA  . ALA C 1 1194 ? 64.998  7.840   113.018 1.00 188.20 ? 1194 ALA B CA  1 
ATOM   21459 C  C   . ALA C 1 1194 ? 64.877  8.781   114.218 1.00 187.65 ? 1194 ALA B C   1 
ATOM   21460 O  O   . ALA C 1 1194 ? 64.945  10.005  114.077 1.00 186.10 ? 1194 ALA B O   1 
ATOM   21461 C  CB  . ALA C 1 1194 ? 63.639  7.300   112.667 1.00 189.92 ? 1194 ALA B CB  1 
ATOM   21462 N  N   . LEU C 1 1195 ? 64.659  8.211   115.395 1.00 139.80 ? 1195 LEU B N   1 
ATOM   21463 C  CA  . LEU C 1 1195 ? 64.716  8.993   116.616 1.00 140.80 ? 1195 LEU B CA  1 
ATOM   21464 C  C   . LEU C 1 1195 ? 66.119  9.551   116.679 1.00 140.93 ? 1195 LEU B C   1 
ATOM   21465 O  O   . LEU C 1 1195 ? 66.312  10.713  117.026 1.00 142.77 ? 1195 LEU B O   1 
ATOM   21466 C  CB  . LEU C 1 1195 ? 64.440  8.082   117.786 1.00 141.90 ? 1195 LEU B CB  1 
ATOM   21467 C  CG  . LEU C 1 1195 ? 63.259  7.240   117.326 1.00 144.39 ? 1195 LEU B CG  1 
ATOM   21468 C  CD1 . LEU C 1 1195 ? 63.038  6.014   118.185 1.00 148.03 ? 1195 LEU B CD1 1 
ATOM   21469 C  CD2 . LEU C 1 1195 ? 62.003  8.102   117.248 1.00 145.19 ? 1195 LEU B CD2 1 
ATOM   21470 N  N   . SER C 1 1196 ? 67.085  8.709   116.297 1.00 84.93  ? 1196 SER B N   1 
ATOM   21471 C  CA  . SER C 1 1196 ? 68.499  9.079   116.134 1.00 85.66  ? 1196 SER B CA  1 
ATOM   21472 C  C   . SER C 1 1196 ? 68.654  10.465  115.522 1.00 86.82  ? 1196 SER B C   1 
ATOM   21473 O  O   . SER C 1 1196 ? 69.576  11.219  115.854 1.00 84.42  ? 1196 SER B O   1 
ATOM   21474 C  CB  . SER C 1 1196 ? 69.238  8.037   115.273 1.00 83.88  ? 1196 SER B CB  1 
ATOM   21475 O  OG  . SER C 1 1196 ? 70.647  8.187   115.331 1.00 83.76  ? 1196 SER B OG  1 
ATOM   21476 N  N   . LEU C 1 1197 ? 67.737  10.819  114.633 1.00 177.10 ? 1197 LEU B N   1 
ATOM   21477 C  CA  . LEU C 1 1197 ? 67.813  12.137  113.996 1.00 184.48 ? 1197 LEU B CA  1 
ATOM   21478 C  C   . LEU C 1 1197 ? 66.922  13.162  114.689 1.00 191.67 ? 1197 LEU B C   1 
ATOM   21479 O  O   . LEU C 1 1197 ? 66.209  13.933  114.051 1.00 190.85 ? 1197 LEU B O   1 
ATOM   21480 C  CB  . LEU C 1 1197 ? 67.542  12.052  112.484 1.00 185.10 ? 1197 LEU B CB  1 
ATOM   21481 C  CG  . LEU C 1 1197 ? 68.537  11.223  111.637 1.00 186.54 ? 1197 LEU B CG  1 
ATOM   21482 C  CD1 . LEU C 1 1197 ? 67.966  10.894  110.264 1.00 187.08 ? 1197 LEU B CD1 1 
ATOM   21483 C  CD2 . LEU C 1 1197 ? 69.920  11.874  111.505 1.00 185.97 ? 1197 LEU B CD2 1 
ATOM   21484 N  N   . GLY C 1 1198 ? 67.003  13.177  116.012 1.00 207.95 ? 1198 GLY B N   1 
ATOM   21485 C  CA  . GLY C 1 1198 ? 66.271  14.143  116.805 1.00 215.65 ? 1198 GLY B CA  1 
ATOM   21486 C  C   . GLY C 1 1198 ? 66.794  14.242  118.231 1.00 221.39 ? 1198 GLY B C   1 
ATOM   21487 O  O   . GLY C 1 1198 ? 67.992  14.485  118.454 1.00 223.60 ? 1198 GLY B O   1 
ATOM   21488 N  N   . ASP C 1 1199 ? 65.882  14.080  119.195 1.00 195.39 ? 1199 ASP B N   1 
ATOM   21489 C  CA  . ASP C 1 1199 ? 66.234  13.966  120.610 1.00 195.28 ? 1199 ASP B CA  1 
ATOM   21490 C  C   . ASP C 1 1199 ? 66.777  12.592  120.940 1.00 187.33 ? 1199 ASP B C   1 
ATOM   21491 O  O   . ASP C 1 1199 ? 66.043  11.627  121.164 1.00 188.03 ? 1199 ASP B O   1 
ATOM   21492 C  CB  . ASP C 1 1199 ? 65.049  14.240  121.518 1.00 204.09 ? 1199 ASP B CB  1 
ATOM   21493 C  CG  . ASP C 1 1199 ? 65.351  13.891  122.945 1.00 213.13 ? 1199 ASP B CG  1 
ATOM   21494 O  OD1 . ASP C 1 1199 ? 66.545  13.716  123.250 1.00 212.63 ? 1199 ASP B OD1 1 
ATOM   21495 O  OD2 . ASP C 1 1199 ? 64.411  13.783  123.755 1.00 220.37 ? 1199 ASP B OD2 1 
ATOM   21496 N  N   . LYS C 1 1200 ? 68.089  12.543  120.996 1.00 191.38 ? 1200 LYS B N   1 
ATOM   21497 C  CA  . LYS C 1 1200 ? 68.812  11.317  121.152 1.00 187.25 ? 1200 LYS B CA  1 
ATOM   21498 C  C   . LYS C 1 1200 ? 68.873  10.928  122.612 1.00 194.96 ? 1200 LYS B C   1 
ATOM   21499 O  O   . LYS C 1 1200 ? 69.683  10.083  122.977 1.00 200.45 ? 1200 LYS B O   1 
ATOM   21500 C  CB  . LYS C 1 1200 ? 70.215  11.556  120.614 1.00 180.03 ? 1200 LYS B CB  1 
ATOM   21501 C  CG  . LYS C 1 1200 ? 70.408  12.997  120.128 1.00 180.15 ? 1200 LYS B CG  1 
ATOM   21502 C  CD  . LYS C 1 1200 ? 71.252  13.025  118.883 1.00 179.96 ? 1200 LYS B CD  1 
ATOM   21503 C  CE  . LYS C 1 1200 ? 72.567  12.327  119.149 1.00 182.35 ? 1200 LYS B CE  1 
ATOM   21504 N  NZ  . LYS C 1 1200 ? 73.335  12.123  117.902 1.00 179.89 ? 1200 LYS B NZ  1 
ATOM   21505 N  N   . THR C 1 1201 ? 68.028  11.534  123.449 1.00 202.50 ? 1201 THR B N   1 
ATOM   21506 C  CA  . THR C 1 1201 ? 68.169  11.384  124.913 1.00 203.91 ? 1201 THR B CA  1 
ATOM   21507 C  C   . THR C 1 1201 ? 66.936  10.976  125.719 1.00 209.16 ? 1201 THR B C   1 
ATOM   21508 O  O   . THR C 1 1201 ? 66.997  10.872  126.948 1.00 213.52 ? 1201 THR B O   1 
ATOM   21509 C  CB  . THR C 1 1201 ? 68.680  12.667  125.568 1.00 202.83 ? 1201 THR B CB  1 
ATOM   21510 O  OG1 . THR C 1 1201 ? 67.908  13.779  125.096 1.00 201.14 ? 1201 THR B OG1 1 
ATOM   21511 C  CG2 . THR C 1 1201 ? 70.149  12.881  125.255 1.00 198.34 ? 1201 THR B CG2 1 
ATOM   21512 N  N   . HIS C 1 1202 ? 65.818  10.765  125.041 1.00 160.57 ? 1202 HIS B N   1 
ATOM   21513 C  CA  . HIS C 1 1202 ? 64.645  10.208  125.693 1.00 168.01 ? 1202 HIS B CA  1 
ATOM   21514 C  C   . HIS C 1 1202 ? 64.960  8.851   126.291 1.00 173.63 ? 1202 HIS B C   1 
ATOM   21515 O  O   . HIS C 1 1202 ? 65.148  7.879   125.564 1.00 171.39 ? 1202 HIS B O   1 
ATOM   21516 C  CB  . HIS C 1 1202 ? 63.524  10.009  124.697 1.00 165.00 ? 1202 HIS B CB  1 
ATOM   21517 C  CG  . HIS C 1 1202 ? 62.237  9.653   125.345 1.00 171.19 ? 1202 HIS B CG  1 
ATOM   21518 N  ND1 . HIS C 1 1202 ? 61.091  10.393  125.165 1.00 173.62 ? 1202 HIS B ND1 1 
ATOM   21519 C  CD2 . HIS C 1 1202 ? 61.926  8.676   126.224 1.00 175.40 ? 1202 HIS B CD2 1 
ATOM   21520 C  CE1 . HIS C 1 1202 ? 60.118  9.863   125.880 1.00 177.25 ? 1202 HIS B CE1 1 
ATOM   21521 N  NE2 . HIS C 1 1202 ? 60.598  8.818   126.530 1.00 179.57 ? 1202 HIS B NE2 1 
ATOM   21522 N  N   . PRO C 1 1203 ? 64.963  8.769   127.615 1.00 179.23 ? 1203 PRO B N   1 
ATOM   21523 C  CA  . PRO C 1 1203 ? 65.278  7.498   128.257 1.00 182.35 ? 1203 PRO B CA  1 
ATOM   21524 C  C   . PRO C 1 1203 ? 64.829  6.363   127.354 1.00 178.51 ? 1203 PRO B C   1 
ATOM   21525 O  O   . PRO C 1 1203 ? 65.581  5.442   127.090 1.00 178.25 ? 1203 PRO B O   1 
ATOM   21526 C  CB  . PRO C 1 1203 ? 64.406  7.534   129.508 1.00 191.01 ? 1203 PRO B CB  1 
ATOM   21527 C  CG  . PRO C 1 1203 ? 64.304  9.001   129.840 1.00 191.22 ? 1203 PRO B CG  1 
ATOM   21528 C  CD  . PRO C 1 1203 ? 64.343  9.736   128.533 1.00 183.57 ? 1203 PRO B CD  1 
ATOM   21529 N  N   . GLN C 1 1204 ? 63.609  6.470   126.845 1.00 152.26 ? 1204 GLN B N   1 
ATOM   21530 C  CA  . GLN C 1 1204 ? 63.032  5.429   126.013 1.00 145.83 ? 1204 GLN B CA  1 
ATOM   21531 C  C   . GLN C 1 1204 ? 63.908  5.080   124.807 1.00 134.80 ? 1204 GLN B C   1 
ATOM   21532 O  O   . GLN C 1 1204 ? 64.199  3.906   124.574 1.00 131.89 ? 1204 GLN B O   1 
ATOM   21533 C  CB  . GLN C 1 1204 ? 61.619  5.823   125.587 1.00 145.40 ? 1204 GLN B CB  1 
ATOM   21534 C  CG  . GLN C 1 1204 ? 60.926  4.820   124.712 1.00 142.69 ? 1204 GLN B CG  1 
ATOM   21535 C  CD  . GLN C 1 1204 ? 60.836  3.465   125.350 1.00 144.24 ? 1204 GLN B CD  1 
ATOM   21536 O  OE1 . GLN C 1 1204 ? 61.221  3.278   126.499 1.00 145.95 ? 1204 GLN B OE1 1 
ATOM   21537 N  NE2 . GLN C 1 1204 ? 60.321  2.506   124.606 1.00 143.90 ? 1204 GLN B NE2 1 
ATOM   21538 N  N   . PHE C 1 1205 ? 64.327  6.087   124.044 1.00 159.57 ? 1205 PHE B N   1 
ATOM   21539 C  CA  . PHE C 1 1205 ? 65.272  5.866   122.949 1.00 153.79 ? 1205 PHE B CA  1 
ATOM   21540 C  C   . PHE C 1 1205 ? 66.346  4.908   123.465 1.00 155.03 ? 1205 PHE B C   1 
ATOM   21541 O  O   . PHE C 1 1205 ? 66.716  3.957   122.773 1.00 154.05 ? 1205 PHE B O   1 
ATOM   21542 C  CB  . PHE C 1 1205 ? 65.850  7.223   122.479 1.00 139.87 ? 1205 PHE B CB  1 
ATOM   21543 C  CG  . PHE C 1 1205 ? 67.092  7.135   121.595 1.00 132.82 ? 1205 PHE B CG  1 
ATOM   21544 C  CD1 . PHE C 1 1205 ? 67.010  6.805   120.260 1.00 130.11 ? 1205 PHE B CD1 1 
ATOM   21545 C  CD2 . PHE C 1 1205 ? 68.335  7.462   122.103 1.00 129.72 ? 1205 PHE B CD2 1 
ATOM   21546 C  CE1 . PHE C 1 1205 ? 68.152  6.754   119.483 1.00 126.30 ? 1205 PHE B CE1 1 
ATOM   21547 C  CE2 . PHE C 1 1205 ? 69.476  7.411   121.321 1.00 125.48 ? 1205 PHE B CE2 1 
ATOM   21548 C  CZ  . PHE C 1 1205 ? 69.383  7.056   120.024 1.00 123.87 ? 1205 PHE B CZ  1 
ATOM   21549 N  N   . ARG C 1 1206 ? 66.785  5.125   124.709 1.00 129.37 ? 1206 ARG B N   1 
ATOM   21550 C  CA  . ARG C 1 1206 ? 67.826  4.303   125.332 1.00 132.06 ? 1206 ARG B CA  1 
ATOM   21551 C  C   . ARG C 1 1206 ? 67.396  2.851   125.345 1.00 133.39 ? 1206 ARG B C   1 
ATOM   21552 O  O   . ARG C 1 1206 ? 68.205  1.933   125.164 1.00 131.54 ? 1206 ARG B O   1 
ATOM   21553 C  CB  . ARG C 1 1206 ? 68.067  4.719   126.789 1.00 140.07 ? 1206 ARG B CB  1 
ATOM   21554 C  CG  . ARG C 1 1206 ? 68.369  6.164   127.014 1.00 143.94 ? 1206 ARG B CG  1 
ATOM   21555 C  CD  . ARG C 1 1206 ? 69.827  6.455   126.759 1.00 148.67 ? 1206 ARG B CD  1 
ATOM   21556 N  NE  . ARG C 1 1206 ? 70.118  7.890   126.734 1.00 152.39 ? 1206 ARG B NE  1 
ATOM   21557 C  CZ  . ARG C 1 1206 ? 69.441  8.825   127.406 1.00 158.43 ? 1206 ARG B CZ  1 
ATOM   21558 N  NH1 . ARG C 1 1206 ? 68.409  8.496   128.185 1.00 163.27 ? 1206 ARG B NH1 1 
ATOM   21559 N  NH2 . ARG C 1 1206 ? 69.811  10.102  127.309 1.00 156.95 ? 1206 ARG B NH2 1 
ATOM   21560 N  N   . SER C 1 1207 ? 66.108  2.655   125.597 1.00 159.90 ? 1207 SER B N   1 
ATOM   21561 C  CA  . SER C 1 1207 ? 65.545  1.324   125.697 1.00 160.69 ? 1207 SER B CA  1 
ATOM   21562 C  C   . SER C 1 1207 ? 65.579  0.726   124.307 1.00 154.48 ? 1207 SER B C   1 
ATOM   21563 O  O   . SER C 1 1207 ? 66.058  -0.387  124.103 1.00 155.90 ? 1207 SER B O   1 
ATOM   21564 C  CB  . SER C 1 1207 ? 64.110  1.388   126.236 1.00 164.37 ? 1207 SER B CB  1 
ATOM   21565 O  OG  . SER C 1 1207 ? 63.692  0.138   126.784 1.00 167.74 ? 1207 SER B OG  1 
ATOM   21566 N  N   . ILE C 1 1208 ? 65.100  1.487   123.335 1.00 156.84 ? 1208 ILE B N   1 
ATOM   21567 C  CA  . ILE C 1 1208 ? 65.074  0.988   121.975 1.00 146.53 ? 1208 ILE B CA  1 
ATOM   21568 C  C   . ILE C 1 1208 ? 66.487  0.652   121.517 1.00 138.39 ? 1208 ILE B C   1 
ATOM   21569 O  O   . ILE C 1 1208 ? 66.777  -0.484  121.119 1.00 135.57 ? 1208 ILE B O   1 
ATOM   21570 C  CB  . ILE C 1 1208 ? 64.416  2.007   121.036 1.00 140.95 ? 1208 ILE B CB  1 
ATOM   21571 C  CG1 . ILE C 1 1208 ? 63.633  3.040   121.869 1.00 140.33 ? 1208 ILE B CG1 1 
ATOM   21572 C  CG2 . ILE C 1 1208 ? 63.561  1.271   120.000 1.00 141.08 ? 1208 ILE B CG2 1 
ATOM   21573 C  CD1 . ILE C 1 1208 ? 62.555  3.868   121.121 1.00 136.80 ? 1208 ILE B CD1 1 
ATOM   21574 N  N   . VAL C 1 1209 ? 67.365  1.644   121.618 1.00 95.01  ? 1209 VAL B N   1 
ATOM   21575 C  CA  . VAL C 1 1209 ? 68.765  1.488   121.248 1.00 96.63  ? 1209 VAL B CA  1 
ATOM   21576 C  C   . VAL C 1 1209 ? 69.311  0.269   121.951 1.00 106.93 ? 1209 VAL B C   1 
ATOM   21577 O  O   . VAL C 1 1209 ? 70.174  -0.440  121.436 1.00 106.24 ? 1209 VAL B O   1 
ATOM   21578 C  CB  . VAL C 1 1209 ? 69.595  2.743   121.650 1.00 95.33  ? 1209 VAL B CB  1 
ATOM   21579 C  CG1 . VAL C 1 1209 ? 71.079  2.543   121.350 1.00 93.34  ? 1209 VAL B CG1 1 
ATOM   21580 C  CG2 . VAL C 1 1209 ? 69.075  3.991   120.952 1.00 92.96  ? 1209 VAL B CG2 1 
ATOM   21581 N  N   . SER C 1 1210 ? 68.791  0.041   123.147 1.00 147.17 ? 1210 SER B N   1 
ATOM   21582 C  CA  . SER C 1 1210 ? 69.156  -1.130  123.905 1.00 156.57 ? 1210 SER B CA  1 
ATOM   21583 C  C   . SER C 1 1210 ? 68.732  -2.352  123.132 1.00 160.38 ? 1210 SER B C   1 
ATOM   21584 O  O   . SER C 1 1210 ? 69.551  -3.167  122.732 1.00 161.46 ? 1210 SER B O   1 
ATOM   21585 C  CB  . SER C 1 1210 ? 68.459  -1.131  125.262 1.00 163.82 ? 1210 SER B CB  1 
ATOM   21586 O  OG  . SER C 1 1210 ? 67.331  -2.004  125.277 1.00 169.31 ? 1210 SER B OG  1 
ATOM   21587 N  N   . ALA C 1 1211 ? 67.434  -2.467  122.920 1.00 181.38 ? 1211 ALA B N   1 
ATOM   21588 C  CA  . ALA C 1 1211 ? 66.877  -3.642  122.288 1.00 181.85 ? 1211 ALA B CA  1 
ATOM   21589 C  C   . ALA C 1 1211 ? 67.622  -3.973  121.002 1.00 175.94 ? 1211 ALA B C   1 
ATOM   21590 O  O   . ALA C 1 1211 ? 68.186  -5.062  120.854 1.00 175.70 ? 1211 ALA B O   1 
ATOM   21591 C  CB  . ALA C 1 1211 ? 65.415  -3.412  122.008 1.00 182.17 ? 1211 ALA B CB  1 
ATOM   21592 N  N   . LEU C 1 1212 ? 67.622  -3.023  120.075 1.00 168.20 ? 1212 LEU B N   1 
ATOM   21593 C  CA  . LEU C 1 1212 ? 68.394  -3.181  118.860 1.00 165.10 ? 1212 LEU B CA  1 
ATOM   21594 C  C   . LEU C 1 1212 ? 69.777  -3.672  119.275 1.00 165.16 ? 1212 LEU B C   1 
ATOM   21595 O  O   . LEU C 1 1212 ? 70.208  -4.764  118.891 1.00 166.38 ? 1212 LEU B O   1 
ATOM   21596 C  CB  . LEU C 1 1212 ? 68.479  -1.845  118.103 1.00 158.69 ? 1212 LEU B CB  1 
ATOM   21597 C  CG  . LEU C 1 1212 ? 69.470  -1.737  116.930 1.00 152.88 ? 1212 LEU B CG  1 
ATOM   21598 C  CD1 . LEU C 1 1212 ? 69.352  -2.943  116.044 1.00 152.98 ? 1212 LEU B CD1 1 
ATOM   21599 C  CD2 . LEU C 1 1212 ? 69.294  -0.453  116.120 1.00 148.53 ? 1212 LEU B CD2 1 
ATOM   21600 N  N   . LYS C 1 1213 ? 70.441  -2.884  120.113 1.00 104.18 ? 1213 LYS B N   1 
ATOM   21601 C  CA  . LYS C 1 1213 ? 71.835  -3.133  120.434 1.00 102.09 ? 1213 LYS B CA  1 
ATOM   21602 C  C   . LYS C 1 1213 ? 71.999  -4.494  121.076 1.00 110.41 ? 1213 LYS B C   1 
ATOM   21603 O  O   . LYS C 1 1213 ? 73.056  -5.128  120.980 1.00 110.39 ? 1213 LYS B O   1 
ATOM   21604 C  CB  . LYS C 1 1213 ? 72.351  -2.029  121.333 1.00 96.02  ? 1213 LYS B CB  1 
ATOM   21605 C  CG  . LYS C 1 1213 ? 73.630  -1.501  120.840 1.00 92.31  ? 1213 LYS B CG  1 
ATOM   21606 C  CD  . LYS C 1 1213 ? 73.712  -0.032  121.053 1.00 91.40  ? 1213 LYS B CD  1 
ATOM   21607 C  CE  . LYS C 1 1213 ? 75.160  0.292   121.345 1.00 92.57  ? 1213 LYS B CE  1 
ATOM   21608 N  NZ  . LYS C 1 1213 ? 75.547  1.718   121.193 1.00 89.57  ? 1213 LYS B NZ  1 
ATOM   21609 N  N   . ARG C 1 1214 ? 70.916  -4.922  121.713 1.00 196.76 ? 1214 ARG B N   1 
ATOM   21610 C  CA  . ARG C 1 1214 ? 70.786  -6.256  122.248 1.00 210.42 ? 1214 ARG B CA  1 
ATOM   21611 C  C   . ARG C 1 1214 ? 70.912  -7.260  121.117 1.00 210.61 ? 1214 ARG B C   1 
ATOM   21612 O  O   . ARG C 1 1214 ? 71.576  -8.280  121.251 1.00 215.11 ? 1214 ARG B O   1 
ATOM   21613 C  CB  . ARG C 1 1214 ? 69.428  -6.411  122.950 1.00 224.67 ? 1214 ARG B CB  1 
ATOM   21614 C  CG  . ARG C 1 1214 ? 68.932  -7.856  123.070 1.00 240.82 ? 1214 ARG B CG  1 
ATOM   21615 C  CD  . ARG C 1 1214 ? 67.727  -8.000  124.004 1.00 254.99 ? 1214 ARG B CD  1 
ATOM   21616 N  NE  . ARG C 1 1214 ? 66.798  -6.880  123.894 1.00 259.48 ? 1214 ARG B NE  1 
ATOM   21617 C  CZ  . ARG C 1 1214 ? 66.149  -6.355  124.927 1.00 267.05 ? 1214 ARG B CZ  1 
ATOM   21618 N  NH1 . ARG C 1 1214 ? 66.335  -6.853  126.138 1.00 274.45 ? 1214 ARG B NH1 1 
ATOM   21619 N  NH2 . ARG C 1 1214 ? 65.320  -5.334  124.755 1.00 265.96 ? 1214 ARG B NH2 1 
ATOM   21620 N  N   . GLU C 1 1215 ? 70.305  -6.946  119.984 1.00 148.00 ? 1215 GLU B N   1 
ATOM   21621 C  CA  . GLU C 1 1215 ? 70.052  -7.961  118.963 1.00 145.76 ? 1215 GLU B CA  1 
ATOM   21622 C  C   . GLU C 1 1215 ? 71.192  -8.333  118.003 1.00 139.72 ? 1215 GLU B C   1 
ATOM   21623 O  O   . GLU C 1 1215 ? 71.140  -9.396  117.373 1.00 141.90 ? 1215 GLU B O   1 
ATOM   21624 C  CB  . GLU C 1 1215 ? 68.796  -7.597  118.178 1.00 142.45 ? 1215 GLU B CB  1 
ATOM   21625 C  CG  . GLU C 1 1215 ? 67.509  -8.018  118.839 1.00 147.02 ? 1215 GLU B CG  1 
ATOM   21626 C  CD  . GLU C 1 1215 ? 67.182  -9.463  118.573 1.00 153.12 ? 1215 GLU B CD  1 
ATOM   21627 O  OE1 . GLU C 1 1215 ? 68.067  -10.210 118.101 1.00 153.87 ? 1215 GLU B OE1 1 
ATOM   21628 O  OE2 . GLU C 1 1215 ? 66.030  -9.846  118.839 1.00 157.47 ? 1215 GLU B OE2 1 
ATOM   21629 N  N   . ALA C 1 1216 ? 72.205  -7.479  117.894 1.00 155.95 ? 1216 ALA B N   1 
ATOM   21630 C  CA  . ALA C 1 1216 ? 73.344  -7.747  117.024 1.00 148.70 ? 1216 ALA B CA  1 
ATOM   21631 C  C   . ALA C 1 1216 ? 73.873  -9.161  117.223 1.00 150.47 ? 1216 ALA B C   1 
ATOM   21632 O  O   . ALA C 1 1216 ? 73.399  -9.872  118.097 1.00 156.64 ? 1216 ALA B O   1 
ATOM   21633 C  CB  . ALA C 1 1216 ? 74.441  -6.757  117.301 1.00 143.78 ? 1216 ALA B CB  1 
ATOM   21634 N  N   . LEU C 1 1217 ? 74.846  -9.560  116.399 1.00 130.26 ? 1217 LEU B N   1 
ATOM   21635 C  CA  . LEU C 1 1217 ? 75.565  -10.841 116.520 1.00 131.13 ? 1217 LEU B CA  1 
ATOM   21636 C  C   . LEU C 1 1217 ? 76.921  -10.599 115.938 1.00 128.39 ? 1217 LEU B C   1 
ATOM   21637 O  O   . LEU C 1 1217 ? 77.255  -9.454  115.675 1.00 120.30 ? 1217 LEU B O   1 
ATOM   21638 C  CB  . LEU C 1 1217 ? 74.882  -11.951 115.735 1.00 130.81 ? 1217 LEU B CB  1 
ATOM   21639 C  CG  . LEU C 1 1217 ? 73.391  -11.684 115.532 1.00 129.70 ? 1217 LEU B CG  1 
ATOM   21640 C  CD1 . LEU C 1 1217 ? 73.057  -11.933 114.093 1.00 125.94 ? 1217 LEU B CD1 1 
ATOM   21641 C  CD2 . LEU C 1 1217 ? 72.514  -12.496 116.478 1.00 136.32 ? 1217 LEU B CD2 1 
ATOM   21642 N  N   . VAL C 1 1218 ? 77.714  -11.640 115.718 1.00 117.51 ? 1218 VAL B N   1 
ATOM   21643 C  CA  . VAL C 1 1218 ? 79.119  -11.349 115.466 1.00 118.47 ? 1218 VAL B CA  1 
ATOM   21644 C  C   . VAL C 1 1218 ? 80.096  -12.485 115.229 1.00 119.66 ? 1218 VAL B C   1 
ATOM   21645 O  O   . VAL C 1 1218 ? 79.817  -13.646 115.531 1.00 119.86 ? 1218 VAL B O   1 
ATOM   21646 C  CB  . VAL C 1 1218 ? 79.678  -10.682 116.653 1.00 125.43 ? 1218 VAL B CB  1 
ATOM   21647 C  CG1 . VAL C 1 1218 ? 79.632  -9.199  116.491 1.00 121.60 ? 1218 VAL B CG1 1 
ATOM   21648 C  CG2 . VAL C 1 1218 ? 78.879  -11.147 117.866 1.00 135.03 ? 1218 VAL B CG2 1 
ATOM   21649 N  N   . LYS C 1 1219 ? 81.296  -12.089 114.791 1.00 147.60 ? 1219 LYS B N   1 
ATOM   21650 C  CA  . LYS C 1 1219 ? 82.273  -12.993 114.186 1.00 160.22 ? 1219 LYS B CA  1 
ATOM   21651 C  C   . LYS C 1 1219 ? 83.640  -12.892 114.832 1.00 168.50 ? 1219 LYS B C   1 
ATOM   21652 O  O   . LYS C 1 1219 ? 84.287  -11.851 114.756 1.00 166.89 ? 1219 LYS B O   1 
ATOM   21653 C  CB  . LYS C 1 1219 ? 82.405  -12.693 112.677 1.00 161.10 ? 1219 LYS B CB  1 
ATOM   21654 C  CG  . LYS C 1 1219 ? 81.322  -13.383 111.749 1.00 224.78 ? 1219 LYS B CG  1 
ATOM   21655 C  CD  . LYS C 1 1219 ? 81.275  -12.823 110.275 1.00 207.81 ? 1219 LYS B CD  1 
ATOM   21656 C  CE  . LYS C 1 1219 ? 80.190  -13.475 109.388 1.00 191.59 ? 1219 LYS B CE  1 
ATOM   21657 N  NZ  . LYS C 1 1219 ? 80.011  -12.731 108.108 1.00 187.01 ? 1219 LYS B NZ  1 
ATOM   21658 N  N   . GLY C 1 1220 ? 84.086  -13.995 115.427 1.00 261.80 ? 1220 GLY B N   1 
ATOM   21659 C  CA  . GLY C 1 1220 ? 85.369  -14.043 116.099 1.00 264.64 ? 1220 GLY B CA  1 
ATOM   21660 C  C   . GLY C 1 1220 ? 85.385  -13.228 117.381 1.00 266.57 ? 1220 GLY B C   1 
ATOM   21661 O  O   . GLY C 1 1220 ? 84.774  -12.160 117.449 1.00 264.08 ? 1220 GLY B O   1 
ATOM   21662 N  N   . ASN C 1 1221 ? 86.076  -13.743 118.397 1.00 192.94 ? 1221 ASN B N   1 
ATOM   21663 C  CA  . ASN C 1 1221 ? 86.243  -13.059 119.675 1.00 194.56 ? 1221 ASN B CA  1 
ATOM   21664 C  C   . ASN C 1 1221 ? 87.685  -12.568 119.815 1.00 190.25 ? 1221 ASN B C   1 
ATOM   21665 O  O   . ASN C 1 1221 ? 88.621  -13.245 119.400 1.00 192.12 ? 1221 ASN B O   1 
ATOM   21666 C  CB  . ASN C 1 1221 ? 85.841  -13.986 120.835 1.00 203.43 ? 1221 ASN B CB  1 
ATOM   21667 C  CG  . ASN C 1 1221 ? 85.952  -13.322 122.206 1.00 205.89 ? 1221 ASN B CG  1 
ATOM   21668 O  OD1 . ASN C 1 1221 ? 86.824  -13.665 123.002 1.00 209.34 ? 1221 ASN B OD1 1 
ATOM   21669 N  ND2 . ASN C 1 1221 ? 85.055  -12.387 122.491 1.00 203.58 ? 1221 ASN B ND2 1 
ATOM   21670 N  N   . PRO C 1 1222 ? 87.860  -11.355 120.341 1.00 165.44 ? 1222 PRO B N   1 
ATOM   21671 C  CA  . PRO C 1 1222 ? 86.749  -10.443 120.622 1.00 160.19 ? 1222 PRO B CA  1 
ATOM   21672 C  C   . PRO C 1 1222 ? 85.999  -10.131 119.319 1.00 155.29 ? 1222 PRO B C   1 
ATOM   21673 O  O   . PRO C 1 1222 ? 86.459  -10.570 118.266 1.00 156.18 ? 1222 PRO B O   1 
ATOM   21674 C  CB  . PRO C 1 1222 ? 87.463  -9.189  121.133 1.00 158.37 ? 1222 PRO B CB  1 
ATOM   21675 C  CG  . PRO C 1 1222 ? 88.808  -9.662  121.600 1.00 161.64 ? 1222 PRO B CG  1 
ATOM   21676 C  CD  . PRO C 1 1222 ? 89.167  -10.770 120.681 1.00 163.22 ? 1222 PRO B CD  1 
ATOM   21677 N  N   . PRO C 1 1223 ? 84.858  -9.419  119.379 1.00 197.94 ? 1223 PRO B N   1 
ATOM   21678 C  CA  . PRO C 1 1223 ? 84.263  -8.962  118.120 1.00 187.23 ? 1223 PRO B CA  1 
ATOM   21679 C  C   . PRO C 1 1223 ? 85.260  -8.385  117.076 1.00 178.38 ? 1223 PRO B C   1 
ATOM   21680 O  O   . PRO C 1 1223 ? 85.927  -7.379  117.358 1.00 173.81 ? 1223 PRO B O   1 
ATOM   21681 C  CB  . PRO C 1 1223 ? 83.281  -7.883  118.600 1.00 184.17 ? 1223 PRO B CB  1 
ATOM   21682 C  CG  . PRO C 1 1223 ? 82.783  -8.413  119.903 1.00 191.40 ? 1223 PRO B CG  1 
ATOM   21683 C  CD  . PRO C 1 1223 ? 83.917  -9.242  120.503 1.00 199.82 ? 1223 PRO B CD  1 
ATOM   21684 N  N   . ILE C 1 1224 ? 85.355  -9.038  115.904 1.00 166.22 ? 1224 ILE B N   1 
ATOM   21685 C  CA  . ILE C 1 1224 ? 85.989  -8.467  114.699 1.00 159.94 ? 1224 ILE B CA  1 
ATOM   21686 C  C   . ILE C 1 1224 ? 84.938  -8.053  113.626 1.00 156.09 ? 1224 ILE B C   1 
ATOM   21687 O  O   . ILE C 1 1224 ? 85.167  -7.103  112.857 1.00 152.56 ? 1224 ILE B O   1 
ATOM   21688 C  CB  . ILE C 1 1224 ? 87.057  -9.399  114.048 1.00 159.59 ? 1224 ILE B CB  1 
ATOM   21689 C  CG1 . ILE C 1 1224 ? 88.036  -9.953  115.059 1.00 166.22 ? 1224 ILE B CG1 1 
ATOM   21690 C  CG2 . ILE C 1 1224 ? 87.897  -8.634  113.054 1.00 152.68 ? 1224 ILE B CG2 1 
ATOM   21691 C  CD1 . ILE C 1 1224 ? 89.281  -10.453 114.380 1.00 169.17 ? 1224 ILE B CD1 1 
ATOM   21692 N  N   . TYR C 1 1225 ? 83.800  -8.760  113.584 1.00 140.77 ? 1225 TYR B N   1 
ATOM   21693 C  CA  . TYR C 1 1225 ? 82.668  -8.350  112.763 1.00 136.41 ? 1225 TYR B CA  1 
ATOM   21694 C  C   . TYR C 1 1225 ? 81.393  -8.353  113.570 1.00 135.73 ? 1225 TYR B C   1 
ATOM   21695 O  O   . TYR C 1 1225 ? 81.051  -9.343  114.192 1.00 139.24 ? 1225 TYR B O   1 
ATOM   21696 C  CB  . TYR C 1 1225 ? 82.478  -9.279  111.572 1.00 138.82 ? 1225 TYR B CB  1 
ATOM   21697 C  CG  . TYR C 1 1225 ? 83.704  -9.468  110.715 1.00 140.14 ? 1225 TYR B CG  1 
ATOM   21698 C  CD1 . TYR C 1 1225 ? 84.060  -8.532  109.748 1.00 137.67 ? 1225 TYR B CD1 1 
ATOM   21699 C  CD2 . TYR C 1 1225 ? 84.506  -10.587 110.865 1.00 145.17 ? 1225 TYR B CD2 1 
ATOM   21700 C  CE1 . TYR C 1 1225 ? 85.195  -8.707  108.956 1.00 138.67 ? 1225 TYR B CE1 1 
ATOM   21701 C  CE2 . TYR C 1 1225 ? 85.637  -10.773 110.076 1.00 146.36 ? 1225 TYR B CE2 1 
ATOM   21702 C  CZ  . TYR C 1 1225 ? 85.980  -9.827  109.126 1.00 142.27 ? 1225 TYR B CZ  1 
ATOM   21703 O  OH  . TYR C 1 1225 ? 87.110  -10.010 108.350 1.00 142.20 ? 1225 TYR B OH  1 
ATOM   21704 N  N   . ARG C 1 1226 ? 80.690  -7.235  113.538 1.00 134.36 ? 1226 ARG B N   1 
ATOM   21705 C  CA  . ARG C 1 1226 ? 79.387  -7.124  114.153 1.00 139.69 ? 1226 ARG B CA  1 
ATOM   21706 C  C   . ARG C 1 1226 ? 78.408  -6.845  113.070 1.00 138.40 ? 1226 ARG B C   1 
ATOM   21707 O  O   . ARG C 1 1226 ? 78.692  -6.030  112.228 1.00 135.21 ? 1226 ARG B O   1 
ATOM   21708 C  CB  . ARG C 1 1226 ? 79.332  -5.918  115.066 1.00 142.83 ? 1226 ARG B CB  1 
ATOM   21709 C  CG  . ARG C 1 1226 ? 77.942  -5.689  115.636 1.00 145.75 ? 1226 ARG B CG  1 
ATOM   21710 C  CD  . ARG C 1 1226 ? 77.957  -4.876  116.961 1.00 145.26 ? 1226 ARG B CD  1 
ATOM   21711 N  NE  . ARG C 1 1226 ? 79.282  -4.434  117.441 1.00 143.10 ? 1226 ARG B NE  1 
ATOM   21712 C  CZ  . ARG C 1 1226 ? 79.958  -4.974  118.461 1.00 140.94 ? 1226 ARG B CZ  1 
ATOM   21713 N  NH1 . ARG C 1 1226 ? 79.451  -6.006  119.147 1.00 141.15 ? 1226 ARG B NH1 1 
ATOM   21714 N  NH2 . ARG C 1 1226 ? 81.148  -4.473  118.796 1.00 138.57 ? 1226 ARG B NH2 1 
ATOM   21715 N  N   . PHE C 1 1227 ? 77.247  -7.481  113.082 1.00 146.41 ? 1227 PHE B N   1 
ATOM   21716 C  CA  . PHE C 1 1227 ? 76.181  -7.094  112.156 1.00 141.59 ? 1227 PHE B CA  1 
ATOM   21717 C  C   . PHE C 1 1227 ? 74.868  -7.579  112.673 1.00 142.63 ? 1227 PHE B C   1 
ATOM   21718 O  O   . PHE C 1 1227 ? 74.819  -8.298  113.660 1.00 146.19 ? 1227 PHE B O   1 
ATOM   21719 C  CB  . PHE C 1 1227 ? 76.413  -7.602  110.738 1.00 142.14 ? 1227 PHE B CB  1 
ATOM   21720 C  CG  . PHE C 1 1227 ? 76.675  -9.064  110.648 1.00 148.29 ? 1227 PHE B CG  1 
ATOM   21721 C  CD1 . PHE C 1 1227 ? 75.626  -9.960  110.656 1.00 150.39 ? 1227 PHE B CD1 1 
ATOM   21722 C  CD2 . PHE C 1 1227 ? 77.973  -9.544  110.515 1.00 149.35 ? 1227 PHE B CD2 1 
ATOM   21723 C  CE1 . PHE C 1 1227 ? 75.857  -11.316 110.553 1.00 152.39 ? 1227 PHE B CE1 1 
ATOM   21724 C  CE2 . PHE C 1 1227 ? 78.217  -10.902 110.405 1.00 150.69 ? 1227 PHE B CE2 1 
ATOM   21725 C  CZ  . PHE C 1 1227 ? 77.154  -11.793 110.429 1.00 152.91 ? 1227 PHE B CZ  1 
ATOM   21726 N  N   . TRP C 1 1228 ? 73.785  -7.164  112.054 1.00 107.44 ? 1228 TRP B N   1 
ATOM   21727 C  CA  . TRP C 1 1228 ? 72.525  -7.635  112.571 1.00 111.97 ? 1228 TRP B CA  1 
ATOM   21728 C  C   . TRP C 1 1228 ? 71.924  -8.419  111.457 1.00 130.76 ? 1228 TRP B C   1 
ATOM   21729 O  O   . TRP C 1 1228 ? 72.509  -8.424  110.390 1.00 127.75 ? 1228 TRP B O   1 
ATOM   21730 C  CB  . TRP C 1 1228 ? 71.620  -6.502  112.977 1.00 108.69 ? 1228 TRP B CB  1 
ATOM   21731 C  CG  . TRP C 1 1228 ? 72.107  -5.542  114.093 1.00 109.70 ? 1228 TRP B CG  1 
ATOM   21732 C  CD1 . TRP C 1 1228 ? 71.407  -5.178  115.213 1.00 112.88 ? 1228 TRP B CD1 1 
ATOM   21733 C  CD2 . TRP C 1 1228 ? 73.336  -4.785  114.149 1.00 107.32 ? 1228 TRP B CD2 1 
ATOM   21734 N  NE1 . TRP C 1 1228 ? 72.113  -4.254  115.949 1.00 111.48 ? 1228 TRP B NE1 1 
ATOM   21735 C  CE2 . TRP C 1 1228 ? 73.296  -3.999  115.311 1.00 108.36 ? 1228 TRP B CE2 1 
ATOM   21736 C  CE3 . TRP C 1 1228 ? 74.460  -4.695  113.329 1.00 102.97 ? 1228 TRP B CE3 1 
ATOM   21737 C  CZ2 . TRP C 1 1228 ? 74.328  -3.153  115.663 1.00 105.32 ? 1228 TRP B CZ2 1 
ATOM   21738 C  CZ3 . TRP C 1 1228 ? 75.492  -3.837  113.700 1.00 100.23 ? 1228 TRP B CZ3 1 
ATOM   21739 C  CH2 . TRP C 1 1228 ? 75.412  -3.086  114.843 1.00 101.07 ? 1228 TRP B CH2 1 
ATOM   21740 N  N   . LYS C 1 1229 ? 70.794  -9.090  111.701 1.00 143.88 ? 1229 LYS B N   1 
ATOM   21741 C  CA  . LYS C 1 1229 ? 70.180  -10.025 110.737 1.00 147.57 ? 1229 LYS B CA  1 
ATOM   21742 C  C   . LYS C 1 1229 ? 68.742  -9.603  110.428 1.00 155.02 ? 1229 LYS B C   1 
ATOM   21743 O  O   . LYS C 1 1229 ? 68.163  -8.803  111.164 1.00 155.64 ? 1229 LYS B O   1 
ATOM   21744 C  CB  . LYS C 1 1229 ? 70.185  -11.453 111.302 1.00 151.50 ? 1229 LYS B CB  1 
ATOM   21745 C  CG  . LYS C 1 1229 ? 70.546  -12.549 110.309 1.00 154.96 ? 1229 LYS B CG  1 
ATOM   21746 C  CD  . LYS C 1 1229 ? 70.986  -13.828 111.034 1.00 193.72 ? 1229 LYS B CD  1 
ATOM   21747 C  CE  . LYS C 1 1229 ? 69.858  -14.524 111.805 1.00 193.26 ? 1229 LYS B CE  1 
ATOM   21748 N  NZ  . LYS C 1 1229 ? 69.088  -15.491 110.978 1.00 189.82 ? 1229 LYS B NZ  1 
ATOM   21749 N  N   . ASP C 1 1230 ? 68.160  -10.134 109.355 1.00 220.14 ? 1230 ASP B N   1 
ATOM   21750 C  CA  . ASP C 1 1230 ? 66.794  -9.758  108.998 1.00 226.87 ? 1230 ASP B CA  1 
ATOM   21751 C  C   . ASP C 1 1230 ? 65.863  -10.016 110.175 1.00 237.32 ? 1230 ASP B C   1 
ATOM   21752 O  O   . ASP C 1 1230 ? 65.107  -9.141  110.592 1.00 235.13 ? 1230 ASP B O   1 
ATOM   21753 C  CB  . ASP C 1 1230 ? 66.316  -10.532 107.762 1.00 230.94 ? 1230 ASP B CB  1 
ATOM   21754 C  CG  . ASP C 1 1230 ? 64.948  -10.066 107.260 1.00 235.23 ? 1230 ASP B CG  1 
ATOM   21755 O  OD1 . ASP C 1 1230 ? 64.269  -9.314  107.988 1.00 236.10 ? 1230 ASP B OD1 1 
ATOM   21756 O  OD2 . ASP C 1 1230 ? 64.553  -10.448 106.136 1.00 237.17 ? 1230 ASP B OD2 1 
ATOM   21757 N  N   . ASN C 1 1231 ? 65.957  -11.219 110.727 1.00 284.83 ? 1231 ASN B N   1 
ATOM   21758 C  CA  . ASN C 1 1231 ? 65.056  -11.668 111.786 1.00 297.68 ? 1231 ASN B CA  1 
ATOM   21759 C  C   . ASN C 1 1231 ? 65.028  -10.795 113.040 1.00 303.97 ? 1231 ASN B C   1 
ATOM   21760 O  O   . ASN C 1 1231 ? 65.279  -9.593  112.994 1.00 299.82 ? 1231 ASN B O   1 
ATOM   21761 C  CB  . ASN C 1 1231 ? 65.396  -13.103 112.200 1.00 306.95 ? 1231 ASN B CB  1 
ATOM   21762 C  CG  . ASN C 1 1231 ? 66.619  -13.175 113.097 1.00 311.47 ? 1231 ASN B CG  1 
ATOM   21763 O  OD1 . ASN C 1 1231 ? 67.736  -12.918 112.659 1.00 310.76 ? 1231 ASN B OD1 1 
ATOM   21764 N  ND2 . ASN C 1 1231 ? 66.410  -13.524 114.362 1.00 316.29 ? 1231 ASN B ND2 1 
ATOM   21765 N  N   . LEU C 1 1232 ? 64.706  -11.435 114.160 1.00 202.27 ? 1232 LEU B N   1 
ATOM   21766 C  CA  . LEU C 1 1232 ? 64.613  -10.798 115.462 1.00 206.44 ? 1232 LEU B CA  1 
ATOM   21767 C  C   . LEU C 1 1232 ? 64.486  -11.891 116.512 1.00 220.79 ? 1232 LEU B C   1 
ATOM   21768 O  O   . LEU C 1 1232 ? 63.374  -12.264 116.880 1.00 229.14 ? 1232 LEU B O   1 
ATOM   21769 C  CB  . LEU C 1 1232 ? 63.378  -9.902  115.531 1.00 196.53 ? 1232 LEU B CB  1 
ATOM   21770 C  CG  . LEU C 1 1232 ? 62.908  -9.553  116.944 1.00 189.44 ? 1232 LEU B CG  1 
ATOM   21771 C  CD1 . LEU C 1 1232 ? 63.298  -8.142  117.312 1.00 182.13 ? 1232 LEU B CD1 1 
ATOM   21772 C  CD2 . LEU C 1 1232 ? 61.416  -9.741  117.084 1.00 189.27 ? 1232 LEU B CD2 1 
ATOM   21773 N  N   . GLN C 1 1233 ? 65.622  -12.421 116.965 1.00 317.07 ? 1233 GLN B N   1 
ATOM   21774 C  CA  . GLN C 1 1233 ? 65.686  -13.395 118.071 1.00 329.42 ? 1233 GLN B CA  1 
ATOM   21775 C  C   . GLN C 1 1233 ? 64.940  -14.724 117.884 1.00 346.09 ? 1233 GLN B C   1 
ATOM   21776 O  O   . GLN C 1 1233 ? 64.786  -15.493 118.835 1.00 349.42 ? 1233 GLN B O   1 
ATOM   21777 C  CB  . GLN C 1 1233 ? 65.272  -12.757 119.401 1.00 340.42 ? 1233 GLN B CB  1 
ATOM   21778 C  CG  . GLN C 1 1233 ? 63.771  -12.678 119.626 1.00 351.30 ? 1233 GLN B CG  1 
ATOM   21779 C  CD  . GLN C 1 1233 ? 63.416  -12.007 120.935 1.00 360.59 ? 1233 GLN B CD  1 
ATOM   21780 O  OE1 . GLN C 1 1233 ? 63.688  -12.539 122.011 1.00 368.34 ? 1233 GLN B OE1 1 
ATOM   21781 N  NE2 . GLN C 1 1233 ? 62.809  -10.828 120.852 1.00 359.21 ? 1233 GLN B NE2 1 
ATOM   21782 N  N   . HIS C 1 1234 ? 64.462  -14.986 116.675 1.00 245.33 ? 1234 HIS B N   1 
ATOM   21783 C  CA  . HIS C 1 1234 ? 63.933  -16.302 116.346 1.00 251.43 ? 1234 HIS B CA  1 
ATOM   21784 C  C   . HIS C 1 1234 ? 65.133  -17.176 116.002 1.00 256.31 ? 1234 HIS B C   1 
ATOM   21785 O  O   . HIS C 1 1234 ? 65.047  -18.401 115.965 1.00 260.16 ? 1234 HIS B O   1 
ATOM   21786 C  CB  . HIS C 1 1234 ? 62.937  -16.222 115.185 1.00 245.76 ? 1234 HIS B CB  1 
ATOM   21787 C  CG  . HIS C 1 1234 ? 61.732  -15.374 115.478 1.00 242.34 ? 1234 HIS B CG  1 
ATOM   21788 N  ND1 . HIS C 1 1234 ? 60.921  -15.585 116.571 1.00 246.90 ? 1234 HIS B ND1 1 
ATOM   21789 C  CD2 . HIS C 1 1234 ? 61.194  -14.326 114.807 1.00 236.80 ? 1234 HIS B CD2 1 
ATOM   21790 C  CE1 . HIS C 1 1234 ? 59.940  -14.697 116.568 1.00 244.76 ? 1234 HIS B CE1 1 
ATOM   21791 N  NE2 . HIS C 1 1234 ? 60.083  -13.923 115.509 1.00 238.67 ? 1234 HIS B NE2 1 
ATOM   21792 N  N   . LYS C 1 1235 ? 66.250  -16.504 115.737 1.00 254.72 ? 1235 LYS B N   1 
ATOM   21793 C  CA  . LYS C 1 1235 ? 67.566  -17.127 115.631 1.00 262.32 ? 1235 LYS B CA  1 
ATOM   21794 C  C   . LYS C 1 1235 ? 67.583  -18.480 114.920 1.00 275.79 ? 1235 LYS B C   1 
ATOM   21795 O  O   . LYS C 1 1235 ? 68.055  -19.470 115.476 1.00 282.26 ? 1235 LYS B O   1 
ATOM   21796 C  CB  . LYS C 1 1235 ? 68.200  -17.255 117.020 1.00 263.32 ? 1235 LYS B CB  1 
ATOM   21797 C  CG  . LYS C 1 1235 ? 68.464  -15.927 117.730 1.00 257.02 ? 1235 LYS B CG  1 
ATOM   21798 C  CD  . LYS C 1 1235 ? 69.784  -15.296 117.297 1.00 248.97 ? 1235 LYS B CD  1 
ATOM   21799 C  CE  . LYS C 1 1235 ? 70.168  -14.119 118.191 1.00 244.20 ? 1235 LYS B CE  1 
ATOM   21800 N  NZ  . LYS C 1 1235 ? 69.233  -12.963 118.083 1.00 239.71 ? 1235 LYS B NZ  1 
ATOM   21801 N  N   . ASP C 1 1236 ? 67.066  -18.526 113.697 1.00 305.59 ? 1236 ASP B N   1 
ATOM   21802 C  CA  . ASP C 1 1236 ? 67.272  -19.699 112.862 1.00 316.87 ? 1236 ASP B CA  1 
ATOM   21803 C  C   . ASP C 1 1236 ? 68.756  -19.731 112.543 1.00 319.92 ? 1236 ASP B C   1 
ATOM   21804 O  O   . ASP C 1 1236 ? 69.306  -20.745 112.109 1.00 322.72 ? 1236 ASP B O   1 
ATOM   21805 C  CB  . ASP C 1 1236 ? 66.455  -19.614 111.582 1.00 318.21 ? 1236 ASP B CB  1 
ATOM   21806 C  CG  . ASP C 1 1236 ? 66.379  -20.938 110.867 1.00 325.96 ? 1236 ASP B CG  1 
ATOM   21807 O  OD1 . ASP C 1 1236 ? 67.284  -21.773 111.073 1.00 329.70 ? 1236 ASP B OD1 1 
ATOM   21808 O  OD2 . ASP C 1 1236 ? 65.413  -21.150 110.107 1.00 328.46 ? 1236 ASP B OD2 1 
ATOM   21809 N  N   . SER C 1 1237 ? 69.385  -18.583 112.771 1.00 311.80 ? 1237 SER B N   1 
ATOM   21810 C  CA  . SER C 1 1237 ? 70.827  -18.412 112.663 1.00 312.45 ? 1237 SER B CA  1 
ATOM   21811 C  C   . SER C 1 1237 ? 71.351  -18.684 111.261 1.00 311.31 ? 1237 SER B C   1 
ATOM   21812 O  O   . SER C 1 1237 ? 72.563  -18.749 111.048 1.00 314.14 ? 1237 SER B O   1 
ATOM   21813 C  CB  . SER C 1 1237 ? 71.557  -19.274 113.692 1.00 317.26 ? 1237 SER B CB  1 
ATOM   21814 O  OG  . SER C 1 1237 ? 72.872  -18.792 113.897 1.00 314.21 ? 1237 SER B OG  1 
ATOM   21815 N  N   . SER C 1 1238 ? 70.435  -18.838 110.309 1.00 430.93 ? 1238 SER B N   1 
ATOM   21816 C  CA  . SER C 1 1238 ? 70.806  -19.015 108.909 1.00 427.02 ? 1238 SER B CA  1 
ATOM   21817 C  C   . SER C 1 1238 ? 71.389  -17.734 108.299 1.00 420.97 ? 1238 SER B C   1 
ATOM   21818 O  O   . SER C 1 1238 ? 70.686  -16.981 107.619 1.00 415.67 ? 1238 SER B O   1 
ATOM   21819 C  CB  . SER C 1 1238 ? 69.609  -19.510 108.085 1.00 431.16 ? 1238 SER B CB  1 
ATOM   21820 O  OG  . SER C 1 1238 ? 68.526  -18.596 108.138 1.00 433.00 ? 1238 SER B OG  1 
ATOM   21821 N  N   . VAL C 1 1239 ? 72.675  -17.495 108.560 1.00 253.28 ? 1239 VAL B N   1 
ATOM   21822 C  CA  . VAL C 1 1239 ? 73.438  -16.433 107.907 1.00 243.48 ? 1239 VAL B CA  1 
ATOM   21823 C  C   . VAL C 1 1239 ? 74.294  -17.067 106.819 1.00 239.92 ? 1239 VAL B C   1 
ATOM   21824 O  O   . VAL C 1 1239 ? 75.469  -16.728 106.687 1.00 236.34 ? 1239 VAL B O   1 
ATOM   21825 C  CB  . VAL C 1 1239 ? 74.385  -15.705 108.903 1.00 243.23 ? 1239 VAL B CB  1 
ATOM   21826 C  CG1 . VAL C 1 1239 ? 73.626  -15.235 110.117 1.00 246.02 ? 1239 VAL B CG1 1 
ATOM   21827 C  CG2 . VAL C 1 1239 ? 75.525  -16.616 109.335 1.00 249.35 ? 1239 VAL B CG2 1 
ATOM   21828 N  N   . PRO C 1 1240 ? 73.694  -17.965 106.014 1.00 321.50 ? 1240 PRO B N   1 
ATOM   21829 C  CA  . PRO C 1 1240 ? 74.456  -18.983 105.281 1.00 323.53 ? 1240 PRO B CA  1 
ATOM   21830 C  C   . PRO C 1 1240 ? 75.631  -18.415 104.491 1.00 314.40 ? 1240 PRO B C   1 
ATOM   21831 O  O   . PRO C 1 1240 ? 75.615  -18.445 103.261 1.00 316.79 ? 1240 PRO B O   1 
ATOM   21832 C  CB  . PRO C 1 1240 ? 73.412  -19.588 104.334 1.00 329.17 ? 1240 PRO B CB  1 
ATOM   21833 C  CG  . PRO C 1 1240 ? 72.375  -18.542 104.189 1.00 325.54 ? 1240 PRO B CG  1 
ATOM   21834 C  CD  . PRO C 1 1240 ? 72.310  -17.863 105.518 1.00 323.03 ? 1240 PRO B CD  1 
ATOM   21835 N  N   . ASN C 1 1241 ? 76.641  -17.915 105.197 1.00 314.03 ? 1241 ASN B N   1 
ATOM   21836 C  CA  . ASN C 1 1241 ? 77.827  -17.367 104.561 1.00 300.02 ? 1241 ASN B CA  1 
ATOM   21837 C  C   . ASN C 1 1241 ? 77.490  -16.338 103.481 1.00 275.67 ? 1241 ASN B C   1 
ATOM   21838 O  O   . ASN C 1 1241 ? 78.271  -16.127 102.555 1.00 270.51 ? 1241 ASN B O   1 
ATOM   21839 C  CB  . ASN C 1 1241 ? 78.660  -18.499 103.962 1.00 314.39 ? 1241 ASN B CB  1 
ATOM   21840 C  CG  . ASN C 1 1241 ? 78.957  -19.593 104.964 1.00 327.11 ? 1241 ASN B CG  1 
ATOM   21841 O  OD1 . ASN C 1 1241 ? 79.190  -19.318 106.142 1.00 328.63 ? 1241 ASN B OD1 1 
ATOM   21842 N  ND2 . ASN C 1 1241 ? 78.951  -20.841 104.504 1.00 334.43 ? 1241 ASN B ND2 1 
ATOM   21843 N  N   . THR C 1 1242 ? 76.330  -15.697 103.602 1.00 228.45 ? 1242 THR B N   1 
ATOM   21844 C  CA  . THR C 1 1242 ? 75.843  -14.827 102.540 1.00 207.55 ? 1242 THR B CA  1 
ATOM   21845 C  C   . THR C 1 1242 ? 75.016  -13.660 103.025 1.00 183.17 ? 1242 THR B C   1 
ATOM   21846 O  O   . THR C 1 1242 ? 74.065  -13.825 103.793 1.00 177.91 ? 1242 THR B O   1 
ATOM   21847 C  CB  . THR C 1 1242 ? 74.905  -15.578 101.617 1.00 213.80 ? 1242 THR B CB  1 
ATOM   21848 O  OG1 . THR C 1 1242 ? 73.852  -16.140 102.407 1.00 218.14 ? 1242 THR B OG1 1 
ATOM   21849 C  CG2 . THR C 1 1242 ? 75.638  -16.674 100.869 1.00 217.90 ? 1242 THR B CG2 1 
ATOM   21850 N  N   . GLY C 1 1243 ? 75.356  -12.488 102.506 1.00 182.46 ? 1243 GLY B N   1 
ATOM   21851 C  CA  . GLY C 1 1243 ? 74.633  -11.272 102.803 1.00 170.19 ? 1243 GLY B CA  1 
ATOM   21852 C  C   . GLY C 1 1243 ? 73.286  -11.179 102.116 1.00 162.38 ? 1243 GLY B C   1 
ATOM   21853 O  O   . GLY C 1 1243 ? 72.848  -12.109 101.440 1.00 165.65 ? 1243 GLY B O   1 
ATOM   21854 N  N   . THR C 1 1244 ? 72.642  -10.027 102.288 1.00 148.65 ? 1244 THR B N   1 
ATOM   21855 C  CA  . THR C 1 1244 ? 71.273  -9.804  101.853 1.00 147.10 ? 1244 THR B CA  1 
ATOM   21856 C  C   . THR C 1 1244 ? 71.069  -8.349  101.521 1.00 151.46 ? 1244 THR B C   1 
ATOM   21857 O  O   . THR C 1 1244 ? 71.814  -7.475  101.948 1.00 152.07 ? 1244 THR B O   1 
ATOM   21858 C  CB  . THR C 1 1244 ? 70.258  -10.148 102.974 1.00 145.03 ? 1244 THR B CB  1 
ATOM   21859 O  OG1 . THR C 1 1244 ? 70.342  -11.541 103.302 1.00 148.20 ? 1244 THR B OG1 1 
ATOM   21860 C  CG2 . THR C 1 1244 ? 68.829  -9.806  102.560 1.00 143.10 ? 1244 THR B CG2 1 
ATOM   21861 N  N   . ALA C 1 1245 ? 70.047  -8.092  100.739 1.00 170.50 ? 1245 ALA B N   1 
ATOM   21862 C  CA  . ALA C 1 1245 ? 69.628  -6.737  100.547 1.00 169.38 ? 1245 ALA B CA  1 
ATOM   21863 C  C   . ALA C 1 1245 ? 69.186  -6.222  101.905 1.00 169.85 ? 1245 ALA B C   1 
ATOM   21864 O  O   . ALA C 1 1245 ? 69.641  -5.180  102.367 1.00 165.49 ? 1245 ALA B O   1 
ATOM   21865 C  CB  . ALA C 1 1245 ? 68.484  -6.708  99.583  1.00 171.67 ? 1245 ALA B CB  1 
ATOM   21866 N  N   . ARG C 1 1246 ? 68.294  -6.977  102.537 1.00 159.59 ? 1246 ARG B N   1 
ATOM   21867 C  CA  . ARG C 1 1246 ? 67.673  -6.574  103.786 1.00 160.99 ? 1246 ARG B CA  1 
ATOM   21868 C  C   . ARG C 1 1246 ? 68.640  -6.640  104.946 1.00 158.84 ? 1246 ARG B C   1 
ATOM   21869 O  O   . ARG C 1 1246 ? 68.634  -5.762  105.807 1.00 156.86 ? 1246 ARG B O   1 
ATOM   21870 C  CB  . ARG C 1 1246 ? 66.458  -7.440  104.084 1.00 164.70 ? 1246 ARG B CB  1 
ATOM   21871 C  CG  . ARG C 1 1246 ? 65.627  -6.908  105.226 1.00 166.09 ? 1246 ARG B CG  1 
ATOM   21872 C  CD  . ARG C 1 1246 ? 64.359  -7.715  105.411 1.00 173.47 ? 1246 ARG B CD  1 
ATOM   21873 N  NE  . ARG C 1 1246 ? 63.445  -7.586  104.286 1.00 179.90 ? 1246 ARG B NE  1 
ATOM   21874 C  CZ  . ARG C 1 1246 ? 62.283  -6.937  104.328 1.00 186.10 ? 1246 ARG B CZ  1 
ATOM   21875 N  NH1 . ARG C 1 1246 ? 61.876  -6.357  105.451 1.00 188.10 ? 1246 ARG B NH1 1 
ATOM   21876 N  NH2 . ARG C 1 1246 ? 61.523  -6.872  103.240 1.00 188.24 ? 1246 ARG B NH2 1 
ATOM   21877 N  N   . MET C 1 1247 ? 69.461  -7.687  104.978 1.00 207.79 ? 1247 MET B N   1 
ATOM   21878 C  CA  . MET C 1 1247 ? 70.520  -7.803  105.990 1.00 205.57 ? 1247 MET B CA  1 
ATOM   21879 C  C   . MET C 1 1247 ? 71.360  -6.520  106.019 1.00 201.15 ? 1247 MET B C   1 
ATOM   21880 O  O   . MET C 1 1247 ? 71.265  -5.714  106.944 1.00 199.60 ? 1247 MET B O   1 
ATOM   21881 C  CB  . MET C 1 1247 ? 71.410  -9.022  105.697 1.00 205.24 ? 1247 MET B CB  1 
ATOM   21882 C  CG  . MET C 1 1247 ? 72.365  -9.454  106.809 1.00 206.05 ? 1247 MET B CG  1 
ATOM   21883 S  SD  . MET C 1 1247 ? 72.774  -11.195 106.595 1.00 225.08 ? 1247 MET B SD  1 
ATOM   21884 C  CE  . MET C 1 1247 ? 71.120  -11.863 106.346 1.00 205.94 ? 1247 MET B CE  1 
ATOM   21885 N  N   . VAL C 1 1248 ? 72.168  -6.319  104.992 1.00 135.52 ? 1248 VAL B N   1 
ATOM   21886 C  CA  . VAL C 1 1248 ? 72.975  -5.132  104.956 1.00 130.23 ? 1248 VAL B CA  1 
ATOM   21887 C  C   . VAL C 1 1248 ? 72.127  -3.870  104.968 1.00 123.92 ? 1248 VAL B C   1 
ATOM   21888 O  O   . VAL C 1 1248 ? 72.634  -2.816  105.287 1.00 119.76 ? 1248 VAL B O   1 
ATOM   21889 C  CB  . VAL C 1 1248 ? 73.973  -5.152  103.793 1.00 105.16 ? 1248 VAL B CB  1 
ATOM   21890 C  CG1 . VAL C 1 1248 ? 74.793  -3.844  103.723 1.00 104.15 ? 1248 VAL B CG1 1 
ATOM   21891 C  CG2 . VAL C 1 1248 ? 74.888  -6.356  103.936 1.00 108.22 ? 1248 VAL B CG2 1 
ATOM   21892 N  N   . GLU C 1 1249 ? 70.843  -3.939  104.639 1.00 187.44 ? 1249 GLU B N   1 
ATOM   21893 C  CA  . GLU C 1 1249 ? 70.048  -2.722  104.806 1.00 188.44 ? 1249 GLU B CA  1 
ATOM   21894 C  C   . GLU C 1 1249 ? 69.910  -2.414  106.294 1.00 190.88 ? 1249 GLU B C   1 
ATOM   21895 O  O   . GLU C 1 1249 ? 70.079  -1.273  106.723 1.00 190.35 ? 1249 GLU B O   1 
ATOM   21896 C  CB  . GLU C 1 1249 ? 68.681  -2.759  104.093 1.00 192.80 ? 1249 GLU B CB  1 
ATOM   21897 C  CG  . GLU C 1 1249 ? 67.825  -1.484  104.337 1.00 196.19 ? 1249 GLU B CG  1 
ATOM   21898 C  CD  . GLU C 1 1249 ? 66.745  -1.221  103.281 1.00 201.65 ? 1249 GLU B CD  1 
ATOM   21899 O  OE1 . GLU C 1 1249 ? 66.756  -1.892  102.229 1.00 206.57 ? 1249 GLU B OE1 1 
ATOM   21900 O  OE2 . GLU C 1 1249 ? 65.888  -0.332  103.502 1.00 201.21 ? 1249 GLU B OE2 1 
ATOM   21901 N  N   . THR C 1 1250 ? 69.658  -3.442  107.092 1.00 147.99 ? 1250 THR B N   1 
ATOM   21902 C  CA  . THR C 1 1250 ? 69.440  -3.248  108.524 1.00 146.07 ? 1250 THR B CA  1 
ATOM   21903 C  C   . THR C 1 1250 ? 70.693  -2.767  109.262 1.00 138.93 ? 1250 THR B C   1 
ATOM   21904 O  O   . THR C 1 1250 ? 70.670  -1.734  109.938 1.00 134.09 ? 1250 THR B O   1 
ATOM   21905 C  CB  . THR C 1 1250 ? 68.949  -4.547  109.167 1.00 153.36 ? 1250 THR B CB  1 
ATOM   21906 O  OG1 . THR C 1 1250 ? 70.024  -5.495  109.182 1.00 157.71 ? 1250 THR B OG1 1 
ATOM   21907 C  CG2 . THR C 1 1250 ? 67.745  -5.113  108.394 1.00 153.30 ? 1250 THR B CG2 1 
ATOM   21908 N  N   . THR C 1 1251 ? 71.779  -3.526  109.131 1.00 138.28 ? 1251 THR B N   1 
ATOM   21909 C  CA  . THR C 1 1251 ? 73.052  -3.176  109.765 1.00 138.80 ? 1251 THR B CA  1 
ATOM   21910 C  C   . THR C 1 1251 ? 73.523  -1.779  109.398 1.00 136.26 ? 1251 THR B C   1 
ATOM   21911 O  O   . THR C 1 1251 ? 74.299  -1.146  110.120 1.00 137.70 ? 1251 THR B O   1 
ATOM   21912 C  CB  . THR C 1 1251 ? 74.176  -4.177  109.413 1.00 140.25 ? 1251 THR B CB  1 
ATOM   21913 O  OG1 . THR C 1 1251 ? 75.040  -3.600  108.418 1.00 140.52 ? 1251 THR B OG1 1 
ATOM   21914 C  CG2 . THR C 1 1251 ? 73.583  -5.510  108.956 1.00 140.37 ? 1251 THR B CG2 1 
ATOM   21915 N  N   . ALA C 1 1252 ? 73.068  -1.297  108.263 1.00 130.25 ? 1252 ALA B N   1 
ATOM   21916 C  CA  . ALA C 1 1252 ? 73.311  0.082   107.978 1.00 129.97 ? 1252 ALA B CA  1 
ATOM   21917 C  C   . ALA C 1 1252 ? 72.438  0.870   108.935 1.00 131.47 ? 1252 ALA B C   1 
ATOM   21918 O  O   . ALA C 1 1252 ? 72.861  1.872   109.483 1.00 128.99 ? 1252 ALA B O   1 
ATOM   21919 C  CB  . ALA C 1 1252 ? 72.965  0.397   106.549 1.00 129.46 ? 1252 ALA B CB  1 
ATOM   21920 N  N   . TYR C 1 1253 ? 71.218  0.416   109.164 1.00 157.55 ? 1253 TYR B N   1 
ATOM   21921 C  CA  . TYR C 1 1253 ? 70.316  1.213   109.977 1.00 160.62 ? 1253 TYR B CA  1 
ATOM   21922 C  C   . TYR C 1 1253 ? 70.773  1.332   111.423 1.00 162.55 ? 1253 TYR B C   1 
ATOM   21923 O  O   . TYR C 1 1253 ? 70.476  2.331   112.077 1.00 164.80 ? 1253 TYR B O   1 
ATOM   21924 C  CB  . TYR C 1 1253 ? 68.886  0.705   109.870 1.00 164.72 ? 1253 TYR B CB  1 
ATOM   21925 C  CG  . TYR C 1 1253 ? 68.201  1.191   108.611 1.00 165.62 ? 1253 TYR B CG  1 
ATOM   21926 C  CD1 . TYR C 1 1253 ? 67.932  2.548   108.426 1.00 163.92 ? 1253 TYR B CD1 1 
ATOM   21927 C  CD2 . TYR C 1 1253 ? 67.813  0.301   107.603 1.00 166.48 ? 1253 TYR B CD2 1 
ATOM   21928 C  CE1 . TYR C 1 1253 ? 67.298  3.004   107.271 1.00 161.61 ? 1253 TYR B CE1 1 
ATOM   21929 C  CE2 . TYR C 1 1253 ? 67.178  0.754   106.449 1.00 164.83 ? 1253 TYR B CE2 1 
ATOM   21930 C  CZ  . TYR C 1 1253 ? 66.929  2.103   106.293 1.00 162.64 ? 1253 TYR B CZ  1 
ATOM   21931 O  OH  . TYR C 1 1253 ? 66.314  2.558   105.157 1.00 164.04 ? 1253 TYR B OH  1 
ATOM   21932 N  N   . ALA C 1 1254 ? 71.499  0.321   111.908 1.00 171.87 ? 1254 ALA B N   1 
ATOM   21933 C  CA  . ALA C 1 1254 ? 72.121  0.368   113.235 1.00 167.59 ? 1254 ALA B CA  1 
ATOM   21934 C  C   . ALA C 1 1254 ? 73.435  1.116   113.156 1.00 164.53 ? 1254 ALA B C   1 
ATOM   21935 O  O   . ALA C 1 1254 ? 73.699  2.004   113.967 1.00 162.08 ? 1254 ALA B O   1 
ATOM   21936 C  CB  . ALA C 1 1254 ? 72.363  -1.025  113.784 1.00 167.09 ? 1254 ALA B CB  1 
ATOM   21937 N  N   . LEU C 1 1255 ? 74.267  0.750   112.185 1.00 109.97 ? 1255 LEU B N   1 
ATOM   21938 C  CA  . LEU C 1 1255 ? 75.545  1.427   112.016 1.00 112.79 ? 1255 LEU B CA  1 
ATOM   21939 C  C   . LEU C 1 1255 ? 75.346  2.939   111.875 1.00 109.47 ? 1255 LEU B C   1 
ATOM   21940 O  O   . LEU C 1 1255 ? 76.165  3.740   112.306 1.00 106.08 ? 1255 LEU B O   1 
ATOM   21941 C  CB  . LEU C 1 1255 ? 76.331  0.856   110.830 1.00 115.66 ? 1255 LEU B CB  1 
ATOM   21942 C  CG  . LEU C 1 1255 ? 77.551  1.694   110.408 1.00 114.41 ? 1255 LEU B CG  1 
ATOM   21943 C  CD1 . LEU C 1 1255 ? 78.356  2.061   111.606 1.00 115.40 ? 1255 LEU B CD1 1 
ATOM   21944 C  CD2 . LEU C 1 1255 ? 78.440  0.983   109.420 1.00 112.81 ? 1255 LEU B CD2 1 
ATOM   21945 N  N   . LEU C 1 1256 ? 74.235  3.331   111.284 1.00 163.00 ? 1256 LEU B N   1 
ATOM   21946 C  CA  . LEU C 1 1256 ? 73.926  4.737   111.228 1.00 166.59 ? 1256 LEU B CA  1 
ATOM   21947 C  C   . LEU C 1 1256 ? 73.486  5.250   112.615 1.00 171.52 ? 1256 LEU B C   1 
ATOM   21948 O  O   . LEU C 1 1256 ? 73.938  6.323   113.044 1.00 172.54 ? 1256 LEU B O   1 
ATOM   21949 C  CB  . LEU C 1 1256 ? 72.889  5.039   110.133 1.00 167.12 ? 1256 LEU B CB  1 
ATOM   21950 C  CG  . LEU C 1 1256 ? 73.380  5.176   108.685 1.00 165.29 ? 1256 LEU B CG  1 
ATOM   21951 C  CD1 . LEU C 1 1256 ? 72.284  5.784   107.863 1.00 166.69 ? 1256 LEU B CD1 1 
ATOM   21952 C  CD2 . LEU C 1 1256 ? 74.619  6.026   108.600 1.00 160.66 ? 1256 LEU B CD2 1 
ATOM   21953 N  N   . THR C 1 1257 ? 72.644  4.504   113.336 1.00 101.37 ? 1257 THR B N   1 
ATOM   21954 C  CA  . THR C 1 1257 ? 72.179  5.054   114.597 1.00 100.84 ? 1257 THR B CA  1 
ATOM   21955 C  C   . THR C 1 1257 ? 73.445  5.313   115.408 1.00 97.26  ? 1257 THR B C   1 
ATOM   21956 O  O   . THR C 1 1257 ? 73.745  6.476   115.707 1.00 93.80  ? 1257 THR B O   1 
ATOM   21957 C  CB  . THR C 1 1257 ? 71.151  4.161   115.368 1.00 92.72  ? 1257 THR B CB  1 
ATOM   21958 O  OG1 . THR C 1 1257 ? 70.631  3.142   114.513 1.00 93.44  ? 1257 THR B OG1 1 
ATOM   21959 C  CG2 . THR C 1 1257 ? 69.989  5.019   115.891 1.00 92.75  ? 1257 THR B CG2 1 
ATOM   21960 N  N   . SER C 1 1258 ? 74.216  4.244   115.675 1.00 119.60 ? 1258 SER B N   1 
ATOM   21961 C  CA  . SER C 1 1258 ? 75.500  4.304   116.410 1.00 124.14 ? 1258 SER B CA  1 
ATOM   21962 C  C   . SER C 1 1258 ? 76.345  5.525   116.069 1.00 122.26 ? 1258 SER B C   1 
ATOM   21963 O  O   . SER C 1 1258 ? 76.815  6.226   116.969 1.00 121.81 ? 1258 SER B O   1 
ATOM   21964 C  CB  . SER C 1 1258 ? 76.361  3.072   116.129 1.00 125.78 ? 1258 SER B CB  1 
ATOM   21965 O  OG  . SER C 1 1258 ? 76.013  1.979   116.942 1.00 129.53 ? 1258 SER B OG  1 
ATOM   21966 N  N   . LEU C 1 1259 ? 76.543  5.750   114.765 1.00 115.70 ? 1259 LEU B N   1 
ATOM   21967 C  CA  . LEU C 1 1259 ? 77.377  6.843   114.239 1.00 111.15 ? 1259 LEU B CA  1 
ATOM   21968 C  C   . LEU C 1 1259 ? 76.785  8.245   114.426 1.00 110.68 ? 1259 LEU B C   1 
ATOM   21969 O  O   . LEU C 1 1259 ? 77.498  9.246   114.345 1.00 108.97 ? 1259 LEU B O   1 
ATOM   21970 C  CB  . LEU C 1 1259 ? 77.722  6.593   112.773 1.00 104.10 ? 1259 LEU B CB  1 
ATOM   21971 C  CG  . LEU C 1 1259 ? 78.753  5.491   112.528 1.00 100.75 ? 1259 LEU B CG  1 
ATOM   21972 C  CD1 . LEU C 1 1259 ? 78.883  5.192   111.044 1.00 99.91  ? 1259 LEU B CD1 1 
ATOM   21973 C  CD2 . LEU C 1 1259 ? 80.096  5.881   113.081 1.00 98.37  ? 1259 LEU B CD2 1 
ATOM   21974 N  N   . ASN C 1 1260 ? 75.479  8.299   114.662 1.00 127.78 ? 1260 ASN B N   1 
ATOM   21975 C  CA  . ASN C 1 1260 ? 74.850  9.461   115.257 1.00 130.24 ? 1260 ASN B CA  1 
ATOM   21976 C  C   . ASN C 1 1260 ? 75.306  9.630   116.711 1.00 136.14 ? 1260 ASN B C   1 
ATOM   21977 O  O   . ASN C 1 1260 ? 75.731  10.713  117.124 1.00 139.37 ? 1260 ASN B O   1 
ATOM   21978 C  CB  . ASN C 1 1260 ? 73.339  9.297   115.232 1.00 128.80 ? 1260 ASN B CB  1 
ATOM   21979 C  CG  . ASN C 1 1260 ? 72.689  10.126  114.169 1.00 127.89 ? 1260 ASN B CG  1 
ATOM   21980 O  OD1 . ASN C 1 1260 ? 72.677  11.348  114.239 1.00 129.12 ? 1260 ASN B OD1 1 
ATOM   21981 N  ND2 . ASN C 1 1260 ? 72.118  9.470   113.187 1.00 126.11 ? 1260 ASN B ND2 1 
ATOM   21982 N  N   . LEU C 1 1261 ? 75.205  8.555   117.488 1.00 125.98 ? 1261 LEU B N   1 
ATOM   21983 C  CA  . LEU C 1 1261 ? 75.526  8.582   118.915 1.00 124.11 ? 1261 LEU B CA  1 
ATOM   21984 C  C   . LEU C 1 1261 ? 77.038  8.457   119.209 1.00 123.86 ? 1261 LEU B C   1 
ATOM   21985 O  O   . LEU C 1 1261 ? 77.459  8.281   120.358 1.00 125.78 ? 1261 LEU B O   1 
ATOM   21986 C  CB  . LEU C 1 1261 ? 74.723  7.493   119.637 1.00 123.09 ? 1261 LEU B CB  1 
ATOM   21987 C  CG  . LEU C 1 1261 ? 73.202  7.598   119.431 1.00 120.71 ? 1261 LEU B CG  1 
ATOM   21988 C  CD1 . LEU C 1 1261 ? 72.479  6.459   120.124 1.00 124.90 ? 1261 LEU B CD1 1 
ATOM   21989 C  CD2 . LEU C 1 1261 ? 72.684  8.951   119.890 1.00 117.00 ? 1261 LEU B CD2 1 
ATOM   21990 N  N   . LYS C 1 1262 ? 77.847  8.553   118.161 1.00 108.36 ? 1262 LYS B N   1 
ATOM   21991 C  CA  . LYS C 1 1262 ? 79.293  8.711   118.312 1.00 107.14 ? 1262 LYS B CA  1 
ATOM   21992 C  C   . LYS C 1 1262 ? 79.964  7.600   119.115 1.00 106.26 ? 1262 LYS B C   1 
ATOM   21993 O  O   . LYS C 1 1262 ? 81.014  7.787   119.697 1.00 106.68 ? 1262 LYS B O   1 
ATOM   21994 C  CB  . LYS C 1 1262 ? 79.574  10.081  118.916 1.00 111.75 ? 1262 LYS B CB  1 
ATOM   21995 C  CG  . LYS C 1 1262 ? 78.752  11.175  118.206 1.00 118.47 ? 1262 LYS B CG  1 
ATOM   21996 C  CD  . LYS C 1 1262 ? 79.644  12.310  117.655 1.00 125.12 ? 1262 LYS B CD  1 
ATOM   21997 C  CE  . LYS C 1 1262 ? 78.951  13.125  116.566 1.00 127.39 ? 1262 LYS B CE  1 
ATOM   21998 N  NZ  . LYS C 1 1262 ? 78.419  12.246  115.471 1.00 127.46 ? 1262 LYS B NZ  1 
ATOM   21999 N  N   . ASP C 1 1263 ? 79.350  6.431   119.076 1.00 110.63 ? 1263 ASP B N   1 
ATOM   22000 C  CA  . ASP C 1 1263 ? 79.779  5.236   119.777 1.00 114.83 ? 1263 ASP B CA  1 
ATOM   22001 C  C   . ASP C 1 1263 ? 81.049  4.581   119.227 1.00 111.73 ? 1263 ASP B C   1 
ATOM   22002 O  O   . ASP C 1 1263 ? 81.209  3.359   119.227 1.00 117.45 ? 1263 ASP B O   1 
ATOM   22003 C  CB  . ASP C 1 1263 ? 78.633  4.261   119.676 1.00 117.75 ? 1263 ASP B CB  1 
ATOM   22004 C  CG  . ASP C 1 1263 ? 78.623  3.291   120.791 1.00 148.78 ? 1263 ASP B CG  1 
ATOM   22005 O  OD1 . ASP C 1 1263 ? 79.644  2.595   120.970 1.00 149.35 ? 1263 ASP B OD1 1 
ATOM   22006 O  OD2 . ASP C 1 1263 ? 77.593  3.240   121.494 1.00 148.75 ? 1263 ASP B OD2 1 
ATOM   22007 N  N   . ILE C 1 1264 ? 81.951  5.422   118.768 1.00 91.62  ? 1264 ILE B N   1 
ATOM   22008 C  CA  . ILE C 1 1264 ? 83.161  5.007   118.070 1.00 92.73  ? 1264 ILE B CA  1 
ATOM   22009 C  C   . ILE C 1 1264 ? 83.729  3.585   118.256 1.00 91.89  ? 1264 ILE B C   1 
ATOM   22010 O  O   . ILE C 1 1264 ? 84.437  3.094   117.390 1.00 91.59  ? 1264 ILE B O   1 
ATOM   22011 C  CB  . ILE C 1 1264 ? 84.249  6.068   118.294 1.00 102.98 ? 1264 ILE B CB  1 
ATOM   22012 C  CG1 . ILE C 1 1264 ? 83.636  7.427   117.943 1.00 99.17  ? 1264 ILE B CG1 1 
ATOM   22013 C  CG2 . ILE C 1 1264 ? 85.562  5.716   117.546 1.00 91.30  ? 1264 ILE B CG2 1 
ATOM   22014 C  CD1 . ILE C 1 1264 ? 84.411  8.610   118.354 1.00 98.23  ? 1264 ILE B CD1 1 
ATOM   22015 N  N   . ASN C 1 1265 ? 83.457  2.900   119.347 1.00 107.80 ? 1265 ASN B N   1 
ATOM   22016 C  CA  . ASN C 1 1265 ? 84.187  1.651   119.484 1.00 116.02 ? 1265 ASN B CA  1 
ATOM   22017 C  C   . ASN C 1 1265 ? 83.305  0.482   119.155 1.00 117.22 ? 1265 ASN B C   1 
ATOM   22018 O  O   . ASN C 1 1265 ? 83.776  -0.548  118.681 1.00 118.48 ? 1265 ASN B O   1 
ATOM   22019 C  CB  . ASN C 1 1265 ? 84.878  1.505   120.859 1.00 123.54 ? 1265 ASN B CB  1 
ATOM   22020 C  CG  . ASN C 1 1265 ? 86.425  1.596   120.776 1.00 128.66 ? 1265 ASN B CG  1 
ATOM   22021 O  OD1 . ASN C 1 1265 ? 87.032  1.161   119.801 1.00 130.42 ? 1265 ASN B OD1 1 
ATOM   22022 N  ND2 . ASN C 1 1265 ? 87.051  2.151   121.812 1.00 130.88 ? 1265 ASN B ND2 1 
ATOM   22023 N  N   . TYR C 1 1266 ? 82.010  0.673   119.381 1.00 116.82 ? 1266 TYR B N   1 
ATOM   22024 C  CA  . TYR C 1 1266 ? 81.008  -0.337  119.036 1.00 116.66 ? 1266 TYR B CA  1 
ATOM   22025 C  C   . TYR C 1 1266 ? 81.052  -0.581  117.556 1.00 116.61 ? 1266 TYR B C   1 
ATOM   22026 O  O   . TYR C 1 1266 ? 80.746  -1.696  117.100 1.00 120.99 ? 1266 TYR B O   1 
ATOM   22027 C  CB  . TYR C 1 1266 ? 79.588  0.158   119.307 1.00 111.61 ? 1266 TYR B CB  1 
ATOM   22028 C  CG  . TYR C 1 1266 ? 78.550  -0.930  119.277 1.00 109.08 ? 1266 TYR B CG  1 
ATOM   22029 C  CD1 . TYR C 1 1266 ? 78.902  -2.224  119.542 1.00 111.91 ? 1266 TYR B CD1 1 
ATOM   22030 C  CD2 . TYR C 1 1266 ? 77.215  -0.659  119.016 1.00 105.72 ? 1266 TYR B CD2 1 
ATOM   22031 C  CE1 . TYR C 1 1266 ? 77.956  -3.232  119.556 1.00 115.99 ? 1266 TYR B CE1 1 
ATOM   22032 C  CE2 . TYR C 1 1266 ? 76.255  -1.680  119.025 1.00 107.70 ? 1266 TYR B CE2 1 
ATOM   22033 C  CZ  . TYR C 1 1266 ? 76.640  -2.968  119.296 1.00 113.24 ? 1266 TYR B CZ  1 
ATOM   22034 O  OH  . TYR C 1 1266 ? 75.742  -4.020  119.328 1.00 115.51 ? 1266 TYR B OH  1 
ATOM   22035 N  N   . VAL C 1 1267 ? 81.423  0.483   116.825 1.00 114.61 ? 1267 VAL B N   1 
ATOM   22036 C  CA  . VAL C 1 1267 ? 81.186  0.635   115.384 1.00 114.69 ? 1267 VAL B CA  1 
ATOM   22037 C  C   . VAL C 1 1267 ? 82.255  -0.022  114.482 1.00 105.00 ? 1267 VAL B C   1 
ATOM   22038 O  O   . VAL C 1 1267 ? 81.918  -0.681  113.507 1.00 103.63 ? 1267 VAL B O   1 
ATOM   22039 C  CB  . VAL C 1 1267 ? 80.946  2.145   115.038 1.00 109.79 ? 1267 VAL B CB  1 
ATOM   22040 C  CG1 . VAL C 1 1267 ? 81.444  2.450   113.673 1.00 106.43 ? 1267 VAL B CG1 1 
ATOM   22041 C  CG2 . VAL C 1 1267 ? 79.474  2.530   115.197 1.00 107.93 ? 1267 VAL B CG2 1 
ATOM   22042 N  N   . ASN C 1 1268 ? 83.519  0.086   114.885 1.00 117.94 ? 1268 ASN B N   1 
ATOM   22043 C  CA  . ASN C 1 1268 ? 84.696  -0.445  114.168 1.00 125.76 ? 1268 ASN B CA  1 
ATOM   22044 C  C   . ASN C 1 1268 ? 84.722  -1.848  113.522 1.00 128.51 ? 1268 ASN B C   1 
ATOM   22045 O  O   . ASN C 1 1268 ? 85.610  -2.143  112.732 1.00 131.65 ? 1268 ASN B O   1 
ATOM   22046 C  CB  . ASN C 1 1268 ? 85.899  -0.361  115.101 1.00 133.56 ? 1268 ASN B CB  1 
ATOM   22047 C  CG  . ASN C 1 1268 ? 86.087  1.030   115.677 1.00 138.74 ? 1268 ASN B CG  1 
ATOM   22048 O  OD1 . ASN C 1 1268 ? 86.127  2.012   114.940 1.00 137.57 ? 1268 ASN B OD1 1 
ATOM   22049 N  ND2 . ASN C 1 1268 ? 86.217  1.120   116.995 1.00 143.24 ? 1268 ASN B ND2 1 
ATOM   22050 N  N   . PRO C 1 1269 ? 83.829  -2.744  113.937 1.00 123.65 ? 1269 PRO B N   1 
ATOM   22051 C  CA  . PRO C 1 1269 ? 83.698  -4.090  113.374 1.00 122.65 ? 1269 PRO B CA  1 
ATOM   22052 C  C   . PRO C 1 1269 ? 82.289  -4.290  112.887 1.00 117.47 ? 1269 PRO B C   1 
ATOM   22053 O  O   . PRO C 1 1269 ? 81.835  -5.423  112.686 1.00 116.06 ? 1269 PRO B O   1 
ATOM   22054 C  CB  . PRO C 1 1269 ? 83.918  -4.992  114.589 1.00 130.34 ? 1269 PRO B CB  1 
ATOM   22055 C  CG  . PRO C 1 1269 ? 84.078  -4.031  115.809 1.00 132.56 ? 1269 PRO B CG  1 
ATOM   22056 C  CD  . PRO C 1 1269 ? 83.458  -2.747  115.352 1.00 127.93 ? 1269 PRO B CD  1 
ATOM   22057 N  N   . VAL C 1 1270 ? 81.587  -3.170  112.778 1.00 118.52 ? 1270 VAL B N   1 
ATOM   22058 C  CA  . VAL C 1 1270 ? 80.406  -3.099  111.952 1.00 113.46 ? 1270 VAL B CA  1 
ATOM   22059 C  C   . VAL C 1 1270 ? 80.922  -2.696  110.583 1.00 106.58 ? 1270 VAL B C   1 
ATOM   22060 O  O   . VAL C 1 1270 ? 80.721  -3.401  109.593 1.00 108.04 ? 1270 VAL B O   1 
ATOM   22061 C  CB  . VAL C 1 1270 ? 79.343  -2.102  112.489 1.00 111.25 ? 1270 VAL B CB  1 
ATOM   22062 C  CG1 . VAL C 1 1270 ? 78.542  -1.525  111.358 1.00 105.90 ? 1270 VAL B CG1 1 
ATOM   22063 C  CG2 . VAL C 1 1270 ? 78.401  -2.810  113.449 1.00 115.25 ? 1270 VAL B CG2 1 
ATOM   22064 N  N   . ILE C 1 1271 ? 81.640  -1.551  110.494 1.00 102.07 ? 1271 ILE B N   1 
ATOM   22065 C  CA  . ILE C 1 1271 ? 82.199  -1.095  109.213 1.00 97.94  ? 1271 ILE B CA  1 
ATOM   22066 C  C   . ILE C 1 1271 ? 83.438  -1.880  108.723 1.00 98.02  ? 1271 ILE B C   1 
ATOM   22067 O  O   . ILE C 1 1271 ? 84.028  -1.496  107.710 1.00 98.66  ? 1271 ILE B O   1 
ATOM   22068 C  CB  . ILE C 1 1271 ? 82.478  0.434   109.205 1.00 97.82  ? 1271 ILE B CB  1 
ATOM   22069 C  CG1 . ILE C 1 1271 ? 83.775  0.771   109.927 1.00 97.86  ? 1271 ILE B CG1 1 
ATOM   22070 C  CG2 . ILE C 1 1271 ? 81.312  1.189   109.820 1.00 97.72  ? 1271 ILE B CG2 1 
ATOM   22071 C  CD1 . ILE C 1 1271 ? 85.016  0.470   109.116 1.00 98.13  ? 1271 ILE B CD1 1 
ATOM   22072 N  N   . LYS C 1 1272 ? 83.872  -2.944  109.374 1.00 126.48 ? 1272 LYS B N   1 
ATOM   22073 C  CA  . LYS C 1 1272 ? 84.943  -3.719  108.772 1.00 134.25 ? 1272 LYS B CA  1 
ATOM   22074 C  C   . LYS C 1 1272 ? 84.241  -4.678  107.838 1.00 138.32 ? 1272 LYS B C   1 
ATOM   22075 O  O   . LYS C 1 1272 ? 84.832  -5.280  106.941 1.00 140.75 ? 1272 LYS B O   1 
ATOM   22076 C  CB  . LYS C 1 1272 ? 85.747  -4.519  109.822 1.00 140.46 ? 1272 LYS B CB  1 
ATOM   22077 C  CG  . LYS C 1 1272 ? 86.322  -5.849  109.320 1.00 141.65 ? 1272 LYS B CG  1 
ATOM   22078 C  CD  . LYS C 1 1272 ? 87.816  -5.749  109.041 1.00 141.40 ? 1272 LYS B CD  1 
ATOM   22079 C  CE  . LYS C 1 1272 ? 88.517  -7.095  109.176 1.00 147.57 ? 1272 LYS B CE  1 
ATOM   22080 N  NZ  . LYS C 1 1272 ? 89.997  -6.980  109.044 1.00 149.90 ? 1272 LYS B NZ  1 
ATOM   22081 N  N   . TRP C 1 1273 ? 82.943  -4.789  108.087 1.00 145.70 ? 1273 TRP B N   1 
ATOM   22082 C  CA  . TRP C 1 1273 ? 82.102  -5.739  107.414 1.00 143.22 ? 1273 TRP B CA  1 
ATOM   22083 C  C   . TRP C 1 1273 ? 81.226  -5.144  106.320 1.00 136.90 ? 1273 TRP B C   1 
ATOM   22084 O  O   . TRP C 1 1273 ? 80.846  -5.823  105.355 1.00 139.19 ? 1273 TRP B O   1 
ATOM   22085 C  CB  . TRP C 1 1273 ? 81.307  -6.433  108.487 1.00 145.26 ? 1273 TRP B CB  1 
ATOM   22086 C  CG  . TRP C 1 1273 ? 80.158  -7.253  108.041 1.00 146.38 ? 1273 TRP B CG  1 
ATOM   22087 C  CD1 . TRP C 1 1273 ? 80.165  -8.599  107.752 1.00 151.23 ? 1273 TRP B CD1 1 
ATOM   22088 C  CD2 . TRP C 1 1273 ? 78.796  -6.808  107.896 1.00 144.94 ? 1273 TRP B CD2 1 
ATOM   22089 N  NE1 . TRP C 1 1273 ? 78.896  -9.004  107.425 1.00 151.51 ? 1273 TRP B NE1 1 
ATOM   22090 C  CE2 . TRP C 1 1273 ? 78.041  -7.934  107.507 1.00 147.40 ? 1273 TRP B CE2 1 
ATOM   22091 C  CE3 . TRP C 1 1273 ? 78.152  -5.571  108.059 1.00 143.38 ? 1273 TRP B CE3 1 
ATOM   22092 C  CZ2 . TRP C 1 1273 ? 76.656  -7.853  107.260 1.00 148.41 ? 1273 TRP B CZ2 1 
ATOM   22093 C  CZ3 . TRP C 1 1273 ? 76.797  -5.501  107.832 1.00 144.14 ? 1273 TRP B CZ3 1 
ATOM   22094 C  CH2 . TRP C 1 1273 ? 76.057  -6.637  107.433 1.00 146.47 ? 1273 TRP B CH2 1 
ATOM   22095 N  N   . LEU C 1 1274 ? 80.935  -3.901  106.433 1.00 106.37 ? 1274 LEU B N   1 
ATOM   22096 C  CA  . LEU C 1 1274 ? 80.214  -3.278  105.366 1.00 109.23 ? 1274 LEU B CA  1 
ATOM   22097 C  C   . LEU C 1 1274 ? 81.176  -3.134  104.157 1.00 104.84 ? 1274 LEU B C   1 
ATOM   22098 O  O   . LEU C 1 1274 ? 80.811  -3.386  103.000 1.00 107.58 ? 1274 LEU B O   1 
ATOM   22099 C  CB  . LEU C 1 1274 ? 79.683  -1.911  105.784 1.00 102.39 ? 1274 LEU B CB  1 
ATOM   22100 C  CG  . LEU C 1 1274 ? 78.297  -1.933  106.384 1.00 106.97 ? 1274 LEU B CG  1 
ATOM   22101 C  CD1 . LEU C 1 1274 ? 77.584  -0.601  106.180 1.00 105.88 ? 1274 LEU B CD1 1 
ATOM   22102 C  CD2 . LEU C 1 1274 ? 77.499  -3.082  105.793 1.00 109.06 ? 1274 LEU B CD2 1 
ATOM   22103 N  N   . SER C 1 1275 ? 82.394  -2.717  104.457 1.00 96.66  ? 1275 SER B N   1 
ATOM   22104 C  CA  . SER C 1 1275 ? 83.446  -2.549  103.471 1.00 101.31 ? 1275 SER B CA  1 
ATOM   22105 C  C   . SER C 1 1275 ? 83.604  -3.816  102.635 1.00 103.38 ? 1275 SER B C   1 
ATOM   22106 O  O   . SER C 1 1275 ? 83.725  -3.776  101.415 1.00 102.20 ? 1275 SER B O   1 
ATOM   22107 C  CB  . SER C 1 1275 ? 84.741  -2.205  104.173 1.00 108.99 ? 1275 SER B CB  1 
ATOM   22108 O  OG  . SER C 1 1275 ? 85.734  -1.796  103.256 1.00 95.06  ? 1275 SER B OG  1 
ATOM   22109 N  N   . GLU C 1 1276 ? 83.635  -4.910  103.327 1.00 132.94 ? 1276 GLU B N   1 
ATOM   22110 C  CA  . GLU C 1 1276 ? 83.837  -6.189  102.689 1.00 140.55 ? 1276 GLU B CA  1 
ATOM   22111 C  C   . GLU C 1 1276 ? 82.592  -6.664  101.892 1.00 142.07 ? 1276 GLU B C   1 
ATOM   22112 O  O   . GLU C 1 1276 ? 82.712  -7.305  100.845 1.00 146.35 ? 1276 GLU B O   1 
ATOM   22113 C  CB  . GLU C 1 1276 ? 84.420  -7.140  103.737 1.00 147.66 ? 1276 GLU B CB  1 
ATOM   22114 C  CG  . GLU C 1 1276 ? 85.671  -6.517  104.321 1.00 149.32 ? 1276 GLU B CG  1 
ATOM   22115 C  CD  . GLU C 1 1276 ? 86.520  -7.436  105.164 1.00 150.87 ? 1276 GLU B CD  1 
ATOM   22116 O  OE1 . GLU C 1 1276 ? 85.954  -8.398  105.719 1.00 151.55 ? 1276 GLU B OE1 1 
ATOM   22117 O  OE2 . GLU C 1 1276 ? 87.734  -7.202  105.285 1.00 151.24 ? 1276 GLU B OE2 1 
ATOM   22118 N  N   . GLU C 1 1277 ? 81.424  -6.320  102.394 1.00 173.45 ? 1277 GLU B N   1 
ATOM   22119 C  CA  . GLU C 1 1277 ? 80.124  -6.649  101.780 1.00 174.98 ? 1277 GLU B CA  1 
ATOM   22120 C  C   . GLU C 1 1277 ? 79.990  -5.985  100.417 1.00 172.93 ? 1277 GLU B C   1 
ATOM   22121 O  O   . GLU C 1 1277 ? 79.642  -6.599  99.414  1.00 174.58 ? 1277 GLU B O   1 
ATOM   22122 C  CB  . GLU C 1 1277 ? 78.977  -6.220  102.694 1.00 174.31 ? 1277 GLU B CB  1 
ATOM   22123 C  CG  . GLU C 1 1277 ? 77.824  -7.184  102.655 1.00 176.07 ? 1277 GLU B CG  1 
ATOM   22124 C  CD  . GLU C 1 1277 ? 78.200  -8.561  103.152 1.00 180.26 ? 1277 GLU B CD  1 
ATOM   22125 O  OE1 . GLU C 1 1277 ? 77.306  -9.435  103.202 1.00 183.41 ? 1277 GLU B OE1 1 
ATOM   22126 O  OE2 . GLU C 1 1277 ? 79.388  -8.772  103.493 1.00 181.50 ? 1277 GLU B OE2 1 
ATOM   22127 N  N   . GLN C 1 1278 ? 80.268  -4.686  100.436 1.00 121.91 ? 1278 GLN B N   1 
ATOM   22128 C  CA  . GLN C 1 1278 ? 80.177  -3.875  99.228  1.00 125.59 ? 1278 GLN B CA  1 
ATOM   22129 C  C   . GLN C 1 1278 ? 80.826  -4.615  98.027  1.00 131.98 ? 1278 GLN B C   1 
ATOM   22130 O  O   . GLN C 1 1278 ? 81.906  -5.199  98.157  1.00 132.94 ? 1278 GLN B O   1 
ATOM   22131 C  CB  . GLN C 1 1278 ? 80.766  -2.483  99.483  1.00 130.22 ? 1278 GLN B CB  1 
ATOM   22132 C  CG  . GLN C 1 1278 ? 79.939  -1.569  100.387 1.00 160.00 ? 1278 GLN B CG  1 
ATOM   22133 C  CD  . GLN C 1 1278 ? 78.424  -1.837  100.432 1.00 114.54 ? 1278 GLN B CD  1 
ATOM   22134 O  OE1 . GLN C 1 1278 ? 77.613  -0.915  100.351 1.00 111.72 ? 1278 GLN B OE1 1 
ATOM   22135 N  NE2 . GLN C 1 1278 ? 77.831  -3.013  100.545 1.00 115.70 ? 1278 GLN B NE2 1 
ATOM   22136 N  N   . ARG C 1 1279 ? 80.143  -4.595  96.877  1.00 190.65 ? 1279 ARG B N   1 
ATOM   22137 C  CA  . ARG C 1 1279 ? 80.612  -5.323  95.702  1.00 192.00 ? 1279 ARG B CA  1 
ATOM   22138 C  C   . ARG C 1 1279 ? 81.283  -4.439  94.670  1.00 186.72 ? 1279 ARG B C   1 
ATOM   22139 O  O   . ARG C 1 1279 ? 80.760  -3.391  94.284  1.00 184.04 ? 1279 ARG B O   1 
ATOM   22140 C  CB  . ARG C 1 1279 ? 79.509  -6.178  95.084  1.00 198.98 ? 1279 ARG B CB  1 
ATOM   22141 C  CG  . ARG C 1 1279 ? 79.169  -7.400  95.965  1.00 204.14 ? 1279 ARG B CG  1 
ATOM   22142 C  CD  . ARG C 1 1279 ? 78.558  -8.541  95.188  1.00 212.92 ? 1279 ARG B CD  1 
ATOM   22143 N  NE  . ARG C 1 1279 ? 78.805  -8.383  93.765  1.00 217.97 ? 1279 ARG B NE  1 
ATOM   22144 C  CZ  . ARG C 1 1279 ? 78.450  -9.274  92.854  1.00 223.86 ? 1279 ARG B CZ  1 
ATOM   22145 N  NH1 . ARG C 1 1279 ? 77.850  -10.395 93.236  1.00 225.01 ? 1279 ARG B NH1 1 
ATOM   22146 N  NH2 . ARG C 1 1279 ? 78.717  -9.051  91.576  1.00 227.56 ? 1279 ARG B NH2 1 
ATOM   22147 N  N   . TYR C 1 1280 ? 82.456  -4.891  94.236  1.00 159.58 ? 1280 TYR B N   1 
ATOM   22148 C  CA  . TYR C 1 1280 ? 83.325  -4.104  93.380  1.00 160.26 ? 1280 TYR B CA  1 
ATOM   22149 C  C   . TYR C 1 1280 ? 82.519  -3.026  92.723  1.00 140.40 ? 1280 TYR B C   1 
ATOM   22150 O  O   . TYR C 1 1280 ? 81.581  -3.303  91.998  1.00 140.27 ? 1280 TYR B O   1 
ATOM   22151 C  CB  . TYR C 1 1280 ? 83.951  -4.986  92.314  1.00 163.63 ? 1280 TYR B CB  1 
ATOM   22152 C  CG  . TYR C 1 1280 ? 84.653  -4.213  91.225  1.00 162.66 ? 1280 TYR B CG  1 
ATOM   22153 C  CD1 . TYR C 1 1280 ? 84.905  -4.806  89.994  1.00 170.60 ? 1280 TYR B CD1 1 
ATOM   22154 C  CD2 . TYR C 1 1280 ? 85.059  -2.891  91.416  1.00 156.37 ? 1280 TYR B CD2 1 
ATOM   22155 C  CE1 . TYR C 1 1280 ? 85.546  -4.117  88.969  1.00 172.24 ? 1280 TYR B CE1 1 
ATOM   22156 C  CE2 . TYR C 1 1280 ? 85.704  -2.186  90.392  1.00 160.37 ? 1280 TYR B CE2 1 
ATOM   22157 C  CZ  . TYR C 1 1280 ? 85.945  -2.817  89.162  1.00 167.93 ? 1280 TYR B CZ  1 
ATOM   22158 O  OH  . TYR C 1 1280 ? 86.576  -2.178  88.115  1.00 171.18 ? 1280 TYR B OH  1 
ATOM   22159 N  N   . GLY C 1 1281 ? 82.875  -1.791  93.010  1.00 97.90  ? 1281 GLY B N   1 
ATOM   22160 C  CA  . GLY C 1 1281 ? 82.195  -0.665  92.426  1.00 97.73  ? 1281 GLY B CA  1 
ATOM   22161 C  C   . GLY C 1 1281 ? 80.998  -0.054  93.148  1.00 95.66  ? 1281 GLY B C   1 
ATOM   22162 O  O   . GLY C 1 1281 ? 80.657  1.093   92.876  1.00 95.78  ? 1281 GLY B O   1 
ATOM   22163 N  N   . GLY C 1 1282 ? 80.339  -0.779  94.043  1.00 101.57 ? 1282 GLY B N   1 
ATOM   22164 C  CA  . GLY C 1 1282 ? 79.134  -0.244  94.663  1.00 106.48 ? 1282 GLY B CA  1 
ATOM   22165 C  C   . GLY C 1 1282 ? 78.368  -1.269  95.482  1.00 120.55 ? 1282 GLY B C   1 
ATOM   22166 O  O   . GLY C 1 1282 ? 78.670  -2.475  95.450  1.00 122.46 ? 1282 GLY B O   1 
ATOM   22167 N  N   . GLY C 1 1283 ? 77.353  -0.794  96.202  1.00 141.87 ? 1283 GLY B N   1 
ATOM   22168 C  CA  . GLY C 1 1283 ? 76.758  -1.556  97.295  1.00 151.78 ? 1283 GLY B CA  1 
ATOM   22169 C  C   . GLY C 1 1283 ? 76.021  -2.857  97.020  1.00 155.51 ? 1283 GLY B C   1 
ATOM   22170 O  O   . GLY C 1 1283 ? 75.039  -3.154  97.689  1.00 152.23 ? 1283 GLY B O   1 
ATOM   22171 N  N   . PHE C 1 1284 ? 76.521  -3.652  96.082  1.00 170.07 ? 1284 PHE B N   1 
ATOM   22172 C  CA  . PHE C 1 1284 ? 75.755  -4.740  95.470  1.00 184.03 ? 1284 PHE B CA  1 
ATOM   22173 C  C   . PHE C 1 1284 ? 74.255  -4.802  95.768  1.00 175.07 ? 1284 PHE B C   1 
ATOM   22174 O  O   . PHE C 1 1284 ? 73.438  -4.327  94.978  1.00 178.91 ? 1284 PHE B O   1 
ATOM   22175 C  CB  . PHE C 1 1284 ? 76.376  -6.107  95.722  1.00 208.59 ? 1284 PHE B CB  1 
ATOM   22176 C  CG  . PHE C 1 1284 ? 75.976  -7.137  94.697  1.00 240.49 ? 1284 PHE B CG  1 
ATOM   22177 C  CD1 . PHE C 1 1284 ? 76.143  -6.881  93.343  1.00 256.49 ? 1284 PHE B CD1 1 
ATOM   22178 C  CD2 . PHE C 1 1284 ? 75.442  -8.354  95.080  1.00 256.53 ? 1284 PHE B CD2 1 
ATOM   22179 C  CE1 . PHE C 1 1284 ? 75.779  -7.816  92.395  1.00 273.98 ? 1284 PHE B CE1 1 
ATOM   22180 C  CE2 . PHE C 1 1284 ? 75.079  -9.295  94.140  1.00 272.17 ? 1284 PHE B CE2 1 
ATOM   22181 C  CZ  . PHE C 1 1284 ? 75.246  -9.025  92.792  1.00 283.43 ? 1284 PHE B CZ  1 
ATOM   22182 N  N   . TYR C 1 1285 ? 73.884  -5.407  96.888  1.00 178.51 ? 1285 TYR B N   1 
ATOM   22183 C  CA  . TYR C 1 1285 ? 72.475  -5.739  97.113  1.00 169.17 ? 1285 TYR B CA  1 
ATOM   22184 C  C   . TYR C 1 1285 ? 71.525  -4.541  96.940  1.00 163.33 ? 1285 TYR B C   1 
ATOM   22185 O  O   . TYR C 1 1285 ? 71.695  -3.525  97.611  1.00 164.56 ? 1285 TYR B O   1 
ATOM   22186 C  CB  . TYR C 1 1285 ? 72.290  -6.397  98.493  1.00 164.20 ? 1285 TYR B CB  1 
ATOM   22187 C  CG  . TYR C 1 1285 ? 73.243  -7.542  98.734  1.00 163.86 ? 1285 TYR B CG  1 
ATOM   22188 C  CD1 . TYR C 1 1285 ? 73.781  -8.251  97.675  1.00 166.14 ? 1285 TYR B CD1 1 
ATOM   22189 C  CD2 . TYR C 1 1285 ? 73.607  -7.909  100.011 1.00 161.24 ? 1285 TYR B CD2 1 
ATOM   22190 C  CE1 . TYR C 1 1285 ? 74.656  -9.292  97.883  1.00 166.73 ? 1285 TYR B CE1 1 
ATOM   22191 C  CE2 . TYR C 1 1285 ? 74.480  -8.947  100.231 1.00 161.25 ? 1285 TYR B CE2 1 
ATOM   22192 C  CZ  . TYR C 1 1285 ? 75.002  -9.636  99.165  1.00 164.21 ? 1285 TYR B CZ  1 
ATOM   22193 O  OH  . TYR C 1 1285 ? 75.867  -10.673 99.381  1.00 167.10 ? 1285 TYR B OH  1 
ATOM   22194 N  N   . SER C 1 1286 ? 70.556  -4.656  96.028  1.00 155.82 ? 1286 SER B N   1 
ATOM   22195 C  CA  . SER C 1 1286 ? 69.442  -3.702  95.937  1.00 148.51 ? 1286 SER B CA  1 
ATOM   22196 C  C   . SER C 1 1286 ? 69.792  -2.204  96.107  1.00 141.81 ? 1286 SER B C   1 
ATOM   22197 O  O   . SER C 1 1286 ? 70.934  -1.782  95.903  1.00 140.49 ? 1286 SER B O   1 
ATOM   22198 C  CB  . SER C 1 1286 ? 68.311  -4.115  96.899  1.00 147.77 ? 1286 SER B CB  1 
ATOM   22199 O  OG  . SER C 1 1286 ? 67.161  -3.272  96.801  1.00 144.99 ? 1286 SER B OG  1 
ATOM   22200 N  N   . THR C 1 1287 ? 68.790  -1.409  96.480  1.00 173.57 ? 1287 THR B N   1 
ATOM   22201 C  CA  . THR C 1 1287 ? 68.938  0.040   96.576  1.00 175.50 ? 1287 THR B CA  1 
ATOM   22202 C  C   . THR C 1 1287 ? 68.907  0.531   98.018  1.00 181.12 ? 1287 THR B C   1 
ATOM   22203 O  O   . THR C 1 1287 ? 69.931  0.958   98.553  1.00 181.55 ? 1287 THR B O   1 
ATOM   22204 C  CB  . THR C 1 1287 ? 67.837  0.774   95.779  1.00 172.92 ? 1287 THR B CB  1 
ATOM   22205 O  OG1 . THR C 1 1287 ? 66.540  0.384   96.253  1.00 172.22 ? 1287 THR B OG1 1 
ATOM   22206 C  CG2 . THR C 1 1287 ? 67.947  0.445   94.309  1.00 175.63 ? 1287 THR B CG2 1 
ATOM   22207 N  N   . GLN C 1 1288 ? 67.730  0.451   98.640  1.00 212.89 ? 1288 GLN B N   1 
ATOM   22208 C  CA  . GLN C 1 1288 ? 67.484  1.047   99.958  1.00 213.00 ? 1288 GLN B CA  1 
ATOM   22209 C  C   . GLN C 1 1288 ? 68.638  0.889   100.931 1.00 214.61 ? 1288 GLN B C   1 
ATOM   22210 O  O   . GLN C 1 1288 ? 68.901  1.773   101.745 1.00 216.23 ? 1288 GLN B O   1 
ATOM   22211 C  CB  . GLN C 1 1288 ? 66.212  0.469   100.583 1.00 212.72 ? 1288 GLN B CB  1 
ATOM   22212 C  CG  . GLN C 1 1288 ? 64.958  1.149   100.122 1.00 213.94 ? 1288 GLN B CG  1 
ATOM   22213 C  CD  . GLN C 1 1288 ? 64.957  2.605   100.482 1.00 211.90 ? 1288 GLN B CD  1 
ATOM   22214 O  OE1 . GLN C 1 1288 ? 65.181  2.967   101.633 1.00 212.48 ? 1288 GLN B OE1 1 
ATOM   22215 N  NE2 . GLN C 1 1288 ? 64.711  3.456   99.499  1.00 209.90 ? 1288 GLN B NE2 1 
ATOM   22216 N  N   . ASP C 1 1289 ? 69.312  -0.249  100.851 1.00 156.14 ? 1289 ASP B N   1 
ATOM   22217 C  CA  . ASP C 1 1289 ? 70.473  -0.502  101.681 1.00 155.28 ? 1289 ASP B CA  1 
ATOM   22218 C  C   . ASP C 1 1289 ? 71.650  0.350   101.209 1.00 153.38 ? 1289 ASP B C   1 
ATOM   22219 O  O   . ASP C 1 1289 ? 72.192  1.131   101.989 1.00 154.74 ? 1289 ASP B O   1 
ATOM   22220 C  CB  . ASP C 1 1289 ? 70.828  -1.984  101.633 1.00 157.64 ? 1289 ASP B CB  1 
ATOM   22221 C  CG  . ASP C 1 1289 ? 71.140  -2.446  100.244 1.00 160.45 ? 1289 ASP B CG  1 
ATOM   22222 O  OD1 . ASP C 1 1289 ? 70.192  -2.782  99.511  1.00 161.11 ? 1289 ASP B OD1 1 
ATOM   22223 O  OD2 . ASP C 1 1289 ? 72.336  -2.437  99.879  1.00 162.47 ? 1289 ASP B OD2 1 
ATOM   22224 N  N   . THR C 1 1290 ? 72.002  0.219   99.923  1.00 113.92 ? 1290 THR B N   1 
ATOM   22225 C  CA  . THR C 1 1290 ? 73.218  0.822   99.347  1.00 106.28 ? 1290 THR B CA  1 
ATOM   22226 C  C   . THR C 1 1290 ? 73.272  2.381   99.354  1.00 96.56  ? 1290 THR B C   1 
ATOM   22227 O  O   . THR C 1 1290 ? 74.288  2.968   98.978  1.00 93.44  ? 1290 THR B O   1 
ATOM   22228 C  CB  . THR C 1 1290 ? 73.590  0.201   97.956  1.00 108.19 ? 1290 THR B CB  1 
ATOM   22229 O  OG1 . THR C 1 1290 ? 73.792  -1.199  98.114  1.00 110.47 ? 1290 THR B OG1 1 
ATOM   22230 C  CG2 . THR C 1 1290 ? 74.873  0.781   97.409  1.00 104.06 ? 1290 THR B CG2 1 
ATOM   22231 N  N   . ILE C 1 1291 ? 72.207  3.048   99.810  1.00 150.52 ? 1291 ILE B N   1 
ATOM   22232 C  CA  . ILE C 1 1291 ? 72.256  4.499   100.070 1.00 147.17 ? 1291 ILE B CA  1 
ATOM   22233 C  C   . ILE C 1 1291 ? 72.580  4.783   101.536 1.00 144.05 ? 1291 ILE B C   1 
ATOM   22234 O  O   . ILE C 1 1291 ? 73.438  5.605   101.858 1.00 144.55 ? 1291 ILE B O   1 
ATOM   22235 C  CB  . ILE C 1 1291 ? 70.930  5.198   99.694  1.00 137.09 ? 1291 ILE B CB  1 
ATOM   22236 C  CG1 . ILE C 1 1291 ? 70.862  6.600   100.297 1.00 130.68 ? 1291 ILE B CG1 1 
ATOM   22237 C  CG2 . ILE C 1 1291 ? 69.730  4.373   100.142 1.00 138.31 ? 1291 ILE B CG2 1 
ATOM   22238 C  CD1 . ILE C 1 1291 ? 69.608  7.339   99.887  1.00 128.19 ? 1291 ILE B CD1 1 
ATOM   22239 N  N   . ASN C 1 1292 ? 71.871  4.086   102.413 1.00 107.68 ? 1292 ASN B N   1 
ATOM   22240 C  CA  . ASN C 1 1292 ? 72.208  4.037   103.806 1.00 106.55 ? 1292 ASN B CA  1 
ATOM   22241 C  C   . ASN C 1 1292 ? 73.606  3.481   103.930 1.00 108.29 ? 1292 ASN B C   1 
ATOM   22242 O  O   . ASN C 1 1292 ? 74.478  4.079   104.553 1.00 110.69 ? 1292 ASN B O   1 
ATOM   22243 C  CB  . ASN C 1 1292 ? 71.218  3.132   104.507 1.00 106.88 ? 1292 ASN B CB  1 
ATOM   22244 C  CG  . ASN C 1 1292 ? 69.792  3.575   104.292 1.00 107.23 ? 1292 ASN B CG  1 
ATOM   22245 O  OD1 . ASN C 1 1292 ? 69.478  4.762   104.369 1.00 106.24 ? 1292 ASN B OD1 1 
ATOM   22246 N  ND2 . ASN C 1 1292 ? 68.919  2.624   104.017 1.00 107.72 ? 1292 ASN B ND2 1 
ATOM   22247 N  N   . ALA C 1 1293 ? 73.829  2.340   103.304 1.00 95.06  ? 1293 ALA B N   1 
ATOM   22248 C  CA  . ALA C 1 1293 ? 75.125  1.700   103.396 1.00 98.26  ? 1293 ALA B CA  1 
ATOM   22249 C  C   . ALA C 1 1293 ? 76.210  2.699   103.011 1.00 99.15  ? 1293 ALA B C   1 
ATOM   22250 O  O   . ALA C 1 1293 ? 77.265  2.766   103.640 1.00 99.29  ? 1293 ALA B O   1 
ATOM   22251 C  CB  . ALA C 1 1293 ? 75.184  0.447   102.512 1.00 101.22 ? 1293 ALA B CB  1 
ATOM   22252 N  N   . ILE C 1 1294 ? 75.933  3.502   101.993 1.00 142.71 ? 1294 ILE B N   1 
ATOM   22253 C  CA  . ILE C 1 1294 ? 76.913  4.473   101.517 1.00 142.77 ? 1294 ILE B CA  1 
ATOM   22254 C  C   . ILE C 1 1294 ? 76.968  5.718   102.413 1.00 143.19 ? 1294 ILE B C   1 
ATOM   22255 O  O   . ILE C 1 1294 ? 78.029  6.320   102.587 1.00 144.74 ? 1294 ILE B O   1 
ATOM   22256 C  CB  . ILE C 1 1294 ? 76.689  4.871   100.030 1.00 141.97 ? 1294 ILE B CB  1 
ATOM   22257 C  CG1 . ILE C 1 1294 ? 76.736  3.640   99.129  1.00 142.12 ? 1294 ILE B CG1 1 
ATOM   22258 C  CG2 . ILE C 1 1294 ? 77.750  5.862   99.570  1.00 140.30 ? 1294 ILE B CG2 1 
ATOM   22259 C  CD1 . ILE C 1 1294 ? 78.101  3.196   98.735  1.00 140.59 ? 1294 ILE B CD1 1 
ATOM   22260 N  N   . GLU C 1 1295 ? 75.835  6.103   102.988 1.00 152.72 ? 1295 GLU B N   1 
ATOM   22261 C  CA  . GLU C 1 1295 ? 75.843  7.231   103.906 1.00 151.46 ? 1295 GLU B CA  1 
ATOM   22262 C  C   . GLU C 1 1295 ? 76.712  6.876   105.092 1.00 147.00 ? 1295 GLU B C   1 
ATOM   22263 O  O   . GLU C 1 1295 ? 77.595  7.641   105.474 1.00 146.06 ? 1295 GLU B O   1 
ATOM   22264 C  CB  . GLU C 1 1295 ? 74.431  7.601   104.364 1.00 157.89 ? 1295 GLU B CB  1 
ATOM   22265 C  CG  . GLU C 1 1295 ? 74.407  8.542   105.562 1.00 163.23 ? 1295 GLU B CG  1 
ATOM   22266 C  CD  . GLU C 1 1295 ? 73.067  9.215   105.761 1.00 167.74 ? 1295 GLU B CD  1 
ATOM   22267 O  OE1 . GLU C 1 1295 ? 72.146  9.023   104.929 1.00 166.17 ? 1295 GLU B OE1 1 
ATOM   22268 O  OE2 . GLU C 1 1295 ? 72.944  9.948   106.761 1.00 171.58 ? 1295 GLU B OE2 1 
ATOM   22269 N  N   . GLY C 1 1296 ? 76.460  5.701   105.659 1.00 124.58 ? 1296 GLY B N   1 
ATOM   22270 C  CA  . GLY C 1 1296 ? 77.363  5.155   106.639 1.00 126.91 ? 1296 GLY B CA  1 
ATOM   22271 C  C   . GLY C 1 1296 ? 78.789  5.369   106.157 1.00 125.39 ? 1296 GLY B C   1 
ATOM   22272 O  O   . GLY C 1 1296 ? 79.410  6.401   106.429 1.00 125.04 ? 1296 GLY B O   1 
ATOM   22273 N  N   . LEU C 1 1297 ? 79.289  4.414   105.389 1.00 85.31  ? 1297 LEU B N   1 
ATOM   22274 C  CA  . LEU C 1 1297 ? 80.708  4.358   105.063 1.00 85.92  ? 1297 LEU B CA  1 
ATOM   22275 C  C   . LEU C 1 1297 ? 81.446  5.661   104.783 1.00 89.12  ? 1297 LEU B C   1 
ATOM   22276 O  O   . LEU C 1 1297 ? 82.685  5.700   104.764 1.00 88.79  ? 1297 LEU B O   1 
ATOM   22277 C  CB  . LEU C 1 1297 ? 80.925  3.372   103.943 1.00 83.30  ? 1297 LEU B CB  1 
ATOM   22278 C  CG  . LEU C 1 1297 ? 81.194  2.056   104.666 1.00 85.69  ? 1297 LEU B CG  1 
ATOM   22279 C  CD1 . LEU C 1 1297 ? 80.021  1.107   104.569 1.00 85.88  ? 1297 LEU B CD1 1 
ATOM   22280 C  CD2 . LEU C 1 1297 ? 82.505  1.440   104.190 1.00 87.55  ? 1297 LEU B CD2 1 
ATOM   22281 N  N   . THR C 1 1298 ? 80.674  6.715   104.567 1.00 161.81 ? 1298 THR B N   1 
ATOM   22282 C  CA  . THR C 1 1298 ? 81.208  8.053   104.425 1.00 161.64 ? 1298 THR B CA  1 
ATOM   22283 C  C   . THR C 1 1298 ? 81.164  8.736   105.784 1.00 161.50 ? 1298 THR B C   1 
ATOM   22284 O  O   . THR C 1 1298 ? 82.193  9.172   106.307 1.00 159.64 ? 1298 THR B O   1 
ATOM   22285 C  CB  . THR C 1 1298 ? 80.387  8.901   103.414 1.00 157.99 ? 1298 THR B CB  1 
ATOM   22286 O  OG1 . THR C 1 1298 ? 79.998  8.107   102.279 1.00 158.48 ? 1298 THR B OG1 1 
ATOM   22287 C  CG2 . THR C 1 1298 ? 81.182  10.129  102.963 1.00 156.51 ? 1298 THR B CG2 1 
ATOM   22288 N  N   . GLU C 1 1299 ? 79.963  8.805   106.357 1.00 144.65 ? 1299 GLU B N   1 
ATOM   22289 C  CA  . GLU C 1 1299 ? 79.746  9.544   107.591 1.00 147.53 ? 1299 GLU B CA  1 
ATOM   22290 C  C   . GLU C 1 1299 ? 80.812  9.129   108.561 1.00 148.69 ? 1299 GLU B C   1 
ATOM   22291 O  O   . GLU C 1 1299 ? 81.421  9.957   109.224 1.00 152.54 ? 1299 GLU B O   1 
ATOM   22292 C  CB  . GLU C 1 1299 ? 78.379  9.225   108.184 1.00 149.98 ? 1299 GLU B CB  1 
ATOM   22293 C  CG  . GLU C 1 1299 ? 77.782  10.373  108.952 1.00 156.09 ? 1299 GLU B CG  1 
ATOM   22294 C  CD  . GLU C 1 1299 ? 77.474  11.548  108.047 1.00 159.61 ? 1299 GLU B CD  1 
ATOM   22295 O  OE1 . GLU C 1 1299 ? 76.642  11.401  107.126 1.00 161.65 ? 1299 GLU B OE1 1 
ATOM   22296 O  OE2 . GLU C 1 1299 ? 78.072  12.621  108.248 1.00 159.83 ? 1299 GLU B OE2 1 
ATOM   22297 N  N   . TYR C 1 1300 ? 81.027  7.819   108.596 1.00 92.02  ? 1300 TYR B N   1 
ATOM   22298 C  CA  . TYR C 1 1300 ? 82.022  7.199   109.445 1.00 90.58  ? 1300 TYR B CA  1 
ATOM   22299 C  C   . TYR C 1 1300 ? 83.481  7.542   109.083 1.00 95.48  ? 1300 TYR B C   1 
ATOM   22300 O  O   . TYR C 1 1300 ? 84.309  7.706   109.987 1.00 91.48  ? 1300 TYR B O   1 
ATOM   22301 C  CB  . TYR C 1 1300 ? 81.839  5.670   109.526 1.00 95.18  ? 1300 TYR B CB  1 
ATOM   22302 C  CG  . TYR C 1 1300 ? 83.042  4.956   110.128 1.00 96.28  ? 1300 TYR B CG  1 
ATOM   22303 C  CD1 . TYR C 1 1300 ? 82.998  4.405   111.402 1.00 99.76  ? 1300 TYR B CD1 1 
ATOM   22304 C  CD2 . TYR C 1 1300 ? 84.250  4.871   109.429 1.00 93.63  ? 1300 TYR B CD2 1 
ATOM   22305 C  CE1 . TYR C 1 1300 ? 84.130  3.772   111.950 1.00 101.66 ? 1300 TYR B CE1 1 
ATOM   22306 C  CE2 . TYR C 1 1300 ? 85.372  4.255   109.978 1.00 95.87  ? 1300 TYR B CE2 1 
ATOM   22307 C  CZ  . TYR C 1 1300 ? 85.306  3.706   111.226 1.00 101.40 ? 1300 TYR B CZ  1 
ATOM   22308 O  OH  . TYR C 1 1300 ? 86.420  3.089   111.727 1.00 106.38 ? 1300 TYR B OH  1 
ATOM   22309 N  N   . SER C 1 1301 ? 83.827  7.621   107.797 1.00 99.89  ? 1301 SER B N   1 
ATOM   22310 C  CA  . SER C 1 1301 ? 85.207  7.983   107.450 1.00 102.81 ? 1301 SER B CA  1 
ATOM   22311 C  C   . SER C 1 1301 ? 85.387  9.489   107.690 1.00 98.33  ? 1301 SER B C   1 
ATOM   22312 O  O   . SER C 1 1301 ? 86.503  10.018  107.672 1.00 94.54  ? 1301 SER B O   1 
ATOM   22313 C  CB  . SER C 1 1301 ? 85.600  7.538   106.036 1.00 107.43 ? 1301 SER B CB  1 
ATOM   22314 O  OG  . SER C 1 1301 ? 86.715  6.640   106.050 1.00 111.08 ? 1301 SER B OG  1 
ATOM   22315 N  N   . LEU C 1 1302 ? 84.263  10.154  107.954 1.00 152.19 ? 1302 LEU B N   1 
ATOM   22316 C  CA  . LEU C 1 1302 ? 84.222  11.563  108.328 1.00 156.55 ? 1302 LEU B CA  1 
ATOM   22317 C  C   . LEU C 1 1302 ? 84.426  11.778  109.811 1.00 160.85 ? 1302 LEU B C   1 
ATOM   22318 O  O   . LEU C 1 1302 ? 85.102  12.724  110.214 1.00 167.24 ? 1302 LEU B O   1 
ATOM   22319 C  CB  . LEU C 1 1302 ? 82.863  12.136  107.981 1.00 159.85 ? 1302 LEU B CB  1 
ATOM   22320 C  CG  . LEU C 1 1302 ? 82.889  13.154  106.855 1.00 161.20 ? 1302 LEU B CG  1 
ATOM   22321 C  CD1 . LEU C 1 1302 ? 81.458  13.518  106.544 1.00 160.31 ? 1302 LEU B CD1 1 
ATOM   22322 C  CD2 . LEU C 1 1302 ? 83.745  14.376  107.203 1.00 162.44 ? 1302 LEU B CD2 1 
ATOM   22323 N  N   . LEU C 1 1303 ? 83.817  10.883  110.596 1.00 150.39 ? 1303 LEU B N   1 
ATOM   22324 C  CA  . LEU C 1 1303 ? 83.748  10.905  112.073 1.00 146.95 ? 1303 LEU B CA  1 
ATOM   22325 C  C   . LEU C 1 1303 ? 85.027  10.421  112.821 1.00 143.26 ? 1303 LEU B C   1 
ATOM   22326 O  O   . LEU C 1 1303 ? 85.559  11.160  113.659 1.00 143.88 ? 1303 LEU B O   1 
ATOM   22327 C  CB  . LEU C 1 1303 ? 82.514  10.100  112.498 1.00 147.65 ? 1303 LEU B CB  1 
ATOM   22328 C  CG  . LEU C 1 1303 ? 81.998  9.999   113.920 1.00 147.47 ? 1303 LEU B CG  1 
ATOM   22329 C  CD1 . LEU C 1 1303 ? 82.881  9.048   114.665 1.00 146.30 ? 1303 LEU B CD1 1 
ATOM   22330 C  CD2 . LEU C 1 1303 ? 81.962  11.366  114.558 1.00 150.13 ? 1303 LEU B CD2 1 
ATOM   22331 N  N   . VAL C 1 1304 ? 85.484  9.193   112.532 1.00 100.00 ? 1304 VAL B N   1 
ATOM   22332 C  CA  . VAL C 1 1304 ? 86.860  8.726   112.804 1.00 104.96 ? 1304 VAL B CA  1 
ATOM   22333 C  C   . VAL C 1 1304 ? 87.889  9.652   112.136 1.00 103.79 ? 1304 VAL B C   1 
ATOM   22334 O  O   . VAL C 1 1304 ? 87.510  10.698  111.625 1.00 105.98 ? 1304 VAL B O   1 
ATOM   22335 C  CB  . VAL C 1 1304 ? 87.063  7.354   112.185 1.00 108.61 ? 1304 VAL B CB  1 
ATOM   22336 C  CG1 . VAL C 1 1304 ? 88.431  6.785   112.529 1.00 113.23 ? 1304 VAL B CG1 1 
ATOM   22337 C  CG2 . VAL C 1 1304 ? 85.981  6.442   112.636 1.00 108.37 ? 1304 VAL B CG2 1 
ATOM   22338 N  N   . LYS C 1 1305 ? 89.176  9.300   112.112 1.00 112.09 ? 1305 LYS B N   1 
ATOM   22339 C  CA  . LYS C 1 1305 ? 90.098  10.066  111.264 1.00 113.48 ? 1305 LYS B CA  1 
ATOM   22340 C  C   . LYS C 1 1305 ? 90.888  9.187   110.324 1.00 114.84 ? 1305 LYS B C   1 
ATOM   22341 O  O   . LYS C 1 1305 ? 91.222  8.058   110.653 1.00 114.90 ? 1305 LYS B O   1 
ATOM   22342 C  CB  . LYS C 1 1305 ? 91.035  10.985  112.049 1.00 116.06 ? 1305 LYS B CB  1 
ATOM   22343 C  CG  . LYS C 1 1305 ? 91.378  12.285  111.307 1.00 123.84 ? 1305 LYS B CG  1 
ATOM   22344 C  CD  . LYS C 1 1305 ? 91.412  13.501  112.275 1.00 137.84 ? 1305 LYS B CD  1 
ATOM   22345 C  CE  . LYS C 1 1305 ? 90.151  13.545  113.187 1.00 151.34 ? 1305 LYS B CE  1 
ATOM   22346 N  NZ  . LYS C 1 1305 ? 90.163  14.439  114.407 1.00 153.01 ? 1305 LYS B NZ  1 
ATOM   22347 N  N   . GLN C 1 1306 ? 91.171  9.729   109.147 1.00 147.17 ? 1306 GLN B N   1 
ATOM   22348 C  CA  . GLN C 1 1306 ? 91.822  8.991   108.075 1.00 146.23 ? 1306 GLN B CA  1 
ATOM   22349 C  C   . GLN C 1 1306 ? 93.265  8.637   108.422 1.00 148.19 ? 1306 GLN B C   1 
ATOM   22350 O  O   . GLN C 1 1306 ? 93.936  9.319   109.211 1.00 150.19 ? 1306 GLN B O   1 
ATOM   22351 C  CB  . GLN C 1 1306 ? 91.777  9.785   106.756 1.00 186.42 ? 1306 GLN B CB  1 
ATOM   22352 C  CG  . GLN C 1 1306 ? 90.567  9.518   105.809 1.00 237.37 ? 1306 GLN B CG  1 
ATOM   22353 C  CD  . GLN C 1 1306 ? 90.648  10.297  104.467 1.00 168.80 ? 1306 GLN B CD  1 
ATOM   22354 O  OE1 . GLN C 1 1306 ? 91.527  10.058  103.634 1.00 169.50 ? 1306 GLN B OE1 1 
ATOM   22355 N  NE2 . GLN C 1 1306 ? 89.725  11.226  104.270 1.00 169.78 ? 1306 GLN B NE2 1 
ATOM   22356 N  N   . LEU C 1 1307 ? 93.732  7.563   107.801 1.00 143.23 ? 1307 LEU B N   1 
ATOM   22357 C  CA  . LEU C 1 1307 ? 94.990  6.947   108.166 1.00 143.66 ? 1307 LEU B CA  1 
ATOM   22358 C  C   . LEU C 1 1307 ? 95.895  6.925   106.966 1.00 144.13 ? 1307 LEU B C   1 
ATOM   22359 O  O   . LEU C 1 1307 ? 95.988  5.919   106.260 1.00 144.33 ? 1307 LEU B O   1 
ATOM   22360 C  CB  . LEU C 1 1307 ? 94.736  5.523   108.653 1.00 143.01 ? 1307 LEU B CB  1 
ATOM   22361 C  CG  . LEU C 1 1307 ? 93.288  5.305   109.112 1.00 141.34 ? 1307 LEU B CG  1 
ATOM   22362 C  CD1 . LEU C 1 1307 ? 92.426  4.889   107.896 1.00 144.66 ? 1307 LEU B CD1 1 
ATOM   22363 C  CD2 . LEU C 1 1307 ? 93.164  4.327   110.327 1.00 140.05 ? 1307 LEU B CD2 1 
ATOM   22364 N  N   . ARG C 1 1308 ? 96.566  8.052   106.760 1.00 146.86 ? 1308 ARG B N   1 
ATOM   22365 C  CA  . ARG C 1 1308 ? 97.431  8.253   105.609 1.00 145.11 ? 1308 ARG B CA  1 
ATOM   22366 C  C   . ARG C 1 1308 ? 97.836  6.954   104.962 1.00 140.97 ? 1308 ARG B C   1 
ATOM   22367 O  O   . ARG C 1 1308 ? 98.475  6.109   105.574 1.00 137.91 ? 1308 ARG B O   1 
ATOM   22368 C  CB  . ARG C 1 1308 ? 98.687  9.021   105.999 1.00 145.58 ? 1308 ARG B CB  1 
ATOM   22369 C  CG  . ARG C 1 1308 ? 99.842  8.746   105.070 1.00 148.15 ? 1308 ARG B CG  1 
ATOM   22370 C  CD  . ARG C 1 1308 ? 100.985 9.690   105.310 1.00 151.96 ? 1308 ARG B CD  1 
ATOM   22371 N  NE  . ARG C 1 1308 ? 102.159 9.281   104.552 1.00 156.27 ? 1308 ARG B NE  1 
ATOM   22372 C  CZ  . ARG C 1 1308 ? 102.875 8.196   104.822 1.00 159.44 ? 1308 ARG B CZ  1 
ATOM   22373 N  NH1 . ARG C 1 1308 ? 102.535 7.403   105.832 1.00 156.15 ? 1308 ARG B NH1 1 
ATOM   22374 N  NH2 . ARG C 1 1308 ? 103.933 7.907   104.078 1.00 163.97 ? 1308 ARG B NH2 1 
ATOM   22375 N  N   . LEU C 1 1309 ? 97.458  6.805   103.709 1.00 118.01 ? 1309 LEU B N   1 
ATOM   22376 C  CA  . LEU C 1 1309 ? 97.740  5.592   102.979 1.00 118.81 ? 1309 LEU B CA  1 
ATOM   22377 C  C   . LEU C 1 1309 ? 99.202  5.458   102.631 1.00 116.05 ? 1309 LEU B C   1 
ATOM   22378 O  O   . LEU C 1 1309 ? 99.877  6.453   102.393 1.00 121.82 ? 1309 LEU B O   1 
ATOM   22379 C  CB  . LEU C 1 1309 ? 96.940  5.621   101.693 1.00 117.44 ? 1309 LEU B CB  1 
ATOM   22380 C  CG  . LEU C 1 1309 ? 95.548  5.006   101.735 1.00 121.48 ? 1309 LEU B CG  1 
ATOM   22381 C  CD1 . LEU C 1 1309 ? 94.673  5.554   100.615 1.00 115.42 ? 1309 LEU B CD1 1 
ATOM   22382 C  CD2 . LEU C 1 1309 ? 95.690  3.501   101.632 1.00 118.03 ? 1309 LEU B CD2 1 
ATOM   22383 N  N   . SER C 1 1310 ? 99.688  4.226   102.567 1.00 120.52 ? 1310 SER B N   1 
ATOM   22384 C  CA  . SER C 1 1310 ? 101.049 4.006   102.090 1.00 118.63 ? 1310 SER B CA  1 
ATOM   22385 C  C   . SER C 1 1310 ? 101.485 2.549   101.965 1.00 122.88 ? 1310 SER B C   1 
ATOM   22386 O  O   . SER C 1 1310 ? 102.655 2.242   102.201 1.00 119.66 ? 1310 SER B O   1 
ATOM   22387 C  CB  . SER C 1 1310 ? 102.056 4.772   102.933 1.00 122.00 ? 1310 SER B CB  1 
ATOM   22388 O  OG  . SER C 1 1310 ? 103.359 4.622   102.404 1.00 125.58 ? 1310 SER B OG  1 
ATOM   22389 N  N   . MET C 1 1311 ? 100.549 1.678   101.576 1.00 108.92 ? 1311 MET B N   1 
ATOM   22390 C  CA  . MET C 1 1311 ? 100.816 0.262   101.288 1.00 112.22 ? 1311 MET B CA  1 
ATOM   22391 C  C   . MET C 1 1311 ? 101.926 0.044   100.276 1.00 118.80 ? 1311 MET B C   1 
ATOM   22392 O  O   . MET C 1 1311 ? 102.766 0.909   100.062 1.00 118.79 ? 1311 MET B O   1 
ATOM   22393 C  CB  . MET C 1 1311 ? 99.557  -0.424  100.771 1.00 124.27 ? 1311 MET B CB  1 
ATOM   22394 C  CG  . MET C 1 1311 ? 98.915  -1.392  101.741 1.00 122.03 ? 1311 MET B CG  1 
ATOM   22395 S  SD  . MET C 1 1311 ? 97.173  -1.051  101.984 1.00 115.03 ? 1311 MET B SD  1 
ATOM   22396 C  CE  . MET C 1 1311 ? 97.241  0.562   102.727 1.00 117.30 ? 1311 MET B CE  1 
ATOM   22397 N  N   . ASP C 1 1312 ? 101.927 -1.120  99.653  1.00 126.45 ? 1312 ASP B N   1 
ATOM   22398 C  CA  . ASP C 1 1312 ? 102.974 -1.432  98.710  1.00 125.50 ? 1312 ASP B CA  1 
ATOM   22399 C  C   . ASP C 1 1312 ? 102.604 -2.722  98.036  1.00 128.53 ? 1312 ASP B C   1 
ATOM   22400 O  O   . ASP C 1 1312 ? 103.371 -3.685  98.032  1.00 129.13 ? 1312 ASP B O   1 
ATOM   22401 C  CB  . ASP C 1 1312 ? 104.303 -1.585  99.425  1.00 131.88 ? 1312 ASP B CB  1 
ATOM   22402 C  CG  . ASP C 1 1312 ? 105.470 -1.445  98.499  1.00 140.75 ? 1312 ASP B CG  1 
ATOM   22403 O  OD1 . ASP C 1 1312 ? 105.322 -1.835  97.332  1.00 143.26 ? 1312 ASP B OD1 1 
ATOM   22404 O  OD2 . ASP C 1 1312 ? 106.529 -0.935  98.930  1.00 144.70 ? 1312 ASP B OD2 1 
ATOM   22405 N  N   . ILE C 1 1313 ? 101.411 -2.727  97.453  1.00 117.49 ? 1313 ILE B N   1 
ATOM   22406 C  CA  . ILE C 1 1313 ? 100.738 -3.969  97.084  1.00 115.90 ? 1313 ILE B CA  1 
ATOM   22407 C  C   . ILE C 1 1313 ? 101.428 -4.825  96.056  1.00 122.03 ? 1313 ILE B C   1 
ATOM   22408 O  O   . ILE C 1 1313 ? 102.330 -4.400  95.334  1.00 129.98 ? 1313 ILE B O   1 
ATOM   22409 C  CB  . ILE C 1 1313 ? 99.324  -3.704  96.608  1.00 110.33 ? 1313 ILE B CB  1 
ATOM   22410 C  CG1 . ILE C 1 1313 ? 98.795  -2.435  97.323  1.00 109.12 ? 1313 ILE B CG1 1 
ATOM   22411 C  CG2 . ILE C 1 1313 ? 98.493  -4.957  96.811  1.00 108.44 ? 1313 ILE B CG2 1 
ATOM   22412 C  CD1 . ILE C 1 1313 ? 97.284  -2.333  97.482  1.00 108.56 ? 1313 ILE B CD1 1 
ATOM   22413 N  N   . ASP C 1 1314 ? 100.990 -6.066  96.015  1.00 158.29 ? 1314 ASP B N   1 
ATOM   22414 C  CA  . ASP C 1 1314 ? 101.421 -6.955  94.970  1.00 159.25 ? 1314 ASP B CA  1 
ATOM   22415 C  C   . ASP C 1 1314 ? 100.402 -8.071  94.797  1.00 156.40 ? 1314 ASP B C   1 
ATOM   22416 O  O   . ASP C 1 1314 ? 100.272 -8.953  95.657  1.00 155.71 ? 1314 ASP B O   1 
ATOM   22417 C  CB  . ASP C 1 1314 ? 102.820 -7.501  95.272  1.00 162.01 ? 1314 ASP B CB  1 
ATOM   22418 C  CG  . ASP C 1 1314 ? 103.233 -8.610  94.322  1.00 167.06 ? 1314 ASP B CG  1 
ATOM   22419 O  OD1 . ASP C 1 1314 ? 102.706 -9.732  94.460  1.00 165.49 ? 1314 ASP B OD1 1 
ATOM   22420 O  OD2 . ASP C 1 1314 ? 104.084 -8.364  93.445  1.00 173.18 ? 1314 ASP B OD2 1 
ATOM   22421 N  N   . VAL C 1 1315 ? 99.651  -7.989  93.699  1.00 133.68 ? 1315 VAL B N   1 
ATOM   22422 C  CA  . VAL C 1 1315 ? 98.811  -9.082  93.244  1.00 132.97 ? 1315 VAL B CA  1 
ATOM   22423 C  C   . VAL C 1 1315 ? 99.705  -10.015 92.432  1.00 135.69 ? 1315 VAL B C   1 
ATOM   22424 O  O   . VAL C 1 1315 ? 100.704 -9.565  91.853  1.00 138.78 ? 1315 VAL B O   1 
ATOM   22425 C  CB  . VAL C 1 1315 ? 97.660  -8.558  92.387  1.00 132.69 ? 1315 VAL B CB  1 
ATOM   22426 C  CG1 . VAL C 1 1315 ? 98.203  -7.938  91.105  1.00 126.10 ? 1315 VAL B CG1 1 
ATOM   22427 C  CG2 . VAL C 1 1315 ? 96.666  -9.663  92.113  1.00 123.71 ? 1315 VAL B CG2 1 
ATOM   22428 N  N   . SER C 1 1316 ? 99.365  -11.307 92.419  1.00 160.41 ? 1316 SER B N   1 
ATOM   22429 C  CA  . SER C 1 1316 ? 100.214 -12.338 91.815  1.00 168.62 ? 1316 SER B CA  1 
ATOM   22430 C  C   . SER C 1 1316 ? 99.553  -13.719 91.761  1.00 173.44 ? 1316 SER B C   1 
ATOM   22431 O  O   . SER C 1 1316 ? 98.782  -14.087 92.643  1.00 172.80 ? 1316 SER B O   1 
ATOM   22432 C  CB  . SER C 1 1316 ? 101.529 -12.446 92.584  1.00 169.73 ? 1316 SER B CB  1 
ATOM   22433 O  OG  . SER C 1 1316 ? 102.630 -12.476 91.700  1.00 173.87 ? 1316 SER B OG  1 
ATOM   22434 N  N   . TYR C 1 1317 ? 99.880  -14.480 90.720  1.00 196.63 ? 1317 TYR B N   1 
ATOM   22435 C  CA  . TYR C 1 1317 ? 99.367  -15.834 90.538  1.00 201.29 ? 1317 TYR B CA  1 
ATOM   22436 C  C   . TYR C 1 1317 ? 100.109 -16.813 91.417  1.00 202.95 ? 1317 TYR B C   1 
ATOM   22437 O  O   . TYR C 1 1317 ? 101.285 -16.612 91.711  1.00 204.52 ? 1317 TYR B O   1 
ATOM   22438 C  CB  . TYR C 1 1317 ? 99.501  -16.254 89.081  1.00 208.44 ? 1317 TYR B CB  1 
ATOM   22439 C  CG  . TYR C 1 1317 ? 98.716  -15.352 88.185  1.00 213.05 ? 1317 TYR B CG  1 
ATOM   22440 C  CD1 . TYR C 1 1317 ? 99.310  -14.257 87.581  1.00 216.67 ? 1317 TYR B CD1 1 
ATOM   22441 C  CD2 . TYR C 1 1317 ? 97.362  -15.562 87.983  1.00 214.80 ? 1317 TYR B CD2 1 
ATOM   22442 C  CE1 . TYR C 1 1317 ? 98.576  -13.406 86.772  1.00 219.29 ? 1317 TYR B CE1 1 
ATOM   22443 C  CE2 . TYR C 1 1317 ? 96.618  -14.719 87.178  1.00 217.67 ? 1317 TYR B CE2 1 
ATOM   22444 C  CZ  . TYR C 1 1317 ? 97.226  -13.638 86.570  1.00 220.34 ? 1317 TYR B CZ  1 
ATOM   22445 O  OH  . TYR C 1 1317 ? 96.485  -12.792 85.759  1.00 221.97 ? 1317 TYR B OH  1 
ATOM   22446 N  N   . LYS C 1 1318 ? 99.427  -17.884 91.816  1.00 194.42 ? 1318 LYS B N   1 
ATOM   22447 C  CA  . LYS C 1 1318 ? 99.993  -18.852 92.755  1.00 196.76 ? 1318 LYS B CA  1 
ATOM   22448 C  C   . LYS C 1 1318 ? 101.243 -19.522 92.202  1.00 204.35 ? 1318 LYS B C   1 
ATOM   22449 O  O   . LYS C 1 1318 ? 102.240 -19.683 92.902  1.00 203.99 ? 1318 LYS B O   1 
ATOM   22450 C  CB  . LYS C 1 1318 ? 98.957  -19.917 93.136  1.00 195.33 ? 1318 LYS B CB  1 
ATOM   22451 C  CG  . LYS C 1 1318 ? 99.531  -21.065 93.959  1.00 198.97 ? 1318 LYS B CG  1 
ATOM   22452 C  CD  . LYS C 1 1318 ? 99.003  -21.108 95.399  1.00 198.43 ? 1318 LYS B CD  1 
ATOM   22453 C  CE  . LYS C 1 1318 ? 97.721  -21.927 95.513  1.00 198.37 ? 1318 LYS B CE  1 
ATOM   22454 N  NZ  . LYS C 1 1318 ? 97.478  -22.411 96.905  1.00 197.34 ? 1318 LYS B NZ  1 
ATOM   22455 N  N   . HIS C 1 1319 ? 101.189 -19.899 90.934  1.00 199.24 ? 1319 HIS B N   1 
ATOM   22456 C  CA  . HIS C 1 1319 ? 102.290 -20.618 90.325  1.00 207.50 ? 1319 HIS B CA  1 
ATOM   22457 C  C   . HIS C 1 1319 ? 102.898 -19.824 89.177  1.00 219.76 ? 1319 HIS B C   1 
ATOM   22458 O  O   . HIS C 1 1319 ? 104.117 -19.799 89.001  1.00 221.93 ? 1319 HIS B O   1 
ATOM   22459 C  CB  . HIS C 1 1319 ? 101.788 -21.966 89.837  1.00 203.81 ? 1319 HIS B CB  1 
ATOM   22460 C  CG  . HIS C 1 1319 ? 101.004 -22.720 90.865  1.00 200.52 ? 1319 HIS B CG  1 
ATOM   22461 N  ND1 . HIS C 1 1319 ? 99.648  -22.552 91.037  1.00 198.28 ? 1319 HIS B ND1 1 
ATOM   22462 C  CD2 . HIS C 1 1319 ? 101.389 -23.652 91.769  1.00 201.72 ? 1319 HIS B CD2 1 
ATOM   22463 C  CE1 . HIS C 1 1319 ? 99.226  -23.353 92.002  1.00 197.69 ? 1319 HIS B CE1 1 
ATOM   22464 N  NE2 . HIS C 1 1319 ? 100.263 -24.028 92.461  1.00 200.00 ? 1319 HIS B NE2 1 
ATOM   22465 N  N   . LYS C 1 1320 ? 102.041 -19.175 88.399  1.00 232.33 ? 1320 LYS B N   1 
ATOM   22466 C  CA  . LYS C 1 1320 ? 102.490 -18.283 87.344  1.00 245.51 ? 1320 LYS B CA  1 
ATOM   22467 C  C   . LYS C 1 1320 ? 103.344 -17.155 87.917  1.00 252.09 ? 1320 LYS B C   1 
ATOM   22468 O  O   . LYS C 1 1320 ? 103.122 -16.709 89.043  1.00 251.92 ? 1320 LYS B O   1 
ATOM   22469 C  CB  . LYS C 1 1320 ? 101.285 -17.692 86.619  1.00 248.75 ? 1320 LYS B CB  1 
ATOM   22470 C  CG  . LYS C 1 1320 ? 101.616 -16.482 85.773  1.00 254.17 ? 1320 LYS B CG  1 
ATOM   22471 C  CD  . LYS C 1 1320 ? 102.655 -16.822 84.721  1.00 261.39 ? 1320 LYS B CD  1 
ATOM   22472 C  CE  . LYS C 1 1320 ? 102.969 -15.609 83.865  1.00 264.11 ? 1320 LYS B CE  1 
ATOM   22473 N  NZ  . LYS C 1 1320 ? 104.068 -15.875 82.903  1.00 267.69 ? 1320 LYS B NZ  1 
ATOM   22474 N  N   . GLY C 1 1321 ? 104.317 -16.695 87.134  1.00 224.08 ? 1321 GLY B N   1 
ATOM   22475 C  CA  . GLY C 1 1321 ? 105.135 -15.554 87.507  1.00 224.02 ? 1321 GLY B CA  1 
ATOM   22476 C  C   . GLY C 1 1321 ? 104.316 -14.357 87.947  1.00 220.09 ? 1321 GLY B C   1 
ATOM   22477 O  O   . GLY C 1 1321 ? 103.092 -14.345 87.839  1.00 221.31 ? 1321 GLY B O   1 
ATOM   22478 N  N   . ALA C 1 1322 ? 104.998 -13.337 88.446  1.00 260.82 ? 1322 ALA B N   1 
ATOM   22479 C  CA  . ALA C 1 1322 ? 104.308 -12.203 89.042  1.00 252.59 ? 1322 ALA B CA  1 
ATOM   22480 C  C   . ALA C 1 1322 ? 103.554 -11.320 88.046  1.00 246.15 ? 1322 ALA B C   1 
ATOM   22481 O  O   . ALA C 1 1322 ? 104.050 -10.994 86.967  1.00 244.24 ? 1322 ALA B O   1 
ATOM   22482 C  CB  . ALA C 1 1322 ? 105.274 -11.366 89.877  1.00 249.73 ? 1322 ALA B CB  1 
ATOM   22483 N  N   . LEU C 1 1323 ? 102.336 -10.963 88.439  1.00 240.32 ? 1323 LEU B N   1 
ATOM   22484 C  CA  . LEU C 1 1323 ? 101.568 -9.890  87.831  1.00 234.40 ? 1323 LEU B CA  1 
ATOM   22485 C  C   . LEU C 1 1323 ? 101.980 -8.587  88.523  1.00 237.90 ? 1323 LEU B C   1 
ATOM   22486 O  O   . LEU C 1 1323 ? 102.896 -8.590  89.349  1.00 244.57 ? 1323 LEU B O   1 
ATOM   22487 C  CB  . LEU C 1 1323 ? 100.082 -10.171 88.033  1.00 210.43 ? 1323 LEU B CB  1 
ATOM   22488 C  CG  . LEU C 1 1323 ? 99.049  -9.088  87.752  1.00 191.62 ? 1323 LEU B CG  1 
ATOM   22489 C  CD1 . LEU C 1 1323 ? 99.302  -8.447  86.407  1.00 183.51 ? 1323 LEU B CD1 1 
ATOM   22490 C  CD2 . LEU C 1 1323 ? 97.656  -9.687  87.823  1.00 178.96 ? 1323 LEU B CD2 1 
ATOM   22491 N  N   . HIS C 1 1324 ? 101.301 -7.484  88.209  1.00 203.12 ? 1324 HIS B N   1 
ATOM   22492 C  CA  . HIS C 1 1324 ? 101.699 -6.161  88.705  1.00 201.03 ? 1324 HIS B CA  1 
ATOM   22493 C  C   . HIS C 1 1324 ? 101.825 -6.006  90.221  1.00 196.69 ? 1324 HIS B C   1 
ATOM   22494 O  O   . HIS C 1 1324 ? 101.411 -6.871  91.005  1.00 193.70 ? 1324 HIS B O   1 
ATOM   22495 C  CB  . HIS C 1 1324 ? 100.827 -5.032  88.118  1.00 201.97 ? 1324 HIS B CB  1 
ATOM   22496 C  CG  . HIS C 1 1324 ? 99.447  -4.943  88.698  1.00 206.10 ? 1324 HIS B CG  1 
ATOM   22497 N  ND1 . HIS C 1 1324 ? 99.087  -3.985  89.621  1.00 206.91 ? 1324 HIS B ND1 1 
ATOM   22498 C  CD2 . HIS C 1 1324 ? 98.333  -5.674  88.462  1.00 208.20 ? 1324 HIS B CD2 1 
ATOM   22499 C  CE1 . HIS C 1 1324 ? 97.815  -4.137  89.936  1.00 206.97 ? 1324 HIS B CE1 1 
ATOM   22500 N  NE2 . HIS C 1 1324 ? 97.333  -5.156  89.248  1.00 208.19 ? 1324 HIS B NE2 1 
ATOM   22501 N  N   . ASN C 1 1325 ? 102.424 -4.882  90.604  1.00 175.18 ? 1325 ASN B N   1 
ATOM   22502 C  CA  . ASN C 1 1325 ? 102.666 -4.549  91.996  1.00 176.02 ? 1325 ASN B CA  1 
ATOM   22503 C  C   . ASN C 1 1325 ? 102.980 -3.085  92.109  1.00 170.85 ? 1325 ASN B C   1 
ATOM   22504 O  O   . ASN C 1 1325 ? 103.880 -2.585  91.453  1.00 171.44 ? 1325 ASN B O   1 
ATOM   22505 C  CB  . ASN C 1 1325 ? 103.806 -5.387  92.582  1.00 184.38 ? 1325 ASN B CB  1 
ATOM   22506 C  CG  . ASN C 1 1325 ? 105.118 -5.213  91.840  1.00 191.27 ? 1325 ASN B CG  1 
ATOM   22507 O  OD1 . ASN C 1 1325 ? 105.549 -6.104  91.106  1.00 193.36 ? 1325 ASN B OD1 1 
ATOM   22508 N  ND2 . ASN C 1 1325 ? 105.768 -4.074  92.043  1.00 193.03 ? 1325 ASN B ND2 1 
ATOM   22509 N  N   . TYR C 1 1326 ? 102.234 -2.388  92.943  1.00 183.94 ? 1326 TYR B N   1 
ATOM   22510 C  CA  . TYR C 1 1326 ? 102.357 -0.956  92.937  1.00 184.62 ? 1326 TYR B CA  1 
ATOM   22511 C  C   . TYR C 1 1326 ? 102.307 -0.316  94.285  1.00 173.33 ? 1326 TYR B C   1 
ATOM   22512 O  O   . TYR C 1 1326 ? 101.414 -0.580  95.080  1.00 170.34 ? 1326 TYR B O   1 
ATOM   22513 C  CB  . TYR C 1 1326 ? 101.278 -0.339  92.066  1.00 192.85 ? 1326 TYR B CB  1 
ATOM   22514 C  CG  . TYR C 1 1326 ? 99.857  -0.733  92.388  1.00 198.48 ? 1326 TYR B CG  1 
ATOM   22515 C  CD1 . TYR C 1 1326 ? 98.947  0.210   92.861  1.00 200.24 ? 1326 TYR B CD1 1 
ATOM   22516 C  CD2 . TYR C 1 1326 ? 99.408  -2.026  92.173  1.00 202.29 ? 1326 TYR B CD2 1 
ATOM   22517 C  CE1 . TYR C 1 1326 ? 97.639  -0.130  93.124  1.00 201.10 ? 1326 TYR B CE1 1 
ATOM   22518 C  CE2 . TYR C 1 1326 ? 98.100  -2.376  92.436  1.00 203.23 ? 1326 TYR B CE2 1 
ATOM   22519 C  CZ  . TYR C 1 1326 ? 97.221  -1.425  92.910  1.00 202.74 ? 1326 TYR B CZ  1 
ATOM   22520 O  OH  . TYR C 1 1326 ? 95.916  -1.768  93.172  1.00 201.93 ? 1326 TYR B OH  1 
ATOM   22521 N  N   . LYS C 1 1327 ? 103.266 0.562   94.525  1.00 172.73 ? 1327 LYS B N   1 
ATOM   22522 C  CA  . LYS C 1 1327 ? 103.229 1.359   95.720  1.00 164.19 ? 1327 LYS B CA  1 
ATOM   22523 C  C   . LYS C 1 1327 ? 102.042 2.314   95.649  1.00 153.28 ? 1327 LYS B C   1 
ATOM   22524 O  O   . LYS C 1 1327 ? 101.973 3.179   94.777  1.00 152.76 ? 1327 LYS B O   1 
ATOM   22525 C  CB  . LYS C 1 1327 ? 104.542 2.113   95.903  1.00 169.21 ? 1327 LYS B CB  1 
ATOM   22526 C  CG  . LYS C 1 1327 ? 104.658 2.769   97.279  1.00 172.29 ? 1327 LYS B CG  1 
ATOM   22527 C  CD  . LYS C 1 1327 ? 106.084 2.722   97.855  1.00 177.20 ? 1327 LYS B CD  1 
ATOM   22528 C  CE  . LYS C 1 1327 ? 106.123 3.127   99.339  1.00 173.97 ? 1327 LYS B CE  1 
ATOM   22529 N  NZ  . LYS C 1 1327 ? 105.743 2.029   100.269 1.00 170.00 ? 1327 LYS B NZ  1 
ATOM   22530 N  N   . MET C 1 1328 ? 101.100 2.120   96.567  1.00 129.19 ? 1328 MET B N   1 
ATOM   22531 C  CA  . MET C 1 1328 ? 99.952  3.004   96.757  1.00 118.09 ? 1328 MET B CA  1 
ATOM   22532 C  C   . MET C 1 1328 ? 100.358 4.219   97.634  1.00 118.34 ? 1328 MET B C   1 
ATOM   22533 O  O   . MET C 1 1328 ? 101.360 4.165   98.318  1.00 117.94 ? 1328 MET B O   1 
ATOM   22534 C  CB  . MET C 1 1328 ? 98.837  2.182   97.406  1.00 111.38 ? 1328 MET B CB  1 
ATOM   22535 C  CG  . MET C 1 1328 ? 97.605  2.945   97.777  1.00 119.42 ? 1328 MET B CG  1 
ATOM   22536 S  SD  . MET C 1 1328 ? 96.207  1.847   98.059  1.00 115.32 ? 1328 MET B SD  1 
ATOM   22537 C  CE  . MET C 1 1328 ? 95.649  1.505   96.411  1.00 119.31 ? 1328 MET B CE  1 
ATOM   22538 N  N   . THR C 1 1329 ? 99.617  5.319   97.594  1.00 125.60 ? 1329 THR B N   1 
ATOM   22539 C  CA  . THR C 1 1329 ? 99.797  6.427   98.535  1.00 125.15 ? 1329 THR B CA  1 
ATOM   22540 C  C   . THR C 1 1329 ? 98.551  7.245   98.352  1.00 122.92 ? 1329 THR B C   1 
ATOM   22541 O  O   . THR C 1 1329 ? 97.571  6.736   97.845  1.00 122.77 ? 1329 THR B O   1 
ATOM   22542 C  CB  . THR C 1 1329 ? 101.028 7.311   98.254  1.00 128.58 ? 1329 THR B CB  1 
ATOM   22543 O  OG1 . THR C 1 1329 ? 101.080 7.634   96.868  1.00 129.77 ? 1329 THR B OG1 1 
ATOM   22544 C  CG2 . THR C 1 1329 ? 102.324 6.622   98.639  1.00 131.09 ? 1329 THR B CG2 1 
ATOM   22545 N  N   . ASP C 1 1330 ? 98.570  8.510   98.737  1.00 147.47 ? 1330 ASP B N   1 
ATOM   22546 C  CA  . ASP C 1 1330 ? 97.416  9.368   98.471  1.00 149.49 ? 1330 ASP B CA  1 
ATOM   22547 C  C   . ASP C 1 1330 ? 97.548  10.062  97.103  1.00 153.69 ? 1330 ASP B C   1 
ATOM   22548 O  O   . ASP C 1 1330 ? 96.720  10.896  96.714  1.00 155.72 ? 1330 ASP B O   1 
ATOM   22549 C  CB  . ASP C 1 1330 ? 97.208  10.393  99.592  1.00 150.42 ? 1330 ASP B CB  1 
ATOM   22550 C  CG  . ASP C 1 1330 ? 97.024  9.754   100.972 1.00 148.95 ? 1330 ASP B CG  1 
ATOM   22551 O  OD1 . ASP C 1 1330 ? 96.154  8.870   101.150 1.00 143.81 ? 1330 ASP B OD1 1 
ATOM   22552 O  OD2 . ASP C 1 1330 ? 97.752  10.170  101.898 1.00 151.98 ? 1330 ASP B OD2 1 
ATOM   22553 N  N   . LYS C 1 1331 ? 98.623  9.709   96.400  1.00 171.76 ? 1331 LYS B N   1 
ATOM   22554 C  CA  . LYS C 1 1331 ? 98.854  10.069  94.997  1.00 174.66 ? 1331 LYS B CA  1 
ATOM   22555 C  C   . LYS C 1 1331 ? 97.875  9.346   94.053  1.00 174.38 ? 1331 LYS B C   1 
ATOM   22556 O  O   . LYS C 1 1331 ? 96.971  9.962   93.480  1.00 174.31 ? 1331 LYS B O   1 
ATOM   22557 C  CB  . LYS C 1 1331 ? 100.287 9.698   94.605  1.00 176.95 ? 1331 LYS B CB  1 
ATOM   22558 C  CG  . LYS C 1 1331 ? 101.358 10.323  95.489  1.00 175.72 ? 1331 LYS B CG  1 
ATOM   22559 C  CD  . LYS C 1 1331 ? 100.948 11.729  95.846  1.00 175.22 ? 1331 LYS B CD  1 
ATOM   22560 C  CE  . LYS C 1 1331 ? 102.139 12.645  96.011  1.00 178.45 ? 1331 LYS B CE  1 
ATOM   22561 N  NZ  . LYS C 1 1331 ? 101.700 14.066  95.881  1.00 180.15 ? 1331 LYS B NZ  1 
ATOM   22562 N  N   . ASN C 1 1332 ? 98.091  8.041   93.876  1.00 134.85 ? 1332 ASN B N   1 
ATOM   22563 C  CA  . ASN C 1 1332 ? 97.084  7.139   93.324  1.00 136.91 ? 1332 ASN B CA  1 
ATOM   22564 C  C   . ASN C 1 1332 ? 96.454  6.318   94.422  1.00 137.23 ? 1332 ASN B C   1 
ATOM   22565 O  O   . ASN C 1 1332 ? 97.151  5.783   95.276  1.00 137.99 ? 1332 ASN B O   1 
ATOM   22566 C  CB  . ASN C 1 1332 ? 97.727  6.116   92.406  1.00 140.96 ? 1332 ASN B CB  1 
ATOM   22567 C  CG  . ASN C 1 1332 ? 97.929  4.771   93.096  1.00 141.41 ? 1332 ASN B CG  1 
ATOM   22568 O  OD1 . ASN C 1 1332 ? 98.958  4.536   93.731  1.00 139.84 ? 1332 ASN B OD1 1 
ATOM   22569 N  ND2 . ASN C 1 1332 ? 96.935  3.893   92.989  1.00 140.51 ? 1332 ASN B ND2 1 
ATOM   22570 N  N   . PHE C 1 1333 ? 95.146  6.162   94.391  1.00 157.66 ? 1333 PHE B N   1 
ATOM   22571 C  CA  . PHE C 1 1333 ? 94.576  5.112   95.204  1.00 153.09 ? 1333 PHE B CA  1 
ATOM   22572 C  C   . PHE C 1 1333 ? 93.343  4.533   94.581  1.00 158.35 ? 1333 PHE B C   1 
ATOM   22573 O  O   . PHE C 1 1333 ? 92.976  3.400   94.861  1.00 159.51 ? 1333 PHE B O   1 
ATOM   22574 C  CB  . PHE C 1 1333 ? 94.400  5.489   96.689  1.00 142.43 ? 1333 PHE B CB  1 
ATOM   22575 C  CG  . PHE C 1 1333 ? 93.426  6.612   96.963  1.00 134.78 ? 1333 PHE B CG  1 
ATOM   22576 C  CD1 . PHE C 1 1333 ? 92.077  6.350   97.177  1.00 130.03 ? 1333 PHE B CD1 1 
ATOM   22577 C  CD2 . PHE C 1 1333 ? 93.877  7.922   97.103  1.00 135.27 ? 1333 PHE B CD2 1 
ATOM   22578 C  CE1 . PHE C 1 1333 ? 91.183  7.383   97.470  1.00 130.28 ? 1333 PHE B CE1 1 
ATOM   22579 C  CE2 . PHE C 1 1333 ? 92.994  8.961   97.393  1.00 128.38 ? 1333 PHE B CE2 1 
ATOM   22580 C  CZ  . PHE C 1 1333 ? 91.642  8.690   97.574  1.00 126.99 ? 1333 PHE B CZ  1 
ATOM   22581 N  N   . LEU C 1 1334 ? 92.731  5.288   93.690  1.00 150.15 ? 1334 LEU B N   1 
ATOM   22582 C  CA  . LEU C 1 1334 ? 91.584  4.769   92.968  1.00 145.50 ? 1334 LEU B CA  1 
ATOM   22583 C  C   . LEU C 1 1334 ? 92.012  4.032   91.688  1.00 153.75 ? 1334 LEU B C   1 
ATOM   22584 O  O   . LEU C 1 1334 ? 91.261  3.966   90.700  1.00 156.42 ? 1334 LEU B O   1 
ATOM   22585 C  CB  . LEU C 1 1334 ? 90.624  5.898   92.618  1.00 136.15 ? 1334 LEU B CB  1 
ATOM   22586 C  CG  . LEU C 1 1334 ? 90.364  7.098   93.531  1.00 128.77 ? 1334 LEU B CG  1 
ATOM   22587 C  CD1 . LEU C 1 1334 ? 89.533  6.701   94.698  1.00 123.38 ? 1334 LEU B CD1 1 
ATOM   22588 C  CD2 . LEU C 1 1334 ? 91.655  7.760   93.971  1.00 127.45 ? 1334 LEU B CD2 1 
ATOM   22589 N  N   . GLY C 1 1335 ? 93.225  3.487   91.720  1.00 158.89 ? 1335 GLY B N   1 
ATOM   22590 C  CA  . GLY C 1 1335 ? 93.831  2.827   90.578  1.00 167.25 ? 1335 GLY B CA  1 
ATOM   22591 C  C   . GLY C 1 1335 ? 92.940  2.089   89.593  1.00 172.54 ? 1335 GLY B C   1 
ATOM   22592 O  O   . GLY C 1 1335 ? 91.728  1.930   89.763  1.00 172.49 ? 1335 GLY B O   1 
ATOM   22593 N  N   . ARG C 1 1336 ? 93.579  1.650   88.523  1.00 198.17 ? 1336 ARG B N   1 
ATOM   22594 C  CA  . ARG C 1 1336 ? 92.937  0.848   87.504  1.00 205.97 ? 1336 ARG B CA  1 
ATOM   22595 C  C   . ARG C 1 1336 ? 92.431  -0.427  88.140  1.00 197.15 ? 1336 ARG B C   1 
ATOM   22596 O  O   . ARG C 1 1336 ? 93.078  -0.949  89.054  1.00 195.91 ? 1336 ARG B O   1 
ATOM   22597 C  CB  . ARG C 1 1336 ? 93.995  0.462   86.488  1.00 221.76 ? 1336 ARG B CB  1 
ATOM   22598 C  CG  . ARG C 1 1336 ? 95.325  0.238   87.171  1.00 233.06 ? 1336 ARG B CG  1 
ATOM   22599 C  CD  . ARG C 1 1336 ? 96.005  -1.020  86.716  1.00 244.90 ? 1336 ARG B CD  1 
ATOM   22600 N  NE  . ARG C 1 1336 ? 97.195  -1.258  87.526  1.00 252.84 ? 1336 ARG B NE  1 
ATOM   22601 C  CZ  . ARG C 1 1336 ? 98.332  -1.757  87.056  1.00 260.68 ? 1336 ARG B CZ  1 
ATOM   22602 N  NH1 . ARG C 1 1336 ? 98.436  -2.075  85.772  1.00 264.97 ? 1336 ARG B NH1 1 
ATOM   22603 N  NH2 . ARG C 1 1336 ? 99.364  -1.934  87.868  1.00 262.08 ? 1336 ARG B NH2 1 
ATOM   22604 N  N   . PRO C 1 1337 ? 91.260  -0.916  87.688  1.00 136.34 ? 1337 PRO B N   1 
ATOM   22605 C  CA  . PRO C 1 1337 ? 90.886  -2.329  87.891  1.00 128.27 ? 1337 PRO B CA  1 
ATOM   22606 C  C   . PRO C 1 1337 ? 91.836  -3.274  87.140  1.00 126.06 ? 1337 PRO B C   1 
ATOM   22607 O  O   . PRO C 1 1337 ? 92.805  -2.817  86.523  1.00 133.33 ? 1337 PRO B O   1 
ATOM   22608 C  CB  . PRO C 1 1337 ? 89.465  -2.404  87.329  1.00 129.92 ? 1337 PRO B CB  1 
ATOM   22609 C  CG  . PRO C 1 1337 ? 88.932  -0.999  87.548  1.00 132.96 ? 1337 PRO B CG  1 
ATOM   22610 C  CD  . PRO C 1 1337 ? 90.104  -0.077  87.320  1.00 135.49 ? 1337 PRO B CD  1 
ATOM   22611 N  N   . VAL C 1 1338 ? 91.595  -4.575  87.224  1.00 136.14 ? 1338 VAL B N   1 
ATOM   22612 C  CA  . VAL C 1 1338 ? 92.357  -5.527  86.414  1.00 142.53 ? 1338 VAL B CA  1 
ATOM   22613 C  C   . VAL C 1 1338 ? 91.666  -6.877  86.401  1.00 148.95 ? 1338 VAL B C   1 
ATOM   22614 O  O   . VAL C 1 1338 ? 91.309  -7.432  87.440  1.00 149.22 ? 1338 VAL B O   1 
ATOM   22615 C  CB  . VAL C 1 1338 ? 93.867  -5.655  86.803  1.00 182.39 ? 1338 VAL B CB  1 
ATOM   22616 C  CG1 . VAL C 1 1338 ? 94.346  -7.110  86.695  1.00 182.44 ? 1338 VAL B CG1 1 
ATOM   22617 C  CG2 . VAL C 1 1338 ? 94.724  -4.764  85.910  1.00 184.52 ? 1338 VAL B CG2 1 
ATOM   22618 N  N   . GLU C 1 1339 ? 91.458  -7.383  85.196  1.00 183.92 ? 1339 GLU B N   1 
ATOM   22619 C  CA  . GLU C 1 1339 ? 90.775  -8.642  85.015  1.00 189.12 ? 1339 GLU B CA  1 
ATOM   22620 C  C   . GLU C 1 1339 ? 91.832  -9.737  85.077  1.00 188.36 ? 1339 GLU B C   1 
ATOM   22621 O  O   . GLU C 1 1339 ? 92.911  -9.635  84.476  1.00 187.90 ? 1339 GLU B O   1 
ATOM   22622 C  CB  . GLU C 1 1339 ? 89.931  -8.624  83.713  1.00 197.54 ? 1339 GLU B CB  1 
ATOM   22623 C  CG  . GLU C 1 1339 ? 88.620  -7.726  83.798  1.00 202.81 ? 1339 GLU B CG  1 
ATOM   22624 C  CD  . GLU C 1 1339 ? 88.035  -7.247  82.438  1.00 209.83 ? 1339 GLU B CD  1 
ATOM   22625 O  OE1 . GLU C 1 1339 ? 87.975  -8.061  81.492  1.00 213.32 ? 1339 GLU B OE1 1 
ATOM   22626 O  OE2 . GLU C 1 1339 ? 87.614  -6.060  82.325  1.00 210.83 ? 1339 GLU B OE2 1 
ATOM   22627 N  N   . VAL C 1 1340 ? 91.541  -10.751 85.876  1.00 165.59 ? 1340 VAL B N   1 
ATOM   22628 C  CA  . VAL C 1 1340 ? 92.453  -11.861 86.020  1.00 168.82 ? 1340 VAL B CA  1 
ATOM   22629 C  C   . VAL C 1 1340 ? 92.308  -12.837 84.882  1.00 172.94 ? 1340 VAL B C   1 
ATOM   22630 O  O   . VAL C 1 1340 ? 91.338  -13.599 84.811  1.00 175.57 ? 1340 VAL B O   1 
ATOM   22631 C  CB  . VAL C 1 1340 ? 92.244  -12.591 87.325  1.00 168.96 ? 1340 VAL B CB  1 
ATOM   22632 C  CG1 . VAL C 1 1340 ? 92.863  -13.986 87.274  1.00 171.25 ? 1340 VAL B CG1 1 
ATOM   22633 C  CG2 . VAL C 1 1340 ? 92.865  -11.773 88.428  1.00 166.74 ? 1340 VAL B CG2 1 
ATOM   22634 N  N   . LEU C 1 1341 ? 93.311  -12.810 84.011  1.00 239.98 ? 1341 LEU B N   1 
ATOM   22635 C  CA  . LEU C 1 1341 ? 93.394  -13.683 82.853  1.00 243.55 ? 1341 LEU B CA  1 
ATOM   22636 C  C   . LEU C 1 1341 ? 93.599  -15.144 83.245  1.00 248.39 ? 1341 LEU B C   1 
ATOM   22637 O  O   . LEU C 1 1341 ? 92.643  -15.905 83.435  1.00 248.31 ? 1341 LEU B O   1 
ATOM   22638 C  CB  . LEU C 1 1341 ? 94.568  -13.253 81.964  1.00 244.19 ? 1341 LEU B CB  1 
ATOM   22639 C  CG  . LEU C 1 1341 ? 94.512  -11.982 81.118  1.00 262.93 ? 1341 LEU B CG  1 
ATOM   22640 C  CD1 . LEU C 1 1341 ? 93.282  -12.003 80.204  1.00 262.94 ? 1341 LEU B CD1 1 
ATOM   22641 C  CD2 . LEU C 1 1341 ? 94.553  -10.735 82.000  1.00 260.96 ? 1341 LEU B CD2 1 
ATOM   22642 N  N   . LEU C 1 1342 ? 94.873  -15.491 83.396  1.00 180.57 ? 1342 LEU B N   1 
ATOM   22643 C  CA  . LEU C 1 1342 ? 95.380  -16.864 83.417  1.00 182.51 ? 1342 LEU B CA  1 
ATOM   22644 C  C   . LEU C 1 1342 ? 94.658  -17.839 84.359  1.00 180.21 ? 1342 LEU B C   1 
ATOM   22645 O  O   . LEU C 1 1342 ? 93.615  -17.519 84.928  1.00 177.17 ? 1342 LEU B O   1 
ATOM   22646 C  CB  . LEU C 1 1342 ? 96.888  -16.821 83.707  1.00 181.46 ? 1342 LEU B CB  1 
ATOM   22647 C  CG  . LEU C 1 1342 ? 97.530  -15.452 83.389  1.00 177.79 ? 1342 LEU B CG  1 
ATOM   22648 C  CD1 . LEU C 1 1342 ? 99.032  -15.414 83.641  1.00 178.06 ? 1342 LEU B CD1 1 
ATOM   22649 C  CD2 . LEU C 1 1342 ? 97.259  -15.019 81.967  1.00 178.79 ? 1342 LEU B CD2 1 
ATOM   22650 N  N   . ASN C 1 1343 ? 95.198  -19.047 84.485  1.00 202.16 ? 1343 ASN B N   1 
ATOM   22651 C  CA  . ASN C 1 1343 ? 94.581  -20.060 85.338  1.00 206.32 ? 1343 ASN B CA  1 
ATOM   22652 C  C   . ASN C 1 1343 ? 95.383  -20.437 86.577  1.00 204.64 ? 1343 ASN B C   1 
ATOM   22653 O  O   . ASN C 1 1343 ? 96.114  -21.431 86.591  1.00 205.58 ? 1343 ASN B O   1 
ATOM   22654 C  CB  . ASN C 1 1343 ? 94.240  -21.303 84.535  1.00 215.96 ? 1343 ASN B CB  1 
ATOM   22655 C  CG  . ASN C 1 1343 ? 92.943  -21.158 83.808  1.00 225.03 ? 1343 ASN B CG  1 
ATOM   22656 O  OD1 . ASN C 1 1343 ? 92.195  -22.117 83.647  1.00 228.85 ? 1343 ASN B OD1 1 
ATOM   22657 N  ND2 . ASN C 1 1343 ? 92.649  -19.937 83.382  1.00 227.36 ? 1343 ASN B ND2 1 
ATOM   22658 N  N   . ASP C 1 1344 ? 95.209  -19.652 87.634  1.00 207.65 ? 1344 ASP B N   1 
ATOM   22659 C  CA  . ASP C 1 1344 ? 96.007  -19.801 88.841  1.00 203.07 ? 1344 ASP B CA  1 
ATOM   22660 C  C   . ASP C 1 1344 ? 95.151  -19.448 90.050  1.00 199.71 ? 1344 ASP B C   1 
ATOM   22661 O  O   . ASP C 1 1344 ? 93.977  -19.089 89.919  1.00 200.10 ? 1344 ASP B O   1 
ATOM   22662 C  CB  . ASP C 1 1344 ? 97.228  -18.870 88.772  1.00 198.18 ? 1344 ASP B CB  1 
ATOM   22663 C  CG  . ASP C 1 1344 ? 98.534  -19.586 89.055  1.00 192.09 ? 1344 ASP B CG  1 
ATOM   22664 O  OD1 . ASP C 1 1344 ? 98.499  -20.701 89.616  1.00 190.23 ? 1344 ASP B OD1 1 
ATOM   22665 O  OD2 . ASP C 1 1344 ? 99.595  -19.024 88.717  1.00 189.49 ? 1344 ASP B OD2 1 
ATOM   22666 N  N   . ASP C 1 1345 ? 95.735  -19.574 91.234  1.00 218.15 ? 1345 ASP B N   1 
ATOM   22667 C  CA  . ASP C 1 1345 ? 95.105  -19.050 92.431  1.00 213.46 ? 1345 ASP B CA  1 
ATOM   22668 C  C   . ASP C 1 1345 ? 95.747  -17.696 92.718  1.00 183.08 ? 1345 ASP B C   1 
ATOM   22669 O  O   . ASP C 1 1345 ? 96.946  -17.507 92.513  1.00 184.92 ? 1345 ASP B O   1 
ATOM   22670 C  CB  . ASP C 1 1345 ? 95.259  -20.023 93.601  1.00 213.37 ? 1345 ASP B CB  1 
ATOM   22671 C  CG  . ASP C 1 1345 ? 94.719  -21.413 93.282  1.00 218.91 ? 1345 ASP B CG  1 
ATOM   22672 O  OD1 . ASP C 1 1345 ? 94.185  -22.069 94.199  1.00 219.52 ? 1345 ASP B OD1 1 
ATOM   22673 O  OD2 . ASP C 1 1345 ? 94.825  -21.851 92.116  1.00 221.92 ? 1345 ASP B OD2 1 
ATOM   22674 N  N   . LEU C 1 1346 ? 94.951  -16.739 93.166  1.00 173.95 ? 1346 LEU B N   1 
ATOM   22675 C  CA  . LEU C 1 1346 ? 95.462  -15.391 93.283  1.00 170.44 ? 1346 LEU B CA  1 
ATOM   22676 C  C   . LEU C 1 1346 ? 95.901  -15.025 94.692  1.00 170.73 ? 1346 LEU B C   1 
ATOM   22677 O  O   . LEU C 1 1346 ? 95.500  -15.671 95.663  1.00 172.83 ? 1346 LEU B O   1 
ATOM   22678 C  CB  . LEU C 1 1346 ? 94.438  -14.385 92.778  1.00 164.37 ? 1346 LEU B CB  1 
ATOM   22679 C  CG  . LEU C 1 1346 ? 95.055  -12.994 92.636  1.00 161.87 ? 1346 LEU B CG  1 
ATOM   22680 C  CD1 . LEU C 1 1346 ? 96.272  -13.025 91.703  1.00 163.85 ? 1346 LEU B CD1 1 
ATOM   22681 C  CD2 . LEU C 1 1346 ? 94.022  -12.013 92.155  1.00 160.88 ? 1346 LEU B CD2 1 
ATOM   22682 N  N   . ILE C 1 1347 ? 96.727  -13.979 94.781  1.00 150.50 ? 1347 ILE B N   1 
ATOM   22683 C  CA  . ILE C 1 1347 ? 97.227  -13.461 96.055  1.00 142.45 ? 1347 ILE B CA  1 
ATOM   22684 C  C   . ILE C 1 1347 ? 97.646  -11.967 96.067  1.00 135.78 ? 1347 ILE B C   1 
ATOM   22685 O  O   . ILE C 1 1347 ? 98.790  -11.620 95.745  1.00 136.18 ? 1347 ILE B O   1 
ATOM   22686 C  CB  . ILE C 1 1347 ? 98.372  -14.352 96.626  1.00 143.11 ? 1347 ILE B CB  1 
ATOM   22687 C  CG1 . ILE C 1 1347 ? 98.863  -15.382 95.602  1.00 146.04 ? 1347 ILE B CG1 1 
ATOM   22688 C  CG2 . ILE C 1 1347 ? 97.892  -15.084 97.869  1.00 141.36 ? 1347 ILE B CG2 1 
ATOM   22689 C  CD1 . ILE C 1 1347 ? 100.041 -16.257 96.102  1.00 149.97 ? 1347 ILE B CD1 1 
ATOM   22690 N  N   . VAL C 1 1348 ? 96.690  -11.107 96.431  1.00 141.96 ? 1348 VAL B N   1 
ATOM   22691 C  CA  . VAL C 1 1348 ? 96.961  -9.748  96.915  1.00 140.56 ? 1348 VAL B CA  1 
ATOM   22692 C  C   . VAL C 1 1348 ? 97.756  -9.897  98.217  1.00 149.91 ? 1348 VAL B C   1 
ATOM   22693 O  O   . VAL C 1 1348 ? 97.450  -10.790 99.016  1.00 151.82 ? 1348 VAL B O   1 
ATOM   22694 C  CB  . VAL C 1 1348 ? 95.639  -8.985  97.265  1.00 133.41 ? 1348 VAL B CB  1 
ATOM   22695 C  CG1 . VAL C 1 1348 ? 95.892  -7.493  97.513  1.00 133.80 ? 1348 VAL B CG1 1 
ATOM   22696 C  CG2 . VAL C 1 1348 ? 94.595  -9.176  96.187  1.00 133.40 ? 1348 VAL B CG2 1 
ATOM   22697 N  N   . SER C 1 1349 ? 98.745  -9.022  98.449  1.00 209.85 ? 1349 SER B N   1 
ATOM   22698 C  CA  . SER C 1 1349 ? 99.687  -9.182  99.574  1.00 210.55 ? 1349 SER B CA  1 
ATOM   22699 C  C   . SER C 1 1349 ? 100.622 -7.994  99.818  1.00 215.35 ? 1349 SER B C   1 
ATOM   22700 O  O   . SER C 1 1349 ? 101.801 -8.034  99.459  1.00 216.62 ? 1349 SER B O   1 
ATOM   22701 C  CB  . SER C 1 1349 ? 100.564 -10.413 99.336  1.00 210.07 ? 1349 SER B CB  1 
ATOM   22702 O  OG  . SER C 1 1349 ? 101.208 -10.318 98.071  1.00 211.49 ? 1349 SER B OG  1 
ATOM   22703 N  N   . THR C 1 1350 ? 100.113 -6.956  100.461 1.00 176.74 ? 1350 THR B N   1 
ATOM   22704 C  CA  . THR C 1 1350 ? 100.944 -5.808  100.777 1.00 178.64 ? 1350 THR B CA  1 
ATOM   22705 C  C   . THR C 1 1350 ? 102.126 -6.200  101.688 1.00 177.68 ? 1350 THR B C   1 
ATOM   22706 O  O   . THR C 1 1350 ? 102.136 -7.291  102.256 1.00 175.33 ? 1350 THR B O   1 
ATOM   22707 C  CB  . THR C 1 1350 ? 100.099 -4.700  101.433 1.00 186.28 ? 1350 THR B CB  1 
ATOM   22708 O  OG1 . THR C 1 1350 ? 100.842 -3.472  101.473 1.00 189.42 ? 1350 THR B OG1 1 
ATOM   22709 C  CG2 . THR C 1 1350 ? 99.675  -5.106  102.841 1.00 183.09 ? 1350 THR B CG2 1 
ATOM   22710 N  N   . GLY C 1 1351 ? 103.128 -5.325  101.782 1.00 147.89 ? 1351 GLY B N   1 
ATOM   22711 C  CA  . GLY C 1 1351 ? 104.217 -5.469  102.738 1.00 147.27 ? 1351 GLY B CA  1 
ATOM   22712 C  C   . GLY C 1 1351 ? 103.809 -4.791  104.029 1.00 141.85 ? 1351 GLY B C   1 
ATOM   22713 O  O   . GLY C 1 1351 ? 102.709 -5.039  104.522 1.00 138.18 ? 1351 GLY B O   1 
ATOM   22714 N  N   . PHE C 1 1352 ? 104.647 -3.921  104.584 1.00 166.58 ? 1352 PHE B N   1 
ATOM   22715 C  CA  . PHE C 1 1352 ? 104.231 -3.301  105.839 1.00 162.96 ? 1352 PHE B CA  1 
ATOM   22716 C  C   . PHE C 1 1352 ? 103.215 -2.192  105.663 1.00 160.25 ? 1352 PHE B C   1 
ATOM   22717 O  O   . PHE C 1 1352 ? 102.027 -2.448  105.491 1.00 159.76 ? 1352 PHE B O   1 
ATOM   22718 C  CB  . PHE C 1 1352 ? 105.380 -2.771  106.693 1.00 162.18 ? 1352 PHE B CB  1 
ATOM   22719 C  CG  . PHE C 1 1352 ? 104.896 -2.220  108.009 1.00 157.88 ? 1352 PHE B CG  1 
ATOM   22720 C  CD1 . PHE C 1 1352 ? 104.107 -3.017  108.835 1.00 153.46 ? 1352 PHE B CD1 1 
ATOM   22721 C  CD2 . PHE C 1 1352 ? 105.151 -0.907  108.396 1.00 158.14 ? 1352 PHE B CD2 1 
ATOM   22722 C  CE1 . PHE C 1 1352 ? 103.607 -2.547  110.039 1.00 149.22 ? 1352 PHE B CE1 1 
ATOM   22723 C  CE2 . PHE C 1 1352 ? 104.650 -0.423  109.618 1.00 154.03 ? 1352 PHE B CE2 1 
ATOM   22724 C  CZ  . PHE C 1 1352 ? 103.876 -1.253  110.437 1.00 150.13 ? 1352 PHE B CZ  1 
ATOM   22725 N  N   . GLY C 1 1353 ? 103.701 -0.958  105.765 1.00 162.05 ? 1353 GLY B N   1 
ATOM   22726 C  CA  . GLY C 1 1353 ? 102.950 0.220   105.373 1.00 160.59 ? 1353 GLY B CA  1 
ATOM   22727 C  C   . GLY C 1 1353 ? 101.981 0.808   106.371 1.00 158.07 ? 1353 GLY B C   1 
ATOM   22728 O  O   . GLY C 1 1353 ? 102.204 0.737   107.571 1.00 155.94 ? 1353 GLY B O   1 
ATOM   22729 N  N   . SER C 1 1354 ? 100.914 1.413   105.851 1.00 135.03 ? 1354 SER B N   1 
ATOM   22730 C  CA  . SER C 1 1354 ? 99.876  2.048   106.664 1.00 131.56 ? 1354 SER B CA  1 
ATOM   22731 C  C   . SER C 1 1354 ? 98.594  2.398   105.886 1.00 128.44 ? 1354 SER B C   1 
ATOM   22732 O  O   . SER C 1 1354 ? 98.575  2.400   104.639 1.00 129.78 ? 1354 SER B O   1 
ATOM   22733 C  CB  . SER C 1 1354 ? 100.411 3.314   107.337 1.00 134.00 ? 1354 SER B CB  1 
ATOM   22734 O  OG  . SER C 1 1354 ? 100.622 4.364   106.409 1.00 135.22 ? 1354 SER B OG  1 
ATOM   22735 N  N   . GLY C 1 1355 ? 97.537  2.724   106.635 1.00 140.60 ? 1355 GLY B N   1 
ATOM   22736 C  CA  . GLY C 1 1355 ? 96.241  3.049   106.060 1.00 139.02 ? 1355 GLY B CA  1 
ATOM   22737 C  C   . GLY C 1 1355 ? 95.366  1.832   105.803 1.00 139.46 ? 1355 GLY B C   1 
ATOM   22738 O  O   . GLY C 1 1355 ? 95.468  0.807   106.496 1.00 141.74 ? 1355 GLY B O   1 
ATOM   22739 N  N   . LEU C 1 1356 ? 94.533  1.933   104.773 1.00 146.69 ? 1356 LEU B N   1 
ATOM   22740 C  CA  . LEU C 1 1356 ? 93.472  0.966   104.527 1.00 147.53 ? 1356 LEU B CA  1 
ATOM   22741 C  C   . LEU C 1 1356 ? 93.226  0.680   103.040 1.00 157.17 ? 1356 LEU B C   1 
ATOM   22742 O  O   . LEU C 1 1356 ? 92.980  1.604   102.263 1.00 162.23 ? 1356 LEU B O   1 
ATOM   22743 C  CB  . LEU C 1 1356 ? 92.188  1.521   105.121 1.00 143.96 ? 1356 LEU B CB  1 
ATOM   22744 C  CG  . LEU C 1 1356 ? 91.914  1.036   106.517 1.00 138.29 ? 1356 LEU B CG  1 
ATOM   22745 C  CD1 . LEU C 1 1356 ? 90.880  1.924   107.150 1.00 133.84 ? 1356 LEU B CD1 1 
ATOM   22746 C  CD2 . LEU C 1 1356 ? 91.429  -0.372  106.375 1.00 136.74 ? 1356 LEU B CD2 1 
ATOM   22747 N  N   . ALA C 1 1357 ? 93.249  -0.592  102.640 1.00 179.71 ? 1357 ALA B N   1 
ATOM   22748 C  CA  . ALA C 1 1357 ? 93.004  -0.942  101.231 1.00 174.94 ? 1357 ALA B CA  1 
ATOM   22749 C  C   . ALA C 1 1357 ? 91.912  -1.992  101.048 1.00 171.30 ? 1357 ALA B C   1 
ATOM   22750 O  O   . ALA C 1 1357 ? 92.045  -3.109  101.541 1.00 169.13 ? 1357 ALA B O   1 
ATOM   22751 C  CB  . ALA C 1 1357 ? 94.284  -1.416  100.567 1.00 173.63 ? 1357 ALA B CB  1 
ATOM   22752 N  N   . THR C 1 1358 ? 90.846  -1.637  100.331 1.00 140.55 ? 1358 THR B N   1 
ATOM   22753 C  CA  . THR C 1 1358 ? 89.764  -2.579  100.059 1.00 139.22 ? 1358 THR B CA  1 
ATOM   22754 C  C   . THR C 1 1358 ? 89.998  -3.376  98.766  1.00 142.98 ? 1358 THR B C   1 
ATOM   22755 O  O   . THR C 1 1358 ? 89.730  -2.891  97.675  1.00 144.21 ? 1358 THR B O   1 
ATOM   22756 C  CB  . THR C 1 1358 ? 88.389  -1.875  100.009 1.00 158.76 ? 1358 THR B CB  1 
ATOM   22757 O  OG1 . THR C 1 1358 ? 88.575  -0.458  99.965  1.00 158.82 ? 1358 THR B OG1 1 
ATOM   22758 C  CG2 . THR C 1 1358 ? 87.574  -2.222  101.234 1.00 156.01 ? 1358 THR B CG2 1 
ATOM   22759 N  N   . VAL C 1 1359 ? 90.523  -4.589  98.901  1.00 119.05 ? 1359 VAL B N   1 
ATOM   22760 C  CA  . VAL C 1 1359 ? 90.679  -5.505  97.781  1.00 125.52 ? 1359 VAL B CA  1 
ATOM   22761 C  C   . VAL C 1 1359 ? 89.300  -6.110  97.468  1.00 130.70 ? 1359 VAL B C   1 
ATOM   22762 O  O   . VAL C 1 1359 ? 88.796  -6.943  98.221  1.00 127.58 ? 1359 VAL B O   1 
ATOM   22763 C  CB  . VAL C 1 1359 ? 91.717  -6.627  98.118  1.00 121.55 ? 1359 VAL B CB  1 
ATOM   22764 C  CG1 . VAL C 1 1359 ? 91.678  -7.734  97.118  1.00 123.67 ? 1359 VAL B CG1 1 
ATOM   22765 C  CG2 . VAL C 1 1359 ? 93.109  -6.067  98.163  1.00 122.33 ? 1359 VAL B CG2 1 
ATOM   22766 N  N   . HIS C 1 1360 ? 88.659  -5.662  96.393  1.00 138.47 ? 1360 HIS B N   1 
ATOM   22767 C  CA  . HIS C 1 1360 ? 87.466  -6.349  95.915  1.00 141.96 ? 1360 HIS B CA  1 
ATOM   22768 C  C   . HIS C 1 1360 ? 87.791  -7.175  94.700  1.00 144.93 ? 1360 HIS B C   1 
ATOM   22769 O  O   . HIS C 1 1360 ? 88.616  -6.801  93.865  1.00 149.12 ? 1360 HIS B O   1 
ATOM   22770 C  CB  . HIS C 1 1360 ? 86.366  -5.391  95.513  1.00 145.61 ? 1360 HIS B CB  1 
ATOM   22771 C  CG  . HIS C 1 1360 ? 85.597  -4.816  96.656  1.00 144.47 ? 1360 HIS B CG  1 
ATOM   22772 N  ND1 . HIS C 1 1360 ? 85.734  -3.504  97.055  1.00 142.81 ? 1360 HIS B ND1 1 
ATOM   22773 C  CD2 . HIS C 1 1360 ? 84.645  -5.360  97.449  1.00 143.49 ? 1360 HIS B CD2 1 
ATOM   22774 C  CE1 . HIS C 1 1360 ? 84.907  -3.264  98.057  1.00 141.49 ? 1360 HIS B CE1 1 
ATOM   22775 N  NE2 . HIS C 1 1360 ? 84.240  -4.373  98.317  1.00 142.29 ? 1360 HIS B NE2 1 
ATOM   22776 N  N   . VAL C 1 1361 ? 87.080  -8.278  94.568  1.00 137.96 ? 1361 VAL B N   1 
ATOM   22777 C  CA  . VAL C 1 1361 ? 87.314  -9.162  93.450  1.00 140.51 ? 1361 VAL B CA  1 
ATOM   22778 C  C   . VAL C 1 1361 ? 86.014  -9.882  93.060  1.00 142.75 ? 1361 VAL B C   1 
ATOM   22779 O  O   . VAL C 1 1361 ? 85.509  -10.773 93.784  1.00 141.95 ? 1361 VAL B O   1 
ATOM   22780 C  CB  . VAL C 1 1361 ? 88.519  -10.110 93.715  1.00 138.43 ? 1361 VAL B CB  1 
ATOM   22781 C  CG1 . VAL C 1 1361 ? 88.163  -11.557 93.486  1.00 133.17 ? 1361 VAL B CG1 1 
ATOM   22782 C  CG2 . VAL C 1 1361 ? 89.685  -9.702  92.848  1.00 133.51 ? 1361 VAL B CG2 1 
ATOM   22783 N  N   . THR C 1 1362 ? 85.481  -9.426  91.916  1.00 114.62 ? 1362 THR B N   1 
ATOM   22784 C  CA  . THR C 1 1362 ? 84.211  -9.864  91.356  1.00 116.31 ? 1362 THR B CA  1 
ATOM   22785 C  C   . THR C 1 1362 ? 84.505  -10.763 90.150  1.00 117.44 ? 1362 THR B C   1 
ATOM   22786 O  O   . THR C 1 1362 ? 84.984  -10.313 89.116  1.00 117.87 ? 1362 THR B O   1 
ATOM   22787 C  CB  . THR C 1 1362 ? 83.284  -8.645  91.074  1.00 117.04 ? 1362 THR B CB  1 
ATOM   22788 O  OG1 . THR C 1 1362 ? 81.933  -9.070  90.828  1.00 118.57 ? 1362 THR B OG1 1 
ATOM   22789 C  CG2 . THR C 1 1362 ? 83.820  -7.836  89.947  1.00 117.42 ? 1362 THR B CG2 1 
ATOM   22790 N  N   . THR C 1 1363 ? 84.286  -12.059 90.378  1.00 126.00 ? 1363 THR B N   1 
ATOM   22791 C  CA  . THR C 1 1363 ? 84.549  -13.144 89.438  1.00 126.63 ? 1363 THR B CA  1 
ATOM   22792 C  C   . THR C 1 1363 ? 83.237  -13.567 88.785  1.00 134.97 ? 1363 THR B C   1 
ATOM   22793 O  O   . THR C 1 1363 ? 82.260  -13.869 89.471  1.00 135.67 ? 1363 THR B O   1 
ATOM   22794 C  CB  . THR C 1 1363 ? 85.191  -14.398 90.128  1.00 183.12 ? 1363 THR B CB  1 
ATOM   22795 O  OG1 . THR C 1 1363 ? 84.175  -15.248 90.680  1.00 182.70 ? 1363 THR B OG1 1 
ATOM   22796 C  CG2 . THR C 1 1363 ? 86.157  -14.000 91.229  1.00 180.56 ? 1363 THR B CG2 1 
ATOM   22797 N  N   . VAL C 1 1364 ? 83.220  -13.587 87.453  1.00 121.98 ? 1364 VAL B N   1 
ATOM   22798 C  CA  . VAL C 1 1364 ? 82.021  -13.949 86.699  1.00 123.90 ? 1364 VAL B CA  1 
ATOM   22799 C  C   . VAL C 1 1364 ? 82.158  -15.181 85.823  1.00 125.04 ? 1364 VAL B C   1 
ATOM   22800 O  O   . VAL C 1 1364 ? 83.175  -15.433 85.176  1.00 124.87 ? 1364 VAL B O   1 
ATOM   22801 C  CB  . VAL C 1 1364 ? 81.537  -12.816 85.815  1.00 124.86 ? 1364 VAL B CB  1 
ATOM   22802 C  CG1 . VAL C 1 1364 ? 80.380  -13.318 84.989  1.00 126.94 ? 1364 VAL B CG1 1 
ATOM   22803 C  CG2 . VAL C 1 1364 ? 81.123  -11.624 86.658  1.00 124.06 ? 1364 VAL B CG2 1 
ATOM   22804 N  N   . VAL C 1 1365 ? 81.095  -15.946 85.782  1.00 167.15 ? 1365 VAL B N   1 
ATOM   22805 C  CA  . VAL C 1 1365 ? 81.197  -17.184 85.084  1.00 170.87 ? 1365 VAL B CA  1 
ATOM   22806 C  C   . VAL C 1 1365 ? 79.834  -17.522 84.492  1.00 180.37 ? 1365 VAL B C   1 
ATOM   22807 O  O   . VAL C 1 1365 ? 78.806  -17.090 85.006  1.00 182.79 ? 1365 VAL B O   1 
ATOM   22808 C  CB  . VAL C 1 1365 ? 81.755  -18.253 86.047  1.00 164.14 ? 1365 VAL B CB  1 
ATOM   22809 C  CG1 . VAL C 1 1365 ? 80.651  -18.854 86.920  1.00 162.37 ? 1365 VAL B CG1 1 
ATOM   22810 C  CG2 . VAL C 1 1365 ? 82.505  -19.319 85.282  1.00 164.87 ? 1365 VAL B CG2 1 
ATOM   22811 N  N   . HIS C 1 1366 ? 79.827  -18.241 83.374  1.00 176.75 ? 1366 HIS B N   1 
ATOM   22812 C  CA  . HIS C 1 1366 ? 78.575  -18.638 82.742  1.00 178.98 ? 1366 HIS B CA  1 
ATOM   22813 C  C   . HIS C 1 1366 ? 78.274  -20.096 83.059  1.00 176.07 ? 1366 HIS B C   1 
ATOM   22814 O  O   . HIS C 1 1366 ? 79.126  -20.979 82.878  1.00 176.17 ? 1366 HIS B O   1 
ATOM   22815 C  CB  . HIS C 1 1366 ? 78.645  -18.412 81.231  1.00 184.60 ? 1366 HIS B CB  1 
ATOM   22816 C  CG  . HIS C 1 1366 ? 79.053  -17.037 80.848  1.00 186.35 ? 1366 HIS B CG  1 
ATOM   22817 N  ND1 . HIS C 1 1366 ? 80.344  -16.547 81.051  1.00 184.99 ? 1366 HIS B ND1 1 
ATOM   22818 C  CD2 . HIS C 1 1366 ? 78.381  -16.014 80.266  1.00 190.10 ? 1366 HIS B CD2 1 
ATOM   22819 C  CE1 . HIS C 1 1366 ? 80.422  -15.318 80.627  1.00 186.34 ? 1366 HIS B CE1 1 
ATOM   22820 N  NE2 . HIS C 1 1366 ? 79.235  -14.954 80.138  1.00 189.53 ? 1366 HIS B NE2 1 
ATOM   22821 N  N   . LYS C 1 1367 ? 77.064  -20.343 83.550  1.00 169.73 ? 1367 LYS B N   1 
ATOM   22822 C  CA  . LYS C 1 1367 ? 76.634  -21.712 83.825  1.00 173.23 ? 1367 LYS B CA  1 
ATOM   22823 C  C   . LYS C 1 1367 ? 75.446  -22.185 82.981  1.00 175.85 ? 1367 LYS B C   1 
ATOM   22824 O  O   . LYS C 1 1367 ? 74.832  -21.416 82.256  1.00 177.87 ? 1367 LYS B O   1 
ATOM   22825 C  CB  . LYS C 1 1367 ? 76.410  -21.961 85.329  1.00 174.52 ? 1367 LYS B CB  1 
ATOM   22826 C  CG  . LYS C 1 1367 ? 75.677  -20.875 86.103  1.00 175.19 ? 1367 LYS B CG  1 
ATOM   22827 C  CD  . LYS C 1 1367 ? 75.779  -21.153 87.599  1.00 173.62 ? 1367 LYS B CD  1 
ATOM   22828 C  CE  . LYS C 1 1367 ? 77.219  -21.461 87.987  1.00 171.95 ? 1367 LYS B CE  1 
ATOM   22829 N  NZ  . LYS C 1 1367 ? 77.441  -21.323 89.453  1.00 169.72 ? 1367 LYS B NZ  1 
ATOM   22830 N  N   . THR C 1 1368 ? 75.143  -23.468 83.093  1.00 194.09 ? 1368 THR B N   1 
ATOM   22831 C  CA  . THR C 1 1368 ? 74.206  -24.119 82.203  1.00 196.41 ? 1368 THR B CA  1 
ATOM   22832 C  C   . THR C 1 1368 ? 72.892  -24.517 82.889  1.00 198.29 ? 1368 THR B C   1 
ATOM   22833 O  O   . THR C 1 1368 ? 71.967  -25.008 82.235  1.00 204.40 ? 1368 THR B O   1 
ATOM   22834 C  CB  . THR C 1 1368 ? 74.834  -25.392 81.641  1.00 200.60 ? 1368 THR B CB  1 
ATOM   22835 O  OG1 . THR C 1 1368 ? 74.804  -26.410 82.648  1.00 203.01 ? 1368 THR B OG1 1 
ATOM   22836 C  CG2 . THR C 1 1368 ? 76.272  -25.141 81.246  1.00 196.32 ? 1368 THR B CG2 1 
ATOM   22837 N  N   . SER C 1 1369 ? 72.802  -24.322 84.203  1.00 177.31 ? 1369 SER B N   1 
ATOM   22838 C  CA  . SER C 1 1369 ? 71.654  -24.837 84.956  1.00 180.27 ? 1369 SER B CA  1 
ATOM   22839 C  C   . SER C 1 1369 ? 71.258  -24.000 86.180  1.00 177.47 ? 1369 SER B C   1 
ATOM   22840 O  O   . SER C 1 1369 ? 72.116  -23.507 86.912  1.00 169.88 ? 1369 SER B O   1 
ATOM   22841 C  CB  . SER C 1 1369 ? 71.918  -26.280 85.401  1.00 184.58 ? 1369 SER B CB  1 
ATOM   22842 O  OG  . SER C 1 1369 ? 72.180  -27.129 84.300  1.00 190.59 ? 1369 SER B OG  1 
ATOM   22843 N  N   . THR C 1 1370 ? 69.947  -23.855 86.386  1.00 192.84 ? 1370 THR B N   1 
ATOM   22844 C  CA  . THR C 1 1370 ? 69.373  -23.259 87.597  1.00 195.48 ? 1370 THR B CA  1 
ATOM   22845 C  C   . THR C 1 1370 ? 68.878  -24.366 88.522  1.00 208.79 ? 1370 THR B C   1 
ATOM   22846 O  O   . THR C 1 1370 ? 68.411  -24.101 89.628  1.00 209.58 ? 1370 THR B O   1 
ATOM   22847 C  CB  . THR C 1 1370 ? 68.182  -22.320 87.279  1.00 191.57 ? 1370 THR B CB  1 
ATOM   22848 O  OG1 . THR C 1 1370 ? 68.666  -21.136 86.650  1.00 184.59 ? 1370 THR B OG1 1 
ATOM   22849 C  CG2 . THR C 1 1370 ? 67.437  -21.908 88.540  1.00 189.63 ? 1370 THR B CG2 1 
ATOM   22850 N  N   . SER C 1 1371 ? 68.979  -25.612 88.067  1.00 234.87 ? 1371 SER B N   1 
ATOM   22851 C  CA  . SER C 1 1371 ? 68.566  -26.752 88.880  1.00 247.81 ? 1371 SER B CA  1 
ATOM   22852 C  C   . SER C 1 1371 ? 69.070  -26.611 90.319  1.00 250.51 ? 1371 SER B C   1 
ATOM   22853 O  O   . SER C 1 1371 ? 68.337  -26.863 91.274  1.00 254.37 ? 1371 SER B O   1 
ATOM   22854 C  CB  . SER C 1 1371 ? 69.086  -28.052 88.273  1.00 255.88 ? 1371 SER B CB  1 
ATOM   22855 O  OG  . SER C 1 1371 ? 70.501  -28.091 88.288  1.00 255.59 ? 1371 SER B OG  1 
ATOM   22856 N  N   . GLU C 1 1372 ? 70.324  -26.200 90.465  1.00 260.61 ? 1372 GLU B N   1 
ATOM   22857 C  CA  . GLU C 1 1372 ? 70.914  -25.968 91.776  1.00 261.13 ? 1372 GLU B CA  1 
ATOM   22858 C  C   . GLU C 1 1372 ? 70.104  -24.967 92.605  1.00 249.72 ? 1372 GLU B C   1 
ATOM   22859 O  O   . GLU C 1 1372 ? 69.426  -25.337 93.570  1.00 251.74 ? 1372 GLU B O   1 
ATOM   22860 C  CB  . GLU C 1 1372 ? 72.338  -25.431 91.598  1.00 268.47 ? 1372 GLU B CB  1 
ATOM   22861 C  CG  . GLU C 1 1372 ? 72.451  -24.348 90.508  1.00 275.31 ? 1372 GLU B CG  1 
ATOM   22862 C  CD  . GLU C 1 1372 ? 73.716  -23.499 90.607  1.00 278.29 ? 1372 GLU B CD  1 
ATOM   22863 O  OE1 . GLU C 1 1372 ? 74.661  -23.908 91.314  1.00 281.59 ? 1372 GLU B OE1 1 
ATOM   22864 O  OE2 . GLU C 1 1372 ? 73.766  -22.420 89.971  1.00 276.41 ? 1372 GLU B OE2 1 
ATOM   22865 N  N   . GLU C 1 1373 ? 70.174  -23.707 92.172  1.00 221.52 ? 1373 GLU B N   1 
ATOM   22866 C  CA  . GLU C 1 1373 ? 69.714  -22.515 92.890  1.00 208.84 ? 1373 GLU B CA  1 
ATOM   22867 C  C   . GLU C 1 1373 ? 68.366  -22.614 93.612  1.00 206.72 ? 1373 GLU B C   1 
ATOM   22868 O  O   . GLU C 1 1373 ? 67.646  -23.612 93.527  1.00 211.45 ? 1373 GLU B O   1 
ATOM   22869 C  CB  . GLU C 1 1373 ? 69.705  -21.307 91.932  1.00 199.01 ? 1373 GLU B CB  1 
ATOM   22870 C  CG  . GLU C 1 1373 ? 71.054  -21.015 91.237  1.00 190.25 ? 1373 GLU B CG  1 
ATOM   22871 C  CD  . GLU C 1 1373 ? 71.012  -19.804 90.290  1.00 180.65 ? 1373 GLU B CD  1 
ATOM   22872 O  OE1 . GLU C 1 1373 ? 69.923  -19.211 90.106  1.00 178.08 ? 1373 GLU B OE1 1 
ATOM   22873 O  OE2 . GLU C 1 1373 ? 72.078  -19.443 89.732  1.00 174.88 ? 1373 GLU B OE2 1 
ATOM   22874 N  N   . VAL C 1 1374 ? 68.056  -21.545 94.335  1.00 165.59 ? 1374 VAL B N   1 
ATOM   22875 C  CA  . VAL C 1 1374 ? 66.851  -21.445 95.134  1.00 163.09 ? 1374 VAL B CA  1 
ATOM   22876 C  C   . VAL C 1 1374 ? 65.744  -20.835 94.348  1.00 161.89 ? 1374 VAL B C   1 
ATOM   22877 O  O   . VAL C 1 1374 ? 65.889  -19.718 93.860  1.00 158.97 ? 1374 VAL B O   1 
ATOM   22878 C  CB  . VAL C 1 1374 ? 67.009  -20.368 96.189  1.00 157.57 ? 1374 VAL B CB  1 
ATOM   22879 C  CG1 . VAL C 1 1374 ? 66.080  -20.657 97.357  1.00 160.35 ? 1374 VAL B CG1 1 
ATOM   22880 C  CG2 . VAL C 1 1374 ? 68.483  -20.184 96.596  1.00 154.12 ? 1374 VAL B CG2 1 
ATOM   22881 N  N   . CYS C 1 1375 ? 64.600  -21.483 94.271  1.00 242.74 ? 1375 CYS B N   1 
ATOM   22882 C  CA  . CYS C 1 1375 ? 63.480  -20.721 93.755  1.00 241.15 ? 1375 CYS B CA  1 
ATOM   22883 C  C   . CYS C 1 1375 ? 62.687  -20.022 94.868  1.00 241.00 ? 1375 CYS B C   1 
ATOM   22884 O  O   . CYS C 1 1375 ? 62.266  -20.637 95.853  1.00 241.85 ? 1375 CYS B O   1 
ATOM   22885 C  CB  . CYS C 1 1375 ? 62.627  -21.516 92.757  1.00 244.99 ? 1375 CYS B CB  1 
ATOM   22886 S  SG  . CYS C 1 1375 ? 63.320  -21.455 91.060  1.00 323.71 ? 1375 CYS B SG  1 
ATOM   22887 N  N   . SER C 1 1376 ? 62.573  -18.706 94.713  1.00 168.74 ? 1376 SER B N   1 
ATOM   22888 C  CA  . SER C 1 1376 ? 61.736  -17.868 95.546  1.00 169.36 ? 1376 SER B CA  1 
ATOM   22889 C  C   . SER C 1 1376 ? 60.536  -17.450 94.707  1.00 176.23 ? 1376 SER B C   1 
ATOM   22890 O  O   . SER C 1 1376 ? 59.596  -16.831 95.209  1.00 178.46 ? 1376 SER B O   1 
ATOM   22891 C  CB  . SER C 1 1376 ? 62.519  -16.633 95.965  1.00 161.39 ? 1376 SER B CB  1 
ATOM   22892 O  OG  . SER C 1 1376 ? 63.911  -16.847 95.808  1.00 155.64 ? 1376 SER B OG  1 
ATOM   22893 N  N   . PHE C 1 1377 ? 60.588  -17.790 93.418  1.00 198.78 ? 1377 PHE B N   1 
ATOM   22894 C  CA  . PHE C 1 1377 ? 59.476  -17.555 92.486  1.00 199.83 ? 1377 PHE B CA  1 
ATOM   22895 C  C   . PHE C 1 1377 ? 59.045  -18.757 91.624  1.00 208.19 ? 1377 PHE B C   1 
ATOM   22896 O  O   . PHE C 1 1377 ? 59.858  -19.405 90.955  1.00 208.90 ? 1377 PHE B O   1 
ATOM   22897 C  CB  . PHE C 1 1377 ? 59.763  -16.363 91.588  1.00 193.94 ? 1377 PHE B CB  1 
ATOM   22898 C  CG  . PHE C 1 1377 ? 59.507  -15.067 92.247  1.00 191.02 ? 1377 PHE B CG  1 
ATOM   22899 C  CD1 . PHE C 1 1377 ? 58.218  -14.581 92.364  1.00 193.83 ? 1377 PHE B CD1 1 
ATOM   22900 C  CD2 . PHE C 1 1377 ? 60.547  -14.340 92.775  1.00 187.02 ? 1377 PHE B CD2 1 
ATOM   22901 C  CE1 . PHE C 1 1377 ? 57.971  -13.381 92.987  1.00 190.69 ? 1377 PHE B CE1 1 
ATOM   22902 C  CE2 . PHE C 1 1377 ? 60.313  -13.136 93.394  1.00 183.95 ? 1377 PHE B CE2 1 
ATOM   22903 C  CZ  . PHE C 1 1377 ? 59.021  -12.653 93.502  1.00 185.89 ? 1377 PHE B CZ  1 
ATOM   22904 N  N   . TYR C 1 1378 ? 57.746  -19.037 91.657  1.00 214.13 ? 1378 TYR B N   1 
ATOM   22905 C  CA  . TYR C 1 1378 ? 57.148  -20.023 90.783  1.00 217.07 ? 1378 TYR B CA  1 
ATOM   22906 C  C   . TYR C 1 1378 ? 56.932  -19.385 89.416  1.00 215.58 ? 1378 TYR B C   1 
ATOM   22907 O  O   . TYR C 1 1378 ? 56.444  -18.259 89.321  1.00 211.50 ? 1378 TYR B O   1 
ATOM   22908 C  CB  . TYR C 1 1378 ? 55.808  -20.495 91.358  1.00 220.71 ? 1378 TYR B CB  1 
ATOM   22909 C  CG  . TYR C 1 1378 ? 55.911  -21.403 92.564  1.00 218.98 ? 1378 TYR B CG  1 
ATOM   22910 C  CD1 . TYR C 1 1378 ? 56.690  -22.548 92.522  1.00 218.28 ? 1378 TYR B CD1 1 
ATOM   22911 C  CD2 . TYR C 1 1378 ? 55.201  -21.131 93.729  1.00 218.51 ? 1378 TYR B CD2 1 
ATOM   22912 C  CE1 . TYR C 1 1378 ? 56.786  -23.392 93.613  1.00 219.56 ? 1378 TYR B CE1 1 
ATOM   22913 C  CE2 . TYR C 1 1378 ? 55.288  -21.970 94.832  1.00 219.50 ? 1378 TYR B CE2 1 
ATOM   22914 C  CZ  . TYR C 1 1378 ? 56.086  -23.105 94.769  1.00 219.79 ? 1378 TYR B CZ  1 
ATOM   22915 O  OH  . TYR C 1 1378 ? 56.200  -23.963 95.850  1.00 220.32 ? 1378 TYR B OH  1 
ATOM   22916 N  N   . LEU C 1 1379 ? 57.294  -20.113 88.363  1.00 208.84 ? 1379 LEU B N   1 
ATOM   22917 C  CA  . LEU C 1 1379 ? 57.166  -19.623 86.991  1.00 214.40 ? 1379 LEU B CA  1 
ATOM   22918 C  C   . LEU C 1 1379 ? 56.582  -20.649 86.014  1.00 228.00 ? 1379 LEU B C   1 
ATOM   22919 O  O   . LEU C 1 1379 ? 56.457  -21.843 86.314  1.00 234.25 ? 1379 LEU B O   1 
ATOM   22920 C  CB  . LEU C 1 1379 ? 58.523  -19.188 86.449  1.00 207.31 ? 1379 LEU B CB  1 
ATOM   22921 C  CG  . LEU C 1 1379 ? 59.228  -18.082 87.198  1.00 199.74 ? 1379 LEU B CG  1 
ATOM   22922 C  CD1 . LEU C 1 1379 ? 60.537  -17.778 86.500  1.00 194.39 ? 1379 LEU B CD1 1 
ATOM   22923 C  CD2 . LEU C 1 1379 ? 58.320  -16.876 87.241  1.00 199.39 ? 1379 LEU B CD2 1 
ATOM   22924 N  N   . LYS C 1 1380 ? 56.235  -20.148 84.833  1.00 240.20 ? 1380 LYS B N   1 
ATOM   22925 C  CA  . LYS C 1 1380 ? 55.989  -20.967 83.653  1.00 246.30 ? 1380 LYS B CA  1 
ATOM   22926 C  C   . LYS C 1 1380 ? 56.127  -20.060 82.418  1.00 243.11 ? 1380 LYS B C   1 
ATOM   22927 O  O   . LYS C 1 1380 ? 55.526  -18.981 82.358  1.00 240.48 ? 1380 LYS B O   1 
ATOM   22928 C  CB  . LYS C 1 1380 ? 54.630  -21.688 83.723  1.00 238.13 ? 1380 LYS B CB  1 
ATOM   22929 C  CG  . LYS C 1 1380 ? 53.464  -20.850 84.239  1.00 244.93 ? 1380 LYS B CG  1 
ATOM   22930 C  CD  . LYS C 1 1380 ? 52.174  -21.670 84.352  1.00 250.40 ? 1380 LYS B CD  1 
ATOM   22931 C  CE  . LYS C 1 1380 ? 50.977  -20.795 84.715  1.00 233.81 ? 1380 LYS B CE  1 
ATOM   22932 N  NZ  . LYS C 1 1380 ? 49.697  -21.558 84.724  1.00 240.63 ? 1380 LYS B NZ  1 
ATOM   22933 N  N   . ILE C 1 1381 ? 56.965  -20.484 81.468  1.00 181.92 ? 1381 ILE B N   1 
ATOM   22934 C  CA  . ILE C 1 1381 ? 57.160  -19.769 80.203  1.00 178.06 ? 1381 ILE B CA  1 
ATOM   22935 C  C   . ILE C 1 1381 ? 57.126  -20.730 79.012  1.00 189.61 ? 1381 ILE B C   1 
ATOM   22936 O  O   . ILE C 1 1381 ? 57.688  -21.832 79.065  1.00 195.74 ? 1381 ILE B O   1 
ATOM   22937 C  CB  . ILE C 1 1381 ? 58.494  -19.029 80.140  1.00 162.67 ? 1381 ILE B CB  1 
ATOM   22938 C  CG1 . ILE C 1 1381 ? 58.326  -17.745 79.377  1.00 158.89 ? 1381 ILE B CG1 1 
ATOM   22939 C  CG2 . ILE C 1 1381 ? 59.526  -19.843 79.399  1.00 159.62 ? 1381 ILE B CG2 1 
ATOM   22940 C  CD1 . ILE C 1 1381 ? 59.604  -17.106 79.116  1.00 153.01 ? 1381 ILE B CD1 1 
ATOM   22941 N  N   . ASP C 1 1382 ? 56.470  -20.295 77.938  1.00 252.76 ? 1382 ASP B N   1 
ATOM   22942 C  CA  . ASP C 1 1382 ? 56.382  -21.068 76.704  1.00 259.34 ? 1382 ASP B CA  1 
ATOM   22943 C  C   . ASP C 1 1382 ? 55.909  -20.179 75.560  1.00 260.80 ? 1382 ASP B C   1 
ATOM   22944 O  O   . ASP C 1 1382 ? 55.195  -19.195 75.767  1.00 257.35 ? 1382 ASP B O   1 
ATOM   22945 C  CB  . ASP C 1 1382 ? 55.455  -22.274 76.872  1.00 270.03 ? 1382 ASP B CB  1 
ATOM   22946 C  CG  . ASP C 1 1382 ? 54.041  -21.878 77.245  1.00 276.24 ? 1382 ASP B CG  1 
ATOM   22947 O  OD1 . ASP C 1 1382 ? 53.790  -21.601 78.436  1.00 274.15 ? 1382 ASP B OD1 1 
ATOM   22948 O  OD2 . ASP C 1 1382 ? 53.177  -21.848 76.345  1.00 283.28 ? 1382 ASP B OD2 1 
ATOM   22949 N  N   . THR C 1 1383 ? 56.323  -20.525 74.352  1.00 218.62 ? 1383 THR B N   1 
ATOM   22950 C  CA  . THR C 1 1383 ? 56.016  -19.704 73.200  1.00 220.88 ? 1383 THR B CA  1 
ATOM   22951 C  C   . THR C 1 1383 ? 54.810  -20.276 72.418  1.00 228.69 ? 1383 THR B C   1 
ATOM   22952 O  O   . THR C 1 1383 ? 54.833  -21.425 71.961  1.00 232.03 ? 1383 THR B O   1 
ATOM   22953 C  CB  . THR C 1 1383 ? 57.288  -19.509 72.352  1.00 218.21 ? 1383 THR B CB  1 
ATOM   22954 O  OG1 . THR C 1 1383 ? 58.161  -20.631 72.541  1.00 219.31 ? 1383 THR B OG1 1 
ATOM   22955 C  CG2 . THR C 1 1383 ? 58.023  -18.280 72.825  1.00 209.53 ? 1383 THR B CG2 1 
ATOM   22956 N  N   . GLN C 1 1384 ? 53.745  -19.480 72.306  1.00 228.15 ? 1384 GLN B N   1 
ATOM   22957 C  CA  . GLN C 1 1384 ? 52.491  -19.926 71.685  1.00 239.46 ? 1384 GLN B CA  1 
ATOM   22958 C  C   . GLN C 1 1384 ? 52.418  -19.611 70.177  1.00 244.35 ? 1384 GLN B C   1 
ATOM   22959 O  O   . GLN C 1 1384 ? 53.375  -19.084 69.611  1.00 239.75 ? 1384 GLN B O   1 
ATOM   22960 C  CB  . GLN C 1 1384 ? 51.289  -19.351 72.449  1.00 242.54 ? 1384 GLN B CB  1 
ATOM   22961 C  CG  . GLN C 1 1384 ? 51.173  -19.886 73.873  1.00 244.71 ? 1384 GLN B CG  1 
ATOM   22962 C  CD  . GLN C 1 1384 ? 49.897  -19.458 74.558  1.00 249.45 ? 1384 GLN B CD  1 
ATOM   22963 O  OE1 . GLN C 1 1384 ? 49.451  -18.336 74.396  1.00 249.13 ? 1384 GLN B OE1 1 
ATOM   22964 N  NE2 . GLN C 1 1384 ? 49.307  -20.356 75.333  1.00 253.67 ? 1384 GLN B NE2 1 
ATOM   22965 N  N   . ASP C 1 1385 ? 51.300  -19.938 69.525  1.00 285.12 ? 1385 ASP B N   1 
ATOM   22966 C  CA  . ASP C 1 1385 ? 51.167  -19.664 68.089  1.00 289.92 ? 1385 ASP B CA  1 
ATOM   22967 C  C   . ASP C 1 1385 ? 49.879  -18.938 67.662  1.00 293.24 ? 1385 ASP B C   1 
ATOM   22968 O  O   . ASP C 1 1385 ? 49.849  -18.294 66.610  1.00 293.41 ? 1385 ASP B O   1 
ATOM   22969 C  CB  . ASP C 1 1385 ? 51.378  -20.938 67.268  1.00 296.22 ? 1385 ASP B CB  1 
ATOM   22970 C  CG  . ASP C 1 1385 ? 52.822  -21.404 67.283  1.00 293.23 ? 1385 ASP B CG  1 
ATOM   22971 O  OD1 . ASP C 1 1385 ? 53.687  -20.680 66.742  1.00 289.76 ? 1385 ASP B OD1 1 
ATOM   22972 O  OD2 . ASP C 1 1385 ? 53.096  -22.489 67.838  1.00 294.75 ? 1385 ASP B OD2 1 
ATOM   22973 N  N   . ILE C 1 1386 ? 48.831  -19.033 68.480  1.00 294.30 ? 1386 ILE B N   1 
ATOM   22974 C  CA  . ILE C 1 1386 ? 47.560  -18.343 68.225  1.00 296.70 ? 1386 ILE B CA  1 
ATOM   22975 C  C   . ILE C 1 1386 ? 47.698  -16.811 68.265  1.00 288.50 ? 1386 ILE B C   1 
ATOM   22976 O  O   . ILE C 1 1386 ? 48.044  -16.159 67.271  1.00 285.25 ? 1386 ILE B O   1 
ATOM   22977 C  CB  . ILE C 1 1386 ? 46.489  -18.764 69.263  1.00 362.77 ? 1386 ILE B CB  1 
ATOM   22978 C  CG1 . ILE C 1 1386 ? 46.567  -20.267 69.544  1.00 365.78 ? 1386 ILE B CG1 1 
ATOM   22979 C  CG2 . ILE C 1 1386 ? 45.093  -18.360 68.806  1.00 368.13 ? 1386 ILE B CG2 1 
ATOM   22980 C  CD1 . ILE C 1 1386 ? 45.641  -20.728 70.644  1.00 367.34 ? 1386 ILE B CD1 1 
ATOM   22981 N  N   . TYR C 1 1399 ? 50.759  -15.284 64.934  1.00 299.63 ? 1399 TYR B N   1 
ATOM   22982 C  CA  . TYR C 1 1399 ? 52.000  -15.717 64.305  1.00 298.51 ? 1399 TYR B CA  1 
ATOM   22983 C  C   . TYR C 1 1399 ? 52.812  -16.494 65.325  1.00 281.74 ? 1399 TYR B C   1 
ATOM   22984 O  O   . TYR C 1 1399 ? 53.077  -17.689 65.165  1.00 284.29 ? 1399 TYR B O   1 
ATOM   22985 C  CB  . TYR C 1 1399 ? 52.783  -14.497 63.806  1.00 307.74 ? 1399 TYR B CB  1 
ATOM   22986 C  CG  . TYR C 1 1399 ? 54.169  -14.777 63.237  1.00 318.71 ? 1399 TYR B CG  1 
ATOM   22987 C  CD1 . TYR C 1 1399 ? 54.412  -15.880 62.418  1.00 329.13 ? 1399 TYR B CD1 1 
ATOM   22988 C  CD2 . TYR C 1 1399 ? 55.230  -13.911 63.495  1.00 316.57 ? 1399 TYR B CD2 1 
ATOM   22989 C  CE1 . TYR C 1 1399 ? 55.682  -16.120 61.894  1.00 330.58 ? 1399 TYR B CE1 1 
ATOM   22990 C  CE2 . TYR C 1 1399 ? 56.495  -14.141 62.977  1.00 317.73 ? 1399 TYR B CE2 1 
ATOM   22991 C  CZ  . TYR C 1 1399 ? 56.718  -15.243 62.178  1.00 324.52 ? 1399 TYR B CZ  1 
ATOM   22992 O  OH  . TYR C 1 1399 ? 57.979  -15.464 61.666  1.00 323.58 ? 1399 TYR B OH  1 
ATOM   22993 N  N   . LYS C 1 1400 ? 53.194  -15.792 66.385  1.00 240.85 ? 1400 LYS B N   1 
ATOM   22994 C  CA  . LYS C 1 1400 ? 53.883  -16.394 67.523  1.00 222.28 ? 1400 LYS B CA  1 
ATOM   22995 C  C   . LYS C 1 1400 ? 54.079  -15.376 68.663  1.00 202.40 ? 1400 LYS B C   1 
ATOM   22996 O  O   . LYS C 1 1400 ? 54.554  -14.255 68.443  1.00 196.83 ? 1400 LYS B O   1 
ATOM   22997 C  CB  . LYS C 1 1400 ? 55.204  -17.074 67.102  1.00 217.62 ? 1400 LYS B CB  1 
ATOM   22998 C  CG  . LYS C 1 1400 ? 56.175  -16.230 66.276  1.00 212.85 ? 1400 LYS B CG  1 
ATOM   22999 C  CD  . LYS C 1 1400 ? 57.532  -16.927 66.140  1.00 208.70 ? 1400 LYS B CD  1 
ATOM   23000 C  CE  . LYS C 1 1400 ? 57.375  -18.390 65.734  1.00 213.62 ? 1400 LYS B CE  1 
ATOM   23001 N  NZ  . LYS C 1 1400 ? 58.680  -19.106 65.695  1.00 210.09 ? 1400 LYS B NZ  1 
ATOM   23002 N  N   . ARG C 1 1401 ? 53.700  -15.790 69.876  1.00 206.98 ? 1401 ARG B N   1 
ATOM   23003 C  CA  . ARG C 1 1401 ? 53.658  -14.908 71.054  1.00 191.22 ? 1401 ARG B CA  1 
ATOM   23004 C  C   . ARG C 1 1401 ? 53.991  -15.631 72.379  1.00 187.58 ? 1401 ARG B C   1 
ATOM   23005 O  O   . ARG C 1 1401 ? 53.742  -16.835 72.545  1.00 192.49 ? 1401 ARG B O   1 
ATOM   23006 C  CB  . ARG C 1 1401 ? 52.313  -14.145 71.098  1.00 184.39 ? 1401 ARG B CB  1 
ATOM   23007 C  CG  . ARG C 1 1401 ? 51.624  -13.935 72.464  1.00 174.97 ? 1401 ARG B CG  1 
ATOM   23008 C  CD  . ARG C 1 1401 ? 50.603  -15.051 72.843  1.00 176.80 ? 1401 ARG B CD  1 
ATOM   23009 N  NE  . ARG C 1 1401 ? 49.866  -14.686 74.055  1.00 174.80 ? 1401 ARG B NE  1 
ATOM   23010 C  CZ  . ARG C 1 1401 ? 48.552  -14.835 74.242  1.00 176.48 ? 1401 ARG B CZ  1 
ATOM   23011 N  NH1 . ARG C 1 1401 ? 47.771  -15.357 73.310  1.00 179.42 ? 1401 ARG B NH1 1 
ATOM   23012 N  NH2 . ARG C 1 1401 ? 48.011  -14.457 75.390  1.00 176.06 ? 1401 ARG B NH2 1 
ATOM   23013 N  N   . ILE C 1 1402 ? 54.580  -14.867 73.298  1.00 218.52 ? 1402 ILE B N   1 
ATOM   23014 C  CA  . ILE C 1 1402 ? 55.106  -15.358 74.569  1.00 211.32 ? 1402 ILE B CA  1 
ATOM   23015 C  C   . ILE C 1 1402 ? 54.148  -15.139 75.755  1.00 212.05 ? 1402 ILE B C   1 
ATOM   23016 O  O   . ILE C 1 1402 ? 53.764  -14.004 76.047  1.00 209.14 ? 1402 ILE B O   1 
ATOM   23017 C  CB  . ILE C 1 1402 ? 56.433  -14.637 74.895  1.00 199.99 ? 1402 ILE B CB  1 
ATOM   23018 C  CG1 . ILE C 1 1402 ? 57.515  -14.935 73.847  1.00 197.97 ? 1402 ILE B CG1 1 
ATOM   23019 C  CG2 . ILE C 1 1402 ? 56.935  -15.030 76.260  1.00 195.76 ? 1402 ILE B CG2 1 
ATOM   23020 C  CD1 . ILE C 1 1402 ? 58.887  -14.314 74.210  1.00 190.40 ? 1402 ILE B CD1 1 
ATOM   23021 N  N   . VAL C 1 1403 ? 53.772  -16.227 76.432  1.00 159.45 ? 1403 VAL B N   1 
ATOM   23022 C  CA  . VAL C 1 1403 ? 52.983  -16.156 77.667  1.00 161.44 ? 1403 VAL B CA  1 
ATOM   23023 C  C   . VAL C 1 1403 ? 53.766  -16.766 78.824  1.00 162.50 ? 1403 VAL B C   1 
ATOM   23024 O  O   . VAL C 1 1403 ? 53.800  -17.998 78.964  1.00 166.88 ? 1403 VAL B O   1 
ATOM   23025 C  CB  . VAL C 1 1403 ? 51.675  -16.949 77.586  1.00 168.94 ? 1403 VAL B CB  1 
ATOM   23026 C  CG1 . VAL C 1 1403 ? 50.833  -16.721 78.834  1.00 169.45 ? 1403 VAL B CG1 1 
ATOM   23027 C  CG2 . VAL C 1 1403 ? 50.906  -16.555 76.363  1.00 173.30 ? 1403 VAL B CG2 1 
ATOM   23028 N  N   . ALA C 1 1404 ? 54.372  -15.893 79.647  1.00 212.69 ? 1404 ALA B N   1 
ATOM   23029 C  CA  . ALA C 1 1404 ? 55.198  -16.252 80.816  1.00 208.32 ? 1404 ALA B CA  1 
ATOM   23030 C  C   . ALA C 1 1404 ? 54.527  -15.838 82.114  1.00 207.73 ? 1404 ALA B C   1 
ATOM   23031 O  O   . ALA C 1 1404 ? 53.969  -14.741 82.216  1.00 204.34 ? 1404 ALA B O   1 
ATOM   23032 C  CB  . ALA C 1 1404 ? 56.553  -15.586 80.725  1.00 199.38 ? 1404 ALA B CB  1 
ATOM   23033 N  N   . CYS C 1 1405 ? 54.624  -16.703 83.117  1.00 315.66 ? 1405 CYS B N   1 
ATOM   23034 C  CA  . CYS C 1 1405 ? 53.874  -16.522 84.353  1.00 317.04 ? 1405 CYS B CA  1 
ATOM   23035 C  C   . CYS C 1 1405 ? 54.765  -16.507 85.576  1.00 311.63 ? 1405 CYS B C   1 
ATOM   23036 O  O   . CYS C 1 1405 ? 55.988  -16.604 85.480  1.00 310.57 ? 1405 CYS B O   1 
ATOM   23037 C  CB  . CYS C 1 1405 ? 52.867  -17.653 84.539  1.00 324.23 ? 1405 CYS B CB  1 
ATOM   23038 S  SG  . CYS C 1 1405 ? 52.041  -18.208 83.051  1.00 348.80 ? 1405 CYS B SG  1 
ATOM   23039 N  N   . ALA C 1 1406 ? 54.124  -16.425 86.735  1.00 211.35 ? 1406 ALA B N   1 
ATOM   23040 C  CA  . ALA C 1 1406 ? 54.834  -16.331 87.988  1.00 204.36 ? 1406 ALA B CA  1 
ATOM   23041 C  C   . ALA C 1 1406 ? 53.845  -16.378 89.138  1.00 208.71 ? 1406 ALA B C   1 
ATOM   23042 O  O   . ALA C 1 1406 ? 52.730  -15.878 89.019  1.00 209.68 ? 1406 ALA B O   1 
ATOM   23043 C  CB  . ALA C 1 1406 ? 55.613  -15.035 88.031  1.00 194.66 ? 1406 ALA B CB  1 
ATOM   23044 N  N   . SER C 1 1407 ? 54.250  -16.994 90.243  1.00 226.77 ? 1407 SER B N   1 
ATOM   23045 C  CA  . SER C 1 1407 ? 53.589  -16.770 91.523  1.00 227.94 ? 1407 SER B CA  1 
ATOM   23046 C  C   . SER C 1 1407 ? 54.607  -16.737 92.624  1.00 224.02 ? 1407 SER B C   1 
ATOM   23047 O  O   . SER C 1 1407 ? 55.521  -17.556 92.665  1.00 224.34 ? 1407 SER B O   1 
ATOM   23048 C  CB  . SER C 1 1407 ? 52.586  -17.852 91.877  1.00 233.15 ? 1407 SER B CB  1 
ATOM   23049 O  OG  . SER C 1 1407 ? 52.383  -17.835 93.287  1.00 231.01 ? 1407 SER B OG  1 
ATOM   23050 N  N   . TYR C 1 1408 ? 54.427  -15.802 93.540  1.00 223.06 ? 1408 TYR B N   1 
ATOM   23051 C  CA  . TYR C 1 1408 ? 55.396  -15.625 94.598  1.00 216.56 ? 1408 TYR B CA  1 
ATOM   23052 C  C   . TYR C 1 1408 ? 55.465  -16.844 95.521  1.00 217.97 ? 1408 TYR B C   1 
ATOM   23053 O  O   . TYR C 1 1408 ? 54.460  -17.526 95.750  1.00 224.51 ? 1408 TYR B O   1 
ATOM   23054 C  CB  . TYR C 1 1408 ? 55.110  -14.352 95.381  1.00 214.13 ? 1408 TYR B CB  1 
ATOM   23055 C  CG  . TYR C 1 1408 ? 56.040  -14.221 96.524  1.00 212.26 ? 1408 TYR B CG  1 
ATOM   23056 C  CD1 . TYR C 1 1408 ? 57.377  -14.520 96.359  1.00 210.66 ? 1408 TYR B CD1 1 
ATOM   23057 C  CD2 . TYR C 1 1408 ? 55.592  -13.834 97.773  1.00 213.27 ? 1408 TYR B CD2 1 
ATOM   23058 C  CE1 . TYR C 1 1408 ? 58.262  -14.435 97.403  1.00 208.85 ? 1408 TYR B CE1 1 
ATOM   23059 C  CE2 . TYR C 1 1408 ? 56.468  -13.736 98.837  1.00 211.55 ? 1408 TYR B CE2 1 
ATOM   23060 C  CZ  . TYR C 1 1408 ? 57.813  -14.039 98.647  1.00 209.87 ? 1408 TYR B CZ  1 
ATOM   23061 O  OH  . TYR C 1 1408 ? 58.716  -13.947 99.695  1.00 207.59 ? 1408 TYR B OH  1 
ATOM   23062 N  N   . LYS C 1 1409 ? 56.672  -17.127 96.012  1.00 225.08 ? 1409 LYS B N   1 
ATOM   23063 C  CA  . LYS C 1 1409 ? 56.907  -18.184 96.993  1.00 225.30 ? 1409 LYS B CA  1 
ATOM   23064 C  C   . LYS C 1 1409 ? 57.130  -17.565 98.361  1.00 225.73 ? 1409 LYS B C   1 
ATOM   23065 O  O   . LYS C 1 1409 ? 58.251  -17.176 98.678  1.00 220.75 ? 1409 LYS B O   1 
ATOM   23066 C  CB  . LYS C 1 1409 ? 58.152  -19.010 96.625  1.00 219.52 ? 1409 LYS B CB  1 
ATOM   23067 C  CG  . LYS C 1 1409 ? 57.977  -19.955 95.440  1.00 218.43 ? 1409 LYS B CG  1 
ATOM   23068 C  CD  . LYS C 1 1409 ? 59.223  -20.821 95.159  1.00 214.09 ? 1409 LYS B CD  1 
ATOM   23069 C  CE  . LYS C 1 1409 ? 59.089  -22.243 95.735  1.00 218.32 ? 1409 LYS B CE  1 
ATOM   23070 N  NZ  . LYS C 1 1409 ? 60.054  -23.261 95.188  1.00 218.88 ? 1409 LYS B NZ  1 
ATOM   23071 N  N   . PRO C 1 1410 ? 56.069  -17.477 99.181  1.00 226.83 ? 1410 PRO B N   1 
ATOM   23072 C  CA  . PRO C 1 1410 ? 56.175  -16.896 100.527 1.00 227.56 ? 1410 PRO B CA  1 
ATOM   23073 C  C   . PRO C 1 1410 ? 57.151  -17.661 101.422 1.00 233.84 ? 1410 PRO B C   1 
ATOM   23074 O  O   . PRO C 1 1410 ? 56.976  -18.866 101.615 1.00 237.19 ? 1410 PRO B O   1 
ATOM   23075 C  CB  . PRO C 1 1410 ? 54.748  -17.025 101.079 1.00 229.48 ? 1410 PRO B CB  1 
ATOM   23076 C  CG  . PRO C 1 1410 ? 53.881  -17.106 99.879  1.00 232.36 ? 1410 PRO B CG  1 
ATOM   23077 C  CD  . PRO C 1 1410 ? 54.684  -17.859 98.855  1.00 233.42 ? 1410 PRO B CD  1 
ATOM   23078 N  N   . SER C 1 1411 ? 58.167  -16.965 101.936 1.00 248.30 ? 1411 SER B N   1 
ATOM   23079 C  CA  . SER C 1 1411 ? 59.077  -17.512 102.941 1.00 259.56 ? 1411 SER B CA  1 
ATOM   23080 C  C   . SER C 1 1411 ? 58.317  -17.675 104.244 1.00 274.88 ? 1411 SER B C   1 
ATOM   23081 O  O   . SER C 1 1411 ? 57.349  -16.961 104.495 1.00 275.57 ? 1411 SER B O   1 
ATOM   23082 C  CB  . SER C 1 1411 ? 60.269  -16.576 103.187 1.00 254.78 ? 1411 SER B CB  1 
ATOM   23083 O  OG  . SER C 1 1411 ? 61.056  -16.379 102.027 1.00 252.13 ? 1411 SER B OG  1 
ATOM   23084 N  N   . ARG C 1 1412 ? 58.767  -18.596 105.086 1.00 260.80 ? 1412 ARG B N   1 
ATOM   23085 C  CA  . ARG C 1 1412 ? 58.065  -18.858 106.329 1.00 276.54 ? 1412 ARG B CA  1 
ATOM   23086 C  C   . ARG C 1 1412 ? 57.783  -17.547 107.052 1.00 272.85 ? 1412 ARG B C   1 
ATOM   23087 O  O   . ARG C 1 1412 ? 58.490  -16.556 106.865 1.00 269.36 ? 1412 ARG B O   1 
ATOM   23088 C  CB  . ARG C 1 1412 ? 58.871  -19.803 107.217 1.00 290.91 ? 1412 ARG B CB  1 
ATOM   23089 C  CG  . ARG C 1 1412 ? 60.296  -19.345 107.447 1.00 297.92 ? 1412 ARG B CG  1 
ATOM   23090 C  CD  . ARG C 1 1412 ? 60.962  -20.122 108.570 1.00 310.20 ? 1412 ARG B CD  1 
ATOM   23091 N  NE  . ARG C 1 1412 ? 62.012  -19.326 109.198 1.00 313.60 ? 1412 ARG B NE  1 
ATOM   23092 C  CZ  . ARG C 1 1412 ? 62.727  -19.720 110.247 1.00 320.14 ? 1412 ARG B CZ  1 
ATOM   23093 N  NH1 . ARG C 1 1412 ? 62.506  -20.910 110.789 1.00 327.05 ? 1412 ARG B NH1 1 
ATOM   23094 N  NH2 . ARG C 1 1412 ? 63.662  -18.922 110.753 1.00 318.01 ? 1412 ARG B NH2 1 
ATOM   23095 N  N   . GLU C 1 1413 ? 56.731  -17.548 107.862 1.00 268.87 ? 1413 GLU B N   1 
ATOM   23096 C  CA  . GLU C 1 1413 ? 56.378  -16.390 108.669 1.00 263.90 ? 1413 GLU B CA  1 
ATOM   23097 C  C   . GLU C 1 1413 ? 55.771  -15.283 107.834 1.00 247.00 ? 1413 GLU B C   1 
ATOM   23098 O  O   . GLU C 1 1413 ? 55.212  -14.339 108.380 1.00 243.82 ? 1413 GLU B O   1 
ATOM   23099 C  CB  . GLU C 1 1413 ? 57.611  -15.842 109.390 1.00 270.50 ? 1413 GLU B CB  1 
ATOM   23100 C  CG  . GLU C 1 1413 ? 58.416  -16.890 110.141 1.00 281.92 ? 1413 GLU B CG  1 
ATOM   23101 C  CD  . GLU C 1 1413 ? 57.731  -17.371 111.411 1.00 292.75 ? 1413 GLU B CD  1 
ATOM   23102 O  OE1 . GLU C 1 1413 ? 57.031  -16.562 112.056 1.00 294.85 ? 1413 GLU B OE1 1 
ATOM   23103 O  OE2 . GLU C 1 1413 ? 57.902  -18.555 111.771 1.00 298.59 ? 1413 GLU B OE2 1 
ATOM   23104 N  N   . GLU C 1 1414 ? 55.889  -15.385 106.515 1.00 239.91 ? 1414 GLU B N   1 
ATOM   23105 C  CA  . GLU C 1 1414 ? 55.449  -14.293 105.647 1.00 223.50 ? 1414 GLU B CA  1 
ATOM   23106 C  C   . GLU C 1 1414 ? 53.959  -14.315 105.325 1.00 222.11 ? 1414 GLU B C   1 
ATOM   23107 O  O   . GLU C 1 1414 ? 53.336  -15.369 105.269 1.00 226.60 ? 1414 GLU B O   1 
ATOM   23108 C  CB  . GLU C 1 1414 ? 56.296  -14.218 104.371 1.00 212.83 ? 1414 GLU B CB  1 
ATOM   23109 C  CG  . GLU C 1 1414 ? 57.641  -13.514 104.574 1.00 198.08 ? 1414 GLU B CG  1 
ATOM   23110 C  CD  . GLU C 1 1414 ? 58.575  -13.638 103.374 1.00 190.05 ? 1414 GLU B CD  1 
ATOM   23111 O  OE1 . GLU C 1 1414 ? 58.264  -14.416 102.454 1.00 191.29 ? 1414 GLU B OE1 1 
ATOM   23112 O  OE2 . GLU C 1 1414 ? 59.628  -12.964 103.350 1.00 184.32 ? 1414 GLU B OE2 1 
ATOM   23113 N  N   . SER C 1 1415 ? 53.395  -13.133 105.123 1.00 261.48 ? 1415 SER B N   1 
ATOM   23114 C  CA  . SER C 1 1415 ? 51.970  -13.010 104.876 1.00 263.83 ? 1415 SER B CA  1 
ATOM   23115 C  C   . SER C 1 1415 ? 51.560  -13.559 103.511 1.00 266.87 ? 1415 SER B C   1 
ATOM   23116 O  O   . SER C 1 1415 ? 52.364  -13.621 102.582 1.00 265.56 ? 1415 SER B O   1 
ATOM   23117 C  CB  . SER C 1 1415 ? 51.541  -11.556 105.013 1.00 259.58 ? 1415 SER B CB  1 
ATOM   23118 O  OG  . SER C 1 1415 ? 50.169  -11.403 104.707 1.00 262.78 ? 1415 SER B OG  1 
ATOM   23119 N  N   . SER C 1 1416 ? 50.296  -13.954 103.407 1.00 233.68 ? 1416 SER B N   1 
ATOM   23120 C  CA  . SER C 1 1416 ? 49.751  -14.520 102.183 1.00 238.57 ? 1416 SER B CA  1 
ATOM   23121 C  C   . SER C 1 1416 ? 49.706  -13.498 101.053 1.00 236.50 ? 1416 SER B C   1 
ATOM   23122 O  O   . SER C 1 1416 ? 49.583  -13.857 99.882  1.00 238.04 ? 1416 SER B O   1 
ATOM   23123 C  CB  . SER C 1 1416 ? 48.345  -15.063 102.439 1.00 246.57 ? 1416 SER B CB  1 
ATOM   23124 O  OG  . SER C 1 1416 ? 47.440  -14.016 102.762 1.00 247.96 ? 1416 SER B OG  1 
ATOM   23125 N  N   . SER C 1 1417 ? 49.803  -12.221 101.396 1.00 260.61 ? 1417 SER B N   1 
ATOM   23126 C  CA  . SER C 1 1417 ? 49.636  -11.195 100.382 1.00 258.92 ? 1417 SER B CA  1 
ATOM   23127 C  C   . SER C 1 1417 ? 50.571  -11.427 99.198  1.00 254.56 ? 1417 SER B C   1 
ATOM   23128 O  O   . SER C 1 1417 ? 50.254  -11.057 98.076  1.00 259.97 ? 1417 SER B O   1 
ATOM   23129 C  CB  . SER C 1 1417 ? 49.791  -9.777  100.955 1.00 255.21 ? 1417 SER B CB  1 
ATOM   23130 O  OG  . SER C 1 1417 ? 51.141  -9.441  101.215 1.00 249.48 ? 1417 SER B OG  1 
ATOM   23131 N  N   . GLY C 1 1418 ? 51.703  -12.078 99.432  1.00 248.78 ? 1418 GLY B N   1 
ATOM   23132 C  CA  . GLY C 1 1418 ? 52.662  -12.284 98.362  1.00 240.12 ? 1418 GLY B CA  1 
ATOM   23133 C  C   . GLY C 1 1418 ? 53.650  -11.135 98.294  1.00 231.49 ? 1418 GLY B C   1 
ATOM   23134 O  O   . GLY C 1 1418 ? 53.868  -10.454 99.288  1.00 225.70 ? 1418 GLY B O   1 
ATOM   23135 N  N   . SER C 1 1419 ? 54.229  -10.895 97.123  1.00 216.81 ? 1419 SER B N   1 
ATOM   23136 C  CA  . SER C 1 1419 ? 55.424  -10.052 97.017  1.00 208.26 ? 1419 SER B CA  1 
ATOM   23137 C  C   . SER C 1 1419 ? 55.278  -8.530  97.240  1.00 198.64 ? 1419 SER B C   1 
ATOM   23138 O  O   . SER C 1 1419 ? 54.171  -7.984  97.303  1.00 200.84 ? 1419 SER B O   1 
ATOM   23139 C  CB  . SER C 1 1419 ? 56.138  -10.330 95.691  1.00 208.00 ? 1419 SER B CB  1 
ATOM   23140 O  OG  . SER C 1 1419 ? 57.485  -9.892  95.734  1.00 201.35 ? 1419 SER B OG  1 
ATOM   23141 N  N   . SER C 1 1420 ? 56.431  -7.878  97.389  1.00 179.54 ? 1420 SER B N   1 
ATOM   23142 C  CA  . SER C 1 1420 ? 56.555  -6.425  97.425  1.00 172.31 ? 1420 SER B CA  1 
ATOM   23143 C  C   . SER C 1 1420 ? 56.821  -5.949  96.009  1.00 172.66 ? 1420 SER B C   1 
ATOM   23144 O  O   . SER C 1 1420 ? 56.665  -6.709  95.063  1.00 178.37 ? 1420 SER B O   1 
ATOM   23145 C  CB  . SER C 1 1420 ? 57.765  -6.029  98.264  1.00 163.43 ? 1420 SER B CB  1 
ATOM   23146 O  OG  . SER C 1 1420 ? 58.955  -6.086  97.480  1.00 157.71 ? 1420 SER B OG  1 
ATOM   23147 N  N   . HIS C 1 1421 ? 57.263  -4.704  95.864  1.00 174.46 ? 1421 HIS B N   1 
ATOM   23148 C  CA  . HIS C 1 1421 ? 57.616  -4.163  94.554  1.00 170.98 ? 1421 HIS B CA  1 
ATOM   23149 C  C   . HIS C 1 1421 ? 58.675  -5.029  93.839  1.00 164.62 ? 1421 HIS B C   1 
ATOM   23150 O  O   . HIS C 1 1421 ? 59.752  -5.300  94.385  1.00 157.63 ? 1421 HIS B O   1 
ATOM   23151 C  CB  . HIS C 1 1421 ? 58.026  -2.693  94.701  1.00 170.05 ? 1421 HIS B CB  1 
ATOM   23152 C  CG  . HIS C 1 1421 ? 58.928  -2.189  93.619  1.00 167.67 ? 1421 HIS B CG  1 
ATOM   23153 N  ND1 . HIS C 1 1421 ? 60.157  -1.625  93.880  1.00 162.25 ? 1421 HIS B ND1 1 
ATOM   23154 C  CD2 . HIS C 1 1421 ? 58.770  -2.149  92.276  1.00 169.53 ? 1421 HIS B CD2 1 
ATOM   23155 C  CE1 . HIS C 1 1421 ? 60.723  -1.259  92.743  1.00 162.05 ? 1421 HIS B CE1 1 
ATOM   23156 N  NE2 . HIS C 1 1421 ? 59.907  -1.576  91.757  1.00 166.14 ? 1421 HIS B NE2 1 
ATOM   23157 N  N   . ALA C 1 1422 ? 58.349  -5.462  92.617  1.00 158.77 ? 1422 ALA B N   1 
ATOM   23158 C  CA  . ALA C 1 1422 ? 59.163  -6.440  91.892  1.00 162.61 ? 1422 ALA B CA  1 
ATOM   23159 C  C   . ALA C 1 1422 ? 59.183  -6.247  90.378  1.00 167.17 ? 1422 ALA B C   1 
ATOM   23160 O  O   . ALA C 1 1422 ? 58.333  -5.564  89.799  1.00 167.69 ? 1422 ALA B O   1 
ATOM   23161 C  CB  . ALA C 1 1422 ? 58.706  -7.854  92.228  1.00 165.13 ? 1422 ALA B CB  1 
ATOM   23162 N  N   . VAL C 1 1423 ? 60.172  -6.887  89.760  1.00 185.02 ? 1423 VAL B N   1 
ATOM   23163 C  CA  . VAL C 1 1423 ? 60.395  -6.821  88.324  1.00 188.90 ? 1423 VAL B CA  1 
ATOM   23164 C  C   . VAL C 1 1423 ? 60.262  -8.202  87.639  1.00 194.85 ? 1423 VAL B C   1 
ATOM   23165 O  O   . VAL C 1 1423 ? 60.429  -9.242  88.288  1.00 198.11 ? 1423 VAL B O   1 
ATOM   23166 C  CB  . VAL C 1 1423 ? 61.801  -6.234  88.020  1.00 166.16 ? 1423 VAL B CB  1 
ATOM   23167 C  CG1 . VAL C 1 1423 ? 62.133  -5.141  88.999  1.00 162.09 ? 1423 VAL B CG1 1 
ATOM   23168 C  CG2 . VAL C 1 1423 ? 62.859  -7.299  88.072  1.00 165.46 ? 1423 VAL B CG2 1 
ATOM   23169 N  N   . MET C 1 1424 ? 59.949  -8.204  86.338  1.00 175.56 ? 1424 MET B N   1 
ATOM   23170 C  CA  . MET C 1 1424 ? 60.045  -9.409  85.510  1.00 174.32 ? 1424 MET B CA  1 
ATOM   23171 C  C   . MET C 1 1424 ? 61.051  -9.178  84.380  1.00 174.54 ? 1424 MET B C   1 
ATOM   23172 O  O   . MET C 1 1424 ? 61.013  -8.140  83.714  1.00 174.83 ? 1424 MET B O   1 
ATOM   23173 C  CB  . MET C 1 1424 ? 58.677  -9.799  84.964  1.00 172.44 ? 1424 MET B CB  1 
ATOM   23174 C  CG  . MET C 1 1424 ? 57.620  -9.837  86.041  1.00 171.89 ? 1424 MET B CG  1 
ATOM   23175 S  SD  . MET C 1 1424 ? 56.177  -10.840 85.613  1.00 184.36 ? 1424 MET B SD  1 
ATOM   23176 C  CE  . MET C 1 1424 ? 56.906  -12.469 85.359  1.00 180.11 ? 1424 MET B CE  1 
ATOM   23177 N  N   . ASP C 1 1425 ? 61.964  -10.133 84.191  1.00 146.37 ? 1425 ASP B N   1 
ATOM   23178 C  CA  . ASP C 1 1425 ? 63.079  -9.980  83.243  1.00 146.53 ? 1425 ASP B CA  1 
ATOM   23179 C  C   . ASP C 1 1425 ? 63.162  -11.140 82.245  1.00 153.90 ? 1425 ASP B C   1 
ATOM   23180 O  O   . ASP C 1 1425 ? 63.541  -12.260 82.619  1.00 156.30 ? 1425 ASP B O   1 
ATOM   23181 C  CB  . ASP C 1 1425 ? 64.408  -9.846  83.991  1.00 143.23 ? 1425 ASP B CB  1 
ATOM   23182 C  CG  . ASP C 1 1425 ? 65.603  -9.723  83.064  1.00 144.93 ? 1425 ASP B CG  1 
ATOM   23183 O  OD1 . ASP C 1 1425 ? 65.970  -8.569  82.758  1.00 142.30 ? 1425 ASP B OD1 1 
ATOM   23184 O  OD2 . ASP C 1 1425 ? 66.184  -10.772 82.687  1.00 148.70 ? 1425 ASP B OD2 1 
ATOM   23185 N  N   . ILE C 1 1426 ? 62.809  -10.856 80.980  1.00 137.58 ? 1426 ILE B N   1 
ATOM   23186 C  CA  . ILE C 1 1426 ? 62.876  -11.835 79.891  1.00 139.60 ? 1426 ILE B CA  1 
ATOM   23187 C  C   . ILE C 1 1426 ? 63.939  -11.493 78.856  1.00 138.56 ? 1426 ILE B C   1 
ATOM   23188 O  O   . ILE C 1 1426 ? 63.934  -10.427 78.245  1.00 137.38 ? 1426 ILE B O   1 
ATOM   23189 C  CB  . ILE C 1 1426 ? 61.547  -12.007 79.165  1.00 141.80 ? 1426 ILE B CB  1 
ATOM   23190 C  CG1 . ILE C 1 1426 ? 60.402  -12.223 80.150  1.00 142.81 ? 1426 ILE B CG1 1 
ATOM   23191 C  CG2 . ILE C 1 1426 ? 61.636  -13.195 78.259  1.00 145.28 ? 1426 ILE B CG2 1 
ATOM   23192 C  CD1 . ILE C 1 1426 ? 59.117  -12.657 79.481  1.00 146.58 ? 1426 ILE B CD1 1 
ATOM   23193 N  N   . SER C 1 1427 ? 64.870  -12.423 78.709  1.00 196.06 ? 1427 SER B N   1 
ATOM   23194 C  CA  . SER C 1 1427 ? 65.884  -12.396 77.679  1.00 194.13 ? 1427 SER B CA  1 
ATOM   23195 C  C   . SER C 1 1427 ? 65.218  -12.935 76.434  1.00 198.89 ? 1427 SER B C   1 
ATOM   23196 O  O   . SER C 1 1427 ? 64.432  -13.877 76.522  1.00 203.28 ? 1427 SER B O   1 
ATOM   23197 C  CB  . SER C 1 1427 ? 67.029  -13.314 78.096  1.00 183.75 ? 1427 SER B CB  1 
ATOM   23198 O  OG  . SER C 1 1427 ? 67.933  -13.557 77.036  1.00 184.51 ? 1427 SER B OG  1 
ATOM   23199 N  N   . LEU C 1 1428 ? 65.504  -12.336 75.280  1.00 165.88 ? 1428 LEU B N   1 
ATOM   23200 C  CA  . LEU C 1 1428 ? 64.879  -12.770 74.022  1.00 170.65 ? 1428 LEU B CA  1 
ATOM   23201 C  C   . LEU C 1 1428 ? 65.856  -13.464 73.082  1.00 172.84 ? 1428 LEU B C   1 
ATOM   23202 O  O   . LEU C 1 1428 ? 66.863  -12.873 72.678  1.00 168.69 ? 1428 LEU B O   1 
ATOM   23203 C  CB  . LEU C 1 1428 ? 64.221  -11.587 73.317  1.00 167.11 ? 1428 LEU B CB  1 
ATOM   23204 C  CG  . LEU C 1 1428 ? 63.071  -11.036 74.152  1.00 164.83 ? 1428 LEU B CG  1 
ATOM   23205 C  CD1 . LEU C 1 1428 ? 62.573  -9.715  73.592  1.00 163.69 ? 1428 LEU B CD1 1 
ATOM   23206 C  CD2 . LEU C 1 1428 ? 61.943  -12.078 74.303  1.00 167.22 ? 1428 LEU B CD2 1 
ATOM   23207 N  N   . PRO C 1 1429 ? 65.526  -14.705 72.696  1.00 163.13 ? 1429 PRO B N   1 
ATOM   23208 C  CA  . PRO C 1 1429 ? 66.390  -15.614 71.930  1.00 163.86 ? 1429 PRO B CA  1 
ATOM   23209 C  C   . PRO C 1 1429 ? 67.064  -14.866 70.793  1.00 162.97 ? 1429 PRO B C   1 
ATOM   23210 O  O   . PRO C 1 1429 ? 66.406  -14.073 70.135  1.00 161.82 ? 1429 PRO B O   1 
ATOM   23211 C  CB  . PRO C 1 1429 ? 65.405  -16.624 71.364  1.00 169.28 ? 1429 PRO B CB  1 
ATOM   23212 C  CG  . PRO C 1 1429 ? 64.243  -16.583 72.285  1.00 170.30 ? 1429 PRO B CG  1 
ATOM   23213 C  CD  . PRO C 1 1429 ? 64.141  -15.195 72.804  1.00 165.59 ? 1429 PRO B CD  1 
ATOM   23214 N  N   . THR C 1 1430 ? 68.341  -15.109 70.542  1.00 204.00 ? 1430 THR B N   1 
ATOM   23215 C  CA  . THR C 1 1430 ? 69.065  -14.227 69.628  1.00 203.63 ? 1430 THR B CA  1 
ATOM   23216 C  C   . THR C 1 1430 ? 68.251  -13.836 68.354  1.00 211.90 ? 1430 THR B C   1 
ATOM   23217 O  O   . THR C 1 1430 ? 67.879  -14.685 67.546  1.00 219.90 ? 1430 THR B O   1 
ATOM   23218 C  CB  . THR C 1 1430 ? 70.474  -14.775 69.313  1.00 201.26 ? 1430 THR B CB  1 
ATOM   23219 O  OG1 . THR C 1 1430 ? 71.119  -15.152 70.536  1.00 198.01 ? 1430 THR B OG1 1 
ATOM   23220 C  CG2 . THR C 1 1430 ? 71.307  -13.717 68.619  1.00 196.39 ? 1430 THR B CG2 1 
ATOM   23221 N  N   . GLY C 1 1431 ? 67.956  -12.540 68.221  1.00 192.32 ? 1431 GLY B N   1 
ATOM   23222 C  CA  . GLY C 1 1431 ? 67.106  -12.011 67.161  1.00 196.36 ? 1431 GLY B CA  1 
ATOM   23223 C  C   . GLY C 1 1431 ? 65.635  -12.396 67.212  1.00 202.47 ? 1431 GLY B C   1 
ATOM   23224 O  O   . GLY C 1 1431 ? 65.199  -13.211 66.407  1.00 203.82 ? 1431 GLY B O   1 
ATOM   23225 N  N   . ILE C 1 1432 ? 64.868  -11.807 68.136  1.00 159.35 ? 1432 ILE B N   1 
ATOM   23226 C  CA  . ILE C 1 1432 ? 63.434  -12.118 68.285  1.00 159.33 ? 1432 ILE B CA  1 
ATOM   23227 C  C   . ILE C 1 1432 ? 62.586  -10.946 68.822  1.00 158.20 ? 1432 ILE B C   1 
ATOM   23228 O  O   . ILE C 1 1432 ? 61.698  -11.146 69.648  1.00 161.30 ? 1432 ILE B O   1 
ATOM   23229 C  CB  . ILE C 1 1432 ? 63.180  -13.362 69.197  1.00 160.50 ? 1432 ILE B CB  1 
ATOM   23230 C  CG1 . ILE C 1 1432 ? 64.083  -14.536 68.810  1.00 160.24 ? 1432 ILE B CG1 1 
ATOM   23231 C  CG2 . ILE C 1 1432 ? 61.712  -13.792 69.170  1.00 172.52 ? 1432 ILE B CG2 1 
ATOM   23232 C  CD1 . ILE C 1 1432 ? 63.538  -15.428 67.743  1.00 167.93 ? 1432 ILE B CD1 1 
ATOM   23233 N  N   . SER C 1 1433 ? 62.848  -9.735  68.333  1.00 263.61 ? 1433 SER B N   1 
ATOM   23234 C  CA  . SER C 1 1433 ? 62.045  -8.553  68.671  1.00 260.68 ? 1433 SER B CA  1 
ATOM   23235 C  C   . SER C 1 1433 ? 60.698  -8.881  69.296  1.00 262.38 ? 1433 SER B C   1 
ATOM   23236 O  O   . SER C 1 1433 ? 60.004  -9.814  68.895  1.00 266.88 ? 1433 SER B O   1 
ATOM   23237 C  CB  . SER C 1 1433 ? 61.789  -7.691  67.426  1.00 264.34 ? 1433 SER B CB  1 
ATOM   23238 O  OG  . SER C 1 1433 ? 62.949  -6.989  67.012  1.00 262.93 ? 1433 SER B OG  1 
ATOM   23239 N  N   . ALA C 1 1434 ? 60.313  -8.074  70.265  1.00 178.97 ? 1434 ALA B N   1 
ATOM   23240 C  CA  . ALA C 1 1434 ? 59.087  -8.322  70.977  1.00 184.26 ? 1434 ALA B CA  1 
ATOM   23241 C  C   . ALA C 1 1434 ? 58.096  -7.223  70.706  1.00 186.42 ? 1434 ALA B C   1 
ATOM   23242 O  O   . ALA C 1 1434 ? 58.468  -6.104  70.347  1.00 185.30 ? 1434 ALA B O   1 
ATOM   23243 C  CB  . ALA C 1 1434 ? 59.367  -8.394  72.439  1.00 182.20 ? 1434 ALA B CB  1 
ATOM   23244 N  N   . ASN C 1 1435 ? 56.832  -7.543  70.941  1.00 177.59 ? 1435 ASN B N   1 
ATOM   23245 C  CA  . ASN C 1 1435 ? 55.737  -6.689  70.521  1.00 180.76 ? 1435 ASN B CA  1 
ATOM   23246 C  C   . ASN C 1 1435 ? 55.635  -5.339  71.229  1.00 174.72 ? 1435 ASN B C   1 
ATOM   23247 O  O   . ASN C 1 1435 ? 54.762  -5.148  72.066  1.00 173.76 ? 1435 ASN B O   1 
ATOM   23248 C  CB  . ASN C 1 1435 ? 54.411  -7.456  70.617  1.00 187.27 ? 1435 ASN B CB  1 
ATOM   23249 C  CG  . ASN C 1 1435 ? 53.325  -6.891  69.687  1.00 192.65 ? 1435 ASN B CG  1 
ATOM   23250 O  OD1 . ASN C 1 1435 ? 53.154  -5.672  69.574  1.00 190.35 ? 1435 ASN B OD1 1 
ATOM   23251 N  ND2 . ASN C 1 1435 ? 52.592  -7.782  69.014  1.00 200.65 ? 1435 ASN B ND2 1 
ATOM   23252 N  N   . GLU C 1 1436 ? 56.494  -4.395  70.853  1.00 186.17 ? 1436 GLU B N   1 
ATOM   23253 C  CA  . GLU C 1 1436 ? 56.463  -3.078  71.462  1.00 184.11 ? 1436 GLU B CA  1 
ATOM   23254 C  C   . GLU C 1 1436 ? 55.048  -2.665  71.830  1.00 185.79 ? 1436 GLU B C   1 
ATOM   23255 O  O   . GLU C 1 1436 ? 54.773  -2.283  72.954  1.00 183.84 ? 1436 GLU B O   1 
ATOM   23256 C  CB  . GLU C 1 1436 ? 57.052  -2.021  70.533  1.00 186.12 ? 1436 GLU B CB  1 
ATOM   23257 C  CG  . GLU C 1 1436 ? 57.265  -0.659  71.216  1.00 184.65 ? 1436 GLU B CG  1 
ATOM   23258 C  CD  . GLU C 1 1436 ? 58.590  -0.588  71.993  1.00 181.10 ? 1436 GLU B CD  1 
ATOM   23259 O  OE1 . GLU C 1 1436 ? 59.344  -1.588  71.954  1.00 182.82 ? 1436 GLU B OE1 1 
ATOM   23260 O  OE2 . GLU C 1 1436 ? 58.885  0.458   72.633  1.00 175.27 ? 1436 GLU B OE2 1 
ATOM   23261 N  N   . GLU C 1 1437 ? 54.144  -2.739  70.872  1.00 192.15 ? 1437 GLU B N   1 
ATOM   23262 C  CA  . GLU C 1 1437 ? 52.776  -2.308  71.106  1.00 193.07 ? 1437 GLU B CA  1 
ATOM   23263 C  C   . GLU C 1 1437 ? 52.128  -3.184  72.175  1.00 196.56 ? 1437 GLU B C   1 
ATOM   23264 O  O   . GLU C 1 1437 ? 51.325  -2.719  72.972  1.00 196.54 ? 1437 GLU B O   1 
ATOM   23265 C  CB  . GLU C 1 1437 ? 51.962  -2.349  69.800  1.00 200.87 ? 1437 GLU B CB  1 
ATOM   23266 C  CG  . GLU C 1 1437 ? 52.803  -2.300  68.505  1.00 246.06 ? 1437 GLU B CG  1 
ATOM   23267 C  CD  . GLU C 1 1437 ? 53.329  -0.911  68.153  1.00 237.62 ? 1437 GLU B CD  1 
ATOM   23268 O  OE1 . GLU C 1 1437 ? 52.817  0.083   68.710  1.00 234.58 ? 1437 GLU B OE1 1 
ATOM   23269 O  OE2 . GLU C 1 1437 ? 54.251  -0.817  67.305  1.00 232.83 ? 1437 GLU B OE2 1 
ATOM   23270 N  N   . ASP C 1 1438 ? 52.485  -4.456  72.198  1.00 213.66 ? 1438 ASP B N   1 
ATOM   23271 C  CA  . ASP C 1 1438 ? 51.811  -5.374  73.092  1.00 216.49 ? 1438 ASP B CA  1 
ATOM   23272 C  C   . ASP C 1 1438 ? 51.913  -4.886  74.514  1.00 209.80 ? 1438 ASP B C   1 
ATOM   23273 O  O   . ASP C 1 1438 ? 50.917  -4.875  75.236  1.00 211.47 ? 1438 ASP B O   1 
ATOM   23274 C  CB  . ASP C 1 1438 ? 52.404  -6.778  72.998  1.00 220.16 ? 1438 ASP B CB  1 
ATOM   23275 C  CG  . ASP C 1 1438 ? 51.648  -7.663  72.041  1.00 227.42 ? 1438 ASP B CG  1 
ATOM   23276 O  OD1 . ASP C 1 1438 ? 50.568  -7.244  71.584  1.00 231.07 ? 1438 ASP B OD1 1 
ATOM   23277 O  OD2 . ASP C 1 1438 ? 52.130  -8.773  71.740  1.00 229.04 ? 1438 ASP B OD2 1 
ATOM   23278 N  N   . LEU C 1 1439 ? 53.125  -4.481  74.908  1.00 167.13 ? 1439 LEU B N   1 
ATOM   23279 C  CA  . LEU C 1 1439 ? 53.468  -4.210  76.327  1.00 157.75 ? 1439 LEU B CA  1 
ATOM   23280 C  C   . LEU C 1 1439 ? 52.797  -2.937  76.845  1.00 154.33 ? 1439 LEU B C   1 
ATOM   23281 O  O   . LEU C 1 1439 ? 52.160  -2.958  77.901  1.00 153.71 ? 1439 LEU B O   1 
ATOM   23282 C  CB  . LEU C 1 1439 ? 54.993  -4.130  76.531  1.00 148.83 ? 1439 LEU B CB  1 
ATOM   23283 C  CG  . LEU C 1 1439 ? 55.837  -5.297  75.993  1.00 147.87 ? 1439 LEU B CG  1 
ATOM   23284 C  CD1 . LEU C 1 1439 ? 57.329  -4.959  75.963  1.00 142.56 ? 1439 LEU B CD1 1 
ATOM   23285 C  CD2 . LEU C 1 1439 ? 55.567  -6.614  76.729  1.00 148.76 ? 1439 LEU B CD2 1 
ATOM   23286 N  N   . LYS C 1 1440 ? 52.938  -1.850  76.082  1.00 185.55 ? 1440 LYS B N   1 
ATOM   23287 C  CA  . LYS C 1 1440 ? 52.245  -0.588  76.335  1.00 186.70 ? 1440 LYS B CA  1 
ATOM   23288 C  C   . LYS C 1 1440 ? 50.771  -0.822  76.687  1.00 188.92 ? 1440 LYS B C   1 
ATOM   23289 O  O   . LYS C 1 1440 ? 50.128  0.020   77.312  1.00 186.37 ? 1440 LYS B O   1 
ATOM   23290 C  CB  . LYS C 1 1440 ? 52.327  0.300   75.087  1.00 193.05 ? 1440 LYS B CB  1 
ATOM   23291 C  CG  . LYS C 1 1440 ? 53.732  0.682   74.653  1.00 195.16 ? 1440 LYS B CG  1 
ATOM   23292 C  CD  . LYS C 1 1440 ? 54.285  1.820   75.507  1.00 195.47 ? 1440 LYS B CD  1 
ATOM   23293 C  CE  . LYS C 1 1440 ? 54.943  2.919   74.654  1.00 200.30 ? 1440 LYS B CE  1 
ATOM   23294 N  NZ  . LYS C 1 1440 ? 55.705  2.358   73.500  1.00 203.79 ? 1440 LYS B NZ  1 
ATOM   23295 N  N   . ALA C 1 1441 ? 50.247  -1.972  76.269  1.00 168.21 ? 1441 ALA B N   1 
ATOM   23296 C  CA  . ALA C 1 1441 ? 48.842  -2.330  76.459  1.00 175.13 ? 1441 ALA B CA  1 
ATOM   23297 C  C   . ALA C 1 1441 ? 48.606  -2.680  77.905  1.00 178.03 ? 1441 ALA B C   1 
ATOM   23298 O  O   . ALA C 1 1441 ? 47.720  -2.147  78.583  1.00 180.56 ? 1441 ALA B O   1 
ATOM   23299 C  CB  . ALA C 1 1441 ? 48.483  -3.542  75.562  1.00 180.86 ? 1441 ALA B CB  1 
ATOM   23300 N  N   . LEU C 1 1442 ? 49.445  -3.597  78.347  1.00 190.88 ? 1442 LEU B N   1 
ATOM   23301 C  CA  . LEU C 1 1442 ? 49.460  -4.080  79.694  1.00 190.71 ? 1442 LEU B CA  1 
ATOM   23302 C  C   . LEU C 1 1442 ? 49.576  -2.921  80.703  1.00 193.22 ? 1442 LEU B C   1 
ATOM   23303 O  O   . LEU C 1 1442 ? 48.771  -2.823  81.633  1.00 198.11 ? 1442 LEU B O   1 
ATOM   23304 C  CB  . LEU C 1 1442 ? 50.617  -5.080  79.810  1.00 185.03 ? 1442 LEU B CB  1 
ATOM   23305 C  CG  . LEU C 1 1442 ? 50.510  -6.349  78.930  1.00 188.79 ? 1442 LEU B CG  1 
ATOM   23306 C  CD1 . LEU C 1 1442 ? 51.878  -6.906  78.523  1.00 186.62 ? 1442 LEU B CD1 1 
ATOM   23307 C  CD2 . LEU C 1 1442 ? 49.659  -7.436  79.610  1.00 192.96 ? 1442 LEU B CD2 1 
ATOM   23308 N  N   . VAL C 1 1443 ? 50.540  -2.024  80.497  1.00 188.65 ? 1443 VAL B N   1 
ATOM   23309 C  CA  . VAL C 1 1443 ? 50.798  -0.933  81.448  1.00 186.71 ? 1443 VAL B CA  1 
ATOM   23310 C  C   . VAL C 1 1443 ? 49.926  0.311   81.252  1.00 188.12 ? 1443 VAL B C   1 
ATOM   23311 O  O   . VAL C 1 1443 ? 49.435  0.889   82.215  1.00 187.20 ? 1443 VAL B O   1 
ATOM   23312 C  CB  . VAL C 1 1443 ? 52.294  -0.512  81.441  1.00 181.60 ? 1443 VAL B CB  1 
ATOM   23313 C  CG1 . VAL C 1 1443 ? 53.147  -1.603  80.830  1.00 183.14 ? 1443 VAL B CG1 1 
ATOM   23314 C  CG2 . VAL C 1 1443 ? 52.491  0.785   80.674  1.00 180.50 ? 1443 VAL B CG2 1 
ATOM   23315 N  N   . GLU C 1 1444 ? 49.730  0.718   80.005  1.00 211.26 ? 1444 GLU B N   1 
ATOM   23316 C  CA  . GLU C 1 1444 ? 49.162  2.032   79.728  1.00 214.40 ? 1444 GLU B CA  1 
ATOM   23317 C  C   . GLU C 1 1444 ? 47.687  2.181   80.107  1.00 215.79 ? 1444 GLU B C   1 
ATOM   23318 O  O   . GLU C 1 1444 ? 47.007  3.056   79.587  1.00 215.10 ? 1444 GLU B O   1 
ATOM   23319 C  CB  . GLU C 1 1444 ? 49.380  2.404   78.256  1.00 223.87 ? 1444 GLU B CB  1 
ATOM   23320 C  CG  . GLU C 1 1444 ? 49.172  3.880   77.924  1.00 229.92 ? 1444 GLU B CG  1 
ATOM   23321 C  CD  . GLU C 1 1444 ? 49.934  4.313   76.683  1.00 234.25 ? 1444 GLU B CD  1 
ATOM   23322 O  OE1 . GLU C 1 1444 ? 51.084  3.848   76.523  1.00 232.40 ? 1444 GLU B OE1 1 
ATOM   23323 O  OE2 . GLU C 1 1444 ? 49.397  5.121   75.882  1.00 238.54 ? 1444 GLU B OE2 1 
ATOM   23324 N  N   . GLY C 1 1445 ? 47.190  1.357   81.022  1.00 234.32 ? 1445 GLY B N   1 
ATOM   23325 C  CA  . GLY C 1 1445 ? 45.787  1.447   81.381  1.00 241.33 ? 1445 GLY B CA  1 
ATOM   23326 C  C   . GLY C 1 1445 ? 45.436  1.264   82.847  1.00 242.37 ? 1445 GLY B C   1 
ATOM   23327 O  O   . GLY C 1 1445 ? 46.208  0.701   83.614  1.00 240.21 ? 1445 GLY B O   1 
ATOM   23328 N  N   . VAL C 1 1446 ? 44.254  1.762   83.211  1.00 158.76 ? 1446 VAL B N   1 
ATOM   23329 C  CA  . VAL C 1 1446 ? 43.627  1.568   84.520  1.00 159.25 ? 1446 VAL B CA  1 
ATOM   23330 C  C   . VAL C 1 1446 ? 43.375  0.092   84.823  1.00 160.74 ? 1446 VAL B C   1 
ATOM   23331 O  O   . VAL C 1 1446 ? 43.049  -0.286  85.943  1.00 159.36 ? 1446 VAL B O   1 
ATOM   23332 C  CB  . VAL C 1 1446 ? 42.285  2.346   84.597  1.00 165.15 ? 1446 VAL B CB  1 
ATOM   23333 C  CG1 . VAL C 1 1446 ? 41.503  2.024   85.863  1.00 167.04 ? 1446 VAL B CG1 1 
ATOM   23334 C  CG2 . VAL C 1 1446 ? 42.529  3.846   84.457  1.00 161.91 ? 1446 VAL B CG2 1 
ATOM   23335 N  N   . ASP C 1 1447 ? 43.509  -0.751  83.814  1.00 269.78 ? 1447 ASP B N   1 
ATOM   23336 C  CA  . ASP C 1 1447 ? 43.615  -2.170  84.083  1.00 273.44 ? 1447 ASP B CA  1 
ATOM   23337 C  C   . ASP C 1 1447 ? 45.099  -2.512  84.170  1.00 266.89 ? 1447 ASP B C   1 
ATOM   23338 O  O   . ASP C 1 1447 ? 45.510  -3.580  83.730  1.00 268.37 ? 1447 ASP B O   1 
ATOM   23339 C  CB  . ASP C 1 1447 ? 42.902  -3.016  83.015  1.00 282.76 ? 1447 ASP B CB  1 
ATOM   23340 C  CG  . ASP C 1 1447 ? 43.545  -2.902  81.640  1.00 284.67 ? 1447 ASP B CG  1 
ATOM   23341 O  OD1 . ASP C 1 1447 ? 44.498  -2.106  81.493  1.00 279.26 ? 1447 ASP B OD1 1 
ATOM   23342 O  OD2 . ASP C 1 1447 ? 43.096  -3.607  80.706  1.00 290.77 ? 1447 ASP B OD2 1 
ATOM   23343 N  N   . GLN C 1 1448 ? 45.901  -1.605  84.731  1.00 179.42 ? 1448 GLN B N   1 
ATOM   23344 C  CA  . GLN C 1 1448 ? 47.355  -1.795  84.741  1.00 173.17 ? 1448 GLN B CA  1 
ATOM   23345 C  C   . GLN C 1 1448 ? 47.828  -2.983  85.557  1.00 171.52 ? 1448 GLN B C   1 
ATOM   23346 O  O   . GLN C 1 1448 ? 47.863  -2.947  86.790  1.00 170.58 ? 1448 GLN B O   1 
ATOM   23347 C  CB  . GLN C 1 1448 ? 48.138  -0.528  85.111  1.00 167.46 ? 1448 GLN B CB  1 
ATOM   23348 C  CG  . GLN C 1 1448 ? 47.983  0.015   86.531  1.00 166.37 ? 1448 GLN B CG  1 
ATOM   23349 C  CD  . GLN C 1 1448 ? 48.862  1.253   86.765  1.00 161.86 ? 1448 GLN B CD  1 
ATOM   23350 O  OE1 . GLN C 1 1448 ? 50.092  1.174   86.708  1.00 157.97 ? 1448 GLN B OE1 1 
ATOM   23351 N  NE2 . GLN C 1 1448 ? 48.229  2.401   87.010  1.00 161.67 ? 1448 GLN B NE2 1 
ATOM   23352 N  N   . LEU C 1 1449 ? 48.193  -4.027  84.816  1.00 193.62 ? 1449 LEU B N   1 
ATOM   23353 C  CA  . LEU C 1 1449 ? 48.680  -5.301  85.332  1.00 195.03 ? 1449 LEU B CA  1 
ATOM   23354 C  C   . LEU C 1 1449 ? 50.165  -5.236  85.614  1.00 184.66 ? 1449 LEU B C   1 
ATOM   23355 O  O   . LEU C 1 1449 ? 50.683  -5.979  86.444  1.00 181.54 ? 1449 LEU B O   1 
ATOM   23356 C  CB  . LEU C 1 1449 ? 48.410  -6.399  84.303  1.00 205.35 ? 1449 LEU B CB  1 
ATOM   23357 C  CG  . LEU C 1 1449 ? 49.349  -7.606  84.303  1.00 210.36 ? 1449 LEU B CG  1 
ATOM   23358 C  CD1 . LEU C 1 1449 ? 49.395  -8.253  85.686  1.00 211.62 ? 1449 LEU B CD1 1 
ATOM   23359 C  CD2 . LEU C 1 1449 ? 48.974  -8.628  83.206  1.00 217.78 ? 1449 LEU B CD2 1 
ATOM   23360 N  N   . PHE C 1 1450 ? 50.840  -4.362  84.877  1.00 183.49 ? 1450 PHE B N   1 
ATOM   23361 C  CA  . PHE C 1 1450 ? 52.207  -3.967  85.165  1.00 175.16 ? 1450 PHE B CA  1 
ATOM   23362 C  C   . PHE C 1 1450 ? 52.195  -2.473  85.121  1.00 172.03 ? 1450 PHE B C   1 
ATOM   23363 O  O   . PHE C 1 1450 ? 51.143  -1.869  84.894  1.00 174.95 ? 1450 PHE B O   1 
ATOM   23364 C  CB  . PHE C 1 1450 ? 53.176  -4.484  84.120  1.00 172.81 ? 1450 PHE B CB  1 
ATOM   23365 C  CG  . PHE C 1 1450 ? 53.165  -5.951  83.997  1.00 175.52 ? 1450 PHE B CG  1 
ATOM   23366 C  CD1 . PHE C 1 1450 ? 52.206  -6.575  83.235  1.00 182.80 ? 1450 PHE B CD1 1 
ATOM   23367 C  CD2 . PHE C 1 1450 ? 54.088  -6.717  84.670  1.00 172.45 ? 1450 PHE B CD2 1 
ATOM   23368 C  CE1 . PHE C 1 1450 ? 52.173  -7.936  83.119  1.00 185.53 ? 1450 PHE B CE1 1 
ATOM   23369 C  CE2 . PHE C 1 1450 ? 54.059  -8.082  84.570  1.00 176.09 ? 1450 PHE B CE2 1 
ATOM   23370 C  CZ  . PHE C 1 1450 ? 53.094  -8.693  83.788  1.00 182.41 ? 1450 PHE B CZ  1 
ATOM   23371 N  N   . THR C 1 1451 ? 53.364  -1.871  85.296  1.00 147.57 ? 1451 THR B N   1 
ATOM   23372 C  CA  . THR C 1 1451 ? 53.431  -0.428  85.447  1.00 140.94 ? 1451 THR B CA  1 
ATOM   23373 C  C   . THR C 1 1451 ? 54.685  0.111   84.805  1.00 136.23 ? 1451 THR B C   1 
ATOM   23374 O  O   . THR C 1 1451 ? 54.895  1.319   84.728  1.00 133.16 ? 1451 THR B O   1 
ATOM   23375 C  CB  . THR C 1 1451 ? 53.523  -0.081  86.901  1.00 134.98 ? 1451 THR B CB  1 
ATOM   23376 O  OG1 . THR C 1 1451 ? 54.783  -0.555  87.383  1.00 129.57 ? 1451 THR B OG1 1 
ATOM   23377 C  CG2 . THR C 1 1451 ? 52.417  -0.773  87.685  1.00 138.40 ? 1451 THR B CG2 1 
ATOM   23378 N  N   . ASP C 1 1452 ? 55.534  -0.795  84.359  1.00 184.57 ? 1452 ASP B N   1 
ATOM   23379 C  CA  . ASP C 1 1452 ? 56.654  -0.356  83.580  1.00 181.59 ? 1452 ASP B CA  1 
ATOM   23380 C  C   . ASP C 1 1452 ? 57.243  -1.487  82.784  1.00 185.02 ? 1452 ASP B C   1 
ATOM   23381 O  O   . ASP C 1 1452 ? 57.574  -2.550  83.306  1.00 184.53 ? 1452 ASP B O   1 
ATOM   23382 C  CB  . ASP C 1 1452 ? 57.701  0.312   84.455  1.00 171.38 ? 1452 ASP B CB  1 
ATOM   23383 C  CG  . ASP C 1 1452 ? 58.462  1.383   83.716  1.00 163.59 ? 1452 ASP B CG  1 
ATOM   23384 O  OD1 . ASP C 1 1452 ? 59.463  1.045   83.055  1.00 162.43 ? 1452 ASP B OD1 1 
ATOM   23385 O  OD2 . ASP C 1 1452 ? 58.053  2.561   83.780  1.00 159.24 ? 1452 ASP B OD2 1 
ATOM   23386 N  N   . TYR C 1 1453 ? 57.341  -1.231  81.491  1.00 201.60 ? 1453 TYR B N   1 
ATOM   23387 C  CA  . TYR C 1 1453 ? 57.955  -2.145  80.562  1.00 203.14 ? 1453 TYR B CA  1 
ATOM   23388 C  C   . TYR C 1 1453 ? 59.191  -1.434  80.035  1.00 198.33 ? 1453 TYR B C   1 
ATOM   23389 O  O   . TYR C 1 1453 ? 59.276  -0.209  80.096  1.00 195.90 ? 1453 TYR B O   1 
ATOM   23390 C  CB  . TYR C 1 1453 ? 56.974  -2.463  79.416  1.00 208.81 ? 1453 TYR B CB  1 
ATOM   23391 C  CG  . TYR C 1 1453 ? 57.012  -1.482  78.261  1.00 209.55 ? 1453 TYR B CG  1 
ATOM   23392 C  CD1 . TYR C 1 1453 ? 56.563  -0.176  78.414  1.00 210.92 ? 1453 TYR B CD1 1 
ATOM   23393 C  CD2 . TYR C 1 1453 ? 57.495  -1.868  77.015  1.00 212.09 ? 1453 TYR B CD2 1 
ATOM   23394 C  CE1 . TYR C 1 1453 ? 56.611  0.721   77.365  1.00 212.53 ? 1453 TYR B CE1 1 
ATOM   23395 C  CE2 . TYR C 1 1453 ? 57.544  -0.981  75.964  1.00 214.02 ? 1453 TYR B CE2 1 
ATOM   23396 C  CZ  . TYR C 1 1453 ? 57.100  0.312   76.145  1.00 212.59 ? 1453 TYR B CZ  1 
ATOM   23397 O  OH  . TYR C 1 1453 ? 57.150  1.215   75.109  1.00 209.93 ? 1453 TYR B OH  1 
ATOM   23398 N  N   . GLN C 1 1454 ? 60.150  -2.185  79.517  1.00 200.10 ? 1454 GLN B N   1 
ATOM   23399 C  CA  . GLN C 1 1454 ? 61.255  -1.563  78.810  1.00 196.42 ? 1454 GLN B CA  1 
ATOM   23400 C  C   . GLN C 1 1454 ? 62.152  -2.582  78.176  1.00 197.39 ? 1454 GLN B C   1 
ATOM   23401 O  O   . GLN C 1 1454 ? 62.684  -3.472  78.834  1.00 195.91 ? 1454 GLN B O   1 
ATOM   23402 C  CB  . GLN C 1 1454 ? 62.087  -0.706  79.742  1.00 191.65 ? 1454 GLN B CB  1 
ATOM   23403 C  CG  . GLN C 1 1454 ? 62.442  -1.407  81.044  1.00 191.09 ? 1454 GLN B CG  1 
ATOM   23404 C  CD  . GLN C 1 1454 ? 63.576  -0.730  81.794  1.00 187.51 ? 1454 GLN B CD  1 
ATOM   23405 O  OE1 . GLN C 1 1454 ? 64.644  -0.478  81.234  1.00 185.46 ? 1454 GLN B OE1 1 
ATOM   23406 N  NE2 . GLN C 1 1454 ? 63.355  -0.451  83.072  1.00 186.35 ? 1454 GLN B NE2 1 
ATOM   23407 N  N   . ILE C 1 1455 ? 62.332  -2.431  76.879  1.00 212.35 ? 1455 ILE B N   1 
ATOM   23408 C  CA  . ILE C 1 1455 ? 63.180  -3.338  76.148  1.00 212.39 ? 1455 ILE B CA  1 
ATOM   23409 C  C   . ILE C 1 1455 ? 64.592  -2.803  76.076  1.00 206.73 ? 1455 ILE B C   1 
ATOM   23410 O  O   . ILE C 1 1455 ? 64.901  -1.945  75.249  1.00 205.36 ? 1455 ILE B O   1 
ATOM   23411 C  CB  . ILE C 1 1455 ? 62.679  -3.547  74.723  1.00 224.63 ? 1455 ILE B CB  1 
ATOM   23412 C  CG1 . ILE C 1 1455 ? 61.381  -4.370  74.721  1.00 230.01 ? 1455 ILE B CG1 1 
ATOM   23413 C  CG2 . ILE C 1 1455 ? 63.765  -4.213  73.894  1.00 225.06 ? 1455 ILE B CG2 1 
ATOM   23414 C  CD1 . ILE C 1 1455 ? 60.109  -3.547  74.842  1.00 231.46 ? 1455 ILE B CD1 1 
ATOM   23415 N  N   . LYS C 1 1456 ? 65.459  -3.308  76.936  1.00 188.11 ? 1456 LYS B N   1 
ATOM   23416 C  CA  . LYS C 1 1456 ? 66.843  -2.908  76.837  1.00 184.00 ? 1456 LYS B CA  1 
ATOM   23417 C  C   . LYS C 1 1456 ? 67.715  -4.051  76.355  1.00 181.05 ? 1456 LYS B C   1 
ATOM   23418 O  O   . LYS C 1 1456 ? 67.487  -5.216  76.684  1.00 180.83 ? 1456 LYS B O   1 
ATOM   23419 C  CB  . LYS C 1 1456 ? 67.369  -2.334  78.149  1.00 183.32 ? 1456 LYS B CB  1 
ATOM   23420 C  CG  . LYS C 1 1456 ? 68.596  -1.469  77.951  1.00 185.32 ? 1456 LYS B CG  1 
ATOM   23421 C  CD  . LYS C 1 1456 ? 69.208  -1.037  79.263  1.00 185.08 ? 1456 LYS B CD  1 
ATOM   23422 C  CE  . LYS C 1 1456 ? 70.399  -0.117  79.032  1.00 183.56 ? 1456 LYS B CE  1 
ATOM   23423 N  NZ  . LYS C 1 1456 ? 69.993  1.202   78.453  1.00 183.93 ? 1456 LYS B NZ  1 
ATOM   23424 N  N   . ASP C 1 1457 ? 68.699  -3.678  75.546  1.00 213.75 ? 1457 ASP B N   1 
ATOM   23425 C  CA  . ASP C 1 1457 ? 69.716  -4.582  75.047  1.00 215.29 ? 1457 ASP B CA  1 
ATOM   23426 C  C   . ASP C 1 1457 ? 69.269  -6.030  75.163  1.00 216.16 ? 1457 ASP B C   1 
ATOM   23427 O  O   . ASP C 1 1457 ? 69.858  -6.810  75.896  1.00 214.52 ? 1457 ASP B O   1 
ATOM   23428 C  CB  . ASP C 1 1457 ? 71.044  -4.341  75.779  1.00 214.08 ? 1457 ASP B CB  1 
ATOM   23429 C  CG  . ASP C 1 1457 ? 71.548  -2.896  75.639  1.00 214.79 ? 1457 ASP B CG  1 
ATOM   23430 O  OD1 . ASP C 1 1457 ? 71.627  -2.385  74.499  1.00 219.00 ? 1457 ASP B OD1 1 
ATOM   23431 O  OD2 . ASP C 1 1457 ? 71.873  -2.271  76.673  1.00 211.36 ? 1457 ASP B OD2 1 
ATOM   23432 N  N   . GLY C 1 1458 ? 68.204  -6.373  74.451  1.00 162.98 ? 1458 GLY B N   1 
ATOM   23433 C  CA  . GLY C 1 1458 ? 67.795  -7.760  74.315  1.00 163.89 ? 1458 GLY B CA  1 
ATOM   23434 C  C   . GLY C 1 1458 ? 66.871  -8.300  75.385  1.00 162.54 ? 1458 GLY B C   1 
ATOM   23435 O  O   . GLY C 1 1458 ? 66.600  -9.499  75.452  1.00 165.05 ? 1458 GLY B O   1 
ATOM   23436 N  N   . HIS C 1 1459 ? 66.368  -7.426  76.232  1.00 182.52 ? 1459 HIS B N   1 
ATOM   23437 C  CA  . HIS C 1 1459 ? 65.569  -7.935  77.305  1.00 183.08 ? 1459 HIS B CA  1 
ATOM   23438 C  C   . HIS C 1 1459 ? 64.331  -7.129  77.479  1.00 181.47 ? 1459 HIS B C   1 
ATOM   23439 O  O   . HIS C 1 1459 ? 64.348  -5.907  77.368  1.00 177.31 ? 1459 HIS B O   1 
ATOM   23440 C  CB  . HIS C 1 1459 ? 66.353  -7.891  78.590  1.00 180.27 ? 1459 HIS B CB  1 
ATOM   23441 C  CG  . HIS C 1 1459 ? 67.599  -8.718  78.571  1.00 183.50 ? 1459 HIS B CG  1 
ATOM   23442 N  ND1 . HIS C 1 1459 ? 67.604  -10.065 78.872  1.00 187.93 ? 1459 HIS B ND1 1 
ATOM   23443 C  CD2 . HIS C 1 1459 ? 68.889  -8.382  78.330  1.00 181.88 ? 1459 HIS B CD2 1 
ATOM   23444 C  CE1 . HIS C 1 1459 ? 68.841  -10.524 78.805  1.00 186.25 ? 1459 HIS B CE1 1 
ATOM   23445 N  NE2 . HIS C 1 1459 ? 69.642  -9.523  78.479  1.00 182.54 ? 1459 HIS B NE2 1 
ATOM   23446 N  N   . VAL C 1 1460 ? 63.252  -7.844  77.756  1.00 186.22 ? 1460 VAL B N   1 
ATOM   23447 C  CA  . VAL C 1 1460 ? 61.987  -7.239  78.121  1.00 189.43 ? 1460 VAL B CA  1 
ATOM   23448 C  C   . VAL C 1 1460 ? 61.923  -7.157  79.628  1.00 190.89 ? 1460 VAL B C   1 
ATOM   23449 O  O   . VAL C 1 1460 ? 61.970  -8.186  80.299  1.00 193.99 ? 1460 VAL B O   1 
ATOM   23450 C  CB  . VAL C 1 1460 ? 60.797  -8.100  77.668  1.00 196.00 ? 1460 VAL B CB  1 
ATOM   23451 C  CG1 . VAL C 1 1460 ? 59.654  -7.980  78.668  1.00 197.09 ? 1460 VAL B CG1 1 
ATOM   23452 C  CG2 . VAL C 1 1460 ? 60.341  -7.716  76.254  1.00 199.68 ? 1460 VAL B CG2 1 
ATOM   23453 N  N   . ILE C 1 1461 ? 61.785  -5.946  80.162  1.00 182.77 ? 1461 ILE B N   1 
ATOM   23454 C  CA  . ILE C 1 1461 ? 61.802  -5.760  81.608  1.00 178.23 ? 1461 ILE B CA  1 
ATOM   23455 C  C   . ILE C 1 1461 ? 60.574  -5.064  82.185  1.00 179.44 ? 1461 ILE B C   1 
ATOM   23456 O  O   . ILE C 1 1461 ? 60.332  -3.878  81.960  1.00 177.10 ? 1461 ILE B O   1 
ATOM   23457 C  CB  . ILE C 1 1461 ? 63.048  -5.031  82.045  1.00 167.88 ? 1461 ILE B CB  1 
ATOM   23458 C  CG1 . ILE C 1 1461 ? 64.231  -5.994  81.990  1.00 166.44 ? 1461 ILE B CG1 1 
ATOM   23459 C  CG2 . ILE C 1 1461 ? 62.844  -4.527  83.428  1.00 161.84 ? 1461 ILE B CG2 1 
ATOM   23460 C  CD1 . ILE C 1 1461 ? 65.570  -5.317  82.052  1.00 161.79 ? 1461 ILE B CD1 1 
ATOM   23461 N  N   . LEU C 1 1462 ? 59.814  -5.824  82.957  1.00 180.28 ? 1462 LEU B N   1 
ATOM   23462 C  CA  . LEU C 1 1462 ? 58.533  -5.362  83.452  1.00 183.32 ? 1462 LEU B CA  1 
ATOM   23463 C  C   . LEU C 1 1462 ? 58.571  -5.111  84.932  1.00 183.15 ? 1462 LEU B C   1 
ATOM   23464 O  O   . LEU C 1 1462 ? 59.073  -5.943  85.676  1.00 182.50 ? 1462 LEU B O   1 
ATOM   23465 C  CB  . LEU C 1 1462 ? 57.475  -6.413  83.173  1.00 186.80 ? 1462 LEU B CB  1 
ATOM   23466 C  CG  . LEU C 1 1462 ? 57.096  -6.406  81.709  1.00 175.88 ? 1462 LEU B CG  1 
ATOM   23467 C  CD1 . LEU C 1 1462 ? 56.226  -7.587  81.405  1.00 182.29 ? 1462 LEU B CD1 1 
ATOM   23468 C  CD2 . LEU C 1 1462 ? 56.379  -5.110  81.436  1.00 175.38 ? 1462 LEU B CD2 1 
ATOM   23469 N  N   . GLN C 1 1463 ? 58.020  -3.976  85.356  1.00 177.05 ? 1463 GLN B N   1 
ATOM   23470 C  CA  . GLN C 1 1463 ? 57.878  -3.684  86.778  1.00 172.39 ? 1463 GLN B CA  1 
ATOM   23471 C  C   . GLN C 1 1463 ? 56.414  -3.638  87.197  1.00 173.09 ? 1463 GLN B C   1 
ATOM   23472 O  O   . GLN C 1 1463 ? 55.509  -3.413  86.386  1.00 173.83 ? 1463 GLN B O   1 
ATOM   23473 C  CB  . GLN C 1 1463 ? 58.573  -2.366  87.163  1.00 168.73 ? 1463 GLN B CB  1 
ATOM   23474 C  CG  . GLN C 1 1463 ? 59.996  -2.471  87.713  1.00 165.80 ? 1463 GLN B CG  1 
ATOM   23475 C  CD  . GLN C 1 1463 ? 60.578  -1.106  87.965  1.00 164.05 ? 1463 GLN B CD  1 
ATOM   23476 O  OE1 . GLN C 1 1463 ? 61.762  -0.860  87.743  1.00 161.15 ? 1463 GLN B OE1 1 
ATOM   23477 N  NE2 . GLN C 1 1463 ? 59.733  -0.197  88.413  1.00 165.90 ? 1463 GLN B NE2 1 
ATOM   23478 N  N   . LEU C 1 1464 ? 56.212  -3.848  88.488  1.00 189.56 ? 1464 LEU B N   1 
ATOM   23479 C  CA  . LEU C 1 1464 ? 54.901  -3.830  89.087  1.00 192.47 ? 1464 LEU B CA  1 
ATOM   23480 C  C   . LEU C 1 1464 ? 55.069  -3.977  90.568  1.00 192.31 ? 1464 LEU B C   1 
ATOM   23481 O  O   . LEU C 1 1464 ? 56.168  -4.225  91.067  1.00 186.60 ? 1464 LEU B O   1 
ATOM   23482 C  CB  . LEU C 1 1464 ? 54.068  -4.994  88.602  1.00 198.66 ? 1464 LEU B CB  1 
ATOM   23483 C  CG  . LEU C 1 1464 ? 54.778  -6.352  88.499  1.00 197.25 ? 1464 LEU B CG  1 
ATOM   23484 C  CD1 . LEU C 1 1464 ? 55.730  -6.676  89.642  1.00 191.93 ? 1464 LEU B CD1 1 
ATOM   23485 C  CD2 . LEU C 1 1464 ? 53.743  -7.456  88.352  1.00 204.05 ? 1464 LEU B CD2 1 
ATOM   23486 N  N   . ASN C 1 1465 ? 53.948  -3.872  91.261  1.00 199.78 ? 1465 ASN B N   1 
ATOM   23487 C  CA  . ASN C 1 1465 ? 53.932  -3.764  92.707  1.00 201.74 ? 1465 ASN B CA  1 
ATOM   23488 C  C   . ASN C 1 1465 ? 54.012  -5.080  93.464  1.00 204.94 ? 1465 ASN B C   1 
ATOM   23489 O  O   . ASN C 1 1465 ? 54.588  -5.131  94.547  1.00 201.52 ? 1465 ASN B O   1 
ATOM   23490 C  CB  . ASN C 1 1465 ? 52.671  -3.029  93.117  1.00 205.47 ? 1465 ASN B CB  1 
ATOM   23491 C  CG  . ASN C 1 1465 ? 52.353  -1.893  92.188  1.00 205.17 ? 1465 ASN B CG  1 
ATOM   23492 O  OD1 . ASN C 1 1465 ? 52.365  -0.735  92.597  1.00 200.07 ? 1465 ASN B OD1 1 
ATOM   23493 N  ND2 . ASN C 1 1465 ? 52.082  -2.210  90.921  1.00 208.36 ? 1465 ASN B ND2 1 
ATOM   23494 N  N   . SER C 1 1466 ? 53.425  -6.138  92.911  1.00 212.51 ? 1466 SER B N   1 
ATOM   23495 C  CA  . SER C 1 1466 ? 53.353  -7.427  93.614  1.00 218.02 ? 1466 SER B CA  1 
ATOM   23496 C  C   . SER C 1 1466 ? 53.367  -8.607  92.651  1.00 220.84 ? 1466 SER B C   1 
ATOM   23497 O  O   . SER C 1 1466 ? 53.280  -8.431  91.444  1.00 220.17 ? 1466 SER B O   1 
ATOM   23498 C  CB  . SER C 1 1466 ? 52.102  -7.497  94.503  1.00 224.21 ? 1466 SER B CB  1 
ATOM   23499 O  OG  . SER C 1 1466 ? 51.977  -8.755  95.142  1.00 230.06 ? 1466 SER B OG  1 
ATOM   23500 N  N   . ILE C 1 1467 ? 53.510  -9.810  93.194  1.00 189.65 ? 1467 ILE B N   1 
ATOM   23501 C  CA  . ILE C 1 1467 ? 53.369  -11.029 92.411  1.00 196.43 ? 1467 ILE B CA  1 
ATOM   23502 C  C   . ILE C 1 1467 ? 52.585  -12.022 93.254  1.00 204.15 ? 1467 ILE B C   1 
ATOM   23503 O  O   . ILE C 1 1467 ? 53.062  -13.127 93.511  1.00 208.19 ? 1467 ILE B O   1 
ATOM   23504 C  CB  . ILE C 1 1467 ? 54.730  -11.671 92.057  1.00 189.85 ? 1467 ILE B CB  1 
ATOM   23505 C  CG1 . ILE C 1 1467 ? 55.695  -10.652 91.452  1.00 179.96 ? 1467 ILE B CG1 1 
ATOM   23506 C  CG2 . ILE C 1 1467 ? 54.541  -12.839 91.097  1.00 196.52 ? 1467 ILE B CG2 1 
ATOM   23507 C  CD1 . ILE C 1 1467 ? 56.911  -11.290 90.804  1.00 176.16 ? 1467 ILE B CD1 1 
ATOM   23508 N  N   . PRO C 1 1468 ? 51.376  -11.629 93.695  1.00 172.63 ? 1468 PRO B N   1 
ATOM   23509 C  CA  . PRO C 1 1468 ? 50.542  -12.407 94.628  1.00 175.98 ? 1468 PRO B CA  1 
ATOM   23510 C  C   . PRO C 1 1468 ? 50.522  -13.938 94.439  1.00 181.31 ? 1468 PRO B C   1 
ATOM   23511 O  O   . PRO C 1 1468 ? 50.768  -14.471 93.358  1.00 180.33 ? 1468 PRO B O   1 
ATOM   23512 C  CB  . PRO C 1 1468 ? 49.159  -11.779 94.451  1.00 179.32 ? 1468 PRO B CB  1 
ATOM   23513 C  CG  . PRO C 1 1468 ? 49.489  -10.326 94.197  1.00 174.33 ? 1468 PRO B CG  1 
ATOM   23514 C  CD  . PRO C 1 1468 ? 50.747  -10.338 93.357  1.00 170.79 ? 1468 PRO B CD  1 
ATOM   23515 N  N   . SER C 1 1469 ? 50.246  -14.636 95.532  1.00 185.25 ? 1469 SER B N   1 
ATOM   23516 C  CA  . SER C 1 1469 ? 50.525  -16.050 95.594  1.00 190.75 ? 1469 SER B CA  1 
ATOM   23517 C  C   . SER C 1 1469 ? 49.243  -16.820 95.698  1.00 199.52 ? 1469 SER B C   1 
ATOM   23518 O  O   . SER C 1 1469 ? 49.255  -18.015 95.956  1.00 205.62 ? 1469 SER B O   1 
ATOM   23519 C  CB  . SER C 1 1469 ? 51.403  -16.367 96.802  1.00 187.91 ? 1469 SER B CB  1 
ATOM   23520 O  OG  . SER C 1 1469 ? 52.502  -15.476 96.896  1.00 181.50 ? 1469 SER B OG  1 
ATOM   23521 N  N   . SER C 1 1470 ? 48.128  -16.131 95.523  1.00 259.23 ? 1470 SER B N   1 
ATOM   23522 C  CA  . SER C 1 1470 ? 46.843  -16.802 95.413  1.00 265.96 ? 1470 SER B CA  1 
ATOM   23523 C  C   . SER C 1 1470 ? 46.806  -17.637 94.127  1.00 267.39 ? 1470 SER B C   1 
ATOM   23524 O  O   . SER C 1 1470 ? 46.291  -18.757 94.100  1.00 274.04 ? 1470 SER B O   1 
ATOM   23525 C  CB  . SER C 1 1470 ? 45.737  -15.757 95.399  1.00 268.42 ? 1470 SER B CB  1 
ATOM   23526 O  OG  . SER C 1 1470 ? 46.178  -14.606 94.698  1.00 266.07 ? 1470 SER B OG  1 
ATOM   23527 N  N   . ASP C 1 1471 ? 47.371  -17.068 93.066  1.00 229.73 ? 1471 ASP B N   1 
ATOM   23528 C  CA  . ASP C 1 1471 ? 47.510  -17.720 91.767  1.00 232.20 ? 1471 ASP B CA  1 
ATOM   23529 C  C   . ASP C 1 1471 ? 48.704  -17.077 91.076  1.00 219.87 ? 1471 ASP B C   1 
ATOM   23530 O  O   . ASP C 1 1471 ? 49.384  -16.244 91.681  1.00 211.50 ? 1471 ASP B O   1 
ATOM   23531 C  CB  . ASP C 1 1471 ? 46.240  -17.549 90.925  1.00 243.93 ? 1471 ASP B CB  1 
ATOM   23532 C  CG  . ASP C 1 1471 ? 45.860  -16.085 90.699  1.00 246.60 ? 1471 ASP B CG  1 
ATOM   23533 O  OD1 . ASP C 1 1471 ? 44.654  -15.797 90.563  1.00 253.33 ? 1471 ASP B OD1 1 
ATOM   23534 O  OD2 . ASP C 1 1471 ? 46.752  -15.219 90.652  1.00 240.84 ? 1471 ASP B OD2 1 
ATOM   23535 N  N   . PHE C 1 1472 ? 48.980  -17.455 89.832  1.00 204.79 ? 1472 PHE B N   1 
ATOM   23536 C  CA  . PHE C 1 1472 ? 50.073  -16.821 89.103  1.00 194.47 ? 1472 PHE B CA  1 
ATOM   23537 C  C   . PHE C 1 1472 ? 49.727  -15.389 88.732  1.00 189.85 ? 1472 PHE B C   1 
ATOM   23538 O  O   . PHE C 1 1472 ? 48.682  -14.859 89.107  1.00 191.01 ? 1472 PHE B O   1 
ATOM   23539 C  CB  . PHE C 1 1472 ? 50.411  -17.566 87.819  1.00 196.82 ? 1472 PHE B CB  1 
ATOM   23540 C  CG  . PHE C 1 1472 ? 51.131  -18.859 88.025  1.00 197.22 ? 1472 PHE B CG  1 
ATOM   23541 C  CD1 . PHE C 1 1472 ? 50.557  -19.884 88.762  1.00 202.94 ? 1472 PHE B CD1 1 
ATOM   23542 C  CD2 . PHE C 1 1472 ? 52.364  -19.072 87.435  1.00 194.26 ? 1472 PHE B CD2 1 
ATOM   23543 C  CE1 . PHE C 1 1472 ? 51.215  -21.092 88.934  1.00 204.63 ? 1472 PHE B CE1 1 
ATOM   23544 C  CE2 . PHE C 1 1472 ? 53.025  -20.275 87.596  1.00 195.89 ? 1472 PHE B CE2 1 
ATOM   23545 C  CZ  . PHE C 1 1472 ? 52.450  -21.290 88.348  1.00 201.09 ? 1472 PHE B CZ  1 
ATOM   23546 N  N   . LEU C 1 1473 ? 50.622  -14.780 87.970  1.00 253.28 ? 1473 LEU B N   1 
ATOM   23547 C  CA  . LEU C 1 1473 ? 50.395  -13.478 87.379  1.00 251.67 ? 1473 LEU B CA  1 
ATOM   23548 C  C   . LEU C 1 1473 ? 51.135  -13.495 86.049  1.00 253.71 ? 1473 LEU B C   1 
ATOM   23549 O  O   . LEU C 1 1473 ? 52.366  -13.603 86.029  1.00 250.01 ? 1473 LEU B O   1 
ATOM   23550 C  CB  . LEU C 1 1473 ? 50.936  -12.379 88.295  1.00 241.65 ? 1473 LEU B CB  1 
ATOM   23551 C  CG  . LEU C 1 1473 ? 50.970  -10.956 87.738  1.00 238.54 ? 1473 LEU B CG  1 
ATOM   23552 C  CD1 . LEU C 1 1473 ? 50.485  -9.965  88.774  1.00 236.59 ? 1473 LEU B CD1 1 
ATOM   23553 C  CD2 . LEU C 1 1473 ? 52.369  -10.609 87.264  1.00 233.22 ? 1473 LEU B CD2 1 
ATOM   23554 N  N   . CYS C 1 1474 ? 50.394  -13.411 84.940  1.00 202.92 ? 1474 CYS B N   1 
ATOM   23555 C  CA  . CYS C 1 1474 ? 51.009  -13.591 83.622  1.00 201.35 ? 1474 CYS B CA  1 
ATOM   23556 C  C   . CYS C 1 1474 ? 50.927  -12.443 82.621  1.00 201.29 ? 1474 CYS B C   1 
ATOM   23557 O  O   . CYS C 1 1474 ? 49.884  -11.815 82.431  1.00 205.04 ? 1474 CYS B O   1 
ATOM   23558 C  CB  . CYS C 1 1474 ? 50.537  -14.890 82.973  1.00 205.16 ? 1474 CYS B CB  1 
ATOM   23559 S  SG  . CYS C 1 1474 ? 51.804  -16.183 83.034  1.00 216.87 ? 1474 CYS B SG  1 
ATOM   23560 N  N   . VAL C 1 1475 ? 52.065  -12.208 81.980  1.00 224.28 ? 1475 VAL B N   1 
ATOM   23561 C  CA  . VAL C 1 1475 ? 52.205  -11.252 80.898  1.00 225.10 ? 1475 VAL B CA  1 
ATOM   23562 C  C   . VAL C 1 1475 ? 51.990  -11.988 79.572  1.00 233.50 ? 1475 VAL B C   1 
ATOM   23563 O  O   . VAL C 1 1475 ? 51.988  -13.221 79.537  1.00 236.47 ? 1475 VAL B O   1 
ATOM   23564 C  CB  . VAL C 1 1475 ? 53.628  -10.689 80.915  1.00 215.82 ? 1475 VAL B CB  1 
ATOM   23565 C  CG1 . VAL C 1 1475 ? 54.643  -11.842 80.957  1.00 215.30 ? 1475 VAL B CG1 1 
ATOM   23566 C  CG2 . VAL C 1 1475 ? 53.867  -9.765  79.728  1.00 213.93 ? 1475 VAL B CG2 1 
ATOM   23567 N  N   . ARG C 1 1476 ? 51.792  -11.244 78.485  1.00 206.95 ? 1476 ARG B N   1 
ATOM   23568 C  CA  . ARG C 1 1476 ? 51.812  -11.838 77.153  1.00 209.36 ? 1476 ARG B CA  1 
ATOM   23569 C  C   . ARG C 1 1476 ? 52.088  -10.802 76.079  1.00 203.18 ? 1476 ARG B C   1 
ATOM   23570 O  O   . ARG C 1 1476 ? 51.536  -9.698  76.098  1.00 199.08 ? 1476 ARG B O   1 
ATOM   23571 C  CB  . ARG C 1 1476 ? 50.517  -12.588 76.844  1.00 219.76 ? 1476 ARG B CB  1 
ATOM   23572 C  CG  . ARG C 1 1476 ? 49.293  -11.949 77.429  1.00 226.45 ? 1476 ARG B CG  1 
ATOM   23573 C  CD  . ARG C 1 1476 ? 48.931  -12.626 78.734  1.00 233.33 ? 1476 ARG B CD  1 
ATOM   23574 N  NE  . ARG C 1 1476 ? 48.228  -11.719 79.627  1.00 237.80 ? 1476 ARG B NE  1 
ATOM   23575 C  CZ  . ARG C 1 1476 ? 47.478  -12.120 80.645  1.00 244.41 ? 1476 ARG B CZ  1 
ATOM   23576 N  NH1 . ARG C 1 1476 ? 47.322  -13.419 80.893  1.00 249.51 ? 1476 ARG B NH1 1 
ATOM   23577 N  NH2 . ARG C 1 1476 ? 46.878  -11.216 81.407  1.00 243.18 ? 1476 ARG B NH2 1 
ATOM   23578 N  N   . PHE C 1 1477 ? 52.953  -11.188 75.147  1.00 236.07 ? 1477 PHE B N   1 
ATOM   23579 C  CA  . PHE C 1 1477 ? 53.376  -10.330 74.048  1.00 233.35 ? 1477 PHE B CA  1 
ATOM   23580 C  C   . PHE C 1 1477 ? 53.843  -11.183 72.863  1.00 236.85 ? 1477 PHE B C   1 
ATOM   23581 O  O   . PHE C 1 1477 ? 54.217  -12.338 73.032  1.00 238.87 ? 1477 PHE B O   1 
ATOM   23582 C  CB  . PHE C 1 1477 ? 54.472  -9.355  74.505  1.00 224.07 ? 1477 PHE B CB  1 
ATOM   23583 C  CG  . PHE C 1 1477 ? 55.774  -10.017 74.885  1.00 221.16 ? 1477 PHE B CG  1 
ATOM   23584 C  CD1 . PHE C 1 1477 ? 56.922  -9.792  74.145  1.00 219.13 ? 1477 PHE B CD1 1 
ATOM   23585 C  CD2 . PHE C 1 1477 ? 55.851  -10.854 75.980  1.00 220.39 ? 1477 PHE B CD2 1 
ATOM   23586 C  CE1 . PHE C 1 1477 ? 58.116  -10.391 74.490  1.00 216.33 ? 1477 PHE B CE1 1 
ATOM   23587 C  CE2 . PHE C 1 1477 ? 57.044  -11.456 76.321  1.00 218.21 ? 1477 PHE B CE2 1 
ATOM   23588 C  CZ  . PHE C 1 1477 ? 58.177  -11.221 75.573  1.00 215.70 ? 1477 PHE B CZ  1 
ATOM   23589 N  N   . ARG C 1 1478 ? 53.822  -10.613 71.667  1.00 166.66 ? 1478 ARG B N   1 
ATOM   23590 C  CA  . ARG C 1 1478 ? 54.062  -11.389 70.468  1.00 169.92 ? 1478 ARG B CA  1 
ATOM   23591 C  C   . ARG C 1 1478 ? 55.434  -11.047 69.894  1.00 165.84 ? 1478 ARG B C   1 
ATOM   23592 O  O   . ARG C 1 1478 ? 56.030  -10.021 70.252  1.00 155.73 ? 1478 ARG B O   1 
ATOM   23593 C  CB  . ARG C 1 1478 ? 52.915  -11.119 69.507  1.00 175.29 ? 1478 ARG B CB  1 
ATOM   23594 C  CG  . ARG C 1 1478 ? 51.603  -10.942 70.299  1.00 178.67 ? 1478 ARG B CG  1 
ATOM   23595 C  CD  . ARG C 1 1478 ? 50.369  -10.562 69.477  1.00 186.95 ? 1478 ARG B CD  1 
ATOM   23596 N  NE  . ARG C 1 1478 ? 50.215  -9.130  69.227  1.00 184.69 ? 1478 ARG B NE  1 
ATOM   23597 C  CZ  . ARG C 1 1478 ? 49.056  -8.548  68.919  1.00 188.27 ? 1478 ARG B CZ  1 
ATOM   23598 N  NH1 . ARG C 1 1478 ? 47.943  -9.276  68.845  1.00 195.77 ? 1478 ARG B NH1 1 
ATOM   23599 N  NH2 . ARG C 1 1478 ? 49.003  -7.236  68.694  1.00 185.03 ? 1478 ARG B NH2 1 
ATOM   23600 N  N   . ILE C 1 1479 ? 55.954  -11.920 69.034  1.00 190.42 ? 1479 ILE B N   1 
ATOM   23601 C  CA  . ILE C 1 1479 ? 57.334  -11.771 68.555  1.00 193.23 ? 1479 ILE B CA  1 
ATOM   23602 C  C   . ILE C 1 1479 ? 57.590  -12.218 67.096  1.00 202.52 ? 1479 ILE B C   1 
ATOM   23603 O  O   . ILE C 1 1479 ? 57.085  -13.245 66.639  1.00 209.79 ? 1479 ILE B O   1 
ATOM   23604 C  CB  . ILE C 1 1479 ? 58.355  -12.447 69.527  1.00 191.26 ? 1479 ILE B CB  1 
ATOM   23605 C  CG1 . ILE C 1 1479 ? 57.939  -13.886 69.846  1.00 197.11 ? 1479 ILE B CG1 1 
ATOM   23606 C  CG2 . ILE C 1 1479 ? 58.458  -11.656 70.814  1.00 187.87 ? 1479 ILE B CG2 1 
ATOM   23607 C  CD1 . ILE C 1 1479 ? 58.917  -14.631 70.701  1.00 193.89 ? 1479 ILE B CD1 1 
ATOM   23608 N  N   . PHE C 1 1480 ? 58.392  -11.426 66.384  1.00 253.77 ? 1480 PHE B N   1 
ATOM   23609 C  CA  . PHE C 1 1480 ? 58.669  -11.640 64.966  1.00 266.39 ? 1480 PHE B CA  1 
ATOM   23610 C  C   . PHE C 1 1480 ? 60.157  -11.671 64.668  1.00 257.84 ? 1480 PHE B C   1 
ATOM   23611 O  O   . PHE C 1 1480 ? 60.813  -10.630 64.616  1.00 252.64 ? 1480 PHE B O   1 
ATOM   23612 C  CB  . PHE C 1 1480 ? 58.036  -10.530 64.131  1.00 286.40 ? 1480 PHE B CB  1 
ATOM   23613 C  CG  . PHE C 1 1480 ? 57.873  -9.228  64.868  1.00 290.83 ? 1480 PHE B CG  1 
ATOM   23614 C  CD1 . PHE C 1 1480 ? 58.964  -8.586  65.432  1.00 284.84 ? 1480 PHE B CD1 1 
ATOM   23615 C  CD2 . PHE C 1 1480 ? 56.620  -8.640  64.983  1.00 295.76 ? 1480 PHE B CD2 1 
ATOM   23616 C  CE1 . PHE C 1 1480 ? 58.805  -7.392  66.104  1.00 279.55 ? 1480 PHE B CE1 1 
ATOM   23617 C  CE2 . PHE C 1 1480 ? 56.454  -7.449  65.650  1.00 289.91 ? 1480 PHE B CE2 1 
ATOM   23618 C  CZ  . PHE C 1 1480 ? 57.547  -6.822  66.211  1.00 282.18 ? 1480 PHE B CZ  1 
ATOM   23619 N  N   . GLU C 1 1481 ? 60.681  -12.867 64.446  1.00 204.34 ? 1481 GLU B N   1 
ATOM   23620 C  CA  . GLU C 1 1481 ? 62.101  -13.018 64.180  1.00 200.59 ? 1481 GLU B CA  1 
ATOM   23621 C  C   . GLU C 1 1481 ? 62.540  -11.918 63.238  1.00 198.26 ? 1481 GLU B C   1 
ATOM   23622 O  O   . GLU C 1 1481 ? 62.061  -11.850 62.121  1.00 203.69 ? 1481 GLU B O   1 
ATOM   23623 C  CB  . GLU C 1 1481 ? 62.387  -14.387 63.551  1.00 206.16 ? 1481 GLU B CB  1 
ATOM   23624 C  CG  . GLU C 1 1481 ? 61.982  -15.569 64.422  1.00 240.88 ? 1481 GLU B CG  1 
ATOM   23625 C  CD  . GLU C 1 1481 ? 62.375  -16.919 63.838  1.00 245.52 ? 1481 GLU B CD  1 
ATOM   23626 O  OE1 . GLU C 1 1481 ? 63.318  -16.987 63.015  1.00 246.33 ? 1481 GLU B OE1 1 
ATOM   23627 O  OE2 . GLU C 1 1481 ? 61.734  -17.917 64.225  1.00 248.30 ? 1481 GLU B OE2 1 
ATOM   23628 N  N   . LEU C 1 1482 ? 63.432  -11.049 63.700  1.00 192.71 ? 1482 LEU B N   1 
ATOM   23629 C  CA  . LEU C 1 1482 ? 63.981  -9.980  62.872  1.00 188.73 ? 1482 LEU B CA  1 
ATOM   23630 C  C   . LEU C 1 1482 ? 64.977  -10.552 61.874  1.00 187.57 ? 1482 LEU B C   1 
ATOM   23631 O  O   . LEU C 1 1482 ? 65.342  -9.889  60.906  1.00 188.33 ? 1482 LEU B O   1 
ATOM   23632 C  CB  . LEU C 1 1482 ? 64.624  -8.891  63.748  1.00 182.77 ? 1482 LEU B CB  1 
ATOM   23633 C  CG  . LEU C 1 1482 ? 65.508  -7.745  63.213  1.00 181.50 ? 1482 LEU B CG  1 
ATOM   23634 C  CD1 . LEU C 1 1482 ? 65.513  -6.524  64.155  1.00 175.38 ? 1482 LEU B CD1 1 
ATOM   23635 C  CD2 . LEU C 1 1482 ? 66.941  -8.205  62.946  1.00 180.61 ? 1482 LEU B CD2 1 
ATOM   23636 N  N   . PHE C 1 1483 ? 65.419  -11.785 62.110  1.00 198.86 ? 1483 PHE B N   1 
ATOM   23637 C  CA  . PHE C 1 1483 ? 66.169  -12.516 61.087  1.00 200.61 ? 1483 PHE B CA  1 
ATOM   23638 C  C   . PHE C 1 1483 ? 66.453  -13.997 61.376  1.00 206.09 ? 1483 PHE B C   1 
ATOM   23639 O  O   . PHE C 1 1483 ? 65.955  -14.589 62.338  1.00 206.61 ? 1483 PHE B O   1 
ATOM   23640 C  CB  . PHE C 1 1483 ? 67.446  -11.777 60.659  1.00 192.67 ? 1483 PHE B CB  1 
ATOM   23641 C  CG  . PHE C 1 1483 ? 68.398  -11.523 61.776  1.00 183.10 ? 1483 PHE B CG  1 
ATOM   23642 C  CD1 . PHE C 1 1483 ? 68.270  -12.202 62.981  1.00 180.56 ? 1483 PHE B CD1 1 
ATOM   23643 C  CD2 . PHE C 1 1483 ? 69.426  -10.613 61.630  1.00 177.39 ? 1483 PHE B CD2 1 
ATOM   23644 C  CE1 . PHE C 1 1483 ? 69.150  -11.978 64.027  1.00 171.49 ? 1483 PHE B CE1 1 
ATOM   23645 C  CE2 . PHE C 1 1483 ? 70.308  -10.383 62.662  1.00 169.41 ? 1483 PHE B CE2 1 
ATOM   23646 C  CZ  . PHE C 1 1483 ? 70.169  -11.068 63.867  1.00 166.45 ? 1483 PHE B CZ  1 
ATOM   23647 N  N   . GLU C 1 1484 ? 67.264  -14.582 60.509  1.00 250.45 ? 1484 GLU B N   1 
ATOM   23648 C  CA  . GLU C 1 1484 ? 67.366  -16.022 60.429  1.00 258.54 ? 1484 GLU B CA  1 
ATOM   23649 C  C   . GLU C 1 1484 ? 68.428  -16.505 61.386  1.00 253.88 ? 1484 GLU B C   1 
ATOM   23650 O  O   . GLU C 1 1484 ? 69.614  -16.232 61.215  1.00 252.23 ? 1484 GLU B O   1 
ATOM   23651 C  CB  . GLU C 1 1484 ? 67.638  -16.460 58.982  1.00 271.28 ? 1484 GLU B CB  1 
ATOM   23652 C  CG  . GLU C 1 1484 ? 66.455  -16.231 57.986  1.00 283.49 ? 1484 GLU B CG  1 
ATOM   23653 C  CD  . GLU C 1 1484 ? 66.419  -14.833 57.341  1.00 286.47 ? 1484 GLU B CD  1 
ATOM   23654 O  OE1 . GLU C 1 1484 ? 67.265  -13.980 57.696  1.00 282.46 ? 1484 GLU B OE1 1 
ATOM   23655 O  OE2 . GLU C 1 1484 ? 65.539  -14.592 56.477  1.00 291.70 ? 1484 GLU B OE2 1 
ATOM   23656 N  N   . VAL C 1 1485 ? 67.978  -17.220 62.404  1.00 214.10 ? 1485 VAL B N   1 
ATOM   23657 C  CA  . VAL C 1 1485 ? 68.842  -17.610 63.496  1.00 206.39 ? 1485 VAL B CA  1 
ATOM   23658 C  C   . VAL C 1 1485 ? 69.056  -19.110 63.528  1.00 208.16 ? 1485 VAL B C   1 
ATOM   23659 O  O   . VAL C 1 1485 ? 68.096  -19.873 63.586  1.00 211.09 ? 1485 VAL B O   1 
ATOM   23660 C  CB  . VAL C 1 1485 ? 68.232  -17.170 64.818  1.00 220.44 ? 1485 VAL B CB  1 
ATOM   23661 C  CG1 . VAL C 1 1485 ? 68.529  -15.703 65.046  1.00 214.06 ? 1485 VAL B CG1 1 
ATOM   23662 C  CG2 . VAL C 1 1485 ? 66.726  -17.430 64.812  1.00 225.49 ? 1485 VAL B CG2 1 
ATOM   23663 N  N   . GLY C 1 1486 ? 70.320  -19.522 63.508  1.00 222.79 ? 1486 GLY B N   1 
ATOM   23664 C  CA  . GLY C 1 1486 ? 70.678  -20.926 63.433  1.00 225.79 ? 1486 GLY B CA  1 
ATOM   23665 C  C   . GLY C 1 1486 ? 70.170  -21.718 64.611  1.00 223.87 ? 1486 GLY B C   1 
ATOM   23666 O  O   . GLY C 1 1486 ? 69.187  -21.342 65.242  1.00 225.72 ? 1486 GLY B O   1 
ATOM   23667 N  N   . PHE C 1 1487 ? 70.821  -22.832 64.901  1.00 250.37 ? 1487 PHE B N   1 
ATOM   23668 C  CA  . PHE C 1 1487 ? 70.544  -23.525 66.139  1.00 250.06 ? 1487 PHE B CA  1 
ATOM   23669 C  C   . PHE C 1 1487 ? 70.716  -22.483 67.229  1.00 239.75 ? 1487 PHE B C   1 
ATOM   23670 O  O   . PHE C 1 1487 ? 71.835  -22.030 67.464  1.00 233.91 ? 1487 PHE B O   1 
ATOM   23671 C  CB  . PHE C 1 1487 ? 71.556  -24.644 66.344  1.00 255.14 ? 1487 PHE B CB  1 
ATOM   23672 C  CG  . PHE C 1 1487 ? 72.459  -24.862 65.163  1.00 260.64 ? 1487 PHE B CG  1 
ATOM   23673 C  CD1 . PHE C 1 1487 ? 72.538  -26.103 64.549  1.00 267.88 ? 1487 PHE B CD1 1 
ATOM   23674 C  CD2 . PHE C 1 1487 ? 73.225  -23.823 64.663  1.00 257.93 ? 1487 PHE B CD2 1 
ATOM   23675 C  CE1 . PHE C 1 1487 ? 73.367  -26.300 63.460  1.00 270.96 ? 1487 PHE B CE1 1 
ATOM   23676 C  CE2 . PHE C 1 1487 ? 74.048  -24.013 63.575  1.00 261.07 ? 1487 PHE B CE2 1 
ATOM   23677 C  CZ  . PHE C 1 1487 ? 74.122  -25.254 62.972  1.00 267.43 ? 1487 PHE B CZ  1 
ATOM   23678 N  N   . LEU C 1 1488 ? 69.622  -22.082 67.876  1.00 228.53 ? 1488 LEU B N   1 
ATOM   23679 C  CA  . LEU C 1 1488 ? 69.713  -21.061 68.927  1.00 220.71 ? 1488 LEU B CA  1 
ATOM   23680 C  C   . LEU C 1 1488 ? 69.865  -21.603 70.350  1.00 219.41 ? 1488 LEU B C   1 
ATOM   23681 O  O   . LEU C 1 1488 ? 69.215  -22.596 70.703  1.00 224.32 ? 1488 LEU B O   1 
ATOM   23682 C  CB  . LEU C 1 1488 ? 68.550  -20.057 68.866  1.00 219.17 ? 1488 LEU B CB  1 
ATOM   23683 C  CG  . LEU C 1 1488 ? 67.150  -20.249 69.467  1.00 221.18 ? 1488 LEU B CG  1 
ATOM   23684 C  CD1 . LEU C 1 1488 ? 67.107  -20.838 70.867  1.00 219.79 ? 1488 LEU B CD1 1 
ATOM   23685 C  CD2 . LEU C 1 1488 ? 66.474  -18.899 69.473  1.00 218.39 ? 1488 LEU B CD2 1 
ATOM   23686 N  N   . SER C 1 1489 ? 70.713  -20.945 71.156  1.00 175.70 ? 1489 SER B N   1 
ATOM   23687 C  CA  . SER C 1 1489 ? 70.826  -21.232 72.593  1.00 169.54 ? 1489 SER B CA  1 
ATOM   23688 C  C   . SER C 1 1489 ? 69.785  -20.409 73.345  1.00 164.78 ? 1489 SER B C   1 
ATOM   23689 O  O   . SER C 1 1489 ? 69.746  -19.187 73.193  1.00 162.79 ? 1489 SER B O   1 
ATOM   23690 C  CB  . SER C 1 1489 ? 72.239  -20.949 73.112  1.00 160.00 ? 1489 SER B CB  1 
ATOM   23691 O  OG  . SER C 1 1489 ? 72.404  -19.588 73.434  1.00 153.33 ? 1489 SER B OG  1 
ATOM   23692 N  N   . PRO C 1 1490 ? 68.933  -21.083 74.144  1.00 206.39 ? 1490 PRO B N   1 
ATOM   23693 C  CA  . PRO C 1 1490 ? 67.720  -20.499 74.731  1.00 203.35 ? 1490 PRO B CA  1 
ATOM   23694 C  C   . PRO C 1 1490 ? 68.004  -19.178 75.420  1.00 198.75 ? 1490 PRO B C   1 
ATOM   23695 O  O   . PRO C 1 1490 ? 69.161  -18.874 75.697  1.00 192.13 ? 1490 PRO B O   1 
ATOM   23696 C  CB  . PRO C 1 1490 ? 67.302  -21.532 75.777  1.00 204.94 ? 1490 PRO B CB  1 
ATOM   23697 C  CG  . PRO C 1 1490 ? 67.886  -22.799 75.326  1.00 209.85 ? 1490 PRO B CG  1 
ATOM   23698 C  CD  . PRO C 1 1490 ? 69.174  -22.448 74.637  1.00 207.06 ? 1490 PRO B CD  1 
ATOM   23699 N  N   . ALA C 1 1491 ? 66.966  -18.389 75.674  1.00 208.51 ? 1491 ALA B N   1 
ATOM   23700 C  CA  . ALA C 1 1491 ? 67.133  -17.198 76.489  1.00 203.47 ? 1491 ALA B CA  1 
ATOM   23701 C  C   . ALA C 1 1491 ? 66.714  -17.520 77.909  1.00 206.29 ? 1491 ALA B C   1 
ATOM   23702 O  O   . ALA C 1 1491 ? 66.586  -18.687 78.275  1.00 207.51 ? 1491 ALA B O   1 
ATOM   23703 C  CB  . ALA C 1 1491 ? 66.340  -16.030 75.932  1.00 200.92 ? 1491 ALA B CB  1 
ATOM   23704 N  N   . THR C 1 1492 ? 66.489  -16.489 78.708  1.00 183.41 ? 1492 THR B N   1 
ATOM   23705 C  CA  . THR C 1 1492 ? 66.343  -16.697 80.132  1.00 181.03 ? 1492 THR B CA  1 
ATOM   23706 C  C   . THR C 1 1492 ? 65.227  -15.863 80.730  1.00 183.25 ? 1492 THR B C   1 
ATOM   23707 O  O   . THR C 1 1492 ? 65.251  -14.641 80.671  1.00 180.36 ? 1492 THR B O   1 
ATOM   23708 C  CB  . THR C 1 1492 ? 67.674  -16.386 80.836  1.00 170.94 ? 1492 THR B CB  1 
ATOM   23709 O  OG1 . THR C 1 1492 ? 68.101  -15.046 80.526  1.00 155.02 ? 1492 THR B OG1 1 
ATOM   23710 C  CG2 . THR C 1 1492 ? 68.737  -17.373 80.374  1.00 160.87 ? 1492 THR B CG2 1 
ATOM   23711 N  N   . PHE C 1 1493 ? 64.232  -16.526 81.294  1.00 187.50 ? 1493 PHE B N   1 
ATOM   23712 C  CA  . PHE C 1 1493 ? 63.199  -15.797 81.996  1.00 184.54 ? 1493 PHE B CA  1 
ATOM   23713 C  C   . PHE C 1 1493 ? 63.568  -15.793 83.451  1.00 184.51 ? 1493 PHE B C   1 
ATOM   23714 O  O   . PHE C 1 1493 ? 63.560  -16.856 84.085  1.00 187.11 ? 1493 PHE B O   1 
ATOM   23715 C  CB  . PHE C 1 1493 ? 61.845  -16.462 81.816  1.00 184.44 ? 1493 PHE B CB  1 
ATOM   23716 C  CG  . PHE C 1 1493 ? 60.754  -15.899 82.701  1.00 179.06 ? 1493 PHE B CG  1 
ATOM   23717 C  CD1 . PHE C 1 1493 ? 60.580  -14.520 82.845  1.00 172.57 ? 1493 PHE B CD1 1 
ATOM   23718 C  CD2 . PHE C 1 1493 ? 59.876  -16.761 83.364  1.00 182.21 ? 1493 PHE B CD2 1 
ATOM   23719 C  CE1 . PHE C 1 1493 ? 59.557  -14.012 83.653  1.00 172.88 ? 1493 PHE B CE1 1 
ATOM   23720 C  CE2 . PHE C 1 1493 ? 58.851  -16.271 84.161  1.00 181.38 ? 1493 PHE B CE2 1 
ATOM   23721 C  CZ  . PHE C 1 1493 ? 58.689  -14.893 84.310  1.00 177.32 ? 1493 PHE B CZ  1 
ATOM   23722 N  N   . THR C 1 1494 ? 63.896  -14.603 83.968  1.00 154.31 ? 1494 THR B N   1 
ATOM   23723 C  CA  . THR C 1 1494 ? 64.236  -14.405 85.384  1.00 150.11 ? 1494 THR B CA  1 
ATOM   23724 C  C   . THR C 1 1494 ? 63.257  -13.427 86.085  1.00 145.23 ? 1494 THR B C   1 
ATOM   23725 O  O   . THR C 1 1494 ? 62.793  -12.453 85.485  1.00 143.96 ? 1494 THR B O   1 
ATOM   23726 C  CB  . THR C 1 1494 ? 65.739  -14.020 85.553  1.00 142.22 ? 1494 THR B CB  1 
ATOM   23727 O  OG1 . THR C 1 1494 ? 66.046  -13.806 86.930  1.00 137.94 ? 1494 THR B OG1 1 
ATOM   23728 C  CG2 . THR C 1 1494 ? 66.103  -12.806 84.730  1.00 137.78 ? 1494 THR B CG2 1 
ATOM   23729 N  N   . VAL C 1 1495 ? 62.901  -13.726 87.334  1.00 168.01 ? 1495 VAL B N   1 
ATOM   23730 C  CA  . VAL C 1 1495 ? 61.984  -12.869 88.102  1.00 173.14 ? 1495 VAL B CA  1 
ATOM   23731 C  C   . VAL C 1 1495 ? 62.425  -12.683 89.577  1.00 173.02 ? 1495 VAL B C   1 
ATOM   23732 O  O   . VAL C 1 1495 ? 62.389  -13.634 90.381  1.00 179.27 ? 1495 VAL B O   1 
ATOM   23733 C  CB  . VAL C 1 1495 ? 60.527  -13.391 88.061  1.00 163.46 ? 1495 VAL B CB  1 
ATOM   23734 C  CG1 . VAL C 1 1495 ? 60.396  -14.686 88.858  1.00 175.87 ? 1495 VAL B CG1 1 
ATOM   23735 C  CG2 . VAL C 1 1495 ? 59.562  -12.326 88.581  1.00 163.52 ? 1495 VAL B CG2 1 
ATOM   23736 N  N   . TYR C 1 1496 ? 62.836  -11.454 89.923  1.00 186.68 ? 1496 TYR B N   1 
ATOM   23737 C  CA  . TYR C 1 1496 ? 63.270  -11.117 91.287  1.00 181.89 ? 1496 TYR B CA  1 
ATOM   23738 C  C   . TYR C 1 1496 ? 62.589  -9.861  91.851  1.00 180.35 ? 1496 TYR B C   1 
ATOM   23739 O  O   . TYR C 1 1496 ? 62.112  -8.999  91.103  1.00 179.26 ? 1496 TYR B O   1 
ATOM   23740 C  CB  . TYR C 1 1496 ? 64.801  -11.007 91.382  1.00 175.47 ? 1496 TYR B CB  1 
ATOM   23741 C  CG  . TYR C 1 1496 ? 65.464  -9.939  90.517  1.00 173.35 ? 1496 TYR B CG  1 
ATOM   23742 C  CD1 . TYR C 1 1496 ? 64.745  -8.867  90.017  1.00 172.16 ? 1496 TYR B CD1 1 
ATOM   23743 C  CD2 . TYR C 1 1496 ? 66.830  -9.997  90.226  1.00 170.37 ? 1496 TYR B CD2 1 
ATOM   23744 C  CE1 . TYR C 1 1496 ? 65.363  -7.890  89.243  1.00 167.95 ? 1496 TYR B CE1 1 
ATOM   23745 C  CE2 . TYR C 1 1496 ? 67.456  -9.020  89.452  1.00 166.70 ? 1496 TYR B CE2 1 
ATOM   23746 C  CZ  . TYR C 1 1496 ? 66.714  -7.972  88.965  1.00 165.85 ? 1496 TYR B CZ  1 
ATOM   23747 O  OH  . TYR C 1 1496 ? 67.306  -7.000  88.199  1.00 162.69 ? 1496 TYR B OH  1 
ATOM   23748 N  N   . GLU C 1 1497 ? 62.556  -9.779  93.182  1.00 210.40 ? 1497 GLU B N   1 
ATOM   23749 C  CA  . GLU C 1 1497 ? 61.914  -8.682  93.922  1.00 207.08 ? 1497 GLU B CA  1 
ATOM   23750 C  C   . GLU C 1 1497 ? 62.810  -7.447  94.041  1.00 200.48 ? 1497 GLU B C   1 
ATOM   23751 O  O   . GLU C 1 1497 ? 63.921  -7.529  94.577  1.00 194.56 ? 1497 GLU B O   1 
ATOM   23752 C  CB  . GLU C 1 1497 ? 61.539  -9.168  95.320  1.00 206.19 ? 1497 GLU B CB  1 
ATOM   23753 C  CG  . GLU C 1 1497 ? 60.532  -8.314  96.050  1.00 205.30 ? 1497 GLU B CG  1 
ATOM   23754 C  CD  . GLU C 1 1497 ? 59.930  -9.053  97.229  1.00 206.57 ? 1497 GLU B CD  1 
ATOM   23755 O  OE1 . GLU C 1 1497 ? 60.398  -10.172 97.535  1.00 204.72 ? 1497 GLU B OE1 1 
ATOM   23756 O  OE2 . GLU C 1 1497 ? 58.988  -8.528  97.851  1.00 209.16 ? 1497 GLU B OE2 1 
ATOM   23757 N  N   . TYR C 1 1498 ? 62.324  -6.302  93.566  1.00 192.59 ? 1498 TYR B N   1 
ATOM   23758 C  CA  . TYR C 1 1498 ? 63.201  -5.150  93.423  1.00 189.61 ? 1498 TYR B CA  1 
ATOM   23759 C  C   . TYR C 1 1498 ? 64.024  -4.987  94.675  1.00 184.47 ? 1498 TYR B C   1 
ATOM   23760 O  O   . TYR C 1 1498 ? 65.248  -4.940  94.624  1.00 179.52 ? 1498 TYR B O   1 
ATOM   23761 C  CB  . TYR C 1 1498 ? 62.430  -3.861  93.142  1.00 190.66 ? 1498 TYR B CB  1 
ATOM   23762 C  CG  . TYR C 1 1498 ? 63.316  -2.741  92.623  1.00 188.97 ? 1498 TYR B CG  1 
ATOM   23763 C  CD1 . TYR C 1 1498 ? 64.029  -2.892  91.444  1.00 191.33 ? 1498 TYR B CD1 1 
ATOM   23764 C  CD2 . TYR C 1 1498 ? 63.431  -1.540  93.302  1.00 186.23 ? 1498 TYR B CD2 1 
ATOM   23765 C  CE1 . TYR C 1 1498 ? 64.827  -1.884  90.956  1.00 188.92 ? 1498 TYR B CE1 1 
ATOM   23766 C  CE2 . TYR C 1 1498 ? 64.227  -0.526  92.818  1.00 184.18 ? 1498 TYR B CE2 1 
ATOM   23767 C  CZ  . TYR C 1 1498 ? 64.925  -0.708  91.647  1.00 185.90 ? 1498 TYR B CZ  1 
ATOM   23768 O  OH  . TYR C 1 1498 ? 65.724  0.288   91.150  1.00 184.86 ? 1498 TYR B OH  1 
ATOM   23769 N  N   . HIS C 1 1499 ? 63.352  -4.923  95.813  1.00 164.00 ? 1499 HIS B N   1 
ATOM   23770 C  CA  . HIS C 1 1499 ? 64.060  -4.571  97.026  1.00 158.25 ? 1499 HIS B CA  1 
ATOM   23771 C  C   . HIS C 1 1499 ? 64.901  -5.685  97.627  1.00 162.31 ? 1499 HIS B C   1 
ATOM   23772 O  O   . HIS C 1 1499 ? 65.857  -5.393  98.321  1.00 163.39 ? 1499 HIS B O   1 
ATOM   23773 C  CB  . HIS C 1 1499 ? 63.148  -3.889  98.043  1.00 153.18 ? 1499 HIS B CB  1 
ATOM   23774 C  CG  . HIS C 1 1499 ? 62.840  -2.473  97.683  1.00 147.62 ? 1499 HIS B CG  1 
ATOM   23775 N  ND1 . HIS C 1 1499 ? 61.592  -1.909  97.851  1.00 150.09 ? 1499 HIS B ND1 1 
ATOM   23776 C  CD2 . HIS C 1 1499 ? 63.613  -1.511  97.126  1.00 144.32 ? 1499 HIS B CD2 1 
ATOM   23777 C  CE1 . HIS C 1 1499 ? 61.614  -0.659  97.430  1.00 149.13 ? 1499 HIS B CE1 1 
ATOM   23778 N  NE2 . HIS C 1 1499 ? 62.831  -0.392  96.982  1.00 145.29 ? 1499 HIS B NE2 1 
ATOM   23779 N  N   . ARG C 1 1500 ? 64.579  -6.947  97.348  1.00 160.99 ? 1500 ARG B N   1 
ATOM   23780 C  CA  . ARG C 1 1500 ? 65.432  -8.057  97.811  1.00 160.77 ? 1500 ARG B CA  1 
ATOM   23781 C  C   . ARG C 1 1500 ? 65.784  -9.080  96.721  1.00 160.64 ? 1500 ARG B C   1 
ATOM   23782 O  O   . ARG C 1 1500 ? 65.086  -10.088 96.526  1.00 166.51 ? 1500 ARG B O   1 
ATOM   23783 C  CB  . ARG C 1 1500 ? 64.876  -8.740  99.070  1.00 165.67 ? 1500 ARG B CB  1 
ATOM   23784 C  CG  . ARG C 1 1500 ? 63.505  -8.270  99.499  1.00 168.77 ? 1500 ARG B CG  1 
ATOM   23785 C  CD  . ARG C 1 1500 ? 62.544  -9.428  99.527  1.00 176.32 ? 1500 ARG B CD  1 
ATOM   23786 N  NE  . ARG C 1 1500 ? 62.138  -9.752  100.881 1.00 179.78 ? 1500 ARG B NE  1 
ATOM   23787 C  CZ  . ARG C 1 1500 ? 61.375  -10.787 101.202 1.00 184.93 ? 1500 ARG B CZ  1 
ATOM   23788 N  NH1 . ARG C 1 1500 ? 60.931  -11.613 100.264 1.00 187.27 ? 1500 ARG B NH1 1 
ATOM   23789 N  NH2 . ARG C 1 1500 ? 61.064  -10.994 102.471 1.00 188.02 ? 1500 ARG B NH2 1 
ATOM   23790 N  N   . PRO C 1 1501 ? 66.896  -8.806  96.021  1.00 162.49 ? 1501 PRO B N   1 
ATOM   23791 C  CA  . PRO C 1 1501 ? 67.553  -9.531  94.924  1.00 163.86 ? 1501 PRO B CA  1 
ATOM   23792 C  C   . PRO C 1 1501 ? 67.897  -10.962 95.319  1.00 170.15 ? 1501 PRO B C   1 
ATOM   23793 O  O   . PRO C 1 1501 ? 68.573  -11.715 94.616  1.00 170.49 ? 1501 PRO B O   1 
ATOM   23794 C  CB  . PRO C 1 1501 ? 68.843  -8.733  94.705  1.00 158.97 ? 1501 PRO B CB  1 
ATOM   23795 C  CG  . PRO C 1 1501 ? 68.536  -7.357  95.215  1.00 156.15 ? 1501 PRO B CG  1 
ATOM   23796 C  CD  . PRO C 1 1501 ? 67.597  -7.552  96.354  1.00 157.60 ? 1501 PRO B CD  1 
ATOM   23797 N  N   . ASP C 1 1502 ? 67.419  -11.334 96.485  1.00 181.24 ? 1502 ASP B N   1 
ATOM   23798 C  CA  . ASP C 1 1502 ? 67.736  -12.622 97.035  1.00 187.88 ? 1502 ASP B CA  1 
ATOM   23799 C  C   . ASP C 1 1502 ? 66.775  -13.636 96.429  1.00 196.93 ? 1502 ASP B C   1 
ATOM   23800 O  O   . ASP C 1 1502 ? 67.063  -14.831 96.343  1.00 202.01 ? 1502 ASP B O   1 
ATOM   23801 C  CB  . ASP C 1 1502 ? 67.601  -12.540 98.558  1.00 188.30 ? 1502 ASP B CB  1 
ATOM   23802 C  CG  . ASP C 1 1502 ? 68.027  -11.172 99.115  1.00 181.81 ? 1502 ASP B CG  1 
ATOM   23803 O  OD1 . ASP C 1 1502 ? 68.936  -10.531 98.528  1.00 175.32 ? 1502 ASP B OD1 1 
ATOM   23804 O  OD2 . ASP C 1 1502 ? 67.454  -10.750 100.144 1.00 182.60 ? 1502 ASP B OD2 1 
ATOM   23805 N  N   . LYS C 1 1503 ? 65.637  -13.128 95.976  1.00 198.53 ? 1503 LYS B N   1 
ATOM   23806 C  CA  . LYS C 1 1503 ? 64.519  -13.961 95.533  1.00 209.45 ? 1503 LYS B CA  1 
ATOM   23807 C  C   . LYS C 1 1503 ? 64.605  -14.488 94.074  1.00 198.33 ? 1503 LYS B C   1 
ATOM   23808 O  O   . LYS C 1 1503 ? 63.594  -14.888 93.479  1.00 198.58 ? 1503 LYS B O   1 
ATOM   23809 C  CB  . LYS C 1 1503 ? 63.212  -13.190 95.753  1.00 214.82 ? 1503 LYS B CB  1 
ATOM   23810 C  CG  . LYS C 1 1503 ? 62.785  -13.061 97.212  1.00 218.07 ? 1503 LYS B CG  1 
ATOM   23811 C  CD  . LYS C 1 1503 ? 63.934  -13.318 98.159  1.00 217.64 ? 1503 LYS B CD  1 
ATOM   23812 C  CE  . LYS C 1 1503 ? 63.529  -14.290 99.262  1.00 225.26 ? 1503 LYS B CE  1 
ATOM   23813 N  NZ  . LYS C 1 1503 ? 64.676  -14.706 100.129 1.00 227.14 ? 1503 LYS B NZ  1 
ATOM   23814 N  N   . GLN C 1 1504 ? 65.815  -14.513 93.519  1.00 198.27 ? 1504 GLN B N   1 
ATOM   23815 C  CA  . GLN C 1 1504 ? 66.026  -14.793 92.095  1.00 192.50 ? 1504 GLN B CA  1 
ATOM   23816 C  C   . GLN C 1 1504 ? 65.732  -16.203 91.643  1.00 198.54 ? 1504 GLN B C   1 
ATOM   23817 O  O   . GLN C 1 1504 ? 66.631  -17.035 91.601  1.00 179.02 ? 1504 GLN B O   1 
ATOM   23818 C  CB  . GLN C 1 1504 ? 67.461  -14.444 91.681  1.00 187.55 ? 1504 GLN B CB  1 
ATOM   23819 C  CG  . GLN C 1 1504 ? 67.567  -13.175 90.831  1.00 228.04 ? 1504 GLN B CG  1 
ATOM   23820 C  CD  . GLN C 1 1504 ? 68.971  -12.562 90.820  1.00 201.14 ? 1504 GLN B CD  1 
ATOM   23821 O  OE1 . GLN C 1 1504 ? 69.182  -11.454 90.299  1.00 193.06 ? 1504 GLN B OE1 1 
ATOM   23822 N  NE2 . GLN C 1 1504 ? 69.935  -13.279 91.401  1.00 202.22 ? 1504 GLN B NE2 1 
ATOM   23823 N  N   . CYS C 1 1505 ? 64.478  -16.456 91.281  1.00 184.70 ? 1505 CYS B N   1 
ATOM   23824 C  CA  . CYS C 1 1505 ? 64.152  -17.633 90.473  1.00 191.62 ? 1505 CYS B CA  1 
ATOM   23825 C  C   . CYS C 1 1505 ? 64.352  -17.397 88.967  1.00 192.76 ? 1505 CYS B C   1 
ATOM   23826 O  O   . CYS C 1 1505 ? 63.533  -16.750 88.306  1.00 188.39 ? 1505 CYS B O   1 
ATOM   23827 C  CB  . CYS C 1 1505 ? 62.738  -18.148 90.734  1.00 197.21 ? 1505 CYS B CB  1 
ATOM   23828 S  SG  . CYS C 1 1505 ? 62.516  -19.852 90.116  1.00 255.67 ? 1505 CYS B SG  1 
ATOM   23829 N  N   . THR C 1 1506 ? 65.444  -17.961 88.453  1.00 183.77 ? 1506 THR B N   1 
ATOM   23830 C  CA  . THR C 1 1506 ? 65.903  -17.782 87.081  1.00 186.14 ? 1506 THR B CA  1 
ATOM   23831 C  C   . THR C 1 1506 ? 65.641  -19.080 86.314  1.00 193.19 ? 1506 THR B C   1 
ATOM   23832 O  O   . THR C 1 1506 ? 65.756  -20.172 86.892  1.00 195.10 ? 1506 THR B O   1 
ATOM   23833 C  CB  . THR C 1 1506 ? 67.424  -17.436 87.080  1.00 185.53 ? 1506 THR B CB  1 
ATOM   23834 O  OG1 . THR C 1 1506 ? 67.636  -16.182 87.743  1.00 184.59 ? 1506 THR B OG1 1 
ATOM   23835 C  CG2 . THR C 1 1506 ? 67.996  -17.360 85.683  1.00 184.60 ? 1506 THR B CG2 1 
ATOM   23836 N  N   . MET C 1 1507 ? 65.285  -18.956 85.027  1.00 195.14 ? 1507 MET B N   1 
ATOM   23837 C  CA  . MET C 1 1507 ? 64.938  -20.117 84.188  1.00 197.78 ? 1507 MET B CA  1 
ATOM   23838 C  C   . MET C 1 1507 ? 65.128  -20.020 82.669  1.00 195.52 ? 1507 MET B C   1 
ATOM   23839 O  O   . MET C 1 1507 ? 64.701  -19.063 82.027  1.00 190.41 ? 1507 MET B O   1 
ATOM   23840 C  CB  . MET C 1 1507 ? 63.507  -20.530 84.424  1.00 200.74 ? 1507 MET B CB  1 
ATOM   23841 C  CG  . MET C 1 1507 ? 63.098  -21.628 83.509  1.00 206.93 ? 1507 MET B CG  1 
ATOM   23842 S  SD  . MET C 1 1507 ? 61.325  -21.607 83.478  1.00 200.71 ? 1507 MET B SD  1 
ATOM   23843 C  CE  . MET C 1 1507 ? 61.030  -19.910 83.989  1.00 191.58 ? 1507 MET B CE  1 
ATOM   23844 N  N   . PHE C 1 1508 ? 65.741  -21.066 82.119  1.00 212.13 ? 1508 PHE B N   1 
ATOM   23845 C  CA  . PHE C 1 1508 ? 65.994  -21.204 80.687  1.00 216.78 ? 1508 PHE B CA  1 
ATOM   23846 C  C   . PHE C 1 1508 ? 64.701  -21.511 79.920  1.00 232.21 ? 1508 PHE B C   1 
ATOM   23847 O  O   . PHE C 1 1508 ? 63.803  -22.150 80.478  1.00 241.40 ? 1508 PHE B O   1 
ATOM   23848 C  CB  . PHE C 1 1508 ? 66.970  -22.362 80.445  1.00 212.86 ? 1508 PHE B CB  1 
ATOM   23849 C  CG  . PHE C 1 1508 ? 68.409  -21.975 80.533  1.00 200.51 ? 1508 PHE B CG  1 
ATOM   23850 C  CD1 . PHE C 1 1508 ? 68.826  -20.707 80.140  1.00 196.88 ? 1508 PHE B CD1 1 
ATOM   23851 C  CD2 . PHE C 1 1508 ? 69.352  -22.881 80.977  1.00 197.85 ? 1508 PHE B CD2 1 
ATOM   23852 C  CE1 . PHE C 1 1508 ? 70.161  -20.337 80.208  1.00 192.20 ? 1508 PHE B CE1 1 
ATOM   23853 C  CE2 . PHE C 1 1508 ? 70.681  -22.521 81.050  1.00 193.78 ? 1508 PHE B CE2 1 
ATOM   23854 C  CZ  . PHE C 1 1508 ? 71.088  -21.239 80.663  1.00 190.51 ? 1508 PHE B CZ  1 
ATOM   23855 N  N   . TYR C 1 1509 ? 64.620  -21.096 78.646  1.00 162.90 ? 1509 TYR B N   1 
ATOM   23856 C  CA  . TYR C 1 1509 ? 63.503  -21.470 77.760  1.00 166.41 ? 1509 TYR B CA  1 
ATOM   23857 C  C   . TYR C 1 1509 ? 63.896  -21.178 76.312  1.00 170.55 ? 1509 TYR B C   1 
ATOM   23858 O  O   . TYR C 1 1509 ? 64.753  -20.321 76.062  1.00 167.80 ? 1509 TYR B O   1 
ATOM   23859 C  CB  . TYR C 1 1509 ? 62.242  -20.685 78.117  1.00 203.91 ? 1509 TYR B CB  1 
ATOM   23860 C  CG  . TYR C 1 1509 ? 62.249  -19.311 77.521  1.00 196.21 ? 1509 TYR B CG  1 
ATOM   23861 C  CD1 . TYR C 1 1509 ? 61.100  -18.758 77.014  1.00 197.27 ? 1509 TYR B CD1 1 
ATOM   23862 C  CD2 . TYR C 1 1509 ? 63.426  -18.579 77.425  1.00 191.34 ? 1509 TYR B CD2 1 
ATOM   23863 C  CE1 . TYR C 1 1509 ? 61.107  -17.490 76.438  1.00 194.97 ? 1509 TYR B CE1 1 
ATOM   23864 C  CE2 . TYR C 1 1509 ? 63.453  -17.317 76.847  1.00 188.49 ? 1509 TYR B CE2 1 
ATOM   23865 C  CZ  . TYR C 1 1509 ? 62.284  -16.765 76.350  1.00 190.63 ? 1509 TYR B CZ  1 
ATOM   23866 O  OH  . TYR C 1 1509 ? 62.266  -15.500 75.762  1.00 187.60 ? 1509 TYR B OH  1 
ATOM   23867 N  N   . SER C 1 1510 ? 63.285  -21.892 75.364  1.00 236.42 ? 1510 SER B N   1 
ATOM   23868 C  CA  . SER C 1 1510 ? 63.553  -21.652 73.941  1.00 236.93 ? 1510 SER B CA  1 
ATOM   23869 C  C   . SER C 1 1510 ? 62.296  -21.354 73.117  1.00 243.17 ? 1510 SER B C   1 
ATOM   23870 O  O   . SER C 1 1510 ? 61.220  -21.914 73.346  1.00 245.82 ? 1510 SER B O   1 
ATOM   23871 C  CB  . SER C 1 1510 ? 64.357  -22.798 73.310  1.00 239.73 ? 1510 SER B CB  1 
ATOM   23872 O  OG  . SER C 1 1510 ? 64.971  -22.377 72.097  1.00 238.01 ? 1510 SER B OG  1 
ATOM   23873 N  N   . THR C 1 1511 ? 62.466  -20.464 72.147  1.00 187.76 ? 1511 THR B N   1 
ATOM   23874 C  CA  . THR C 1 1511 ? 61.356  -19.835 71.452  1.00 191.55 ? 1511 THR B CA  1 
ATOM   23875 C  C   . THR C 1 1511 ? 60.958  -20.666 70.254  1.00 207.07 ? 1511 THR B C   1 
ATOM   23876 O  O   . THR C 1 1511 ? 60.289  -20.186 69.350  1.00 211.33 ? 1511 THR B O   1 
ATOM   23877 C  CB  . THR C 1 1511 ? 61.742  -18.398 71.005  1.00 181.77 ? 1511 THR B CB  1 
ATOM   23878 O  OG1 . THR C 1 1511 ? 60.568  -17.587 70.872  1.00 182.30 ? 1511 THR B OG1 1 
ATOM   23879 C  CG2 . THR C 1 1511 ? 62.545  -18.408 69.701  1.00 181.12 ? 1511 THR B CG2 1 
ATOM   23880 N  N   . SER C 1 1512 ? 61.372  -21.923 70.248  1.00 238.55 ? 1512 SER B N   1 
ATOM   23881 C  CA  . SER C 1 1512 ? 61.105  -22.773 69.102  1.00 254.23 ? 1512 SER B CA  1 
ATOM   23882 C  C   . SER C 1 1512 ? 61.167  -24.240 69.462  1.00 268.29 ? 1512 SER B C   1 
ATOM   23883 O  O   . SER C 1 1512 ? 61.952  -24.656 70.308  1.00 266.02 ? 1512 SER B O   1 
ATOM   23884 C  CB  . SER C 1 1512 ? 62.115  -22.502 67.991  1.00 252.59 ? 1512 SER B CB  1 
ATOM   23885 O  OG  . SER C 1 1512 ? 63.280  -23.290 68.172  1.00 250.68 ? 1512 SER B OG  1 
ATOM   23886 N  N   . ASN C 1 1513 ? 60.335  -25.024 68.796  1.00 319.43 ? 1513 ASN B N   1 
ATOM   23887 C  CA  . ASN C 1 1513 ? 60.288  -26.450 69.039  1.00 334.50 ? 1513 ASN B CA  1 
ATOM   23888 C  C   . ASN C 1 1513 ? 61.223  -27.187 68.087  1.00 343.63 ? 1513 ASN B C   1 
ATOM   23889 O  O   . ASN C 1 1513 ? 61.402  -28.402 68.194  1.00 349.68 ? 1513 ASN B O   1 
ATOM   23890 C  CB  . ASN C 1 1513 ? 58.850  -26.933 68.892  1.00 344.51 ? 1513 ASN B CB  1 
ATOM   23891 C  CG  . ASN C 1 1513 ? 57.847  -25.909 69.396  1.00 345.19 ? 1513 ASN B CG  1 
ATOM   23892 O  OD1 . ASN C 1 1513 ? 57.993  -25.368 70.492  1.00 340.00 ? 1513 ASN B OD1 1 
ATOM   23893 N  ND2 . ASN C 1 1513 ? 56.831  -25.628 68.589  1.00 351.16 ? 1513 ASN B ND2 1 
ATOM   23894 N  N   . ILE C 1 1514 ? 61.829  -26.436 67.167  1.00 296.66 ? 1514 ILE B N   1 
ATOM   23895 C  CA  . ILE C 1 1514 ? 62.688  -27.015 66.132  1.00 301.40 ? 1514 ILE B CA  1 
ATOM   23896 C  C   . ILE C 1 1514 ? 63.857  -27.818 66.722  1.00 300.54 ? 1514 ILE B C   1 
ATOM   23897 O  O   . ILE C 1 1514 ? 64.647  -27.312 67.525  1.00 294.45 ? 1514 ILE B O   1 
ATOM   23898 C  CB  . ILE C 1 1514 ? 63.217  -25.940 65.134  1.00 312.10 ? 1514 ILE B CB  1 
ATOM   23899 C  CG1 . ILE C 1 1514 ? 62.091  -24.999 64.691  1.00 311.13 ? 1514 ILE B CG1 1 
ATOM   23900 C  CG2 . ILE C 1 1514 ? 63.860  -26.604 63.923  1.00 317.56 ? 1514 ILE B CG2 1 
ATOM   23901 C  CD1 . ILE C 1 1514 ? 62.527  -23.934 63.697  1.00 307.44 ? 1514 ILE B CD1 1 
ATOM   23902 N  N   . SER D 2 1    ? 89.814  50.534  76.570  1.00 410.18 ? 129  SER Y N   1 
ATOM   23903 C  CA  . SER D 2 1    ? 88.977  50.436  75.379  1.00 411.34 ? 129  SER Y CA  1 
ATOM   23904 C  C   . SER D 2 1    ? 87.516  50.744  75.700  1.00 412.45 ? 129  SER Y C   1 
ATOM   23905 O  O   . SER D 2 1    ? 86.626  49.938  75.424  1.00 411.73 ? 129  SER Y O   1 
ATOM   23906 C  CB  . SER D 2 1    ? 89.100  49.048  74.750  1.00 220.17 ? 129  SER Y CB  1 
ATOM   23907 O  OG  . SER D 2 1    ? 88.629  48.046  75.634  1.00 219.72 ? 129  SER Y OG  1 
ATOM   23908 N  N   . SER D 2 2    ? 87.282  51.912  76.290  1.00 277.87 ? 130  SER Y N   1 
ATOM   23909 C  CA  . SER D 2 2    ? 85.934  52.374  76.606  1.00 279.45 ? 130  SER Y CA  1 
ATOM   23910 C  C   . SER D 2 2    ? 85.114  52.529  75.321  1.00 282.24 ? 130  SER Y C   1 
ATOM   23911 O  O   . SER D 2 2    ? 85.662  52.851  74.265  1.00 282.48 ? 130  SER Y O   1 
ATOM   23912 C  CB  . SER D 2 2    ? 86.003  53.702  77.376  1.00 277.99 ? 130  SER Y CB  1 
ATOM   23913 O  OG  . SER D 2 2    ? 84.745  54.084  77.911  1.00 276.55 ? 130  SER Y OG  1 
ATOM   23914 N  N   . GLU D 2 3    ? 83.807  52.289  75.415  1.00 273.19 ? 131  GLU Y N   1 
ATOM   23915 C  CA  . GLU D 2 3    ? 82.903  52.384  74.264  1.00 273.23 ? 131  GLU Y CA  1 
ATOM   23916 C  C   . GLU D 2 3    ? 81.654  53.206  74.595  1.00 272.96 ? 131  GLU Y C   1 
ATOM   23917 O  O   . GLU D 2 3    ? 80.570  52.644  74.759  1.00 273.94 ? 131  GLU Y O   1 
ATOM   23918 C  CB  . GLU D 2 3    ? 82.465  50.986  73.797  1.00 272.87 ? 131  GLU Y CB  1 
ATOM   23919 C  CG  . GLU D 2 3    ? 83.529  50.159  73.084  1.00 271.61 ? 131  GLU Y CG  1 
ATOM   23920 C  CD  . GLU D 2 3    ? 82.983  48.846  72.535  1.00 271.17 ? 131  GLU Y CD  1 
ATOM   23921 O  OE1 . GLU D 2 3    ? 81.855  48.459  72.910  1.00 270.91 ? 131  GLU Y OE1 1 
ATOM   23922 O  OE2 . GLU D 2 3    ? 83.684  48.200  71.728  1.00 270.99 ? 131  GLU Y OE2 1 
ATOM   23923 N  N   . THR D 2 4    ? 81.797  54.526  74.692  1.00 293.56 ? 132  THR Y N   1 
ATOM   23924 C  CA  . THR D 2 4    ? 80.658  55.388  75.020  1.00 292.42 ? 132  THR Y CA  1 
ATOM   23925 C  C   . THR D 2 4    ? 79.796  55.681  73.784  1.00 290.36 ? 132  THR Y C   1 
ATOM   23926 O  O   . THR D 2 4    ? 80.319  55.935  72.696  1.00 290.02 ? 132  THR Y O   1 
ATOM   23927 C  CB  . THR D 2 4    ? 81.108  56.710  75.705  1.00 292.94 ? 132  THR Y CB  1 
ATOM   23928 O  OG1 . THR D 2 4    ? 81.800  56.416  76.928  1.00 293.22 ? 132  THR Y OG1 1 
ATOM   23929 C  CG2 . THR D 2 4    ? 79.911  57.592  76.015  1.00 292.26 ? 132  THR Y CG2 1 
ATOM   23930 N  N   . ASN D 2 5    ? 78.477  55.621  73.952  1.00 290.08 ? 133  ASN Y N   1 
ATOM   23931 C  CA  . ASN D 2 5    ? 77.547  55.971  72.880  1.00 286.35 ? 133  ASN Y CA  1 
ATOM   23932 C  C   . ASN D 2 5    ? 77.040  57.409  73.012  1.00 282.46 ? 133  ASN Y C   1 
ATOM   23933 O  O   . ASN D 2 5    ? 75.981  57.650  73.591  1.00 285.26 ? 133  ASN Y O   1 
ATOM   23934 C  CB  . ASN D 2 5    ? 76.371  54.987  72.826  1.00 285.49 ? 133  ASN Y CB  1 
ATOM   23935 C  CG  . ASN D 2 5    ? 75.603  54.919  74.131  1.00 281.23 ? 133  ASN Y CG  1 
ATOM   23936 O  OD1 . ASN D 2 5    ? 76.186  54.991  75.212  1.00 278.44 ? 133  ASN Y OD1 1 
ATOM   23937 N  ND2 . ASN D 2 5    ? 74.287  54.772  74.037  1.00 281.00 ? 133  ASN Y ND2 1 
ATOM   23938 N  N   . THR D 2 6    ? 77.807  58.357  72.473  1.00 283.03 ? 134  THR Y N   1 
ATOM   23939 C  CA  . THR D 2 6    ? 77.461  59.782  72.524  1.00 277.18 ? 134  THR Y CA  1 
ATOM   23940 C  C   . THR D 2 6    ? 76.342  60.170  71.560  1.00 273.72 ? 134  THR Y C   1 
ATOM   23941 O  O   . THR D 2 6    ? 76.130  59.513  70.547  1.00 271.81 ? 134  THR Y O   1 
ATOM   23942 C  CB  . THR D 2 6    ? 78.679  60.670  72.205  1.00 299.54 ? 134  THR Y CB  1 
ATOM   23943 O  OG1 . THR D 2 6    ? 78.229  61.977  71.828  1.00 300.82 ? 134  THR Y OG1 1 
ATOM   23944 C  CG2 . THR D 2 6    ? 79.481  60.081  71.060  1.00 298.97 ? 134  THR Y CG2 1 
ATOM   23945 N  N   . HIS D 2 7    ? 75.642  61.257  71.871  1.00 417.96 ? 135  HIS Y N   1 
ATOM   23946 C  CA  . HIS D 2 7    ? 74.538  61.720  71.036  1.00 418.91 ? 135  HIS Y CA  1 
ATOM   23947 C  C   . HIS D 2 7    ? 74.809  63.105  70.432  1.00 417.56 ? 135  HIS Y C   1 
ATOM   23948 O  O   . HIS D 2 7    ? 75.023  64.074  71.162  1.00 416.95 ? 135  HIS Y O   1 
ATOM   23949 C  CB  . HIS D 2 7    ? 73.230  61.739  71.842  1.00 261.70 ? 135  HIS Y CB  1 
ATOM   23950 C  CG  . HIS D 2 7    ? 72.835  60.403  72.399  1.00 260.66 ? 135  HIS Y CG  1 
ATOM   23951 N  ND1 . HIS D 2 7    ? 72.177  59.448  71.655  1.00 261.35 ? 135  HIS Y ND1 1 
ATOM   23952 C  CD2 . HIS D 2 7    ? 72.989  59.872  73.637  1.00 259.06 ? 135  HIS Y CD2 1 
ATOM   23953 C  CE1 . HIS D 2 7    ? 71.952  58.381  72.404  1.00 260.14 ? 135  HIS Y CE1 1 
ATOM   23954 N  NE2 . HIS D 2 7    ? 72.437  58.615  73.610  1.00 258.77 ? 135  HIS Y NE2 1 
ATOM   23955 N  N   . LEU D 2 8    ? 74.802  63.190  69.101  1.00 190.03 ? 136  LEU Y N   1 
ATOM   23956 C  CA  . LEU D 2 8    ? 74.965  64.478  68.407  1.00 187.15 ? 136  LEU Y CA  1 
ATOM   23957 C  C   . LEU D 2 8    ? 73.755  64.910  67.567  1.00 188.58 ? 136  LEU Y C   1 
ATOM   23958 O  O   . LEU D 2 8    ? 73.177  64.113  66.829  1.00 188.44 ? 136  LEU Y O   1 
ATOM   23959 C  CB  . LEU D 2 8    ? 76.262  64.537  67.568  1.00 181.33 ? 136  LEU Y CB  1 
ATOM   23960 C  CG  . LEU D 2 8    ? 76.859  63.386  66.750  1.00 175.59 ? 136  LEU Y CG  1 
ATOM   23961 C  CD1 . LEU D 2 8    ? 78.136  63.859  66.058  1.00 177.18 ? 136  LEU Y CD1 1 
ATOM   23962 C  CD2 . LEU D 2 8    ? 77.158  62.194  67.631  1.00 174.16 ? 136  LEU Y CD2 1 
ATOM   23963 N  N   . PHE D 2 9    ? 73.379  66.181  67.698  1.00 280.27 ? 137  PHE Y N   1 
ATOM   23964 C  CA  . PHE D 2 9    ? 72.254  66.730  66.949  1.00 282.38 ? 137  PHE Y CA  1 
ATOM   23965 C  C   . PHE D 2 9    ? 72.721  67.340  65.624  1.00 280.09 ? 137  PHE Y C   1 
ATOM   23966 O  O   . PHE D 2 9    ? 73.727  68.046  65.567  1.00 276.96 ? 137  PHE Y O   1 
ATOM   23967 C  CB  . PHE D 2 9    ? 71.482  67.771  67.781  1.00 286.94 ? 137  PHE Y CB  1 
ATOM   23968 C  CG  . PHE D 2 9    ? 71.339  67.414  69.243  1.00 291.16 ? 137  PHE Y CG  1 
ATOM   23969 C  CD1 . PHE D 2 9    ? 71.217  66.096  69.646  1.00 289.11 ? 137  PHE Y CD1 1 
ATOM   23970 C  CD2 . PHE D 2 9    ? 71.314  68.409  70.214  1.00 291.94 ? 137  PHE Y CD2 1 
ATOM   23971 C  CE1 . PHE D 2 9    ? 71.089  65.777  70.989  1.00 288.51 ? 137  PHE Y CE1 1 
ATOM   23972 C  CE2 . PHE D 2 9    ? 71.182  68.094  71.560  1.00 291.74 ? 137  PHE Y CE2 1 
ATOM   23973 C  CZ  . PHE D 2 9    ? 71.070  66.780  71.946  1.00 289.47 ? 137  PHE Y CZ  1 
ATOM   23974 N  N   . VAL D 2 10   ? 71.986  67.046  64.559  1.00 217.59 ? 138  VAL Y N   1 
ATOM   23975 C  CA  . VAL D 2 10   ? 72.243  67.635  63.259  1.00 213.42 ? 138  VAL Y CA  1 
ATOM   23976 C  C   . VAL D 2 10   ? 71.140  68.638  62.943  1.00 217.19 ? 138  VAL Y C   1 
ATOM   23977 O  O   . VAL D 2 10   ? 69.969  68.386  63.225  1.00 219.64 ? 138  VAL Y O   1 
ATOM   23978 C  CB  . VAL D 2 10   ? 72.328  66.546  62.158  1.00 209.06 ? 138  VAL Y CB  1 
ATOM   23979 C  CG1 . VAL D 2 10   ? 71.671  67.006  60.863  1.00 207.78 ? 138  VAL Y CG1 1 
ATOM   23980 C  CG2 . VAL D 2 10   ? 73.778  66.139  61.914  1.00 204.10 ? 138  VAL Y CG2 1 
ATOM   23981 N  N   . ASN D 2 11   ? 71.522  69.779  62.371  1.00 232.76 ? 139  ASN Y N   1 
ATOM   23982 C  CA  . ASN D 2 11   ? 70.558  70.788  61.927  1.00 233.82 ? 139  ASN Y CA  1 
ATOM   23983 C  C   . ASN D 2 11   ? 70.940  71.448  60.588  1.00 231.93 ? 139  ASN Y C   1 
ATOM   23984 O  O   . ASN D 2 11   ? 71.896  72.222  60.518  1.00 230.15 ? 139  ASN Y O   1 
ATOM   23985 C  CB  . ASN D 2 11   ? 70.394  71.867  63.000  1.00 234.48 ? 139  ASN Y CB  1 
ATOM   23986 C  CG  . ASN D 2 11   ? 70.445  71.309  64.394  1.00 236.93 ? 139  ASN Y CG  1 
ATOM   23987 O  OD1 . ASN D 2 11   ? 69.525  70.625  64.834  1.00 238.09 ? 139  ASN Y OD1 1 
ATOM   23988 N  ND2 . ASN D 2 11   ? 71.525  71.594  65.101  1.00 237.74 ? 139  ASN Y ND2 1 
ATOM   23989 N  N   . LYS D 2 12   ? 70.200  71.147  59.524  1.00 252.58 ? 140  LYS Y N   1 
ATOM   23990 C  CA  . LYS D 2 12   ? 70.462  71.787  58.238  1.00 247.47 ? 140  LYS Y CA  1 
ATOM   23991 C  C   . LYS D 2 12   ? 69.797  73.178  58.187  1.00 246.66 ? 140  LYS Y C   1 
ATOM   23992 O  O   . LYS D 2 12   ? 68.645  73.334  58.588  1.00 248.47 ? 140  LYS Y O   1 
ATOM   23993 C  CB  . LYS D 2 12   ? 70.021  70.883  57.070  1.00 244.24 ? 140  LYS Y CB  1 
ATOM   23994 C  CG  . LYS D 2 12   ? 70.541  69.436  57.149  1.00 244.00 ? 140  LYS Y CG  1 
ATOM   23995 C  CD  . LYS D 2 12   ? 70.444  68.680  55.815  1.00 237.37 ? 140  LYS Y CD  1 
ATOM   23996 C  CE  . LYS D 2 12   ? 71.717  68.823  54.978  1.00 231.08 ? 140  LYS Y CE  1 
ATOM   23997 N  NZ  . LYS D 2 12   ? 71.814  67.789  53.909  1.00 226.72 ? 140  LYS Y NZ  1 
ATOM   23998 N  N   . VAL D 2 13   ? 70.522  74.193  57.718  1.00 277.47 ? 141  VAL Y N   1 
ATOM   23999 C  CA  . VAL D 2 13   ? 69.954  75.545  57.630  1.00 279.54 ? 141  VAL Y CA  1 
ATOM   24000 C  C   . VAL D 2 13   ? 69.655  75.981  56.187  1.00 276.41 ? 141  VAL Y C   1 
ATOM   24001 O  O   . VAL D 2 13   ? 70.458  76.673  55.556  1.00 269.35 ? 141  VAL Y O   1 
ATOM   24002 C  CB  . VAL D 2 13   ? 70.859  76.601  58.317  1.00 281.77 ? 141  VAL Y CB  1 
ATOM   24003 C  CG1 . VAL D 2 13   ? 70.132  77.929  58.430  1.00 283.65 ? 141  VAL Y CG1 1 
ATOM   24004 C  CG2 . VAL D 2 13   ? 71.288  76.126  59.693  1.00 286.83 ? 141  VAL Y CG2 1 
ATOM   24005 N  N   . TYR D 2 14   ? 68.500  75.569  55.668  1.00 439.08 ? 142  TYR Y N   1 
ATOM   24006 C  CA  . TYR D 2 14   ? 68.071  75.997  54.340  1.00 434.75 ? 142  TYR Y CA  1 
ATOM   24007 C  C   . TYR D 2 14   ? 67.466  77.389  54.427  1.00 437.05 ? 142  TYR Y C   1 
ATOM   24008 O  O   . TYR D 2 14   ? 66.402  77.649  53.866  1.00 437.88 ? 142  TYR Y O   1 
ATOM   24009 C  CB  . TYR D 2 14   ? 67.055  75.019  53.737  1.00 264.24 ? 142  TYR Y CB  1 
ATOM   24010 C  CG  . TYR D 2 14   ? 67.623  73.645  53.438  1.00 264.28 ? 142  TYR Y CG  1 
ATOM   24011 C  CD1 . TYR D 2 14   ? 68.118  73.325  52.174  1.00 258.95 ? 142  TYR Y CD1 1 
ATOM   24012 C  CD2 . TYR D 2 14   ? 67.669  72.668  54.422  1.00 269.63 ? 142  TYR Y CD2 1 
ATOM   24013 C  CE1 . TYR D 2 14   ? 68.645  72.059  51.905  1.00 258.81 ? 142  TYR Y CE1 1 
ATOM   24014 C  CE2 . TYR D 2 14   ? 68.192  71.409  54.166  1.00 269.62 ? 142  TYR Y CE2 1 
ATOM   24015 C  CZ  . TYR D 2 14   ? 68.679  71.106  52.910  1.00 264.12 ? 142  TYR Y CZ  1 
ATOM   24016 O  OH  . TYR D 2 14   ? 69.197  69.850  52.665  1.00 263.99 ? 142  TYR Y OH  1 
ATOM   24017 N  N   . GLY D 2 15   ? 68.151  78.283  55.133  1.00 234.96 ? 143  GLY Y N   1 
ATOM   24018 C  CA  . GLY D 2 15   ? 67.595  79.590  55.436  1.00 238.26 ? 143  GLY Y CA  1 
ATOM   24019 C  C   . GLY D 2 15   ? 66.457  79.455  56.434  1.00 247.71 ? 143  GLY Y C   1 
ATOM   24020 O  O   . GLY D 2 15   ? 66.562  78.671  57.382  1.00 253.55 ? 143  GLY Y O   1 
ATOM   24021 N  N   . GLY D 2 16   ? 65.377  80.214  56.227  1.00 150.82 ? 144  GLY Y N   1 
ATOM   24022 C  CA  . GLY D 2 16   ? 64.169  80.115  57.045  1.00 157.51 ? 144  GLY Y CA  1 
ATOM   24023 C  C   . GLY D 2 16   ? 63.581  78.714  57.083  1.00 156.79 ? 144  GLY Y C   1 
ATOM   24024 O  O   . GLY D 2 16   ? 62.363  78.523  57.194  1.00 157.25 ? 144  GLY Y O   1 
ATOM   24025 N  N   . ASN D 2 17   ? 64.472  77.735  56.955  1.00 384.41 ? 145  ASN Y N   1 
ATOM   24026 C  CA  . ASN D 2 17   ? 64.142  76.327  57.051  1.00 381.90 ? 145  ASN Y CA  1 
ATOM   24027 C  C   . ASN D 2 17   ? 65.205  75.644  57.875  1.00 378.41 ? 145  ASN Y C   1 
ATOM   24028 O  O   . ASN D 2 17   ? 66.372  76.032  57.857  1.00 376.93 ? 145  ASN Y O   1 
ATOM   24029 C  CB  . ASN D 2 17   ? 64.130  75.680  55.671  1.00 202.26 ? 145  ASN Y CB  1 
ATOM   24030 C  CG  . ASN D 2 17   ? 63.396  76.509  54.653  1.00 197.96 ? 145  ASN Y CG  1 
ATOM   24031 O  OD1 . ASN D 2 17   ? 62.310  77.031  54.925  1.00 199.68 ? 145  ASN Y OD1 1 
ATOM   24032 N  ND2 . ASN D 2 17   ? 63.984  76.645  53.468  1.00 192.16 ? 145  ASN Y ND2 1 
ATOM   24033 N  N   . LEU D 2 18   ? 64.790  74.621  58.601  1.00 197.45 ? 146  LEU Y N   1 
ATOM   24034 C  CA  . LEU D 2 18   ? 65.728  73.745  59.265  1.00 194.86 ? 146  LEU Y CA  1 
ATOM   24035 C  C   . LEU D 2 18   ? 65.147  72.356  59.481  1.00 193.37 ? 146  LEU Y C   1 
ATOM   24036 O  O   . LEU D 2 18   ? 64.098  72.186  60.107  1.00 193.93 ? 146  LEU Y O   1 
ATOM   24037 C  CB  . LEU D 2 18   ? 66.177  74.333  60.592  1.00 198.50 ? 146  LEU Y CB  1 
ATOM   24038 C  CG  . LEU D 2 18   ? 66.794  73.325  61.571  1.00 199.33 ? 146  LEU Y CG  1 
ATOM   24039 C  CD1 . LEU D 2 18   ? 65.739  72.572  62.397  1.00 202.76 ? 146  LEU Y CD1 1 
ATOM   24040 C  CD2 . LEU D 2 18   ? 67.736  72.356  60.872  1.00 195.80 ? 146  LEU Y CD2 1 
ATOM   24041 N  N   . ASP D 2 19   ? 65.851  71.366  58.944  1.00 178.56 ? 147  ASP Y N   1 
ATOM   24042 C  CA  . ASP D 2 19   ? 65.548  69.963  59.184  1.00 178.50 ? 147  ASP Y CA  1 
ATOM   24043 C  C   . ASP D 2 19   ? 66.625  69.420  60.131  1.00 185.10 ? 147  ASP Y C   1 
ATOM   24044 O  O   . ASP D 2 19   ? 67.798  69.292  59.754  1.00 184.17 ? 147  ASP Y O   1 
ATOM   24045 C  CB  . ASP D 2 19   ? 65.492  69.171  57.861  1.00 168.23 ? 147  ASP Y CB  1 
ATOM   24046 C  CG  . ASP D 2 19   ? 64.551  69.812  56.813  1.00 159.83 ? 147  ASP Y CG  1 
ATOM   24047 O  OD1 . ASP D 2 19   ? 63.397  70.197  57.135  1.00 159.71 ? 147  ASP Y OD1 1 
ATOM   24048 O  OD2 . ASP D 2 19   ? 64.981  69.933  55.647  1.00 153.91 ? 147  ASP Y OD2 1 
ATOM   24049 N  N   . ALA D 2 20   ? 66.206  69.134  61.368  1.00 199.58 ? 148  ALA Y N   1 
ATOM   24050 C  CA  . ALA D 2 20   ? 67.096  68.703  62.457  1.00 203.94 ? 148  ALA Y CA  1 
ATOM   24051 C  C   . ALA D 2 20   ? 66.877  67.255  62.915  1.00 206.63 ? 148  ALA Y C   1 
ATOM   24052 O  O   . ALA D 2 20   ? 65.765  66.856  63.277  1.00 211.24 ? 148  ALA Y O   1 
ATOM   24053 C  CB  . ALA D 2 20   ? 66.970  69.650  63.646  1.00 206.01 ? 148  ALA Y CB  1 
ATOM   24054 N  N   . SER D 2 21   ? 67.959  66.484  62.889  1.00 224.72 ? 149  SER Y N   1 
ATOM   24055 C  CA  . SER D 2 21   ? 67.954  65.089  63.295  1.00 223.22 ? 149  SER Y CA  1 
ATOM   24056 C  C   . SER D 2 21   ? 68.785  64.990  64.567  1.00 216.47 ? 149  SER Y C   1 
ATOM   24057 O  O   . SER D 2 21   ? 69.829  65.637  64.647  1.00 212.77 ? 149  SER Y O   1 
ATOM   24058 C  CB  . SER D 2 21   ? 68.632  64.235  62.218  1.00 223.72 ? 149  SER Y CB  1 
ATOM   24059 O  OG  . SER D 2 21   ? 68.297  64.661  60.908  1.00 225.19 ? 149  SER Y OG  1 
ATOM   24060 N  N   . ILE D 2 22   ? 68.334  64.204  65.555  1.00 247.93 ? 150  ILE Y N   1 
ATOM   24061 C  CA  . ILE D 2 22   ? 69.164  63.840  66.722  1.00 239.12 ? 150  ILE Y CA  1 
ATOM   24062 C  C   . ILE D 2 22   ? 69.705  62.423  66.518  1.00 235.42 ? 150  ILE Y C   1 
ATOM   24063 O  O   . ILE D 2 22   ? 68.978  61.542  66.056  1.00 236.35 ? 150  ILE Y O   1 
ATOM   24064 C  CB  . ILE D 2 22   ? 68.390  63.902  68.070  1.00 223.42 ? 150  ILE Y CB  1 
ATOM   24065 C  CG1 . ILE D 2 22   ? 68.094  62.500  68.592  1.00 217.66 ? 150  ILE Y CG1 1 
ATOM   24066 C  CG2 . ILE D 2 22   ? 67.115  64.708  67.941  1.00 230.74 ? 150  ILE Y CG2 1 
ATOM   24067 C  CD1 . ILE D 2 22   ? 69.182  61.945  69.466  1.00 203.70 ? 150  ILE Y CD1 1 
ATOM   24068 N  N   . ASP D 2 23   ? 70.966  62.190  66.867  1.00 241.77 ? 151  ASP Y N   1 
ATOM   24069 C  CA  . ASP D 2 23   ? 71.614  60.938  66.483  1.00 239.65 ? 151  ASP Y CA  1 
ATOM   24070 C  C   . ASP D 2 23   ? 72.738  60.572  67.451  1.00 245.32 ? 151  ASP Y C   1 
ATOM   24071 O  O   . ASP D 2 23   ? 72.851  61.172  68.519  1.00 243.42 ? 151  ASP Y O   1 
ATOM   24072 C  CB  . ASP D 2 23   ? 72.150  61.062  65.055  1.00 231.56 ? 151  ASP Y CB  1 
ATOM   24073 C  CG  . ASP D 2 23   ? 72.429  59.721  64.409  1.00 224.93 ? 151  ASP Y CG  1 
ATOM   24074 O  OD1 . ASP D 2 23   ? 71.975  58.682  64.947  1.00 225.75 ? 151  ASP Y OD1 1 
ATOM   24075 O  OD2 . ASP D 2 23   ? 73.104  59.722  63.352  1.00 219.53 ? 151  ASP Y OD2 1 
ATOM   24076 N  N   . SER D 2 24   ? 73.566  59.594  67.076  1.00 222.20 ? 152  SER Y N   1 
ATOM   24077 C  CA  . SER D 2 24   ? 74.616  59.082  67.964  1.00 230.67 ? 152  SER Y CA  1 
ATOM   24078 C  C   . SER D 2 24   ? 75.972  58.881  67.277  1.00 239.78 ? 152  SER Y C   1 
ATOM   24079 O  O   . SER D 2 24   ? 76.037  58.629  66.076  1.00 237.45 ? 152  SER Y O   1 
ATOM   24080 C  CB  . SER D 2 24   ? 74.174  57.756  68.593  1.00 230.25 ? 152  SER Y CB  1 
ATOM   24081 O  OG  . SER D 2 24   ? 74.106  56.721  67.630  1.00 232.15 ? 152  SER Y OG  1 
ATOM   24082 N  N   . PHE D 2 25   ? 77.051  58.993  68.050  1.00 289.58 ? 153  PHE Y N   1 
ATOM   24083 C  CA  . PHE D 2 25   ? 78.392  58.643  67.583  1.00 298.07 ? 153  PHE Y CA  1 
ATOM   24084 C  C   . PHE D 2 25   ? 78.883  57.496  68.453  1.00 303.41 ? 153  PHE Y C   1 
ATOM   24085 O  O   . PHE D 2 25   ? 78.219  57.109  69.419  1.00 302.70 ? 153  PHE Y O   1 
ATOM   24086 C  CB  . PHE D 2 25   ? 79.344  59.848  67.681  1.00 303.72 ? 153  PHE Y CB  1 
ATOM   24087 C  CG  . PHE D 2 25   ? 80.771  59.561  67.250  1.00 308.36 ? 153  PHE Y CG  1 
ATOM   24088 C  CD1 . PHE D 2 25   ? 81.183  59.799  65.949  1.00 307.65 ? 153  PHE Y CD1 1 
ATOM   24089 C  CD2 . PHE D 2 25   ? 81.709  59.091  68.159  1.00 312.44 ? 153  PHE Y CD2 1 
ATOM   24090 C  CE1 . PHE D 2 25   ? 82.490  59.549  65.563  1.00 307.60 ? 153  PHE Y CE1 1 
ATOM   24091 C  CE2 . PHE D 2 25   ? 83.014  58.838  67.770  1.00 312.17 ? 153  PHE Y CE2 1 
ATOM   24092 C  CZ  . PHE D 2 25   ? 83.402  59.069  66.475  1.00 309.40 ? 153  PHE Y CZ  1 
ATOM   24093 N  N   . SER D 2 26   ? 80.038  56.943  68.115  1.00 417.51 ? 154  SER Y N   1 
ATOM   24094 C  CA  . SER D 2 26   ? 80.593  55.874  68.921  1.00 418.52 ? 154  SER Y CA  1 
ATOM   24095 C  C   . SER D 2 26   ? 82.098  56.026  69.103  1.00 419.75 ? 154  SER Y C   1 
ATOM   24096 O  O   . SER D 2 26   ? 82.888  55.746  68.200  1.00 417.94 ? 154  SER Y O   1 
ATOM   24097 C  CB  . SER D 2 26   ? 80.216  54.519  68.328  1.00 221.02 ? 154  SER Y CB  1 
ATOM   24098 O  OG  . SER D 2 26   ? 78.804  54.380  68.315  1.00 219.12 ? 154  SER Y OG  1 
ATOM   24099 N  N   . ILE D 2 27   ? 82.469  56.503  70.286  1.00 237.83 ? 155  ILE Y N   1 
ATOM   24100 C  CA  . ILE D 2 27   ? 83.858  56.685  70.672  1.00 240.17 ? 155  ILE Y CA  1 
ATOM   24101 C  C   . ILE D 2 27   ? 84.414  55.378  71.218  1.00 243.16 ? 155  ILE Y C   1 
ATOM   24102 O  O   . ILE D 2 27   ? 83.955  54.878  72.244  1.00 242.74 ? 155  ILE Y O   1 
ATOM   24103 C  CB  . ILE D 2 27   ? 83.976  57.763  71.753  1.00 237.12 ? 155  ILE Y CB  1 
ATOM   24104 C  CG1 . ILE D 2 27   ? 83.176  59.001  71.347  1.00 236.42 ? 155  ILE Y CG1 1 
ATOM   24105 C  CG2 . ILE D 2 27   ? 85.433  58.099  72.008  1.00 237.47 ? 155  ILE Y CG2 1 
ATOM   24106 C  CD1 . ILE D 2 27   ? 83.081  60.048  72.425  1.00 235.79 ? 155  ILE Y CD1 1 
ATOM   24107 N  N   . ASN D 2 28   ? 85.413  54.835  70.532  1.00 485.20 ? 156  ASN Y N   1 
ATOM   24108 C  CA  . ASN D 2 28   ? 85.915  53.499  70.830  1.00 490.82 ? 156  ASN Y CA  1 
ATOM   24109 C  C   . ASN D 2 28   ? 87.153  53.485  71.712  1.00 492.32 ? 156  ASN Y C   1 
ATOM   24110 O  O   . ASN D 2 28   ? 87.890  52.501  71.740  1.00 491.96 ? 156  ASN Y O   1 
ATOM   24111 C  CB  . ASN D 2 28   ? 86.209  52.767  69.527  1.00 269.42 ? 156  ASN Y CB  1 
ATOM   24112 C  CG  . ASN D 2 28   ? 85.080  52.894  68.535  1.00 271.07 ? 156  ASN Y CG  1 
ATOM   24113 O  OD1 . ASN D 2 28   ? 83.949  53.202  68.909  1.00 271.20 ? 156  ASN Y OD1 1 
ATOM   24114 N  ND2 . ASN D 2 28   ? 85.378  52.665  67.260  1.00 269.62 ? 156  ASN Y ND2 1 
ATOM   24115 N  N   . LYS D 2 29   ? 87.375  54.576  72.435  1.00 275.98 ? 157  LYS Y N   1 
ATOM   24116 C  CA  . LYS D 2 29   ? 88.577  54.718  73.251  1.00 279.78 ? 157  LYS Y CA  1 
ATOM   24117 C  C   . LYS D 2 29   ? 88.304  55.553  74.514  1.00 282.46 ? 157  LYS Y C   1 
ATOM   24118 O  O   . LYS D 2 29   ? 87.190  56.047  74.707  1.00 282.70 ? 157  LYS Y O   1 
ATOM   24119 C  CB  . LYS D 2 29   ? 89.720  55.331  72.419  1.00 280.74 ? 157  LYS Y CB  1 
ATOM   24120 C  CG  . LYS D 2 29   ? 90.186  54.475  71.224  1.00 281.60 ? 157  LYS Y CG  1 
ATOM   24121 C  CD  . LYS D 2 29   ? 91.167  55.216  70.296  1.00 281.54 ? 157  LYS Y CD  1 
ATOM   24122 C  CE  . LYS D 2 29   ? 92.595  55.236  70.838  1.00 279.45 ? 157  LYS Y CE  1 
ATOM   24123 N  NZ  . LYS D 2 29   ? 93.540  55.946  69.925  1.00 279.27 ? 157  LYS Y NZ  1 
ATOM   24124 N  N   . GLU D 2 30   ? 89.315  55.680  75.376  1.00 291.48 ? 158  GLU Y N   1 
ATOM   24125 C  CA  . GLU D 2 30   ? 89.228  56.495  76.594  1.00 293.80 ? 158  GLU Y CA  1 
ATOM   24126 C  C   . GLU D 2 30   ? 89.698  57.933  76.350  1.00 292.84 ? 158  GLU Y C   1 
ATOM   24127 O  O   . GLU D 2 30   ? 89.269  58.867  77.035  1.00 293.38 ? 158  GLU Y O   1 
ATOM   24128 C  CB  . GLU D 2 30   ? 90.035  55.858  77.733  1.00 298.38 ? 158  GLU Y CB  1 
ATOM   24129 C  CG  . GLU D 2 30   ? 91.433  55.404  77.329  1.00 303.61 ? 158  GLU Y CG  1 
ATOM   24130 C  CD  . GLU D 2 30   ? 92.291  55.025  78.518  1.00 306.33 ? 158  GLU Y CD  1 
ATOM   24131 O  OE1 . GLU D 2 30   ? 91.773  55.039  79.654  1.00 305.75 ? 158  GLU Y OE1 1 
ATOM   24132 O  OE2 . GLU D 2 30   ? 93.484  54.716  78.316  1.00 308.79 ? 158  GLU Y OE2 1 
ATOM   24133 N  N   . GLU D 2 31   ? 90.584  58.092  75.370  1.00 423.43 ? 159  GLU Y N   1 
ATOM   24134 C  CA  . GLU D 2 31   ? 91.039  59.403  74.921  1.00 420.57 ? 159  GLU Y CA  1 
ATOM   24135 C  C   . GLU D 2 31   ? 91.283  59.345  73.413  1.00 416.22 ? 159  GLU Y C   1 
ATOM   24136 O  O   . GLU D 2 31   ? 91.931  58.423  72.921  1.00 415.53 ? 159  GLU Y O   1 
ATOM   24137 C  CB  . GLU D 2 31   ? 92.319  59.822  75.656  1.00 421.99 ? 159  GLU Y CB  1 
ATOM   24138 C  CG  . GLU D 2 31   ? 93.585  59.069  75.242  1.00 422.92 ? 159  GLU Y CG  1 
ATOM   24139 C  CD  . GLU D 2 31   ? 93.834  57.815  76.064  1.00 425.07 ? 159  GLU Y CD  1 
ATOM   24140 O  OE1 . GLU D 2 31   ? 93.200  57.657  77.127  1.00 426.07 ? 159  GLU Y OE1 1 
ATOM   24141 O  OE2 . GLU D 2 31   ? 94.676  56.989  75.651  1.00 426.07 ? 159  GLU Y OE2 1 
ATOM   24142 N  N   . VAL D 2 32   ? 90.756  60.318  72.676  1.00 428.24 ? 160  VAL Y N   1 
ATOM   24143 C  CA  . VAL D 2 32   ? 90.890  60.298  71.223  1.00 423.22 ? 160  VAL Y CA  1 
ATOM   24144 C  C   . VAL D 2 32   ? 91.468  61.590  70.667  1.00 421.97 ? 160  VAL Y C   1 
ATOM   24145 O  O   . VAL D 2 32   ? 91.225  62.676  71.193  1.00 423.01 ? 160  VAL Y O   1 
ATOM   24146 C  CB  . VAL D 2 32   ? 89.544  60.000  70.521  1.00 201.40 ? 160  VAL Y CB  1 
ATOM   24147 C  CG1 . VAL D 2 32   ? 89.718  60.004  69.005  1.00 199.00 ? 160  VAL Y CG1 1 
ATOM   24148 C  CG2 . VAL D 2 32   ? 88.986  58.668  70.983  1.00 201.06 ? 160  VAL Y CG2 1 
ATOM   24149 N  N   . SER D 2 33   ? 92.244  61.452  69.598  1.00 344.25 ? 161  SER Y N   1 
ATOM   24150 C  CA  . SER D 2 33   ? 92.792  62.596  68.892  1.00 341.98 ? 161  SER Y CA  1 
ATOM   24151 C  C   . SER D 2 33   ? 91.678  63.387  68.224  1.00 340.51 ? 161  SER Y C   1 
ATOM   24152 O  O   . SER D 2 33   ? 90.821  62.819  67.549  1.00 339.71 ? 161  SER Y O   1 
ATOM   24153 C  CB  . SER D 2 33   ? 93.800  62.134  67.840  1.00 338.53 ? 161  SER Y CB  1 
ATOM   24154 O  OG  . SER D 2 33   ? 94.298  63.235  67.100  1.00 335.71 ? 161  SER Y OG  1 
ATOM   24155 N  N   . LEU D 2 34   ? 91.701  64.701  68.415  1.00 272.83 ? 162  LEU Y N   1 
ATOM   24156 C  CA  . LEU D 2 34   ? 90.735  65.596  67.794  1.00 271.40 ? 162  LEU Y CA  1 
ATOM   24157 C  C   . LEU D 2 34   ? 90.764  65.417  66.276  1.00 267.34 ? 162  LEU Y C   1 
ATOM   24158 O  O   . LEU D 2 34   ? 89.820  65.783  65.572  1.00 264.97 ? 162  LEU Y O   1 
ATOM   24159 C  CB  . LEU D 2 34   ? 91.052  67.041  68.178  1.00 272.96 ? 162  LEU Y CB  1 
ATOM   24160 C  CG  . LEU D 2 34   ? 90.102  68.157  67.753  1.00 273.01 ? 162  LEU Y CG  1 
ATOM   24161 C  CD1 . LEU D 2 34   ? 88.680  67.816  68.122  1.00 274.32 ? 162  LEU Y CD1 1 
ATOM   24162 C  CD2 . LEU D 2 34   ? 90.529  69.458  68.406  1.00 274.94 ? 162  LEU Y CD2 1 
ATOM   24163 N  N   . LYS D 2 35   ? 91.865  64.855  65.785  1.00 360.02 ? 163  LYS Y N   1 
ATOM   24164 C  CA  . LYS D 2 35   ? 91.981  64.467  64.388  1.00 356.64 ? 163  LYS Y CA  1 
ATOM   24165 C  C   . LYS D 2 35   ? 90.997  63.343  64.126  1.00 357.54 ? 163  LYS Y C   1 
ATOM   24166 O  O   . LYS D 2 35   ? 90.104  63.465  63.293  1.00 358.23 ? 163  LYS Y O   1 
ATOM   24167 C  CB  . LYS D 2 35   ? 93.401  63.986  64.081  1.00 354.01 ? 163  LYS Y CB  1 
ATOM   24168 C  CG  . LYS D 2 35   ? 93.585  63.418  62.675  1.00 349.10 ? 163  LYS Y CG  1 
ATOM   24169 C  CD  . LYS D 2 35   ? 94.917  62.687  62.540  1.00 346.79 ? 163  LYS Y CD  1 
ATOM   24170 C  CE  . LYS D 2 35   ? 95.109  62.124  61.140  1.00 342.74 ? 163  LYS Y CE  1 
ATOM   24171 N  NZ  . LYS D 2 35   ? 95.188  63.200  60.114  1.00 340.28 ? 163  LYS Y NZ  1 
ATOM   24172 N  N   . GLU D 2 36   ? 91.167  62.246  64.855  1.00 343.97 ? 164  GLU Y N   1 
ATOM   24173 C  CA  . GLU D 2 36   ? 90.271  61.105  64.742  1.00 344.92 ? 164  GLU Y CA  1 
ATOM   24174 C  C   . GLU D 2 36   ? 88.858  61.530  65.125  1.00 339.53 ? 164  GLU Y C   1 
ATOM   24175 O  O   . GLU D 2 36   ? 87.870  61.004  64.605  1.00 336.35 ? 164  GLU Y O   1 
ATOM   24176 C  CB  . GLU D 2 36   ? 90.746  59.958  65.637  1.00 354.56 ? 164  GLU Y CB  1 
ATOM   24177 C  CG  . GLU D 2 36   ? 92.110  59.405  65.257  1.00 360.49 ? 164  GLU Y CG  1 
ATOM   24178 C  CD  . GLU D 2 36   ? 92.537  58.260  66.152  1.00 372.89 ? 164  GLU Y CD  1 
ATOM   24179 O  OE1 . GLU D 2 36   ? 91.925  58.084  67.228  1.00 379.94 ? 164  GLU Y OE1 1 
ATOM   24180 O  OE2 . GLU D 2 36   ? 93.485  57.537  65.784  1.00 375.13 ? 164  GLU Y OE2 1 
ATOM   24181 N  N   . LEU D 2 37   ? 88.779  62.491  66.041  1.00 244.63 ? 165  LEU Y N   1 
ATOM   24182 C  CA  . LEU D 2 37   ? 87.509  63.057  66.468  1.00 241.65 ? 165  LEU Y CA  1 
ATOM   24183 C  C   . LEU D 2 37   ? 86.847  63.694  65.264  1.00 240.04 ? 165  LEU Y C   1 
ATOM   24184 O  O   . LEU D 2 37   ? 85.649  63.536  65.015  1.00 240.12 ? 165  LEU Y O   1 
ATOM   24185 C  CB  . LEU D 2 37   ? 87.759  64.134  67.521  1.00 238.83 ? 165  LEU Y CB  1 
ATOM   24186 C  CG  . LEU D 2 37   ? 86.572  64.446  68.418  1.00 235.84 ? 165  LEU Y CG  1 
ATOM   24187 C  CD1 . LEU D 2 37   ? 86.241  63.203  69.213  1.00 236.20 ? 165  LEU Y CD1 1 
ATOM   24188 C  CD2 . LEU D 2 37   ? 86.865  65.606  69.347  1.00 235.02 ? 165  LEU Y CD2 1 
ATOM   24189 N  N   . ASP D 2 38   ? 87.669  64.412  64.515  1.00 312.03 ? 166  ASP Y N   1 
ATOM   24190 C  CA  . ASP D 2 38   ? 87.208  65.192  63.391  1.00 311.38 ? 166  ASP Y CA  1 
ATOM   24191 C  C   . ASP D 2 38   ? 87.012  64.356  62.131  1.00 310.83 ? 166  ASP Y C   1 
ATOM   24192 O  O   . ASP D 2 38   ? 86.102  64.626  61.350  1.00 309.71 ? 166  ASP Y O   1 
ATOM   24193 C  CB  . ASP D 2 38   ? 88.188  66.325  63.126  1.00 311.56 ? 166  ASP Y CB  1 
ATOM   24194 C  CG  . ASP D 2 38   ? 87.494  67.632  62.893  1.00 313.42 ? 166  ASP Y CG  1 
ATOM   24195 O  OD1 . ASP D 2 38   ? 86.246  67.640  62.917  1.00 315.79 ? 166  ASP Y OD1 1 
ATOM   24196 O  OD2 . ASP D 2 38   ? 88.190  68.648  62.691  1.00 313.45 ? 166  ASP Y OD2 1 
ATOM   24197 N  N   . PHE D 2 39   ? 87.862  63.350  61.928  1.00 344.00 ? 167  PHE Y N   1 
ATOM   24198 C  CA  . PHE D 2 39   ? 87.752  62.497  60.740  1.00 345.62 ? 167  PHE Y CA  1 
ATOM   24199 C  C   . PHE D 2 39   ? 86.500  61.630  60.793  1.00 343.41 ? 167  PHE Y C   1 
ATOM   24200 O  O   . PHE D 2 39   ? 85.964  61.235  59.755  1.00 344.13 ? 167  PHE Y O   1 
ATOM   24201 C  CB  . PHE D 2 39   ? 88.992  61.610  60.552  1.00 349.89 ? 167  PHE Y CB  1 
ATOM   24202 C  CG  . PHE D 2 39   ? 88.937  60.733  59.315  1.00 352.58 ? 167  PHE Y CG  1 
ATOM   24203 C  CD1 . PHE D 2 39   ? 88.340  59.479  59.354  1.00 354.78 ? 167  PHE Y CD1 1 
ATOM   24204 C  CD2 . PHE D 2 39   ? 89.484  61.164  58.117  1.00 352.14 ? 167  PHE Y CD2 1 
ATOM   24205 C  CE1 . PHE D 2 39   ? 88.287  58.677  58.224  1.00 354.57 ? 167  PHE Y CE1 1 
ATOM   24206 C  CE2 . PHE D 2 39   ? 89.434  60.365  56.986  1.00 352.03 ? 167  PHE Y CE2 1 
ATOM   24207 C  CZ  . PHE D 2 39   ? 88.836  59.122  57.041  1.00 352.99 ? 167  PHE Y CZ  1 
ATOM   24208 N  N   . LYS D 2 40   ? 86.045  61.327  62.005  1.00 298.89 ? 168  LYS Y N   1 
ATOM   24209 C  CA  . LYS D 2 40   ? 84.843  60.521  62.182  1.00 293.43 ? 168  LYS Y CA  1 
ATOM   24210 C  C   . LYS D 2 40   ? 83.574  61.369  62.026  1.00 289.93 ? 168  LYS Y C   1 
ATOM   24211 O  O   . LYS D 2 40   ? 82.608  60.949  61.376  1.00 288.43 ? 168  LYS Y O   1 
ATOM   24212 C  CB  . LYS D 2 40   ? 84.876  59.791  63.531  1.00 293.91 ? 168  LYS Y CB  1 
ATOM   24213 C  CG  . LYS D 2 40   ? 85.961  58.721  63.623  1.00 291.32 ? 168  LYS Y CG  1 
ATOM   24214 C  CD  . LYS D 2 40   ? 85.666  57.692  64.702  1.00 292.40 ? 168  LYS Y CD  1 
ATOM   24215 C  CE  . LYS D 2 40   ? 86.560  56.469  64.556  1.00 290.76 ? 168  LYS Y CE  1 
ATOM   24216 N  NZ  . LYS D 2 40   ? 86.229  55.400  65.539  1.00 293.55 ? 168  LYS Y NZ  1 
ATOM   24217 N  N   . ILE D 2 41   ? 83.599  62.571  62.601  1.00 250.36 ? 169  ILE Y N   1 
ATOM   24218 C  CA  . ILE D 2 41   ? 82.462  63.495  62.546  1.00 246.64 ? 169  ILE Y CA  1 
ATOM   24219 C  C   . ILE D 2 41   ? 81.993  63.758  61.099  1.00 245.77 ? 169  ILE Y C   1 
ATOM   24220 O  O   . ILE D 2 41   ? 80.841  63.482  60.741  1.00 248.11 ? 169  ILE Y O   1 
ATOM   24221 C  CB  . ILE D 2 41   ? 82.787  64.825  63.297  1.00 240.21 ? 169  ILE Y CB  1 
ATOM   24222 C  CG1 . ILE D 2 41   ? 83.132  64.552  64.768  1.00 238.39 ? 169  ILE Y CG1 1 
ATOM   24223 C  CG2 . ILE D 2 41   ? 81.632  65.810  63.199  1.00 239.52 ? 169  ILE Y CG2 1 
ATOM   24224 C  CD1 . ILE D 2 41   ? 82.023  63.886  65.560  1.00 237.65 ? 169  ILE Y CD1 1 
ATOM   24225 N  N   . ARG D 2 42   ? 82.895  64.272  60.269  1.00 307.56 ? 170  ARG Y N   1 
ATOM   24226 C  CA  . ARG D 2 42   ? 82.594  64.471  58.857  1.00 307.64 ? 170  ARG Y CA  1 
ATOM   24227 C  C   . ARG D 2 42   ? 82.353  63.144  58.130  1.00 304.48 ? 170  ARG Y C   1 
ATOM   24228 O  O   . ARG D 2 42   ? 81.541  63.086  57.213  1.00 303.76 ? 170  ARG Y O   1 
ATOM   24229 C  CB  . ARG D 2 42   ? 83.703  65.274  58.160  1.00 310.38 ? 170  ARG Y CB  1 
ATOM   24230 C  CG  . ARG D 2 42   ? 85.090  64.631  58.206  1.00 317.85 ? 170  ARG Y CG  1 
ATOM   24231 C  CD  . ARG D 2 42   ? 86.112  65.424  57.387  1.00 321.17 ? 170  ARG Y CD  1 
ATOM   24232 N  NE  . ARG D 2 42   ? 87.491  65.043  57.699  1.00 326.29 ? 170  ARG Y NE  1 
ATOM   24233 C  CZ  . ARG D 2 42   ? 88.568  65.609  57.160  1.00 327.00 ? 170  ARG Y CZ  1 
ATOM   24234 N  NH1 . ARG D 2 42   ? 88.436  66.585  56.273  1.00 325.53 ? 170  ARG Y NH1 1 
ATOM   24235 N  NH2 . ARG D 2 42   ? 89.781  65.199  57.508  1.00 328.23 ? 170  ARG Y NH2 1 
ATOM   24236 N  N   . GLN D 2 43   ? 83.049  62.085  58.543  1.00 243.96 ? 171  GLN Y N   1 
ATOM   24237 C  CA  . GLN D 2 43   ? 82.945  60.776  57.883  1.00 242.69 ? 171  GLN Y CA  1 
ATOM   24238 C  C   . GLN D 2 43   ? 81.482  60.347  57.762  1.00 243.66 ? 171  GLN Y C   1 
ATOM   24239 O  O   . GLN D 2 43   ? 81.035  59.860  56.710  1.00 242.19 ? 171  GLN Y O   1 
ATOM   24240 C  CB  . GLN D 2 43   ? 83.739  59.717  58.663  1.00 241.71 ? 171  GLN Y CB  1 
ATOM   24241 C  CG  . GLN D 2 43   ? 84.090  58.455  57.876  1.00 239.05 ? 171  GLN Y CG  1 
ATOM   24242 C  CD  . GLN D 2 43   ? 84.619  57.338  58.758  1.00 237.81 ? 171  GLN Y CD  1 
ATOM   24243 O  OE1 . GLN D 2 43   ? 84.034  57.020  59.792  1.00 239.13 ? 171  GLN Y OE1 1 
ATOM   24244 N  NE2 . GLN D 2 43   ? 85.726  56.732  58.348  1.00 235.22 ? 171  GLN Y NE2 1 
ATOM   24245 N  N   . HIS D 2 44   ? 80.752  60.542  58.858  1.00 470.11 ? 172  HIS Y N   1 
ATOM   24246 C  CA  . HIS D 2 44   ? 79.334  60.214  58.950  1.00 470.72 ? 172  HIS Y CA  1 
ATOM   24247 C  C   . HIS D 2 44   ? 78.460  61.248  58.264  1.00 473.28 ? 172  HIS Y C   1 
ATOM   24248 O  O   . HIS D 2 44   ? 77.625  60.906  57.431  1.00 474.24 ? 172  HIS Y O   1 
ATOM   24249 C  CB  . HIS D 2 44   ? 78.919  60.092  60.412  1.00 299.24 ? 172  HIS Y CB  1 
ATOM   24250 C  CG  . HIS D 2 44   ? 79.569  58.948  61.126  1.00 299.53 ? 172  HIS Y CG  1 
ATOM   24251 N  ND1 . HIS D 2 44   ? 80.365  59.116  62.231  1.00 300.01 ? 172  HIS Y ND1 1 
ATOM   24252 C  CD2 . HIS D 2 44   ? 79.548  57.618  60.868  1.00 299.45 ? 172  HIS Y CD2 1 
ATOM   24253 C  CE1 . HIS D 2 44   ? 80.800  57.935  62.641  1.00 300.28 ? 172  HIS Y CE1 1 
ATOM   24254 N  NE2 . HIS D 2 44   ? 80.321  57.012  61.831  1.00 299.88 ? 172  HIS Y NE2 1 
ATOM   24255 N  N   . LEU D 2 45   ? 78.642  62.512  58.627  1.00 243.44 ? 173  LEU Y N   1 
ATOM   24256 C  CA  . LEU D 2 45   ? 77.979  63.586  57.905  1.00 244.58 ? 173  LEU Y CA  1 
ATOM   24257 C  C   . LEU D 2 45   ? 78.082  63.328  56.392  1.00 242.07 ? 173  LEU Y C   1 
ATOM   24258 O  O   . LEU D 2 45   ? 77.107  63.498  55.649  1.00 240.54 ? 173  LEU Y O   1 
ATOM   24259 C  CB  . LEU D 2 45   ? 78.618  64.925  58.267  1.00 244.20 ? 173  LEU Y CB  1 
ATOM   24260 C  CG  . LEU D 2 45   ? 78.561  65.283  59.747  1.00 246.45 ? 173  LEU Y CG  1 
ATOM   24261 C  CD1 . LEU D 2 45   ? 79.485  66.446  60.037  1.00 246.57 ? 173  LEU Y CD1 1 
ATOM   24262 C  CD2 . LEU D 2 45   ? 77.132  65.604  60.139  1.00 249.39 ? 173  LEU Y CD2 1 
ATOM   24263 N  N   . VAL D 2 46   ? 79.269  62.900  55.957  1.00 284.24 ? 174  VAL Y N   1 
ATOM   24264 C  CA  . VAL D 2 46   ? 79.555  62.624  54.548  1.00 276.51 ? 174  VAL Y CA  1 
ATOM   24265 C  C   . VAL D 2 46   ? 78.809  61.399  54.058  1.00 275.42 ? 174  VAL Y C   1 
ATOM   24266 O  O   . VAL D 2 46   ? 78.429  61.308  52.897  1.00 270.17 ? 174  VAL Y O   1 
ATOM   24267 C  CB  . VAL D 2 46   ? 81.067  62.418  54.287  1.00 281.33 ? 174  VAL Y CB  1 
ATOM   24268 C  CG1 . VAL D 2 46   ? 81.295  61.734  52.949  1.00 276.23 ? 174  VAL Y CG1 1 
ATOM   24269 C  CG2 . VAL D 2 46   ? 81.789  63.746  54.337  1.00 280.76 ? 174  VAL Y CG2 1 
ATOM   24270 N  N   . LYS D 2 47   ? 78.569  60.445  54.934  1.00 407.46 ? 175  LYS Y N   1 
ATOM   24271 C  CA  . LYS D 2 47   ? 77.914  59.246  54.452  1.00 404.71 ? 175  LYS Y CA  1 
ATOM   24272 C  C   . LYS D 2 47   ? 76.456  59.158  54.876  1.00 404.26 ? 175  LYS Y C   1 
ATOM   24273 O  O   . LYS D 2 47   ? 75.810  58.135  54.617  1.00 403.37 ? 175  LYS Y O   1 
ATOM   24274 C  CB  . LYS D 2 47   ? 78.646  57.993  54.946  1.00 406.95 ? 175  LYS Y CB  1 
ATOM   24275 C  CG  . LYS D 2 47   ? 80.027  57.716  54.294  1.00 402.76 ? 175  LYS Y CG  1 
ATOM   24276 C  CD  . LYS D 2 47   ? 80.751  56.602  54.916  1.00 163.11 ? 175  LYS Y CD  1 
ATOM   24277 C  CE  . LYS D 2 47   ? 81.299  55.557  53.940  1.00 163.83 ? 175  LYS Y CE  1 
ATOM   24278 N  NZ  . LYS D 2 47   ? 81.457  55.789  52.504  1.00 163.95 ? 175  LYS Y NZ  1 
ATOM   24279 N  N   . ASN D 2 48   ? 75.952  60.192  55.560  1.00 271.16 ? 176  ASN Y N   1 
ATOM   24280 C  CA  . ASN D 2 48   ? 74.583  60.167  56.097  1.00 271.73 ? 176  ASN Y CA  1 
ATOM   24281 C  C   . ASN D 2 48   ? 73.738  61.459  56.067  1.00 266.71 ? 176  ASN Y C   1 
ATOM   24282 O  O   . ASN D 2 48   ? 72.517  61.386  55.927  1.00 266.92 ? 176  ASN Y O   1 
ATOM   24283 C  CB  . ASN D 2 48   ? 74.584  59.620  57.523  1.00 277.36 ? 176  ASN Y CB  1 
ATOM   24284 C  CG  . ASN D 2 48   ? 75.252  58.274  57.623  1.00 276.71 ? 176  ASN Y CG  1 
ATOM   24285 O  OD1 . ASN D 2 48   ? 74.586  57.252  57.766  1.00 278.31 ? 176  ASN Y OD1 1 
ATOM   24286 N  ND2 . ASN D 2 48   ? 76.578  58.263  57.547  1.00 274.21 ? 176  ASN Y ND2 1 
ATOM   24287 N  N   . TYR D 2 49   ? 74.356  62.626  56.229  1.00 217.58 ? 177  TYR Y N   1 
ATOM   24288 C  CA  . TYR D 2 49   ? 73.584  63.872  56.287  1.00 216.92 ? 177  TYR Y CA  1 
ATOM   24289 C  C   . TYR D 2 49   ? 73.852  64.793  55.110  1.00 215.24 ? 177  TYR Y C   1 
ATOM   24290 O  O   . TYR D 2 49   ? 73.617  66.001  55.179  1.00 217.17 ? 177  TYR Y O   1 
ATOM   24291 C  CB  . TYR D 2 49   ? 73.823  64.618  57.606  1.00 216.09 ? 177  TYR Y CB  1 
ATOM   24292 C  CG  . TYR D 2 49   ? 73.179  63.934  58.787  1.00 213.75 ? 177  TYR Y CG  1 
ATOM   24293 C  CD1 . TYR D 2 49   ? 73.921  63.116  59.633  1.00 210.88 ? 177  TYR Y CD1 1 
ATOM   24294 C  CD2 . TYR D 2 49   ? 71.818  64.076  59.040  1.00 213.78 ? 177  TYR Y CD2 1 
ATOM   24295 C  CE1 . TYR D 2 49   ? 73.330  62.468  60.712  1.00 210.60 ? 177  TYR Y CE1 1 
ATOM   24296 C  CE2 . TYR D 2 49   ? 71.216  63.435  60.115  1.00 213.94 ? 177  TYR Y CE2 1 
ATOM   24297 C  CZ  . TYR D 2 49   ? 71.980  62.632  60.944  1.00 211.73 ? 177  TYR Y CZ  1 
ATOM   24298 O  OH  . TYR D 2 49   ? 71.401  61.989  62.007  1.00 211.61 ? 177  TYR Y OH  1 
ATOM   24299 N  N   . GLY D 2 50   ? 74.351  64.215  54.028  1.00 284.41 ? 178  GLY Y N   1 
ATOM   24300 C  CA  . GLY D 2 50   ? 74.649  64.981  52.838  1.00 282.55 ? 178  GLY Y CA  1 
ATOM   24301 C  C   . GLY D 2 50   ? 75.579  66.145  53.117  1.00 286.92 ? 178  GLY Y C   1 
ATOM   24302 O  O   . GLY D 2 50   ? 75.132  67.287  53.253  1.00 284.91 ? 178  GLY Y O   1 
ATOM   24303 N  N   . LEU D 2 51   ? 76.871  65.846  53.227  1.00 255.94 ? 179  LEU Y N   1 
ATOM   24304 C  CA  . LEU D 2 51   ? 77.908  66.873  53.276  1.00 261.23 ? 179  LEU Y CA  1 
ATOM   24305 C  C   . LEU D 2 51   ? 78.929  66.630  52.169  1.00 262.14 ? 179  LEU Y C   1 
ATOM   24306 O  O   . LEU D 2 51   ? 79.289  65.486  51.890  1.00 260.78 ? 179  LEU Y O   1 
ATOM   24307 C  CB  . LEU D 2 51   ? 78.620  66.894  54.627  1.00 265.68 ? 179  LEU Y CB  1 
ATOM   24308 C  CG  . LEU D 2 51   ? 79.936  67.678  54.561  1.00 263.39 ? 179  LEU Y CG  1 
ATOM   24309 C  CD1 . LEU D 2 51   ? 79.675  69.129  54.183  1.00 261.95 ? 179  LEU Y CD1 1 
ATOM   24310 C  CD2 . LEU D 2 51   ? 80.705  67.588  55.867  1.00 267.61 ? 179  LEU Y CD2 1 
ATOM   24311 N  N   . TYR D 2 52   ? 79.404  67.712  51.556  1.00 282.33 ? 180  TYR Y N   1 
ATOM   24312 C  CA  . TYR D 2 52   ? 80.328  67.623  50.428  1.00 284.06 ? 180  TYR Y CA  1 
ATOM   24313 C  C   . TYR D 2 52   ? 79.666  67.086  49.155  1.00 285.41 ? 180  TYR Y C   1 
ATOM   24314 O  O   . TYR D 2 52   ? 80.353  66.751  48.189  1.00 283.31 ? 180  TYR Y O   1 
ATOM   24315 C  CB  . TYR D 2 52   ? 81.565  66.789  50.788  1.00 286.43 ? 180  TYR Y CB  1 
ATOM   24316 C  CG  . TYR D 2 52   ? 82.497  67.489  51.740  1.00 291.63 ? 180  TYR Y CG  1 
ATOM   24317 C  CD1 . TYR D 2 52   ? 82.716  68.851  51.633  1.00 291.87 ? 180  TYR Y CD1 1 
ATOM   24318 C  CD2 . TYR D 2 52   ? 83.161  66.792  52.740  1.00 295.88 ? 180  TYR Y CD2 1 
ATOM   24319 C  CE1 . TYR D 2 52   ? 83.562  69.505  52.495  1.00 295.28 ? 180  TYR Y CE1 1 
ATOM   24320 C  CE2 . TYR D 2 52   ? 84.015  67.440  53.610  1.00 299.43 ? 180  TYR Y CE2 1 
ATOM   24321 C  CZ  . TYR D 2 52   ? 84.210  68.798  53.481  1.00 298.76 ? 180  TYR Y CZ  1 
ATOM   24322 O  OH  . TYR D 2 52   ? 85.058  69.456  54.338  1.00 301.78 ? 180  TYR Y OH  1 
ATOM   24323 N  N   . LYS D 2 53   ? 78.335  67.001  49.164  1.00 247.56 ? 181  LYS Y N   1 
ATOM   24324 C  CA  . LYS D 2 53   ? 77.572  66.615  47.976  1.00 247.12 ? 181  LYS Y CA  1 
ATOM   24325 C  C   . LYS D 2 53   ? 76.528  67.684  47.630  1.00 245.63 ? 181  LYS Y C   1 
ATOM   24326 O  O   . LYS D 2 53   ? 75.362  67.585  48.023  1.00 247.59 ? 181  LYS Y O   1 
ATOM   24327 C  CB  . LYS D 2 53   ? 76.893  65.246  48.155  1.00 253.77 ? 181  LYS Y CB  1 
ATOM   24328 C  CG  . LYS D 2 53   ? 77.783  64.123  48.700  1.00 257.00 ? 181  LYS Y CG  1 
ATOM   24329 C  CD  . LYS D 2 53   ? 79.036  63.880  47.856  1.00 259.48 ? 181  LYS Y CD  1 
ATOM   24330 C  CE  . LYS D 2 53   ? 78.738  63.233  46.511  1.00 256.93 ? 181  LYS Y CE  1 
ATOM   24331 N  NZ  . LYS D 2 53   ? 79.988  63.100  45.706  1.00 257.01 ? 181  LYS Y NZ  1 
ATOM   24332 N  N   . GLY D 2 54   ? 76.958  68.704  46.892  1.00 285.53 ? 182  GLY Y N   1 
ATOM   24333 C  CA  . GLY D 2 54   ? 76.074  69.780  46.485  1.00 283.16 ? 182  GLY Y CA  1 
ATOM   24334 C  C   . GLY D 2 54   ? 76.413  71.086  47.172  1.00 282.33 ? 182  GLY Y C   1 
ATOM   24335 O  O   . GLY D 2 54   ? 77.582  71.481  47.243  1.00 279.96 ? 182  GLY Y O   1 
ATOM   24336 N  N   . THR D 2 55   ? 75.385  71.763  47.671  1.00 267.77 ? 183  THR Y N   1 
ATOM   24337 C  CA  . THR D 2 55   ? 75.560  73.035  48.362  1.00 269.76 ? 183  THR Y CA  1 
ATOM   24338 C  C   . THR D 2 55   ? 76.044  72.824  49.796  1.00 277.80 ? 183  THR Y C   1 
ATOM   24339 O  O   . THR D 2 55   ? 76.163  73.750  50.566  1.00 281.14 ? 183  THR Y O   1 
ATOM   24340 C  CB  . THR D 2 55   ? 74.253  73.826  48.357  1.00 262.96 ? 183  THR Y CB  1 
ATOM   24341 O  OG1 . THR D 2 55   ? 73.175  72.936  48.668  1.00 264.43 ? 183  THR Y OG1 1 
ATOM   24342 C  CG2 . THR D 2 55   ? 74.021  74.445  47.001  1.00 258.22 ? 183  THR Y CG2 1 
ATOM   24343 N  N   . THR D 2 56   ? 76.316  71.582  50.154  1.00 439.89 ? 184  THR Y N   1 
ATOM   24344 C  CA  . THR D 2 56   ? 76.802  71.287  51.497  1.00 446.63 ? 184  THR Y CA  1 
ATOM   24345 C  C   . THR D 2 56   ? 78.326  71.308  51.629  1.00 447.40 ? 184  THR Y C   1 
ATOM   24346 O  O   . THR D 2 56   ? 79.052  70.586  50.926  1.00 444.54 ? 184  THR Y O   1 
ATOM   24347 C  CB  . THR D 2 56   ? 76.284  69.929  52.003  1.00 449.27 ? 184  THR Y CB  1 
ATOM   24348 O  OG1 . THR D 2 56   ? 75.407  69.331  51.021  1.00 197.83 ? 184  THR Y OG1 1 
ATOM   24349 C  CG2 . THR D 2 56   ? 75.545  70.087  53.408  1.00 196.76 ? 184  THR Y CG2 1 
ATOM   24350 N  N   . LYS D 2 57   ? 78.798  72.123  52.567  1.00 258.23 ? 185  LYS Y N   1 
ATOM   24351 C  CA  . LYS D 2 57   ? 80.232  72.248  52.831  1.00 259.01 ? 185  LYS Y CA  1 
ATOM   24352 C  C   . LYS D 2 57   ? 80.572  73.292  53.906  1.00 259.08 ? 185  LYS Y C   1 
ATOM   24353 O  O   . LYS D 2 57   ? 81.598  73.187  54.589  1.00 261.37 ? 185  LYS Y O   1 
ATOM   24354 C  CB  . LYS D 2 57   ? 81.002  72.543  51.533  1.00 256.95 ? 185  LYS Y CB  1 
ATOM   24355 C  CG  . LYS D 2 57   ? 80.568  73.814  50.832  1.00 257.18 ? 185  LYS Y CG  1 
ATOM   24356 C  CD  . LYS D 2 57   ? 81.354  74.087  49.555  1.00 253.50 ? 185  LYS Y CD  1 
ATOM   24357 C  CE  . LYS D 2 57   ? 80.832  73.268  48.377  1.00 251.16 ? 185  LYS Y CE  1 
ATOM   24358 N  NZ  . LYS D 2 57   ? 81.330  73.769  47.060  1.00 246.38 ? 185  LYS Y NZ  1 
ATOM   24359 N  N   . TYR D 2 58   ? 79.717  74.301  54.052  1.00 292.11 ? 186  TYR Y N   1 
ATOM   24360 C  CA  . TYR D 2 58   ? 79.969  75.375  55.009  1.00 292.25 ? 186  TYR Y CA  1 
ATOM   24361 C  C   . TYR D 2 58   ? 79.166  75.234  56.307  1.00 294.68 ? 186  TYR Y C   1 
ATOM   24362 O  O   . TYR D 2 58   ? 77.936  75.296  56.289  1.00 294.26 ? 186  TYR Y O   1 
ATOM   24363 C  CB  . TYR D 2 58   ? 79.687  76.730  54.364  1.00 289.14 ? 186  TYR Y CB  1 
ATOM   24364 C  CG  . TYR D 2 58   ? 79.953  77.888  55.292  1.00 284.56 ? 186  TYR Y CG  1 
ATOM   24365 C  CD1 . TYR D 2 58   ? 81.234  78.402  55.445  1.00 282.24 ? 186  TYR Y CD1 1 
ATOM   24366 C  CD2 . TYR D 2 58   ? 78.926  78.460  56.028  1.00 283.74 ? 186  TYR Y CD2 1 
ATOM   24367 C  CE1 . TYR D 2 58   ? 81.482  79.461  56.303  1.00 278.73 ? 186  TYR Y CE1 1 
ATOM   24368 C  CE2 . TYR D 2 58   ? 79.163  79.520  56.885  1.00 280.27 ? 186  TYR Y CE2 1 
ATOM   24369 C  CZ  . TYR D 2 58   ? 80.442  80.016  57.019  1.00 277.79 ? 186  TYR Y CZ  1 
ATOM   24370 O  OH  . TYR D 2 58   ? 80.680  81.068  57.873  1.00 274.12 ? 186  TYR Y OH  1 
ATOM   24371 N  N   . GLY D 2 59   ? 79.870  75.072  57.427  1.00 256.16 ? 187  GLY Y N   1 
ATOM   24372 C  CA  . GLY D 2 59   ? 79.236  74.888  58.725  1.00 259.35 ? 187  GLY Y CA  1 
ATOM   24373 C  C   . GLY D 2 59   ? 80.210  74.920  59.900  1.00 257.70 ? 187  GLY Y C   1 
ATOM   24374 O  O   . GLY D 2 59   ? 81.403  75.164  59.714  1.00 255.06 ? 187  GLY Y O   1 
ATOM   24375 N  N   . LYS D 2 60   ? 79.704  74.673  61.111  1.00 244.29 ? 188  LYS Y N   1 
ATOM   24376 C  CA  . LYS D 2 60   ? 80.527  74.700  62.326  1.00 245.47 ? 188  LYS Y CA  1 
ATOM   24377 C  C   . LYS D 2 60   ? 80.090  73.660  63.355  1.00 245.77 ? 188  LYS Y C   1 
ATOM   24378 O  O   . LYS D 2 60   ? 78.995  73.738  63.911  1.00 249.25 ? 188  LYS Y O   1 
ATOM   24379 C  CB  . LYS D 2 60   ? 80.502  76.089  62.970  1.00 247.73 ? 188  LYS Y CB  1 
ATOM   24380 C  CG  . LYS D 2 60   ? 81.261  77.166  62.205  1.00 246.95 ? 188  LYS Y CG  1 
ATOM   24381 C  CD  . LYS D 2 60   ? 82.764  76.969  62.307  1.00 245.76 ? 188  LYS Y CD  1 
ATOM   24382 C  CE  . LYS D 2 60   ? 83.517  78.210  61.857  1.00 244.02 ? 188  LYS Y CE  1 
ATOM   24383 N  NZ  . LYS D 2 60   ? 83.350  78.486  60.409  1.00 241.16 ? 188  LYS Y NZ  1 
ATOM   24384 N  N   . ILE D 2 61   ? 80.966  72.692  63.604  1.00 362.44 ? 189  ILE Y N   1 
ATOM   24385 C  CA  . ILE D 2 61   ? 80.709  71.637  64.575  1.00 362.15 ? 189  ILE Y CA  1 
ATOM   24386 C  C   . ILE D 2 61   ? 81.015  72.147  65.983  1.00 364.22 ? 189  ILE Y C   1 
ATOM   24387 O  O   . ILE D 2 61   ? 82.120  72.611  66.243  1.00 363.84 ? 189  ILE Y O   1 
ATOM   24388 C  CB  . ILE D 2 61   ? 81.590  70.405  64.281  1.00 358.59 ? 189  ILE Y CB  1 
ATOM   24389 C  CG1 . ILE D 2 61   ? 81.722  70.181  62.773  1.00 355.23 ? 189  ILE Y CG1 1 
ATOM   24390 C  CG2 . ILE D 2 61   ? 81.032  69.167  64.957  1.00 359.96 ? 189  ILE Y CG2 1 
ATOM   24391 C  CD1 . ILE D 2 61   ? 82.653  69.047  62.409  1.00 352.91 ? 189  ILE Y CD1 1 
ATOM   24392 N  N   . THR D 2 62   ? 80.049  72.053  66.893  1.00 456.37 ? 190  THR Y N   1 
ATOM   24393 C  CA  . THR D 2 62   ? 80.228  72.595  68.242  1.00 460.39 ? 190  THR Y CA  1 
ATOM   24394 C  C   . THR D 2 62   ? 80.299  71.517  69.330  1.00 463.87 ? 190  THR Y C   1 
ATOM   24395 O  O   . THR D 2 62   ? 79.269  71.041  69.809  1.00 465.54 ? 190  THR Y O   1 
ATOM   24396 C  CB  . THR D 2 62   ? 79.108  73.594  68.590  1.00 261.57 ? 190  THR Y CB  1 
ATOM   24397 O  OG1 . THR D 2 62   ? 77.890  72.886  68.853  1.00 263.90 ? 190  THR Y OG1 1 
ATOM   24398 C  CG2 . THR D 2 62   ? 78.890  74.560  67.435  1.00 259.98 ? 190  THR Y CG2 1 
ATOM   24399 N  N   . ILE D 2 63   ? 81.516  71.147  69.726  1.00 358.97 ? 191  ILE Y N   1 
ATOM   24400 C  CA  . ILE D 2 63   ? 81.712  70.114  70.746  1.00 364.15 ? 191  ILE Y CA  1 
ATOM   24401 C  C   . ILE D 2 63   ? 81.418  70.627  72.150  1.00 370.64 ? 191  ILE Y C   1 
ATOM   24402 O  O   . ILE D 2 63   ? 81.981  71.632  72.578  1.00 373.12 ? 191  ILE Y O   1 
ATOM   24403 C  CB  . ILE D 2 63   ? 83.158  69.563  70.765  1.00 309.53 ? 191  ILE Y CB  1 
ATOM   24404 C  CG1 . ILE D 2 63   ? 83.680  69.302  69.356  1.00 301.69 ? 191  ILE Y CG1 1 
ATOM   24405 C  CG2 . ILE D 2 63   ? 83.235  68.288  71.602  1.00 312.06 ? 191  ILE Y CG2 1 
ATOM   24406 C  CD1 . ILE D 2 63   ? 85.044  68.629  69.338  1.00 296.66 ? 191  ILE Y CD1 1 
ATOM   24407 N  N   . ASN D 2 64   ? 80.543  69.926  72.865  1.00 371.74 ? 192  ASN Y N   1 
ATOM   24408 C  CA  . ASN D 2 64   ? 80.320  70.200  74.280  1.00 375.78 ? 192  ASN Y CA  1 
ATOM   24409 C  C   . ASN D 2 64   ? 81.279  69.392  75.149  1.00 378.39 ? 192  ASN Y C   1 
ATOM   24410 O  O   . ASN D 2 64   ? 81.517  68.214  74.887  1.00 376.34 ? 192  ASN Y O   1 
ATOM   24411 C  CB  . ASN D 2 64   ? 78.872  69.902  74.678  1.00 376.59 ? 192  ASN Y CB  1 
ATOM   24412 C  CG  . ASN D 2 64   ? 77.881  70.843  74.023  1.00 378.80 ? 192  ASN Y CG  1 
ATOM   24413 O  OD1 . ASN D 2 64   ? 78.266  71.826  73.391  1.00 380.61 ? 192  ASN Y OD1 1 
ATOM   24414 N  ND2 . ASN D 2 64   ? 76.593  70.543  74.171  1.00 378.43 ? 192  ASN Y ND2 1 
ATOM   24415 N  N   . LEU D 2 65   ? 81.823  70.026  76.185  1.00 495.45 ? 193  LEU Y N   1 
ATOM   24416 C  CA  . LEU D 2 65   ? 82.782  69.368  77.069  1.00 495.72 ? 193  LEU Y CA  1 
ATOM   24417 C  C   . LEU D 2 65   ? 82.491  69.657  78.551  1.00 497.52 ? 193  LEU Y C   1 
ATOM   24418 O  O   . LEU D 2 65   ? 82.649  68.780  79.403  1.00 497.15 ? 193  LEU Y O   1 
ATOM   24419 C  CB  . LEU D 2 65   ? 84.219  69.777  76.701  1.00 493.92 ? 193  LEU Y CB  1 
ATOM   24420 C  CG  . LEU D 2 65   ? 84.711  69.481  75.273  1.00 492.53 ? 193  LEU Y CG  1 
ATOM   24421 C  CD1 . LEU D 2 65   ? 85.967  70.278  74.931  1.00 491.50 ? 193  LEU Y CD1 1 
ATOM   24422 C  CD2 . LEU D 2 65   ? 84.948  67.991  75.057  1.00 491.33 ? 193  LEU Y CD2 1 
ATOM   24423 N  N   . LYS D 2 66   ? 82.051  70.879  78.848  1.00 318.08 ? 194  LYS Y N   1 
ATOM   24424 C  CA  . LYS D 2 66   ? 81.726  71.279  80.220  1.00 322.66 ? 194  LYS Y CA  1 
ATOM   24425 C  C   . LYS D 2 66   ? 80.766  72.477  80.232  1.00 324.37 ? 194  LYS Y C   1 
ATOM   24426 O  O   . LYS D 2 66   ? 80.472  73.048  79.183  1.00 322.50 ? 194  LYS Y O   1 
ATOM   24427 C  CB  . LYS D 2 66   ? 83.004  71.596  81.006  1.00 326.99 ? 194  LYS Y CB  1 
ATOM   24428 C  CG  . LYS D 2 66   ? 82.800  71.677  82.506  1.00 331.90 ? 194  LYS Y CG  1 
ATOM   24429 C  CD  . LYS D 2 66   ? 82.158  70.409  83.033  1.00 338.59 ? 194  LYS Y CD  1 
ATOM   24430 C  CE  . LYS D 2 66   ? 81.632  70.621  84.433  1.00 342.85 ? 194  LYS Y CE  1 
ATOM   24431 N  NZ  . LYS D 2 66   ? 80.644  71.731  84.463  1.00 346.14 ? 194  LYS Y NZ  1 
ATOM   24432 N  N   . ASP D 2 67   ? 80.287  72.853  81.418  1.00 238.71 ? 195  ASP Y N   1 
ATOM   24433 C  CA  . ASP D 2 67   ? 79.256  73.889  81.561  1.00 240.47 ? 195  ASP Y CA  1 
ATOM   24434 C  C   . ASP D 2 67   ? 79.635  75.281  81.052  1.00 247.86 ? 195  ASP Y C   1 
ATOM   24435 O  O   . ASP D 2 67   ? 78.975  76.263  81.392  1.00 250.70 ? 195  ASP Y O   1 
ATOM   24436 C  CB  . ASP D 2 67   ? 78.798  73.997  83.020  1.00 234.69 ? 195  ASP Y CB  1 
ATOM   24437 C  CG  . ASP D 2 67   ? 77.706  73.001  83.369  1.00 225.30 ? 195  ASP Y CG  1 
ATOM   24438 O  OD1 . ASP D 2 67   ? 76.606  73.087  82.784  1.00 221.59 ? 195  ASP Y OD1 1 
ATOM   24439 O  OD2 . ASP D 2 67   ? 77.942  72.140  84.239  1.00 222.66 ? 195  ASP Y OD2 1 
ATOM   24440 N  N   . GLY D 2 68   ? 80.681  75.377  80.239  1.00 387.81 ? 196  GLY Y N   1 
ATOM   24441 C  CA  . GLY D 2 68   ? 81.100  76.672  79.739  1.00 394.27 ? 196  GLY Y CA  1 
ATOM   24442 C  C   . GLY D 2 68   ? 82.068  76.666  78.572  1.00 387.96 ? 196  GLY Y C   1 
ATOM   24443 O  O   . GLY D 2 68   ? 82.591  77.718  78.200  1.00 389.08 ? 196  GLY Y O   1 
ATOM   24444 N  N   . GLU D 2 69   ? 82.314  75.499  77.987  1.00 516.16 ? 197  GLU Y N   1 
ATOM   24445 C  CA  . GLU D 2 69   ? 83.260  75.418  76.880  1.00 513.30 ? 197  GLU Y CA  1 
ATOM   24446 C  C   . GLU D 2 69   ? 82.603  75.049  75.559  1.00 511.79 ? 197  GLU Y C   1 
ATOM   24447 O  O   . GLU D 2 69   ? 81.948  74.012  75.447  1.00 513.13 ? 197  GLU Y O   1 
ATOM   24448 C  CB  . GLU D 2 69   ? 84.377  74.437  77.212  1.00 303.79 ? 197  GLU Y CB  1 
ATOM   24449 C  CG  . GLU D 2 69   ? 85.660  74.705  76.482  1.00 303.47 ? 197  GLU Y CG  1 
ATOM   24450 C  CD  . GLU D 2 69   ? 86.851  74.159  77.229  1.00 302.06 ? 197  GLU Y CD  1 
ATOM   24451 O  OE1 . GLU D 2 69   ? 86.765  74.041  78.469  1.00 301.24 ? 197  GLU Y OE1 1 
ATOM   24452 O  OE2 . GLU D 2 69   ? 87.866  73.838  76.580  1.00 301.87 ? 197  GLU Y OE2 1 
ATOM   24453 N  N   . LYS D 2 70   ? 82.804  75.904  74.561  1.00 321.97 ? 198  LYS Y N   1 
ATOM   24454 C  CA  . LYS D 2 70   ? 82.193  75.730  73.249  1.00 313.12 ? 198  LYS Y CA  1 
ATOM   24455 C  C   . LYS D 2 70   ? 83.177  76.070  72.122  1.00 308.43 ? 198  LYS Y C   1 
ATOM   24456 O  O   . LYS D 2 70   ? 83.607  77.219  71.986  1.00 309.31 ? 198  LYS Y O   1 
ATOM   24457 C  CB  . LYS D 2 70   ? 80.933  76.601  73.128  1.00 308.26 ? 198  LYS Y CB  1 
ATOM   24458 C  CG  . LYS D 2 70   ? 79.858  76.330  74.169  1.00 302.94 ? 198  LYS Y CG  1 
ATOM   24459 C  CD  . LYS D 2 70   ? 78.530  76.976  73.788  1.00 297.33 ? 198  LYS Y CD  1 
ATOM   24460 C  CE  . LYS D 2 70   ? 78.534  78.473  74.030  1.00 293.96 ? 198  LYS Y CE  1 
ATOM   24461 N  NZ  . LYS D 2 70   ? 78.665  78.770  75.474  1.00 288.34 ? 198  LYS Y NZ  1 
ATOM   24462 N  N   . GLN D 2 71   ? 83.514  75.064  71.317  1.00 493.59 ? 199  GLN Y N   1 
ATOM   24463 C  CA  . GLN D 2 71   ? 84.485  75.204  70.231  1.00 490.39 ? 199  GLN Y CA  1 
ATOM   24464 C  C   . GLN D 2 71   ? 83.981  74.549  68.937  1.00 484.98 ? 199  GLN Y C   1 
ATOM   24465 O  O   . GLN D 2 71   ? 83.010  73.790  68.965  1.00 484.07 ? 199  GLN Y O   1 
ATOM   24466 C  CB  . GLN D 2 71   ? 85.846  74.623  70.651  1.00 281.93 ? 199  GLN Y CB  1 
ATOM   24467 C  CG  . GLN D 2 71   ? 85.760  73.503  71.698  1.00 285.57 ? 199  GLN Y CG  1 
ATOM   24468 C  CD  . GLN D 2 71   ? 87.085  72.776  71.921  1.00 285.25 ? 199  GLN Y CD  1 
ATOM   24469 O  OE1 . GLN D 2 71   ? 87.603  72.113  71.026  1.00 283.69 ? 199  GLN Y OE1 1 
ATOM   24470 N  NE2 . GLN D 2 71   ? 87.625  72.886  73.125  1.00 284.19 ? 199  GLN Y NE2 1 
ATOM   24471 N  N   . GLU D 2 72   ? 84.654  74.833  67.818  1.00 341.88 ? 200  GLU Y N   1 
ATOM   24472 C  CA  . GLU D 2 72   ? 84.199  74.402  66.487  1.00 335.80 ? 200  GLU Y CA  1 
ATOM   24473 C  C   . GLU D 2 72   ? 85.331  74.040  65.515  1.00 330.59 ? 200  GLU Y C   1 
ATOM   24474 O  O   . GLU D 2 72   ? 86.507  74.236  65.809  1.00 327.86 ? 200  GLU Y O   1 
ATOM   24475 C  CB  . GLU D 2 72   ? 83.336  75.494  65.845  1.00 336.11 ? 200  GLU Y CB  1 
ATOM   24476 C  CG  . GLU D 2 72   ? 82.281  76.075  66.763  1.00 338.79 ? 200  GLU Y CG  1 
ATOM   24477 C  CD  . GLU D 2 72   ? 81.810  77.445  66.315  1.00 339.82 ? 200  GLU Y CD  1 
ATOM   24478 O  OE1 . GLU D 2 72   ? 82.000  77.792  65.129  1.00 337.97 ? 200  GLU Y OE1 1 
ATOM   24479 O  OE2 . GLU D 2 72   ? 81.245  78.176  67.153  1.00 342.83 ? 200  GLU Y OE2 1 
ATOM   24480 N  N   . ILE D 2 73   ? 84.954  73.530  64.345  1.00 326.05 ? 201  ILE Y N   1 
ATOM   24481 C  CA  . ILE D 2 73   ? 85.903  73.207  63.282  1.00 322.23 ? 201  ILE Y CA  1 
ATOM   24482 C  C   . ILE D 2 73   ? 85.289  73.598  61.952  1.00 324.35 ? 201  ILE Y C   1 
ATOM   24483 O  O   . ILE D 2 73   ? 84.392  72.915  61.456  1.00 324.75 ? 201  ILE Y O   1 
ATOM   24484 C  CB  . ILE D 2 73   ? 86.197  71.703  63.216  1.00 315.91 ? 201  ILE Y CB  1 
ATOM   24485 C  CG1 . ILE D 2 73   ? 86.506  71.163  64.611  1.00 314.86 ? 201  ILE Y CG1 1 
ATOM   24486 C  CG2 . ILE D 2 73   ? 87.335  71.430  62.242  1.00 311.80 ? 201  ILE Y CG2 1 
ATOM   24487 C  CD1 . ILE D 2 73   ? 86.214  69.692  64.783  1.00 312.32 ? 201  ILE Y CD1 1 
ATOM   24488 N  N   . ASP D 2 74   ? 85.766  74.694  61.373  1.00 257.47 ? 202  ASP Y N   1 
ATOM   24489 C  CA  . ASP D 2 74   ? 85.181  75.172  60.134  1.00 261.02 ? 202  ASP Y CA  1 
ATOM   24490 C  C   . ASP D 2 74   ? 85.119  74.011  59.163  1.00 263.02 ? 202  ASP Y C   1 
ATOM   24491 O  O   . ASP D 2 74   ? 86.100  73.288  58.982  1.00 260.24 ? 202  ASP Y O   1 
ATOM   24492 C  CB  . ASP D 2 74   ? 85.997  76.320  59.537  1.00 261.56 ? 202  ASP Y CB  1 
ATOM   24493 C  CG  . ASP D 2 74   ? 85.368  76.889  58.270  1.00 262.72 ? 202  ASP Y CG  1 
ATOM   24494 O  OD1 . ASP D 2 74   ? 86.064  77.625  57.538  1.00 259.45 ? 202  ASP Y OD1 1 
ATOM   24495 O  OD2 . ASP D 2 74   ? 84.182  76.601  58.000  1.00 263.17 ? 202  ASP Y OD2 1 
ATOM   24496 N  N   . LEU D 2 75   ? 83.949  73.818  58.568  1.00 302.06 ? 203  LEU Y N   1 
ATOM   24497 C  CA  . LEU D 2 75   ? 83.774  72.800  57.549  1.00 306.05 ? 203  LEU Y CA  1 
ATOM   24498 C  C   . LEU D 2 75   ? 84.075  73.395  56.187  1.00 308.19 ? 203  LEU Y C   1 
ATOM   24499 O  O   . LEU D 2 75   ? 84.091  72.691  55.180  1.00 304.45 ? 203  LEU Y O   1 
ATOM   24500 C  CB  . LEU D 2 75   ? 82.360  72.233  57.597  1.00 303.80 ? 203  LEU Y CB  1 
ATOM   24501 C  CG  . LEU D 2 75   ? 82.026  71.615  58.954  1.00 302.99 ? 203  LEU Y CG  1 
ATOM   24502 C  CD1 . LEU D 2 75   ? 80.623  71.036  58.961  1.00 303.69 ? 203  LEU Y CD1 1 
ATOM   24503 C  CD2 . LEU D 2 75   ? 83.048  70.549  59.314  1.00 300.75 ? 203  LEU Y CD2 1 
ATOM   24504 N  N   . GLY D 2 76   ? 84.310  74.702  56.165  1.00 295.97 ? 204  GLY Y N   1 
ATOM   24505 C  CA  . GLY D 2 76   ? 84.750  75.376  54.961  1.00 297.80 ? 204  GLY Y CA  1 
ATOM   24506 C  C   . GLY D 2 76   ? 86.191  75.033  54.631  1.00 304.05 ? 204  GLY Y C   1 
ATOM   24507 O  O   . GLY D 2 76   ? 86.640  75.235  53.503  1.00 300.16 ? 204  GLY Y O   1 
ATOM   24508 N  N   . ASP D 2 77   ? 86.918  74.501  55.611  1.00 286.81 ? 205  ASP Y N   1 
ATOM   24509 C  CA  . ASP D 2 77   ? 88.334  74.208  55.418  1.00 292.60 ? 205  ASP Y CA  1 
ATOM   24510 C  C   . ASP D 2 77   ? 88.906  73.266  56.481  1.00 296.19 ? 205  ASP Y C   1 
ATOM   24511 O  O   . ASP D 2 77   ? 88.679  73.448  57.680  1.00 298.24 ? 205  ASP Y O   1 
ATOM   24512 C  CB  . ASP D 2 77   ? 89.134  75.512  55.395  1.00 297.30 ? 205  ASP Y CB  1 
ATOM   24513 C  CG  . ASP D 2 77   ? 90.385  75.412  54.551  1.00 300.09 ? 205  ASP Y CG  1 
ATOM   24514 O  OD1 . ASP D 2 77   ? 90.518  74.415  53.808  1.00 299.72 ? 205  ASP Y OD1 1 
ATOM   24515 O  OD2 . ASP D 2 77   ? 91.229  76.332  54.624  1.00 302.38 ? 205  ASP Y OD2 1 
ATOM   24516 N  N   . LYS D 2 78   ? 89.654  72.264  56.024  1.00 299.86 ? 206  LYS Y N   1 
ATOM   24517 C  CA  . LYS D 2 78   ? 90.345  71.323  56.907  1.00 298.33 ? 206  LYS Y CA  1 
ATOM   24518 C  C   . LYS D 2 78   ? 91.732  71.840  57.305  1.00 295.01 ? 206  LYS Y C   1 
ATOM   24519 O  O   . LYS D 2 78   ? 92.640  71.054  57.586  1.00 294.99 ? 206  LYS Y O   1 
ATOM   24520 C  CB  . LYS D 2 78   ? 90.464  69.944  56.237  1.00 297.72 ? 206  LYS Y CB  1 
ATOM   24521 C  CG  . LYS D 2 78   ? 91.170  69.956  54.882  1.00 296.90 ? 206  LYS Y CG  1 
ATOM   24522 C  CD  . LYS D 2 78   ? 91.130  68.590  54.218  1.00 296.12 ? 206  LYS Y CD  1 
ATOM   24523 C  CE  . LYS D 2 78   ? 91.781  68.636  52.853  1.00 294.33 ? 206  LYS Y CE  1 
ATOM   24524 N  NZ  . LYS D 2 78   ? 93.196  69.076  52.952  1.00 290.72 ? 206  LYS Y NZ  1 
ATOM   24525 N  N   . LEU D 2 79   ? 91.883  73.163  57.325  1.00 368.10 ? 207  LEU Y N   1 
ATOM   24526 C  CA  . LEU D 2 79   ? 93.176  73.812  57.564  1.00 362.88 ? 207  LEU Y CA  1 
ATOM   24527 C  C   . LEU D 2 79   ? 93.660  73.701  59.014  1.00 360.45 ? 207  LEU Y C   1 
ATOM   24528 O  O   . LEU D 2 79   ? 94.621  74.369  59.396  1.00 360.74 ? 207  LEU Y O   1 
ATOM   24529 C  CB  . LEU D 2 79   ? 93.122  75.288  57.123  1.00 362.63 ? 207  LEU Y CB  1 
ATOM   24530 C  CG  . LEU D 2 79   ? 94.384  76.164  57.061  1.00 362.08 ? 207  LEU Y CG  1 
ATOM   24531 C  CD1 . LEU D 2 79   ? 95.426  75.594  56.110  1.00 360.07 ? 207  LEU Y CD1 1 
ATOM   24532 C  CD2 . LEU D 2 79   ? 94.028  77.591  56.659  1.00 362.53 ? 207  LEU Y CD2 1 
ATOM   24533 N  N   . GLN D 2 80   ? 92.998  72.868  59.817  1.00 326.94 ? 208  GLN Y N   1 
ATOM   24534 C  CA  . GLN D 2 80   ? 93.372  72.691  61.228  1.00 324.49 ? 208  GLN Y CA  1 
ATOM   24535 C  C   . GLN D 2 80   ? 94.509  71.661  61.422  1.00 321.54 ? 208  GLN Y C   1 
ATOM   24536 O  O   . GLN D 2 80   ? 94.249  70.508  61.767  1.00 321.52 ? 208  GLN Y O   1 
ATOM   24537 C  CB  . GLN D 2 80   ? 92.141  72.301  62.068  1.00 324.04 ? 208  GLN Y CB  1 
ATOM   24538 C  CG  . GLN D 2 80   ? 91.019  73.345  62.113  1.00 327.35 ? 208  GLN Y CG  1 
ATOM   24539 C  CD  . GLN D 2 80   ? 90.030  73.237  60.954  1.00 331.33 ? 208  GLN Y CD  1 
ATOM   24540 O  OE1 . GLN D 2 80   ? 90.148  72.360  60.104  1.00 334.71 ? 208  GLN Y OE1 1 
ATOM   24541 N  NE2 . GLN D 2 80   ? 89.047  74.133  60.924  1.00 331.44 ? 208  GLN Y NE2 1 
ATOM   24542 N  N   . PHE D 2 81   ? 95.762  72.079  61.218  1.00 294.46 ? 209  PHE Y N   1 
ATOM   24543 C  CA  . PHE D 2 81   ? 96.904  71.148  61.255  1.00 293.29 ? 209  PHE Y CA  1 
ATOM   24544 C  C   . PHE D 2 81   ? 97.741  71.148  62.540  1.00 299.17 ? 209  PHE Y C   1 
ATOM   24545 O  O   . PHE D 2 81   ? 98.435  70.171  62.823  1.00 300.17 ? 209  PHE Y O   1 
ATOM   24546 C  CB  . PHE D 2 81   ? 97.817  71.312  60.021  1.00 286.52 ? 209  PHE Y CB  1 
ATOM   24547 C  CG  . PHE D 2 81   ? 98.428  72.685  59.874  1.00 281.61 ? 209  PHE Y CG  1 
ATOM   24548 C  CD1 . PHE D 2 81   ? 99.503  73.071  60.661  1.00 281.23 ? 209  PHE Y CD1 1 
ATOM   24549 C  CD2 . PHE D 2 81   ? 97.943  73.576  58.926  1.00 277.56 ? 209  PHE Y CD2 1 
ATOM   24550 C  CE1 . PHE D 2 81   ? 100.067 74.324  60.518  1.00 279.70 ? 209  PHE Y CE1 1 
ATOM   24551 C  CE2 . PHE D 2 81   ? 98.503  74.829  58.779  1.00 276.00 ? 209  PHE Y CE2 1 
ATOM   24552 C  CZ  . PHE D 2 81   ? 99.567  75.203  59.576  1.00 277.52 ? 209  PHE Y CZ  1 
ATOM   24553 N  N   . GLU D 2 82   ? 97.685  72.236  63.305  1.00 291.18 ? 210  GLU Y N   1 
ATOM   24554 C  CA  . GLU D 2 82   ? 98.466  72.343  64.540  1.00 297.16 ? 210  GLU Y CA  1 
ATOM   24555 C  C   . GLU D 2 82   ? 97.711  71.824  65.763  1.00 298.88 ? 210  GLU Y C   1 
ATOM   24556 O  O   . GLU D 2 82   ? 98.303  71.238  66.674  1.00 302.38 ? 210  GLU Y O   1 
ATOM   24557 C  CB  . GLU D 2 82   ? 98.908  73.791  64.777  1.00 303.14 ? 210  GLU Y CB  1 
ATOM   24558 C  CG  . GLU D 2 82   ? 98.165  74.510  65.904  1.00 311.07 ? 210  GLU Y CG  1 
ATOM   24559 C  CD  . GLU D 2 82   ? 96.764  74.948  65.511  1.00 314.69 ? 210  GLU Y CD  1 
ATOM   24560 O  OE1 . GLU D 2 82   ? 96.482  75.035  64.298  1.00 313.21 ? 210  GLU Y OE1 1 
ATOM   24561 O  OE2 . GLU D 2 82   ? 95.947  75.210  66.419  1.00 318.85 ? 210  GLU Y OE2 1 
ATOM   24562 N  N   . ARG D 2 83   ? 96.403  72.056  65.780  1.00 296.98 ? 211  ARG Y N   1 
ATOM   24563 C  CA  . ARG D 2 83   ? 95.555  71.629  66.883  1.00 294.23 ? 211  ARG Y CA  1 
ATOM   24564 C  C   . ARG D 2 83   ? 95.274  70.128  66.818  1.00 293.29 ? 211  ARG Y C   1 
ATOM   24565 O  O   . ARG D 2 83   ? 94.847  69.532  67.805  1.00 293.72 ? 211  ARG Y O   1 
ATOM   24566 C  CB  . ARG D 2 83   ? 94.243  72.420  66.882  1.00 289.54 ? 211  ARG Y CB  1 
ATOM   24567 C  CG  . ARG D 2 83   ? 93.525  72.430  65.533  1.00 289.19 ? 211  ARG Y CG  1 
ATOM   24568 C  CD  . ARG D 2 83   ? 92.224  73.209  65.592  1.00 286.09 ? 211  ARG Y CD  1 
ATOM   24569 N  NE  . ARG D 2 83   ? 92.431  74.564  66.089  1.00 276.71 ? 211  ARG Y NE  1 
ATOM   24570 C  CZ  . ARG D 2 83   ? 92.749  75.596  65.320  1.00 274.51 ? 211  ARG Y CZ  1 
ATOM   24571 N  NH1 . ARG D 2 83   ? 92.896  75.424  64.017  1.00 279.78 ? 211  ARG Y NH1 1 
ATOM   24572 N  NH2 . ARG D 2 83   ? 92.921  76.797  65.855  1.00 268.45 ? 211  ARG Y NH2 1 
ATOM   24573 N  N   . MET D 2 84   ? 95.518  69.527  65.651  1.00 358.95 ? 212  MET Y N   1 
ATOM   24574 C  CA  . MET D 2 84   ? 95.306  68.089  65.447  1.00 357.67 ? 212  MET Y CA  1 
ATOM   24575 C  C   . MET D 2 84   ? 96.145  67.242  66.413  1.00 357.28 ? 212  MET Y C   1 
ATOM   24576 O  O   . MET D 2 84   ? 96.022  66.017  66.441  1.00 359.25 ? 212  MET Y O   1 
ATOM   24577 C  CB  . MET D 2 84   ? 95.579  67.677  63.985  1.00 354.16 ? 212  MET Y CB  1 
ATOM   24578 C  CG  . MET D 2 84   ? 94.407  67.874  63.003  1.00 352.61 ? 212  MET Y CG  1 
ATOM   24579 S  SD  . MET D 2 84   ? 94.773  67.284  61.328  1.00 327.69 ? 212  MET Y SD  1 
ATOM   24580 C  CE  . MET D 2 84   ? 93.283  67.729  60.428  1.00 229.26 ? 212  MET Y CE  1 
ATOM   24581 N  N   . GLY D 2 85   ? 97.003  67.901  67.190  1.00 307.19 ? 213  GLY Y N   1 
ATOM   24582 C  CA  . GLY D 2 85   ? 97.761  67.239  68.240  1.00 307.43 ? 213  GLY Y CA  1 
ATOM   24583 C  C   . GLY D 2 85   ? 96.977  67.185  69.540  1.00 310.00 ? 213  GLY Y C   1 
ATOM   24584 O  O   . GLY D 2 85   ? 97.176  66.294  70.373  1.00 311.46 ? 213  GLY Y O   1 
ATOM   24585 N  N   . ASP D 2 86   ? 96.080  68.154  69.705  1.00 362.22 ? 214  ASP Y N   1 
ATOM   24586 C  CA  . ASP D 2 86   ? 95.193  68.231  70.861  1.00 363.04 ? 214  ASP Y CA  1 
ATOM   24587 C  C   . ASP D 2 86   ? 94.558  66.862  71.117  1.00 365.46 ? 214  ASP Y C   1 
ATOM   24588 O  O   . ASP D 2 86   ? 94.289  66.111  70.181  1.00 365.75 ? 214  ASP Y O   1 
ATOM   24589 C  CB  . ASP D 2 86   ? 94.109  69.289  70.601  1.00 356.92 ? 214  ASP Y CB  1 
ATOM   24590 C  CG  . ASP D 2 86   ? 93.736  70.078  71.846  1.00 353.39 ? 214  ASP Y CG  1 
ATOM   24591 O  OD1 . ASP D 2 86   ? 93.587  69.466  72.924  1.00 352.93 ? 214  ASP Y OD1 1 
ATOM   24592 O  OD2 . ASP D 2 86   ? 93.578  71.314  71.741  1.00 351.27 ? 214  ASP Y OD2 1 
ATOM   24593 N  N   . VAL D 2 87   ? 94.330  66.533  72.384  1.00 364.13 ? 215  VAL Y N   1 
ATOM   24594 C  CA  . VAL D 2 87   ? 93.709  65.260  72.739  1.00 360.08 ? 215  VAL Y CA  1 
ATOM   24595 C  C   . VAL D 2 87   ? 92.535  65.492  73.693  1.00 356.98 ? 215  VAL Y C   1 
ATOM   24596 O  O   . VAL D 2 87   ? 92.542  66.450  74.466  1.00 356.22 ? 215  VAL Y O   1 
ATOM   24597 C  CB  . VAL D 2 87   ? 94.732  64.292  73.368  1.00 397.47 ? 215  VAL Y CB  1 
ATOM   24598 C  CG1 . VAL D 2 87   ? 95.725  63.815  72.319  1.00 397.13 ? 215  VAL Y CG1 1 
ATOM   24599 C  CG2 . VAL D 2 87   ? 95.456  64.964  74.521  1.00 398.87 ? 215  VAL Y CG2 1 
ATOM   24600 N  N   . LEU D 2 88   ? 91.526  64.624  73.633  1.00 376.68 ? 216  LEU Y N   1 
ATOM   24601 C  CA  . LEU D 2 88   ? 90.302  64.822  74.415  1.00 372.86 ? 216  LEU Y CA  1 
ATOM   24602 C  C   . LEU D 2 88   ? 89.937  63.634  75.310  1.00 369.21 ? 216  LEU Y C   1 
ATOM   24603 O  O   . LEU D 2 88   ? 90.320  62.496  75.036  1.00 367.64 ? 216  LEU Y O   1 
ATOM   24604 C  CB  . LEU D 2 88   ? 89.119  65.159  73.501  1.00 369.88 ? 216  LEU Y CB  1 
ATOM   24605 C  CG  . LEU D 2 88   ? 89.158  66.471  72.712  1.00 366.75 ? 216  LEU Y CG  1 
ATOM   24606 C  CD1 . LEU D 2 88   ? 89.547  67.633  73.615  1.00 366.83 ? 216  LEU Y CD1 1 
ATOM   24607 C  CD2 . LEU D 2 88   ? 90.102  66.370  71.525  1.00 363.20 ? 216  LEU Y CD2 1 
ATOM   24608 N  N   . ASN D 2 89   ? 89.184  63.914  76.372  1.00 384.83 ? 217  ASN Y N   1 
ATOM   24609 C  CA  . ASN D 2 89   ? 88.794  62.900  77.352  1.00 383.50 ? 217  ASN Y CA  1 
ATOM   24610 C  C   . ASN D 2 89   ? 87.439  62.276  77.028  1.00 382.57 ? 217  ASN Y C   1 
ATOM   24611 O  O   . ASN D 2 89   ? 86.469  62.989  76.767  1.00 381.12 ? 217  ASN Y O   1 
ATOM   24612 C  CB  . ASN D 2 89   ? 88.765  63.503  78.758  1.00 384.94 ? 217  ASN Y CB  1 
ATOM   24613 C  CG  . ASN D 2 89   ? 89.925  64.451  79.011  1.00 387.59 ? 217  ASN Y CG  1 
ATOM   24614 O  OD1 . ASN D 2 89   ? 90.893  64.481  78.253  1.00 388.65 ? 217  ASN Y OD1 1 
ATOM   24615 N  ND2 . ASN D 2 89   ? 89.831  65.232  80.081  1.00 388.69 ? 217  ASN Y ND2 1 
ATOM   24616 N  N   . SER D 2 90   ? 87.372  60.947  77.069  1.00 282.22 ? 218  SER Y N   1 
ATOM   24617 C  CA  . SER D 2 90   ? 86.207  60.223  76.561  1.00 284.72 ? 218  SER Y CA  1 
ATOM   24618 C  C   . SER D 2 90   ? 84.900  60.507  77.277  1.00 289.40 ? 218  SER Y C   1 
ATOM   24619 O  O   . SER D 2 90   ? 83.912  60.885  76.654  1.00 288.27 ? 218  SER Y O   1 
ATOM   24620 C  CB  . SER D 2 90   ? 86.458  58.720  76.557  1.00 281.99 ? 218  SER Y CB  1 
ATOM   24621 O  OG  . SER D 2 90   ? 87.152  58.356  75.384  1.00 280.25 ? 218  SER Y OG  1 
ATOM   24622 N  N   . LYS D 2 91   ? 84.890  60.311  78.585  1.00 204.27 ? 219  LYS Y N   1 
ATOM   24623 C  CA  . LYS D 2 91   ? 83.647  60.398  79.337  1.00 211.69 ? 219  LYS Y CA  1 
ATOM   24624 C  C   . LYS D 2 91   ? 83.327  61.840  79.753  1.00 205.86 ? 219  LYS Y C   1 
ATOM   24625 O  O   . LYS D 2 91   ? 82.305  62.117  80.389  1.00 208.48 ? 219  LYS Y O   1 
ATOM   24626 C  CB  . LYS D 2 91   ? 83.694  59.437  80.524  1.00 227.92 ? 219  LYS Y CB  1 
ATOM   24627 C  CG  . LYS D 2 91   ? 84.108  58.018  80.116  1.00 249.35 ? 219  LYS Y CG  1 
ATOM   24628 C  CD  . LYS D 2 91   ? 85.589  57.959  79.793  1.00 251.46 ? 219  LYS Y CD  1 
ATOM   24629 C  CE  . LYS D 2 91   ? 85.989  56.629  79.213  1.00 259.27 ? 219  LYS Y CE  1 
ATOM   24630 N  NZ  . LYS D 2 91   ? 87.462  56.579  79.080  1.00 262.94 ? 219  LYS Y NZ  1 
ATOM   24631 N  N   . ASP D 2 92   ? 84.208  62.753  79.359  1.00 277.33 ? 220  ASP Y N   1 
ATOM   24632 C  CA  . ASP D 2 92   ? 84.039  64.172  79.630  1.00 272.15 ? 220  ASP Y CA  1 
ATOM   24633 C  C   . ASP D 2 92   ? 82.918  64.787  78.803  1.00 267.99 ? 220  ASP Y C   1 
ATOM   24634 O  O   . ASP D 2 92   ? 81.935  65.305  79.339  1.00 269.65 ? 220  ASP Y O   1 
ATOM   24635 C  CB  . ASP D 2 92   ? 85.346  64.907  79.337  1.00 271.26 ? 220  ASP Y CB  1 
ATOM   24636 C  CG  . ASP D 2 92   ? 86.366  64.742  80.445  1.00 272.42 ? 220  ASP Y CG  1 
ATOM   24637 O  OD1 . ASP D 2 92   ? 86.141  63.910  81.348  1.00 273.53 ? 220  ASP Y OD1 1 
ATOM   24638 O  OD2 . ASP D 2 92   ? 87.390  65.453  80.419  1.00 272.72 ? 220  ASP Y OD2 1 
ATOM   24639 N  N   . ILE D 2 93   ? 83.088  64.723  77.489  1.00 397.33 ? 221  ILE Y N   1 
ATOM   24640 C  CA  . ILE D 2 93   ? 82.164  65.332  76.546  1.00 391.70 ? 221  ILE Y CA  1 
ATOM   24641 C  C   . ILE D 2 93   ? 80.716  65.177  77.005  1.00 386.37 ? 221  ILE Y C   1 
ATOM   24642 O  O   . ILE D 2 93   ? 80.345  64.152  77.575  1.00 387.34 ? 221  ILE Y O   1 
ATOM   24643 C  CB  . ILE D 2 93   ? 82.341  64.712  75.145  1.00 350.17 ? 221  ILE Y CB  1 
ATOM   24644 C  CG1 . ILE D 2 93   ? 83.821  64.712  74.742  1.00 347.00 ? 221  ILE Y CG1 1 
ATOM   24645 C  CG2 . ILE D 2 93   ? 81.495  65.444  74.116  1.00 352.99 ? 221  ILE Y CG2 1 
ATOM   24646 C  CD1 . ILE D 2 93   ? 84.080  64.197  73.339  1.00 343.77 ? 221  ILE Y CD1 1 
ATOM   24647 N  N   . ASN D 2 94   ? 79.902  66.202  76.771  1.00 354.21 ? 222  ASN Y N   1 
ATOM   24648 C  CA  . ASN D 2 94   ? 78.494  66.149  77.157  1.00 351.28 ? 222  ASN Y CA  1 
ATOM   24649 C  C   . ASN D 2 94   ? 77.537  65.887  75.991  1.00 349.71 ? 222  ASN Y C   1 
ATOM   24650 O  O   . ASN D 2 94   ? 76.755  64.941  76.034  1.00 346.27 ? 222  ASN Y O   1 
ATOM   24651 C  CB  . ASN D 2 94   ? 78.084  67.425  77.892  1.00 176.92 ? 222  ASN Y CB  1 
ATOM   24652 C  CG  . ASN D 2 94   ? 76.704  67.320  78.512  1.00 176.90 ? 222  ASN Y CG  1 
ATOM   24653 O  OD1 . ASN D 2 94   ? 75.695  67.639  77.878  1.00 176.57 ? 222  ASN Y OD1 1 
ATOM   24654 N  ND2 . ASN D 2 94   ? 76.653  66.866  79.761  1.00 177.33 ? 222  ASN Y ND2 1 
ATOM   24655 N  N   . LYS D 2 95   ? 77.605  66.721  74.954  1.00 396.44 ? 223  LYS Y N   1 
ATOM   24656 C  CA  . LYS D 2 95   ? 76.702  66.620  73.803  1.00 393.89 ? 223  LYS Y CA  1 
ATOM   24657 C  C   . LYS D 2 95   ? 77.298  67.307  72.574  1.00 386.69 ? 223  LYS Y C   1 
ATOM   24658 O  O   . LYS D 2 95   ? 77.550  68.505  72.598  1.00 387.46 ? 223  LYS Y O   1 
ATOM   24659 C  CB  . LYS D 2 95   ? 75.347  67.270  74.126  1.00 228.68 ? 223  LYS Y CB  1 
ATOM   24660 C  CG  . LYS D 2 95   ? 74.513  66.539  75.168  1.00 227.07 ? 223  LYS Y CG  1 
ATOM   24661 C  CD  . LYS D 2 95   ? 73.342  67.382  75.659  1.00 226.32 ? 223  LYS Y CD  1 
ATOM   24662 C  CE  . LYS D 2 95   ? 72.486  66.609  76.664  1.00 225.86 ? 223  LYS Y CE  1 
ATOM   24663 N  NZ  . LYS D 2 95   ? 73.265  66.049  77.807  1.00 224.97 ? 223  LYS Y NZ  1 
ATOM   24664 N  N   . ILE D 2 96   ? 77.518  66.561  71.498  1.00 278.74 ? 224  ILE Y N   1 
ATOM   24665 C  CA  . ILE D 2 96   ? 77.982  67.175  70.259  1.00 279.79 ? 224  ILE Y CA  1 
ATOM   24666 C  C   . ILE D 2 96   ? 76.794  67.838  69.558  1.00 285.54 ? 224  ILE Y C   1 
ATOM   24667 O  O   . ILE D 2 96   ? 75.653  67.435  69.773  1.00 287.38 ? 224  ILE Y O   1 
ATOM   24668 C  CB  . ILE D 2 96   ? 78.648  66.144  69.329  1.00 260.46 ? 224  ILE Y CB  1 
ATOM   24669 C  CG1 . ILE D 2 96   ? 79.750  65.385  70.065  1.00 259.13 ? 224  ILE Y CG1 1 
ATOM   24670 C  CG2 . ILE D 2 96   ? 79.227  66.822  68.100  1.00 257.56 ? 224  ILE Y CG2 1 
ATOM   24671 C  CD1 . ILE D 2 96   ? 80.442  64.359  69.201  1.00 254.98 ? 224  ILE Y CD1 1 
ATOM   24672 N  N   . GLU D 2 97   ? 77.059  68.850  68.730  1.00 453.68 ? 225  GLU Y N   1 
ATOM   24673 C  CA  . GLU D 2 97   ? 75.994  69.608  68.062  1.00 458.50 ? 225  GLU Y CA  1 
ATOM   24674 C  C   . GLU D 2 97   ? 76.465  70.324  66.790  1.00 460.27 ? 225  GLU Y C   1 
ATOM   24675 O  O   . GLU D 2 97   ? 77.339  71.190  66.843  1.00 460.88 ? 225  GLU Y O   1 
ATOM   24676 C  CB  . GLU D 2 97   ? 75.388  70.626  69.034  1.00 291.51 ? 225  GLU Y CB  1 
ATOM   24677 C  CG  . GLU D 2 97   ? 74.589  69.998  70.171  1.00 293.78 ? 225  GLU Y CG  1 
ATOM   24678 C  CD  . GLU D 2 97   ? 74.489  70.892  71.391  1.00 292.59 ? 225  GLU Y CD  1 
ATOM   24679 O  OE1 . GLU D 2 97   ? 75.021  72.023  71.345  1.00 293.05 ? 225  GLU Y OE1 1 
ATOM   24680 O  OE2 . GLU D 2 97   ? 73.881  70.458  72.397  1.00 291.26 ? 225  GLU Y OE2 1 
ATOM   24681 N  N   . VAL D 2 98   ? 75.867  69.973  65.652  1.00 336.60 ? 226  VAL Y N   1 
ATOM   24682 C  CA  . VAL D 2 98   ? 76.258  70.550  64.363  1.00 335.74 ? 226  VAL Y CA  1 
ATOM   24683 C  C   . VAL D 2 98   ? 75.162  71.439  63.767  1.00 339.46 ? 226  VAL Y C   1 
ATOM   24684 O  O   . VAL D 2 98   ? 73.987  71.301  64.109  1.00 339.64 ? 226  VAL Y O   1 
ATOM   24685 C  CB  . VAL D 2 98   ? 76.631  69.447  63.343  1.00 368.55 ? 226  VAL Y CB  1 
ATOM   24686 C  CG1 . VAL D 2 98   ? 77.243  70.055  62.090  1.00 365.78 ? 226  VAL Y CG1 1 
ATOM   24687 C  CG2 . VAL D 2 98   ? 77.598  68.456  63.964  1.00 367.69 ? 226  VAL Y CG2 1 
ATOM   24688 N  N   . THR D 2 99   ? 75.560  72.346  62.876  1.00 336.49 ? 227  THR Y N   1 
ATOM   24689 C  CA  . THR D 2 99   ? 74.630  73.234  62.178  1.00 340.60 ? 227  THR Y CA  1 
ATOM   24690 C  C   . THR D 2 99   ? 75.110  73.458  60.743  1.00 343.21 ? 227  THR Y C   1 
ATOM   24691 O  O   . THR D 2 99   ? 76.275  73.779  60.518  1.00 342.85 ? 227  THR Y O   1 
ATOM   24692 C  CB  . THR D 2 99   ? 74.505  74.592  62.892  1.00 338.92 ? 227  THR Y CB  1 
ATOM   24693 O  OG1 . THR D 2 99   ? 74.058  74.389  64.238  1.00 339.95 ? 227  THR Y OG1 1 
ATOM   24694 C  CG2 . THR D 2 99   ? 73.518  75.489  62.166  1.00 338.98 ? 227  THR Y CG2 1 
ATOM   24695 N  N   . LEU D 2 100  ? 74.212  73.305  59.775  1.00 390.25 ? 228  LEU Y N   1 
ATOM   24696 C  CA  . LEU D 2 100  ? 74.622  73.208  58.377  1.00 387.33 ? 228  LEU Y CA  1 
ATOM   24697 C  C   . LEU D 2 100  ? 74.233  74.401  57.507  1.00 385.68 ? 228  LEU Y C   1 
ATOM   24698 O  O   . LEU D 2 100  ? 73.116  74.904  57.593  1.00 387.35 ? 228  LEU Y O   1 
ATOM   24699 C  CB  . LEU D 2 100  ? 74.052  71.927  57.774  1.00 191.51 ? 228  LEU Y CB  1 
ATOM   24700 C  CG  . LEU D 2 100  ? 74.190  70.672  58.640  1.00 195.41 ? 228  LEU Y CG  1 
ATOM   24701 C  CD1 . LEU D 2 100  ? 73.878  69.422  57.831  1.00 192.77 ? 228  LEU Y CD1 1 
ATOM   24702 C  CD2 . LEU D 2 100  ? 75.580  70.570  59.249  1.00 194.72 ? 228  LEU Y CD2 1 
ATOM   24703 N  N   . LYS D 2 101  ? 75.157  74.837  56.654  1.00 436.38 ? 229  LYS Y N   1 
ATOM   24704 C  CA  . LYS D 2 101  ? 74.860  75.885  55.683  1.00 432.34 ? 229  LYS Y CA  1 
ATOM   24705 C  C   . LYS D 2 101  ? 75.142  75.472  54.246  1.00 419.37 ? 229  LYS Y C   1 
ATOM   24706 O  O   . LYS D 2 101  ? 76.297  75.289  53.860  1.00 414.88 ? 229  LYS Y O   1 
ATOM   24707 C  CB  . LYS D 2 101  ? 75.656  77.149  55.970  1.00 231.60 ? 229  LYS Y CB  1 
ATOM   24708 C  CG  . LYS D 2 101  ? 75.693  78.079  54.764  1.00 225.54 ? 229  LYS Y CG  1 
ATOM   24709 C  CD  . LYS D 2 101  ? 76.096  79.483  55.152  1.00 225.68 ? 229  LYS Y CD  1 
ATOM   24710 C  CE  . LYS D 2 101  ? 75.861  80.471  54.023  1.00 219.82 ? 229  LYS Y CE  1 
ATOM   24711 N  NZ  . LYS D 2 101  ? 76.196  81.856  54.467  1.00 219.98 ? 229  LYS Y NZ  1 
ATOM   24712 N  N   . GLN D 2 102  ? 74.082  75.349  53.454  1.00 328.54 ? 230  GLN Y N   1 
ATOM   24713 C  CA  . GLN D 2 102  ? 74.215  75.098  52.023  1.00 317.30 ? 230  GLN Y CA  1 
ATOM   24714 C  C   . GLN D 2 102  ? 74.114  76.405  51.239  1.00 312.43 ? 230  GLN Y C   1 
ATOM   24715 O  O   . GLN D 2 102  ? 73.439  76.480  50.210  1.00 307.14 ? 230  GLN Y O   1 
ATOM   24716 C  CB  . GLN D 2 102  ? 73.165  74.093  51.532  1.00 313.39 ? 230  GLN Y CB  1 
ATOM   24717 C  CG  . GLN D 2 102  ? 73.389  72.659  52.007  1.00 312.25 ? 230  GLN Y CG  1 
ATOM   24718 C  CD  . GLN D 2 102  ? 72.318  71.695  51.510  1.00 308.50 ? 230  GLN Y CD  1 
ATOM   24719 O  OE1 . GLN D 2 102  ? 71.761  71.869  50.426  1.00 304.48 ? 230  GLN Y OE1 1 
ATOM   24720 N  NE2 . GLN D 2 102  ? 72.033  70.669  52.303  1.00 310.71 ? 230  GLN Y NE2 1 
HETATM 24721 CD CD  . CD  E 3 .    ? 41.271  12.146  42.548  0.50 229.55 ? 1677 CD  A CD  1 
HETATM 24722 CD CD  . CD  F 3 .    ? -4.766  16.554  37.988  1.00 481.40 ? 1678 CD  A CD  1 
HETATM 24723 CD CD  . CD  G 3 .    ? 56.145  2.725   22.351  1.00 402.32 ? 1679 CD  A CD  1 
HETATM 24724 C  C1  . NAG H 4 .    ? 30.914  -37.537 26.969  1.00 293.12 ? 2001 NAG A C1  1 
HETATM 24725 C  C2  . NAG H 4 .    ? 29.468  -37.455 27.473  1.00 293.12 ? 2001 NAG A C2  1 
HETATM 24726 C  C3  . NAG H 4 .    ? 28.724  -38.787 27.464  1.00 293.12 ? 2001 NAG A C3  1 
HETATM 24727 C  C4  . NAG H 4 .    ? 29.022  -39.623 26.230  1.00 293.12 ? 2001 NAG A C4  1 
HETATM 24728 C  C5  . NAG H 4 .    ? 30.539  -39.723 26.055  1.00 293.12 ? 2001 NAG A C5  1 
HETATM 24729 C  C6  . NAG H 4 .    ? 30.947  -40.539 24.834  1.00 293.12 ? 2001 NAG A C6  1 
HETATM 24730 C  C7  . NAG H 4 .    ? 28.374  -36.323 29.369  1.00 293.12 ? 2001 NAG A C7  1 
HETATM 24731 C  C8  . NAG H 4 .    ? 27.990  -36.721 30.767  1.00 293.12 ? 2001 NAG A C8  1 
HETATM 24732 N  N2  . NAG H 4 .    ? 29.440  -36.927 28.832  1.00 293.12 ? 2001 NAG A N2  1 
HETATM 24733 O  O3  . NAG H 4 .    ? 27.338  -38.531 27.546  1.00 293.12 ? 2001 NAG A O3  1 
HETATM 24734 O  O4  . NAG H 4 .    ? 28.416  -40.896 26.393  1.00 293.12 ? 2001 NAG A O4  1 
HETATM 24735 O  O5  . NAG H 4 .    ? 31.097  -38.436 25.894  1.00 293.12 ? 2001 NAG A O5  1 
HETATM 24736 O  O6  . NAG H 4 .    ? 30.917  -39.717 23.687  1.00 293.12 ? 2001 NAG A O6  1 
HETATM 24737 O  O7  . NAG H 4 .    ? 27.718  -35.469 28.774  1.00 293.12 ? 2001 NAG A O7  1 
HETATM 24738 C  C1  . NAG I 4 .    ? 27.069  -40.958 26.133  1.00 343.98 ? 2002 NAG A C1  1 
HETATM 24739 C  C2  . NAG I 4 .    ? 26.775  -42.237 25.343  1.00 343.98 ? 2002 NAG A C2  1 
HETATM 24740 C  C3  . NAG I 4 .    ? 25.374  -42.232 24.726  1.00 343.98 ? 2002 NAG A C3  1 
HETATM 24741 C  C4  . NAG I 4 .    ? 24.320  -41.822 25.741  1.00 343.98 ? 2002 NAG A C4  1 
HETATM 24742 C  C5  . NAG I 4 .    ? 24.716  -40.503 26.379  1.00 343.98 ? 2002 NAG A C5  1 
HETATM 24743 C  C6  . NAG I 4 .    ? 23.664  -40.108 27.408  1.00 343.98 ? 2002 NAG A C6  1 
HETATM 24744 C  C7  . NAG I 4 .    ? 28.651  -43.438 24.288  1.00 343.98 ? 2002 NAG A C7  1 
HETATM 24745 C  C8  . NAG I 4 .    ? 28.849  -44.139 22.973  1.00 343.98 ? 2002 NAG A C8  1 
HETATM 24746 N  N2  . NAG I 4 .    ? 27.777  -42.426 24.302  1.00 343.98 ? 2002 NAG A N2  1 
HETATM 24747 O  O3  . NAG I 4 .    ? 25.056  -43.515 24.240  1.00 343.98 ? 2002 NAG A O3  1 
HETATM 24748 O  O4  . NAG I 4 .    ? 23.059  -41.689 25.123  1.00 343.98 ? 2002 NAG A O4  1 
HETATM 24749 O  O5  . NAG I 4 .    ? 25.986  -40.625 26.992  1.00 343.98 ? 2002 NAG A O5  1 
HETATM 24750 O  O6  . NAG I 4 .    ? 23.280  -41.249 28.142  1.00 343.98 ? 2002 NAG A O6  1 
HETATM 24751 O  O7  . NAG I 4 .    ? 29.284  -43.799 25.281  1.00 343.98 ? 2002 NAG A O7  1 
HETATM 24752 C  C1  . NAG J 4 .    ? 68.315  14.014  20.244  1.00 301.45 ? 1680 NAG A C1  1 
HETATM 24753 C  C2  . NAG J 4 .    ? 68.609  13.892  21.757  1.00 301.45 ? 1680 NAG A C2  1 
HETATM 24754 C  C3  . NAG J 4 .    ? 69.027  15.192  22.447  1.00 301.45 ? 1680 NAG A C3  1 
HETATM 24755 C  C4  . NAG J 4 .    ? 69.924  16.040  21.552  1.00 301.45 ? 1680 NAG A C4  1 
HETATM 24756 C  C5  . NAG J 4 .    ? 69.236  16.209  20.210  1.00 301.45 ? 1680 NAG A C5  1 
HETATM 24757 C  C6  . NAG J 4 .    ? 69.953  17.234  19.334  1.00 301.45 ? 1680 NAG A C6  1 
HETATM 24758 C  C7  . NAG J 4 .    ? 67.577  12.814  23.690  1.00 301.45 ? 1680 NAG A C7  1 
HETATM 24759 C  C8  . NAG J 4 .    ? 66.555  13.237  24.699  1.00 301.45 ? 1680 NAG A C8  1 
HETATM 24760 N  N2  . NAG J 4 .    ? 67.465  13.350  22.478  1.00 301.45 ? 1680 NAG A N2  1 
HETATM 24761 O  O3  . NAG J 4 .    ? 69.688  14.867  23.654  1.00 301.45 ? 1680 NAG A O3  1 
HETATM 24762 O  O4  . NAG J 4 .    ? 70.148  17.318  22.104  1.00 301.45 ? 1680 NAG A O4  1 
HETATM 24763 O  O5  . NAG J 4 .    ? 69.162  14.946  19.583  1.00 301.45 ? 1680 NAG A O5  1 
HETATM 24764 O  O6  . NAG J 4 .    ? 71.258  16.796  19.030  1.00 301.45 ? 1680 NAG A O6  1 
HETATM 24765 O  O7  . NAG J 4 .    ? 68.457  12.015  23.994  1.00 301.45 ? 1680 NAG A O7  1 
HETATM 24766 CD CD  . CD  K 3 .    ? 60.575  54.412  46.322  1.00 466.47 ? 1677 CD  B CD  1 
HETATM 24767 CD CD  . CD  L 3 .    ? 41.709  -5.803  62.130  1.00 397.01 ? 1678 CD  B CD  1 
HETATM 24768 C  C1  . NAG M 4 .    ? 89.431  -3.775  57.798  1.00 280.61 ? 2001 NAG B C1  1 
HETATM 24769 C  C2  . NAG M 4 .    ? 90.084  -2.428  57.452  1.00 280.61 ? 2001 NAG B C2  1 
HETATM 24770 C  C3  . NAG M 4 .    ? 91.610  -2.449  57.375  1.00 280.61 ? 2001 NAG B C3  1 
HETATM 24771 C  C4  . NAG M 4 .    ? 92.232  -3.364  58.416  1.00 280.61 ? 2001 NAG B C4  1 
HETATM 24772 C  C5  . NAG M 4 .    ? 91.552  -4.721  58.287  1.00 280.61 ? 2001 NAG B C5  1 
HETATM 24773 C  C6  . NAG M 4 .    ? 92.188  -5.793  59.159  1.00 280.61 ? 2001 NAG B C6  1 
HETATM 24774 C  C7  . NAG M 4 .    ? 89.603  -0.657  55.809  1.00 280.61 ? 2001 NAG B C7  1 
HETATM 24775 C  C8  . NAG M 4 .    ? 89.887  -0.369  54.362  1.00 280.61 ? 2001 NAG B C8  1 
HETATM 24776 N  N2  . NAG M 4 .    ? 89.566  -1.941  56.180  1.00 280.61 ? 2001 NAG B N2  1 
HETATM 24777 O  O3  . NAG M 4 .    ? 92.095  -1.135  57.542  1.00 280.61 ? 2001 NAG B O3  1 
HETATM 24778 O  O4  . NAG M 4 .    ? 93.630  -3.443  58.202  1.00 280.61 ? 2001 NAG B O4  1 
HETATM 24779 O  O5  . NAG M 4 .    ? 90.201  -4.581  58.669  1.00 280.61 ? 2001 NAG B O5  1 
HETATM 24780 O  O6  . NAG M 4 .    ? 91.365  -5.998  60.286  1.00 280.61 ? 2001 NAG B O6  1 
HETATM 24781 O  O7  . NAG M 4 .    ? 89.418  0.273   56.591  1.00 280.61 ? 2001 NAG B O7  1 
HETATM 24782 C  C1  . NAG N 4 .    ? 94.329  -2.343  58.630  1.00 363.72 ? 2002 NAG B C1  1 
HETATM 24783 C  C2  . NAG N 4 .    ? 95.426  -2.616  59.659  1.00 363.72 ? 2002 NAG B C2  1 
HETATM 24784 C  C3  . NAG N 4 .    ? 95.835  -1.349  60.409  1.00 363.72 ? 2002 NAG B C3  1 
HETATM 24785 C  C4  . NAG N 4 .    ? 96.134  -0.222  59.436  1.00 363.72 ? 2002 NAG B C4  1 
HETATM 24786 C  C5  . NAG N 4 .    ? 94.943  -0.025  58.518  1.00 363.72 ? 2002 NAG B C5  1 
HETATM 24787 C  C6  . NAG N 4 .    ? 95.241  1.105   57.542  1.00 363.72 ? 2002 NAG B C6  1 
HETATM 24788 C  C7  . NAG N 4 .    ? 95.523  -4.875  60.591  1.00 363.72 ? 2002 NAG B C7  1 
HETATM 24789 C  C8  . NAG N 4 .    ? 96.277  -5.283  61.825  1.00 363.72 ? 2002 NAG B C8  1 
HETATM 24790 N  N2  . NAG N 4 .    ? 94.996  -3.649  60.589  1.00 363.72 ? 2002 NAG B N2  1 
HETATM 24791 O  O3  . NAG N 4 .    ? 96.986  -1.600  61.179  1.00 363.72 ? 2002 NAG B O3  1 
HETATM 24792 O  O4  . NAG N 4 .    ? 96.402  0.982   60.119  1.00 363.72 ? 2002 NAG B O4  1 
HETATM 24793 O  O5  . NAG N 4 .    ? 94.664  -1.225  57.822  1.00 363.72 ? 2002 NAG B O5  1 
HETATM 24794 O  O6  . NAG N 4 .    ? 96.576  0.996   57.100  1.00 363.72 ? 2002 NAG B O6  1 
HETATM 24795 O  O7  . NAG N 4 .    ? 95.411  -5.658  59.646  1.00 363.72 ? 2002 NAG B O7  1 
HETATM 24796 C  C1  . NAG O 4 .    ? 26.133  -10.207 64.407  1.00 290.85 ? 1679 NAG B C1  1 
HETATM 24797 C  C2  . NAG O 4 .    ? 26.089  -10.527 62.893  1.00 290.85 ? 1679 NAG B C2  1 
HETATM 24798 C  C3  . NAG O 4 .    ? 24.758  -10.242 62.191  1.00 290.85 ? 1679 NAG B C3  1 
HETATM 24799 C  C4  . NAG O 4 .    ? 23.585  -10.567 63.108  1.00 290.85 ? 1679 NAG B C4  1 
HETATM 24800 C  C5  . NAG O 4 .    ? 23.786  -9.792  64.394  1.00 290.85 ? 1679 NAG B C5  1 
HETATM 24801 C  C6  . NAG O 4 .    ? 22.531  -9.825  65.255  1.00 290.85 ? 1679 NAG B C6  1 
HETATM 24802 C  C7  . NAG O 4 .    ? 27.471  -10.079 60.934  1.00 290.85 ? 1679 NAG B C7  1 
HETATM 24803 C  C8  . NAG O 4 .    ? 27.743  -8.912  60.035  1.00 290.85 ? 1679 NAG B C8  1 
HETATM 24804 N  N2  . NAG O 4 .    ? 27.125  -9.792  62.185  1.00 290.85 ? 1679 NAG B N2  1 
HETATM 24805 O  O3  . NAG O 4 .    ? 24.694  -10.981 60.987  1.00 290.85 ? 1679 NAG B O3  1 
HETATM 24806 O  O4  . NAG O 4 .    ? 22.352  -10.181 62.547  1.00 290.85 ? 1679 NAG B O4  1 
HETATM 24807 O  O5  . NAG O 4 .    ? 24.885  -10.355 65.073  1.00 290.85 ? 1679 NAG B O5  1 
HETATM 24808 O  O6  . NAG O 4 .    ? 22.315  -11.140 65.706  1.00 290.85 ? 1679 NAG B O6  1 
HETATM 24809 O  O7  . NAG O 4 .    ? 27.574  -11.230 60.516  1.00 290.85 ? 1679 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   ? 2.1475 3.9488 2.5292 0.8430  -0.1464 0.0432  22   THR A N   
2     C CA  . THR A 22   ? 2.1224 3.9108 2.4855 0.8608  -0.1570 0.0739  22   THR A CA  
3     C C   . THR A 22   ? 2.1279 3.8908 2.4264 0.8527  -0.1532 0.0833  22   THR A C   
4     O O   . THR A 22   ? 2.1490 3.9016 2.4147 0.8335  -0.1431 0.0681  22   THR A O   
5     C CB  . THR A 22   ? 2.0757 3.8611 2.4594 0.8752  -0.1658 0.0917  22   THR A CB  
6     O OG1 . THR A 22   ? 2.0447 3.8299 2.4332 0.8628  -0.1593 0.0769  22   THR A OG1 
7     C CG2 . THR A 22   ? 2.0339 3.8390 2.4746 0.8927  -0.1746 0.0972  22   THR A CG2 
8     N N   . TYR A 23   ? 1.7721 3.5246 2.0532 0.8670  -0.1611 0.1083  23   TYR A N   
9     C CA  . TYR A 23   ? 1.8666 3.5967 2.0918 0.8619  -0.1578 0.1182  23   TYR A CA  
10    C C   . TYR A 23   ? 1.8603 3.5674 2.0550 0.8698  -0.1638 0.1417  23   TYR A C   
11    O O   . TYR A 23   ? 1.7998 3.5097 2.0174 0.8854  -0.1734 0.1579  23   TYR A O   
12    C CB  . TYR A 23   ? 1.9551 3.6926 2.1802 0.8687  -0.1595 0.1243  23   TYR A CB  
13    C CG  . TYR A 23   ? 2.0035 3.7547 2.2663 0.8894  -0.1720 0.1424  23   TYR A CG  
14    C CD1 . TYR A 23   ? 1.9813 3.7335 2.2708 0.9017  -0.1805 0.1543  23   TYR A CD1 
15    C CD2 . TYR A 23   ? 2.0613 3.8243 2.3314 0.8958  -0.1748 0.1475  23   TYR A CD2 
16    C CE1 . TYR A 23   ? 1.9804 3.7428 2.3011 0.9192  -0.1914 0.1709  23   TYR A CE1 
17    C CE2 . TYR A 23   ? 2.0451 3.8195 2.3465 0.9132  -0.1865 0.1646  23   TYR A CE2 
18    C CZ  . TYR A 23   ? 2.0162 3.7892 2.3421 0.9247  -0.1946 0.1764  23   TYR A CZ  
19    O OH  . TYR A 23   ? 1.9975 3.7802 2.3523 0.9410  -0.2059 0.1936  23   TYR A OH  
20    N N   . VAL A 24   ? 1.9094 3.5934 2.0524 0.8587  -0.1580 0.1430  24   VAL A N   
21    C CA  . VAL A 24   ? 1.8837 3.5446 1.9943 0.8652  -0.1633 0.1641  24   VAL A CA  
22    C C   . VAL A 24   ? 1.8977 3.5390 1.9644 0.8643  -0.1604 0.1749  24   VAL A C   
23    O O   . VAL A 24   ? 1.9357 3.5715 1.9768 0.8502  -0.1506 0.1620  24   VAL A O   
24    C CB  . VAL A 24   ? 1.9267 3.5746 2.0141 0.8527  -0.1601 0.1576  24   VAL A CB  
25    C CG1 . VAL A 24   ? 1.9737 3.5921 2.0070 0.8512  -0.1605 0.1730  24   VAL A CG1 
26    C CG2 . VAL A 24   ? 1.8673 3.5262 1.9897 0.8614  -0.1673 0.1613  24   VAL A CG2 
27    N N   . ILE A 25   ? 2.0242 3.6548 2.0830 0.8790  -0.1685 0.1981  25   ILE A N   
28    C CA  . ILE A 25   ? 2.1160 3.7289 2.1389 0.8809  -0.1665 0.2108  25   ILE A CA  
29    C C   . ILE A 25   ? 2.0973 3.6920 2.1042 0.8912  -0.1744 0.2312  25   ILE A C   
30    O O   . ILE A 25   ? 2.0634 3.6651 2.0945 0.9066  -0.1834 0.2456  25   ILE A O   
31    C CB  . ILE A 25   ? 2.1664 3.7953 2.2124 0.8913  -0.1693 0.2174  25   ILE A CB  
32    C CG1 . ILE A 25   ? 2.2132 3.8659 2.2858 0.8835  -0.1640 0.1967  25   ILE A CG1 
33    C CG2 . ILE A 25   ? 2.2258 3.8374 2.2351 0.8916  -0.1656 0.2290  25   ILE A CG2 
34    C CD1 . ILE A 25   ? 2.2976 3.9427 2.3372 0.8657  -0.1510 0.1799  25   ILE A CD1 
35    N N   . SER A 26   ? 1.7267 3.2983 1.6931 0.8825  -0.1712 0.2321  26   SER A N   
36    C CA  . SER A 26   ? 1.6972 3.2526 1.6496 0.8927  -0.1794 0.2507  26   SER A CA  
37    C C   . SER A 26   ? 1.7467 3.2843 1.6732 0.8998  -0.1795 0.2671  26   SER A C   
38    O O   . SER A 26   ? 1.7770 3.3092 1.6843 0.8926  -0.1710 0.2625  26   SER A O   
39    C CB  . SER A 26   ? 1.7715 3.3110 1.6947 0.8813  -0.1780 0.2458  26   SER A CB  
40    O OG  . SER A 26   ? 1.7709 3.3273 1.7148 0.8700  -0.1743 0.2262  26   SER A OG  
41    N N   . ALA A 27   ? 2.0434 3.5732 1.9710 0.9136  -0.1884 0.2851  27   ALA A N   
42    C CA  . ALA A 27   ? 2.0364 3.5474 1.9396 0.9204  -0.1887 0.3008  27   ALA A CA  
43    C C   . ALA A 27   ? 1.9500 3.4523 1.8549 0.9333  -0.1992 0.3168  27   ALA A C   
44    O O   . ALA A 27   ? 1.8823 3.3983 1.8144 0.9390  -0.2061 0.3164  27   ALA A O   
45    C CB  . ALA A 27   ? 2.0205 3.5447 1.9425 0.9265  -0.1873 0.3045  27   ALA A CB  
46    N N   . PRO A 28   ? 1.8951 3.3754 1.7725 0.9381  -0.1998 0.3301  28   PRO A N   
47    C CA  . PRO A 28   ? 1.8969 3.3671 1.7721 0.9493  -0.2096 0.3437  28   PRO A CA  
48    C C   . PRO A 28   ? 1.8996 3.3911 1.8166 0.9622  -0.2178 0.3487  28   PRO A C   
49    O O   . PRO A 28   ? 1.8915 3.4028 1.8365 0.9626  -0.2162 0.3432  28   PRO A O   
50    C CB  . PRO A 28   ? 1.8762 3.3251 1.7267 0.9541  -0.2076 0.3563  28   PRO A CB  
51    C CG  . PRO A 28   ? 1.9071 3.3482 1.7344 0.9415  -0.1954 0.3479  28   PRO A CG  
52    C CD  . PRO A 28   ? 1.9118 3.3778 1.7638 0.9343  -0.1914 0.3329  28   PRO A CD  
53    N N   . LYS A 29   ? 2.4908 3.9782 2.4122 0.9725  -0.2267 0.3587  29   LYS A N   
54    C CA  . LYS A 29   ? 2.4482 3.9526 2.4060 0.9850  -0.2336 0.3648  29   LYS A CA  
55    C C   . LYS A 29   ? 2.4626 3.9617 2.4204 0.9933  -0.2335 0.3766  29   LYS A C   
56    O O   . LYS A 29   ? 2.4013 3.9135 2.3869 1.0020  -0.2376 0.3819  29   LYS A O   
57    C CB  . LYS A 29   ? 2.4474 3.9527 2.4127 0.9918  -0.2424 0.3686  29   LYS A CB  
58    C CG  . LYS A 29   ? 2.4442 3.9581 2.4363 1.0061  -0.2495 0.3785  29   LYS A CG  
59    C CD  . LYS A 29   ? 2.9343 4.4704 2.9643 1.0088  -0.2491 0.3750  29   LYS A CD  
60    C CE  . LYS A 29   ? 2.8099 4.3494 2.8581 1.0211  -0.2542 0.3865  29   LYS A CE  
61    N NZ  . LYS A 29   ? 2.7524 4.3106 2.8344 1.0240  -0.2544 0.3858  29   LYS A NZ  
62    N N   . ILE A 30   ? 1.6366 3.1161 1.5632 0.9896  -0.2282 0.3804  30   ILE A N   
63    C CA  . ILE A 30   ? 1.6330 3.1073 1.5582 0.9951  -0.2260 0.3899  30   ILE A CA  
64    C C   . ILE A 30   ? 1.6502 3.1114 1.5469 0.9851  -0.2152 0.3865  30   ILE A C   
65    O O   . ILE A 30   ? 1.6660 3.1207 1.5426 0.9741  -0.2097 0.3771  30   ILE A O   
66    C CB  . ILE A 30   ? 1.6413 3.1001 1.5582 1.0054  -0.2321 0.4019  30   ILE A CB  
67    C CG1 . ILE A 30   ? 1.6293 3.0985 1.5687 1.0143  -0.2425 0.4039  30   ILE A CG1 
68    C CG2 . ILE A 30   ? 1.6350 3.0914 1.5556 1.0103  -0.2293 0.4100  30   ILE A CG2 
69    C CD1 . ILE A 30   ? 1.6017 3.0925 1.5775 1.0205  -0.2458 0.4047  30   ILE A CD1 
70    N N   . PHE A 31   ? 1.6478 3.1054 1.5424 0.9877  -0.2113 0.3932  31   PHE A N   
71    C CA  . PHE A 31   ? 1.6651 3.1090 1.5320 0.9785  -0.2000 0.3906  31   PHE A CA  
72    C C   . PHE A 31   ? 1.7019 3.1235 1.5509 0.9841  -0.1993 0.4014  31   PHE A C   
73    O O   . PHE A 31   ? 1.6731 3.0941 1.5357 0.9953  -0.2075 0.4104  31   PHE A O   
74    C CB  . PHE A 31   ? 1.6490 3.1116 1.5301 0.9738  -0.1934 0.3864  31   PHE A CB  
75    C CG  . PHE A 31   ? 1.6361 3.1208 1.5353 0.9677  -0.1931 0.3744  31   PHE A CG  
76    C CD1 . PHE A 31   ? 1.6103 3.1198 1.5456 0.9735  -0.1994 0.3754  31   PHE A CD1 
77    C CD2 . PHE A 31   ? 1.6572 3.1372 1.5374 0.9557  -0.1862 0.3616  31   PHE A CD2 
78    C CE1 . PHE A 31   ? 1.5993 3.1288 1.5540 0.9688  -0.1994 0.3643  31   PHE A CE1 
79    C CE2 . PHE A 31   ? 1.6393 3.1406 1.5392 0.9500  -0.1856 0.3490  31   PHE A CE2 
80    C CZ  . PHE A 31   ? 1.6130 3.1393 1.5513 0.9572  -0.1924 0.3505  31   PHE A CZ  
81    N N   . ARG A 32   ? 1.7310 3.1344 1.5504 0.9759  -0.1888 0.3996  32   ARG A N   
82    C CA  . ARG A 32   ? 1.7163 3.0987 1.5203 0.9801  -0.1856 0.4088  32   ARG A CA  
83    C C   . ARG A 32   ? 1.7214 3.1016 1.5124 0.9703  -0.1713 0.4045  32   ARG A C   
84    O O   . ARG A 32   ? 1.7233 3.1104 1.5058 0.9590  -0.1634 0.3939  32   ARG A O   
85    C CB  . ARG A 32   ? 1.7941 3.1471 1.5677 0.9810  -0.1881 0.4131  32   ARG A CB  
86    C CG  . ARG A 32   ? 1.7909 3.1394 1.5745 0.9945  -0.2024 0.4225  32   ARG A CG  
87    C CD  . ARG A 32   ? 1.8408 3.1619 1.5917 0.9935  -0.2062 0.4262  32   ARG A CD  
88    N NE  . ARG A 32   ? 1.7941 3.1139 1.5542 1.0055  -0.2206 0.4339  32   ARG A NE  
89    C CZ  . ARG A 32   ? 1.7915 3.1117 1.5444 1.0039  -0.2285 0.4321  32   ARG A CZ  
90    N NH1 . ARG A 32   ? 1.8106 3.1316 1.5474 0.9904  -0.2236 0.4223  32   ARG A NH1 
91    N NH2 . ARG A 32   ? 1.7914 3.1124 1.5540 1.0151  -0.2411 0.4391  32   ARG A NH2 
92    N N   . VAL A 33   ? 1.7235 3.0949 1.5142 0.9746  -0.1677 0.4120  33   VAL A N   
93    C CA  . VAL A 33   ? 1.7555 3.1187 1.5292 0.9656  -0.1530 0.4093  33   VAL A CA  
94    C C   . VAL A 33   ? 1.8252 3.1570 1.5599 0.9584  -0.1441 0.4075  33   VAL A C   
95    O O   . VAL A 33   ? 1.8220 3.1305 1.5425 0.9648  -0.1498 0.4147  33   VAL A O   
96    C CB  . VAL A 33   ? 1.7419 3.1033 1.5280 0.9724  -0.1521 0.4178  33   VAL A CB  
97    C CG1 . VAL A 33   ? 1.7887 3.1558 1.5701 0.9621  -0.1371 0.4132  33   VAL A CG1 
98    C CG2 . VAL A 33   ? 1.6997 3.0839 1.5208 0.9824  -0.1647 0.4224  33   VAL A CG2 
99    N N   . GLY A 34   ? 2.2733 3.6044 1.9902 0.9450  -0.1300 0.3979  34   GLY A N   
100   C CA  . GLY A 34   ? 2.3778 3.6789 2.0559 0.9361  -0.1198 0.3949  34   GLY A CA  
101   C C   . GLY A 34   ? 2.4433 3.7342 2.1061 0.9346  -0.1274 0.3927  34   GLY A C   
102   O O   . GLY A 34   ? 2.4938 3.7543 2.1256 0.9325  -0.1258 0.3961  34   GLY A O   
103   N N   . ALA A 35   ? 1.8938 3.2104 1.5789 0.9352  -0.1358 0.3869  35   ALA A N   
104   C CA  . ALA A 35   ? 1.9268 3.2395 1.6034 0.9332  -0.1436 0.3836  35   ALA A CA  
105   C C   . ALA A 35   ? 2.0023 3.3243 1.6687 0.9177  -0.1350 0.3672  35   ALA A C   
106   O O   . ALA A 35   ? 1.9678 3.3183 1.6589 0.9151  -0.1336 0.3586  35   ALA A O   
107   C CB  . ALA A 35   ? 1.8656 3.2001 1.5766 0.9450  -0.1588 0.3879  35   ALA A CB  
108   N N   . SER A 36   ? 2.7785 4.0765 2.4089 0.9072  -0.1296 0.3625  36   SER A N   
109   C CA  . SER A 36   ? 2.8261 4.1316 2.4454 0.8911  -0.1212 0.3452  36   SER A CA  
110   C C   . SER A 36   ? 2.8028 4.1327 2.4486 0.8926  -0.1319 0.3388  36   SER A C   
111   O O   . SER A 36   ? 2.8257 4.1468 2.4549 0.8849  -0.1339 0.3332  36   SER A O   
112   C CB  . SER A 36   ? 2.8679 4.1385 2.4396 0.8790  -0.1134 0.3430  36   SER A CB  
113   O OG  . SER A 36   ? 2.8686 4.1112 2.4188 0.8831  -0.1081 0.3547  36   SER A OG  
114   N N   . GLU A 37   ? 2.3955 3.7556 2.0823 0.9018  -0.1384 0.3396  37   GLU A N   
115   C CA  . GLU A 37   ? 2.3919 3.7757 2.1086 0.9047  -0.1484 0.3342  37   GLU A CA  
116   C C   . GLU A 37   ? 2.4022 3.7948 2.1131 0.8888  -0.1414 0.3149  37   GLU A C   
117   O O   . GLU A 37   ? 2.4136 3.8195 2.1283 0.8801  -0.1317 0.3027  37   GLU A O   
118   C CB  . GLU A 37   ? 2.4099 3.8235 2.1704 0.9160  -0.1548 0.3380  37   GLU A CB  
119   C CG  . GLU A 37   ? 2.4453 3.8533 2.2150 0.9306  -0.1611 0.3553  37   GLU A CG  
120   C CD  . GLU A 37   ? 2.4779 3.8752 2.2490 0.9410  -0.1733 0.3658  37   GLU A CD  
121   O OE1 . GLU A 37   ? 2.5169 3.9010 2.2679 0.9354  -0.1749 0.3624  37   GLU A OE1 
122   O OE2 . GLU A 37   ? 2.4606 3.8634 2.2524 0.9540  -0.1811 0.3770  37   GLU A OE2 
123   N N   . ASN A 38   ? 2.3757 3.7619 2.0778 0.8845  -0.1464 0.3114  38   ASN A N   
124   C CA  . ASN A 38   ? 2.3732 3.7685 2.0723 0.8688  -0.1404 0.2920  38   ASN A CA  
125   C C   . ASN A 38   ? 2.3187 3.7493 2.0655 0.8733  -0.1466 0.2837  38   ASN A C   
126   O O   . ASN A 38   ? 2.2716 3.7118 2.0439 0.8859  -0.1584 0.2930  38   ASN A O   
127   C CB  . ASN A 38   ? 2.3750 3.7476 2.0415 0.8599  -0.1422 0.2913  38   ASN A CB  
128   C CG  . ASN A 38   ? 2.3948 3.7299 2.0124 0.8548  -0.1360 0.2996  38   ASN A CG  
129   O OD1 . ASN A 38   ? 2.3925 3.7187 2.0009 0.8569  -0.1286 0.3041  38   ASN A OD1 
130   N ND2 . ASN A 38   ? 2.4171 3.7299 2.0032 0.8475  -0.1388 0.3016  38   ASN A ND2 
131   N N   . ILE A 39   ? 1.7588 3.2085 1.5183 0.8633  -0.1385 0.2661  39   ILE A N   
132   C CA  . ILE A 39   ? 1.7285 3.2115 1.5346 0.8671  -0.1434 0.2571  39   ILE A CA  
133   C C   . ILE A 39   ? 1.7330 3.2283 1.5420 0.8503  -0.1350 0.2330  39   ILE A C   
134   O O   . ILE A 39   ? 1.7357 3.2375 1.5396 0.8409  -0.1247 0.2204  39   ILE A O   
135   C CB  . ILE A 39   ? 1.7040 3.2066 1.5375 0.8769  -0.1444 0.2622  39   ILE A CB  
136   C CG1 . ILE A 39   ? 1.7020 3.1912 1.5295 0.8909  -0.1504 0.2841  39   ILE A CG1 
137   C CG2 . ILE A 39   ? 1.6742 3.2085 1.5572 0.8836  -0.1519 0.2566  39   ILE A CG2 
138   C CD1 . ILE A 39   ? 1.7485 3.2338 1.5880 0.9029  -0.1630 0.2966  39   ILE A CD1 
139   N N   . VAL A 40   ? 2.0051 3.5045 1.8230 0.8461  -0.1389 0.2258  40   VAL A N   
140   C CA  . VAL A 40   ? 2.0574 3.5674 1.8782 0.8289  -0.1310 0.2018  40   VAL A CA  
141   C C   . VAL A 40   ? 2.0393 3.5839 1.9126 0.8341  -0.1338 0.1914  40   VAL A C   
142   O O   . VAL A 40   ? 1.9595 3.5180 1.8673 0.8503  -0.1445 0.2031  40   VAL A O   
143   C CB  . VAL A 40   ? 2.1324 3.6343 1.9431 0.8206  -0.1338 0.1973  40   VAL A CB  
144   C CG1 . VAL A 40   ? 2.1905 3.6577 1.9522 0.8187  -0.1351 0.2118  40   VAL A CG1 
145   C CG2 . VAL A 40   ? 2.0510 3.5738 1.9063 0.8338  -0.1454 0.2023  40   VAL A CG2 
146   N N   . ILE A 41   ? 2.2185 3.7763 2.0976 0.8200  -0.1242 0.1688  41   ILE A N   
147   C CA  . ILE A 41   ? 2.1931 3.7836 2.1228 0.8225  -0.1264 0.1551  41   ILE A CA  
148   C C   . ILE A 41   ? 2.1945 3.7893 2.1226 0.8032  -0.1182 0.1302  41   ILE A C   
149   O O   . ILE A 41   ? 2.2306 3.8104 2.1212 0.7857  -0.1068 0.1178  41   ILE A O   
150   C CB  . ILE A 41   ? 2.2636 3.8717 2.2081 0.8243  -0.1222 0.1494  41   ILE A CB  
151   C CG1 . ILE A 41   ? 2.2464 3.8858 2.2358 0.8204  -0.1211 0.1278  41   ILE A CG1 
152   C CG2 . ILE A 41   ? 2.3440 3.9339 2.2423 0.8096  -0.1090 0.1422  41   ILE A CG2 
153   C CD1 . ILE A 41   ? 2.2730 3.9317 2.2752 0.8191  -0.1162 0.1182  41   ILE A CD1 
154   N N   . GLN A 42   ? 2.6868 4.3014 2.6555 0.8058  -0.1232 0.1222  42   GLN A N   
155   C CA  . GLN A 42   ? 2.7672 4.3897 2.7418 0.7872  -0.1154 0.0968  42   GLN A CA  
156   C C   . GLN A 42   ? 2.7557 4.4104 2.7927 0.7956  -0.1206 0.0876  42   GLN A C   
157   O O   . GLN A 42   ? 2.6911 4.3541 2.7574 0.8149  -0.1318 0.1050  42   GLN A O   
158   C CB  . GLN A 42   ? 2.8119 4.4141 2.7569 0.7790  -0.1164 0.1010  42   GLN A CB  
159   C CG  . GLN A 42   ? 2.7931 4.4123 2.7702 0.7723  -0.1169 0.0858  42   GLN A CG  
160   C CD  . GLN A 42   ? 2.7908 4.4000 2.7624 0.7797  -0.1262 0.1026  42   GLN A CD  
161   O OE1 . GLN A 42   ? 2.7740 4.3988 2.7777 0.7794  -0.1287 0.0954  42   GLN A OE1 
162   N NE2 . GLN A 42   ? 2.8119 4.3957 2.7442 0.7867  -0.1312 0.1246  42   GLN A NE2 
163   N N   . VAL A 43   ? 2.0140 3.6866 2.0729 0.7814  -0.1125 0.0604  43   VAL A N   
164   C CA  . VAL A 43   ? 1.9260 3.6295 2.0473 0.7916  -0.1175 0.0525  43   VAL A CA  
165   C C   . VAL A 43   ? 1.9729 3.6948 2.1221 0.7754  -0.1091 0.0219  43   VAL A C   
166   O O   . VAL A 43   ? 2.0334 3.7500 2.1566 0.7541  -0.0970 0.0011  43   VAL A O   
167   C CB  . VAL A 43   ? 1.8343 3.5530 1.9757 0.8042  -0.1209 0.0577  43   VAL A CB  
168   C CG1 . VAL A 43   ? 1.8552 3.5771 1.9774 0.7878  -0.1084 0.0366  43   VAL A CG1 
169   C CG2 . VAL A 43   ? 1.7227 3.4702 1.9280 0.8183  -0.1292 0.0557  43   VAL A CG2 
170   N N   . TYR A 44   ? 2.8317 4.5750 3.0351 0.7853  -0.1152 0.0191  44   TYR A N   
171   C CA  . TYR A 44   ? 2.8888 4.6528 3.1293 0.7723  -0.1079 -0.0100 44   TYR A CA  
172   C C   . TYR A 44   ? 3.1059 4.8954 3.3842 0.7737  -0.1055 -0.0274 44   TYR A C   
173   O O   . TYR A 44   ? 3.0282 4.8412 3.3572 0.7724  -0.1041 -0.0463 44   TYR A O   
174   C CB  . TYR A 44   ? 2.9472 4.7216 3.2300 0.7824  -0.1149 -0.0050 44   TYR A CB  
175   C CG  . TYR A 44   ? 3.0938 4.8812 3.4003 0.7641  -0.1053 -0.0337 44   TYR A CG  
176   C CD1 . TYR A 44   ? 3.1910 4.9631 3.4582 0.7430  -0.0970 -0.0431 44   TYR A CD1 
177   C CD2 . TYR A 44   ? 3.1201 4.9353 3.4888 0.7673  -0.1046 -0.0515 44   TYR A CD2 
178   C CE1 . TYR A 44   ? 3.2146 4.9994 3.5027 0.7242  -0.0873 -0.0703 44   TYR A CE1 
179   C CE2 . TYR A 44   ? 3.1427 4.9706 3.5354 0.7495  -0.0947 -0.0793 44   TYR A CE2 
180   C CZ  . TYR A 44   ? 3.1815 4.9945 3.5333 0.7273  -0.0857 -0.0890 44   TYR A CZ  
181   O OH  . TYR A 44   ? 3.1713 4.9979 3.5465 0.7077  -0.0750 -0.1177 44   TYR A OH  
182   N N   . GLY A 45   ? 2.0738 3.8596 2.3292 0.7764  -0.1049 -0.0216 45   GLY A N   
183   C CA  . GLY A 45   ? 2.0863 3.8974 2.3755 0.7787  -0.1037 -0.0365 45   GLY A CA  
184   C C   . GLY A 45   ? 2.1060 3.9295 2.4038 0.7557  -0.0899 -0.0731 45   GLY A C   
185   O O   . GLY A 45   ? 2.1198 3.9261 2.3785 0.7351  -0.0793 -0.0850 45   GLY A O   
186   N N   . TYR A 46   ? 2.7110 4.5641 3.0597 0.7589  -0.0903 -0.0912 46   TYR A N   
187   C CA  . TYR A 46   ? 2.7695 4.6383 3.1333 0.7376  -0.0770 -0.1289 46   TYR A CA  
188   C C   . TYR A 46   ? 2.8282 4.6918 3.1503 0.7211  -0.0652 -0.1439 46   TYR A C   
189   O O   . TYR A 46   ? 2.9141 4.7618 3.1957 0.7265  -0.0671 -0.1244 46   TYR A O   
190   C CB  . TYR A 46   ? 2.7729 4.6763 3.2108 0.7483  -0.0823 -0.1433 46   TYR A CB  
191   C CG  . TYR A 46   ? 2.8002 4.7168 3.2606 0.7720  -0.0957 -0.1231 46   TYR A CG  
192   C CD1 . TYR A 46   ? 2.8607 4.7856 3.3065 0.7694  -0.0927 -0.1293 46   TYR A CD1 
193   C CD2 . TYR A 46   ? 2.7660 4.6861 3.2597 0.7959  -0.1110 -0.0975 46   TYR A CD2 
194   C CE1 . TYR A 46   ? 2.8634 4.8015 3.3280 0.7898  -0.1052 -0.1105 46   TYR A CE1 
195   C CE2 . TYR A 46   ? 2.7685 4.7001 3.2802 0.8162  -0.1236 -0.0783 46   TYR A CE2 
196   C CZ  . TYR A 46   ? 2.8212 4.7623 3.3183 0.8129  -0.1209 -0.0847 46   TYR A CZ  
197   O OH  . TYR A 46   ? 2.8252 4.7791 3.3390 0.8318  -0.1335 -0.0655 46   TYR A OH  
198   N N   . THR A 47   ? 4.4975 6.3755 4.8317 0.7005  -0.0522 -0.1797 47   THR A N   
199   C CA  . THR A 47   ? 4.5050 6.3756 4.7953 0.6789  -0.0374 -0.1996 47   THR A CA  
200   C C   . THR A 47   ? 4.5055 6.3740 4.7723 0.6892  -0.0403 -0.1843 47   THR A C   
201   O O   . THR A 47   ? 4.5507 6.3979 4.7607 0.6753  -0.0301 -0.1851 47   THR A O   
202   C CB  . THR A 47   ? 5.1279 6.7608 5.4762 0.5698  -0.0130 -0.2014 47   THR A CB  
203   O OG1 . THR A 47   ? 5.0964 6.7596 5.4626 0.5691  -0.0093 -0.2198 47   THR A OG1 
204   C CG2 . THR A 47   ? 5.1972 6.7743 5.4958 0.5334  0.0062  -0.2143 47   THR A CG2 
205   N N   . GLU A 48   ? 3.5925 5.4830 3.9026 0.7127  -0.0538 -0.1703 48   GLU A N   
206   C CA  . GLU A 48   ? 3.5997 5.4931 3.8933 0.7223  -0.0570 -0.1568 48   GLU A CA  
207   C C   . GLU A 48   ? 3.5783 5.4370 3.8110 0.7251  -0.0577 -0.1275 48   GLU A C   
208   O O   . GLU A 48   ? 3.5402 5.3883 3.7755 0.7428  -0.0702 -0.0982 48   GLU A O   
209   C CB  . GLU A 48   ? 3.5629 5.4838 3.9132 0.7482  -0.0739 -0.1421 48   GLU A CB  
210   C CG  . GLU A 48   ? 3.5880 5.5218 3.9316 0.7552  -0.0761 -0.1361 48   GLU A CG  
211   C CD  . GLU A 48   ? 3.6207 5.5735 3.9658 0.7369  -0.0625 -0.1713 48   GLU A CD  
212   O OE1 . GLU A 48   ? 3.6028 5.5681 3.9746 0.7240  -0.0553 -0.2009 48   GLU A OE1 
213   O OE2 . GLU A 48   ? 3.6571 5.6131 3.9773 0.7346  -0.0584 -0.1706 48   GLU A OE2 
214   N N   . ALA A 49   ? 3.5356 5.3766 3.7145 0.7073  -0.0438 -0.1363 49   ALA A N   
215   C CA  . ALA A 49   ? 3.5239 5.3334 3.6468 0.7102  -0.0435 -0.1101 49   ALA A CA  
216   C C   . ALA A 49   ? 3.4709 5.2932 3.6129 0.7337  -0.0566 -0.0850 49   ALA A C   
217   O O   . ALA A 49   ? 3.4592 5.3134 3.6437 0.7414  -0.0612 -0.0938 49   ALA A O   
218   C CB  . ALA A 49   ? 3.5965 5.3892 3.6653 0.6874  -0.0255 -0.1269 49   ALA A CB  
219   N N   . PHE A 50   ? 3.3121 5.1105 3.4240 0.7449  -0.0629 -0.0543 50   PHE A N   
220   C CA  . PHE A 50   ? 3.2922 5.1022 3.4216 0.7660  -0.0752 -0.0300 50   PHE A CA  
221   C C   . PHE A 50   ? 3.2525 5.0335 3.3354 0.7716  -0.0761 -0.0022 50   PHE A C   
222   O O   . PHE A 50   ? 3.2386 4.9894 3.2871 0.7679  -0.0743 0.0081  50   PHE A O   
223   C CB  . PHE A 50   ? 3.3193 5.1493 3.5065 0.7860  -0.0921 -0.0185 50   PHE A CB  
224   C CG  . PHE A 50   ? 3.3970 5.2059 3.5799 0.7927  -0.0990 -0.0011 50   PHE A CG  
225   C CD1 . PHE A 50   ? 3.4159 5.2177 3.6033 0.8123  -0.1122 0.0298  50   PHE A CD1 
226   C CD2 . PHE A 50   ? 3.4593 5.2571 3.6344 0.7785  -0.0920 -0.0166 50   PHE A CD2 
227   C CE1 . PHE A 50   ? 3.4170 5.2014 3.6017 0.8184  -0.1183 0.0446  50   PHE A CE1 
228   C CE2 . PHE A 50   ? 3.4536 5.2345 3.6254 0.7844  -0.0984 -0.0011 50   PHE A CE2 
229   C CZ  . PHE A 50   ? 3.4327 5.2072 3.6098 0.8047  -0.1116 0.0293  50   PHE A CZ  
230   N N   . ASP A 51   ? 2.1303 3.9218 2.2137 0.7805  -0.0790 0.0094  51   ASP A N   
231   C CA  . ASP A 51   ? 2.1360 3.9029 2.1767 0.7841  -0.0776 0.0324  51   ASP A CA  
232   C C   . ASP A 51   ? 2.0895 3.8430 2.1361 0.8024  -0.0918 0.0629  51   ASP A C   
233   O O   . ASP A 51   ? 2.0433 3.8133 2.1339 0.8162  -0.1050 0.0695  51   ASP A O   
234   C CB  . ASP A 51   ? 2.1297 3.9149 2.1709 0.7862  -0.0753 0.0335  51   ASP A CB  
235   C CG  . ASP A 51   ? 2.1734 3.9412 2.1633 0.7680  -0.0570 0.0222  51   ASP A CG  
236   O OD1 . ASP A 51   ? 2.1820 3.9362 2.1480 0.7501  -0.0444 0.0016  51   ASP A OD1 
237   O OD2 . ASP A 51   ? 2.1958 3.9633 2.1689 0.7708  -0.0545 0.0336  51   ASP A OD2 
238   N N   . ALA A 52   ? 3.3915 5.1148 3.3940 0.8023  -0.0886 0.0806  52   ALA A N   
239   C CA  . ALA A 52   ? 3.3125 5.0196 3.3140 0.8181  -0.1004 0.1088  52   ALA A CA  
240   C C   . ALA A 52   ? 3.3277 5.0112 3.2887 0.8203  -0.0969 0.1281  52   ALA A C   
241   O O   . ALA A 52   ? 3.3814 5.0360 3.2974 0.8094  -0.0868 0.1270  52   ALA A O   
242   C CB  . ALA A 52   ? 3.2717 4.9602 3.2664 0.8152  -0.1023 0.1081  52   ALA A CB  
243   N N   . THR A 53   ? 2.9827 4.6785 2.9607 0.8341  -0.1053 0.1458  53   THR A N   
244   C CA  . THR A 53   ? 2.9772 4.6534 2.9243 0.8379  -0.1032 0.1654  53   THR A CA  
245   C C   . THR A 53   ? 2.9009 4.5706 2.8626 0.8555  -0.1176 0.1907  53   THR A C   
246   O O   . THR A 53   ? 2.8402 4.5320 2.8419 0.8678  -0.1298 0.1980  53   THR A O   
247   C CB  . THR A 53   ? 3.0608 4.7562 3.0095 0.8364  -0.0987 0.1647  53   THR A CB  
248   O OG1 . THR A 53   ? 3.1281 4.8156 3.0426 0.8187  -0.0812 0.1466  53   THR A OG1 
249   C CG2 . THR A 53   ? 3.0481 4.7329 2.9856 0.8463  -0.1026 0.1891  53   THR A CG2 
250   N N   . ILE A 54   ? 2.2315 3.8702 2.1606 0.8566  -0.1160 0.2040  54   ILE A N   
251   C CA  . ILE A 54   ? 2.1724 3.8029 2.1114 0.8722  -0.1282 0.2269  54   ILE A CA  
252   C C   . ILE A 54   ? 2.1550 3.7771 2.0756 0.8755  -0.1253 0.2421  54   ILE A C   
253   O O   . ILE A 54   ? 2.1578 3.7754 2.0528 0.8649  -0.1128 0.2348  54   ILE A O   
254   C CB  . ILE A 54   ? 2.2173 3.8192 2.1341 0.8720  -0.1295 0.2318  54   ILE A CB  
255   C CG1 . ILE A 54   ? 2.2220 3.8269 2.1438 0.8621  -0.1270 0.2125  54   ILE A CG1 
256   C CG2 . ILE A 54   ? 2.1615 3.7604 2.0969 0.8886  -0.1433 0.2522  54   ILE A CG2 
257   C CD1 . ILE A 54   ? 2.2300 3.8079 2.1271 0.8598  -0.1281 0.2165  54   ILE A CD1 
258   N N   . SER A 55   ? 1.6168 3.2369 1.5507 0.8894  -0.1360 0.2620  55   SER A N   
259   C CA  . SER A 55   ? 1.6328 3.2407 1.5478 0.8923  -0.1331 0.2769  55   SER A CA  
260   C C   . SER A 55   ? 1.6194 3.2261 1.5533 0.9076  -0.1461 0.2969  55   SER A C   
261   O O   . SER A 55   ? 1.5926 3.2084 1.5547 0.9163  -0.1574 0.2997  55   SER A O   
262   C CB  . SER A 55   ? 1.6705 3.2981 1.5869 0.8862  -0.1261 0.2724  55   SER A CB  
263   O OG  . SER A 55   ? 1.5935 3.2526 1.5495 0.8933  -0.1365 0.2740  55   SER A OG  
264   N N   . ILE A 56   ? 2.1302 3.7256 2.0488 0.9099  -0.1434 0.3096  56   ILE A N   
265   C CA  . ILE A 56   ? 2.1911 3.7777 2.1180 0.9223  -0.1529 0.3275  56   ILE A CA  
266   C C   . ILE A 56   ? 2.2306 3.8336 2.1725 0.9260  -0.1556 0.3380  56   ILE A C   
267   O O   . ILE A 56   ? 2.2445 3.8444 2.1678 0.9192  -0.1458 0.3385  56   ILE A O   
268   C CB  . ILE A 56   ? 2.2830 3.8369 2.1754 0.9210  -0.1468 0.3332  56   ILE A CB  
269   C CG1 . ILE A 56   ? 2.3789 3.9237 2.2408 0.9088  -0.1311 0.3266  56   ILE A CG1 
270   C CG2 . ILE A 56   ? 2.3935 3.9303 2.2733 0.9195  -0.1481 0.3270  56   ILE A CG2 
271   C CD1 . ILE A 56   ? 2.4579 3.9673 2.2819 0.9050  -0.1232 0.3282  56   ILE A CD1 
272   N N   . LYS A 57   ? 2.5194 4.1397 2.4944 0.9359  -0.1683 0.3461  57   LYS A N   
273   C CA  . LYS A 57   ? 2.5497 4.1886 2.5405 0.9382  -0.1720 0.3557  57   LYS A CA  
274   C C   . LYS A 57   ? 2.5304 4.1649 2.5358 0.9494  -0.1823 0.3720  57   LYS A C   
275   O O   . LYS A 57   ? 2.5223 4.1474 2.5365 0.9575  -0.1896 0.3748  57   LYS A O   
276   C CB  . LYS A 57   ? 2.5257 4.1952 2.5438 0.9371  -0.1770 0.3491  57   LYS A CB  
277   C CG  . LYS A 57   ? 2.5575 4.2358 2.5610 0.9244  -0.1653 0.3329  57   LYS A CG  
278   C CD  . LYS A 57   ? 2.5318 4.2406 2.5650 0.9243  -0.1713 0.3244  57   LYS A CD  
279   C CE  . LYS A 57   ? 2.5744 4.2907 2.5923 0.9112  -0.1588 0.3053  57   LYS A CE  
280   N NZ  . LYS A 57   ? 2.5681 4.3141 2.6171 0.9116  -0.1648 0.2947  57   LYS A NZ  
281   N N   . SER A 58   ? 3.1965 4.8387 3.2038 0.9487  -0.1822 0.3816  58   SER A N   
282   C CA  . SER A 58   ? 3.1824 4.8167 3.1957 0.9563  -0.1883 0.3959  58   SER A CA  
283   C C   . SER A 58   ? 3.1112 4.7623 3.1574 0.9650  -0.2021 0.4045  58   SER A C   
284   O O   . SER A 58   ? 3.1138 4.7875 3.1769 0.9632  -0.2062 0.4042  58   SER A O   
285   C CB  . SER A 58   ? 3.2266 4.8598 3.2243 0.9491  -0.1798 0.4009  58   SER A CB  
286   O OG  . SER A 58   ? 3.2602 4.9170 3.2619 0.9408  -0.1767 0.3972  58   SER A OG  
287   N N   . TYR A 59   ? 2.7928 4.4324 2.8473 0.9742  -0.2091 0.4125  59   TYR A N   
288   C CA  . TYR A 59   ? 2.7363 4.3867 2.8208 0.9832  -0.2217 0.4201  59   TYR A CA  
289   C C   . TYR A 59   ? 3.0934 4.7695 3.2031 0.9831  -0.2286 0.4202  59   TYR A C   
290   O O   . TYR A 59   ? 3.1268 4.8114 3.2434 0.9816  -0.2280 0.4095  59   TYR A O   
291   C CB  . TYR A 59   ? 2.6888 4.3303 2.7750 0.9880  -0.2252 0.4323  59   TYR A CB  
292   C CG  . TYR A 59   ? 2.6187 4.2620 2.7301 0.9983  -0.2363 0.4376  59   TYR A CG  
293   C CD1 . TYR A 59   ? 2.6011 4.2421 2.7226 1.0034  -0.2395 0.4304  59   TYR A CD1 
294   C CD2 . TYR A 59   ? 2.5671 4.2142 2.6918 1.0017  -0.2425 0.4489  59   TYR A CD2 
295   C CE1 . TYR A 59   ? 2.5455 4.1885 2.6907 1.0120  -0.2482 0.4341  59   TYR A CE1 
296   C CE2 . TYR A 59   ? 2.5137 4.1617 2.6610 1.0104  -0.2515 0.4530  59   TYR A CE2 
297   C CZ  . TYR A 59   ? 2.5029 4.1489 2.6609 1.0159  -0.2541 0.4455  59   TYR A CZ  
298   O OH  . TYR A 59   ? 2.4527 4.0997 2.6337 1.0240  -0.2618 0.4486  59   TYR A OH  
299   N N   . PRO A 60   ? 2.0883 3.7766 2.2121 0.9845  -0.2354 0.4319  60   PRO A N   
300   C CA  . PRO A 60   ? 2.0361 3.7468 2.1869 0.9869  -0.2444 0.4332  60   PRO A CA  
301   C C   . PRO A 60   ? 2.0118 3.7427 2.1602 0.9785  -0.2410 0.4266  60   PRO A C   
302   O O   . PRO A 60   ? 1.9964 3.7433 2.1662 0.9810  -0.2466 0.4212  60   PRO A O   
303   C CB  . PRO A 60   ? 2.0203 3.7344 2.1846 0.9910  -0.2534 0.4490  60   PRO A CB  
304   C CG  . PRO A 60   ? 2.0092 3.7019 2.1587 0.9928  -0.2497 0.4531  60   PRO A CG  
305   C CD  . PRO A 60   ? 2.0543 3.7367 2.1750 0.9852  -0.2371 0.4444  60   PRO A CD  
306   N N   . ASP A 61   ? 2.3447 4.0760 2.4692 0.9685  -0.2316 0.4262  61   ASP A N   
307   C CA  . ASP A 61   ? 2.3492 4.0995 2.4679 0.9592  -0.2263 0.4183  61   ASP A CA  
308   C C   . ASP A 61   ? 2.3602 4.1022 2.4608 0.9536  -0.2147 0.4015  61   ASP A C   
309   O O   . ASP A 61   ? 2.3745 4.0993 2.4472 0.9475  -0.2031 0.3983  61   ASP A O   
310   C CB  . ASP A 61   ? 2.3774 4.1325 2.4780 0.9493  -0.2199 0.4248  61   ASP A CB  
311   C CG  . ASP A 61   ? 2.4146 4.1459 2.4859 0.9443  -0.2068 0.4222  61   ASP A CG  
312   O OD1 . ASP A 61   ? 2.4673 4.1970 2.5172 0.9348  -0.1940 0.4120  61   ASP A OD1 
313   O OD2 . ASP A 61   ? 2.3793 4.0931 2.4496 0.9500  -0.2091 0.4301  61   ASP A OD2 
314   N N   . LYS A 62   ? 2.7851 4.5384 2.9009 0.9550  -0.2171 0.3902  62   LYS A N   
315   C CA  . LYS A 62   ? 2.8120 4.5572 2.9090 0.9479  -0.2055 0.3731  62   LYS A CA  
316   C C   . LYS A 62   ? 2.8625 4.6156 2.9363 0.9349  -0.1932 0.3662  62   LYS A C   
317   O O   . LYS A 62   ? 2.9195 4.6841 2.9912 0.9281  -0.1872 0.3512  62   LYS A O   
318   C CB  . LYS A 62   ? 2.7642 4.5208 2.8844 0.9510  -0.2101 0.3605  62   LYS A CB  
319   C CG  . LYS A 62   ? 2.6741 4.4139 2.8036 0.9591  -0.2145 0.3598  62   LYS A CG  
320   C CD  . LYS A 62   ? 2.5888 4.3452 2.7520 0.9638  -0.2220 0.3508  62   LYS A CD  
321   C CE  . LYS A 62   ? 2.4949 4.2380 2.6717 0.9720  -0.2272 0.3518  62   LYS A CE  
322   N NZ  . LYS A 62   ? 2.4375 4.1984 2.6522 0.9771  -0.2348 0.3443  62   LYS A NZ  
323   N N   . LYS A 63   ? 3.0622 4.8096 3.1193 0.9309  -0.1886 0.3761  63   LYS A N   
324   C CA  . LYS A 63   ? 3.0932 4.8479 3.1283 0.9178  -0.1758 0.3705  63   LYS A CA  
325   C C   . LYS A 63   ? 3.1054 4.8352 3.1067 0.9101  -0.1594 0.3606  63   LYS A C   
326   O O   . LYS A 63   ? 3.1462 4.8795 3.1357 0.9018  -0.1498 0.3454  63   LYS A O   
327   C CB  . LYS A 63   ? 3.0956 4.8587 3.1303 0.9151  -0.1776 0.3847  63   LYS A CB  
328   C CG  . LYS A 63   ? 3.1049 4.8960 3.1682 0.9191  -0.1923 0.3937  63   LYS A CG  
329   C CD  . LYS A 63   ? 3.1655 4.9826 3.2412 0.9159  -0.1936 0.3816  63   LYS A CD  
330   C CE  . LYS A 63   ? 3.2283 5.0554 3.2805 0.9009  -0.1783 0.3702  63   LYS A CE  
331   N NZ  . LYS A 63   ? 3.2644 5.1174 3.3288 0.8975  -0.1790 0.3561  63   LYS A NZ  
332   N N   . PHE A 64   ? 2.6508 4.3553 2.6369 0.9127  -0.1561 0.3690  64   PHE A N   
333   C CA  . PHE A 64   ? 2.6474 4.3254 2.6017 0.9066  -0.1418 0.3615  64   PHE A CA  
334   C C   . PHE A 64   ? 2.6609 4.3264 2.6110 0.9086  -0.1417 0.3504  64   PHE A C   
335   O O   . PHE A 64   ? 2.6272 4.2919 2.5964 0.9185  -0.1535 0.3535  64   PHE A O   
336   C CB  . PHE A 64   ? 2.6012 4.2547 2.5440 0.9108  -0.1402 0.3731  64   PHE A CB  
337   C CG  . PHE A 64   ? 2.5974 4.2435 2.5164 0.9000  -0.1249 0.3723  64   PHE A CG  
338   C CD1 . PHE A 64   ? 2.5538 4.2091 2.4792 0.8980  -0.1252 0.3822  64   PHE A CD1 
339   C CD2 . PHE A 64   ? 2.6280 4.2573 2.5184 0.8911  -0.1094 0.3611  64   PHE A CD2 
340   C CE1 . PHE A 64   ? 2.5646 4.2138 2.4702 0.8873  -0.1101 0.3804  64   PHE A CE1 
341   C CE2 . PHE A 64   ? 2.6408 4.2625 2.5108 0.8811  -0.0943 0.3599  64   PHE A CE2 
342   C CZ  . PHE A 64   ? 2.6093 4.2418 2.4880 0.8792  -0.0944 0.3692  64   PHE A CZ  
343   N N   . SER A 65   ? 2.6433 4.2991 2.5674 0.8980  -0.1276 0.3370  65   SER A N   
344   C CA  . SER A 65   ? 2.6780 4.3189 2.5913 0.8966  -0.1249 0.3253  65   SER A CA  
345   C C   . SER A 65   ? 2.7275 4.3389 2.6018 0.8880  -0.1094 0.3211  65   SER A C   
346   O O   . SER A 65   ? 2.7845 4.3987 2.6403 0.8761  -0.0955 0.3120  65   SER A O   
347   C CB  . SER A 65   ? 2.7190 4.3839 2.6446 0.8904  -0.1241 0.3090  65   SER A CB  
348   O OG  . SER A 65   ? 2.7826 4.4540 2.6883 0.8767  -0.1092 0.2972  65   SER A OG  
349   N N   . TYR A 66   ? 2.5553 4.1386 2.4178 0.8944  -0.1121 0.3281  66   TYR A N   
350   C CA  . TYR A 66   ? 2.5387 4.0900 2.3659 0.8893  -0.0999 0.3284  66   TYR A CA  
351   C C   . TYR A 66   ? 2.5999 4.1392 2.4006 0.8774  -0.0882 0.3120  66   TYR A C   
352   O O   . TYR A 66   ? 2.6427 4.1692 2.4157 0.8666  -0.0727 0.3060  66   TYR A O   
353   C CB  . TYR A 66   ? 2.4261 3.9540 2.2526 0.9012  -0.1090 0.3417  66   TYR A CB  
354   C CG  . TYR A 66   ? 2.2742 3.8170 2.1313 0.9129  -0.1223 0.3553  66   TYR A CG  
355   C CD1 . TYR A 66   ? 2.2259 3.7676 2.0834 0.9139  -0.1195 0.3650  66   TYR A CD1 
356   C CD2 . TYR A 66   ? 2.1868 3.7446 2.0723 0.9219  -0.1368 0.3576  66   TYR A CD2 
357   C CE1 . TYR A 66   ? 2.1296 3.6842 2.0130 0.9229  -0.1308 0.3766  66   TYR A CE1 
358   C CE2 . TYR A 66   ? 2.0960 3.6658 2.0076 0.9318  -0.1482 0.3700  66   TYR A CE2 
359   C CZ  . TYR A 66   ? 2.0562 3.6241 1.9657 0.9319  -0.1452 0.3794  66   TYR A CZ  
360   O OH  . TYR A 66   ? 1.9503 3.5290 1.8835 0.9400  -0.1556 0.3910  66   TYR A OH  
361   N N   . SER A 67   ? 1.9868 3.5305 1.7963 0.8783  -0.0949 0.3040  67   SER A N   
362   C CA  . SER A 67   ? 2.0131 3.5505 1.8013 0.8654  -0.0842 0.2860  67   SER A CA  
363   C C   . SER A 67   ? 1.9518 3.5078 1.7636 0.8662  -0.0928 0.2753  67   SER A C   
364   O O   . SER A 67   ? 1.8793 3.4516 1.7240 0.8776  -0.1072 0.2826  67   SER A O   
365   C CB  . SER A 67   ? 2.0576 3.5554 1.8064 0.8609  -0.0763 0.2870  67   SER A CB  
366   O OG  . SER A 67   ? 2.0223 3.5055 1.7746 0.8703  -0.0884 0.2953  67   SER A OG  
367   N N   . SER A 68   ? 2.6364 4.1894 2.4313 0.8533  -0.0830 0.2570  68   SER A N   
368   C CA  . SER A 68   ? 2.6437 4.2175 2.4619 0.8510  -0.0880 0.2426  68   SER A CA  
369   C C   . SER A 68   ? 2.7199 4.2761 2.5067 0.8356  -0.0757 0.2248  68   SER A C   
370   O O   . SER A 68   ? 2.7363 4.2633 2.4843 0.8283  -0.0649 0.2263  68   SER A O   
371   C CB  . SER A 68   ? 2.6524 4.2622 2.4964 0.8487  -0.0873 0.2336  68   SER A CB  
372   O OG  . SER A 68   ? 2.7264 4.3341 2.5433 0.8336  -0.0703 0.2196  68   SER A OG  
373   N N   . GLY A 69   ? 2.3742 3.9479 2.1781 0.8299  -0.0767 0.2075  69   GLY A N   
374   C CA  . GLY A 69   ? 2.4786 4.0369 2.2541 0.8136  -0.0651 0.1889  69   GLY A CA  
375   C C   . GLY A 69   ? 2.4933 4.0799 2.2967 0.8073  -0.0656 0.1674  69   GLY A C   
376   O O   . GLY A 69   ? 2.4380 4.0425 2.2785 0.8168  -0.0785 0.1690  69   GLY A O   
377   N N   . HIS A 70   ? 3.7031 5.2933 3.4890 0.7907  -0.0509 0.1462  70   HIS A N   
378   C CA  . HIS A 70   ? 3.7248 5.3444 3.5382 0.7835  -0.0496 0.1229  70   HIS A CA  
379   C C   . HIS A 70   ? 3.7045 5.3085 3.5021 0.7707  -0.0448 0.1071  70   HIS A C   
380   O O   . HIS A 70   ? 3.7349 5.3285 3.5023 0.7524  -0.0296 0.0882  70   HIS A O   
381   C CB  . HIS A 70   ? 3.8451 5.4805 3.6500 0.7717  -0.0358 0.1066  70   HIS A CB  
382   C CG  . HIS A 70   ? 3.9101 5.5863 3.7573 0.7712  -0.0392 0.0884  70   HIS A CG  
383   N ND1 . HIS A 70   ? 3.9037 5.6114 3.7899 0.7846  -0.0506 0.0975  70   HIS A ND1 
384   C CD2 . HIS A 70   ? 3.9759 5.6665 3.8329 0.7586  -0.0328 0.0615  70   HIS A CD2 
385   C CE1 . HIS A 70   ? 3.9172 5.6570 3.8365 0.7816  -0.0520 0.0777  70   HIS A CE1 
386   N NE2 . HIS A 70   ? 3.9605 5.6913 3.8640 0.7659  -0.0409 0.0549  70   HIS A NE2 
387   N N   . VAL A 71   ? 2.9044 4.5067 2.7215 0.7793  -0.0572 0.1145  71   VAL A N   
388   C CA  . VAL A 71   ? 2.9138 4.4994 2.7134 0.7670  -0.0535 0.1023  71   VAL A CA  
389   C C   . VAL A 71   ? 2.8859 4.5006 2.7253 0.7625  -0.0559 0.0804  71   VAL A C   
390   O O   . VAL A 71   ? 2.8154 4.4452 2.6935 0.7748  -0.0691 0.0867  71   VAL A O   
391   C CB  . VAL A 71   ? 2.8661 4.4256 2.6521 0.7764  -0.0633 0.1239  71   VAL A CB  
392   C CG1 . VAL A 71   ? 2.9027 4.4282 2.6419 0.7757  -0.0572 0.1398  71   VAL A CG1 
393   C CG2 . VAL A 71   ? 2.7796 4.3580 2.6100 0.7977  -0.0805 0.1415  71   VAL A CG2 
394   N N   . HIS A 72   ? 2.2567 3.8789 2.0868 0.7441  -0.0422 0.0538  72   HIS A N   
395   C CA  . HIS A 72   ? 2.2786 3.9318 2.1492 0.7388  -0.0426 0.0296  72   HIS A CA  
396   C C   . HIS A 72   ? 2.2792 3.9225 2.1453 0.7267  -0.0406 0.0161  72   HIS A C   
397   O O   . HIS A 72   ? 2.3327 3.9518 2.1550 0.7079  -0.0282 0.0052  72   HIS A O   
398   C CB  . HIS A 72   ? 2.3965 4.0659 2.2626 0.7240  -0.0283 0.0043  72   HIS A CB  
399   C CG  . HIS A 72   ? 2.4549 4.1513 2.3556 0.7142  -0.0257 -0.0250 72   HIS A CG  
400   N ND1 . HIS A 72   ? 2.4349 4.1699 2.3936 0.7262  -0.0356 -0.0304 72   HIS A ND1 
401   C CD2 . HIS A 72   ? 2.5194 4.2100 2.4063 0.6934  -0.0143 -0.0508 72   HIS A CD2 
402   C CE1 . HIS A 72   ? 2.4517 4.2037 2.4327 0.7138  -0.0302 -0.0589 72   HIS A CE1 
403   N NE2 . HIS A 72   ? 2.5015 4.2276 2.4395 0.6931  -0.0169 -0.0724 72   HIS A NE2 
404   N N   . LEU A 73   ? 2.6002 4.2632 2.5121 0.7363  -0.0521 0.0157  73   LEU A N   
405   C CA  . LEU A 73   ? 2.6234 4.2816 2.5374 0.7247  -0.0505 0.0019  73   LEU A CA  
406   C C   . LEU A 73   ? 2.6804 4.3645 2.6220 0.7095  -0.0419 -0.0324 73   LEU A C   
407   O O   . LEU A 73   ? 2.6662 4.3776 2.6373 0.7129  -0.0410 -0.0434 73   LEU A O   
408   C CB  . LEU A 73   ? 2.5122 4.1757 2.4600 0.7424  -0.0665 0.0198  73   LEU A CB  
409   C CG  . LEU A 73   ? 2.4246 4.1137 2.4206 0.7656  -0.0799 0.0347  73   LEU A CG  
410   C CD1 . LEU A 73   ? 2.3407 4.0417 2.3795 0.7777  -0.0922 0.0409  73   LEU A CD1 
411   C CD2 . LEU A 73   ? 2.4204 4.0940 2.3924 0.7787  -0.0846 0.0621  73   LEU A CD2 
412   N N   . SER A 74   ? 3.0840 4.7606 3.0166 0.6924  -0.0357 -0.0497 74   SER A N   
413   C CA  . SER A 74   ? 3.1356 4.8361 3.0955 0.6763  -0.0267 -0.0843 74   SER A CA  
414   C C   . SER A 74   ? 3.1845 4.8744 3.1360 0.6603  -0.0230 -0.0966 74   SER A C   
415   O O   . SER A 74   ? 3.2272 4.8901 3.1465 0.6609  -0.0270 -0.0781 74   SER A O   
416   C CB  . SER A 74   ? 3.1866 4.8854 3.1162 0.6575  -0.0100 -0.1063 74   SER A CB  
417   O OG  . SER A 74   ? 3.2308 4.8948 3.0993 0.6362  0.0023  -0.1110 74   SER A OG  
418   N N   . SER A 75   ? 2.9991 4.7111 2.9803 0.6456  -0.0155 -0.1283 75   SER A N   
419   C CA  . SER A 75   ? 3.0476 4.7522 3.0215 0.6268  -0.0101 -0.1438 75   SER A CA  
420   C C   . SER A 75   ? 3.1332 4.8002 3.0342 0.6047  0.0015  -0.1446 75   SER A C   
421   O O   . SER A 75   ? 3.1288 4.7800 3.0087 0.5916  0.0030  -0.1462 75   SER A O   
422   C CB  . SER A 75   ? 3.0869 4.8228 3.1054 0.6127  -0.0017 -0.1812 75   SER A CB  
423   O OG  . SER A 75   ? 3.0391 4.8052 3.1257 0.6321  -0.0138 -0.1788 75   SER A OG  
424   N N   . GLU A 76   ? 3.3384 4.9911 3.2011 0.6002  0.0096  -0.1432 76   GLU A N   
425   C CA  . GLU A 76   ? 3.3877 5.0014 3.1789 0.5811  0.0204  -0.1409 76   GLU A CA  
426   C C   . GLU A 76   ? 3.3136 4.8969 3.0729 0.5956  0.0089  -0.1043 76   GLU A C   
427   O O   . GLU A 76   ? 3.3734 4.9244 3.0815 0.5818  0.0127  -0.0986 76   GLU A O   
428   C CB  . GLU A 76   ? 3.4726 5.0806 3.2355 0.5737  0.0329  -0.1496 76   GLU A CB  
429   C CG  . GLU A 76   ? 3.5592 5.1232 3.2475 0.5581  0.0428  -0.1414 76   GLU A CG  
430   C CD  . GLU A 76   ? 3.6083 5.1658 3.2707 0.5553  0.0540  -0.1445 76   GLU A CD  
431   O OE1 . GLU A 76   ? 3.5718 5.1614 3.2748 0.5651  0.0534  -0.1534 76   GLU A OE1 
432   O OE2 . GLU A 76   ? 3.6794 5.2001 3.2813 0.5431  0.0633  -0.1381 76   GLU A OE2 
433   N N   . ASN A 77   ? 2.8368 4.4310 2.6267 0.6234  -0.0053 -0.0797 77   ASN A N   
434   C CA  . ASN A 77   ? 2.7262 4.2975 2.4974 0.6405  -0.0179 -0.0455 77   ASN A CA  
435   C C   . ASN A 77   ? 2.4886 4.0766 2.3037 0.6537  -0.0317 -0.0375 77   ASN A C   
436   O O   . ASN A 77   ? 2.3992 3.9797 2.2183 0.6736  -0.0448 -0.0098 77   ASN A O   
437   C CB  . ASN A 77   ? 2.7799 4.3502 2.5523 0.6612  -0.0234 -0.0233 77   ASN A CB  
438   C CG  . ASN A 77   ? 2.9068 4.4398 2.6308 0.6676  -0.0271 0.0050  77   ASN A CG  
439   O OD1 . ASN A 77   ? 2.9697 4.4777 2.6598 0.6584  -0.0275 0.0103  77   ASN A OD1 
440   N ND2 . ASN A 77   ? 2.9347 4.4645 2.6557 0.6829  -0.0299 0.0230  77   ASN A ND2 
441   N N   . LYS A 78   ? 2.4955 4.1067 2.3448 0.6421  -0.0278 -0.0631 78   LYS A N   
442   C CA  . LYS A 78   ? 2.3193 3.9490 2.2145 0.6522  -0.0384 -0.0601 78   LYS A CA  
443   C C   . LYS A 78   ? 2.1767 3.8188 2.1092 0.6827  -0.0539 -0.0344 78   LYS A C   
444   O O   . LYS A 78   ? 2.1116 3.7561 2.0644 0.6951  -0.0648 -0.0198 78   LYS A O   
445   C CB  . LYS A 78   ? 2.2350 3.8414 2.0968 0.6430  -0.0407 -0.0514 78   LYS A CB  
446   C CG  . LYS A 78   ? 2.1934 3.7824 2.0097 0.6113  -0.0262 -0.0734 78   LYS A CG  
447   C CD  . LYS A 78   ? 2.0400 3.6567 1.8917 0.5926  -0.0154 -0.1104 78   LYS A CD  
448   C CE  . LYS A 78   ? 2.0329 3.6315 1.8383 0.5593  -0.0015 -0.1317 78   LYS A CE  
449   N NZ  . LYS A 78   ? 2.0007 3.6270 1.8418 0.5397  0.0102  -0.1701 78   LYS A NZ  
450   N N   . PHE A 79   ? 2.4415 4.0913 2.3809 0.6935  -0.0543 -0.0292 79   PHE A N   
451   C CA  . PHE A 79   ? 2.3769 4.0373 2.3468 0.7208  -0.0682 -0.0045 79   PHE A CA  
452   C C   . PHE A 79   ? 2.3978 4.0328 2.3405 0.7339  -0.0779 0.0266  79   PHE A C   
453   O O   . PHE A 79   ? 2.3623 4.0026 2.3308 0.7471  -0.0890 0.0396  79   PHE A O   
454   C CB  . PHE A 79   ? 2.2868 3.9802 2.3239 0.7327  -0.0765 -0.0109 79   PHE A CB  
455   C CG  . PHE A 79   ? 2.3118 4.0342 2.3846 0.7273  -0.0704 -0.0364 79   PHE A CG  
456   C CD1 . PHE A 79   ? 2.2889 4.0290 2.3906 0.7129  -0.0637 -0.0651 79   PHE A CD1 
457   C CD2 . PHE A 79   ? 2.3288 4.0613 2.4055 0.7355  -0.0708 -0.0327 79   PHE A CD2 
458   C CE1 . PHE A 79   ? 2.2806 4.0482 2.4169 0.7082  -0.0583 -0.0897 79   PHE A CE1 
459   C CE2 . PHE A 79   ? 2.3247 4.0855 2.4344 0.7307  -0.0658 -0.0566 79   PHE A CE2 
460   C CZ  . PHE A 79   ? 2.2979 4.0762 2.4384 0.7177  -0.0599 -0.0852 79   PHE A CZ  
461   N N   . GLN A 80   ? 2.6357 4.2431 2.5269 0.7301  -0.0732 0.0378  80   GLN A N   
462   C CA  . GLN A 80   ? 2.6679 4.2500 2.5316 0.7426  -0.0819 0.0670  80   GLN A CA  
463   C C   . GLN A 80   ? 2.7087 4.2704 2.5318 0.7422  -0.0756 0.0765  80   GLN A C   
464   O O   . GLN A 80   ? 2.7571 4.3174 2.5606 0.7264  -0.0625 0.0584  80   GLN A O   
465   C CB  . GLN A 80   ? 2.7233 4.2829 2.5548 0.7310  -0.0819 0.0684  80   GLN A CB  
466   C CG  . GLN A 80   ? 2.6960 4.2746 2.5632 0.7271  -0.0856 0.0561  80   GLN A CG  
467   C CD  . GLN A 80   ? 2.7156 4.2731 2.5532 0.7213  -0.0897 0.0654  80   GLN A CD  
468   O OE1 . GLN A 80   ? 2.7774 4.3044 2.5620 0.7137  -0.0872 0.0748  80   GLN A OE1 
469   N NE2 . GLN A 80   ? 2.6588 4.2330 2.5311 0.7247  -0.0961 0.0629  80   GLN A NE2 
470   N N   . ASN A 81   ? 2.1244 3.6712 1.9363 0.7590  -0.0842 0.1038  81   ASN A N   
471   C CA  . ASN A 81   ? 2.1945 3.7182 1.9658 0.7586  -0.0780 0.1147  81   ASN A CA  
472   C C   . ASN A 81   ? 2.1362 3.6451 1.9010 0.7784  -0.0885 0.1448  81   ASN A C   
473   O O   . ASN A 81   ? 2.0447 3.5680 1.8449 0.7957  -0.1013 0.1580  81   ASN A O   
474   C CB  . ASN A 81   ? 2.2563 3.7985 2.0381 0.7544  -0.0686 0.1005  81   ASN A CB  
475   C CG  . ASN A 81   ? 2.3810 3.9011 2.1133 0.7343  -0.0520 0.0877  81   ASN A CG  
476   O OD1 . ASN A 81   ? 2.4250 3.9151 2.1159 0.7344  -0.0488 0.1024  81   ASN A OD1 
477   N ND2 . ASN A 81   ? 2.4276 3.9619 2.1642 0.7167  -0.0409 0.0596  81   ASN A ND2 
478   N N   . SER A 82   ? 2.0826 3.5621 1.8022 0.7750  -0.0821 0.1547  82   SER A N   
479   C CA  . SER A 82   ? 2.0898 3.5504 1.7972 0.7911  -0.0902 0.1816  82   SER A CA  
480   C C   . SER A 82   ? 2.1334 3.5941 1.8370 0.7974  -0.0851 0.1893  82   SER A C   
481   O O   . SER A 82   ? 2.1905 3.6533 1.8803 0.7852  -0.0720 0.1750  82   SER A O   
482   C CB  . SER A 82   ? 2.1324 3.5543 1.7892 0.7838  -0.0885 0.1904  82   SER A CB  
483   O OG  . SER A 82   ? 2.1165 3.5363 1.7753 0.7815  -0.0964 0.1901  82   SER A OG  
484   N N   . ALA A 83   ? 1.9264 3.3839 1.6401 0.8152  -0.0947 0.2115  83   ALA A N   
485   C CA  . ALA A 83   ? 1.9235 3.3835 1.6377 0.8218  -0.0909 0.2200  83   ALA A CA  
486   C C   . ALA A 83   ? 1.9318 3.3696 1.6326 0.8353  -0.0972 0.2443  83   ALA A C   
487   O O   . ALA A 83   ? 1.9113 3.3542 1.6350 0.8498  -0.1107 0.2579  83   ALA A O   
488   C CB  . ALA A 83   ? 1.8577 3.3553 1.6204 0.8308  -0.0968 0.2172  83   ALA A CB  
489   N N   . ILE A 84   ? 2.1889 3.6022 1.8538 0.8301  -0.0867 0.2485  84   ILE A N   
490   C CA  . ILE A 84   ? 2.1419 3.5365 1.7978 0.8427  -0.0907 0.2697  84   ILE A CA  
491   C C   . ILE A 84   ? 2.1086 3.5248 1.7913 0.8517  -0.0908 0.2757  84   ILE A C   
492   O O   . ILE A 84   ? 2.1229 3.5358 1.7907 0.8453  -0.0785 0.2727  84   ILE A O   
493   C CB  . ILE A 84   ? 2.9276 4.2823 2.5332 0.8344  -0.0802 0.2739  84   ILE A CB  
494   C CG1 . ILE A 84   ? 2.9797 4.3321 2.5627 0.8179  -0.0616 0.2579  84   ILE A CG1 
495   C CG2 . ILE A 84   ? 2.9302 4.2615 2.5101 0.8291  -0.0847 0.2744  84   ILE A CG2 
496   C CD1 . ILE A 84   ? 3.0058 4.3196 2.5433 0.8116  -0.0500 0.2640  84   ILE A CD1 
497   N N   . LEU A 85   ? 2.6128 4.0515 2.3347 0.8655  -0.1044 0.2838  85   LEU A N   
498   C CA  . LEU A 85   ? 2.5508 4.0074 2.2979 0.8756  -0.1076 0.2935  85   LEU A CA  
499   C C   . LEU A 85   ? 2.4701 3.9005 2.1967 0.8820  -0.1065 0.3098  85   LEU A C   
500   O O   . LEU A 85   ? 2.4904 3.8907 2.1812 0.8761  -0.0999 0.3105  85   LEU A O   
501   C CB  . LEU A 85   ? 2.4796 3.9603 2.2694 0.8888  -0.1231 0.2998  85   LEU A CB  
502   C CG  . LEU A 85   ? 2.4621 3.9675 2.2760 0.8837  -0.1253 0.2838  85   LEU A CG  
503   C CD1 . LEU A 85   ? 2.5014 4.0225 2.3129 0.8716  -0.1136 0.2680  85   LEU A CD1 
504   C CD2 . LEU A 85   ? 2.4726 3.9639 2.2712 0.8769  -0.1257 0.2754  85   LEU A CD2 
505   N N   . THR A 86   ? 2.7491 4.1904 2.4982 0.8935  -0.1126 0.3224  86   THR A N   
506   C CA  . THR A 86   ? 2.6890 4.1073 2.4248 0.9011  -0.1129 0.3376  86   THR A CA  
507   C C   . THR A 86   ? 2.6573 4.0912 2.4156 0.9083  -0.1144 0.3470  86   THR A C   
508   O O   . THR A 86   ? 2.6570 4.0993 2.4110 0.9006  -0.1034 0.3421  86   THR A O   
509   C CB  . THR A 86   ? 2.5493 3.9356 2.2416 0.8905  -0.0983 0.3348  86   THR A CB  
510   O OG1 . THR A 86   ? 2.5337 3.8964 2.2160 0.8992  -0.0999 0.3497  86   THR A OG1 
511   C CG2 . THR A 86   ? 2.5818 3.9779 2.2651 0.8776  -0.0823 0.3231  86   THR A CG2 
512   N N   . ILE A 87   ? 1.8299 3.2682 1.6111 0.9220  -0.1273 0.3596  87   ILE A N   
513   C CA  . ILE A 87   ? 1.8191 3.2673 1.6178 0.9283  -0.1285 0.3695  87   ILE A CA  
514   C C   . ILE A 87   ? 2.0291 3.4511 1.8049 0.9280  -0.1199 0.3764  87   ILE A C   
515   O O   . ILE A 87   ? 2.0645 3.4667 1.8357 0.9370  -0.1262 0.3857  87   ILE A O   
516   C CB  . ILE A 87   ? 1.6693 3.1268 1.4977 0.9428  -0.1442 0.3808  87   ILE A CB  
517   C CG1 . ILE A 87   ? 1.6472 3.1315 1.5050 0.9455  -0.1539 0.3766  87   ILE A CG1 
518   C CG2 . ILE A 87   ? 1.6574 3.1220 1.4992 0.9468  -0.1438 0.3899  87   ILE A CG2 
519   C CD1 . ILE A 87   ? 1.6286 3.1215 1.5144 0.9585  -0.1672 0.3876  87   ILE A CD1 
520   N N   . GLN A 88   ? 2.6030 4.0256 2.3664 0.9181  -0.1057 0.3718  88   GLN A N   
521   C CA  . GLN A 88   ? 2.7047 4.1041 2.4511 0.9180  -0.0967 0.3781  88   GLN A CA  
522   C C   . GLN A 88   ? 2.7922 4.2046 2.5652 0.9265  -0.1027 0.3883  88   GLN A C   
523   O O   . GLN A 88   ? 2.7652 4.2008 2.5658 0.9325  -0.1144 0.3911  88   GLN A O   
524   C CB  . GLN A 88   ? 2.7694 4.1641 2.4919 0.9030  -0.0776 0.3680  88   GLN A CB  
525   C CG  . GLN A 88   ? 2.8213 4.2062 2.5186 0.8929  -0.0711 0.3559  88   GLN A CG  
526   C CD  . GLN A 88   ? 2.8773 4.2300 2.5369 0.8837  -0.0548 0.3526  88   GLN A CD  
527   O OE1 . GLN A 88   ? 2.9318 4.2779 2.5681 0.8716  -0.0449 0.3406  88   GLN A OE1 
528   N NE2 . GLN A 88   ? 2.8524 4.1841 2.5062 0.8889  -0.0516 0.3628  88   GLN A NE2 
529   N N   . PRO A 89   ? 1.8822 3.2781 1.6472 0.9268  -0.0949 0.3936  89   PRO A N   
530   C CA  . PRO A 89   ? 1.8968 3.3024 1.6838 0.9319  -0.0972 0.4014  89   PRO A CA  
531   C C   . PRO A 89   ? 1.8476 3.2834 1.6505 0.9233  -0.0915 0.3984  89   PRO A C   
532   O O   . PRO A 89   ? 1.8017 3.2347 1.5969 0.9150  -0.0778 0.3965  89   PRO A O   
533   C CB  . PRO A 89   ? 1.9205 3.2956 1.6893 0.9323  -0.0874 0.4049  89   PRO A CB  
534   C CG  . PRO A 89   ? 1.9331 3.2801 1.6761 0.9346  -0.0889 0.4045  89   PRO A CG  
535   C CD  . PRO A 89   ? 1.9393 3.2994 1.6735 0.9254  -0.0868 0.3942  89   PRO A CD  
536   N N   . LYS A 90   ? 1.6919 3.1558 1.5171 0.9251  -0.1020 0.3983  90   LYS A N   
537   C CA  . LYS A 90   ? 1.7433 3.2366 1.5865 0.9191  -0.1009 0.3985  90   LYS A CA  
538   C C   . LYS A 90   ? 1.8564 3.3500 1.7168 0.9253  -0.1059 0.4082  90   LYS A C   
539   O O   . LYS A 90   ? 1.8597 3.3379 1.7116 0.9230  -0.0964 0.4096  90   LYS A O   
540   C CB  . LYS A 90   ? 1.6259 3.1465 1.4899 0.9215  -0.1130 0.3974  90   LYS A CB  
541   C CG  . LYS A 90   ? 1.7007 3.2239 1.5543 0.9170  -0.1111 0.3869  90   LYS A CG  
542   C CD  . LYS A 90   ? 1.6505 3.1738 1.4818 0.9025  -0.0938 0.3764  90   LYS A CD  
543   C CE  . LYS A 90   ? 1.6604 3.1716 1.4720 0.8984  -0.0894 0.3655  90   LYS A CE  
544   N NZ  . LYS A 90   ? 1.6949 3.2192 1.4938 0.8840  -0.0761 0.3519  90   LYS A NZ  
545   N N   . GLN A 91   ? 3.9911 5.5015 3.8762 0.9331  -0.1205 0.4143  91   GLN A N   
546   C CA  . GLN A 91   ? 4.1623 5.6775 4.0665 0.9380  -0.1264 0.4226  91   GLN A CA  
547   C C   . GLN A 91   ? 4.3465 5.8357 4.2448 0.9439  -0.1234 0.4260  91   GLN A C   
548   O O   . GLN A 91   ? 4.3468 5.8189 4.2440 0.9550  -0.1315 0.4288  91   GLN A O   
549   C CB  . GLN A 91   ? 4.1425 5.6712 4.0705 0.9481  -0.1435 0.4282  91   GLN A CB  
550   C CG  . GLN A 91   ? 4.1740 5.7306 4.1143 0.9435  -0.1482 0.4267  91   GLN A CG  
551   C CD  . GLN A 91   ? 4.2173 5.7928 4.1593 0.9315  -0.1407 0.4271  91   GLN A CD  
552   O OE1 . GLN A 91   ? 4.2628 5.8498 4.1949 0.9213  -0.1324 0.4205  91   GLN A OE1 
553   N NE2 . GLN A 91   ? 4.1995 5.7790 4.1533 0.9315  -0.1430 0.4340  91   GLN A NE2 
554   N N   . LEU A 92   ? 2.8317 4.3190 2.7274 0.9362  -0.1118 0.4254  92   LEU A N   
555   C CA  . LEU A 92   ? 3.0027 4.4667 2.8962 0.9413  -0.1079 0.4278  92   LEU A CA  
556   C C   . LEU A 92   ? 3.0948 4.5682 3.0106 0.9426  -0.1111 0.4322  92   LEU A C   
557   O O   . LEU A 92   ? 3.0802 4.5366 2.9980 0.9463  -0.1073 0.4329  92   LEU A O   
558   C CB  . LEU A 92   ? 3.0968 4.5435 2.9677 0.9318  -0.0895 0.4220  92   LEU A CB  
559   C CG  . LEU A 92   ? 3.1831 4.6135 3.0270 0.9290  -0.0830 0.4166  92   LEU A CG  
560   C CD1 . LEU A 92   ? 3.2365 4.6568 3.0608 0.9159  -0.0624 0.4098  92   LEU A CD1 
561   C CD2 . LEU A 92   ? 3.1841 4.5873 3.0190 0.9420  -0.0916 0.4207  92   LEU A CD2 
562   N N   . PRO A 93   ? 3.4031 4.9026 3.3361 0.9394  -0.1182 0.4348  93   PRO A N   
563   C CA  . PRO A 93   ? 3.4380 4.9454 3.3894 0.9382  -0.1198 0.4380  93   PRO A CA  
564   C C   . PRO A 93   ? 3.4619 4.9568 3.4271 0.9530  -0.1315 0.4421  93   PRO A C   
565   O O   . PRO A 93   ? 3.4584 4.9623 3.4361 0.9607  -0.1450 0.4462  93   PRO A O   
566   C CB  . PRO A 93   ? 3.4195 4.9559 3.3833 0.9324  -0.1270 0.4412  93   PRO A CB  
567   C CG  . PRO A 93   ? 3.4486 4.9936 3.4003 0.9285  -0.1257 0.4381  93   PRO A CG  
568   C CD  . PRO A 93   ? 3.4553 4.9768 3.3928 0.9374  -0.1258 0.4353  93   PRO A CD  
569   N N   . GLY A 94   ? 3.6723 5.1472 3.6363 0.9570  -0.1262 0.4407  94   GLY A N   
570   C CA  . GLY A 94   ? 3.6655 5.1304 3.6441 0.9706  -0.1368 0.4436  94   GLY A CA  
571   C C   . GLY A 94   ? 3.6544 5.1391 3.6549 0.9694  -0.1444 0.4460  94   GLY A C   
572   O O   . GLY A 94   ? 3.6653 5.1662 3.6699 0.9566  -0.1378 0.4450  94   GLY A O   
573   N N   . GLY A 95   ? 3.2651 4.7486 3.2788 0.9819  -0.1578 0.4490  95   GLY A N   
574   C CA  . GLY A 95   ? 3.2319 4.7325 3.2652 0.9812  -0.1654 0.4512  95   GLY A CA  
575   C C   . GLY A 95   ? 3.2484 4.7652 3.2841 0.9812  -0.1743 0.4554  95   GLY A C   
576   O O   . GLY A 95   ? 3.2238 4.7431 3.2713 0.9909  -0.1860 0.4579  95   GLY A O   
577   N N   . GLN A 96   ? 3.5136 5.0422 3.5395 0.9706  -0.1688 0.4555  96   GLN A N   
578   C CA  . GLN A 96   ? 3.5014 5.0443 3.5299 0.9716  -0.1771 0.4587  96   GLN A CA  
579   C C   . GLN A 96   ? 3.5339 5.0645 3.5605 0.9850  -0.1853 0.4582  96   GLN A C   
580   O O   . GLN A 96   ? 3.5740 5.0863 3.5877 0.9891  -0.1812 0.4553  96   GLN A O   
581   C CB  . GLN A 96   ? 3.4871 5.0402 3.5016 0.9600  -0.1688 0.4566  96   GLN A CB  
582   C CG  . GLN A 96   ? 3.4525 5.0193 3.4699 0.9620  -0.1770 0.4582  96   GLN A CG  
583   C CD  . GLN A 96   ? 3.4775 5.0559 3.4820 0.9506  -0.1686 0.4547  96   GLN A CD  
584   O OE1 . GLN A 96   ? 3.4985 5.0768 3.4918 0.9397  -0.1563 0.4517  96   GLN A OE1 
585   N NE2 . GLN A 96   ? 3.4813 5.0706 3.4884 0.9526  -0.1748 0.4542  96   GLN A NE2 
586   N N   . ASN A 97   ? 4.1504 5.6902 4.1900 0.9916  -0.1967 0.4610  97   ASN A N   
587   C CA  . ASN A 97   ? 4.1315 5.6626 4.1696 1.0024  -0.2040 0.4597  97   ASN A CA  
588   C C   . ASN A 97   ? 4.0866 5.6213 4.1122 0.9982  -0.2013 0.4565  97   ASN A C   
589   O O   . ASN A 97   ? 4.0797 5.6264 4.1151 1.0002  -0.2082 0.4568  97   ASN A O   
590   C CB  . ASN A 97   ? 4.1380 5.6777 4.1970 1.0105  -0.2160 0.4626  97   ASN A CB  
591   C CG  . ASN A 97   ? 4.1483 5.6862 4.2205 1.0138  -0.2184 0.4644  97   ASN A CG  
592   O OD1 . ASN A 97   ? 4.1521 5.6791 4.2190 1.0130  -0.2126 0.4625  97   ASN A OD1 
593   N ND2 . ASN A 97   ? 4.1281 5.6763 4.2186 1.0171  -0.2265 0.4672  97   ASN A ND2 
594   N N   . PRO A 98   ? 4.4872 6.0112 4.4918 0.9922  -0.1907 0.4526  98   PRO A N   
595   C CA  . PRO A 98   ? 4.4129 5.9437 4.4057 0.9850  -0.1860 0.4483  98   PRO A CA  
596   C C   . PRO A 98   ? 4.2455 5.7673 4.2323 0.9917  -0.1911 0.4448  98   PRO A C   
597   O O   . PRO A 98   ? 4.2452 5.7543 4.2339 1.0011  -0.1972 0.4463  98   PRO A O   
598   C CB  . PRO A 98   ? 4.5129 6.0317 4.4842 0.9763  -0.1716 0.4447  98   PRO A CB  
599   C CG  . PRO A 98   ? 4.5086 6.0108 4.4813 0.9815  -0.1702 0.4473  98   PRO A CG  
600   C CD  . PRO A 98   ? 4.4843 5.9865 4.4746 0.9938  -0.1837 0.4512  98   PRO A CD  
601   N N   . VAL A 99   ? 4.1950 5.7246 4.1749 0.9861  -0.1885 0.4394  99   VAL A N   
602   C CA  . VAL A 99   ? 4.0245 5.5427 3.9921 0.9887  -0.1896 0.4339  99   VAL A CA  
603   C C   . VAL A 99   ? 3.7536 5.2753 3.7384 0.9985  -0.2020 0.4350  99   VAL A C   
604   O O   . VAL A 99   ? 3.7680 5.2878 3.7478 0.9985  -0.2036 0.4292  99   VAL A O   
605   C CB  . VAL A 99   ? 4.0973 5.5886 4.0407 0.9894  -0.1830 0.4335  99   VAL A CB  
606   C CG1 . VAL A 99   ? 4.1434 5.6216 4.0704 0.9902  -0.1839 0.4282  99   VAL A CG1 
607   C CG2 . VAL A 99   ? 4.1392 5.6261 4.0660 0.9790  -0.1690 0.4314  99   VAL A CG2 
608   N N   . SER A 100  ? 2.0263 3.5533 2.0312 1.0057  -0.2099 0.4412  100  SER A N   
609   C CA  . SER A 100  ? 1.7589 3.2895 1.7808 1.0147  -0.2205 0.4416  100  SER A CA  
610   C C   . SER A 100  ? 1.5553 3.1042 1.5929 1.0130  -0.2245 0.4379  100  SER A C   
611   O O   . SER A 100  ? 1.5574 3.1222 1.6145 1.0132  -0.2284 0.4419  100  SER A O   
612   C CB  . SER A 100  ? 1.6569 3.1905 1.6976 1.0216  -0.2269 0.4482  100  SER A CB  
613   O OG  . SER A 100  ? 1.6403 3.1665 1.6735 1.0190  -0.2210 0.4515  100  SER A OG  
614   N N   . TYR A 101  ? 2.3802 3.9266 2.4098 1.0111  -0.2236 0.4302  101  TYR A N   
615   C CA  . TYR A 101  ? 2.1932 3.7565 2.2384 1.0090  -0.2264 0.4241  101  TYR A CA  
616   C C   . TYR A 101  ? 2.1320 3.7014 2.1649 0.9988  -0.2182 0.4169  101  TYR A C   
617   O O   . TYR A 101  ? 2.1411 3.7126 2.1649 0.9931  -0.2121 0.4194  101  TYR A O   
618   C CB  . TYR A 101  ? 2.0833 3.6652 2.1590 1.0134  -0.2341 0.4296  101  TYR A CB  
619   C CG  . TYR A 101  ? 2.0091 3.5897 2.1030 1.0229  -0.2424 0.4335  101  TYR A CG  
620   C CD1 . TYR A 101  ? 1.9955 3.5870 2.1123 1.0267  -0.2484 0.4301  101  TYR A CD1 
621   C CD2 . TYR A 101  ? 1.9780 3.5475 2.0679 1.0278  -0.2438 0.4396  101  TYR A CD2 
622   C CE1 . TYR A 101  ? 1.9608 3.5518 2.0942 1.0346  -0.2547 0.4328  101  TYR A CE1 
623   C CE2 . TYR A 101  ? 1.9457 3.5155 2.0523 1.0359  -0.2508 0.4420  101  TYR A CE2 
624   C CZ  . TYR A 101  ? 1.9431 3.5235 2.0707 1.0390  -0.2560 0.4386  101  TYR A CZ  
625   O OH  . TYR A 101  ? 1.9102 3.4913 2.0543 1.0464  -0.2618 0.4401  101  TYR A OH  
626   N N   . VAL A 102  ? 2.2974 3.8711 2.3308 0.9954  -0.2175 0.4070  102  VAL A N   
627   C CA  . VAL A 102  ? 2.2827 3.8660 2.3087 0.9857  -0.2101 0.3985  102  VAL A CA  
628   C C   . VAL A 102  ? 2.2931 3.8925 2.3382 0.9842  -0.2131 0.3886  102  VAL A C   
629   O O   . VAL A 102  ? 2.2579 3.8591 2.3199 0.9899  -0.2197 0.3870  102  VAL A O   
630   C CB  . VAL A 102  ? 2.2910 3.8558 2.2817 0.9770  -0.1989 0.3920  102  VAL A CB  
631   C CG1 . VAL A 102  ? 2.2714 3.8168 2.2433 0.9790  -0.1954 0.4008  102  VAL A CG1 
632   C CG2 . VAL A 102  ? 2.2987 3.8531 2.2794 0.9752  -0.1987 0.3829  102  VAL A CG2 
633   N N   . TYR A 103  ? 2.7510 4.3632 2.7942 0.9761  -0.2075 0.3812  103  TYR A N   
634   C CA  . TYR A 103  ? 2.7621 4.3913 2.8232 0.9732  -0.2087 0.3695  103  TYR A CA  
635   C C   . TYR A 103  ? 2.7911 4.4118 2.8265 0.9621  -0.1979 0.3549  103  TYR A C   
636   O O   . TYR A 103  ? 2.7644 4.3791 2.7750 0.9540  -0.1884 0.3525  103  TYR A O   
637   C CB  . TYR A 103  ? 2.8886 4.5428 2.9723 0.9732  -0.2123 0.3719  103  TYR A CB  
638   C CG  . TYR A 103  ? 2.9267 4.5925 3.0434 0.9838  -0.2246 0.3828  103  TYR A CG  
639   C CD1 . TYR A 103  ? 2.9720 4.6284 3.0882 0.9902  -0.2289 0.3967  103  TYR A CD1 
640   C CD2 . TYR A 103  ? 2.9633 4.6487 3.1122 0.9871  -0.2314 0.3787  103  TYR A CD2 
641   C CE1 . TYR A 103  ? 2.9666 4.6318 3.1108 0.9989  -0.2393 0.4063  103  TYR A CE1 
642   C CE2 . TYR A 103  ? 2.9572 4.6509 3.1353 0.9966  -0.2422 0.3893  103  TYR A CE2 
643   C CZ  . TYR A 103  ? 2.9648 4.6478 3.1391 1.0021  -0.2459 0.4031  103  TYR A CZ  
644   O OH  . TYR A 103  ? 2.9432 4.6327 3.1444 1.0105  -0.2557 0.4131  103  TYR A OH  
645   N N   . LEU A 104  ? 1.5706 3.1898 1.6114 0.9609  -0.1990 0.3449  104  LEU A N   
646   C CA  . LEU A 104  ? 1.6296 3.2414 1.6483 0.9493  -0.1895 0.3295  104  LEU A CA  
647   C C   . LEU A 104  ? 1.6291 3.2662 1.6739 0.9457  -0.1898 0.3167  104  LEU A C   
648   O O   . LEU A 104  ? 1.5490 3.2012 1.6281 0.9531  -0.1987 0.3176  104  LEU A O   
649   C CB  . LEU A 104  ? 1.6213 3.2180 1.6330 0.9499  -0.1916 0.3263  104  LEU A CB  
650   C CG  . LEU A 104  ? 1.6399 3.2201 1.6205 0.9378  -0.1826 0.3135  104  LEU A CG  
651   C CD1 . LEU A 104  ? 1.6865 3.2441 1.6267 0.9321  -0.1736 0.3177  104  LEU A CD1 
652   C CD2 . LEU A 104  ? 1.6087 3.1787 1.5896 0.9407  -0.1882 0.3139  104  LEU A CD2 
653   N N   . GLU A 105  ? 2.2262 3.8678 2.2560 0.9343  -0.1799 0.3040  105  GLU A N   
654   C CA  . GLU A 105  ? 2.2703 3.9386 2.3271 0.9313  -0.1806 0.2915  105  GLU A CA  
655   C C   . GLU A 105  ? 2.3199 3.9879 2.3628 0.9174  -0.1700 0.2697  105  GLU A C   
656   O O   . GLU A 105  ? 2.3651 4.0163 2.3712 0.9071  -0.1588 0.2645  105  GLU A O   
657   C CB  . GLU A 105  ? 2.3073 3.9926 2.3703 0.9320  -0.1809 0.2977  105  GLU A CB  
658   C CG  . GLU A 105  ? 2.3147 4.0314 2.4161 0.9346  -0.1874 0.2914  105  GLU A CG  
659   C CD  . GLU A 105  ? 2.3322 4.0656 2.4444 0.9391  -0.1928 0.3045  105  GLU A CD  
660   O OE1 . GLU A 105  ? 2.3795 4.1132 2.4683 0.9312  -0.1844 0.3039  105  GLU A OE1 
661   O OE2 . GLU A 105  ? 2.2977 4.0439 2.4414 0.9497  -0.2052 0.3152  105  GLU A OE2 
662   N N   . VAL A 106  ? 2.3151 4.0018 2.3887 0.9169  -0.1731 0.2566  106  VAL A N   
663   C CA  . VAL A 106  ? 2.3568 4.0478 2.4228 0.9029  -0.1631 0.2334  106  VAL A CA  
664   C C   . VAL A 106  ? 2.3577 4.0804 2.4567 0.9025  -0.1648 0.2224  106  VAL A C   
665   O O   . VAL A 106  ? 2.3234 4.0636 2.4529 0.9140  -0.1754 0.2338  106  VAL A O   
666   C CB  . VAL A 106  ? 2.3438 4.0274 2.4151 0.8996  -0.1634 0.2233  106  VAL A CB  
667   C CG1 . VAL A 106  ? 2.3936 4.0795 2.4528 0.8825  -0.1515 0.1981  106  VAL A CG1 
668   C CG2 . VAL A 106  ? 2.3567 4.0111 2.3977 0.9016  -0.1640 0.2363  106  VAL A CG2 
669   N N   . VAL A 107  ? 2.2007 3.9306 2.2929 0.8890  -0.1546 0.2001  107  VAL A N   
670   C CA  . VAL A 107  ? 2.2003 3.9615 2.3229 0.8877  -0.1556 0.1870  107  VAL A CA  
671   C C   . VAL A 107  ? 2.2050 3.9731 2.3334 0.8746  -0.1471 0.1594  107  VAL A C   
672   O O   . VAL A 107  ? 2.2329 3.9795 2.3295 0.8627  -0.1372 0.1499  107  VAL A O   
673   C CB  . VAL A 107  ? 2.3148 4.0833 2.4178 0.8828  -0.1493 0.1887  107  VAL A CB  
674   C CG1 . VAL A 107  ? 2.3129 4.1165 2.4503 0.8832  -0.1525 0.1768  107  VAL A CG1 
675   C CG2 . VAL A 107  ? 2.2934 4.0532 2.3870 0.8931  -0.1556 0.2146  107  VAL A CG2 
676   N N   . SER A 108  ? 1.8342 3.6321 2.0037 0.8767  -0.1514 0.1467  108  SER A N   
677   C CA  . SER A 108  ? 1.8848 3.6938 2.0653 0.8639  -0.1431 0.1180  108  SER A CA  
678   C C   . SER A 108  ? 1.9467 3.7920 2.1777 0.8698  -0.1502 0.1075  108  SER A C   
679   O O   . SER A 108  ? 1.9403 3.8005 2.1954 0.8838  -0.1623 0.1242  108  SER A O   
680   C CB  . SER A 108  ? 1.8658 3.6602 2.0490 0.8605  -0.1423 0.1116  108  SER A CB  
681   O OG  . SER A 108  ? 1.8140 3.6045 2.0192 0.8765  -0.1553 0.1320  108  SER A OG  
682   N N   . LYS A 109  ? 2.9619 4.8212 3.2085 0.8585  -0.1429 0.0796  109  LYS A N   
683   C CA  . LYS A 109  ? 3.0095 4.9039 3.3066 0.8635  -0.1492 0.0663  109  LYS A CA  
684   C C   . LYS A 109  ? 3.0074 4.9121 3.3557 0.8789  -0.1634 0.0741  109  LYS A C   
685   O O   . LYS A 109  ? 2.9904 4.9206 3.3812 0.8908  -0.1746 0.0775  109  LYS A O   
686   C CB  . LYS A 109  ? 3.0478 4.9539 3.3463 0.8454  -0.1357 0.0315  109  LYS A CB  
687   C CG  . LYS A 109  ? 3.0830 4.9704 3.3685 0.8317  -0.1258 0.0148  109  LYS A CG  
688   C CD  . LYS A 109  ? 3.0018 4.9006 3.3385 0.8398  -0.1344 0.0102  109  LYS A CD  
689   C CE  . LYS A 109  ? 2.9905 4.8721 3.3130 0.8245  -0.1240 -0.0067 109  LYS A CE  
690   N NZ  . LYS A 109  ? 3.0046 4.9028 3.3416 0.8070  -0.1123 -0.0429 109  LYS A NZ  
691   N N   . HIS A 110  ? 3.0960 4.9809 3.4401 0.8785  -0.1627 0.0771  110  HIS A N   
692   C CA  . HIS A 110  ? 3.0805 4.9744 3.4732 0.8895  -0.1723 0.0783  110  HIS A CA  
693   C C   . HIS A 110  ? 2.9941 4.8799 3.3966 0.9083  -0.1865 0.1096  110  HIS A C   
694   O O   . HIS A 110  ? 2.9560 4.8514 3.4023 0.9201  -0.1962 0.1142  110  HIS A O   
695   C CB  . HIS A 110  ? 3.1602 5.0405 3.5462 0.8766  -0.1627 0.0606  110  HIS A CB  
696   C CG  . HIS A 110  ? 3.2071 5.0940 3.6394 0.8858  -0.1701 0.0609  110  HIS A CG  
697   N ND1 . HIS A 110  ? 3.2366 5.1061 3.6593 0.8799  -0.1658 0.0585  110  HIS A ND1 
698   C CD2 . HIS A 110  ? 3.2080 5.1167 3.6966 0.9002  -0.1813 0.0633  110  HIS A CD2 
699   C CE1 . HIS A 110  ? 3.2111 5.0918 3.6824 0.8898  -0.1729 0.0585  110  HIS A CE1 
700   N NE2 . HIS A 110  ? 3.1930 5.0964 3.7051 0.9026  -0.1824 0.0617  110  HIS A NE2 
701   N N   . PHE A 111  ? 2.6720 4.5401 3.0341 0.9103  -0.1868 0.1301  111  PHE A N   
702   C CA  . PHE A 111  ? 2.5726 4.4290 2.9359 0.9255  -0.1981 0.1588  111  PHE A CA  
703   C C   . PHE A 111  ? 2.4862 4.3218 2.7988 0.9232  -0.1945 0.1756  111  PHE A C   
704   O O   . PHE A 111  ? 2.4837 4.3146 2.7621 0.9107  -0.1836 0.1660  111  PHE A O   
705   C CB  . PHE A 111  ? 2.5683 4.4109 2.9422 0.9281  -0.1993 0.1600  111  PHE A CB  
706   C CG  . PHE A 111  ? 2.5435 4.3861 2.9455 0.9458  -0.2129 0.1824  111  PHE A CG  
707   C CD1 . PHE A 111  ? 2.5239 4.3861 2.9797 0.9555  -0.2215 0.1794  111  PHE A CD1 
708   C CD2 . PHE A 111  ? 2.5395 4.3620 2.9149 0.9523  -0.2168 0.2057  111  PHE A CD2 
709   C CE1 . PHE A 111  ? 2.4889 4.3493 2.9689 0.9710  -0.2332 0.1999  111  PHE A CE1 
710   C CE2 . PHE A 111  ? 2.4978 4.3199 2.8976 0.9673  -0.2284 0.2251  111  PHE A CE2 
711   C CZ  . PHE A 111  ? 2.4735 4.3138 2.9246 0.9764  -0.2364 0.2225  111  PHE A CZ  
712   N N   . SER A 112  ? 1.8926 3.7156 2.2017 0.9349  -0.2030 0.1999  112  SER A N   
713   C CA  . SER A 112  ? 1.8513 3.6523 2.1160 0.9337  -0.1999 0.2163  112  SER A CA  
714   C C   . SER A 112  ? 1.8040 3.5908 2.0737 0.9463  -0.2091 0.2380  112  SER A C   
715   O O   . SER A 112  ? 1.7688 3.5677 2.0759 0.9584  -0.2203 0.2472  112  SER A O   
716   C CB  . SER A 112  ? 1.8230 3.6358 2.0776 0.9337  -0.2003 0.2235  112  SER A CB  
717   O OG  . SER A 112  ? 1.8328 3.6266 2.0388 0.9238  -0.1893 0.2247  112  SER A OG  
718   N N   . LYS A 113  ? 1.7933 3.5543 2.0261 0.9434  -0.2044 0.2456  113  LYS A N   
719   C CA  . LYS A 113  ? 1.7125 3.4596 1.9476 0.9542  -0.2121 0.2640  113  LYS A CA  
720   C C   . LYS A 113  ? 1.6791 3.4000 1.8701 0.9520  -0.2077 0.2754  113  LYS A C   
721   O O   . LYS A 113  ? 1.7036 3.4126 1.8592 0.9409  -0.1975 0.2678  113  LYS A O   
722   C CB  . LYS A 113  ? 1.6979 3.4451 1.9582 0.9562  -0.2143 0.2559  113  LYS A CB  
723   C CG  . LYS A 113  ? 1.6942 3.4304 1.9621 0.9675  -0.2222 0.2729  113  LYS A CG  
724   C CD  . LYS A 113  ? 1.6865 3.4363 1.9895 0.9811  -0.2337 0.2876  113  LYS A CD  
725   C CE  . LYS A 113  ? 1.6592 3.3980 1.9708 0.9909  -0.2399 0.3012  113  LYS A CE  
726   N NZ  . LYS A 113  ? 1.6193 3.3661 1.9672 0.9933  -0.2415 0.2910  113  LYS A NZ  
727   N N   . SER A 114  ? 1.9147 3.6267 2.1095 0.9627  -0.2153 0.2934  114  SER A N   
728   C CA  . SER A 114  ? 1.9862 3.6782 2.1476 0.9639  -0.2137 0.3077  114  SER A CA  
729   C C   . SER A 114  ? 1.9623 3.6463 2.1353 0.9756  -0.2226 0.3233  114  SER A C   
730   O O   . SER A 114  ? 1.9064 3.6006 2.1128 0.9823  -0.2293 0.3229  114  SER A O   
731   C CB  . SER A 114  ? 2.0349 3.7352 2.1891 0.9632  -0.2130 0.3152  114  SER A CB  
732   O OG  . SER A 114  ? 2.0309 3.7567 2.2204 0.9673  -0.2196 0.3138  114  SER A OG  
733   N N   . LYS A 115  ? 2.0698 3.7363 2.2172 0.9780  -0.2221 0.3362  115  LYS A N   
734   C CA  . LYS A 115  ? 2.0358 3.6917 2.1886 0.9870  -0.2285 0.3470  115  LYS A CA  
735   C C   . LYS A 115  ? 2.0386 3.6800 2.1711 0.9915  -0.2296 0.3627  115  LYS A C   
736   O O   . LYS A 115  ? 2.0529 3.6869 2.1595 0.9860  -0.2233 0.3644  115  LYS A O   
737   C CB  . LYS A 115  ? 2.0459 3.6900 2.1873 0.9827  -0.2252 0.3369  115  LYS A CB  
738   C CG  . LYS A 115  ? 1.9924 3.6236 2.1311 0.9901  -0.2302 0.3464  115  LYS A CG  
739   C CD  . LYS A 115  ? 1.9209 3.5598 2.0860 0.9924  -0.2337 0.3392  115  LYS A CD  
740   C CE  . LYS A 115  ? 1.8783 3.5027 2.0319 0.9968  -0.2367 0.3454  115  LYS A CE  
741   N NZ  . LYS A 115  ? 1.8233 3.4561 2.0032 0.9989  -0.2396 0.3388  115  LYS A NZ  
742   N N   . ARG A 116  ? 2.5081 4.1459 2.6538 1.0009  -0.2368 0.3731  116  ARG A N   
743   C CA  . ARG A 116  ? 2.5595 4.1834 2.6892 1.0054  -0.2380 0.3863  116  ARG A CA  
744   C C   . ARG A 116  ? 2.5705 4.1782 2.6892 1.0088  -0.2392 0.3868  116  ARG A C   
745   O O   . ARG A 116  ? 2.5647 4.1771 2.7034 1.0131  -0.2439 0.3840  116  ARG A O   
746   C CB  . ARG A 116  ? 2.5618 4.1958 2.7158 1.0133  -0.2456 0.3985  116  ARG A CB  
747   C CG  . ARG A 116  ? 2.6012 4.2222 2.7475 1.0193  -0.2483 0.4098  116  ARG A CG  
748   C CD  . ARG A 116  ? 2.6301 4.2474 2.7907 1.0264  -0.2535 0.4094  116  ARG A CD  
749   N NE  . ARG A 116  ? 2.6483 4.2665 2.8236 1.0338  -0.2593 0.4204  116  ARG A NE  
750   C CZ  . ARG A 116  ? 2.6552 4.2694 2.8410 1.0403  -0.2633 0.4218  116  ARG A CZ  
751   N NH1 . ARG A 116  ? 2.6668 4.2766 2.8500 1.0405  -0.2627 0.4135  116  ARG A NH1 
752   N NH2 . ARG A 116  ? 2.6348 4.2498 2.8327 1.0456  -0.2676 0.4310  116  ARG A NH2 
753   N N   . MET A 117  ? 2.4835 4.0729 2.5719 1.0072  -0.2354 0.3906  117  MET A N   
754   C CA  . MET A 117  ? 2.4739 4.0467 2.5459 1.0089  -0.2362 0.3900  117  MET A CA  
755   C C   . MET A 117  ? 2.4613 4.0149 2.5060 1.0102  -0.2337 0.3984  117  MET A C   
756   O O   . MET A 117  ? 2.4737 4.0192 2.4955 1.0033  -0.2262 0.3968  117  MET A O   
757   C CB  . MET A 117  ? 2.5206 4.0897 2.5779 0.9997  -0.2311 0.3768  117  MET A CB  
758   C CG  . MET A 117  ? 2.5699 4.1380 2.6084 0.9897  -0.2222 0.3706  117  MET A CG  
759   S SD  . MET A 117  ? 2.6252 4.1937 2.6513 0.9764  -0.2149 0.3521  117  MET A SD  
760   C CE  . MET A 117  ? 2.0916 3.6774 2.1551 0.9804  -0.2219 0.3454  117  MET A CE  
761   N N   . PRO A 118  ? 1.8869 3.4330 1.9345 1.0187  -0.2394 0.4062  118  PRO A N   
762   C CA  . PRO A 118  ? 1.8795 3.4102 1.9094 1.0216  -0.2378 0.4148  118  PRO A CA  
763   C C   . PRO A 118  ? 1.9192 3.4310 1.9144 1.0147  -0.2301 0.4124  118  PRO A C   
764   O O   . PRO A 118  ? 1.9252 3.4335 1.9076 1.0082  -0.2274 0.4041  118  PRO A O   
765   C CB  . PRO A 118  ? 1.8477 3.3732 1.8848 1.0309  -0.2455 0.4191  118  PRO A CB  
766   C CG  . PRO A 118  ? 1.8120 3.3549 1.8785 1.0340  -0.2509 0.4157  118  PRO A CG  
767   C CD  . PRO A 118  ? 1.8438 3.3968 1.9138 1.0259  -0.2470 0.4063  118  PRO A CD  
768   N N   . ILE A 119  ? 2.1347 3.6344 2.1153 1.0151  -0.2260 0.4188  119  ILE A N   
769   C CA  . ILE A 119  ? 2.1525 3.6308 2.0998 1.0095  -0.2185 0.4175  119  ILE A CA  
770   C C   . ILE A 119  ? 2.1217 3.5834 2.0599 1.0157  -0.2186 0.4263  119  ILE A C   
771   O O   . ILE A 119  ? 2.0582 3.5279 2.0160 1.0220  -0.2225 0.4320  119  ILE A O   
772   C CB  . ILE A 119  ? 2.1684 3.6498 2.1032 0.9984  -0.2076 0.4118  119  ILE A CB  
773   C CG1 . ILE A 119  ? 2.1365 3.6091 2.0607 0.9971  -0.2005 0.4176  119  ILE A CG1 
774   C CG2 . ILE A 119  ? 2.1436 3.6508 2.1031 0.9955  -0.2090 0.4067  119  ILE A CG2 
775   C CD1 . ILE A 119  ? 2.1826 3.6509 2.0847 0.9852  -0.1877 0.4113  119  ILE A CD1 
776   N N   . THR A 120  ? 1.6374 3.0759 1.5467 1.0135  -0.2142 0.4270  120  THR A N   
777   C CA  . THR A 120  ? 1.6482 3.0695 1.5501 1.0200  -0.2143 0.4348  120  THR A CA  
778   C C   . THR A 120  ? 1.6719 3.0713 1.5439 1.0132  -0.2033 0.4348  120  THR A C   
779   O O   . THR A 120  ? 1.6803 3.0779 1.5351 1.0025  -0.1945 0.4282  120  THR A O   
780   C CB  . THR A 120  ? 1.6542 3.0669 1.5594 1.0313  -0.2259 0.4398  120  THR A CB  
781   O OG1 . THR A 120  ? 1.6319 3.0652 1.5657 1.0369  -0.2345 0.4390  120  THR A OG1 
782   C CG2 . THR A 120  ? 1.6627 3.0607 1.5670 1.0394  -0.2268 0.4473  120  THR A CG2 
783   N N   . TYR A 121  ? 2.1877 4.0795 2.0566 0.9246  -0.0421 -0.4340 121  TYR A N   
784   C CA  . TYR A 121  ? 2.1898 4.0845 2.0806 0.8841  -0.0495 -0.4129 121  TYR A CA  
785   C C   . TYR A 121  ? 2.1015 3.9911 1.9906 0.8869  -0.0538 -0.4148 121  TYR A C   
786   O O   . TYR A 121  ? 2.1186 3.9748 2.0213 0.8562  -0.0619 -0.4169 121  TYR A O   
787   C CB  . TYR A 121  ? 2.2490 4.0751 2.1496 0.8509  -0.0559 -0.4335 121  TYR A CB  
788   C CG  . TYR A 121  ? 2.3001 4.1099 2.1989 0.8480  -0.0527 -0.4421 121  TYR A CG  
789   C CD1 . TYR A 121  ? 2.3472 4.1875 2.2591 0.8242  -0.0540 -0.4152 121  TYR A CD1 
790   C CD2 . TYR A 121  ? 2.2951 4.0567 2.1799 0.8676  -0.0495 -0.4768 121  TYR A CD2 
791   C CE1 . TYR A 121  ? 2.3761 4.2008 2.2857 0.8211  -0.0517 -0.4226 121  TYR A CE1 
792   C CE2 . TYR A 121  ? 2.3157 4.0622 2.1991 0.8644  -0.0466 -0.4839 121  TYR A CE2 
793   C CZ  . TYR A 121  ? 2.3746 4.1529 2.2697 0.8413  -0.0475 -0.4568 121  TYR A CZ  
794   O OH  . TYR A 121  ? 2.4309 4.1946 2.3239 0.8378  -0.0452 -0.4630 121  TYR A OH  
795   N N   . ASP A 122  ? 2.2286 4.1498 2.0997 0.9243  -0.0485 -0.4145 122  ASP A N   
796   C CA  . ASP A 122  ? 2.1520 4.0687 2.0174 0.9321  -0.0525 -0.4179 122  ASP A CA  
797   C C   . ASP A 122  ? 2.1043 4.0934 1.9757 0.9336  -0.0502 -0.3783 122  ASP A C   
798   O O   . ASP A 122  ? 2.1403 4.1624 1.9930 0.9679  -0.0448 -0.3746 122  ASP A O   
799   C CB  . ASP A 122  ? 2.1576 4.0506 1.9952 0.9744  -0.0501 -0.4486 122  ASP A CB  
800   C CG  . ASP A 122  ? 2.1659 4.0027 2.0006 0.9707  -0.0590 -0.4741 122  ASP A CG  
801   O OD1 . ASP A 122  ? 2.1632 3.9628 1.9785 0.9984  -0.0603 -0.5050 122  ASP A OD1 
802   O OD2 . ASP A 122  ? 2.1714 4.0006 2.0242 0.9398  -0.0655 -0.4630 122  ASP A OD2 
803   N N   . ASN A 123  ? 2.4541 4.4659 2.3507 0.8966  -0.0547 -0.3490 123  ASN A N   
804   C CA  . ASN A 123  ? 2.4398 4.5239 2.3468 0.8945  -0.0528 -0.3072 123  ASN A CA  
805   C C   . ASN A 123  ? 2.4508 4.5264 2.3656 0.8785  -0.0609 -0.3010 123  ASN A C   
806   O O   . ASN A 123  ? 2.4621 4.5059 2.3966 0.8400  -0.0708 -0.2994 123  ASN A O   
807   C CB  . ASN A 123  ? 2.4587 4.5814 2.3904 0.8648  -0.0540 -0.2735 123  ASN A CB  
808   C CG  . ASN A 123  ? 2.4593 4.6646 2.4041 0.8655  -0.0508 -0.2267 123  ASN A CG  
809   O OD1 . ASN A 123  ? 2.4797 4.7344 2.4389 0.8581  -0.0480 -0.1969 123  ASN A OD1 
810   N ND2 . ASN A 123  ? 2.4598 4.6812 2.4007 0.8740  -0.0516 -0.2188 123  ASN A ND2 
811   N N   . GLY A 124  ? 1.4928 3.5966 1.3910 0.9089  -0.0567 -0.2974 124  GLY A N   
812   C CA  . GLY A 124  ? 1.5255 3.6308 1.4303 0.8969  -0.0636 -0.2872 124  GLY A CA  
813   C C   . GLY A 124  ? 1.6289 3.6645 1.5215 0.9008  -0.0710 -0.3251 124  GLY A C   
814   O O   . GLY A 124  ? 1.6152 3.6131 1.4864 0.9272  -0.0687 -0.3585 124  GLY A O   
815   N N   . PHE A 125  ? 1.7028 3.7210 1.6100 0.8748  -0.0805 -0.3196 125  PHE A N   
816   C CA  . PHE A 125  ? 1.6792 3.6314 1.5784 0.8763  -0.0883 -0.3538 125  PHE A CA  
817   C C   . PHE A 125  ? 1.6728 3.5988 1.5961 0.8364  -0.0995 -0.3468 125  PHE A C   
818   O O   . PHE A 125  ? 1.6744 3.6420 1.6172 0.8125  -0.1020 -0.3118 125  PHE A O   
819   C CB  . PHE A 125  ? 1.6753 3.6453 1.5487 0.9148  -0.0857 -0.3587 125  PHE A CB  
820   C CG  . PHE A 125  ? 1.6842 3.7065 1.5357 0.9535  -0.0735 -0.3492 125  PHE A CG  
821   C CD1 . PHE A 125  ? 1.7043 3.8056 1.5603 0.9586  -0.0660 -0.3076 125  PHE A CD1 
822   C CD2 . PHE A 125  ? 1.6728 3.6662 1.5008 0.9842  -0.0695 -0.3804 125  PHE A CD2 
823   C CE1 . PHE A 125  ? 1.7195 3.8713 1.5558 0.9957  -0.0534 -0.2976 125  PHE A CE1 
824   C CE2 . PHE A 125  ? 1.6983 3.7396 1.5053 1.0212  -0.0580 -0.3718 125  PHE A CE2 
825   C CZ  . PHE A 125  ? 1.7234 3.8445 1.5340 1.0276  -0.0493 -0.3303 125  PHE A CZ  
826   N N   . LEU A 126  ? 1.3431 3.1991 1.2658 0.8297  -0.1067 -0.3801 126  LEU A N   
827   C CA  . LEU A 126  ? 1.3344 3.1566 1.2789 0.7934  -0.1175 -0.3783 126  LEU A CA  
828   C C   . LEU A 126  ? 1.3446 3.1407 1.2810 0.8052  -0.1240 -0.3935 126  LEU A C   
829   O O   . LEU A 126  ? 1.3519 3.1039 1.2725 0.8270  -0.1248 -0.4268 126  LEU A O   
830   C CB  . LEU A 126  ? 1.3209 3.0814 1.2794 0.7644  -0.1211 -0.3991 126  LEU A CB  
831   C CG  . LEU A 126  ? 1.3096 3.0826 1.2847 0.7344  -0.1208 -0.3802 126  LEU A CG  
832   C CD1 . LEU A 126  ? 1.3087 3.1504 1.2981 0.7189  -0.1225 -0.3348 126  LEU A CD1 
833   C CD2 . LEU A 126  ? 1.3082 3.0811 1.2713 0.7511  -0.1119 -0.3924 126  LEU A CD2 
834   N N   . PHE A 127  ? 1.3460 3.1710 1.2941 0.7902  -0.1295 -0.3673 127  PHE A N   
835   C CA  . PHE A 127  ? 1.3558 3.1639 1.2987 0.7977  -0.1365 -0.3751 127  PHE A CA  
836   C C   . PHE A 127  ? 1.3450 3.1105 1.3134 0.7585  -0.1476 -0.3764 127  PHE A C   
837   O O   . PHE A 127  ? 1.3373 3.1281 1.3266 0.7286  -0.1513 -0.3476 127  PHE A O   
838   C CB  . PHE A 127  ? 1.3681 3.2473 1.3034 0.8132  -0.1336 -0.3411 127  PHE A CB  
839   C CG  . PHE A 127  ? 1.3844 3.3050 1.2899 0.8579  -0.1224 -0.3409 127  PHE A CG  
840   C CD1 . PHE A 127  ? 1.3929 3.2749 1.2751 0.8870  -0.1198 -0.3769 127  PHE A CD1 
841   C CD2 . PHE A 127  ? 1.3928 3.3907 1.2936 0.8714  -0.1148 -0.3041 127  PHE A CD2 
842   C CE1 . PHE A 127  ? 1.4108 3.3287 1.2635 0.9295  -0.1101 -0.3775 127  PHE A CE1 
843   C CE2 . PHE A 127  ? 1.4103 3.4457 1.2819 0.9145  -0.1036 -0.3041 127  PHE A CE2 
844   C CZ  . PHE A 127  ? 1.4198 3.4141 1.2665 0.9436  -0.1016 -0.3415 127  PHE A CZ  
845   N N   . ILE A 128  ? 1.3456 3.0462 1.3131 0.7588  -0.1537 -0.4094 128  ILE A N   
846   C CA  . ILE A 128  ? 1.3359 2.9900 1.3276 0.7228  -0.1634 -0.4139 128  ILE A CA  
847   C C   . ILE A 128  ? 1.3434 2.9874 1.3383 0.7218  -0.1726 -0.4131 128  ILE A C   
848   O O   . ILE A 128  ? 1.3462 2.9364 1.3394 0.7277  -0.1777 -0.4422 128  ILE A O   
849   C CB  . ILE A 128  ? 1.3292 2.9114 1.3243 0.7174  -0.1640 -0.4505 128  ILE A CB  
850   C CG1 . ILE A 128  ? 1.3314 2.9140 1.3072 0.7450  -0.1545 -0.4681 128  ILE A CG1 
851   C CG2 . ILE A 128  ? 1.3165 2.8721 1.3350 0.6771  -0.1674 -0.4448 128  ILE A CG2 
852   C CD1 . ILE A 128  ? 1.3212 2.8442 1.3055 0.7308  -0.1530 -0.4943 128  ILE A CD1 
853   N N   . HIS A 129  ? 1.7762 3.4718 1.7781 0.7127  -0.1752 -0.3786 129  HIS A N   
854   C CA  . HIS A 129  ? 1.8099 3.5053 1.8139 0.7125  -0.1838 -0.3727 129  HIS A CA  
855   C C   . HIS A 129  ? 1.8529 3.4853 1.8795 0.6818  -0.1945 -0.3878 129  HIS A C   
856   O O   . HIS A 129  ? 1.8974 3.5371 1.9458 0.6501  -0.2011 -0.3658 129  HIS A O   
857   C CB  . HIS A 129  ? 1.7862 3.5546 1.7961 0.7061  -0.1835 -0.3281 129  HIS A CB  
858   C CG  . HIS A 129  ? 1.7621 3.5335 1.7804 0.6968  -0.1935 -0.3153 129  HIS A CG  
859   N ND1 . HIS A 129  ? 1.7607 3.5966 1.7837 0.6936  -0.1938 -0.2756 129  HIS A ND1 
860   C CD2 . HIS A 129  ? 1.7552 3.4745 1.7795 0.6893  -0.2035 -0.3352 129  HIS A CD2 
861   C CE1 . HIS A 129  ? 1.7832 3.6061 1.8135 0.6847  -0.2037 -0.2720 129  HIS A CE1 
862   N NE2 . HIS A 129  ? 1.7862 3.5385 1.8175 0.6819  -0.2100 -0.3080 129  HIS A NE2 
863   N N   . THR A 130  ? 1.3473 2.9176 1.3698 0.6908  -0.1966 -0.4248 130  THR A N   
864   C CA  . THR A 130  ? 1.3424 2.8556 1.3857 0.6662  -0.2066 -0.4385 130  THR A CA  
865   C C   . THR A 130  ? 1.3521 2.8917 1.3968 0.6670  -0.2148 -0.4192 130  THR A C   
866   O O   . THR A 130  ? 1.3652 2.9449 1.3886 0.6957  -0.2123 -0.4113 130  THR A O   
867   C CB  . THR A 130  ? 1.3426 2.7883 1.3826 0.6789  -0.2076 -0.4798 130  THR A CB  
868   O OG1 . THR A 130  ? 1.3441 2.7491 1.3992 0.6665  -0.2182 -0.4890 130  THR A OG1 
869   C CG2 . THR A 130  ? 1.3555 2.8120 1.3669 0.7207  -0.2034 -0.4959 130  THR A CG2 
870   N N   . ASP A 131  ? 1.8007 3.3208 1.8688 0.6363  -0.2242 -0.4099 131  ASP A N   
871   C CA  . ASP A 131  ? 1.8125 3.3620 1.8825 0.6361  -0.2321 -0.3884 131  ASP A CA  
872   C C   . ASP A 131  ? 1.8508 3.3740 1.9054 0.6635  -0.2367 -0.4122 131  ASP A C   
873   O O   . ASP A 131  ? 1.8725 3.4356 1.9058 0.6901  -0.2358 -0.4022 131  ASP A O   
874   C CB  . ASP A 131  ? 1.8169 3.3459 1.9159 0.5974  -0.2424 -0.3752 131  ASP A CB  
875   C CG  . ASP A 131  ? 1.8299 3.2976 1.9387 0.5934  -0.2514 -0.4005 131  ASP A CG  
876   O OD1 . ASP A 131  ? 1.8192 3.2316 1.9310 0.5936  -0.2493 -0.4314 131  ASP A OD1 
877   O OD2 . ASP A 131  ? 1.8564 3.3317 1.9698 0.5914  -0.2603 -0.3896 131  ASP A OD2 
878   N N   . LYS A 132  ? 1.3655 2.8209 1.4312 0.6566  -0.2420 -0.4428 132  LYS A N   
879   C CA  . LYS A 132  ? 1.3771 2.7973 1.4309 0.6810  -0.2479 -0.4695 132  LYS A CA  
880   C C   . LYS A 132  ? 1.3712 2.7387 1.4239 0.6896  -0.2436 -0.5047 132  LYS A C   
881   O O   . LYS A 132  ? 1.3577 2.7112 1.4220 0.6719  -0.2371 -0.5074 132  LYS A O   
882   C CB  . LYS A 132  ? 1.5144 2.9049 1.5873 0.6638  -0.2608 -0.4693 132  LYS A CB  
883   C CG  . LYS A 132  ? 1.4388 2.7741 1.5427 0.6305  -0.2646 -0.4802 132  LYS A CG  
884   C CD  . LYS A 132  ? 1.3937 2.7318 1.5179 0.6053  -0.2753 -0.4598 132  LYS A CD  
885   C CE  . LYS A 132  ? 1.3706 2.6441 1.5237 0.5783  -0.2811 -0.4761 132  LYS A CE  
886   N NZ  . LYS A 132  ? 1.4371 2.7193 1.6111 0.5488  -0.2902 -0.4511 132  LYS A NZ  
887   N N   . PRO A 133  ? 1.3830 2.7222 1.4207 0.7173  -0.2476 -0.5307 133  PRO A N   
888   C CA  . PRO A 133  ? 1.3807 2.6817 1.4122 0.7325  -0.2429 -0.5611 133  PRO A CA  
889   C C   . PRO A 133  ? 1.3797 2.6145 1.4291 0.7266  -0.2521 -0.5874 133  PRO A C   
890   O O   . PRO A 133  ? 1.3874 2.5904 1.4270 0.7491  -0.2544 -0.6136 133  PRO A O   
891   C CB  . PRO A 133  ? 1.4007 2.7288 1.3975 0.7730  -0.2425 -0.5664 133  PRO A CB  
892   C CG  . PRO A 133  ? 1.4158 2.7621 1.4067 0.7781  -0.2530 -0.5526 133  PRO A CG  
893   C CD  . PRO A 133  ? 1.4020 2.7461 1.4242 0.7394  -0.2572 -0.5329 133  PRO A CD  
894   N N   . VAL A 134  ? 1.5628 2.7788 1.6383 0.6974  -0.2581 -0.5790 134  VAL A N   
895   C CA  . VAL A 134  ? 1.5192 2.6694 1.6202 0.6833  -0.2635 -0.6018 134  VAL A CA  
896   C C   . VAL A 134  ? 1.5856 2.7195 1.7162 0.6467  -0.2673 -0.5886 134  VAL A C   
897   O O   . VAL A 134  ? 1.6582 2.8228 1.7914 0.6360  -0.2733 -0.5648 134  VAL A O   
898   C CB  . VAL A 134  ? 1.5503 2.6694 1.6450 0.7070  -0.2746 -0.6236 134  VAL A CB  
899   C CG1 . VAL A 134  ? 1.5557 2.6222 1.6816 0.6868  -0.2836 -0.6340 134  VAL A CG1 
900   C CG2 . VAL A 134  ? 1.5235 2.6201 1.6047 0.7319  -0.2705 -0.6498 134  VAL A CG2 
901   N N   . TYR A 135  ? 1.4619 2.5465 1.6142 0.6284  -0.2634 -0.6043 135  TYR A N   
902   C CA  . TYR A 135  ? 1.4564 2.5199 1.6349 0.5944  -0.2654 -0.5946 135  TYR A CA  
903   C C   . TYR A 135  ? 1.4405 2.4376 1.6442 0.5858  -0.2685 -0.6183 135  TYR A C   
904   O O   . TYR A 135  ? 1.4483 2.4111 1.6526 0.6010  -0.2656 -0.6431 135  TYR A O   
905   C CB  . TYR A 135  ? 1.4529 2.5293 1.6321 0.5751  -0.2553 -0.5833 135  TYR A CB  
906   C CG  . TYR A 135  ? 1.4577 2.6007 1.6163 0.5812  -0.2516 -0.5577 135  TYR A CG  
907   C CD1 . TYR A 135  ? 1.4856 2.6652 1.6502 0.5596  -0.2556 -0.5270 135  TYR A CD1 
908   C CD2 . TYR A 135  ? 1.4360 2.6055 1.5706 0.6086  -0.2443 -0.5634 135  TYR A CD2 
909   C CE1 . TYR A 135  ? 1.4904 2.7336 1.6391 0.5650  -0.2519 -0.5013 135  TYR A CE1 
910   C CE2 . TYR A 135  ? 1.4416 2.6738 1.5586 0.6154  -0.2399 -0.5390 135  TYR A CE2 
911   C CZ  . TYR A 135  ? 1.4679 2.7382 1.5928 0.5936  -0.2434 -0.5073 135  TYR A CZ  
912   O OH  . TYR A 135  ? 1.4734 2.8089 1.5830 0.6012  -0.2386 -0.4812 135  TYR A OH  
913   N N   . THR A 136  ? 1.5983 2.5787 1.8238 0.5607  -0.2746 -0.6086 136  THR A N   
914   C CA  . THR A 136  ? 1.6112 2.5318 1.8639 0.5492  -0.2773 -0.6264 136  THR A CA  
915   C C   . THR A 136  ? 1.5139 2.4141 1.7816 0.5190  -0.2708 -0.6204 136  THR A C   
916   O O   . THR A 136  ? 1.6456 2.5812 1.9050 0.5049  -0.2691 -0.5986 136  THR A O   
917   C CB  . THR A 136  ? 1.5197 2.4375 1.7845 0.5461  -0.2913 -0.6194 136  THR A CB  
918   O OG1 . THR A 136  ? 1.5534 2.5156 1.8135 0.5310  -0.2955 -0.5896 136  THR A OG1 
919   C CG2 . THR A 136  ? 1.6398 2.5684 1.8883 0.5771  -0.2989 -0.6290 136  THR A CG2 
920   N N   . PRO A 137  ? 1.6655 2.5085 1.9554 0.5091  -0.2676 -0.6389 137  PRO A N   
921   C CA  . PRO A 137  ? 1.6487 2.4674 1.9484 0.4834  -0.2602 -0.6363 137  PRO A CA  
922   C C   . PRO A 137  ? 1.6890 2.5376 1.9878 0.4594  -0.2662 -0.6084 137  PRO A C   
923   O O   . PRO A 137  ? 1.7042 2.5620 2.0128 0.4521  -0.2774 -0.5956 137  PRO A O   
924   C CB  . PRO A 137  ? 1.6853 2.4442 2.0134 0.4756  -0.2613 -0.6532 137  PRO A CB  
925   C CG  . PRO A 137  ? 1.6227 2.3682 1.9533 0.5012  -0.2635 -0.6724 137  PRO A CG  
926   C CD  . PRO A 137  ? 1.6349 2.4327 1.9433 0.5198  -0.2716 -0.6609 137  PRO A CD  
927   N N   . ASP A 138  ? 1.8898 2.7532 2.1774 0.4471  -0.2595 -0.5986 138  ASP A N   
928   C CA  . ASP A 138  ? 1.9365 2.8137 2.2277 0.4194  -0.2653 -0.5749 138  ASP A CA  
929   C C   . ASP A 138  ? 1.9909 2.9341 2.2697 0.4198  -0.2725 -0.5457 138  ASP A C   
930   O O   . ASP A 138  ? 2.0212 2.9810 2.3047 0.3968  -0.2795 -0.5229 138  ASP A O   
931   C CB  . ASP A 138  ? 2.1038 2.9392 2.4196 0.4004  -0.2731 -0.5762 138  ASP A CB  
932   C CG  . ASP A 138  ? 2.1734 2.9469 2.5005 0.3891  -0.2646 -0.5959 138  ASP A CG  
933   O OD1 . ASP A 138  ? 2.2046 2.9734 2.5215 0.3765  -0.2585 -0.5930 138  ASP A OD1 
934   O OD2 . ASP A 138  ? 2.1712 2.9012 2.5171 0.3931  -0.2642 -0.6135 138  ASP A OD2 
935   N N   . GLN A 139  ? 1.5244 2.5059 1.7874 0.4459  -0.2712 -0.5453 139  GLN A N   
936   C CA  . GLN A 139  ? 1.5389 2.5860 1.7889 0.4472  -0.2755 -0.5162 139  GLN A CA  
937   C C   . GLN A 139  ? 1.5709 2.6430 1.8083 0.4399  -0.2677 -0.5054 139  GLN A C   
938   O O   . GLN A 139  ? 1.5629 2.6043 1.7967 0.4412  -0.2584 -0.5240 139  GLN A O   
939   C CB  . GLN A 139  ? 1.5362 2.6178 1.7701 0.4792  -0.2763 -0.5180 139  GLN A CB  
940   C CG  . GLN A 139  ? 1.5379 2.6009 1.7821 0.4872  -0.2866 -0.5253 139  GLN A CG  
941   C CD  . GLN A 139  ? 1.5312 2.6371 1.7545 0.5170  -0.2893 -0.5205 139  GLN A CD  
942   O OE1 . GLN A 139  ? 1.4779 2.5689 1.6905 0.5428  -0.2872 -0.5427 139  GLN A OE1 
943   N NE2 . GLN A 139  ? 1.5682 2.7277 1.7851 0.5137  -0.2944 -0.4908 139  GLN A NE2 
944   N N   . SER A 140  ? 1.6892 2.8163 1.9214 0.4312  -0.2721 -0.4744 140  SER A N   
945   C CA  . SER A 140  ? 1.7007 2.8618 1.9200 0.4285  -0.2655 -0.4614 140  SER A CA  
946   C C   . SER A 140  ? 1.6423 2.8613 1.8409 0.4583  -0.2597 -0.4537 140  SER A C   
947   O O   . SER A 140  ? 1.6398 2.9085 1.8353 0.4641  -0.2648 -0.4303 140  SER A O   
948   C CB  . SER A 140  ? 1.7498 2.9328 1.9788 0.3971  -0.2742 -0.4306 140  SER A CB  
949   O OG  . SER A 140  ? 1.7584 2.9361 1.9818 0.3841  -0.2693 -0.4292 140  SER A OG  
950   N N   . VAL A 141  ? 1.3842 2.5952 1.5682 0.4778  -0.2487 -0.4735 141  VAL A N   
951   C CA  . VAL A 141  ? 1.3154 2.5769 1.4778 0.5066  -0.2418 -0.4684 141  VAL A CA  
952   C C   . VAL A 141  ? 1.3475 2.6737 1.5050 0.4982  -0.2415 -0.4334 141  VAL A C   
953   O O   . VAL A 141  ? 1.3423 2.6749 1.4960 0.4905  -0.2357 -0.4299 141  VAL A O   
954   C CB  . VAL A 141  ? 1.3536 2.5883 1.5040 0.5238  -0.2304 -0.4960 141  VAL A CB  
955   C CG1 . VAL A 141  ? 1.3187 2.6059 1.4460 0.5523  -0.2229 -0.4896 141  VAL A CG1 
956   C CG2 . VAL A 141  ? 1.3227 2.5004 1.4782 0.5360  -0.2306 -0.5286 141  VAL A CG2 
957   N N   . LYS A 142  ? 1.5969 2.9718 1.7555 0.4993  -0.2477 -0.4063 142  LYS A N   
958   C CA  . LYS A 142  ? 1.6408 3.0843 1.7938 0.4983  -0.2456 -0.3727 142  LYS A CA  
959   C C   . LYS A 142  ? 1.6523 3.1224 1.7824 0.5296  -0.2331 -0.3817 142  LYS A C   
960   O O   . LYS A 142  ? 1.6652 3.1190 1.7809 0.5580  -0.2289 -0.4059 142  LYS A O   
961   C CB  . LYS A 142  ? 1.6338 3.1281 1.7899 0.5000  -0.2526 -0.3427 142  LYS A CB  
962   C CG  . LYS A 142  ? 1.6776 3.1689 1.8577 0.4638  -0.2653 -0.3193 142  LYS A CG  
963   C CD  . LYS A 142  ? 1.6942 3.2571 1.8775 0.4622  -0.2696 -0.2780 142  LYS A CD  
964   C CE  . LYS A 142  ? 1.7377 3.2945 1.9464 0.4248  -0.2837 -0.2549 142  LYS A CE  
965   N NZ  . LYS A 142  ? 1.7519 3.2382 1.9715 0.4128  -0.2909 -0.2810 142  LYS A NZ  
966   N N   . VAL A 143  ? 1.4058 2.9148 1.5329 0.5244  -0.2281 -0.3625 143  VAL A N   
967   C CA  . VAL A 143  ? 1.3669 2.9061 1.4728 0.5544  -0.2163 -0.3679 143  VAL A CA  
968   C C   . VAL A 143  ? 1.3391 2.9340 1.4467 0.5451  -0.2131 -0.3367 143  VAL A C   
969   O O   . VAL A 143  ? 1.3701 2.9599 1.4942 0.5129  -0.2194 -0.3212 143  VAL A O   
970   C CB  . VAL A 143  ? 1.3775 2.8604 1.4756 0.5640  -0.2095 -0.4057 143  VAL A CB  
971   C CG1 . VAL A 143  ? 1.3344 2.7660 1.4493 0.5309  -0.2135 -0.4138 143  VAL A CG1 
972   C CG2 . VAL A 143  ? 1.3195 2.8353 1.3994 0.5865  -0.1982 -0.4060 143  VAL A CG2 
973   N N   . ARG A 144  ? 1.3184 2.9668 1.4087 0.5740  -0.2041 -0.3267 144  ARG A N   
974   C CA  . ARG A 144  ? 1.3157 3.0165 1.4070 0.5695  -0.1992 -0.2997 144  ARG A CA  
975   C C   . ARG A 144  ? 1.3168 3.0373 1.3850 0.6044  -0.1861 -0.3125 144  ARG A C   
976   O O   . ARG A 144  ? 1.3188 3.0013 1.3717 0.6274  -0.1818 -0.3458 144  ARG A O   
977   C CB  . ARG A 144  ? 1.3403 3.1096 1.4419 0.5621  -0.2034 -0.2559 144  ARG A CB  
978   C CG  . ARG A 144  ? 1.3585 3.1450 1.4545 0.5789  -0.2059 -0.2508 144  ARG A CG  
979   C CD  . ARG A 144  ? 1.3857 3.2516 1.4894 0.5769  -0.2064 -0.2042 144  ARG A CD  
980   N NE  . ARG A 144  ? 1.3976 3.2930 1.4899 0.6006  -0.2057 -0.1961 144  ARG A NE  
981   C CZ  . ARG A 144  ? 1.4366 3.3473 1.5436 0.5844  -0.2152 -0.1732 144  ARG A CZ  
982   N NH1 . ARG A 144  ? 1.4565 3.3555 1.5910 0.5444  -0.2268 -0.1561 144  ARG A NH1 
983   N NH2 . ARG A 144  ? 1.4472 3.3840 1.5405 0.6085  -0.2138 -0.1671 144  ARG A NH2 
984   N N   . VAL A 145  ? 1.3161 3.0958 1.3833 0.6077  -0.1803 -0.2852 145  VAL A N   
985   C CA  . VAL A 145  ? 1.3180 3.1221 1.3642 0.6406  -0.1677 -0.2936 145  VAL A CA  
986   C C   . VAL A 145  ? 1.3218 3.2100 1.3664 0.6526  -0.1613 -0.2551 145  VAL A C   
987   O O   . VAL A 145  ? 1.3175 3.2412 1.3815 0.6269  -0.1655 -0.2221 145  VAL A O   
988   C CB  . VAL A 145  ? 1.3100 3.0729 1.3549 0.6329  -0.1642 -0.3161 145  VAL A CB  
989   C CG1 . VAL A 145  ? 1.3109 3.1195 1.3417 0.6573  -0.1527 -0.3085 145  VAL A CG1 
990   C CG2 . VAL A 145  ? 1.3099 3.0015 1.3455 0.6434  -0.1640 -0.3595 145  VAL A CG2 
991   N N   . TYR A 146  ? 1.5240 3.4432 1.5451 0.6929  -0.1517 -0.2594 146  TYR A N   
992   C CA  . TYR A 146  ? 1.5308 3.5289 1.5457 0.7128  -0.1422 -0.2272 146  TYR A CA  
993   C C   . TYR A 146  ? 1.5670 3.5639 1.5679 0.7319  -0.1320 -0.2428 146  TYR A C   
994   O O   . TYR A 146  ? 1.5742 3.5209 1.5580 0.7496  -0.1295 -0.2809 146  TYR A O   
995   C CB  . TYR A 146  ? 1.5739 3.6055 1.5686 0.7473  -0.1377 -0.2223 146  TYR A CB  
996   C CG  . TYR A 146  ? 1.5605 3.5715 1.5652 0.7309  -0.1489 -0.2199 146  TYR A CG  
997   C CD1 . TYR A 146  ? 1.6022 3.6353 1.6350 0.6953  -0.1577 -0.1869 146  TYR A CD1 
998   C CD2 . TYR A 146  ? 1.5805 3.5476 1.5679 0.7495  -0.1521 -0.2504 146  TYR A CD2 
999   C CE1 . TYR A 146  ? 1.6087 3.6218 1.6518 0.6794  -0.1685 -0.1844 146  TYR A CE1 
1000  C CE2 . TYR A 146  ? 1.5750 3.5228 1.5728 0.7337  -0.1628 -0.2478 146  TYR A CE2 
1001  C CZ  . TYR A 146  ? 1.5828 3.5538 1.6083 0.6989  -0.1706 -0.2149 146  TYR A CZ  
1002  O OH  . TYR A 146  ? 1.5661 3.5174 1.6023 0.6832  -0.1817 -0.2120 146  TYR A OH  
1003  N N   . SER A 147  ? 1.7400 3.7920 1.7497 0.7277  -0.1267 -0.2127 147  SER A N   
1004  C CA  . SER A 147  ? 1.7740 3.8257 1.7739 0.7412  -0.1181 -0.2247 147  SER A CA  
1005  C C   . SER A 147  ? 1.8011 3.9348 1.7984 0.7619  -0.1073 -0.1908 147  SER A C   
1006  O O   . SER A 147  ? 1.8192 4.0069 1.8374 0.7434  -0.1096 -0.1501 147  SER A O   
1007  C CB  . SER A 147  ? 1.8077 3.8193 1.8263 0.7035  -0.1252 -0.2300 147  SER A CB  
1008  O OG  . SER A 147  ? 1.8445 3.9007 1.8878 0.6739  -0.1311 -0.1892 147  SER A OG  
1009  N N   . LEU A 148  ? 2.2764 4.4185 2.2485 0.8006  -0.0957 -0.2076 148  LEU A N   
1010  C CA  . LEU A 148  ? 2.2866 4.5044 2.2524 0.8267  -0.0834 -0.1792 148  LEU A CA  
1011  C C   . LEU A 148  ? 2.3666 4.5773 2.3247 0.8380  -0.0762 -0.1935 148  LEU A C   
1012  O O   . LEU A 148  ? 2.4085 4.5549 2.3564 0.8389  -0.0783 -0.2316 148  LEU A O   
1013  C CB  . LEU A 148  ? 2.2619 4.5065 2.1992 0.8710  -0.0748 -0.1826 148  LEU A CB  
1014  C CG  . LEU A 148  ? 2.2497 4.5599 2.1967 0.8702  -0.0738 -0.1409 148  LEU A CG  
1015  C CD1 . LEU A 148  ? 2.2374 4.5250 2.2133 0.8246  -0.0886 -0.1292 148  LEU A CD1 
1016  C CD2 . LEU A 148  ? 2.2551 4.5755 2.1704 0.9114  -0.0678 -0.1506 148  LEU A CD2 
1017  N N   . ASN A 149  ? 2.2043 4.4828 2.1689 0.8464  -0.0678 -0.1610 149  ASN A N   
1018  C CA  . ASN A 149  ? 2.1997 4.4834 2.1552 0.8634  -0.0592 -0.1702 149  ASN A CA  
1019  C C   . ASN A 149  ? 2.1815 4.4966 2.1060 0.9161  -0.0453 -0.1773 149  ASN A C   
1020  O O   . ASN A 149  ? 2.1554 4.5043 2.0691 0.9367  -0.0414 -0.1644 149  ASN A O   
1021  C CB  . ASN A 149  ? 2.2610 4.5997 2.2433 0.8410  -0.0589 -0.1300 149  ASN A CB  
1022  C CG  . ASN A 149  ? 2.3153 4.7386 2.3095 0.8480  -0.0538 -0.0826 149  ASN A CG  
1023  O OD1 . ASN A 149  ? 2.3117 4.7466 2.3012 0.8554  -0.0544 -0.0759 149  ASN A OD1 
1024  N ND2 . ASN A 149  ? 2.3600 4.8439 2.3710 0.8454  -0.0487 -0.0482 149  ASN A ND2 
1025  N N   . ASP A 150  ? 1.7260 4.0270 1.6347 0.9380  -0.0384 -0.1987 150  ASP A N   
1026  C CA  . ASP A 150  ? 1.7666 4.1014 1.6466 0.9879  -0.0249 -0.2026 150  ASP A CA  
1027  C C   . ASP A 150  ? 1.7432 4.1575 1.6218 1.0074  -0.0163 -0.1634 150  ASP A C   
1028  O O   . ASP A 150  ? 1.7498 4.1753 1.5987 1.0476  -0.0090 -0.1726 150  ASP A O   
1029  C CB  . ASP A 150  ? 1.7935 4.1479 1.6760 0.9951  -0.0175 -0.1986 150  ASP A CB  
1030  C CG  . ASP A 150  ? 1.9948 4.4013 1.9122 0.9620  -0.0190 -0.1553 150  ASP A CG  
1031  O OD1 . ASP A 150  ? 1.9944 4.4601 1.9151 0.9782  -0.0088 -0.1305 150  ASP A OD1 
1032  O OD2 . ASP A 150  ? 2.0138 4.4019 1.9556 0.9198  -0.0310 -0.1451 150  ASP A OD2 
1033  N N   . ASP A 151  ? 2.2779 4.7481 2.1876 0.9806  -0.0171 -0.1191 151  ASP A N   
1034  C CA  . ASP A 151  ? 2.3364 4.8897 2.2485 0.9988  -0.0074 -0.0767 151  ASP A CA  
1035  C C   . ASP A 151  ? 2.3147 4.8667 2.2284 0.9894  -0.0141 -0.0681 151  ASP A C   
1036  O O   . ASP A 151  ? 2.3434 4.9622 2.2647 0.9961  -0.0082 -0.0293 151  ASP A O   
1037  C CB  . ASP A 151  ? 2.3996 5.0202 2.3468 0.9760  -0.0053 -0.0288 151  ASP A CB  
1038  C CG  . ASP A 151  ? 2.4548 5.1442 2.3926 1.0149  0.0124  -0.0080 151  ASP A CG  
1039  O OD1 . ASP A 151  ? 2.5166 5.2126 2.4193 1.0618  0.0241  -0.0242 151  ASP A OD1 
1040  O OD2 . ASP A 151  ? 2.4289 5.1659 2.3946 0.9983  0.0140  0.0254  151  ASP A OD2 
1041  N N   . LEU A 152  ? 1.6141 4.0906 1.5219 0.9737  -0.0262 -0.1033 152  LEU A N   
1042  C CA  . LEU A 152  ? 1.6378 4.1030 1.5460 0.9644  -0.0340 -0.1007 152  LEU A CA  
1043  C C   . LEU A 152  ? 1.6744 4.1966 1.6176 0.9323  -0.0379 -0.0506 152  LEU A C   
1044  O O   . LEU A 152  ? 1.6687 4.2365 1.6094 0.9441  -0.0343 -0.0252 152  LEU A O   
1045  C CB  . LEU A 152  ? 1.6515 4.1242 1.5205 1.0127  -0.0258 -0.1146 152  LEU A CB  
1046  C CG  . LEU A 152  ? 1.6657 4.0741 1.4986 1.0441  -0.0256 -0.1663 152  LEU A CG  
1047  C CD1 . LEU A 152  ? 1.6410 3.9632 1.4843 1.0129  -0.0397 -0.2032 152  LEU A CD1 
1048  C CD2 . LEU A 152  ? 1.7082 4.1394 1.5218 1.0795  -0.0125 -0.1722 152  LEU A CD2 
1049  N N   . LYS A 153  ? 2.0066 4.5252 1.9820 0.8920  -0.0460 -0.0365 153  LYS A N   
1050  C CA  . LYS A 153  ? 2.0141 4.5704 2.0265 0.8531  -0.0548 0.0064  153  LYS A CA  
1051  C C   . LYS A 153  ? 2.0207 4.5085 2.0534 0.8053  -0.0728 -0.0104 153  LYS A C   
1052  O O   . LYS A 153  ? 1.9788 4.4006 2.0002 0.8025  -0.0758 -0.0501 153  LYS A O   
1053  C CB  . LYS A 153  ? 2.0670 4.6997 2.1014 0.8509  -0.0476 0.0500  153  LYS A CB  
1054  C CG  . LYS A 153  ? 2.0857 4.8047 2.1174 0.8807  -0.0340 0.0895  153  LYS A CG  
1055  C CD  . LYS A 153  ? 2.1354 4.9302 2.1907 0.8800  -0.0261 0.1324  153  LYS A CD  
1056  C CE  . LYS A 153  ? 2.1667 5.0516 2.2227 0.9084  -0.0117 0.1760  153  LYS A CE  
1057  N NZ  . LYS A 153  ? 2.1700 5.0599 2.1812 0.9640  0.0046  0.1540  153  LYS A NZ  
1058  N N   . PRO A 154  ? 1.7227 4.2258 1.7853 0.7683  -0.0847 0.0201  154  PRO A N   
1059  C CA  . PRO A 154  ? 1.7756 4.2119 1.8538 0.7260  -0.1024 0.0041  154  PRO A CA  
1060  C C   . PRO A 154  ? 1.8018 4.1649 1.8723 0.7153  -0.1063 -0.0366 154  PRO A C   
1061  O O   . PRO A 154  ? 1.8161 4.1080 1.8790 0.7053  -0.1137 -0.0714 154  PRO A O   
1062  C CB  . PRO A 154  ? 1.7826 4.2640 1.8989 0.6875  -0.1127 0.0518  154  PRO A CB  
1063  C CG  . PRO A 154  ? 1.7889 4.3586 1.9081 0.7120  -0.1015 0.0930  154  PRO A CG  
1064  C CD  . PRO A 154  ? 1.7624 4.3511 1.8485 0.7632  -0.0823 0.0753  154  PRO A CD  
1065  N N   . ALA A 155  ? 3.1293 5.5119 3.2024 0.7181  -0.1008 -0.0308 155  ALA A N   
1066  C CA  . ALA A 155  ? 3.1528 5.4744 3.2163 0.7133  -0.1019 -0.0671 155  ALA A CA  
1067  C C   . ALA A 155  ? 3.2138 5.4804 3.2972 0.6654  -0.1185 -0.0728 155  ALA A C   
1068  O O   . ALA A 155  ? 3.2125 5.4075 3.2854 0.6586  -0.1216 -0.1112 155  ALA A O   
1069  C CB  . ALA A 155  ? 3.1172 5.3857 3.1486 0.7454  -0.0952 -0.1145 155  ALA A CB  
1070  N N   . LYS A 156  ? 1.5835 3.8844 1.6955 0.6329  -0.1293 -0.0337 156  LYS A N   
1071  C CA  . LYS A 156  ? 1.5964 3.8487 1.7269 0.5868  -0.1467 -0.0349 156  LYS A CA  
1072  C C   . LYS A 156  ? 1.5672 3.7586 1.6856 0.5816  -0.1467 -0.0699 156  LYS A C   
1073  O O   . LYS A 156  ? 1.5722 3.7851 1.6820 0.6007  -0.1370 -0.0714 156  LYS A O   
1074  C CB  . LYS A 156  ? 1.6559 3.9648 1.8183 0.5566  -0.1572 0.0159  156  LYS A CB  
1075  C CG  . LYS A 156  ? 1.6699 4.0411 1.8471 0.5598  -0.1575 0.0538  156  LYS A CG  
1076  C CD  . LYS A 156  ? 1.7225 4.1764 1.9284 0.5480  -0.1601 0.1090  156  LYS A CD  
1077  C CE  . LYS A 156  ? 1.7401 4.2587 1.9577 0.5578  -0.1570 0.1453  156  LYS A CE  
1078  N NZ  . LYS A 156  ? 1.7865 4.3932 2.0328 0.5518  -0.1567 0.2012  156  LYS A NZ  
1079  N N   . ARG A 157  ? 2.0831 4.1985 2.2000 0.5579  -0.1565 -0.0983 157  ARG A N   
1080  C CA  . ARG A 157  ? 2.0622 4.1152 2.1678 0.5508  -0.1567 -0.1315 157  ARG A CA  
1081  C C   . ARG A 157  ? 2.0930 4.0681 2.2006 0.5220  -0.1683 -0.1560 157  ARG A C   
1082  O O   . ARG A 157  ? 2.0987 4.0677 2.2160 0.5093  -0.1761 -0.1489 157  ARG A O   
1083  C CB  . ARG A 157  ? 1.9670 4.0045 2.0461 0.5916  -0.1411 -0.1657 157  ARG A CB  
1084  C CG  . ARG A 157  ? 1.9018 4.0035 1.9749 0.6208  -0.1287 -0.1487 157  ARG A CG  
1085  C CD  . ARG A 157  ? 1.8244 3.9017 1.8705 0.6591  -0.1155 -0.1853 157  ARG A CD  
1086  N NE  . ARG A 157  ? 1.8103 3.9547 1.8469 0.6966  -0.1024 -0.1690 157  ARG A NE  
1087  C CZ  . ARG A 157  ? 1.7933 3.9292 1.8050 0.7358  -0.0907 -0.1957 157  ARG A CZ  
1088  N NH1 . ARG A 157  ? 1.7642 3.8282 1.7606 0.7410  -0.0911 -0.2389 157  ARG A NH1 
1089  N NH2 . ARG A 157  ? 1.8036 4.0025 1.8060 0.7701  -0.0789 -0.1787 157  ARG A NH2 
1090  N N   . GLU A 158  ? 2.5577 4.4736 2.6562 0.5122  -0.1691 -0.1843 158  GLU A N   
1091  C CA  . GLU A 158  ? 2.5809 4.4171 2.6770 0.4916  -0.1766 -0.2138 158  GLU A CA  
1092  C C   . GLU A 158  ? 2.5272 4.3140 2.6028 0.5194  -0.1652 -0.2578 158  GLU A C   
1093  O O   . GLU A 158  ? 2.5421 4.3247 2.6035 0.5401  -0.1551 -0.2747 158  GLU A O   
1094  C CB  . GLU A 158  ? 2.6835 4.4806 2.7837 0.4579  -0.1868 -0.2145 158  GLU A CB  
1095  C CG  . GLU A 158  ? 2.7753 4.5958 2.8974 0.4213  -0.2040 -0.1772 158  GLU A CG  
1096  C CD  . GLU A 158  ? 2.8730 4.6271 2.9952 0.3858  -0.2171 -0.1891 158  GLU A CD  
1097  O OE1 . GLU A 158  ? 2.8877 4.5763 3.0021 0.3815  -0.2173 -0.2198 158  GLU A OE1 
1098  O OE2 . GLU A 158  ? 2.9339 4.7006 3.0634 0.3627  -0.2274 -0.1673 158  GLU A OE2 
1099  N N   . THR A 159  ? 1.6546 3.4038 1.7302 0.5191  -0.1678 -0.2755 159  THR A N   
1100  C CA  . THR A 159  ? 1.5499 3.2525 1.6094 0.5444  -0.1591 -0.3154 159  THR A CA  
1101  C C   . THR A 159  ? 1.4433 3.0705 1.5068 0.5229  -0.1658 -0.3404 159  THR A C   
1102  O O   . THR A 159  ? 1.4432 3.0586 1.5211 0.4919  -0.1775 -0.3261 159  THR A O   
1103  C CB  . THR A 159  ? 1.5659 3.2994 1.6193 0.5744  -0.1542 -0.3148 159  THR A CB  
1104  O OG1 . THR A 159  ? 1.5774 3.3890 1.6291 0.5936  -0.1484 -0.2849 159  THR A OG1 
1105  C CG2 . THR A 159  ? 1.5526 3.2427 1.5881 0.6036  -0.1458 -0.3549 159  THR A CG2 
1106  N N   . VAL A 160  ? 1.3035 2.8806 1.3547 0.5408  -0.1583 -0.3776 160  VAL A N   
1107  C CA  . VAL A 160  ? 1.2994 2.8036 1.3538 0.5272  -0.1618 -0.4052 160  VAL A CA  
1108  C C   . VAL A 160  ? 1.2977 2.7777 1.3432 0.5572  -0.1552 -0.4344 160  VAL A C   
1109  O O   . VAL A 160  ? 1.3470 2.8379 1.3784 0.5868  -0.1459 -0.4475 160  VAL A O   
1110  C CB  . VAL A 160  ? 1.3004 2.7483 1.3497 0.5137  -0.1593 -0.4269 160  VAL A CB  
1111  C CG1 . VAL A 160  ? 1.2986 2.6859 1.3414 0.5298  -0.1524 -0.4662 160  VAL A CG1 
1112  C CG2 . VAL A 160  ? 1.3163 2.7345 1.3762 0.4749  -0.1704 -0.4169 160  VAL A CG2 
1113  N N   . LEU A 161  ? 1.7440 3.1883 1.7982 0.5486  -0.1610 -0.4447 161  LEU A N   
1114  C CA  . LEU A 161  ? 1.7236 3.1250 1.7731 0.5691  -0.1574 -0.4769 161  LEU A CA  
1115  C C   . LEU A 161  ? 1.7452 3.0710 1.8005 0.5524  -0.1572 -0.5040 161  LEU A C   
1116  O O   . LEU A 161  ? 1.7767 3.0808 1.8374 0.5246  -0.1602 -0.4986 161  LEU A O   
1117  C CB  . LEU A 161  ? 1.7017 3.1170 1.7569 0.5750  -0.1637 -0.4700 161  LEU A CB  
1118  C CG  . LEU A 161  ? 1.7014 3.1476 1.7711 0.5477  -0.1735 -0.4370 161  LEU A CG  
1119  C CD1 . LEU A 161  ? 1.7235 3.1133 1.8088 0.5168  -0.1821 -0.4448 161  LEU A CD1 
1120  C CD2 . LEU A 161  ? 1.6677 3.1629 1.7352 0.5661  -0.1755 -0.4205 161  LEU A CD2 
1121  N N   . THR A 162  ? 2.0255 3.3114 2.0794 0.5701  -0.1542 -0.5325 162  THR A N   
1122  C CA  . THR A 162  ? 2.0037 3.2215 2.0617 0.5626  -0.1506 -0.5606 162  THR A CA  
1123  C C   . THR A 162  ? 1.9706 3.1502 2.0348 0.5775  -0.1516 -0.5848 162  THR A C   
1124  O O   . THR A 162  ? 1.9453 3.1096 2.0022 0.6024  -0.1462 -0.6064 162  THR A O   
1125  C CB  . THR A 162  ? 2.2831 3.4951 2.3282 0.5745  -0.1408 -0.5729 162  THR A CB  
1126  O OG1 . THR A 162  ? 2.2555 3.4238 2.2990 0.5942  -0.1351 -0.6041 162  THR A OG1 
1127  C CG2 . THR A 162  ? 2.2510 3.5288 2.2830 0.5948  -0.1379 -0.5551 162  THR A CG2 
1128  N N   . PHE A 163  ? 1.9868 3.1501 2.0651 0.5615  -0.1597 -0.5805 163  PHE A N   
1129  C CA  . PHE A 163  ? 1.9539 3.0839 2.0407 0.5732  -0.1629 -0.5998 163  PHE A CA  
1130  C C   . PHE A 163  ? 1.9429 3.0159 2.0322 0.5813  -0.1558 -0.6309 163  PHE A C   
1131  O O   . PHE A 163  ? 1.9706 3.0182 2.0594 0.5683  -0.1497 -0.6364 163  PHE A O   
1132  C CB  . PHE A 163  ? 1.9737 3.0833 2.0781 0.5485  -0.1718 -0.5920 163  PHE A CB  
1133  C CG  . PHE A 163  ? 1.9871 3.1488 2.0927 0.5355  -0.1796 -0.5594 163  PHE A CG  
1134  C CD1 . PHE A 163  ? 2.0192 3.2190 2.1186 0.5234  -0.1788 -0.5367 163  PHE A CD1 
1135  C CD2 . PHE A 163  ? 1.9636 3.1360 2.0781 0.5342  -0.1885 -0.5502 163  PHE A CD2 
1136  C CE1 . PHE A 163  ? 2.0566 3.3057 2.1600 0.5105  -0.1865 -0.5047 163  PHE A CE1 
1137  C CE2 . PHE A 163  ? 1.9907 3.2122 2.1078 0.5217  -0.1956 -0.5185 163  PHE A CE2 
1138  C CZ  . PHE A 163  ? 2.0428 3.3029 2.1552 0.5097  -0.1946 -0.4954 163  PHE A CZ  
1139  N N   . ILE A 164  ? 1.5960 2.6478 1.6883 0.6023  -0.1572 -0.6505 164  ILE A N   
1140  C CA  . ILE A 164  ? 1.6197 2.6226 1.7153 0.6135  -0.1508 -0.6787 164  ILE A CA  
1141  C C   . ILE A 164  ? 1.6352 2.5973 1.7465 0.6206  -0.1561 -0.6972 164  ILE A C   
1142  O O   . ILE A 164  ? 1.6092 2.5818 1.7152 0.6447  -0.1610 -0.7044 164  ILE A O   
1143  C CB  . ILE A 164  ? 1.6467 2.6725 1.7238 0.6421  -0.1453 -0.6863 164  ILE A CB  
1144  C CG1 . ILE A 164  ? 1.6878 2.7478 1.7518 0.6344  -0.1389 -0.6701 164  ILE A CG1 
1145  C CG2 . ILE A 164  ? 1.6446 2.6198 1.7275 0.6552  -0.1406 -0.7152 164  ILE A CG2 
1146  C CD1 . ILE A 164  ? 1.6750 2.7561 1.7214 0.6616  -0.1328 -0.6774 164  ILE A CD1 
1147  N N   . ASP A 165  ? 2.1618 3.0758 2.2920 0.6001  -0.1552 -0.7050 165  ASP A N   
1148  C CA  . ASP A 165  ? 2.2010 3.0753 2.3504 0.6031  -0.1606 -0.7202 165  ASP A CA  
1149  C C   . ASP A 165  ? 2.1024 2.9658 2.2497 0.6328  -0.1620 -0.7402 165  ASP A C   
1150  O O   . ASP A 165  ? 2.0496 2.9208 2.1834 0.6491  -0.1561 -0.7479 165  ASP A O   
1151  C CB  . ASP A 165  ? 2.3332 3.1514 2.5023 0.5812  -0.1554 -0.7301 165  ASP A CB  
1152  C CG  . ASP A 165  ? 2.4395 3.2184 2.6123 0.5903  -0.1450 -0.7518 165  ASP A CG  
1153  O OD1 . ASP A 165  ? 2.4608 3.2516 2.6227 0.6137  -0.1432 -0.7611 165  ASP A OD1 
1154  O OD2 . ASP A 165  ? 2.4869 3.2219 2.6731 0.5741  -0.1385 -0.7591 165  ASP A OD2 
1155  N N   . PRO A 166  ? 1.8832 2.7276 2.0439 0.6397  -0.1711 -0.7484 166  PRO A N   
1156  C CA  . PRO A 166  ? 1.8537 2.6856 2.0139 0.6671  -0.1773 -0.7663 166  PRO A CA  
1157  C C   . PRO A 166  ? 1.8169 2.6085 1.9844 0.6778  -0.1704 -0.7890 166  PRO A C   
1158  O O   . PRO A 166  ? 1.7847 2.5565 1.9571 0.6975  -0.1770 -0.8051 166  PRO A O   
1159  C CB  . PRO A 166  ? 1.8863 2.6964 2.0664 0.6611  -0.1882 -0.7679 166  PRO A CB  
1160  C CG  . PRO A 166  ? 1.9277 2.7665 2.1071 0.6386  -0.1903 -0.7440 166  PRO A CG  
1161  C CD  . PRO A 166  ? 1.9290 2.7717 2.1035 0.6203  -0.1788 -0.7359 166  PRO A CD  
1162  N N   . GLU A 167  ? 2.0127 2.7923 2.1803 0.6653  -0.1581 -0.7896 167  GLU A N   
1163  C CA  . GLU A 167  ? 2.0225 2.7681 2.1959 0.6756  -0.1507 -0.8088 167  GLU A CA  
1164  C C   . GLU A 167  ? 2.0283 2.8012 2.1791 0.6813  -0.1417 -0.8045 167  GLU A C   
1165  O O   . GLU A 167  ? 2.0437 2.8012 2.1923 0.6957  -0.1370 -0.8185 167  GLU A O   
1166  C CB  . GLU A 167  ? 2.0758 2.7689 2.2751 0.6561  -0.1430 -0.8173 167  GLU A CB  
1167  C CG  . GLU A 167  ? 2.1108 2.7688 2.3376 0.6544  -0.1513 -0.8257 167  GLU A CG  
1168  C CD  . GLU A 167  ? 2.1802 2.7870 2.4337 0.6358  -0.1421 -0.8329 167  GLU A CD  
1169  O OE1 . GLU A 167  ? 2.1872 2.7636 2.4496 0.6410  -0.1331 -0.8461 167  GLU A OE1 
1170  O OE2 . GLU A 167  ? 2.2171 2.8136 2.4830 0.6169  -0.1439 -0.8249 167  GLU A OE2 
1171  N N   . GLY A 168  ? 2.2673 3.0810 2.4027 0.6694  -0.1401 -0.7841 168  GLY A N   
1172  C CA  . GLY A 168  ? 2.2810 3.1298 2.3939 0.6768  -0.1338 -0.7768 168  GLY A CA  
1173  C C   . GLY A 168  ? 2.3484 3.1869 2.4605 0.6541  -0.1232 -0.7708 168  GLY A C   
1174  O O   . GLY A 168  ? 2.3565 3.1978 2.4576 0.6606  -0.1154 -0.7748 168  GLY A O   
1175  N N   . SER A 169  ? 1.6596 2.4843 1.7824 0.6278  -0.1237 -0.7614 169  SER A N   
1176  C CA  . SER A 169  ? 1.7435 2.5581 1.8624 0.6045  -0.1157 -0.7539 169  SER A CA  
1177  C C   . SER A 169  ? 1.7383 2.5887 1.8507 0.5843  -0.1217 -0.7288 169  SER A C   
1178  O O   . SER A 169  ? 1.7209 2.5676 1.8450 0.5731  -0.1291 -0.7222 169  SER A O   
1179  C CB  . SER A 169  ? 1.8132 2.5674 1.9512 0.5899  -0.1101 -0.7676 169  SER A CB  
1180  O OG  . SER A 169  ? 1.8856 2.6312 2.0219 0.5623  -0.1085 -0.7555 169  SER A OG  
1181  N N   . GLU A 170  ? 1.5738 2.4581 1.6693 0.5788  -0.1192 -0.7140 170  GLU A N   
1182  C CA  . GLU A 170  ? 1.6010 2.5237 1.6919 0.5602  -0.1261 -0.6878 170  GLU A CA  
1183  C C   . GLU A 170  ? 1.5654 2.4576 1.6722 0.5364  -0.1317 -0.6846 170  GLU A C   
1184  O O   . GLU A 170  ? 1.6365 2.4763 1.7553 0.5318  -0.1275 -0.7020 170  GLU A O   
1185  C CB  . GLU A 170  ? 1.7154 2.6535 1.7921 0.5468  -0.1219 -0.6756 170  GLU A CB  
1186  C CG  . GLU A 170  ? 1.7667 2.7433 1.8270 0.5677  -0.1171 -0.6734 170  GLU A CG  
1187  C CD  . GLU A 170  ? 1.8826 2.8859 1.9306 0.5516  -0.1164 -0.6542 170  GLU A CD  
1188  O OE1 . GLU A 170  ? 1.9578 2.9367 2.0081 0.5246  -0.1184 -0.6483 170  GLU A OE1 
1189  O OE2 . GLU A 170  ? 1.8956 2.9432 1.9314 0.5662  -0.1145 -0.6450 170  GLU A OE2 
1190  N N   . VAL A 171  ? 1.4677 2.3921 1.5754 0.5213  -0.1409 -0.6617 171  VAL A N   
1191  C CA  . VAL A 171  ? 1.4996 2.3940 1.6217 0.4978  -0.1469 -0.6580 171  VAL A CA  
1192  C C   . VAL A 171  ? 1.4974 2.4212 1.6159 0.4727  -0.1554 -0.6306 171  VAL A C   
1193  O O   . VAL A 171  ? 1.5329 2.4292 1.6601 0.4496  -0.1606 -0.6262 171  VAL A O   
1194  C CB  . VAL A 171  ? 1.5321 2.4152 1.6707 0.5077  -0.1528 -0.6660 171  VAL A CB  
1195  C CG1 . VAL A 171  ? 1.5778 2.4378 1.7316 0.4831  -0.1605 -0.6583 171  VAL A CG1 
1196  C CG2 . VAL A 171  ? 1.5043 2.3438 1.6512 0.5255  -0.1456 -0.6939 171  VAL A CG2 
1197  N N   . ASP A 172  ? 1.7784 2.7565 1.8844 0.4769  -0.1569 -0.6117 172  ASP A N   
1198  C CA  . ASP A 172  ? 1.8354 2.8442 1.9404 0.4531  -0.1662 -0.5835 172  ASP A CA  
1199  C C   . ASP A 172  ? 1.8372 2.8993 1.9279 0.4617  -0.1638 -0.5678 172  ASP A C   
1200  O O   . ASP A 172  ? 1.8050 2.8620 1.8850 0.4781  -0.1543 -0.5820 172  ASP A O   
1201  C CB  . ASP A 172  ? 1.8539 2.8893 1.9710 0.4494  -0.1769 -0.5672 172  ASP A CB  
1202  C CG  . ASP A 172  ? 1.9424 2.9946 2.0644 0.4193  -0.1885 -0.5397 172  ASP A CG  
1203  O OD1 . ASP A 172  ? 1.9581 2.9910 2.0937 0.4052  -0.1966 -0.5366 172  ASP A OD1 
1204  O OD2 . ASP A 172  ? 1.9709 3.0555 2.0846 0.4097  -0.1907 -0.5206 172  ASP A OD2 
1205  N N   . MET A 173  ? 1.7195 2.8334 1.8112 0.4513  -0.1726 -0.5379 173  MET A N   
1206  C CA  . MET A 173  ? 1.7027 2.8725 1.7837 0.4582  -0.1710 -0.5187 173  MET A CA  
1207  C C   . MET A 173  ? 1.6911 2.9002 1.7797 0.4350  -0.1831 -0.4849 173  MET A C   
1208  O O   . MET A 173  ? 1.7328 2.9173 1.8324 0.4126  -0.1922 -0.4800 173  MET A O   
1209  C CB  . MET A 173  ? 1.7526 2.8970 1.8221 0.4519  -0.1646 -0.5284 173  MET A CB  
1210  C CG  . MET A 173  ? 1.7567 2.9338 1.8131 0.4765  -0.1555 -0.5309 173  MET A CG  
1211  S SD  . MET A 173  ? 1.9729 3.0996 2.0169 0.4733  -0.1459 -0.5532 173  MET A SD  
1212  C CE  . MET A 173  ? 1.8610 2.9205 1.9115 0.4854  -0.1385 -0.5896 173  MET A CE  
1213  N N   . VAL A 174  ? 1.7270 2.9971 1.8108 0.4403  -0.1835 -0.4609 174  VAL A N   
1214  C CA  . VAL A 174  ? 1.7669 3.0753 1.8590 0.4157  -0.1954 -0.4262 174  VAL A CA  
1215  C C   . VAL A 174  ? 1.7441 3.1289 1.8330 0.4325  -0.1927 -0.4011 174  VAL A C   
1216  O O   . VAL A 174  ? 1.7336 3.1427 1.8153 0.4636  -0.1837 -0.4093 174  VAL A O   
1217  C CB  . VAL A 174  ? 1.8088 3.1111 1.9166 0.3995  -0.2065 -0.4155 174  VAL A CB  
1218  C CG1 . VAL A 174  ? 1.7794 3.0968 1.8890 0.4259  -0.2022 -0.4239 174  VAL A CG1 
1219  C CG2 . VAL A 174  ? 1.8312 3.1812 1.9496 0.3763  -0.2195 -0.3763 174  VAL A CG2 
1220  N N   . GLU A 175  ? 1.7267 3.1480 1.8206 0.4126  -0.2006 -0.3708 175  GLU A N   
1221  C CA  . GLU A 175  ? 1.7163 3.2123 1.8094 0.4264  -0.1978 -0.3436 175  GLU A CA  
1222  C C   . GLU A 175  ? 1.7050 3.2483 1.8153 0.4107  -0.2094 -0.3073 175  GLU A C   
1223  O O   . GLU A 175  ? 1.6998 3.2141 1.8202 0.3927  -0.2186 -0.3079 175  GLU A O   
1224  C CB  . GLU A 175  ? 1.7964 3.2972 1.8835 0.4156  -0.1978 -0.3365 175  GLU A CB  
1225  C CG  . GLU A 175  ? 1.8760 3.3033 1.9581 0.3905  -0.2025 -0.3567 175  GLU A CG  
1226  C CD  . GLU A 175  ? 1.9040 3.3199 1.9718 0.3933  -0.1962 -0.3663 175  GLU A CD  
1227  O OE1 . GLU A 175  ? 1.9065 3.3668 1.9760 0.3861  -0.2005 -0.3404 175  GLU A OE1 
1228  O OE2 . GLU A 175  ? 1.9070 3.2692 1.9629 0.4024  -0.1872 -0.3990 175  GLU A OE2 
1229  N N   . GLU A 176  ? 1.5310 3.1469 1.6456 0.4177  -0.2089 -0.2752 176  GLU A N   
1230  C CA  . GLU A 176  ? 1.4067 3.0677 1.5407 0.3949  -0.2221 -0.2350 176  GLU A CA  
1231  C C   . GLU A 176  ? 1.4659 3.2075 1.6048 0.4041  -0.2193 -0.1998 176  GLU A C   
1232  O O   . GLU A 176  ? 1.4461 3.2061 1.5723 0.4273  -0.2074 -0.2076 176  GLU A O   
1233  C CB  . GLU A 176  ? 1.5270 3.1904 1.6702 0.3964  -0.2264 -0.2313 176  GLU A CB  
1234  C CG  . GLU A 176  ? 1.6047 3.2677 1.7688 0.3594  -0.2447 -0.2044 176  GLU A CG  
1235  C CD  . GLU A 176  ? 1.7962 3.3854 1.9627 0.3426  -0.2519 -0.2293 176  GLU A CD  
1236  O OE1 . GLU A 176  ? 1.8181 3.3456 1.9720 0.3472  -0.2457 -0.2653 176  GLU A OE1 
1237  O OE2 . GLU A 176  ? 1.7843 3.3773 1.9663 0.3246  -0.2638 -0.2120 176  GLU A OE2 
1238  N N   . ILE A 177  ? 2.0033 3.7921 2.1620 0.3851  -0.2306 -0.1604 177  ILE A N   
1239  C CA  . ILE A 177  ? 2.0558 3.9241 2.2244 0.3893  -0.2296 -0.1213 177  ILE A CA  
1240  C C   . ILE A 177  ? 2.0646 3.9989 2.2341 0.4195  -0.2195 -0.1035 177  ILE A C   
1241  O O   . ILE A 177  ? 2.0304 3.9661 2.2058 0.4192  -0.2230 -0.0994 177  ILE A O   
1242  C CB  . ILE A 177  ? 2.1153 4.0011 2.3076 0.3490  -0.2491 -0.0838 177  ILE A CB  
1243  C CG1 . ILE A 177  ? 2.1111 4.0486 2.3241 0.3429  -0.2562 -0.0482 177  ILE A CG1 
1244  C CG2 . ILE A 177  ? 2.1578 3.9627 2.3481 0.3169  -0.2625 -0.1052 177  ILE A CG2 
1245  C CD1 . ILE A 177  ? 2.0796 4.1117 2.3046 0.3581  -0.2502 -0.0063 177  ILE A CD1 
1246  N N   . ASP A 178  ? 2.1709 4.1602 2.3338 0.4461  -0.2070 -0.0923 178  ASP A N   
1247  C CA  . ASP A 178  ? 2.1931 4.2485 2.3549 0.4758  -0.1970 -0.0726 178  ASP A CA  
1248  C C   . ASP A 178  ? 2.2510 4.3836 2.4376 0.4618  -0.2033 -0.0194 178  ASP A C   
1249  O O   . ASP A 178  ? 2.2759 4.4562 2.4676 0.4664  -0.1991 0.0025  178  ASP A O   
1250  C CB  . ASP A 178  ? 2.1429 4.2159 2.2815 0.5181  -0.1785 -0.0912 178  ASP A CB  
1251  C CG  . ASP A 178  ? 2.0563 4.1716 2.1844 0.5531  -0.1679 -0.0862 178  ASP A CG  
1252  O OD1 . ASP A 178  ? 2.0239 4.1467 2.1297 0.5903  -0.1536 -0.1052 178  ASP A OD1 
1253  O OD2 . ASP A 178  ? 2.0308 4.1702 2.1721 0.5433  -0.1744 -0.0632 178  ASP A OD2 
1254  N N   . HIS A 179  ? 2.6962 4.8413 2.8994 0.4448  -0.2135 0.0021  179  HIS A N   
1255  C CA  . HIS A 179  ? 2.7360 4.9562 2.9653 0.4319  -0.2198 0.0547  179  HIS A CA  
1256  C C   . HIS A 179  ? 2.6831 4.9775 2.9060 0.4707  -0.2033 0.0742  179  HIS A C   
1257  O O   . HIS A 179  ? 2.6823 5.0498 2.9193 0.4754  -0.1994 0.1130  179  HIS A O   
1258  C CB  . HIS A 179  ? 2.8291 5.0304 3.0797 0.3962  -0.2386 0.0706  179  HIS A CB  
1259  C CG  . HIS A 179  ? 2.9490 5.2021 3.2315 0.3656  -0.2531 0.1213  179  HIS A CG  
1260  N ND1 . HIS A 179  ? 3.0177 5.2348 3.3152 0.3249  -0.2726 0.1273  179  HIS A ND1 
1261  C CD2 . HIS A 179  ? 2.9872 5.3247 3.2901 0.3698  -0.2516 0.1690  179  HIS A CD2 
1262  C CE1 . HIS A 179  ? 3.0697 5.3460 3.3964 0.3042  -0.2839 0.1766  179  HIS A CE1 
1263  N NE2 . HIS A 179  ? 3.0501 5.4015 3.3820 0.3306  -0.2709 0.2035  179  HIS A NE2 
1264  N N   . ILE A 180  ? 2.2775 4.5531 2.4792 0.4989  -0.1940 0.0480  180  ILE A N   
1265  C CA  . ILE A 180  ? 2.2306 4.5702 2.4208 0.5383  -0.1785 0.0630  180  ILE A CA  
1266  C C   . ILE A 180  ? 2.1414 4.4600 2.2962 0.5822  -0.1618 0.0233  180  ILE A C   
1267  O O   . ILE A 180  ? 2.0789 4.4514 2.2215 0.6159  -0.1469 0.0341  180  ILE A O   
1268  C CB  . ILE A 180  ? 2.0235 4.3812 2.2224 0.5344  -0.1840 0.0816  180  ILE A CB  
1269  C CG1 . ILE A 180  ? 1.9925 4.2685 2.1873 0.5166  -0.1953 0.0471  180  ILE A CG1 
1270  C CG2 . ILE A 180  ? 2.0621 4.4747 2.2961 0.5035  -0.1957 0.1343  180  ILE A CG2 
1271  C CD1 . ILE A 180  ? 1.9744 4.2619 2.1902 0.4932  -0.2083 0.0732  180  ILE A CD1 
1272  N N   . GLY A 181  ? 1.3151 3.5554 1.4542 0.5820  -0.1646 -0.0218 181  GLY A N   
1273  C CA  . GLY A 181  ? 1.3174 3.5286 1.4250 0.6198  -0.1518 -0.0617 181  GLY A CA  
1274  C C   . GLY A 181  ? 1.3193 3.4628 1.4169 0.6187  -0.1576 -0.0967 181  GLY A C   
1275  O O   . GLY A 181  ? 1.3197 3.4133 1.3959 0.6385  -0.1525 -0.1372 181  GLY A O   
1276  N N   . ILE A 182  ? 2.1322 4.2760 2.2472 0.5952  -0.1690 -0.0791 182  ILE A N   
1277  C CA  . ILE A 182  ? 2.1095 4.1887 2.2210 0.5875  -0.1769 -0.1081 182  ILE A CA  
1278  C C   . ILE A 182  ? 2.0971 4.1120 2.2235 0.5492  -0.1887 -0.1238 182  ILE A C   
1279  O O   . ILE A 182  ? 2.1124 4.1257 2.2620 0.5141  -0.2020 -0.1021 182  ILE A O   
1280  C CB  . ILE A 182  ? 2.0986 4.2073 2.2229 0.5787  -0.1844 -0.0808 182  ILE A CB  
1281  C CG1 . ILE A 182  ? 2.1009 4.2958 2.2191 0.6071  -0.1735 -0.0463 182  ILE A CG1 
1282  C CG2 . ILE A 182  ? 2.0827 4.1338 2.1965 0.5847  -0.1889 -0.1129 182  ILE A CG2 
1283  C CD1 . ILE A 182  ? 2.1178 4.3513 2.2511 0.5968  -0.1804 -0.0124 182  ILE A CD1 
1284  N N   . ILE A 183  ? 1.8340 3.7953 1.9464 0.5562  -0.1841 -0.1611 183  ILE A N   
1285  C CA  . ILE A 183  ? 1.8200 3.7189 1.9426 0.5230  -0.1933 -0.1775 183  ILE A CA  
1286  C C   . ILE A 183  ? 1.8103 3.6508 1.9398 0.5053  -0.2036 -0.1953 183  ILE A C   
1287  O O   . ILE A 183  ? 1.8132 3.6167 1.9291 0.5254  -0.1994 -0.2263 183  ILE A O   
1288  C CB  . ILE A 183  ? 1.8016 3.6581 1.9068 0.5369  -0.1844 -0.2130 183  ILE A CB  
1289  C CG1 . ILE A 183  ? 1.7939 3.7059 1.8935 0.5526  -0.1749 -0.1954 183  ILE A CG1 
1290  C CG2 . ILE A 183  ? 1.8268 3.6174 1.9406 0.5036  -0.1933 -0.2298 183  ILE A CG2 
1291  C CD1 . ILE A 183  ? 1.7951 3.6745 1.8746 0.5744  -0.1642 -0.2294 183  ILE A CD1 
1292  N N   . SER A 184  ? 1.6407 3.4711 1.7918 0.4677  -0.2177 -0.1762 184  SER A N   
1293  C CA  . SER A 184  ? 1.6236 3.4100 1.7846 0.4501  -0.2285 -0.1851 184  SER A CA  
1294  C C   . SER A 184  ? 1.7318 3.4331 1.8930 0.4307  -0.2334 -0.2194 184  SER A C   
1295  O O   . SER A 184  ? 1.7693 3.4455 1.9456 0.3965  -0.2459 -0.2101 184  SER A O   
1296  C CB  . SER A 184  ? 1.6460 3.4690 1.8313 0.4203  -0.2424 -0.1435 184  SER A CB  
1297  O OG  . SER A 184  ? 1.6210 3.5247 1.8113 0.4282  -0.2385 -0.1051 184  SER A OG  
1298  N N   . PHE A 185  ? 1.8070 3.4633 1.9517 0.4526  -0.2241 -0.2583 185  PHE A N   
1299  C CA  . PHE A 185  ? 1.8232 3.4005 1.9682 0.4368  -0.2265 -0.2905 185  PHE A CA  
1300  C C   . PHE A 185  ? 1.8147 3.3513 1.9757 0.4114  -0.2392 -0.2915 185  PHE A C   
1301  O O   . PHE A 185  ? 1.7819 3.3536 1.9545 0.4043  -0.2471 -0.2654 185  PHE A O   
1302  C CB  . PHE A 185  ? 1.8002 3.3414 1.9274 0.4668  -0.2144 -0.3295 185  PHE A CB  
1303  C CG  . PHE A 185  ? 1.7869 3.3520 1.8988 0.4868  -0.2030 -0.3334 185  PHE A CG  
1304  C CD1 . PHE A 185  ? 1.8100 3.3285 1.9152 0.4827  -0.1983 -0.3578 185  PHE A CD1 
1305  C CD2 . PHE A 185  ? 1.7697 3.4042 1.8738 0.5103  -0.1967 -0.3121 185  PHE A CD2 
1306  C CE1 . PHE A 185  ? 1.8145 3.3548 1.9062 0.5007  -0.1883 -0.3610 185  PHE A CE1 
1307  C CE2 . PHE A 185  ? 1.7742 3.4302 1.8646 0.5295  -0.1862 -0.3160 185  PHE A CE2 
1308  C CZ  . PHE A 185  ? 1.8051 3.4136 1.8898 0.5243  -0.1825 -0.3406 185  PHE A CZ  
1309  N N   . PRO A 186  ? 1.3654 2.8287 1.5272 0.3978  -0.2408 -0.3205 186  PRO A N   
1310  C CA  . PRO A 186  ? 1.4297 2.8462 1.6061 0.3729  -0.2522 -0.3245 186  PRO A CA  
1311  C C   . PRO A 186  ? 1.4211 2.7842 1.5954 0.3878  -0.2479 -0.3591 186  PRO A C   
1312  O O   . PRO A 186  ? 1.4262 2.7562 1.5888 0.4052  -0.2373 -0.3890 186  PRO A O   
1313  C CB  . PRO A 186  ? 1.4758 2.8505 1.6534 0.3451  -0.2569 -0.3289 186  PRO A CB  
1314  C CG  . PRO A 186  ? 1.4677 2.8557 1.6288 0.3609  -0.2451 -0.3372 186  PRO A CG  
1315  C CD  . PRO A 186  ? 1.3977 2.8230 1.5483 0.3981  -0.2333 -0.3435 186  PRO A CD  
1316  N N   . ASP A 187  ? 1.9833 3.3379 2.1706 0.3794  -0.2569 -0.3537 187  ASP A N   
1317  C CA  . ASP A 187  ? 1.9628 3.2768 2.1512 0.3945  -0.2547 -0.3810 187  ASP A CA  
1318  C C   . ASP A 187  ? 1.9434 3.1916 2.1266 0.3976  -0.2466 -0.4173 187  ASP A C   
1319  O O   . ASP A 187  ? 1.9387 3.1543 2.1237 0.3763  -0.2478 -0.4207 187  ASP A O   
1320  C CB  . ASP A 187  ? 2.0176 3.3131 2.2246 0.3734  -0.2679 -0.3716 187  ASP A CB  
1321  C CG  . ASP A 187  ? 2.0471 3.4040 2.2587 0.3788  -0.2743 -0.3412 187  ASP A CG  
1322  O OD1 . ASP A 187  ? 2.0372 3.4552 2.2390 0.3941  -0.2692 -0.3221 187  ASP A OD1 
1323  O OD2 . ASP A 187  ? 2.0724 3.4166 2.2977 0.3680  -0.2841 -0.3359 187  ASP A OD2 
1324  N N   . PHE A 188  ? 1.6420 2.8711 1.8182 0.4247  -0.2388 -0.4437 188  PHE A N   
1325  C CA  . PHE A 188  ? 1.6007 2.7656 1.7761 0.4285  -0.2315 -0.4780 188  PHE A CA  
1326  C C   . PHE A 188  ? 1.6040 2.7284 1.7936 0.4283  -0.2367 -0.4927 188  PHE A C   
1327  O O   . PHE A 188  ? 1.5763 2.7193 1.7646 0.4483  -0.2384 -0.4942 188  PHE A O   
1328  C CB  . PHE A 188  ? 1.5329 2.7072 1.6914 0.4600  -0.2195 -0.4961 188  PHE A CB  
1329  C CG  . PHE A 188  ? 1.4808 2.5922 1.6400 0.4679  -0.2118 -0.5312 188  PHE A CG  
1330  C CD1 . PHE A 188  ? 1.4671 2.5397 1.6367 0.4762  -0.2137 -0.5512 188  PHE A CD1 
1331  C CD2 . PHE A 188  ? 1.5057 2.5993 1.6556 0.4681  -0.2025 -0.5431 188  PHE A CD2 
1332  C CE1 . PHE A 188  ? 1.4463 2.4640 1.6193 0.4838  -0.2063 -0.5813 188  PHE A CE1 
1333  C CE2 . PHE A 188  ? 1.4933 2.5319 1.6448 0.4761  -0.1946 -0.5735 188  PHE A CE2 
1334  C CZ  . PHE A 188  ? 1.4633 2.4646 1.6273 0.4839  -0.1964 -0.5920 188  PHE A CZ  
1335  N N   . LYS A 189  ? 2.3709 3.4403 2.5733 0.4061  -0.2396 -0.5029 189  LYS A N   
1336  C CA  . LYS A 189  ? 2.3427 3.3698 2.5614 0.4038  -0.2444 -0.5167 189  LYS A CA  
1337  C C   . LYS A 189  ? 2.3129 3.2917 2.5324 0.4222  -0.2349 -0.5507 189  LYS A C   
1338  O O   . LYS A 189  ? 2.3047 3.2562 2.5177 0.4231  -0.2252 -0.5662 189  LYS A O   
1339  C CB  . LYS A 189  ? 2.4325 3.4236 2.6657 0.3715  -0.2525 -0.5100 189  LYS A CB  
1340  C CG  . LYS A 189  ? 2.4716 3.3938 2.7190 0.3682  -0.2503 -0.5361 189  LYS A CG  
1341  C CD  . LYS A 189  ? 2.5145 3.4285 2.7807 0.3605  -0.2617 -0.5296 189  LYS A CD  
1342  C CE  . LYS A 189  ? 2.5679 3.4185 2.8497 0.3398  -0.2638 -0.5409 189  LYS A CE  
1343  N NZ  . LYS A 189  ? 2.5585 3.3546 2.8420 0.3500  -0.2510 -0.5719 189  LYS A NZ  
1344  N N   . ILE A 190  ? 2.1977 3.1661 2.4260 0.4365  -0.2384 -0.5610 190  ILE A N   
1345  C CA  . ILE A 190  ? 2.1814 3.1048 2.4147 0.4538  -0.2319 -0.5913 190  ILE A CA  
1346  C C   . ILE A 190  ? 2.2554 3.1159 2.5079 0.4346  -0.2310 -0.6048 190  ILE A C   
1347  O O   . ILE A 190  ? 2.3681 3.2192 2.6340 0.4149  -0.2399 -0.5934 190  ILE A O   
1348  C CB  . ILE A 190  ? 2.1143 3.0506 2.3496 0.4759  -0.2382 -0.5959 190  ILE A CB  
1349  C CG1 . ILE A 190  ? 2.0021 3.0036 2.2164 0.4936  -0.2392 -0.5787 190  ILE A CG1 
1350  C CG2 . ILE A 190  ? 1.9963 2.8923 2.2355 0.4965  -0.2326 -0.6259 190  ILE A CG2 
1351  C CD1 . ILE A 190  ? 1.9674 2.9848 2.1631 0.5073  -0.2281 -0.5847 190  ILE A CD1 
1352  N N   . PRO A 191  ? 1.9542 2.7716 2.2080 0.4406  -0.2200 -0.6284 191  PRO A N   
1353  C CA  . PRO A 191  ? 1.9639 2.7191 2.2350 0.4271  -0.2161 -0.6440 191  PRO A CA  
1354  C C   . PRO A 191  ? 2.0299 2.7604 2.3242 0.4234  -0.2247 -0.6469 191  PRO A C   
1355  O O   . PRO A 191  ? 1.9775 2.7220 2.2765 0.4407  -0.2304 -0.6500 191  PRO A O   
1356  C CB  . PRO A 191  ? 1.9204 2.6470 2.1899 0.4463  -0.2036 -0.6692 191  PRO A CB  
1357  C CG  . PRO A 191  ? 1.8918 2.6610 2.1376 0.4584  -0.1990 -0.6634 191  PRO A CG  
1358  C CD  . PRO A 191  ? 1.8884 2.7173 2.1250 0.4599  -0.2096 -0.6393 191  PRO A CD  
1359  N N   . SER A 192  ? 1.9826 2.6744 2.2905 0.4014  -0.2259 -0.6464 192  SER A N   
1360  C CA  . SER A 192  ? 1.9803 2.6416 2.3125 0.3962  -0.2329 -0.6504 192  SER A CA  
1361  C C   . SER A 192  ? 1.8582 2.4937 2.2034 0.4186  -0.2278 -0.6734 192  SER A C   
1362  O O   . SER A 192  ? 1.8077 2.4271 2.1730 0.4219  -0.2348 -0.6776 192  SER A O   
1363  C CB  . SER A 192  ? 2.0586 2.6712 2.4013 0.3730  -0.2304 -0.6527 192  SER A CB  
1364  O OG  . SER A 192  ? 2.1140 2.7374 2.4387 0.3552  -0.2300 -0.6395 192  SER A OG  
1365  N N   . ASN A 193  ? 1.7496 2.3811 2.0837 0.4335  -0.2164 -0.6874 193  ASN A N   
1366  C CA  . ASN A 193  ? 1.7380 2.3464 2.0831 0.4553  -0.2116 -0.7089 193  ASN A CA  
1367  C C   . ASN A 193  ? 1.7194 2.3423 2.0445 0.4710  -0.2014 -0.7172 193  ASN A C   
1368  O O   . ASN A 193  ? 1.7450 2.3376 2.0697 0.4685  -0.1890 -0.7285 193  ASN A O   
1369  C CB  . ASN A 193  ? 1.7709 2.3191 2.1416 0.4481  -0.2048 -0.7240 193  ASN A CB  
1370  C CG  . ASN A 193  ? 1.7540 2.2763 2.1386 0.4691  -0.1990 -0.7453 193  ASN A CG  
1371  O OD1 . ASN A 193  ? 1.7132 2.2602 2.0872 0.4892  -0.2012 -0.7500 193  ASN A OD1 
1372  N ND2 . ASN A 193  ? 1.7793 2.2512 2.1882 0.4648  -0.1917 -0.7578 193  ASN A ND2 
1373  N N   . PRO A 194  ? 2.2036 2.8737 2.5107 0.4879  -0.2065 -0.7108 194  PRO A N   
1374  C CA  . PRO A 194  ? 2.1553 2.8482 2.4409 0.5053  -0.1989 -0.7161 194  PRO A CA  
1375  C C   . PRO A 194  ? 2.0909 2.7631 2.3826 0.5302  -0.1960 -0.7384 194  PRO A C   
1376  O O   . PRO A 194  ? 2.0647 2.7110 2.3769 0.5358  -0.2021 -0.7480 194  PRO A O   
1377  C CB  . PRO A 194  ? 2.1644 2.9189 2.4301 0.5130  -0.2077 -0.6970 194  PRO A CB  
1378  C CG  . PRO A 194  ? 2.2124 2.9755 2.4898 0.4987  -0.2198 -0.6814 194  PRO A CG  
1379  C CD  . PRO A 194  ? 2.2138 2.9217 2.5188 0.4902  -0.2205 -0.6950 194  PRO A CD  
1380  N N   . ARG A 195  ? 1.9365 2.6204 2.2113 0.5445  -0.1880 -0.7455 195  ARG A N   
1381  C CA  . ARG A 195  ? 1.9341 2.6056 2.2110 0.5699  -0.1875 -0.7644 195  ARG A CA  
1382  C C   . ARG A 195  ? 1.9202 2.6272 2.1851 0.5908  -0.2002 -0.7609 195  ARG A C   
1383  O O   . ARG A 195  ? 1.9251 2.6809 2.1667 0.5953  -0.2024 -0.7460 195  ARG A O   
1384  C CB  . ARG A 195  ? 1.9680 2.6422 2.2289 0.5788  -0.1755 -0.7720 195  ARG A CB  
1385  C CG  . ARG A 195  ? 2.0034 2.6310 2.2775 0.5672  -0.1620 -0.7833 195  ARG A CG  
1386  C CD  . ARG A 195  ? 2.0899 2.7294 2.3465 0.5495  -0.1531 -0.7718 195  ARG A CD  
1387  N NE  . ARG A 195  ? 2.1333 2.7686 2.3772 0.5584  -0.1415 -0.7810 195  ARG A NE  
1388  C CZ  . ARG A 195  ? 2.1474 2.7447 2.4040 0.5681  -0.1334 -0.7994 195  ARG A CZ  
1389  N NH1 . ARG A 195  ? 2.1310 2.6912 2.4147 0.5703  -0.1354 -0.8106 195  ARG A NH1 
1390  N NH2 . ARG A 195  ? 2.1676 2.7646 2.4112 0.5756  -0.1234 -0.8057 195  ARG A NH2 
1391  N N   . TYR A 196  ? 1.9188 2.6015 2.1993 0.6043  -0.2085 -0.7745 196  TYR A N   
1392  C CA  . TYR A 196  ? 1.8644 2.5745 2.1335 0.6233  -0.2225 -0.7718 196  TYR A CA  
1393  C C   . TYR A 196  ? 1.8005 2.5305 2.0462 0.6525  -0.2237 -0.7813 196  TYR A C   
1394  O O   . TYR A 196  ? 1.7701 2.4700 2.0232 0.6658  -0.2220 -0.8001 196  TYR A O   
1395  C CB  . TYR A 196  ? 1.9030 2.5802 2.1985 0.6224  -0.2343 -0.7790 196  TYR A CB  
1396  C CG  . TYR A 196  ? 1.9414 2.6146 2.2527 0.5965  -0.2368 -0.7642 196  TYR A CG  
1397  C CD1 . TYR A 196  ? 1.9449 2.6625 2.2398 0.5883  -0.2416 -0.7423 196  TYR A CD1 
1398  C CD2 . TYR A 196  ? 1.9517 2.5775 2.2947 0.5808  -0.2345 -0.7712 196  TYR A CD2 
1399  C CE1 . TYR A 196  ? 1.9777 2.6918 2.2870 0.5644  -0.2452 -0.7282 196  TYR A CE1 
1400  C CE2 . TYR A 196  ? 1.9740 2.5955 2.3304 0.5577  -0.2374 -0.7578 196  TYR A CE2 
1401  C CZ  . TYR A 196  ? 1.9828 2.6481 2.3218 0.5493  -0.2434 -0.7365 196  TYR A CZ  
1402  O OH  . TYR A 196  ? 2.0017 2.6640 2.3533 0.5264  -0.2477 -0.7222 196  TYR A OH  
1403  N N   . GLY A 197  ? 2.0068 2.7882 2.2245 0.6626  -0.2266 -0.7672 197  GLY A N   
1404  C CA  . GLY A 197  ? 2.0073 2.8106 2.1997 0.6915  -0.2279 -0.7746 197  GLY A CA  
1405  C C   . GLY A 197  ? 2.0063 2.8706 2.1683 0.6985  -0.2257 -0.7551 197  GLY A C   
1406  O O   . GLY A 197  ? 2.0435 2.9392 2.2011 0.6898  -0.2306 -0.7357 197  GLY A O   
1407  N N   . MET A 198  ? 1.7644 2.6459 1.9065 0.7142  -0.2180 -0.7594 198  MET A N   
1408  C CA  . MET A 198  ? 1.7718 2.7122 1.8841 0.7269  -0.2152 -0.7428 198  MET A CA  
1409  C C   . MET A 198  ? 1.7254 2.6897 1.8331 0.7104  -0.2020 -0.7288 198  MET A C   
1410  O O   . MET A 198  ? 1.6638 2.6162 1.7680 0.7149  -0.1932 -0.7394 198  MET A O   
1411  C CB  . MET A 198  ? 1.8161 2.7626 1.9055 0.7622  -0.2186 -0.7577 198  MET A CB  
1412  C CG  . MET A 198  ? 2.1310 3.1376 2.1886 0.7797  -0.2147 -0.7418 198  MET A CG  
1413  S SD  . MET A 198  ? 2.3142 3.3736 2.3641 0.7710  -0.2196 -0.7114 198  MET A SD  
1414  C CE  . MET A 198  ? 1.6407 2.6732 1.6916 0.7870  -0.2370 -0.7247 198  MET A CE  
1415  N N   . TRP A 199  ? 1.8577 2.8561 1.9652 0.6913  -0.2017 -0.7042 199  TRP A N   
1416  C CA  . TRP A 199  ? 1.8796 2.9031 1.9828 0.6743  -0.1919 -0.6881 199  TRP A CA  
1417  C C   . TRP A 199  ? 1.8900 2.9654 1.9662 0.6958  -0.1870 -0.6787 199  TRP A C   
1418  O O   . TRP A 199  ? 1.9161 3.0176 1.9754 0.7210  -0.1920 -0.6780 199  TRP A O   
1419  C CB  . TRP A 199  ? 1.9328 2.9750 2.0462 0.6472  -0.1958 -0.6640 199  TRP A CB  
1420  C CG  . TRP A 199  ? 1.9901 2.9802 2.1292 0.6219  -0.1969 -0.6721 199  TRP A CG  
1421  C CD1 . TRP A 199  ? 2.0068 2.9539 2.1640 0.6222  -0.2034 -0.6876 199  TRP A CD1 
1422  C CD2 . TRP A 199  ? 2.0272 3.0011 2.1765 0.5931  -0.1913 -0.6652 199  TRP A CD2 
1423  N NE1 . TRP A 199  ? 2.0513 2.9577 2.2301 0.5959  -0.2010 -0.6903 199  TRP A NE1 
1424  C CE2 . TRP A 199  ? 2.0518 2.9728 2.2245 0.5780  -0.1937 -0.6772 199  TRP A CE2 
1425  C CE3 . TRP A 199  ? 2.0456 3.0441 2.1860 0.5788  -0.1851 -0.6496 199  TRP A CE3 
1426  C CZ2 . TRP A 199  ? 2.0551 2.9464 2.2397 0.5506  -0.1895 -0.6749 199  TRP A CZ2 
1427  C CZ3 . TRP A 199  ? 2.0620 3.0298 2.2140 0.5505  -0.1825 -0.6475 199  TRP A CZ3 
1428  C CH2 . TRP A 199  ? 2.0767 2.9910 2.2493 0.5373  -0.1843 -0.6605 199  TRP A CH2 
1429  N N   . THR A 200  ? 1.3300 2.4198 1.4013 0.6867  -0.1773 -0.6713 200  THR A N   
1430  C CA  . THR A 200  ? 1.4041 2.5450 1.4519 0.7057  -0.1718 -0.6605 200  THR A CA  
1431  C C   . THR A 200  ? 1.3273 2.5092 1.3746 0.6839  -0.1672 -0.6325 200  THR A C   
1432  O O   . THR A 200  ? 1.3201 2.4804 1.3764 0.6628  -0.1623 -0.6335 200  THR A O   
1433  C CB  . THR A 200  ? 1.3321 2.4500 1.3723 0.7220  -0.1643 -0.6820 200  THR A CB  
1434  O OG1 . THR A 200  ? 1.3669 2.4329 1.4157 0.7336  -0.1690 -0.7092 200  THR A OG1 
1435  C CG2 . THR A 200  ? 1.3396 2.5055 1.3540 0.7505  -0.1610 -0.6759 200  THR A CG2 
1436  N N   . ILE A 201  ? 1.3474 2.5882 1.3845 0.6887  -0.1691 -0.6069 201  ILE A N   
1437  C CA  . ILE A 201  ? 1.3272 2.6076 1.3653 0.6690  -0.1653 -0.5800 201  ILE A CA  
1438  C C   . ILE A 201  ? 1.3291 2.6538 1.3472 0.6911  -0.1571 -0.5734 201  ILE A C   
1439  O O   . ILE A 201  ? 1.3810 2.7429 1.3821 0.7194  -0.1567 -0.5691 201  ILE A O   
1440  C CB  . ILE A 201  ? 1.3291 2.6491 1.3746 0.6526  -0.1724 -0.5496 201  ILE A CB  
1441  C CG1 . ILE A 201  ? 1.3270 2.6023 1.3936 0.6273  -0.1805 -0.5546 201  ILE A CG1 
1442  C CG2 . ILE A 201  ? 1.3638 2.7251 1.4121 0.6320  -0.1701 -0.5207 201  ILE A CG2 
1443  C CD1 . ILE A 201  ? 1.3394 2.6484 1.4167 0.6026  -0.1871 -0.5230 201  ILE A CD1 
1444  N N   . LYS A 202  ? 1.7769 3.0955 1.7960 0.6792  -0.1504 -0.5734 202  LYS A N   
1445  C CA  . LYS A 202  ? 1.7648 3.1265 1.7682 0.6950  -0.1426 -0.5639 202  LYS A CA  
1446  C C   . LYS A 202  ? 1.7823 3.1914 1.7911 0.6726  -0.1426 -0.5300 202  LYS A C   
1447  O O   . LYS A 202  ? 1.7969 3.1949 1.8215 0.6419  -0.1485 -0.5180 202  LYS A O   
1448  C CB  . LYS A 202  ? 1.8302 3.1524 1.8300 0.6999  -0.1356 -0.5881 202  LYS A CB  
1449  C CG  . LYS A 202  ? 1.8566 3.1424 1.8492 0.7273  -0.1356 -0.6186 202  LYS A CG  
1450  C CD  . LYS A 202  ? 1.9091 3.1682 1.8965 0.7355  -0.1282 -0.6378 202  LYS A CD  
1451  C CE  . LYS A 202  ? 1.9236 3.1390 1.9086 0.7585  -0.1302 -0.6684 202  LYS A CE  
1452  N NZ  . LYS A 202  ? 1.9461 3.1124 1.9385 0.7510  -0.1246 -0.6886 202  LYS A NZ  
1453  N N   . ALA A 203  ? 1.6056 3.0674 1.6021 0.6882  -0.1366 -0.5143 203  ALA A N   
1454  C CA  . ALA A 203  ? 1.6507 3.1618 1.6541 0.6682  -0.1374 -0.4799 203  ALA A CA  
1455  C C   . ALA A 203  ? 1.6852 3.2299 1.6772 0.6822  -0.1288 -0.4737 203  ALA A C   
1456  O O   . ALA A 203  ? 1.6553 3.2195 1.6302 0.7164  -0.1225 -0.4824 203  ALA A O   
1457  C CB  . ALA A 203  ? 1.6073 3.1726 1.6127 0.6719  -0.1417 -0.4518 203  ALA A CB  
1458  N N   . LYS A 204  ? 1.6001 3.1504 1.6009 0.6558  -0.1295 -0.4583 204  LYS A N   
1459  C CA  . LYS A 204  ? 1.6505 3.2324 1.6438 0.6630  -0.1226 -0.4490 204  LYS A CA  
1460  C C   . LYS A 204  ? 1.6523 3.2784 1.6577 0.6365  -0.1271 -0.4124 204  LYS A C   
1461  O O   . LYS A 204  ? 1.6362 3.2448 1.6561 0.6039  -0.1361 -0.4019 204  LYS A O   
1462  C CB  . LYS A 204  ? 1.7011 3.2260 1.6901 0.6592  -0.1187 -0.4774 204  LYS A CB  
1463  C CG  . LYS A 204  ? 1.7999 3.2645 1.8015 0.6264  -0.1250 -0.4885 204  LYS A CG  
1464  C CD  . LYS A 204  ? 1.8523 3.2579 1.8487 0.6266  -0.1195 -0.5187 204  LYS A CD  
1465  C CE  . LYS A 204  ? 1.8996 3.2412 1.9070 0.5995  -0.1241 -0.5332 204  LYS A CE  
1466  N NZ  . LYS A 204  ? 1.9354 3.2270 1.9381 0.5940  -0.1183 -0.5548 204  LYS A NZ  
1467  N N   . TYR A 205  ? 1.9464 3.6290 1.9464 0.6509  -0.1213 -0.3928 205  TYR A N   
1468  C CA  . TYR A 205  ? 2.0452 3.7716 2.0583 0.6268  -0.1260 -0.3571 205  TYR A CA  
1469  C C   . TYR A 205  ? 2.1687 3.8488 2.1857 0.5981  -0.1302 -0.3661 205  TYR A C   
1470  O O   . TYR A 205  ? 2.2211 3.8638 2.2266 0.6085  -0.1238 -0.3927 205  TYR A O   
1471  C CB  . TYR A 205  ? 2.0423 3.8387 2.0493 0.6513  -0.1178 -0.3353 205  TYR A CB  
1472  C CG  . TYR A 205  ? 2.0332 3.8902 2.0415 0.6687  -0.1162 -0.3108 205  TYR A CG  
1473  C CD1 . TYR A 205  ? 2.0146 3.8941 2.0044 0.7101  -0.1064 -0.3209 205  TYR A CD1 
1474  C CD2 . TYR A 205  ? 2.0509 3.9395 2.0781 0.6437  -0.1251 -0.2781 205  TYR A CD2 
1475  C CE1 . TYR A 205  ? 2.0010 3.9347 1.9895 0.7268  -0.1045 -0.2984 205  TYR A CE1 
1476  C CE2 . TYR A 205  ? 2.0326 3.9766 2.0613 0.6591  -0.1232 -0.2546 205  TYR A CE2 
1477  C CZ  . TYR A 205  ? 2.0085 3.9753 2.0171 0.7010  -0.1124 -0.2647 205  TYR A CZ  
1478  O OH  . TYR A 205  ? 1.9857 4.0080 1.9939 0.7169  -0.1101 -0.2402 205  TYR A OH  
1479  N N   . LYS A 206  ? 2.0605 3.7415 2.0927 0.5622  -0.1413 -0.3440 206  LYS A N   
1480  C CA  . LYS A 206  ? 2.1110 3.7463 2.1442 0.5340  -0.1465 -0.3516 206  LYS A CA  
1481  C C   . LYS A 206  ? 2.1471 3.8038 2.1710 0.5464  -0.1394 -0.3499 206  LYS A C   
1482  O O   . LYS A 206  ? 2.1472 3.7612 2.1584 0.5564  -0.1325 -0.3787 206  LYS A O   
1483  C CB  . LYS A 206  ? 2.1549 3.7977 2.2046 0.4950  -0.1614 -0.3227 206  LYS A CB  
1484  C CG  . LYS A 206  ? 2.2104 3.7935 2.2576 0.4650  -0.1684 -0.3347 206  LYS A CG  
1485  C CD  . LYS A 206  ? 2.2571 3.8355 2.3191 0.4271  -0.1852 -0.3112 206  LYS A CD  
1486  C CE  . LYS A 206  ? 2.2961 3.9462 2.3719 0.4167  -0.1931 -0.2678 206  LYS A CE  
1487  N NZ  . LYS A 206  ? 2.3461 3.9817 2.4343 0.3763  -0.2117 -0.2472 206  LYS A NZ  
1488  N N   . GLU A 207  ? 2.0287 3.7541 2.0604 0.5469  -0.1408 -0.3149 207  GLU A N   
1489  C CA  . GLU A 207  ? 2.0606 3.8164 2.0868 0.5571  -0.1351 -0.3068 207  GLU A CA  
1490  C C   . GLU A 207  ? 2.0082 3.7653 2.0169 0.5979  -0.1205 -0.3312 207  GLU A C   
1491  O O   . GLU A 207  ? 1.9655 3.6786 1.9641 0.6134  -0.1158 -0.3628 207  GLU A O   
1492  C CB  . GLU A 207  ? 2.1206 3.9559 2.1621 0.5516  -0.1393 -0.2614 207  GLU A CB  
1493  C CG  . GLU A 207  ? 2.1799 4.0156 2.2394 0.5088  -0.1561 -0.2341 207  GLU A CG  
1494  C CD  . GLU A 207  ? 2.2414 4.0374 2.2966 0.4849  -0.1626 -0.2409 207  GLU A CD  
1495  O OE1 . GLU A 207  ? 2.2443 4.0171 2.2838 0.5016  -0.1532 -0.2645 207  GLU A OE1 
1496  O OE2 . GLU A 207  ? 2.2909 4.0779 2.3574 0.4496  -0.1779 -0.2222 207  GLU A OE2 
1497  N N   . ASP A 208  ? 2.2510 4.0574 2.2569 0.6146  -0.1143 -0.3160 208  ASP A N   
1498  C CA  . ASP A 208  ? 2.1588 3.9717 2.1478 0.6539  -0.1013 -0.3359 208  ASP A CA  
1499  C C   . ASP A 208  ? 2.0829 3.9257 2.0668 0.6834  -0.0959 -0.3357 208  ASP A C   
1500  O O   . ASP A 208  ? 2.0987 3.9755 2.0942 0.6744  -0.1009 -0.3113 208  ASP A O   
1501  C CB  . ASP A 208  ? 2.1375 4.0047 2.1274 0.6633  -0.0969 -0.3136 208  ASP A CB  
1502  C CG  . ASP A 208  ? 2.1279 4.0664 2.1361 0.6515  -0.1020 -0.2683 208  ASP A CG  
1503  O OD1 . ASP A 208  ? 2.0750 4.0500 2.0865 0.6648  -0.1000 -0.2551 208  ASP A OD1 
1504  O OD2 . ASP A 208  ? 2.1747 4.1316 2.1945 0.6283  -0.1086 -0.2455 208  ASP A OD2 
1505  N N   . PHE A 209  ? 2.2019 4.0329 2.1677 0.7191  -0.0863 -0.3617 209  PHE A N   
1506  C CA  . PHE A 209  ? 2.1335 3.9767 2.0882 0.7508  -0.0817 -0.3710 209  PHE A CA  
1507  C C   . PHE A 209  ? 2.1043 3.8735 2.0503 0.7552  -0.0832 -0.4114 209  PHE A C   
1508  O O   . PHE A 209  ? 2.1206 3.8455 2.0768 0.7273  -0.0909 -0.4190 209  PHE A O   
1509  C CB  . PHE A 209  ? 2.0921 3.9830 2.0584 0.7434  -0.0860 -0.3399 209  PHE A CB  
1510  C CG  . PHE A 209  ? 2.0743 4.0460 2.0493 0.7468  -0.0828 -0.2987 209  PHE A CG  
1511  C CD1 . PHE A 209  ? 2.0800 4.0906 2.0755 0.7213  -0.0903 -0.2628 209  PHE A CD1 
1512  C CD2 . PHE A 209  ? 2.0314 4.0407 1.9960 0.7754  -0.0726 -0.2948 209  PHE A CD2 
1513  C CE1 . PHE A 209  ? 2.0628 4.1496 2.0695 0.7240  -0.0876 -0.2227 209  PHE A CE1 
1514  C CE2 . PHE A 209  ? 2.0491 4.1348 2.0240 0.7792  -0.0690 -0.2552 209  PHE A CE2 
1515  C CZ  . PHE A 209  ? 2.0583 4.1836 2.0551 0.7533  -0.0764 -0.2186 209  PHE A CZ  
1516  N N   . SER A 210  ? 2.2792 4.0356 2.2069 0.7906  -0.0764 -0.4365 210  SER A N   
1517  C CA  . SER A 210  ? 2.2470 3.9369 2.1671 0.7992  -0.0780 -0.4743 210  SER A CA  
1518  C C   . SER A 210  ? 2.2135 3.9008 2.1328 0.8062  -0.0826 -0.4768 210  SER A C   
1519  O O   . SER A 210  ? 2.1682 3.8001 2.0854 0.8086  -0.0860 -0.5052 210  SER A O   
1520  C CB  . SER A 210  ? 2.2355 3.9147 2.1365 0.8354  -0.0708 -0.4984 210  SER A CB  
1521  O OG  . SER A 210  ? 2.2159 3.8301 2.1120 0.8427  -0.0734 -0.5341 210  SER A OG  
1522  N N   . THR A 211  ? 1.9162 3.6637 1.8383 0.8091  -0.0829 -0.4460 211  THR A N   
1523  C CA  . THR A 211  ? 1.9030 3.6620 1.8187 0.8254  -0.0855 -0.4454 211  THR A CA  
1524  C C   . THR A 211  ? 1.8834 3.5827 1.8069 0.8084  -0.0942 -0.4659 211  THR A C   
1525  O O   . THR A 211  ? 1.8861 3.5654 1.8281 0.7729  -0.1005 -0.4582 211  THR A O   
1526  C CB  . THR A 211  ? 1.9307 3.7662 1.8524 0.8247  -0.0845 -0.4037 211  THR A CB  
1527  O OG1 . THR A 211  ? 1.9718 3.8230 1.9164 0.7858  -0.0893 -0.3768 211  THR A OG1 
1528  C CG2 . THR A 211  ? 1.9180 3.8133 1.8236 0.8603  -0.0739 -0.3903 211  THR A CG2 
1529  N N   . THR A 212  ? 1.6985 3.3699 1.6074 0.8350  -0.0951 -0.4917 212  THR A N   
1530  C CA  . THR A 212  ? 1.6942 3.3057 1.6099 0.8241  -0.1031 -0.5149 212  THR A CA  
1531  C C   . THR A 212  ? 1.7160 3.3447 1.6338 0.8238  -0.1095 -0.5025 212  THR A C   
1532  O O   . THR A 212  ? 1.7515 3.4092 1.6514 0.8547  -0.1083 -0.5005 212  THR A O   
1533  C CB  . THR A 212  ? 1.6688 3.2315 1.5695 0.8520  -0.1028 -0.5527 212  THR A CB  
1534  O OG1 . THR A 212  ? 1.6799 3.2349 1.5755 0.8585  -0.0961 -0.5625 212  THR A OG1 
1535  C CG2 . THR A 212  ? 1.6562 3.1502 1.5696 0.8355  -0.1104 -0.5774 212  THR A CG2 
1536  N N   . GLY A 213  ? 2.4741 4.0825 2.4123 0.7895  -0.1166 -0.4948 213  GLY A N   
1537  C CA  . GLY A 213  ? 2.4657 4.0718 2.4075 0.7876  -0.1241 -0.4913 213  GLY A CA  
1538  C C   . GLY A 213  ? 2.4408 3.9739 2.3864 0.7855  -0.1300 -0.5257 213  GLY A C   
1539  O O   . GLY A 213  ? 2.4515 3.9365 2.4091 0.7654  -0.1302 -0.5414 213  GLY A O   
1540  N N   . THR A 214  ? 1.6662 3.1907 1.6016 0.8067  -0.1350 -0.5371 214  THR A N   
1541  C CA  . THR A 214  ? 1.6288 3.0886 1.5736 0.7998  -0.1429 -0.5639 214  THR A CA  
1542  C C   . THR A 214  ? 1.5711 3.0436 1.5175 0.7994  -0.1511 -0.5528 214  THR A C   
1543  O O   . THR A 214  ? 1.5675 3.0975 1.5040 0.8099  -0.1496 -0.5277 214  THR A O   
1544  C CB  . THR A 214  ? 1.6440 3.0643 1.5738 0.8297  -0.1430 -0.5977 214  THR A CB  
1545  O OG1 . THR A 214  ? 1.6545 3.0744 1.5787 0.8357  -0.1345 -0.6046 214  THR A OG1 
1546  C CG2 . THR A 214  ? 1.6040 2.9544 1.5502 0.8169  -0.1505 -0.6238 214  THR A CG2 
1547  N N   . ALA A 215  ? 2.0448 3.4649 2.0052 0.7863  -0.1593 -0.5699 215  ALA A N   
1548  C CA  . ALA A 215  ? 2.0146 3.4367 1.9761 0.7883  -0.1685 -0.5650 215  ALA A CA  
1549  C C   . ALA A 215  ? 1.9985 3.3500 1.9764 0.7765  -0.1757 -0.5923 215  ALA A C   
1550  O O   . ALA A 215  ? 1.9731 3.2828 1.9599 0.7683  -0.1722 -0.6111 215  ALA A O   
1551  C CB  . ALA A 215  ? 2.0127 3.4736 1.9882 0.7618  -0.1707 -0.5313 215  ALA A CB  
1552  N N   . TYR A 216  ? 1.7055 3.0431 1.6882 0.7758  -0.1855 -0.5940 216  TYR A N   
1553  C CA  . TYR A 216  ? 1.7863 3.0580 1.7888 0.7625  -0.1924 -0.6175 216  TYR A CA  
1554  C C   . TYR A 216  ? 1.7731 3.0390 1.7921 0.7425  -0.2017 -0.6060 216  TYR A C   
1555  O O   . TYR A 216  ? 1.7379 3.0511 1.7532 0.7384  -0.2035 -0.5792 216  TYR A O   
1556  C CB  . TYR A 216  ? 1.8243 3.0597 1.8149 0.7921  -0.1973 -0.6476 216  TYR A CB  
1557  C CG  . TYR A 216  ? 1.8753 3.1064 1.8513 0.8125  -0.1897 -0.6631 216  TYR A CG  
1558  C CD1 . TYR A 216  ? 1.9045 3.0791 1.8917 0.8119  -0.1896 -0.6904 216  TYR A CD1 
1559  C CD2 . TYR A 216  ? 1.9465 3.2312 1.8982 0.8331  -0.1824 -0.6495 216  TYR A CD2 
1560  C CE1 . TYR A 216  ? 1.9312 3.1019 1.9055 0.8304  -0.1831 -0.7040 216  TYR A CE1 
1561  C CE2 . TYR A 216  ? 1.9763 3.2576 1.9147 0.8521  -0.1757 -0.6633 216  TYR A CE2 
1562  C CZ  . TYR A 216  ? 1.9708 3.1944 1.9203 0.8504  -0.1765 -0.6908 216  TYR A CZ  
1563  O OH  . TYR A 216  ? 1.9910 3.2114 1.9275 0.8693  -0.1703 -0.7039 216  TYR A OH  
1564  N N   . PHE A 217  ? 1.5520 2.7585 1.5908 0.7301  -0.2071 -0.6264 217  PHE A N   
1565  C CA  . PHE A 217  ? 1.5343 2.7223 1.5915 0.7121  -0.2170 -0.6217 217  PHE A CA  
1566  C C   . PHE A 217  ? 1.5520 2.6699 1.6316 0.7026  -0.2210 -0.6483 217  PHE A C   
1567  O O   . PHE A 217  ? 1.5590 2.6439 1.6493 0.6922  -0.2139 -0.6613 217  PHE A O   
1568  C CB  . PHE A 217  ? 1.5358 2.7543 1.6057 0.6814  -0.2163 -0.5916 217  PHE A CB  
1569  C CG  . PHE A 217  ? 1.5490 2.7299 1.6416 0.6494  -0.2129 -0.5949 217  PHE A CG  
1570  C CD1 . PHE A 217  ? 1.5381 2.6771 1.6543 0.6272  -0.2197 -0.5997 217  PHE A CD1 
1571  C CD2 . PHE A 217  ? 1.5637 2.7524 1.6530 0.6414  -0.2032 -0.5918 217  PHE A CD2 
1572  C CE1 . PHE A 217  ? 1.5293 2.6334 1.6635 0.5995  -0.2163 -0.6024 217  PHE A CE1 
1573  C CE2 . PHE A 217  ? 1.5233 2.6769 1.6298 0.6132  -0.2006 -0.5945 217  PHE A CE2 
1574  C CZ  . PHE A 217  ? 1.5315 2.6422 1.6598 0.5926  -0.2069 -0.6001 217  PHE A CZ  
1575  N N   . GLU A 218  ? 2.0111 3.1083 2.0973 0.7074  -0.2323 -0.6553 218  GLU A N   
1576  C CA  . GLU A 218  ? 2.0539 3.0883 2.1614 0.7035  -0.2377 -0.6798 218  GLU A CA  
1577  C C   . GLU A 218  ? 2.0485 3.0619 2.1834 0.6722  -0.2420 -0.6706 218  GLU A C   
1578  O O   . GLU A 218  ? 2.0514 3.0965 2.1859 0.6622  -0.2472 -0.6485 218  GLU A O   
1579  C CB  . GLU A 218  ? 2.1479 3.1728 2.2434 0.7319  -0.2495 -0.6939 218  GLU A CB  
1580  C CG  . GLU A 218  ? 2.2300 3.1926 2.3436 0.7367  -0.2553 -0.7224 218  GLU A CG  
1581  C CD  . GLU A 218  ? 2.3070 3.2631 2.4031 0.7680  -0.2682 -0.7364 218  GLU A CD  
1582  O OE1 . GLU A 218  ? 2.3324 3.2396 2.4453 0.7716  -0.2771 -0.7567 218  GLU A OE1 
1583  O OE2 . GLU A 218  ? 2.3432 3.3432 2.4084 0.7894  -0.2699 -0.7266 218  GLU A OE2 
1584  N N   . VAL A 219  ? 1.4383 2.3985 1.5973 0.6570  -0.2395 -0.6868 219  VAL A N   
1585  C CA  . VAL A 219  ? 1.4416 2.3742 1.6272 0.6302  -0.2439 -0.6819 219  VAL A CA  
1586  C C   . VAL A 219  ? 1.4323 2.3175 1.6352 0.6384  -0.2522 -0.7029 219  VAL A C   
1587  O O   . VAL A 219  ? 1.4122 2.2638 1.6194 0.6505  -0.2490 -0.7248 219  VAL A O   
1588  C CB  . VAL A 219  ? 1.4188 2.3210 1.6209 0.6056  -0.2338 -0.6848 219  VAL A CB  
1589  C CG1 . VAL A 219  ? 1.4565 2.3171 1.6878 0.5832  -0.2389 -0.6868 219  VAL A CG1 
1590  C CG2 . VAL A 219  ? 1.4257 2.3694 1.6151 0.5910  -0.2271 -0.6623 219  VAL A CG2 
1591  N N   . LYS A 220  ? 1.8868 2.7687 2.1015 0.6308  -0.2634 -0.6954 220  LYS A N   
1592  C CA  . LYS A 220  ? 1.8733 2.7122 2.1063 0.6378  -0.2735 -0.7129 220  LYS A CA  
1593  C C   . LYS A 220  ? 1.8630 2.6733 2.1262 0.6100  -0.2762 -0.7073 220  LYS A C   
1594  O O   . LYS A 220  ? 1.7982 2.6315 2.0623 0.5896  -0.2751 -0.6866 220  LYS A O   
1595  C CB  . LYS A 220  ? 1.8654 2.7279 2.0799 0.6610  -0.2873 -0.7107 220  LYS A CB  
1596  C CG  . LYS A 220  ? 1.8655 2.7455 2.0497 0.6941  -0.2872 -0.7219 220  LYS A CG  
1597  C CD  . LYS A 220  ? 1.9486 2.8626 2.1070 0.7160  -0.2994 -0.7137 220  LYS A CD  
1598  C CE  . LYS A 220  ? 1.9344 2.8652 2.0597 0.7502  -0.2995 -0.7247 220  LYS A CE  
1599  N NZ  . LYS A 220  ? 1.9209 2.8021 2.0532 0.7668  -0.3081 -0.7526 220  LYS A NZ  
1600  N N   . GLU A 221  ? 1.9333 2.6930 2.2221 0.6096  -0.2800 -0.7253 221  GLU A N   
1601  C CA  . GLU A 221  ? 2.0710 2.7978 2.3907 0.5856  -0.2822 -0.7226 221  GLU A CA  
1602  C C   . GLU A 221  ? 2.0611 2.7937 2.3876 0.5855  -0.2984 -0.7140 221  GLU A C   
1603  O O   . GLU A 221  ? 2.0331 2.7453 2.3666 0.6010  -0.3090 -0.7270 221  GLU A O   
1604  C CB  . GLU A 221  ? 2.1922 2.8622 2.5394 0.5853  -0.2778 -0.7445 221  GLU A CB  
1605  C CG  . GLU A 221  ? 2.3402 2.9750 2.7204 0.5660  -0.2826 -0.7432 221  GLU A CG  
1606  C CD  . GLU A 221  ? 2.4192 2.9995 2.8298 0.5666  -0.2781 -0.7629 221  GLU A CD  
1607  O OE1 . GLU A 221  ? 2.4119 2.9809 2.8180 0.5784  -0.2691 -0.7767 221  GLU A OE1 
1608  O OE2 . GLU A 221  ? 2.4719 3.0218 2.9118 0.5551  -0.2833 -0.7635 221  GLU A OE2 
1609  N N   . TYR A 222  ? 2.2736 3.0324 2.5993 0.5671  -0.3011 -0.6919 222  TYR A N   
1610  C CA  . TYR A 222  ? 2.2812 3.0451 2.6151 0.5642  -0.3162 -0.6818 222  TYR A CA  
1611  C C   . TYR A 222  ? 2.2977 3.0071 2.6662 0.5579  -0.3224 -0.6963 222  TYR A C   
1612  O O   . TYR A 222  ? 2.3080 2.9797 2.6999 0.5427  -0.3137 -0.7042 222  TYR A O   
1613  C CB  . TYR A 222  ? 2.2828 3.0776 2.6161 0.5409  -0.3173 -0.6550 222  TYR A CB  
1614  C CG  . TYR A 222  ? 2.2887 3.0879 2.6320 0.5363  -0.3327 -0.6436 222  TYR A CG  
1615  C CD1 . TYR A 222  ? 2.2810 3.1201 2.6012 0.5545  -0.3425 -0.6335 222  TYR A CD1 
1616  C CD2 . TYR A 222  ? 2.3228 3.0855 2.6977 0.5149  -0.3373 -0.6431 222  TYR A CD2 
1617  C CE1 . TYR A 222  ? 2.3140 3.1569 2.6423 0.5506  -0.3567 -0.6228 222  TYR A CE1 
1618  C CE2 . TYR A 222  ? 2.3519 3.1182 2.7366 0.5106  -0.3518 -0.6324 222  TYR A CE2 
1619  C CZ  . TYR A 222  ? 2.3462 3.1525 2.7074 0.5281  -0.3617 -0.6222 222  TYR A CZ  
1620  O OH  . TYR A 222  ? 2.3666 3.1764 2.7366 0.5238  -0.3763 -0.6111 222  TYR A OH  
1621  N N   . VAL A 223  ? 1.6792 2.3846 2.0504 0.5706  -0.3376 -0.6994 223  VAL A N   
1622  C CA  . VAL A 223  ? 1.6542 2.3137 2.0600 0.5631  -0.3461 -0.7085 223  VAL A CA  
1623  C C   . VAL A 223  ? 1.6923 2.3708 2.0983 0.5581  -0.3614 -0.6919 223  VAL A C   
1624  O O   . VAL A 223  ? 1.6814 2.4067 2.0587 0.5659  -0.3655 -0.6767 223  VAL A O   
1625  C CB  . VAL A 223  ? 1.6065 2.2320 2.0207 0.5847  -0.3515 -0.7324 223  VAL A CB  
1626  C CG1 . VAL A 223  ? 1.5968 2.1747 2.0513 0.5758  -0.3600 -0.7404 223  VAL A CG1 
1627  C CG2 . VAL A 223  ? 1.5754 2.1879 1.9861 0.5912  -0.3361 -0.7470 223  VAL A CG2 
1628  N N   . LEU A 224  ? 2.2522 2.8962 2.6907 0.5450  -0.3694 -0.6933 224  LEU A N   
1629  C CA  . LEU A 224  ? 2.3103 2.9699 2.7504 0.5404  -0.3849 -0.6779 224  LEU A CA  
1630  C C   . LEU A 224  ? 2.3258 2.9721 2.7649 0.5622  -0.4013 -0.6899 224  LEU A C   
1631  O O   . LEU A 224  ? 2.3229 2.9250 2.7870 0.5669  -0.4042 -0.7084 224  LEU A O   
1632  C CB  . LEU A 224  ? 2.3125 2.9459 2.7866 0.5129  -0.3861 -0.6695 224  LEU A CB  
1633  C CG  . LEU A 224  ? 2.3577 3.0227 2.8276 0.4989  -0.3960 -0.6444 224  LEU A CG  
1634  C CD1 . LEU A 224  ? 2.3827 3.0531 2.8496 0.5130  -0.4149 -0.6428 224  LEU A CD1 
1635  C CD2 . LEU A 224  ? 2.3468 3.0661 2.7848 0.4965  -0.3892 -0.6249 224  LEU A CD2 
1636  N N   . PRO A 225  ? 4.0214 3.0661 2.7138 0.6099  -0.6486 -0.3756 225  PRO A N   
1637  C CA  . PRO A 225  ? 3.8848 2.9672 2.6336 0.6327  -0.6272 -0.3706 225  PRO A CA  
1638  C C   . PRO A 225  ? 3.9468 2.9757 2.7013 0.6453  -0.6296 -0.3915 225  PRO A C   
1639  O O   . PRO A 225  ? 3.9769 2.9710 2.7217 0.6250  -0.6590 -0.3850 225  PRO A O   
1640  C CB  . PRO A 225  ? 3.8222 2.9632 2.6060 0.6096  -0.6470 -0.3315 225  PRO A CB  
1641  C CG  . PRO A 225  ? 3.8771 3.0196 2.6251 0.5776  -0.6740 -0.3156 225  PRO A CG  
1642  C CD  . PRO A 225  ? 4.0146 3.0811 2.7055 0.5736  -0.6834 -0.3452 225  PRO A CD  
1643  N N   . HIS A 226  ? 3.4071 2.4305 2.1782 0.6787  -0.5980 -0.4162 226  HIS A N   
1644  C CA  . HIS A 226  ? 3.4998 2.4878 2.2876 0.6963  -0.5958 -0.4337 226  HIS A CA  
1645  C C   . HIS A 226  ? 3.3702 2.4144 2.2157 0.6994  -0.5965 -0.4100 226  HIS A C   
1646  O O   . HIS A 226  ? 3.3708 2.3930 2.2258 0.6939  -0.6162 -0.4036 226  HIS A O   
1647  C CB  . HIS A 226  ? 3.5942 2.5594 2.3793 0.7310  -0.5611 -0.4705 226  HIS A CB  
1648  C CG  . HIS A 226  ? 3.7787 2.6898 2.5078 0.7302  -0.5578 -0.4953 226  HIS A CG  
1649  N ND1 . HIS A 226  ? 3.8044 2.7354 2.5209 0.7419  -0.5309 -0.5043 226  HIS A ND1 
1650  C CD2 . HIS A 226  ? 3.9222 2.7600 2.6041 0.7194  -0.5771 -0.5135 226  HIS A CD2 
1651  C CE1 . HIS A 226  ? 3.9314 2.8057 2.5942 0.7385  -0.5345 -0.5265 226  HIS A CE1 
1652  N NE2 . HIS A 226  ? 4.0046 2.8216 2.6457 0.7245  -0.5624 -0.5336 226  HIS A NE2 
1653  N N   . PHE A 227  ? 3.2943 2.4109 2.1777 0.7083  -0.5744 -0.3966 227  PHE A N   
1654  C CA  . PHE A 227  ? 3.1792 2.3570 2.1181 0.7109  -0.5728 -0.3748 227  PHE A CA  
1655  C C   . PHE A 227  ? 3.0835 2.3381 2.0497 0.7025  -0.5628 -0.3485 227  PHE A C   
1656  O O   . PHE A 227  ? 3.0991 2.3718 2.0596 0.7120  -0.5389 -0.3555 227  PHE A O   
1657  C CB  . PHE A 227  ? 3.0987 2.2844 2.0727 0.7453  -0.5453 -0.3984 227  PHE A CB  
1658  C CG  . PHE A 227  ? 2.9984 2.1971 1.9769 0.7708  -0.5060 -0.4233 227  PHE A CG  
1659  C CD1 . PHE A 227  ? 2.8688 2.1330 1.8751 0.7731  -0.4836 -0.4104 227  PHE A CD1 
1660  C CD2 . PHE A 227  ? 3.0591 2.2039 2.0152 0.7926  -0.4903 -0.4596 227  PHE A CD2 
1661  C CE1 . PHE A 227  ? 2.8478 2.1214 1.8588 0.7962  -0.4459 -0.4326 227  PHE A CE1 
1662  C CE2 . PHE A 227  ? 3.0268 2.1829 1.9874 0.8153  -0.4531 -0.4822 227  PHE A CE2 
1663  C CZ  . PHE A 227  ? 2.9290 2.1486 1.9168 0.8168  -0.4307 -0.4685 227  PHE A CZ  
1664  N N   . SER A 228  ? 3.5687 2.8680 2.5652 0.6851  -0.5802 -0.3176 228  SER A N   
1665  C CA  . SER A 228  ? 3.5005 2.8713 2.5226 0.6736  -0.5752 -0.2897 228  SER A CA  
1666  C C   . SER A 228  ? 3.3527 2.7829 2.4230 0.7003  -0.5359 -0.2965 228  SER A C   
1667  O O   . SER A 228  ? 3.2951 2.7550 2.4072 0.7122  -0.5284 -0.2967 228  SER A O   
1668  C CB  . SER A 228  ? 3.5282 2.9272 2.5696 0.6473  -0.6054 -0.2561 228  SER A CB  
1669  O OG  . SER A 228  ? 3.4571 2.9324 2.5334 0.6397  -0.5977 -0.2297 228  SER A OG  
1670  N N   . VAL A 229  ? 2.7898 2.2374 1.8547 0.7100  -0.5102 -0.3025 229  VAL A N   
1671  C CA  . VAL A 229  ? 2.5504 2.0601 1.6641 0.7309  -0.4724 -0.3046 229  VAL A CA  
1672  C C   . VAL A 229  ? 2.5256 2.1007 1.6617 0.7143  -0.4738 -0.2704 229  VAL A C   
1673  O O   . VAL A 229  ? 2.5124 2.0840 1.6181 0.7015  -0.4808 -0.2580 229  VAL A O   
1674  C CB  . VAL A 229  ? 2.6231 2.1143 1.7246 0.7567  -0.4351 -0.3339 229  VAL A CB  
1675  C CG1 . VAL A 229  ? 2.4865 2.0443 1.6292 0.7680  -0.4002 -0.3252 229  VAL A CG1 
1676  C CG2 . VAL A 229  ? 2.6322 2.0887 1.7404 0.7817  -0.4196 -0.3691 229  VAL A CG2 
1677  N N   . SER A 230  ? 2.9072 2.5436 2.0961 0.7146  -0.4681 -0.2551 230  SER A N   
1678  C CA  . SER A 230  ? 2.7999 2.5041 2.0178 0.7026  -0.4639 -0.2247 230  SER A CA  
1679  C C   . SER A 230  ? 2.7216 2.4681 1.9771 0.7278  -0.4178 -0.2370 230  SER A C   
1680  O O   . SER A 230  ? 2.7479 2.4685 2.0025 0.7522  -0.3913 -0.2686 230  SER A O   
1681  C CB  . SER A 230  ? 2.7364 2.4858 1.9905 0.6857  -0.4847 -0.1991 230  SER A CB  
1682  O OG  . SER A 230  ? 2.6857 2.4652 1.9861 0.7051  -0.4645 -0.2129 230  SER A OG  
1683  N N   . ILE A 231  ? 2.0381 1.8495 1.3281 0.7217  -0.4074 -0.2124 231  ILE A N   
1684  C CA  . ILE A 231  ? 1.9774 1.8345 1.3106 0.7438  -0.3624 -0.2217 231  ILE A CA  
1685  C C   . ILE A 231  ? 1.9614 1.8919 1.3350 0.7309  -0.3606 -0.1888 231  ILE A C   
1686  O O   . ILE A 231  ? 1.9827 1.9239 1.3381 0.7157  -0.3728 -0.1634 231  ILE A O   
1687  C CB  . ILE A 231  ? 2.0604 1.8846 1.3636 0.7605  -0.3355 -0.2389 231  ILE A CB  
1688  C CG1 . ILE A 231  ? 1.9844 1.8599 1.3303 0.7778  -0.2905 -0.2386 231  ILE A CG1 
1689  C CG2 . ILE A 231  ? 2.1105 1.9065 1.3605 0.7417  -0.3618 -0.2198 231  ILE A CG2 
1690  C CD1 . ILE A 231  ? 2.0290 1.8799 1.3409 0.7877  -0.2699 -0.2413 231  ILE A CD1 
1691  N N   . GLU A 232  ? 2.5830 2.5652 2.0114 0.7366  -0.3471 -0.1897 232  GLU A N   
1692  C CA  . GLU A 232  ? 2.5560 2.6108 2.0287 0.7260  -0.3427 -0.1616 232  GLU A CA  
1693  C C   . GLU A 232  ? 2.4824 2.5812 2.0037 0.7489  -0.2933 -0.1762 232  GLU A C   
1694  O O   . GLU A 232  ? 2.4643 2.5588 2.0066 0.7695  -0.2680 -0.2072 232  GLU A O   
1695  C CB  . GLU A 232  ? 2.6142 2.6993 2.1128 0.7110  -0.3682 -0.1484 232  GLU A CB  
1696  C CG  . GLU A 232  ? 2.7940 2.8230 2.2504 0.6966  -0.4095 -0.1480 232  GLU A CG  
1697  C CD  . GLU A 232  ? 2.8767 2.9091 2.3565 0.7045  -0.4137 -0.1625 232  GLU A CD  
1698  O OE1 . GLU A 232  ? 2.8397 2.9307 2.3717 0.7144  -0.3919 -0.1658 232  GLU A OE1 
1699  O OE2 . GLU A 232  ? 2.9713 2.9477 2.4169 0.7012  -0.4387 -0.1706 232  GLU A OE2 
1700  N N   . PRO A 233  ? 2.1996 2.3424 1.7407 0.7449  -0.2791 -0.1535 233  PRO A N   
1701  C CA  . PRO A 233  ? 2.1721 2.3558 1.7569 0.7640  -0.2311 -0.1614 233  PRO A CA  
1702  C C   . PRO A 233  ? 2.0860 2.3403 1.7337 0.7608  -0.2215 -0.1549 233  PRO A C   
1703  O O   . PRO A 233  ? 2.0912 2.3678 1.7427 0.7399  -0.2548 -0.1324 233  PRO A O   
1704  C CB  . PRO A 233  ? 2.1735 2.3665 1.7402 0.7561  -0.2318 -0.1318 233  PRO A CB  
1705  C CG  . PRO A 233  ? 2.1798 2.3462 1.6982 0.7290  -0.2849 -0.1076 233  PRO A CG  
1706  C CD  . PRO A 233  ? 2.1882 2.3464 1.7116 0.7194  -0.3111 -0.1158 233  PRO A CD  
1707  N N   . GLU A 234  ? 2.3335 2.6231 2.0298 0.7802  -0.1766 -0.1743 234  GLU A N   
1708  C CA  . GLU A 234  ? 2.2191 2.5796 1.9766 0.7772  -0.1649 -0.1699 234  GLU A CA  
1709  C C   . GLU A 234  ? 2.1322 2.5356 1.8980 0.7538  -0.1884 -0.1280 234  GLU A C   
1710  O O   . GLU A 234  ? 2.1357 2.5599 1.9071 0.7362  -0.2198 -0.1132 234  GLU A O   
1711  C CB  . GLU A 234  ? 2.1982 2.5925 2.0066 0.7992  -0.1094 -0.1933 234  GLU A CB  
1712  C CG  . GLU A 234  ? 2.3522 2.7956 2.2153 0.8051  -0.0948 -0.2154 234  GLU A CG  
1713  C CD  . GLU A 234  ? 2.3347 2.8184 2.2541 0.8238  -0.0387 -0.2383 234  GLU A CD  
1714  O OE1 . GLU A 234  ? 2.3693 2.8329 2.2820 0.8354  -0.0087 -0.2406 234  GLU A OE1 
1715  O OE2 . GLU A 234  ? 2.2847 2.8206 2.2550 0.8267  -0.0239 -0.2541 234  GLU A OE2 
1716  N N   . TYR A 235  ? 1.8552 2.2711 1.6208 0.7541  -0.1735 -0.1081 235  TYR A N   
1717  C CA  . TYR A 235  ? 1.7710 2.2267 1.5426 0.7331  -0.1952 -0.0682 235  TYR A CA  
1718  C C   . TYR A 235  ? 1.7808 2.1942 1.4967 0.7272  -0.2135 -0.0497 235  TYR A C   
1719  O O   . TYR A 235  ? 1.8404 2.1926 1.5107 0.7346  -0.2186 -0.0676 235  TYR A O   
1720  C CB  . TYR A 235  ? 1.7156 2.2386 1.5477 0.7399  -0.1576 -0.0590 235  TYR A CB  
1721  C CG  . TYR A 235  ? 1.7114 2.2785 1.6023 0.7499  -0.1291 -0.0837 235  TYR A CG  
1722  C CD1 . TYR A 235  ? 1.6887 2.3271 1.6331 0.7412  -0.1217 -0.0687 235  TYR A CD1 
1723  C CD2 . TYR A 235  ? 1.7601 2.3003 1.6539 0.7682  -0.1089 -0.1234 235  TYR A CD2 
1724  C CE1 . TYR A 235  ? 1.6937 2.3761 1.6922 0.7499  -0.0952 -0.0935 235  TYR A CE1 
1725  C CE2 . TYR A 235  ? 1.7619 2.3468 1.7102 0.7771  -0.0832 -0.1478 235  TYR A CE2 
1726  C CZ  . TYR A 235  ? 1.7352 2.3912 1.7350 0.7678  -0.0764 -0.1332 235  TYR A CZ  
1727  O OH  . TYR A 235  ? 1.7266 2.4284 1.7791 0.7764  -0.0509 -0.1595 235  TYR A OH  
1728  N N   . ASN A 236  ? 2.3813 2.8281 2.1005 0.7147  -0.2226 -0.0152 236  ASN A N   
1729  C CA  . ASN A 236  ? 2.4170 2.8289 2.0823 0.7083  -0.2424 0.0031  236  ASN A CA  
1730  C C   . ASN A 236  ? 2.3655 2.7866 2.0337 0.7253  -0.2083 0.0125  236  ASN A C   
1731  O O   . ASN A 236  ? 2.4686 2.8609 2.0899 0.7229  -0.2223 0.0256  236  ASN A O   
1732  C CB  . ASN A 236  ? 2.4665 2.8969 2.1156 0.6785  -0.2890 0.0371  236  ASN A CB  
1733  C CG  . ASN A 236  ? 2.6105 2.9887 2.2120 0.6614  -0.3323 0.0301  236  ASN A CG  
1734  O OD1 . ASN A 236  ? 2.6456 2.9913 2.2436 0.6693  -0.3302 0.0021  236  ASN A OD1 
1735  N ND2 . ASN A 236  ? 2.6874 3.0577 2.2533 0.6380  -0.3714 0.0549  236  ASN A ND2 
1736  N N   . PHE A 237  ? 1.6060 2.0683 1.3292 0.7421  -0.1638 0.0065  237  PHE A N   
1737  C CA  . PHE A 237  ? 1.6567 2.1268 1.3883 0.7612  -0.1251 0.0141  237  PHE A CA  
1738  C C   . PHE A 237  ? 1.6166 2.0836 1.3844 0.7846  -0.0769 -0.0203 237  PHE A C   
1739  O O   . PHE A 237  ? 1.6533 2.0966 1.4194 0.7867  -0.0801 -0.0500 237  PHE A O   
1740  C CB  . PHE A 237  ? 1.5365 2.0729 1.3101 0.7549  -0.1184 0.0477  237  PHE A CB  
1741  C CG  . PHE A 237  ? 1.5437 2.0928 1.2884 0.7302  -0.1659 0.0829  237  PHE A CG  
1742  C CD1 . PHE A 237  ? 1.5562 2.1169 1.2838 0.7318  -0.1665 0.1129  237  PHE A CD1 
1743  C CD2 . PHE A 237  ? 1.5437 2.0937 1.2779 0.7053  -0.2098 0.0864  237  PHE A CD2 
1744  C CE1 . PHE A 237  ? 1.5720 2.1483 1.2741 0.7083  -0.2109 0.1444  237  PHE A CE1 
1745  C CE2 . PHE A 237  ? 1.5487 2.1108 1.2577 0.6809  -0.2528 0.1178  237  PHE A CE2 
1746  C CZ  . PHE A 237  ? 1.5674 2.1439 1.2607 0.6820  -0.2538 0.1461  237  PHE A CZ  
1747  N N   . ILE A 238  ? 1.2768 1.7689 1.0800 0.8022  -0.0314 -0.0174 238  ILE A N   
1748  C CA  . ILE A 238  ? 1.2424 1.7391 1.0886 0.8215  0.0151  -0.0520 238  ILE A CA  
1749  C C   . ILE A 238  ? 1.2337 1.7837 1.1373 0.8307  0.0561  -0.0388 238  ILE A C   
1750  O O   . ILE A 238  ? 1.2604 1.7986 1.1604 0.8475  0.0885  -0.0320 238  ILE A O   
1751  C CB  . ILE A 238  ? 1.2791 1.7149 1.0916 0.8417  0.0389  -0.0798 238  ILE A CB  
1752  C CG1 . ILE A 238  ? 1.3133 1.6990 1.0805 0.8343  0.0034  -0.1016 238  ILE A CG1 
1753  C CG2 . ILE A 238  ? 1.2608 1.7096 1.1252 0.8620  0.0936  -0.1120 238  ILE A CG2 
1754  C CD1 . ILE A 238  ? 1.3310 1.6683 1.0854 0.8551  0.0329  -0.1409 238  ILE A CD1 
1755  N N   . GLY A 239  ? 1.6676 2.2758 1.6227 0.8192  0.0534  -0.0339 239  GLY A N   
1756  C CA  . GLY A 239  ? 1.6347 2.3027 1.6537 0.8246  0.0902  -0.0231 239  GLY A CA  
1757  C C   . GLY A 239  ? 1.6672 2.3443 1.7361 0.8431  0.1429  -0.0613 239  GLY A C   
1758  O O   . GLY A 239  ? 1.6857 2.3441 1.7537 0.8457  0.1426  -0.0959 239  GLY A O   
1759  N N   . TYR A 240  ? 1.8135 2.5210 1.9280 0.8559  0.1889  -0.0551 240  TYR A N   
1760  C CA  . TYR A 240  ? 1.8729 2.5753 2.0256 0.8766  0.2454  -0.0904 240  TYR A CA  
1761  C C   . TYR A 240  ? 1.8662 2.5830 2.0504 0.8749  0.2512  -0.1319 240  TYR A C   
1762  O O   . TYR A 240  ? 1.8309 2.5358 2.0390 0.8912  0.2937  -0.1667 240  TYR A O   
1763  C CB  . TYR A 240  ? 1.8086 2.5578 2.0208 0.8849  0.2903  -0.0775 240  TYR A CB  
1764  C CG  . TYR A 240  ? 1.6712 2.4865 1.9392 0.8709  0.2866  -0.0793 240  TYR A CG  
1765  C CD1 . TYR A 240  ? 1.5473 2.3926 1.8740 0.8772  0.3256  -0.1164 240  TYR A CD1 
1766  C CD2 . TYR A 240  ? 1.6622 2.5112 1.9231 0.8503  0.2427  -0.0454 240  TYR A CD2 
1767  C CE1 . TYR A 240  ? 1.4516 2.3606 1.8282 0.8639  0.3212  -0.1189 240  TYR A CE1 
1768  C CE2 . TYR A 240  ? 1.5747 2.4858 1.8854 0.8368  0.2385  -0.0461 240  TYR A CE2 
1769  C CZ  . TYR A 240  ? 1.4845 2.4262 1.8522 0.8437  0.2772  -0.0826 240  TYR A CZ  
1770  O OH  . TYR A 240  ? 1.4495 2.4565 1.8651 0.8294  0.2714  -0.0824 240  TYR A OH  
1771  N N   . LYS A 241  ? 2.6564 3.4013 2.8428 0.8558  0.2108  -0.1283 241  LYS A N   
1772  C CA  . LYS A 241  ? 2.6719 3.4359 2.8879 0.8547  0.2140  -0.1658 241  LYS A CA  
1773  C C   . LYS A 241  ? 2.7735 3.4813 2.9595 0.8684  0.2212  -0.2028 241  LYS A C   
1774  O O   . LYS A 241  ? 2.7506 3.4676 2.9747 0.8816  0.2606  -0.2404 241  LYS A O   
1775  C CB  . LYS A 241  ? 2.4552 3.2482 2.6648 0.8321  0.1630  -0.1515 241  LYS A CB  
1776  C CG  . LYS A 241  ? 2.1576 3.0197 2.4141 0.8194  0.1643  -0.1258 241  LYS A CG  
1777  C CD  . LYS A 241  ? 2.3438 3.2273 2.5835 0.7956  0.1099  -0.1037 241  LYS A CD  
1778  C CE  . LYS A 241  ? 2.6689 3.6252 2.9593 0.7832  0.1140  -0.0805 241  LYS A CE  
1779  N NZ  . LYS A 241  ? 2.6472 3.6128 2.9424 0.7850  0.1273  -0.0466 241  LYS A NZ  
1780  N N   . ASN A 242  ? 1.8275 2.4783 1.9463 0.8649  0.1838  -0.1934 242  ASN A N   
1781  C CA  . ASN A 242  ? 1.8928 2.4846 1.9776 0.8788  0.1906  -0.2259 242  ASN A CA  
1782  C C   . ASN A 242  ? 1.9903 2.5367 2.0419 0.8920  0.2118  -0.2155 242  ASN A C   
1783  O O   . ASN A 242  ? 1.9821 2.5096 1.9904 0.8839  0.1833  -0.1814 242  ASN A O   
1784  C CB  . ASN A 242  ? 1.8727 2.4263 1.9021 0.8668  0.1358  -0.2241 242  ASN A CB  
1785  C CG  . ASN A 242  ? 1.7529 2.3470 1.7893 0.8440  0.0926  -0.2002 242  ASN A CG  
1786  O OD1 . ASN A 242  ? 1.7293 2.3274 1.7659 0.8381  0.0692  -0.2157 242  ASN A OD1 
1787  N ND2 . ASN A 242  ? 1.6692 2.2939 1.7112 0.8316  0.0818  -0.1614 242  ASN A ND2 
1788  N N   . PHE A 243  ? 2.1180 2.6477 2.1888 0.9121  0.2615  -0.2444 243  PHE A N   
1789  C CA  . PHE A 243  ? 2.2725 2.7578 2.3101 0.9261  0.2840  -0.2335 243  PHE A CA  
1790  C C   . PHE A 243  ? 2.3666 2.8098 2.3986 0.9439  0.3150  -0.2765 243  PHE A C   
1791  O O   . PHE A 243  ? 2.4408 2.8323 2.4320 0.9563  0.3279  -0.2776 243  PHE A O   
1792  C CB  . PHE A 243  ? 2.2386 2.7600 2.3191 0.9332  0.3251  -0.2117 243  PHE A CB  
1793  C CG  . PHE A 243  ? 2.3402 2.8210 2.3829 0.9467  0.3429  -0.1905 243  PHE A CG  
1794  C CD1 . PHE A 243  ? 2.3943 2.8408 2.3697 0.9395  0.3003  -0.1614 243  PHE A CD1 
1795  C CD2 . PHE A 243  ? 2.3422 2.8215 2.4178 0.9663  0.4031  -0.1991 243  PHE A CD2 
1796  C CE1 . PHE A 243  ? 2.4472 2.8607 2.3870 0.9524  0.3161  -0.1418 243  PHE A CE1 
1797  C CE2 . PHE A 243  ? 2.4187 2.8619 2.4589 0.9798  0.4200  -0.1779 243  PHE A CE2 
1798  C CZ  . PHE A 243  ? 2.4771 2.8888 2.4486 0.9732  0.3760  -0.1491 243  PHE A CZ  
1799  N N   . LYS A 244  ? 3.7085 4.1778 3.7826 0.9448  0.3261  -0.3122 244  LYS A N   
1800  C CA  . LYS A 244  ? 3.8322 4.2678 3.9021 0.9584  0.3451  -0.3566 244  LYS A CA  
1801  C C   . LYS A 244  ? 3.8781 4.2991 3.9171 0.9483  0.2951  -0.3677 244  LYS A C   
1802  O O   . LYS A 244  ? 3.9707 4.3703 4.0085 0.9580  0.3028  -0.4055 244  LYS A O   
1803  C CB  . LYS A 244  ? 3.8063 4.2840 3.9493 0.9684  0.3978  -0.3922 244  LYS A CB  
1804  C CG  . LYS A 244  ? 3.8256 4.3130 4.0020 0.9797  0.4522  -0.3839 244  LYS A CG  
1805  C CD  . LYS A 244  ? 3.8515 4.3399 4.0620 0.9637  0.4853  -0.4105 244  LYS A CD  
1806  C CE  . LYS A 244  ? 3.8611 4.3503 4.0973 0.9602  0.5297  -0.3923 244  LYS A CE  
1807  N NZ  . LYS A 244  ? 3.7640 4.3111 4.0434 0.9528  0.5328  -0.3674 244  LYS A NZ  
1808  N N   . ASN A 245  ? 2.2416 2.6735 2.2561 0.9293  0.2447  -0.3347 245  ASN A N   
1809  C CA  . ASN A 245  ? 2.2575 2.6690 2.2378 0.9194  0.1956  -0.3413 245  ASN A CA  
1810  C C   . ASN A 245  ? 2.2010 2.6103 2.1423 0.8975  0.1379  -0.3024 245  ASN A C   
1811  O O   . ASN A 245  ? 2.1531 2.6049 2.1141 0.8848  0.1295  -0.2712 245  ASN A O   
1812  C CB  . ASN A 245  ? 2.2072 2.6652 2.2390 0.9199  0.2021  -0.3707 245  ASN A CB  
1813  C CG  . ASN A 245  ? 2.1611 2.6865 2.2354 0.9050  0.1933  -0.3486 245  ASN A CG  
1814  O OD1 . ASN A 245  ? 2.1494 2.6950 2.2330 0.8992  0.2009  -0.3177 245  ASN A OD1 
1815  N ND2 . ASN A 245  ? 2.1615 2.7237 2.2616 0.8990  0.1766  -0.3628 245  ASN A ND2 
1816  N N   . PHE A 246  ? 1.3860 1.7461 1.2748 0.8930  0.0992  -0.3074 246  PHE A N   
1817  C CA  . PHE A 246  ? 1.6857 2.0331 1.5322 0.8717  0.0428  -0.2763 246  PHE A CA  
1818  C C   . PHE A 246  ? 1.6466 1.9585 1.4650 0.8701  0.0106  -0.2973 246  PHE A C   
1819  O O   . PHE A 246  ? 1.6815 1.9426 1.4719 0.8838  0.0191  -0.3238 246  PHE A O   
1820  C CB  . PHE A 246  ? 1.5948 1.8954 1.3844 0.8695  0.0311  -0.2531 246  PHE A CB  
1821  C CG  . PHE A 246  ? 1.4365 1.7454 1.1987 0.8461  -0.0145 -0.2119 246  PHE A CG  
1822  C CD1 . PHE A 246  ? 1.4000 1.7660 1.1973 0.8362  -0.0112 -0.1819 246  PHE A CD1 
1823  C CD2 . PHE A 246  ? 1.5589 1.8171 1.2597 0.8341  -0.0587 -0.2036 246  PHE A CD2 
1824  C CE1 . PHE A 246  ? 1.3415 1.7164 1.1143 0.8146  -0.0523 -0.1447 246  PHE A CE1 
1825  C CE2 . PHE A 246  ? 1.5007 1.7672 1.1772 0.8116  -0.0991 -0.1672 246  PHE A CE2 
1826  C CZ  . PHE A 246  ? 1.3990 1.7248 1.1118 0.8019  -0.0961 -0.1377 246  PHE A CZ  
1827  N N   . GLU A 247  ? 2.5479 2.8844 2.3725 0.8540  -0.0260 -0.2850 247  GLU A N   
1828  C CA  . GLU A 247  ? 2.5964 2.8978 2.3944 0.8536  -0.0563 -0.3025 247  GLU A CA  
1829  C C   . GLU A 247  ? 2.7004 2.9479 2.4332 0.8372  -0.1048 -0.2794 247  GLU A C   
1830  O O   . GLU A 247  ? 2.6905 2.9556 2.4162 0.8158  -0.1405 -0.2485 247  GLU A O   
1831  C CB  . GLU A 247  ? 3.1163 3.4717 2.9575 0.8481  -0.0670 -0.3065 247  GLU A CB  
1832  C CG  . GLU A 247  ? 2.9079 3.2467 2.7528 0.8631  -0.0659 -0.3442 247  GLU A CG  
1833  C CD  . GLU A 247  ? 2.2317 2.6134 2.1011 0.8539  -0.0912 -0.3385 247  GLU A CD  
1834  O OE1 . GLU A 247  ? 2.1266 2.5675 2.0319 0.8422  -0.0893 -0.3182 247  GLU A OE1 
1835  O OE2 . GLU A 247  ? 2.1858 2.5435 2.0388 0.8584  -0.1128 -0.3528 247  GLU A OE2 
1836  N N   . ILE A 248  ? 2.1016 2.2833 1.7877 0.8471  -0.1051 -0.2966 248  ILE A N   
1837  C CA  . ILE A 248  ? 2.0884 2.2127 1.7117 0.8333  -0.1486 -0.2829 248  ILE A CA  
1838  C C   . ILE A 248  ? 2.1016 2.1918 1.7098 0.8367  -0.1709 -0.3050 248  ILE A C   
1839  O O   . ILE A 248  ? 2.1417 2.2193 1.7627 0.8572  -0.1465 -0.3402 248  ILE A O   
1840  C CB  . ILE A 248  ? 2.1298 2.1984 1.7047 0.8413  -0.1380 -0.2879 248  ILE A CB  
1841  C CG1 . ILE A 248  ? 2.0751 2.1759 1.6699 0.8463  -0.1042 -0.2726 248  ILE A CG1 
1842  C CG2 . ILE A 248  ? 2.1840 2.2042 1.6966 0.8218  -0.1849 -0.2677 248  ILE A CG2 
1843  C CD1 . ILE A 248  ? 2.1298 2.1818 1.6863 0.8610  -0.0809 -0.2839 248  ILE A CD1 
1844  N N   . THR A 249  ? 2.2180 2.2914 1.7982 0.8166  -0.2169 -0.2840 249  THR A N   
1845  C CA  . THR A 249  ? 2.2761 2.3136 1.8382 0.8178  -0.2429 -0.2987 249  THR A CA  
1846  C C   . THR A 249  ? 2.3871 2.3516 1.8825 0.8062  -0.2768 -0.2919 249  THR A C   
1847  O O   . THR A 249  ? 2.3761 2.3390 1.8484 0.7832  -0.3057 -0.2608 249  THR A O   
1848  C CB  . THR A 249  ? 2.3205 2.4013 1.9084 0.8018  -0.2700 -0.2773 249  THR A CB  
1849  O OG1 . THR A 249  ? 2.2413 2.3892 1.8687 0.7921  -0.2577 -0.2536 249  THR A OG1 
1850  C CG2 . THR A 249  ? 2.3160 2.4137 1.9356 0.8182  -0.2616 -0.3035 249  THR A CG2 
1851  N N   . ILE A 250  ? 2.0072 1.9128 1.4724 0.8212  -0.2734 -0.3215 250  ILE A N   
1852  C CA  . ILE A 250  ? 2.1138 1.9467 1.5150 0.8112  -0.3033 -0.3196 250  ILE A CA  
1853  C C   . ILE A 250  ? 2.2143 2.0102 1.6011 0.8101  -0.3323 -0.3291 250  ILE A C   
1854  O O   . ILE A 250  ? 2.2221 2.0130 1.6271 0.8310  -0.3165 -0.3578 250  ILE A O   
1855  C CB  . ILE A 250  ? 2.1541 1.9398 1.5255 0.8296  -0.2770 -0.3470 250  ILE A CB  
1856  C CG1 . ILE A 250  ? 2.1924 1.9810 1.5953 0.8573  -0.2446 -0.3854 250  ILE A CG1 
1857  C CG2 . ILE A 250  ? 2.0902 1.8992 1.4613 0.8284  -0.2539 -0.3321 250  ILE A CG2 
1858  C CD1 . ILE A 250  ? 2.2688 2.0090 1.6453 0.8773  -0.2173 -0.4168 250  ILE A CD1 
1859  N N   . LYS A 251  ? 2.8176 2.5866 2.1715 0.7861  -0.3739 -0.3055 251  LYS A N   
1860  C CA  . LYS A 251  ? 2.9536 2.6952 2.2998 0.7821  -0.4033 -0.3066 251  LYS A CA  
1861  C C   . LYS A 251  ? 3.1466 2.8064 2.4322 0.7721  -0.4328 -0.3107 251  LYS A C   
1862  O O   . LYS A 251  ? 3.1731 2.8171 2.4294 0.7460  -0.4626 -0.2858 251  LYS A O   
1863  C CB  . LYS A 251  ? 2.9187 2.7099 2.2915 0.7609  -0.4273 -0.2726 251  LYS A CB  
1864  C CG  . LYS A 251  ? 2.8327 2.7078 2.2652 0.7670  -0.4009 -0.2659 251  LYS A CG  
1865  C CD  . LYS A 251  ? 2.8106 2.7303 2.2707 0.7511  -0.4241 -0.2394 251  LYS A CD  
1866  C CE  . LYS A 251  ? 2.8240 2.7338 2.2565 0.7188  -0.4605 -0.2033 251  LYS A CE  
1867  N NZ  . LYS A 251  ? 2.7558 2.7276 2.2254 0.7032  -0.4737 -0.1748 251  LYS A NZ  
1868  N N   . ALA A 252  ? 2.9431 2.5526 2.2120 0.7924  -0.4243 -0.3431 252  ALA A N   
1869  C CA  . ALA A 252  ? 3.0779 2.6064 2.2907 0.7857  -0.4488 -0.3521 252  ALA A CA  
1870  C C   . ALA A 252  ? 3.1332 2.6339 2.3431 0.7810  -0.4785 -0.3478 252  ALA A C   
1871  O O   . ALA A 252  ? 3.1140 2.6479 2.3628 0.7947  -0.4720 -0.3514 252  ALA A O   
1872  C CB  . ALA A 252  ? 3.1382 2.6226 2.3303 0.8101  -0.4221 -0.3899 252  ALA A CB  
1873  N N   . ARG A 253  ? 3.6848 3.1238 2.8481 0.7623  -0.5103 -0.3408 253  ARG A N   
1874  C CA  . ARG A 253  ? 3.7614 3.1675 2.9189 0.7565  -0.5389 -0.3341 253  ARG A CA  
1875  C C   . ARG A 253  ? 3.7985 3.1257 2.8992 0.7374  -0.5679 -0.3342 253  ARG A C   
1876  O O   . ARG A 253  ? 3.8153 3.1359 2.8884 0.7136  -0.5809 -0.3197 253  ARG A O   
1877  C CB  . ARG A 253  ? 3.7799 3.2425 2.9702 0.7380  -0.5565 -0.2984 253  ARG A CB  
1878  C CG  . ARG A 253  ? 3.8551 3.3326 3.0295 0.7048  -0.5764 -0.2674 253  ARG A CG  
1879  C CD  . ARG A 253  ? 3.9384 3.4456 3.1319 0.6825  -0.6036 -0.2330 253  ARG A CD  
1880  N NE  . ARG A 253  ? 4.1088 3.5655 3.2895 0.6833  -0.6253 -0.2345 253  ARG A NE  
1881  C CZ  . ARG A 253  ? 4.1567 3.6291 3.3673 0.7043  -0.6184 -0.2408 253  ARG A CZ  
1882  N NH1 . ARG A 253  ? 4.0844 3.6225 3.3399 0.7250  -0.5906 -0.2486 253  ARG A NH1 
1883  N NH2 . ARG A 253  ? 4.2574 3.6807 3.4536 0.7050  -0.6389 -0.2396 253  ARG A NH2 
1884  N N   . TYR A 254  ? 3.2246 2.4929 2.3086 0.7479  -0.5779 -0.3509 254  TYR A N   
1885  C CA  . TYR A 254  ? 3.2445 2.4336 2.2764 0.7305  -0.6041 -0.3543 254  TYR A CA  
1886  C C   . TYR A 254  ? 3.1924 2.3834 2.2187 0.6961  -0.6395 -0.3182 254  TYR A C   
1887  O O   . TYR A 254  ? 3.0955 2.3450 2.1590 0.6892  -0.6441 -0.2919 254  TYR A O   
1888  C CB  . TYR A 254  ? 3.3328 2.4575 2.3511 0.7529  -0.6031 -0.3824 254  TYR A CB  
1889  C CG  . TYR A 254  ? 3.3267 2.4519 2.3541 0.7875  -0.5673 -0.4191 254  TYR A CG  
1890  C CD1 . TYR A 254  ? 3.3520 2.4770 2.4059 0.8170  -0.5549 -0.4376 254  TYR A CD1 
1891  C CD2 . TYR A 254  ? 3.3157 2.4436 2.3260 0.7908  -0.5456 -0.4348 254  TYR A CD2 
1892  C CE1 . TYR A 254  ? 3.3389 2.4665 2.4032 0.8475  -0.5217 -0.4722 254  TYR A CE1 
1893  C CE2 . TYR A 254  ? 3.3149 2.4430 2.3344 0.8214  -0.5115 -0.4681 254  TYR A CE2 
1894  C CZ  . TYR A 254  ? 3.3283 2.4564 2.3755 0.8490  -0.4996 -0.4875 254  TYR A CZ  
1895  O OH  . TYR A 254  ? 3.3139 2.4440 2.3720 0.8783  -0.4651 -0.5217 254  TYR A OH  
1896  N N   . PHE A 255  ? 3.3630 2.4911 2.3428 0.6736  -0.6636 -0.3180 255  PHE A N   
1897  C CA  . PHE A 255  ? 3.4130 2.5359 2.3840 0.6385  -0.6973 -0.2866 255  PHE A CA  
1898  C C   . PHE A 255  ? 3.5413 2.6454 2.5286 0.6402  -0.7132 -0.2747 255  PHE A C   
1899  O O   . PHE A 255  ? 3.5121 2.6390 2.5123 0.6167  -0.7342 -0.2429 255  PHE A O   
1900  C CB  . PHE A 255  ? 3.4935 2.5553 2.4101 0.6130  -0.7172 -0.2931 255  PHE A CB  
1901  C CG  . PHE A 255  ? 3.4230 2.5209 2.3266 0.5996  -0.7120 -0.2878 255  PHE A CG  
1902  C CD1 . PHE A 255  ? 3.4203 2.5255 2.3064 0.5631  -0.7382 -0.2643 255  PHE A CD1 
1903  C CD2 . PHE A 255  ? 3.3603 2.4878 2.2714 0.6238  -0.6801 -0.3054 255  PHE A CD2 
1904  C CE1 . PHE A 255  ? 3.3750 2.5171 2.2499 0.5526  -0.7337 -0.2580 255  PHE A CE1 
1905  C CE2 . PHE A 255  ? 3.3100 2.4715 2.2097 0.6135  -0.6743 -0.2980 255  PHE A CE2 
1906  C CZ  . PHE A 255  ? 3.3227 2.4924 2.2039 0.5785  -0.7018 -0.2740 255  PHE A CZ  
1907  N N   . TYR A 256  ? 4.0853 3.1500 3.0729 0.6689  -0.7025 -0.2993 256  TYR A N   
1908  C CA  . TYR A 256  ? 4.2535 3.2988 3.2561 0.6758  -0.7155 -0.2888 256  TYR A CA  
1909  C C   . TYR A 256  ? 4.3407 3.4624 3.3973 0.6943  -0.7029 -0.2747 256  TYR A C   
1910  O O   . TYR A 256  ? 4.4306 3.5449 3.5044 0.7201  -0.6969 -0.2837 256  TYR A O   
1911  C CB  . TYR A 256  ? 4.3177 3.2821 3.2947 0.6967  -0.7137 -0.3190 256  TYR A CB  
1912  C CG  . TYR A 256  ? 4.2467 3.2062 3.2217 0.7286  -0.6832 -0.3574 256  TYR A CG  
1913  C CD1 . TYR A 256  ? 4.1881 3.1862 3.2010 0.7631  -0.6601 -0.3704 256  TYR A CD1 
1914  C CD2 . TYR A 256  ? 4.2625 3.1792 3.1972 0.7240  -0.6774 -0.3813 256  TYR A CD2 
1915  C CE1 . TYR A 256  ? 4.1409 3.1349 3.1537 0.7913  -0.6312 -0.4061 256  TYR A CE1 
1916  C CE2 . TYR A 256  ? 4.2325 3.1438 3.1650 0.7528  -0.6484 -0.4158 256  TYR A CE2 
1917  C CZ  . TYR A 256  ? 4.1687 3.1181 3.1411 0.7860  -0.6251 -0.4281 256  TYR A CZ  
1918  O OH  . TYR A 256  ? 4.1284 3.0731 3.1004 0.8138  -0.5952 -0.4632 256  TYR A OH  
1919  N N   . ASN A 257  ? 5.3166 4.5126 4.3993 0.6803  -0.6994 -0.2525 257  ASN A N   
1920  C CA  . ASN A 257  ? 5.2993 4.5766 4.4337 0.6919  -0.6883 -0.2366 257  ASN A CA  
1921  C C   . ASN A 257  ? 5.2261 4.5254 4.3898 0.7318  -0.6615 -0.2626 257  ASN A C   
1922  O O   . ASN A 257  ? 5.1945 4.5227 4.3879 0.7446  -0.6631 -0.2531 257  ASN A O   
1923  C CB  . ASN A 257  ? 5.4579 4.7466 4.6044 0.6720  -0.7146 -0.2002 257  ASN A CB  
1924  C CG  . ASN A 257  ? 5.7147 4.9301 4.8398 0.6770  -0.7322 -0.2023 257  ASN A CG  
1925  O OD1 . ASN A 257  ? 5.8544 4.9936 4.9381 0.6669  -0.7441 -0.2140 257  ASN A OD1 
1926  N ND2 . ASN A 257  ? 5.7502 4.9887 4.9036 0.6929  -0.7336 -0.1906 257  ASN A ND2 
1927  N N   . LYS A 258  ? 3.8332 3.1213 2.9887 0.7510  -0.6365 -0.2954 258  LYS A N   
1928  C CA  . LYS A 258  ? 3.8079 3.1212 2.9926 0.7879  -0.6075 -0.3239 258  LYS A CA  
1929  C C   . LYS A 258  ? 3.6530 2.9947 2.8429 0.7965  -0.5768 -0.3449 258  LYS A C   
1930  O O   . LYS A 258  ? 3.7094 3.0022 2.8625 0.7940  -0.5726 -0.3624 258  LYS A O   
1931  C CB  . LYS A 258  ? 3.9566 3.1969 3.1185 0.8097  -0.6097 -0.3499 258  LYS A CB  
1932  C CG  . LYS A 258  ? 4.0170 3.2616 3.2010 0.8253  -0.6204 -0.3410 258  LYS A CG  
1933  C CD  . LYS A 258  ? 3.9604 3.2738 3.1931 0.8573  -0.5936 -0.3572 258  LYS A CD  
1934  C CE  . LYS A 258  ? 4.0076 3.3245 3.2590 0.8754  -0.6049 -0.3493 258  LYS A CE  
1935  N NZ  . LYS A 258  ? 3.9360 3.3292 3.2370 0.9040  -0.5810 -0.3636 258  LYS A NZ  
1936  N N   . VAL A 259  ? 3.5729 2.9942 2.8090 0.8064  -0.5545 -0.3428 259  VAL A N   
1937  C CA  . VAL A 259  ? 3.4330 2.8863 2.6804 0.8160  -0.5220 -0.3610 259  VAL A CA  
1938  C C   . VAL A 259  ? 3.4459 2.8532 2.6774 0.8431  -0.5000 -0.4018 259  VAL A C   
1939  O O   . VAL A 259  ? 3.4857 2.8579 2.7137 0.8609  -0.5044 -0.4181 259  VAL A O   
1940  C CB  . VAL A 259  ? 3.2540 2.7981 2.5601 0.8281  -0.4978 -0.3586 259  VAL A CB  
1941  C CG1 . VAL A 259  ? 3.2027 2.7962 2.5311 0.8062  -0.5196 -0.3200 259  VAL A CG1 
1942  C CG2 . VAL A 259  ? 3.2725 2.8279 2.6068 0.8616  -0.4790 -0.3878 259  VAL A CG2 
1943  N N   . VAL A 260  ? 3.3333 2.7422 2.5558 0.8469  -0.4755 -0.4178 260  VAL A N   
1944  C CA  . VAL A 260  ? 3.3814 2.7590 2.5960 0.8740  -0.4480 -0.4577 260  VAL A CA  
1945  C C   . VAL A 260  ? 3.3554 2.7893 2.6234 0.9019  -0.4202 -0.4768 260  VAL A C   
1946  O O   . VAL A 260  ? 3.2771 2.7813 2.5875 0.8986  -0.4159 -0.4600 260  VAL A O   
1947  C CB  . VAL A 260  ? 3.3297 2.7041 2.5253 0.8713  -0.4253 -0.4670 260  VAL A CB  
1948  C CG1 . VAL A 260  ? 3.3668 2.7134 2.5580 0.9001  -0.3936 -0.5087 260  VAL A CG1 
1949  C CG2 . VAL A 260  ? 3.3657 2.6891 2.5074 0.8437  -0.4524 -0.4503 260  VAL A CG2 
1950  N N   . THR A 261  ? 2.6544 2.0592 1.9211 0.9289  -0.4013 -0.5130 261  THR A N   
1951  C CA  . THR A 261  ? 2.6413 2.1017 1.9578 0.9556  -0.3676 -0.5377 261  THR A CA  
1952  C C   . THR A 261  ? 2.6556 2.1082 1.9660 0.9668  -0.3313 -0.5652 261  THR A C   
1953  O O   . THR A 261  ? 2.6400 2.1147 1.9486 0.9527  -0.3207 -0.5517 261  THR A O   
1954  C CB  . THR A 261  ? 2.6959 2.1445 2.0265 0.9802  -0.3718 -0.5574 261  THR A CB  
1955  O OG1 . THR A 261  ? 2.7397 2.1757 2.0614 0.9670  -0.4094 -0.5282 261  THR A OG1 
1956  C CG2 . THR A 261  ? 2.6421 2.1682 2.0330 1.0028  -0.3423 -0.5759 261  THR A CG2 
1957  N N   . GLU A 262  ? 4.4648 3.8860 3.7715 0.9919  -0.3115 -0.6024 262  GLU A N   
1958  C CA  . GLU A 262  ? 4.5147 3.9314 3.8173 1.0020  -0.2747 -0.6271 262  GLU A CA  
1959  C C   . GLU A 262  ? 4.5441 3.9160 3.7951 0.9808  -0.2843 -0.6121 262  GLU A C   
1960  O O   . GLU A 262  ? 4.5929 3.9040 3.7973 0.9677  -0.3149 -0.6033 262  GLU A O   
1961  C CB  . GLU A 262  ? 4.6539 4.0370 3.9553 1.0309  -0.2529 -0.6701 262  GLU A CB  
1962  C CG  . GLU A 262  ? 4.7444 4.1286 4.0462 1.0417  -0.2108 -0.6954 262  GLU A CG  
1963  C CD  . GLU A 262  ? 4.8937 4.2366 4.1874 1.0680  -0.1903 -0.7380 262  GLU A CD  
1964  O OE1 . GLU A 262  ? 4.9731 4.2736 4.2334 1.0704  -0.1729 -0.7538 262  GLU A OE1 
1965  O OE2 . GLU A 262  ? 4.9280 4.2826 4.2488 1.0867  -0.1915 -0.7554 262  GLU A OE2 
1966  N N   . ALA A 263  ? 3.6839 3.0885 2.9446 0.9775  -0.2575 -0.6089 263  ALA A N   
1967  C CA  . ALA A 263  ? 3.7336 3.1035 2.9477 0.9617  -0.2597 -0.5979 263  ALA A CA  
1968  C C   . ALA A 263  ? 3.6628 3.0696 2.8984 0.9716  -0.2159 -0.6076 263  ALA A C   
1969  O O   . ALA A 263  ? 3.6058 3.0782 2.8945 0.9781  -0.1939 -0.6062 263  ALA A O   
1970  C CB  . ALA A 263  ? 3.7508 3.1312 2.9494 0.9308  -0.2947 -0.5559 263  ALA A CB  
1971  N N   . ASP A 264  ? 4.6401 4.0046 3.8346 0.9729  -0.2027 -0.6177 264  ASP A N   
1972  C CA  . ASP A 264  ? 4.6052 4.0023 3.8183 0.9816  -0.1612 -0.6230 264  ASP A CA  
1973  C C   . ASP A 264  ? 4.5444 3.9766 3.7551 0.9591  -0.1708 -0.5833 264  ASP A C   
1974  O O   . ASP A 264  ? 4.5319 3.9368 3.7005 0.9375  -0.2053 -0.5593 264  ASP A O   
1975  C CB  . ASP A 264  ? 4.7470 4.0899 3.9203 0.9951  -0.1377 -0.6504 264  ASP A CB  
1976  C CG  . ASP A 264  ? 4.8115 4.1788 4.0243 1.0217  -0.0848 -0.6835 264  ASP A CG  
1977  O OD1 . ASP A 264  ? 4.7520 4.1858 4.0176 1.0221  -0.0662 -0.6731 264  ASP A OD1 
1978  O OD2 . ASP A 264  ? 4.9225 4.2440 4.1126 1.0386  -0.0655 -0.7161 264  ASP A OD2 
1979  N N   . VAL A 265  ? 2.9552 2.4481 2.2120 0.9646  -0.1387 -0.5779 265  VAL A N   
1980  C CA  . VAL A 265  ? 2.8425 2.3779 2.1074 0.9463  -0.1436 -0.5408 265  VAL A CA  
1981  C C   . VAL A 265  ? 2.8691 2.4033 2.1218 0.9535  -0.1082 -0.5417 265  VAL A C   
1982  O O   . VAL A 265  ? 2.8983 2.4451 2.1790 0.9740  -0.0654 -0.5664 265  VAL A O   
1983  C CB  . VAL A 265  ? 2.6298 2.2404 1.9611 0.9460  -0.1355 -0.5308 265  VAL A CB  
1984  C CG1 . VAL A 265  ? 2.5151 2.1733 1.8605 0.9298  -0.1347 -0.4948 265  VAL A CG1 
1985  C CG2 . VAL A 265  ? 2.6047 2.2153 1.9417 0.9375  -0.1734 -0.5246 265  VAL A CG2 
1986  N N   . TYR A 266  ? 4.1542 3.6730 3.3647 0.9372  -0.1252 -0.5151 266  TYR A N   
1987  C CA  . TYR A 266  ? 4.1870 3.7104 3.3867 0.9441  -0.0924 -0.5101 266  TYR A CA  
1988  C C   . TYR A 266  ? 4.0602 3.6281 3.2666 0.9259  -0.1039 -0.4680 266  TYR A C   
1989  O O   . TYR A 266  ? 4.0676 3.6213 3.2371 0.9046  -0.1436 -0.4439 266  TYR A O   
1990  C CB  . TYR A 266  ? 4.3921 3.8478 3.5252 0.9473  -0.0953 -0.5234 266  TYR A CB  
1991  C CG  . TYR A 266  ? 4.5852 4.0033 3.7164 0.9712  -0.0661 -0.5666 266  TYR A CG  
1992  C CD1 . TYR A 266  ? 4.6828 4.0766 3.8201 0.9768  -0.0810 -0.5915 266  TYR A CD1 
1993  C CD2 . TYR A 266  ? 4.7023 4.1091 3.8256 0.9887  -0.0233 -0.5820 266  TYR A CD2 
1994  C CE1 . TYR A 266  ? 4.7983 4.1599 3.9354 0.9991  -0.0548 -0.6316 266  TYR A CE1 
1995  C CE2 . TYR A 266  ? 4.8220 4.1955 3.9447 1.0100  0.0041  -0.6224 266  TYR A CE2 
1996  C CZ  . TYR A 266  ? 4.8699 4.2218 4.0001 1.0151  -0.0122 -0.6476 266  TYR A CZ  
1997  O OH  . TYR A 266  ? 4.9313 4.2522 4.0624 1.0367  0.0146  -0.6881 266  TYR A OH  
1998  N N   . ILE A 267  ? 2.4259 2.0483 1.6805 0.9338  -0.0689 -0.4598 267  ILE A N   
1999  C CA  . ILE A 267  ? 2.2861 1.9533 1.5503 0.9179  -0.0784 -0.4195 267  ILE A CA  
2000  C C   . ILE A 267  ? 2.2754 1.9584 1.5402 0.9276  -0.0415 -0.4073 267  ILE A C   
2001  O O   . ILE A 267  ? 2.2860 1.9975 1.5954 0.9448  0.0036  -0.4195 267  ILE A O   
2002  C CB  . ILE A 267  ? 2.2025 1.9336 1.5287 0.9114  -0.0804 -0.4073 267  ILE A CB  
2003  C CG1 . ILE A 267  ? 2.1702 1.8903 1.5043 0.9073  -0.1085 -0.4226 267  ILE A CG1 
2004  C CG2 . ILE A 267  ? 2.1512 1.9178 1.4751 0.8898  -0.1049 -0.3640 267  ILE A CG2 
2005  C CD1 . ILE A 267  ? 2.0543 1.8386 1.4493 0.9031  -0.1082 -0.4139 267  ILE A CD1 
2006  N N   . THR A 268  ? 3.1486 2.8150 2.3648 0.9165  -0.0604 -0.3824 268  THR A N   
2007  C CA  . THR A 268  ? 3.1311 2.8182 2.3489 0.9253  -0.0283 -0.3643 268  THR A CA  
2008  C C   . THR A 268  ? 3.0483 2.8008 2.3056 0.9130  -0.0334 -0.3269 268  THR A C   
2009  O O   . THR A 268  ? 3.0072 2.7861 2.2848 0.8958  -0.0650 -0.3145 268  THR A O   
2010  C CB  . THR A 268  ? 3.2599 2.8999 2.4059 0.9246  -0.0375 -0.3581 268  THR A CB  
2011  O OG1 . THR A 268  ? 3.2826 2.9107 2.3869 0.8997  -0.0908 -0.3372 268  THR A OG1 
2012  C CG2 . THR A 268  ? 3.3586 2.9386 2.4736 0.9407  -0.0216 -0.3979 268  THR A CG2 
2013  N N   . PHE A 269  ? 3.3894 3.1678 2.6594 0.9231  -0.0002 -0.3092 269  PHE A N   
2014  C CA  . PHE A 269  ? 3.2602 3.0970 2.5605 0.9124  -0.0048 -0.2709 269  PHE A CA  
2015  C C   . PHE A 269  ? 3.2013 3.0360 2.4708 0.9192  0.0101  -0.2469 269  PHE A C   
2016  O O   . PHE A 269  ? 3.2942 3.0857 2.5251 0.9334  0.0290  -0.2618 269  PHE A O   
2017  C CB  . PHE A 269  ? 3.1990 3.0877 2.5746 0.9227  0.0335  -0.2764 269  PHE A CB  
2018  C CG  . PHE A 269  ? 3.1767 3.0686 2.5861 0.9229  0.0304  -0.3061 269  PHE A CG  
2019  C CD1 . PHE A 269  ? 3.2117 3.0806 2.6354 0.9428  0.0655  -0.3455 269  PHE A CD1 
2020  C CD2 . PHE A 269  ? 3.1145 3.0337 2.5410 0.9035  -0.0077 -0.2946 269  PHE A CD2 
2021  C CE1 . PHE A 269  ? 3.1964 3.0720 2.6517 0.9442  0.0620  -0.3729 269  PHE A CE1 
2022  C CE2 . PHE A 269  ? 3.0969 3.0214 2.5537 0.9051  -0.0110 -0.3206 269  PHE A CE2 
2023  C CZ  . PHE A 269  ? 3.1402 3.0441 2.6117 0.9258  0.0234  -0.3599 269  PHE A CZ  
2024  N N   . GLY A 270  ? 3.6403 3.5235 2.9275 0.9100  0.0030  -0.2092 270  GLY A N   
2025  C CA  . GLY A 270  ? 3.6431 3.5299 2.9030 0.9177  0.0168  -0.1827 270  GLY A CA  
2026  C C   . GLY A 270  ? 3.5087 3.4582 2.8067 0.9131  0.0211  -0.1436 270  GLY A C   
2027  O O   . GLY A 270  ? 3.4652 3.4568 2.8062 0.8992  0.0054  -0.1342 270  GLY A O   
2028  N N   . ILE A 271  ? 2.4968 2.4529 1.7798 0.9262  0.0446  -0.1210 271  ILE A N   
2029  C CA  . ILE A 271  ? 2.3414 2.3514 1.6443 0.9209  0.0400  -0.0786 271  ILE A CA  
2030  C C   . ILE A 271  ? 2.4077 2.4066 1.6452 0.9048  -0.0078 -0.0543 271  ILE A C   
2031  O O   . ILE A 271  ? 2.4818 2.4373 1.6707 0.8932  -0.0408 -0.0722 271  ILE A O   
2032  C CB  . ILE A 271  ? 2.2621 2.2915 1.5959 0.9461  0.0969  -0.0666 271  ILE A CB  
2033  C CG1 . ILE A 271  ? 2.2295 2.2445 1.6064 0.9641  0.1462  -0.1042 271  ILE A CG1 
2034  C CG2 . ILE A 271  ? 2.1751 2.2703 1.5605 0.9408  0.0996  -0.0324 271  ILE A CG2 
2035  C CD1 . ILE A 271  ? 2.1009 2.1568 1.5458 0.9556  0.1491  -0.1151 271  ILE A CD1 
2036  N N   . ARG A 272  ? 2.9444 2.9835 2.1817 0.9035  -0.0123 -0.0146 272  ARG A N   
2037  C CA  . ARG A 272  ? 3.0687 3.1116 2.2545 0.8837  -0.0627 0.0098  272  ARG A CA  
2038  C C   . ARG A 272  ? 3.1168 3.2210 2.3304 0.8844  -0.0590 0.0529  272  ARG A C   
2039  O O   . ARG A 272  ? 3.0477 3.1858 2.3195 0.8984  -0.0200 0.0603  272  ARG A O   
2040  C CB  . ARG A 272  ? 3.0185 3.0587 2.2026 0.8547  -0.1122 0.0005  272  ARG A CB  
2041  C CG  . ARG A 272  ? 3.0422 3.0860 2.1773 0.8301  -0.1665 0.0218  272  ARG A CG  
2042  C CD  . ARG A 272  ? 3.0242 3.0479 2.1561 0.8053  -0.2065 0.0028  272  ARG A CD  
2043  N NE  . ARG A 272  ? 3.0778 3.0863 2.1549 0.7802  -0.2587 0.0111  272  ARG A NE  
2044  C CZ  . ARG A 272  ? 3.1396 3.1025 2.1862 0.7633  -0.2906 -0.0131 272  ARG A CZ  
2045  N NH1 . ARG A 272  ? 3.1479 3.0775 2.2128 0.7708  -0.2759 -0.0459 272  ARG A NH1 
2046  N NH2 . ARG A 272  ? 3.1886 3.1395 2.1872 0.7393  -0.3366 -0.0053 272  ARG A NH2 
2047  N N   . GLU A 273  ? 2.7163 2.8372 1.8912 0.8695  -0.0985 0.0809  273  GLU A N   
2048  C CA  . GLU A 273  ? 2.7519 2.9359 1.9578 0.8696  -0.0970 0.1225  273  GLU A CA  
2049  C C   . GLU A 273  ? 2.7033 2.9249 1.9259 0.8389  -0.1447 0.1373  273  GLU A C   
2050  O O   . GLU A 273  ? 2.6219 2.8925 1.9046 0.8353  -0.1363 0.1517  273  GLU A O   
2051  C CB  . GLU A 273  ? 2.9226 3.1117 2.0816 0.8821  -0.0955 0.1506  273  GLU A CB  
2052  C CG  . GLU A 273  ? 3.0048 3.1924 2.1828 0.9165  -0.0347 0.1566  273  GLU A CG  
2053  C CD  . GLU A 273  ? 2.9543 3.1623 2.2107 0.9269  0.0083  0.1464  273  GLU A CD  
2054  O OE1 . GLU A 273  ? 2.8794 3.1437 2.1863 0.9234  0.0108  0.1729  273  GLU A OE1 
2055  O OE2 . GLU A 273  ? 2.9840 3.1531 2.2517 0.9380  0.0390  0.1107  273  GLU A OE2 
2056  N N   . ASP A 274  ? 4.0550 4.2524 3.2247 0.8161  -0.1938 0.1321  274  ASP A N   
2057  C CA  . ASP A 274  ? 4.0145 4.2439 3.1927 0.7846  -0.2422 0.1471  274  ASP A CA  
2058  C C   . ASP A 274  ? 4.0847 4.2638 3.2221 0.7622  -0.2818 0.1190  274  ASP A C   
2059  O O   . ASP A 274  ? 4.1091 4.2319 3.2228 0.7725  -0.2679 0.0858  274  ASP A O   
2060  C CB  . ASP A 274  ? 4.0533 4.3283 3.2119 0.7764  -0.2672 0.1873  274  ASP A CB  
2061  C CG  . ASP A 274  ? 4.5640 4.8077 3.6496 0.7832  -0.2768 0.1881  274  ASP A CG  
2062  O OD1 . ASP A 274  ? 4.6080 4.8723 3.6595 0.7646  -0.3176 0.2078  274  ASP A OD1 
2063  O OD2 . ASP A 274  ? 4.6182 4.8194 3.6810 0.8068  -0.2436 0.1692  274  ASP A OD2 
2064  N N   . LEU A 275  ? 2.8431 3.0427 1.9750 0.7316  -0.3295 0.1324  275  LEU A N   
2065  C CA  . LEU A 275  ? 2.9426 3.0956 2.0343 0.7073  -0.3707 0.1097  275  LEU A CA  
2066  C C   . LEU A 275  ? 3.1466 3.2787 2.1668 0.6948  -0.4052 0.1144  275  LEU A C   
2067  O O   . LEU A 275  ? 3.2064 3.2995 2.1891 0.6728  -0.4412 0.0968  275  LEU A O   
2068  C CB  . LEU A 275  ? 2.8175 2.9966 1.9466 0.6796  -0.4014 0.1159  275  LEU A CB  
2069  C CG  . LEU A 275  ? 2.6808 2.8722 1.8725 0.6846  -0.3794 0.1037  275  LEU A CG  
2070  C CD1 . LEU A 275  ? 2.6405 2.8274 1.8393 0.6546  -0.4195 0.0994  275  LEU A CD1 
2071  C CD2 . LEU A 275  ? 2.6845 2.8301 1.8792 0.7107  -0.3399 0.0688  275  LEU A CD2 
2072  N N   . LYS A 276  ? 2.8336 2.9925 1.8358 0.7090  -0.3933 0.1379  276  LYS A N   
2073  C CA  . LYS A 276  ? 3.0067 3.1514 1.9406 0.7008  -0.4215 0.1423  276  LYS A CA  
2074  C C   . LYS A 276  ? 3.1991 3.2985 2.0909 0.7293  -0.3888 0.1243  276  LYS A C   
2075  O O   . LYS A 276  ? 3.3386 3.4280 2.1729 0.7295  -0.4027 0.1282  276  LYS A O   
2076  C CB  . LYS A 276  ? 2.9276 3.1410 1.8665 0.6943  -0.4383 0.1846  276  LYS A CB  
2077  C CG  . LYS A 276  ? 2.9650 3.1770 1.8407 0.6727  -0.4839 0.1902  276  LYS A CG  
2078  C CD  . LYS A 276  ? 2.8833 3.1683 1.7652 0.6702  -0.4973 0.2327  276  LYS A CD  
2079  C CE  . LYS A 276  ? 2.8289 3.1276 1.6916 0.7044  -0.4629 0.2504  276  LYS A CE  
2080  N NZ  . LYS A 276  ? 2.9284 3.1819 1.7152 0.7108  -0.4688 0.2326  276  LYS A NZ  
2081  N N   . ASP A 277  ? 3.1846 3.2590 2.1063 0.7528  -0.3448 0.1043  277  ASP A N   
2082  C CA  . ASP A 277  ? 3.3591 3.3891 2.2498 0.7810  -0.3075 0.0846  277  ASP A CA  
2083  C C   . ASP A 277  ? 3.4460 3.4055 2.3092 0.7762  -0.3135 0.0404  277  ASP A C   
2084  O O   . ASP A 277  ? 3.4016 3.3475 2.3054 0.7769  -0.3013 0.0202  277  ASP A O   
2085  C CB  . ASP A 277  ? 3.3685 3.4203 2.3152 0.8111  -0.2505 0.0916  277  ASP A CB  
2086  C CG  . ASP A 277  ? 3.5342 3.5478 2.4517 0.8416  -0.2077 0.0779  277  ASP A CG  
2087  O OD1 . ASP A 277  ? 3.6810 3.6591 2.5328 0.8409  -0.2226 0.0684  277  ASP A OD1 
2088  O OD2 . ASP A 277  ? 3.5109 3.5306 2.4714 0.8660  -0.1581 0.0761  277  ASP A OD2 
2089  N N   . ASP A 278  ? 4.3597 4.2764 3.1543 0.7719  -0.3322 0.0252  278  ASP A N   
2090  C CA  . ASP A 278  ? 4.4072 4.2543 3.1696 0.7674  -0.3397 -0.0168 278  ASP A CA  
2091  C C   . ASP A 278  ? 4.3657 4.1745 3.1385 0.7980  -0.2889 -0.0440 278  ASP A C   
2092  O O   . ASP A 278  ? 4.4033 4.1549 3.1544 0.7985  -0.2892 -0.0801 278  ASP A O   
2093  C CB  . ASP A 278  ? 4.9404 4.7549 3.6260 0.7519  -0.3758 -0.0258 278  ASP A CB  
2094  C CG  . ASP A 278  ? 4.9825 4.8193 3.6280 0.7663  -0.3660 -0.0032 278  ASP A CG  
2095  O OD1 . ASP A 278  ? 4.9233 4.7868 3.5951 0.7930  -0.3247 0.0145  278  ASP A OD1 
2096  O OD2 . ASP A 278  ? 5.0711 4.8990 3.6583 0.7510  -0.3993 -0.0035 278  ASP A OD2 
2097  N N   . GLN A 279  ? 2.9542 2.7955 1.7628 0.8231  -0.2449 -0.0265 279  GLN A N   
2098  C CA  . GLN A 279  ? 2.9026 2.7144 1.7238 0.8532  -0.1918 -0.0486 279  GLN A CA  
2099  C C   . GLN A 279  ? 2.6791 2.5311 1.5756 0.8699  -0.1497 -0.0376 279  GLN A C   
2100  O O   . GLN A 279  ? 2.5723 2.4777 1.4972 0.8743  -0.1403 -0.0026 279  GLN A O   
2101  C CB  . GLN A 279  ? 3.0691 2.8625 1.8366 0.8732  -0.1709 -0.0441 279  GLN A CB  
2102  C CG  . GLN A 279  ? 3.1300 2.8974 1.9130 0.9053  -0.1116 -0.0627 279  GLN A CG  
2103  C CD  . GLN A 279  ? 3.2023 2.9085 1.9754 0.9073  -0.1049 -0.1099 279  GLN A CD  
2104  O OE1 . GLN A 279  ? 3.1608 2.8566 1.9755 0.9249  -0.0640 -0.1297 279  GLN A OE1 
2105  N NE2 . GLN A 279  ? 3.3109 2.9772 2.0300 0.8891  -0.1448 -0.1288 279  GLN A NE2 
2106  N N   . LYS A 280  ? 3.1031 2.9277 2.0307 0.8802  -0.1229 -0.0699 280  LYS A N   
2107  C CA  . LYS A 280  ? 2.9372 2.7957 1.9391 0.8921  -0.0862 -0.0688 280  LYS A CA  
2108  C C   . LYS A 280  ? 2.9645 2.7853 1.9762 0.9180  -0.0362 -0.1016 280  LYS A C   
2109  O O   . LYS A 280  ? 3.0435 2.8146 2.0329 0.9177  -0.0408 -0.1372 280  LYS A O   
2110  C CB  . LYS A 280  ? 2.7946 2.6692 1.8365 0.8705  -0.1149 -0.0763 280  LYS A CB  
2111  C CG  . LYS A 280  ? 2.7794 2.5987 1.7914 0.8585  -0.1421 -0.1124 280  LYS A CG  
2112  C CD  . LYS A 280  ? 2.7983 2.6003 1.7519 0.8324  -0.1977 -0.1037 280  LYS A CD  
2113  C CE  . LYS A 280  ? 2.8235 2.5700 1.7511 0.8199  -0.2246 -0.1380 280  LYS A CE  
2114  N NZ  . LYS A 280  ? 2.8650 2.5963 1.7397 0.7926  -0.2774 -0.1296 280  LYS A NZ  
2115  N N   . GLU A 281  ? 2.5570 2.4020 1.6041 0.9405  0.0127  -0.0896 281  GLU A N   
2116  C CA  . GLU A 281  ? 2.6107 2.4218 1.6640 0.9661  0.0644  -0.1171 281  GLU A CA  
2117  C C   . GLU A 281  ? 2.4724 2.2801 1.5824 0.9691  0.0852  -0.1512 281  GLU A C   
2118  O O   . GLU A 281  ? 2.3552 2.2004 1.5291 0.9774  0.1180  -0.1470 281  GLU A O   
2119  C CB  . GLU A 281  ? 2.7138 2.5505 1.7832 0.9887  0.1101  -0.0901 281  GLU A CB  
2120  C CG  . GLU A 281  ? 2.8825 2.7490 1.9164 0.9826  0.0838  -0.0458 281  GLU A CG  
2121  C CD  . GLU A 281  ? 3.1388 2.9657 2.0889 0.9769  0.0524  -0.0488 281  GLU A CD  
2122  O OE1 . GLU A 281  ? 3.2527 3.0252 2.1697 0.9826  0.0598  -0.0835 281  GLU A OE1 
2123  O OE2 . GLU A 281  ? 3.2143 3.0664 2.1322 0.9666  0.0202  -0.0169 281  GLU A OE2 
2124  N N   . MET A 282  ? 2.5467 2.3090 1.6315 0.9627  0.0662  -0.1859 282  MET A N   
2125  C CA  . MET A 282  ? 2.5101 2.2649 1.6403 0.9666  0.0828  -0.2213 282  MET A CA  
2126  C C   . MET A 282  ? 2.5051 2.2772 1.6921 0.9897  0.1444  -0.2328 282  MET A C   
2127  O O   . MET A 282  ? 2.5201 2.3086 1.7153 1.0046  0.1796  -0.2123 282  MET A O   
2128  C CB  . MET A 282  ? 2.5971 2.2887 1.6835 0.9679  0.0719  -0.2601 282  MET A CB  
2129  C CG  . MET A 282  ? 2.6238 2.2911 1.6646 0.9437  0.0122  -0.2611 282  MET A CG  
2130  S SD  . MET A 282  ? 2.6020 2.2976 1.6873 0.9211  -0.0260 -0.2620 282  MET A SD  
2131  C CE  . MET A 282  ? 2.2601 1.9967 1.3272 0.8971  -0.0689 -0.2126 282  MET A CE  
2132  N N   . MET A 283  ? 2.9311 2.6974 2.1563 0.9923  0.1560  -0.2677 283  MET A N   
2133  C CA  . MET A 283  ? 2.9831 2.7703 2.2728 1.0093  0.2090  -0.2868 283  MET A CA  
2134  C C   . MET A 283  ? 3.1765 2.9172 2.4564 1.0185  0.2200  -0.3334 283  MET A C   
2135  O O   . MET A 283  ? 3.2010 2.9110 2.4465 1.0069  0.1801  -0.3481 283  MET A O   
2136  C CB  . MET A 283  ? 2.8535 2.6983 2.2105 0.9976  0.2012  -0.2801 283  MET A CB  
2137  C CG  . MET A 283  ? 2.9557 2.8531 2.3292 0.9869  0.1879  -0.2330 283  MET A CG  
2138  S SD  . MET A 283  ? 2.0479 2.0153 1.4916 0.9692  0.1703  -0.2189 283  MET A SD  
2139  C CE  . MET A 283  ? 1.9937 1.9358 1.4027 0.9463  0.1071  -0.2323 283  MET A CE  
2140  N N   . GLN A 284  ? 3.7352 3.4699 3.0451 1.0394  0.2751  -0.3566 284  GLN A N   
2141  C CA  . GLN A 284  ? 3.8808 3.5805 3.1947 1.0497  0.2921  -0.4031 284  GLN A CA  
2142  C C   . GLN A 284  ? 3.8565 3.5969 3.2434 1.0481  0.3027  -0.4242 284  GLN A C   
2143  O O   . GLN A 284  ? 3.7776 3.5707 3.2095 1.0398  0.3006  -0.4025 284  GLN A O   
2144  C CB  . GLN A 284  ? 3.9786 3.6488 3.2835 1.0727  0.3469  -0.4181 284  GLN A CB  
2145  C CG  . GLN A 284  ? 3.9277 3.6365 3.2844 1.0850  0.3989  -0.4015 284  GLN A CG  
2146  C CD  . GLN A 284  ? 3.9042 3.6286 3.2345 1.0831  0.3925  -0.3523 284  GLN A CD  
2147  O OE1 . GLN A 284  ? 3.8609 3.5927 3.1569 1.0663  0.3426  -0.3251 284  GLN A OE1 
2148  N NE2 . GLN A 284  ? 3.9398 3.6701 3.2876 1.1007  0.4444  -0.3408 284  GLN A NE2 
2149  N N   . THR A 285  ? 3.6399 3.3578 3.0380 1.0560  0.3131  -0.4668 285  THR A N   
2150  C CA  . THR A 285  ? 3.5995 3.3559 3.0637 1.0556  0.3218  -0.4910 285  THR A CA  
2151  C C   . THR A 285  ? 3.4958 3.2839 2.9701 1.0345  0.2701  -0.4734 285  THR A C   
2152  O O   . THR A 285  ? 3.3969 3.2371 2.9312 1.0306  0.2768  -0.4747 285  THR A O   
2153  C CB  . THR A 285  ? 3.6003 3.4022 3.1321 1.0663  0.3768  -0.4921 285  THR A CB  
2154  O OG1 . THR A 285  ? 3.6957 3.4694 3.2100 1.0830  0.4216  -0.4925 285  THR A OG1 
2155  C CG2 . THR A 285  ? 3.6008 3.4271 3.1930 1.0726  0.3991  -0.5335 285  THR A CG2 
2156  N N   . ALA A 286  ? 4.4157 4.1722 3.8310 1.0204  0.2196  -0.4574 286  ALA A N   
2157  C CA  . ALA A 286  ? 4.3214 4.0966 3.7373 0.9997  0.1674  -0.4431 286  ALA A CA  
2158  C C   . ALA A 286  ? 4.3171 4.0648 3.7289 1.0011  0.1485  -0.4784 286  ALA A C   
2159  O O   . ALA A 286  ? 4.3637 4.0547 3.7237 1.0041  0.1347  -0.4941 286  ALA A O   
2160  C CB  . ALA A 286  ? 4.3382 4.0946 3.6949 0.9825  0.1237  -0.4078 286  ALA A CB  
2161  N N   . MET A 287  ? 3.1475 2.9370 2.6137 0.9990  0.1471  -0.4895 287  MET A N   
2162  C CA  . MET A 287  ? 3.1434 2.9185 2.6216 1.0062  0.1415  -0.5268 287  MET A CA  
2163  C C   . MET A 287  ? 3.2173 2.9379 2.6398 0.9988  0.0956  -0.5328 287  MET A C   
2164  O O   . MET A 287  ? 3.1878 2.9103 2.5919 0.9798  0.0495  -0.5090 287  MET A O   
2165  C CB  . MET A 287  ? 3.0153 2.8523 2.5588 1.0026  0.1412  -0.5309 287  MET A CB  
2166  C CG  . MET A 287  ? 2.9470 2.8329 2.5548 1.0149  0.1949  -0.5436 287  MET A CG  
2167  S SD  . MET A 287  ? 3.3438 3.3118 3.0227 1.0043  0.1877  -0.5354 287  MET A SD  
2168  C CE  . MET A 287  ? 2.8112 2.7965 2.4662 0.9799  0.1473  -0.4791 287  MET A CE  
2169  N N   . GLN A 288  ? 5.8619 5.5340 5.2606 1.0144  0.1112  -0.5665 288  GLN A N   
2170  C CA  . GLN A 288  ? 5.9898 5.6097 5.3469 1.0130  0.0773  -0.5836 288  GLN A CA  
2171  C C   . GLN A 288  ? 5.9755 5.6197 5.3764 1.0177  0.0696  -0.6060 288  GLN A C   
2172  O O   . GLN A 288  ? 5.9136 5.6065 5.3741 1.0277  0.1014  -0.6208 288  GLN A O   
2173  C CB  . GLN A 288  ? 6.1140 5.6856 5.4803 0.9823  0.1161  -0.5992 288  GLN A CB  
2174  C CG  . GLN A 288  ? 6.1386 5.7330 5.5950 0.9588  0.1873  -0.6190 288  GLN A CG  
2175  C CD  . GLN A 288  ? 6.2184 5.7741 5.7142 0.9016  0.2316  -0.6300 288  GLN A CD  
2176  O OE1 . GLN A 288  ? 6.2704 5.7897 5.7546 0.8607  0.2167  -0.6244 288  GLN A OE1 
2177  N NE2 . GLN A 288  ? 6.2274 5.7960 5.7761 0.8962  0.2880  -0.6470 288  GLN A NE2 
2178  N N   . ASN A 289  ? 3.9744 3.5856 3.3451 1.0099  0.0269  -0.6073 289  ASN A N   
2179  C CA  . ASN A 289  ? 3.9893 3.6069 3.3873 1.0183  0.0172  -0.6322 289  ASN A CA  
2180  C C   . ASN A 289  ? 3.8284 3.5196 3.2966 1.0201  0.0281  -0.6331 289  ASN A C   
2181  O O   . ASN A 289  ? 3.7486 3.4790 3.2642 1.0329  0.0715  -0.6507 289  ASN A O   
2182  C CB  . ASN A 289  ? 4.1388 3.7140 3.5268 1.0409  0.0425  -0.6759 289  ASN A CB  
2183  C CG  . ASN A 289  ? 4.3081 3.8110 3.6263 1.0402  0.0348  -0.6781 289  ASN A CG  
2184  O OD1 . ASN A 289  ? 4.3708 3.8533 3.6457 1.0222  0.0062  -0.6482 289  ASN A OD1 
2185  N ND2 . ASN A 289  ? 4.3762 3.8425 3.6840 1.0596  0.0609  -0.7148 289  ASN A ND2 
2186  N N   . THR A 290  ? 2.9280 2.6367 2.4016 1.0065  -0.0116 -0.6145 290  THR A N   
2187  C CA  . THR A 290  ? 2.8319 2.5987 2.3632 1.0112  -0.0100 -0.6234 290  THR A CA  
2188  C C   . THR A 290  ? 2.8113 2.5511 2.3205 1.0068  -0.0551 -0.6212 290  THR A C   
2189  O O   . THR A 290  ? 2.7829 2.5649 2.3264 1.0051  -0.0698 -0.6172 290  THR A O   
2190  C CB  . THR A 290  ? 2.3586 2.1980 1.9356 0.9983  -0.0036 -0.5962 290  THR A CB  
2191  O OG1 . THR A 290  ? 2.3226 2.1983 1.9438 1.0118  0.0485  -0.6155 290  THR A OG1 
2192  C CG2 . THR A 290  ? 2.2951 2.1837 1.9093 0.9932  -0.0268 -0.5902 290  THR A CG2 
2193  N N   . MET A 291  ? 4.2304 3.8978 3.6808 1.0054  -0.0754 -0.6241 291  MET A N   
2194  C CA  . MET A 291  ? 4.2253 3.8517 3.6473 1.0029  -0.1153 -0.6248 291  MET A CA  
2195  C C   . MET A 291  ? 4.1146 3.7730 3.5471 0.9828  -0.1529 -0.5900 291  MET A C   
2196  O O   . MET A 291  ? 4.0504 3.7695 3.5330 0.9858  -0.1484 -0.5886 291  MET A O   
2197  C CB  . MET A 291  ? 4.2665 3.8901 3.7123 1.0278  -0.1011 -0.6641 291  MET A CB  
2198  C CG  . MET A 291  ? 4.3428 3.9218 3.7697 1.0471  -0.0696 -0.7002 291  MET A CG  
2199  S SD  . MET A 291  ? 4.6731 4.2422 4.1215 1.0752  -0.0611 -0.7447 291  MET A SD  
2200  C CE  . MET A 291  ? 4.5349 4.1996 4.0591 1.0788  -0.0529 -0.7431 291  MET A CE  
2201  N N   . LEU A 292  ? 3.6971 3.3160 3.0822 0.9616  -0.1893 -0.5623 292  LEU A N   
2202  C CA  . LEU A 292  ? 3.6027 3.2418 2.9917 0.9416  -0.2277 -0.5299 292  LEU A CA  
2203  C C   . LEU A 292  ? 3.5329 3.1803 2.9472 0.9569  -0.2344 -0.5478 292  LEU A C   
2204  O O   . LEU A 292  ? 3.5871 3.1877 2.9833 0.9737  -0.2322 -0.5757 292  LEU A O   
2205  C CB  . LEU A 292  ? 3.6548 3.2315 2.9833 0.9208  -0.2674 -0.5094 292  LEU A CB  
2206  C CG  . LEU A 292  ? 3.6088 3.2031 2.9370 0.8956  -0.3075 -0.4718 292  LEU A CG  
2207  C CD1 . LEU A 292  ? 3.6108 3.2180 2.9644 0.9032  -0.3232 -0.4753 292  LEU A CD1 
2208  C CD2 . LEU A 292  ? 3.4920 3.1547 2.8527 0.8818  -0.2987 -0.4442 292  LEU A CD2 
2209  N N   . ILE A 293  ? 3.1266 2.8353 2.5831 0.9521  -0.2420 -0.5320 293  ILE A N   
2210  C CA  . ILE A 293  ? 3.0532 2.7783 2.5367 0.9684  -0.2472 -0.5481 293  ILE A CA  
2211  C C   . ILE A 293  ? 3.0022 2.7513 2.4934 0.9528  -0.2843 -0.5161 293  ILE A C   
2212  O O   . ILE A 293  ? 2.9319 2.7476 2.4605 0.9433  -0.2825 -0.4969 293  ILE A O   
2213  C CB  . ILE A 293  ? 2.9748 2.7580 2.5142 0.9914  -0.2044 -0.5799 293  ILE A CB  
2214  C CG1 . ILE A 293  ? 2.9867 2.7266 2.5099 1.0104  -0.1731 -0.6165 293  ILE A CG1 
2215  C CG2 . ILE A 293  ? 2.9621 2.7803 2.5353 1.0055  -0.2133 -0.5902 293  ILE A CG2 
2216  C CD1 . ILE A 293  ? 2.9257 2.7166 2.4979 1.0269  -0.1235 -0.6449 293  ILE A CD1 
2217  N N   . ASN A 294  ? 2.6040 2.2956 2.0589 0.9508  -0.3167 -0.5114 294  ASN A N   
2218  C CA  . ASN A 294  ? 2.6122 2.3066 2.0614 0.9337  -0.3554 -0.4786 294  ASN A CA  
2219  C C   . ASN A 294  ? 2.5147 2.2248 1.9533 0.9023  -0.3738 -0.4394 294  ASN A C   
2220  O O   . ASN A 294  ? 2.4372 2.2080 1.9083 0.8916  -0.3801 -0.4162 294  ASN A O   
2221  C CB  . ASN A 294  ? 2.6459 2.4033 2.1433 0.9462  -0.3544 -0.4793 294  ASN A CB  
2222  C CG  . ASN A 294  ? 2.7436 2.4965 2.2306 0.9300  -0.3944 -0.4451 294  ASN A CG  
2223  O OD1 . ASN A 294  ? 2.7225 2.5237 2.2276 0.9107  -0.4046 -0.4151 294  ASN A OD1 
2224  N ND2 . ASN A 294  ? 2.8424 2.5338 2.2989 0.9369  -0.4168 -0.4485 294  ASN A ND2 
2225  N N   . GLY A 295  ? 3.4578 3.1141 2.8502 0.8875  -0.3831 -0.4326 295  GLY A N   
2226  C CA  . GLY A 295  ? 3.3865 3.0516 2.7638 0.8569  -0.4048 -0.3957 295  GLY A CA  
2227  C C   . GLY A 295  ? 3.2597 2.9929 2.6719 0.8522  -0.3794 -0.3860 295  GLY A C   
2228  O O   . GLY A 295  ? 3.1948 2.9504 2.6044 0.8281  -0.3949 -0.3540 295  GLY A O   
2229  N N   . ILE A 296  ? 2.5588 2.3253 2.0053 0.8752  -0.3399 -0.4139 296  ILE A N   
2230  C CA  . ILE A 296  ? 2.4298 2.2504 1.9064 0.8736  -0.3093 -0.4095 296  ILE A CA  
2231  C C   . ILE A 296  ? 2.4717 2.2990 1.9685 0.8994  -0.2627 -0.4468 296  ILE A C   
2232  O O   . ILE A 296  ? 2.5515 2.3351 2.0326 0.9183  -0.2538 -0.4777 296  ILE A O   
2233  C CB  . ILE A 296  ? 2.2242 2.1275 1.7525 0.8645  -0.3093 -0.3875 296  ILE A CB  
2234  C CG1 . ILE A 296  ? 2.2030 2.1048 1.7241 0.8491  -0.3508 -0.3621 296  ILE A CG1 
2235  C CG2 . ILE A 296  ? 2.0836 2.0257 1.6239 0.8498  -0.2961 -0.3652 296  ILE A CG2 
2236  C CD1 . ILE A 296  ? 2.1608 2.0600 1.6591 0.8174  -0.3821 -0.3211 296  ILE A CD1 
2237  N N   . ALA A 297  ? 2.5313 2.4111 2.0612 0.8986  -0.2332 -0.4418 297  ALA A N   
2238  C CA  . ALA A 297  ? 2.4962 2.4058 2.0633 0.9199  -0.1845 -0.4718 297  ALA A CA  
2239  C C   . ALA A 297  ? 2.4402 2.4021 2.0329 0.9073  -0.1684 -0.4472 297  ALA A C   
2240  O O   . ALA A 297  ? 2.4189 2.3978 2.0053 0.8851  -0.1965 -0.4118 297  ALA A O   
2241  C CB  . ALA A 297  ? 2.5417 2.3903 2.0741 0.9351  -0.1647 -0.4994 297  ALA A CB  
2242  N N   . GLN A 298  ? 2.5113 2.4985 2.1334 0.9207  -0.1235 -0.4646 298  GLN A N   
2243  C CA  . GLN A 298  ? 2.4409 2.4762 2.0888 0.9104  -0.1061 -0.4409 298  GLN A CA  
2244  C C   . GLN A 298  ? 2.4008 2.4484 2.0731 0.9268  -0.0544 -0.4615 298  GLN A C   
2245  O O   . GLN A 298  ? 2.4515 2.4778 2.1280 0.9469  -0.0282 -0.4976 298  GLN A O   
2246  C CB  . GLN A 298  ? 2.4120 2.5223 2.1135 0.9030  -0.1087 -0.4290 298  GLN A CB  
2247  C CG  . GLN A 298  ? 2.4573 2.5778 2.1444 0.8788  -0.1535 -0.3911 298  GLN A CG  
2248  C CD  . GLN A 298  ? 2.4563 2.6549 2.1999 0.8741  -0.1508 -0.3834 298  GLN A CD  
2249  O OE1 . GLN A 298  ? 2.4493 2.6976 2.2435 0.8869  -0.1128 -0.4038 298  GLN A OE1 
2250  N NE2 . GLN A 298  ? 2.4600 2.6705 2.1958 0.8553  -0.1900 -0.3548 298  GLN A NE2 
2251  N N   . VAL A 299  ? 1.7508 1.8347 1.4415 0.9180  -0.0395 -0.4374 299  VAL A N   
2252  C CA  . VAL A 299  ? 1.6725 1.7795 1.3967 0.9319  0.0127  -0.4515 299  VAL A CA  
2253  C C   . VAL A 299  ? 1.6277 1.7921 1.3864 0.9202  0.0241  -0.4208 299  VAL A C   
2254  O O   . VAL A 299  ? 1.5676 1.7592 1.3276 0.9011  -0.0088 -0.3902 299  VAL A O   
2255  C CB  . VAL A 299  ? 1.7278 1.7731 1.4090 0.9440  0.0327  -0.4639 299  VAL A CB  
2256  C CG1 . VAL A 299  ? 1.7892 1.8067 1.4749 0.9659  0.0562  -0.5101 299  VAL A CG1 
2257  C CG2 . VAL A 299  ? 1.7683 1.7578 1.3805 0.9296  -0.0089 -0.4389 299  VAL A CG2 
2258  N N   . THR A 300  ? 2.2836 2.4655 2.0714 0.9322  0.0721  -0.4299 300  THR A N   
2259  C CA  . THR A 300  ? 2.1977 2.4365 2.0277 0.9259  0.0932  -0.4071 300  THR A CA  
2260  C C   . THR A 300  ? 2.2703 2.4939 2.1013 0.9394  0.1388  -0.4101 300  THR A C   
2261  O O   . THR A 300  ? 2.2687 2.4798 2.1162 0.9577  0.1782  -0.4444 300  THR A O   
2262  C CB  . THR A 300  ? 2.6078 2.9146 2.5071 0.9287  0.1134  -0.4254 300  THR A CB  
2263  O OG1 . THR A 300  ? 2.6222 2.9192 2.5403 0.9481  0.1431  -0.4709 300  THR A OG1 
2264  C CG2 . THR A 300  ? 2.5796 2.9133 2.4809 0.9125  0.0678  -0.4106 300  THR A CG2 
2265  N N   . PHE A 301  ? 1.8816 2.1084 1.6968 0.9306  0.1347  -0.3736 301  PHE A N   
2266  C CA  . PHE A 301  ? 2.0291 2.2150 1.8126 0.9419  0.1598  -0.3697 301  PHE A CA  
2267  C C   . PHE A 301  ? 2.0980 2.3224 1.9218 0.9476  0.2024  -0.3538 301  PHE A C   
2268  O O   . PHE A 301  ? 2.1130 2.3512 1.9255 0.9378  0.1897  -0.3156 301  PHE A O   
2269  C CB  . PHE A 301  ? 2.0241 2.1606 1.7344 0.9293  0.1125  -0.3441 301  PHE A CB  
2270  C CG  . PHE A 301  ? 2.0006 2.1119 1.6749 0.9331  0.1239  -0.3214 301  PHE A CG  
2271  C CD1 . PHE A 301  ? 2.0573 2.1148 1.6949 0.9488  0.1447  -0.3402 301  PHE A CD1 
2272  C CD2 . PHE A 301  ? 1.9373 2.0781 1.6092 0.9200  0.1086  -0.2791 301  PHE A CD2 
2273  C CE1 . PHE A 301  ? 2.0837 2.1197 1.6845 0.9523  0.1525  -0.3169 301  PHE A CE1 
2274  C CE2 . PHE A 301  ? 1.9484 2.0692 1.5847 0.9238  0.1156  -0.2556 301  PHE A CE2 
2275  C CZ  . PHE A 301  ? 2.0335 2.1022 1.6335 0.9400  0.1374  -0.2740 301  PHE A CZ  
2276  N N   . ASP A 302  ? 2.4752 2.7174 2.3481 0.9639  0.2540  -0.3846 302  ASP A N   
2277  C CA  . ASP A 302  ? 2.4406 2.7161 2.3580 0.9719  0.3026  -0.3754 302  ASP A CA  
2278  C C   . ASP A 302  ? 2.4790 2.7202 2.3513 0.9755  0.3059  -0.3443 302  ASP A C   
2279  O O   . ASP A 302  ? 2.5235 2.7183 2.3678 0.9905  0.3305  -0.3579 302  ASP A O   
2280  C CB  . ASP A 302  ? 2.4860 2.7671 2.4506 0.9907  0.3603  -0.4186 302  ASP A CB  
2281  C CG  . ASP A 302  ? 2.5383 2.8355 2.5380 1.0016  0.4152  -0.4092 302  ASP A CG  
2282  O OD1 . ASP A 302  ? 2.5754 2.8651 2.6028 1.0134  0.4627  -0.4386 302  ASP A OD1 
2283  O OD2 . ASP A 302  ? 2.5467 2.8631 2.5447 0.9947  0.4083  -0.3694 302  ASP A OD2 
2284  N N   . SER A 303  ? 2.5413 2.8084 2.4075 0.9620  0.2815  -0.3022 303  SER A N   
2285  C CA  . SER A 303  ? 2.5551 2.7962 2.3749 0.9633  0.2756  -0.2676 303  SER A CA  
2286  C C   . SER A 303  ? 2.5992 2.8304 2.4346 0.9846  0.3348  -0.2700 303  SER A C   
2287  O O   . SER A 303  ? 2.6708 2.8602 2.4573 0.9934  0.3394  -0.2568 303  SER A O   
2288  C CB  . SER A 303  ? 2.4520 2.7369 2.2781 0.9454  0.2440  -0.2242 303  SER A CB  
2289  O OG  . SER A 303  ? 2.3864 2.6761 2.1953 0.9253  0.1904  -0.2211 303  SER A OG  
2290  N N   . GLU A 304  ? 3.2553 3.5259 3.1597 0.9925  0.3805  -0.2876 304  GLU A N   
2291  C CA  . GLU A 304  ? 3.2017 3.4691 3.1352 1.0121  0.4430  -0.2933 304  GLU A CA  
2292  C C   . GLU A 304  ? 3.2551 3.4584 3.1424 1.0284  0.4626  -0.3114 304  GLU A C   
2293  O O   . GLU A 304  ? 3.2858 3.4584 3.1291 1.0359  0.4661  -0.2856 304  GLU A O   
2294  C CB  . GLU A 304  ? 3.1296 3.4370 3.1392 1.0166  0.4842  -0.3293 304  GLU A CB  
2295  C CG  . GLU A 304  ? 3.1026 3.4514 3.1728 1.0234  0.5332  -0.3173 304  GLU A CG  
2296  C CD  . GLU A 304  ? 3.0724 3.4589 3.2064 1.0091  0.5549  -0.3458 304  GLU A CD  
2297  O OE1 . GLU A 304  ? 3.1025 3.4756 3.2316 0.9995  0.5414  -0.3784 304  GLU A OE1 
2298  O OE2 . GLU A 304  ? 3.0378 3.4635 3.2199 0.9990  0.5778  -0.3300 304  GLU A OE2 
2299  N N   . THR A 305  ? 2.1496 2.3373 2.0509 1.0345  0.4777  -0.3569 305  THR A N   
2300  C CA  . THR A 305  ? 2.2799 2.4070 2.1367 1.0472  0.4881  -0.3812 305  THR A CA  
2301  C C   . THR A 305  ? 2.3881 2.4758 2.1678 1.0423  0.4479  -0.3478 305  THR A C   
2302  O O   . THR A 305  ? 2.4064 2.4830 2.1662 1.0505  0.4658  -0.3201 305  THR A O   
2303  C CB  . THR A 305  ? 2.2580 2.3738 2.1146 1.0438  0.4675  -0.4229 305  THR A CB  
2304  O OG1 . THR A 305  ? 2.1686 2.3408 2.0959 1.0395  0.4811  -0.4436 305  THR A OG1 
2305  C CG2 . THR A 305  ? 2.3461 2.4106 2.1827 1.0611  0.4988  -0.4592 305  THR A CG2 
2306  N N   . ALA A 306  ? 2.2207 2.2917 1.9597 1.0281  0.3925  -0.3490 306  ALA A N   
2307  C CA  . ALA A 306  ? 2.3906 2.4116 2.0503 1.0242  0.3553  -0.3322 306  ALA A CA  
2308  C C   . ALA A 306  ? 2.4795 2.5085 2.1065 1.0179  0.3360  -0.2828 306  ALA A C   
2309  O O   . ALA A 306  ? 2.4899 2.5180 2.0798 1.0003  0.2831  -0.2609 306  ALA A O   
2310  C CB  . ALA A 306  ? 2.3555 2.3568 1.9843 1.0099  0.3025  -0.3469 306  ALA A CB  
2311  N N   . VAL A 307  ? 5.5785 5.6146 5.2199 1.0328  0.3803  -0.2661 307  VAL A N   
2312  C CA  . VAL A 307  ? 5.7687 5.8018 5.3703 1.0341  0.3714  -0.2225 307  VAL A CA  
2313  C C   . VAL A 307  ? 5.9604 5.9952 5.6647 0.9734  0.4198  -0.2281 307  VAL A C   
2314  O O   . VAL A 307  ? 5.9808 5.9907 5.6575 0.9626  0.4196  -0.2128 307  VAL A O   
2315  C CB  . VAL A 307  ? 4.9163 5.0024 4.5354 1.0168  0.3382  -0.1825 307  VAL A CB  
2316  C CG1 . VAL A 307  ? 4.9390 5.0281 4.5283 1.0234  0.3418  -0.1394 307  VAL A CG1 
2317  C CG2 . VAL A 307  ? 4.8879 4.9712 4.4742 0.9931  0.2731  -0.1799 307  VAL A CG2 
2318  N N   . LYS A 308  ? 3.1777 3.2373 2.8689 1.0654  0.4806  -0.2316 308  LYS A N   
2319  C CA  . LYS A 308  ? 3.4538 3.5143 3.1724 1.0860  0.5423  -0.2231 308  LYS A CA  
2320  C C   . LYS A 308  ? 3.7942 3.7956 3.4565 1.1030  0.5629  -0.2284 308  LYS A C   
2321  O O   . LYS A 308  ? 3.8549 3.8427 3.4693 1.1079  0.5532  -0.1934 308  LYS A O   
2322  C CB  . LYS A 308  ? 3.4126 3.5004 3.2116 1.0922  0.5929  -0.2562 308  LYS A CB  
2323  C CG  . LYS A 308  ? 3.2476 3.4003 3.1089 1.0778  0.5821  -0.2480 308  LYS A CG  
2324  C CD  . LYS A 308  ? 3.1879 3.3663 3.1263 1.0843  0.6343  -0.2851 308  LYS A CD  
2325  C CE  . LYS A 308  ? 3.2025 3.3520 3.1344 1.0815  0.6318  -0.3333 308  LYS A CE  
2326  N NZ  . LYS A 308  ? 3.2221 3.3739 3.2011 1.0610  0.6670  -0.3495 308  LYS A NZ  
2327  N N   . GLU A 309  ? 4.2813 4.2497 3.9485 1.1120  0.5906  -0.2721 309  GLU A N   
2328  C CA  . GLU A 309  ? 4.5378 4.4487 4.1494 1.1273  0.6090  -0.2798 309  GLU A CA  
2329  C C   . GLU A 309  ? 4.4459 4.3236 3.9769 1.1163  0.5491  -0.2705 309  GLU A C   
2330  O O   . GLU A 309  ? 4.6960 4.5291 4.1687 1.1266  0.5538  -0.2672 309  GLU A O   
2331  C CB  . GLU A 309  ? 4.8753 4.7599 4.5129 1.1386  0.6520  -0.3311 309  GLU A CB  
2332  C CG  . GLU A 309  ? 5.3033 5.1261 4.8826 1.1536  0.6705  -0.3443 309  GLU A CG  
2333  C CD  . GLU A 309  ? 5.5764 5.3863 5.1520 1.1737  0.7232  -0.3202 309  GLU A CD  
2334  O OE1 . GLU A 309  ? 5.6186 5.4650 5.2494 1.1786  0.7576  -0.3024 309  GLU A OE1 
2335  O OE2 . GLU A 309  ? 5.7563 5.5190 5.2738 1.1851  0.7314  -0.3193 309  GLU A OE2 
2336  N N   . LEU A 310  ? 4.3786 4.2779 3.9057 1.0951  0.4935  -0.2658 310  LEU A N   
2337  C CA  . LEU A 310  ? 4.2685 4.1339 3.7235 1.0824  0.4365  -0.2636 310  LEU A CA  
2338  C C   . LEU A 310  ? 4.0554 3.9292 3.4613 1.0745  0.3998  -0.2157 310  LEU A C   
2339  O O   . LEU A 310  ? 4.0488 3.8972 3.3943 1.0623  0.3517  -0.2116 310  LEU A O   
2340  C CB  . LEU A 310  ? 4.2548 4.1278 3.7231 1.0642  0.3952  -0.2888 310  LEU A CB  
2341  C CG  . LEU A 310  ? 4.2496 4.1240 3.7702 1.0706  0.4254  -0.3361 310  LEU A CG  
2342  C CD1 . LEU A 310  ? 4.2293 4.0875 3.7327 1.0571  0.3799  -0.3620 310  LEU A CD1 
2343  C CD2 . LEU A 310  ? 4.3518 4.1885 3.8697 1.0928  0.4800  -0.3633 310  LEU A CD2 
2344  N N   . SER A 311  ? 4.0475 3.9577 3.4814 1.0817  0.4240  -0.1807 311  SER A N   
2345  C CA  . SER A 311  ? 3.8919 3.8134 3.2836 1.0799  0.4008  -0.1336 311  SER A CA  
2346  C C   . SER A 311  ? 3.7793 3.7452 3.2228 1.0919  0.4405  -0.1016 311  SER A C   
2347  O O   . SER A 311  ? 3.7306 3.7123 3.2383 1.1010  0.4869  -0.1189 311  SER A O   
2348  C CB  . SER A 311  ? 3.7581 3.6978 3.1229 1.0537  0.3317  -0.1166 311  SER A CB  
2349  O OG  . SER A 311  ? 3.7675 3.6597 3.0646 1.0453  0.2941  -0.1335 311  SER A OG  
2350  N N   . TYR A 312  ? 3.5637 3.5501 2.9801 1.0919  0.4227  -0.0560 312  TYR A N   
2351  C CA  . TYR A 312  ? 3.5223 3.5517 2.9830 1.1039  0.4561  -0.0195 312  TYR A CA  
2352  C C   . TYR A 312  ? 2.8637 2.9506 2.4042 1.0928  0.4594  -0.0166 312  TYR A C   
2353  O O   . TYR A 312  ? 2.8132 2.9369 2.3948 1.1025  0.4879  0.0126  312  TYR A O   
2354  C CB  . TYR A 312  ? 3.5676 3.6096 2.9769 1.1051  0.4281  0.0295  312  TYR A CB  
2355  C CG  . TYR A 312  ? 3.7054 3.7173 3.0729 1.1307  0.4636  0.0474  312  TYR A CG  
2356  C CD1 . TYR A 312  ? 3.7869 3.7880 3.0805 1.1305  0.4293  0.0743  312  TYR A CD1 
2357  C CD2 . TYR A 312  ? 3.7591 3.7558 3.1618 1.1547  0.5315  0.0382  312  TYR A CD2 
2358  C CE1 . TYR A 312  ? 3.9027 3.8792 3.1565 1.1545  0.4611  0.0923  312  TYR A CE1 
2359  C CE2 . TYR A 312  ? 3.8730 3.8420 3.2370 1.1784  0.5648  0.0567  312  TYR A CE2 
2360  C CZ  . TYR A 312  ? 3.9386 3.8982 3.2274 1.1788  0.5291  0.0843  312  TYR A CZ  
2361  O OH  . TYR A 312  ? 4.0517 3.9857 3.3009 1.2033  0.5626  0.1036  312  TYR A OH  
2362  N N   . TYR A 313  ? 3.5243 3.6195 3.0858 1.0735  0.4309  -0.0455 313  TYR A N   
2363  C CA  . TYR A 313  ? 3.3602 3.5094 2.9949 1.0622  0.4328  -0.0473 313  TYR A CA  
2364  C C   . TYR A 313  ? 3.3873 3.5354 3.0826 1.0693  0.4789  -0.0915 313  TYR A C   
2365  O O   . TYR A 313  ? 3.4144 3.5365 3.1001 1.0634  0.4670  -0.1296 313  TYR A O   
2366  C CB  . TYR A 313  ? 3.1842 3.3551 2.8067 1.0340  0.3669  -0.0436 313  TYR A CB  
2367  C CG  . TYR A 313  ? 3.1258 3.2788 2.6734 1.0226  0.3128  -0.0189 313  TYR A CG  
2368  C CD1 . TYR A 313  ? 3.1557 3.2610 2.6464 1.0138  0.2789  -0.0432 313  TYR A CD1 
2369  C CD2 . TYR A 313  ? 3.0805 3.2655 2.6151 1.0207  0.2959  0.0277  313  TYR A CD2 
2370  C CE1 . TYR A 313  ? 3.1942 3.2827 2.6162 1.0021  0.2300  -0.0232 313  TYR A CE1 
2371  C CE2 . TYR A 313  ? 3.1140 3.2856 2.5800 1.0093  0.2462  0.0485  313  TYR A CE2 
2372  C CZ  . TYR A 313  ? 3.1650 3.2878 2.5745 0.9993  0.2133  0.0223  313  TYR A CZ  
2373  O OH  . TYR A 313  ? 3.2018 3.3110 2.5437 0.9867  0.1646  0.0401  313  TYR A OH  
2374  N N   . SER A 314  ? 3.3377 3.5148 3.0959 1.0820  0.5315  -0.0868 314  SER A N   
2375  C CA  . SER A 314  ? 3.3076 3.4944 3.1316 1.0864  0.5753  -0.1280 314  SER A CA  
2376  C C   . SER A 314  ? 3.1069 3.3583 3.0001 1.0739  0.5732  -0.1212 314  SER A C   
2377  O O   . SER A 314  ? 3.0053 3.2770 2.9551 1.0714  0.5962  -0.1557 314  SER A O   
2378  C CB  . SER A 314  ? 3.4599 3.6235 3.3049 1.1116  0.6458  -0.1357 314  SER A CB  
2379  O OG  . SER A 314  ? 3.5013 3.6806 3.3491 1.1234  0.6657  -0.0905 314  SER A OG  
2380  N N   . LEU A 315  ? 2.4440 2.7287 2.3305 1.0660  0.5445  -0.0767 315  LEU A N   
2381  C CA  . LEU A 315  ? 2.3183 2.6667 2.2656 1.0550  0.5416  -0.0610 315  LEU A CA  
2382  C C   . LEU A 315  ? 2.1520 2.5277 2.0854 1.0286  0.4758  -0.0533 315  LEU A C   
2383  O O   . LEU A 315  ? 2.1550 2.5153 2.0277 1.0194  0.4276  -0.0295 315  LEU A O   
2384  C CB  . LEU A 315  ? 2.3976 2.7693 2.3543 1.0663  0.5605  -0.0135 315  LEU A CB  
2385  C CG  . LEU A 315  ? 2.4640 2.8535 2.4882 1.0846  0.6303  -0.0155 315  LEU A CG  
2386  C CD1 . LEU A 315  ? 2.5151 2.9113 2.5287 1.1003  0.6466  0.0341  315  LEU A CD1 
2387  C CD2 . LEU A 315  ? 2.3286 2.7748 2.4301 1.0720  0.6391  -0.0309 315  LEU A CD2 
2388  N N   . GLU A 316  ? 1.7511 2.1682 1.7411 1.0163  0.4752  -0.0733 316  GLU A N   
2389  C CA  . GLU A 316  ? 1.6201 2.0726 1.6086 0.9917  0.4192  -0.0610 316  GLU A CA  
2390  C C   . GLU A 316  ? 1.5427 2.0126 1.5054 0.9887  0.3955  -0.0090 316  GLU A C   
2391  O O   . GLU A 316  ? 1.5457 1.9817 1.4412 0.9879  0.3641  0.0096  316  GLU A O   
2392  C CB  . GLU A 316  ? 1.5659 2.0762 1.6317 0.9834  0.4356  -0.0764 316  GLU A CB  
2393  C CG  . GLU A 316  ? 1.5806 2.1127 1.6462 0.9598  0.3850  -0.0887 316  GLU A CG  
2394  C CD  . GLU A 316  ? 1.6054 2.1775 1.6649 0.9400  0.3382  -0.0488 316  GLU A CD  
2395  O OE1 . GLU A 316  ? 1.6062 2.2168 1.6973 0.9427  0.3547  -0.0186 316  GLU A OE1 
2396  O OE2 . GLU A 316  ? 1.6130 2.1785 1.6383 0.9215  0.2856  -0.0483 316  GLU A OE2 
2397  N N   . ASP A 317  ? 1.9822 2.5069 1.9997 0.9874  0.4114  0.0131  317  ASP A N   
2398  C CA  . ASP A 317  ? 2.0017 2.5461 2.0105 0.9931  0.4100  0.0608  317  ASP A CA  
2399  C C   . ASP A 317  ? 2.1010 2.6005 2.0276 0.9958  0.3784  0.0802  317  ASP A C   
2400  O O   . ASP A 317  ? 2.0650 2.5729 1.9525 0.9777  0.3228  0.1018  317  ASP A O   
2401  C CB  . ASP A 317  ? 2.0394 2.5905 2.0970 1.0174  0.4788  0.0634  317  ASP A CB  
2402  C CG  . ASP A 317  ? 2.1854 2.7855 2.2748 1.0205  0.4861  0.1078  317  ASP A CG  
2403  O OD1 . ASP A 317  ? 2.1967 2.8130 2.2507 1.0097  0.4397  0.1436  317  ASP A OD1 
2404  O OD2 . ASP A 317  ? 2.1672 2.7897 2.3182 1.0339  0.5396  0.1060  317  ASP A OD2 
2405  N N   . LEU A 318  ? 3.4096 3.8616 3.3108 1.0176  0.4147  0.0703  318  LEU A N   
2406  C CA  . LEU A 318  ? 3.5189 3.9264 3.3423 1.0244  0.3943  0.0869  318  LEU A CA  
2407  C C   . LEU A 318  ? 3.5016 3.8841 3.2673 1.0029  0.3326  0.0747  318  LEU A C   
2408  O O   . LEU A 318  ? 3.5508 3.8848 3.2520 1.0070  0.3183  0.0701  318  LEU A O   
2409  C CB  . LEU A 318  ? 3.6405 3.9970 3.4489 1.0501  0.4460  0.0683  318  LEU A CB  
2410  C CG  . LEU A 318  ? 3.7623 4.1128 3.5623 1.0752  0.4853  0.1019  318  LEU A CG  
2411  C CD1 . LEU A 318  ? 3.8576 4.1642 3.6655 1.0985  0.5465  0.0746  318  LEU A CD1 
2412  C CD2 . LEU A 318  ? 3.8599 4.1963 3.5843 1.0750  0.4448  0.1372  318  LEU A CD2 
2413  N N   . ASN A 319  ? 1.5390 1.9540 1.3281 0.9798  0.2969  0.0693  319  ASN A N   
2414  C CA  . ASN A 319  ? 1.4570 1.8534 1.1935 0.9580  0.2360  0.0662  319  ASN A CA  
2415  C C   . ASN A 319  ? 1.4169 1.8617 1.1642 0.9331  0.1885  0.0921  319  ASN A C   
2416  O O   . ASN A 319  ? 1.4149 1.8992 1.2164 0.9232  0.1907  0.0847  319  ASN A O   
2417  C CB  . ASN A 319  ? 1.4598 1.8215 1.1935 0.9539  0.2339  0.0196  319  ASN A CB  
2418  C CG  . ASN A 319  ? 1.5760 1.8937 1.2384 0.9405  0.1836  0.0135  319  ASN A CG  
2419  O OD1 . ASN A 319  ? 1.6425 1.9458 1.2511 0.9391  0.1597  0.0394  319  ASN A OD1 
2420  N ND2 . ASN A 319  ? 1.6077 1.9050 1.2684 0.9304  0.1659  -0.0205 319  ASN A ND2 
2421  N N   . ASN A 320  ? 2.0099 2.4524 1.7049 0.9227  0.1458  0.1218  320  ASN A N   
2422  C CA  . ASN A 320  ? 1.9502 2.4337 1.6474 0.8966  0.0957  0.1458  320  ASN A CA  
2423  C C   . ASN A 320  ? 2.0255 2.4750 1.6490 0.8806  0.0425  0.1505  320  ASN A C   
2424  O O   . ASN A 320  ? 2.0137 2.4906 1.6223 0.8599  -0.0021 0.1765  320  ASN A O   
2425  C CB  . ASN A 320  ? 1.9192 2.4593 1.6487 0.9003  0.1048  0.1878  320  ASN A CB  
2426  C CG  . ASN A 320  ? 1.8876 2.4714 1.6973 0.9073  0.1463  0.1829  320  ASN A CG  
2427  O OD1 . ASN A 320  ? 1.8217 2.4587 1.6699 0.8926  0.1308  0.2008  320  ASN A OD1 
2428  N ND2 . ASN A 320  ? 1.9265 2.4885 1.7632 0.9286  0.2000  0.1563  320  ASN A ND2 
2429  N N   . LYS A 321  ? 2.7889 3.1782 2.3680 0.8909  0.0503  0.1235  321  LYS A N   
2430  C CA  . LYS A 321  ? 2.8754 3.2198 2.3834 0.8774  0.0055  0.1160  321  LYS A CA  
2431  C C   . LYS A 321  ? 2.8260 3.1397 2.3346 0.8652  -0.0106 0.0775  321  LYS A C   
2432  O O   . LYS A 321  ? 2.7482 3.0872 2.3116 0.8625  0.0030  0.0636  321  LYS A O   
2433  C CB  . LYS A 321  ? 3.0543 3.3517 2.5109 0.8986  0.0269  0.1120  321  LYS A CB  
2434  C CG  . LYS A 321  ? 3.1347 3.4069 2.6186 0.9249  0.0865  0.0841  321  LYS A CG  
2435  C CD  . LYS A 321  ? 3.3119 3.5388 2.7429 0.9463  0.1089  0.0835  321  LYS A CD  
2436  C CE  . LYS A 321  ? 3.3524 3.6096 2.7834 0.9621  0.1288  0.1255  321  LYS A CE  
2437  N NZ  . LYS A 321  ? 3.4731 3.6880 2.8513 0.9840  0.1516  0.1271  321  LYS A NZ  
2438  N N   . TYR A 322  ? 2.3745 2.6343 1.8221 0.8586  -0.0385 0.0599  322  TYR A N   
2439  C CA  . TYR A 322  ? 2.3563 2.5900 1.7970 0.8420  -0.0676 0.0314  322  TYR A CA  
2440  C C   . TYR A 322  ? 2.4117 2.6031 1.8600 0.8576  -0.0375 -0.0125 322  TYR A C   
2441  O O   . TYR A 322  ? 2.4670 2.6461 1.9270 0.8820  0.0104  -0.0244 322  TYR A O   
2442  C CB  . TYR A 322  ? 2.3950 2.5975 1.7689 0.8208  -0.1224 0.0376  322  TYR A CB  
2443  C CG  . TYR A 322  ? 2.3542 2.6045 1.7316 0.7981  -0.1603 0.0749  322  TYR A CG  
2444  C CD1 . TYR A 322  ? 2.3398 2.5823 1.6919 0.7695  -0.2129 0.0768  322  TYR A CD1 
2445  C CD2 . TYR A 322  ? 2.3683 2.6727 1.7778 0.8056  -0.1420 0.1081  322  TYR A CD2 
2446  C CE1 . TYR A 322  ? 2.3561 2.6452 1.7146 0.7476  -0.2467 0.1105  322  TYR A CE1 
2447  C CE2 . TYR A 322  ? 2.3698 2.7217 1.7860 0.7854  -0.1754 0.1420  322  TYR A CE2 
2448  C CZ  . TYR A 322  ? 2.3811 2.7265 1.7722 0.7558  -0.2279 0.1429  322  TYR A CZ  
2449  O OH  . TYR A 322  ? 2.3830 2.7782 1.7833 0.7349  -0.2602 0.1764  322  TYR A OH  
2450  N N   . LEU A 323  ? 1.8127 1.9834 1.2553 0.8428  -0.0665 -0.0353 323  LEU A N   
2451  C CA  . LEU A 323  ? 1.8797 2.0062 1.3206 0.8535  -0.0509 -0.0786 323  LEU A CA  
2452  C C   . LEU A 323  ? 1.9829 2.0602 1.3707 0.8364  -0.0986 -0.0934 323  LEU A C   
2453  O O   . LEU A 323  ? 1.9601 2.0516 1.3606 0.8171  -0.1314 -0.0911 323  LEU A O   
2454  C CB  . LEU A 323  ? 1.7987 1.9627 1.3099 0.8572  -0.0270 -0.0953 323  LEU A CB  
2455  C CG  . LEU A 323  ? 1.8215 1.9601 1.3537 0.8746  0.0063  -0.1391 323  LEU A CG  
2456  C CD1 . LEU A 323  ? 1.8347 1.9455 1.3502 0.8625  -0.0288 -0.1616 323  LEU A CD1 
2457  C CD2 . LEU A 323  ? 1.9091 2.0012 1.4090 0.8961  0.0387  -0.1552 323  LEU A CD2 
2458  N N   . TYR A 324  ? 2.2599 2.2793 1.5895 0.8440  -0.1004 -0.1087 324  TYR A N   
2459  C CA  . TYR A 324  ? 2.3833 2.3502 1.6565 0.8289  -0.1434 -0.1226 324  TYR A CA  
2460  C C   . TYR A 324  ? 2.4161 2.3415 1.6925 0.8382  -0.1338 -0.1643 324  TYR A C   
2461  O O   . TYR A 324  ? 2.4279 2.3355 1.7145 0.8617  -0.0915 -0.1890 324  TYR A O   
2462  C CB  . TYR A 324  ? 2.5406 2.4679 1.7450 0.8309  -0.1530 -0.1168 324  TYR A CB  
2463  C CG  . TYR A 324  ? 2.6921 2.5517 1.8391 0.8246  -0.1797 -0.1446 324  TYR A CG  
2464  C CD1 . TYR A 324  ? 2.7816 2.6212 1.8762 0.8015  -0.2279 -0.1327 324  TYR A CD1 
2465  C CD2 . TYR A 324  ? 2.7557 2.5714 1.9016 0.8418  -0.1555 -0.1839 324  TYR A CD2 
2466  C CE1 . TYR A 324  ? 2.8847 2.6601 1.9272 0.7956  -0.2506 -0.1595 324  TYR A CE1 
2467  C CE2 . TYR A 324  ? 2.8567 2.6094 1.9511 0.8372  -0.1785 -0.2099 324  TYR A CE2 
2468  C CZ  . TYR A 324  ? 2.9112 2.6427 1.9540 0.8142  -0.2255 -0.1977 324  TYR A CZ  
2469  O OH  . TYR A 324  ? 2.9903 2.6583 1.9840 0.8097  -0.2463 -0.2246 324  TYR A OH  
2470  N N   . ILE A 325  ? 2.1861 2.0956 1.4528 0.8198  -0.1734 -0.1715 325  ILE A N   
2471  C CA  . ILE A 325  ? 2.1789 2.0506 1.4482 0.8269  -0.1715 -0.2087 325  ILE A CA  
2472  C C   . ILE A 325  ? 2.2472 2.0542 1.4532 0.8154  -0.2095 -0.2223 325  ILE A C   
2473  O O   . ILE A 325  ? 2.2615 2.0631 1.4350 0.7922  -0.2512 -0.2016 325  ILE A O   
2474  C CB  . ILE A 325  ? 2.0665 1.9779 1.3921 0.8200  -0.1779 -0.2109 325  ILE A CB  
2475  C CG1 . ILE A 325  ? 1.9877 1.9648 1.3774 0.8289  -0.1422 -0.1988 325  ILE A CG1 
2476  C CG2 . ILE A 325  ? 2.0785 1.9602 1.4153 0.8343  -0.1645 -0.2501 325  ILE A CG2 
2477  C CD1 . ILE A 325  ? 1.9091 1.9195 1.3528 0.8288  -0.1381 -0.2117 325  ILE A CD1 
2478  N N   . ALA A 326  ? 2.4001 2.1591 1.5919 0.8316  -0.1936 -0.2587 326  ALA A N   
2479  C CA  . ALA A 326  ? 2.4849 2.1792 1.6220 0.8242  -0.2237 -0.2774 326  ALA A CA  
2480  C C   . ALA A 326  ? 2.5097 2.1727 1.6613 0.8427  -0.2041 -0.3173 326  ALA A C   
2481  O O   . ALA A 326  ? 2.5003 2.1614 1.6689 0.8664  -0.1609 -0.3385 326  ALA A O   
2482  C CB  . ALA A 326  ? 2.5533 2.2103 1.6302 0.8264  -0.2236 -0.2763 326  ALA A CB  
2483  N N   . VAL A 327  ? 2.2743 1.9148 1.4213 0.8317  -0.2359 -0.3264 327  VAL A N   
2484  C CA  . VAL A 327  ? 2.3266 1.9347 1.4828 0.8478  -0.2249 -0.3631 327  VAL A CA  
2485  C C   . VAL A 327  ? 2.4573 1.9907 1.5491 0.8434  -0.2492 -0.3807 327  VAL A C   
2486  O O   . VAL A 327  ? 2.5239 2.0368 1.5700 0.8239  -0.2800 -0.3629 327  VAL A O   
2487  C CB  . VAL A 327  ? 2.2162 1.8533 1.4171 0.8413  -0.2421 -0.3618 327  VAL A CB  
2488  C CG1 . VAL A 327  ? 2.2481 1.8612 1.4651 0.8622  -0.2250 -0.4000 327  VAL A CG1 
2489  C CG2 . VAL A 327  ? 2.0820 1.7957 1.3425 0.8391  -0.2269 -0.3397 327  VAL A CG2 
2490  N N   . THR A 328  ? 2.8938 2.3883 1.9835 0.8620  -0.2338 -0.4170 328  THR A N   
2491  C CA  . THR A 328  ? 3.0140 2.4395 2.0555 0.8583  -0.2595 -0.4373 328  THR A CA  
2492  C C   . THR A 328  ? 3.0214 2.4421 2.0980 0.8722  -0.2548 -0.4626 328  THR A C   
2493  O O   . THR A 328  ? 2.9521 2.3969 2.0695 0.8945  -0.2175 -0.4826 328  THR A O   
2494  C CB  . THR A 328  ? 3.1401 2.5132 2.1285 0.8696  -0.2429 -0.4581 328  THR A CB  
2495  O OG1 . THR A 328  ? 3.1714 2.5551 2.1276 0.8562  -0.2504 -0.4315 328  THR A OG1 
2496  C CG2 . THR A 328  ? 3.2364 2.5375 2.1772 0.8659  -0.2684 -0.4815 328  THR A CG2 
2497  N N   . VAL A 329  ? 2.9284 2.3221 1.9918 0.8583  -0.2930 -0.4598 329  VAL A N   
2498  C CA  . VAL A 329  ? 2.9761 2.3600 2.0655 0.8706  -0.2950 -0.4810 329  VAL A CA  
2499  C C   . VAL A 329  ? 3.1969 2.5025 2.2361 0.8698  -0.3174 -0.5018 329  VAL A C   
2500  O O   . VAL A 329  ? 3.2942 2.5722 2.3058 0.8481  -0.3565 -0.4864 329  VAL A O   
2501  C CB  . VAL A 329  ? 2.8387 2.2656 1.9645 0.8555  -0.3206 -0.4553 329  VAL A CB  
2502  C CG1 . VAL A 329  ? 2.7990 2.2353 1.9640 0.8742  -0.3122 -0.4767 329  VAL A CG1 
2503  C CG2 . VAL A 329  ? 2.7185 2.2175 1.8813 0.8475  -0.3083 -0.4269 329  VAL A CG2 
2504  N N   . ILE A 330  ? 3.6372 2.9066 2.6650 0.8929  -0.2912 -0.5373 330  ILE A N   
2505  C CA  . ILE A 330  ? 3.8165 3.0123 2.8026 0.8964  -0.3074 -0.5618 330  ILE A CA  
2506  C C   . ILE A 330  ? 3.9120 3.1095 2.9347 0.9116  -0.3090 -0.5781 330  ILE A C   
2507  O O   . ILE A 330  ? 3.8426 3.0774 2.9107 0.9335  -0.2778 -0.5945 330  ILE A O   
2508  C CB  . ILE A 330  ? 4.0365 3.1880 2.9849 0.9124  -0.2801 -0.5917 330  ILE A CB  
2509  C CG1 . ILE A 330  ? 4.0061 3.1852 2.9951 0.9416  -0.2326 -0.6174 330  ILE A CG1 
2510  C CG2 . ILE A 330  ? 4.0304 3.1859 2.9434 0.8988  -0.2786 -0.5732 330  ILE A CG2 
2511  C CD1 . ILE A 330  ? 4.0706 3.2211 3.0261 0.9541  -0.2016 -0.6373 330  ILE A CD1 
2512  N N   . GLU A 331  ? 4.4606 3.6201 3.4647 0.8996  -0.3456 -0.5724 331  GLU A N   
2513  C CA  . GLU A 331  ? 4.5864 3.7491 3.6229 0.9121  -0.3530 -0.5809 331  GLU A CA  
2514  C C   . GLU A 331  ? 4.7264 3.8548 3.7642 0.9420  -0.3292 -0.6227 331  GLU A C   
2515  O O   . GLU A 331  ? 4.8240 3.8945 3.8186 0.9463  -0.3248 -0.6441 331  GLU A O   
2516  C CB  . GLU A 331  ? 4.6455 3.7694 3.6572 0.8909  -0.3977 -0.5623 331  GLU A CB  
2517  C CG  . GLU A 331  ? 4.6864 3.7759 3.7059 0.9076  -0.4062 -0.5808 331  GLU A CG  
2518  C CD  . GLU A 331  ? 4.7979 3.8152 3.7714 0.8904  -0.4427 -0.5761 331  GLU A CD  
2519  O OE1 . GLU A 331  ? 4.8389 3.8362 3.7752 0.8637  -0.4624 -0.5589 331  GLU A OE1 
2520  O OE2 . GLU A 331  ? 4.8412 3.8221 3.8163 0.9038  -0.4512 -0.5899 331  GLU A OE2 
2521  N N   . SER A 332  ? 4.0958 3.2616 3.1834 0.9626  -0.3143 -0.6348 332  SER A N   
2522  C CA  . SER A 332  ? 4.2178 3.3629 3.3151 0.9929  -0.2880 -0.6754 332  SER A CA  
2523  C C   . SER A 332  ? 4.3894 3.4640 3.4561 0.9995  -0.3097 -0.6920 332  SER A C   
2524  O O   . SER A 332  ? 4.4474 3.4798 3.4967 1.0181  -0.2921 -0.7256 332  SER A O   
2525  C CB  . SER A 332  ? 4.1536 3.3661 3.3158 1.0128  -0.2657 -0.6845 332  SER A CB  
2526  O OG  . SER A 332  ? 4.2062 3.3961 3.3778 1.0409  -0.2484 -0.7223 332  SER A OG  
2527  N N   . THR A 333  ? 3.9979 3.0602 3.0602 0.9851  -0.3464 -0.6688 333  THR A N   
2528  C CA  . THR A 333  ? 4.1419 3.1375 3.1791 0.9918  -0.3672 -0.6820 333  THR A CA  
2529  C C   . THR A 333  ? 4.2689 3.1866 3.2423 0.9780  -0.3798 -0.6902 333  THR A C   
2530  O O   . THR A 333  ? 4.3494 3.2157 3.3011 0.9951  -0.3685 -0.7225 333  THR A O   
2531  C CB  . THR A 333  ? 4.1501 3.1543 3.2026 0.9813  -0.4012 -0.6536 333  THR A CB  
2532  O OG1 . THR A 333  ? 4.2499 3.1838 3.2538 0.9607  -0.4343 -0.6428 333  THR A OG1 
2533  C CG2 . THR A 333  ? 4.0525 3.1311 3.1376 0.9635  -0.4059 -0.6189 333  THR A CG2 
2534  N N   . GLY A 334  ? 4.5612 3.4731 3.5054 0.9471  -0.4023 -0.6624 334  GLY A N   
2535  C CA  . GLY A 334  ? 4.6538 3.4950 3.5370 0.9301  -0.4194 -0.6678 334  GLY A CA  
2536  C C   . GLY A 334  ? 4.6514 3.4768 3.5021 0.9337  -0.3946 -0.6883 334  GLY A C   
2537  O O   . GLY A 334  ? 4.7910 3.5506 3.5953 0.9329  -0.3987 -0.7093 334  GLY A O   
2538  N N   . GLY A 335  ? 4.4003 3.2851 3.2748 0.9378  -0.3680 -0.6821 335  GLY A N   
2539  C CA  . GLY A 335  ? 4.3204 3.1953 3.1648 0.9407  -0.3435 -0.6964 335  GLY A CA  
2540  C C   . GLY A 335  ? 4.2270 3.1097 3.0386 0.9110  -0.3620 -0.6674 335  GLY A C   
2541  O O   . GLY A 335  ? 4.2518 3.1227 3.0293 0.9092  -0.3482 -0.6741 335  GLY A O   
2542  N N   . PHE A 336  ? 3.8752 2.7794 2.6973 0.8878  -0.3937 -0.6345 336  PHE A N   
2543  C CA  . PHE A 336  ? 3.7203 2.6416 2.5186 0.8583  -0.4138 -0.6038 336  PHE A CA  
2544  C C   . PHE A 336  ? 3.5339 2.5202 2.3553 0.8627  -0.3859 -0.5902 336  PHE A C   
2545  O O   . PHE A 336  ? 3.4933 2.5069 2.3465 0.8876  -0.3494 -0.6067 336  PHE A O   
2546  C CB  . PHE A 336  ? 3.6141 2.5554 2.4308 0.8351  -0.4491 -0.5711 336  PHE A CB  
2547  C CG  . PHE A 336  ? 3.6349 2.5099 2.4174 0.8192  -0.4840 -0.5738 336  PHE A CG  
2548  C CD1 . PHE A 336  ? 3.5933 2.4578 2.4014 0.8239  -0.4986 -0.5712 336  PHE A CD1 
2549  C CD2 . PHE A 336  ? 3.7002 2.5252 2.4258 0.7990  -0.5022 -0.5779 336  PHE A CD2 
2550  C CE1 . PHE A 336  ? 3.6735 2.4755 2.4523 0.8094  -0.5289 -0.5722 336  PHE A CE1 
2551  C CE2 . PHE A 336  ? 3.7886 2.5519 2.4849 0.7831  -0.5329 -0.5814 336  PHE A CE2 
2552  C CZ  . PHE A 336  ? 3.7817 2.5316 2.5050 0.7883  -0.5457 -0.5780 336  PHE A CZ  
2553  N N   . SER A 337  ? 3.8621 2.8739 2.6692 0.8377  -0.4034 -0.5595 337  SER A N   
2554  C CA  . SER A 337  ? 3.6831 2.7613 2.5163 0.8388  -0.3818 -0.5390 337  SER A CA  
2555  C C   . SER A 337  ? 3.6259 2.7391 2.4598 0.8085  -0.4128 -0.4992 337  SER A C   
2556  O O   . SER A 337  ? 3.6897 2.7677 2.4821 0.7846  -0.4462 -0.4908 337  SER A O   
2557  C CB  . SER A 337  ? 3.6760 2.7408 2.4740 0.8481  -0.3559 -0.5521 337  SER A CB  
2558  O OG  . SER A 337  ? 3.5267 2.6545 2.3518 0.8507  -0.3332 -0.5309 337  SER A OG  
2559  N N   . GLU A 338  ? 3.4934 2.6767 2.3758 0.8091  -0.4011 -0.4759 338  GLU A N   
2560  C CA  . GLU A 338  ? 3.4364 2.6617 2.3247 0.7820  -0.4263 -0.4371 338  GLU A CA  
2561  C C   . GLU A 338  ? 3.3041 2.5957 2.2225 0.7886  -0.3981 -0.4192 338  GLU A C   
2562  O O   . GLU A 338  ? 3.2272 2.5496 2.1866 0.8116  -0.3630 -0.4307 338  GLU A O   
2563  C CB  . GLU A 338  ? 3.4377 2.6825 2.3610 0.7705  -0.4506 -0.4205 338  GLU A CB  
2564  C CG  . GLU A 338  ? 3.4883 2.7438 2.3970 0.7363  -0.4894 -0.3872 338  GLU A CG  
2565  C CD  . GLU A 338  ? 3.6590 2.8483 2.5052 0.7180  -0.5169 -0.3954 338  GLU A CD  
2566  O OE1 . GLU A 338  ? 3.7576 2.8851 2.5791 0.7291  -0.5161 -0.4251 338  GLU A OE1 
2567  O OE2 . GLU A 338  ? 3.6945 2.8946 2.5169 0.6926  -0.5391 -0.3734 338  GLU A OE2 
2568  N N   . GLU A 339  ? 3.8057 3.1198 2.7047 0.7685  -0.4129 -0.3916 339  GLU A N   
2569  C CA  . GLU A 339  ? 3.7308 3.1048 2.6554 0.7750  -0.3865 -0.3727 339  GLU A CA  
2570  C C   . GLU A 339  ? 3.5602 2.9915 2.5128 0.7523  -0.4086 -0.3340 339  GLU A C   
2571  O O   . GLU A 339  ? 3.5373 2.9553 2.4721 0.7268  -0.4478 -0.3195 339  GLU A O   
2572  C CB  . GLU A 339  ? 3.8961 3.2503 2.7717 0.7772  -0.3769 -0.3749 339  GLU A CB  
2573  C CG  . GLU A 339  ? 4.0803 3.3859 2.9330 0.8023  -0.3475 -0.4125 339  GLU A CG  
2574  C CD  . GLU A 339  ? 4.2984 3.5685 3.0882 0.7991  -0.3500 -0.4173 339  GLU A CD  
2575  O OE1 . GLU A 339  ? 4.3440 3.6370 3.1129 0.7803  -0.3692 -0.3897 339  GLU A OE1 
2576  O OE2 . GLU A 339  ? 4.4133 3.6343 3.1745 0.8155  -0.3328 -0.4490 339  GLU A OE2 
2577  N N   . ALA A 340  ? 2.7301 2.2247 1.7279 0.7613  -0.3823 -0.3177 340  ALA A N   
2578  C CA  . ALA A 340  ? 2.6376 2.1927 1.6675 0.7418  -0.3990 -0.2811 340  ALA A CA  
2579  C C   . ALA A 340  ? 2.5302 2.1460 1.5945 0.7537  -0.3650 -0.2646 340  ALA A C   
2580  O O   . ALA A 340  ? 2.4959 2.1240 1.5899 0.7788  -0.3245 -0.2821 340  ALA A O   
2581  C CB  . ALA A 340  ? 2.6162 2.1891 1.6880 0.7371  -0.4118 -0.2791 340  ALA A CB  
2582  N N   . GLU A 341  ? 2.9602 2.6141 2.0216 0.7358  -0.3806 -0.2310 341  GLU A N   
2583  C CA  . GLU A 341  ? 2.9203 2.6250 2.0064 0.7475  -0.3490 -0.2139 341  GLU A CA  
2584  C C   . GLU A 341  ? 2.5084 2.2812 1.6368 0.7317  -0.3599 -0.1786 341  GLU A C   
2585  O O   . GLU A 341  ? 2.4962 2.2744 1.6215 0.7067  -0.3982 -0.1625 341  GLU A O   
2586  C CB  . GLU A 341  ? 3.0140 2.6986 2.0465 0.7467  -0.3506 -0.2070 341  GLU A CB  
2587  C CG  . GLU A 341  ? 3.0776 2.7660 2.0752 0.7159  -0.3966 -0.1806 341  GLU A CG  
2588  C CD  . GLU A 341  ? 3.1527 2.8318 2.1002 0.7168  -0.3962 -0.1723 341  GLU A CD  
2589  O OE1 . GLU A 341  ? 3.1693 2.8345 2.1067 0.7415  -0.3603 -0.1865 341  GLU A OE1 
2590  O OE2 . GLU A 341  ? 3.1989 2.8860 2.1171 0.6929  -0.4314 -0.1516 341  GLU A OE2 
2591  N N   . ILE A 342  ? 2.2581 2.0819 1.4267 0.7463  -0.3248 -0.1668 342  ILE A N   
2592  C CA  . ILE A 342  ? 2.1487 2.0396 1.3538 0.7330  -0.3312 -0.1308 342  ILE A CA  
2593  C C   . ILE A 342  ? 2.1698 2.0856 1.3645 0.7398  -0.3139 -0.1094 342  ILE A C   
2594  O O   . ILE A 342  ? 2.1769 2.0953 1.3840 0.7646  -0.2714 -0.1194 342  ILE A O   
2595  C CB  . ILE A 342  ? 1.9884 1.9303 1.2633 0.7425  -0.3057 -0.1318 342  ILE A CB  
2596  C CG1 . ILE A 342  ? 2.0007 1.9209 1.2876 0.7395  -0.3199 -0.1536 342  ILE A CG1 
2597  C CG2 . ILE A 342  ? 1.9708 1.9807 1.2809 0.7262  -0.3161 -0.0939 342  ILE A CG2 
2598  C CD1 . ILE A 342  ? 1.9180 1.8954 1.2717 0.7426  -0.3049 -0.1506 342  ILE A CD1 
2599  N N   . PRO A 343  ? 2.5446 2.4820 1.7192 0.7177  -0.3463 -0.0786 343  PRO A N   
2600  C CA  . PRO A 343  ? 2.5616 2.5184 1.7151 0.7225  -0.3378 -0.0563 343  PRO A CA  
2601  C C   . PRO A 343  ? 2.4710 2.4645 1.6704 0.7487  -0.2869 -0.0531 343  PRO A C   
2602  O O   . PRO A 343  ? 2.5479 2.5188 1.7326 0.7720  -0.2528 -0.0664 343  PRO A O   
2603  C CB  . PRO A 343  ? 2.5236 2.5302 1.6878 0.6957  -0.3726 -0.0196 343  PRO A CB  
2604  C CG  . PRO A 343  ? 2.5342 2.5214 1.6955 0.6719  -0.4103 -0.0269 343  PRO A CG  
2605  C CD  . PRO A 343  ? 2.5150 2.4735 1.6989 0.6881  -0.3886 -0.0595 343  PRO A CD  
2606  N N   . GLY A 344  ? 2.7152 2.7663 1.9726 0.7437  -0.2816 -0.0355 344  GLY A N   
2607  C CA  . GLY A 344  ? 2.6235 2.7174 1.9344 0.7648  -0.2346 -0.0305 344  GLY A CA  
2608  C C   . GLY A 344  ? 2.4811 2.6287 1.8570 0.7571  -0.2323 -0.0228 344  GLY A C   
2609  O O   . GLY A 344  ? 2.4803 2.6370 1.8606 0.7344  -0.2687 -0.0164 344  GLY A O   
2610  N N   . ILE A 345  ? 1.6493 1.8328 1.0763 0.7766  -0.1870 -0.0234 345  ILE A N   
2611  C CA  . ILE A 345  ? 1.5627 1.8000 1.0564 0.7743  -0.1742 -0.0203 345  ILE A CA  
2612  C C   . ILE A 345  ? 1.5281 1.8118 1.0587 0.7890  -0.1359 0.0007  345  ILE A C   
2613  O O   . ILE A 345  ? 1.5438 1.8186 1.0906 0.8132  -0.0899 -0.0158 345  ILE A O   
2614  C CB  . ILE A 345  ? 1.8262 2.0443 1.3459 0.7887  -0.1488 -0.0601 345  ILE A CB  
2615  C CG1 . ILE A 345  ? 1.7146 1.8986 1.2096 0.7728  -0.1886 -0.0757 345  ILE A CG1 
2616  C CG2 . ILE A 345  ? 1.7435 2.0201 1.3362 0.7950  -0.1181 -0.0615 345  ILE A CG2 
2617  C CD1 . ILE A 345  ? 1.6929 1.8764 1.2242 0.7841  -0.1689 -0.1084 345  ILE A CD1 
2618  N N   . LYS A 346  ? 2.1788 2.5103 1.7215 0.7746  -0.1542 0.0373  346  LYS A N   
2619  C CA  . LYS A 346  ? 2.0114 2.3859 1.5848 0.7885  -0.1211 0.0619  346  LYS A CA  
2620  C C   . LYS A 346  ? 1.9418 2.3508 1.5853 0.8043  -0.0734 0.0474  346  LYS A C   
2621  O O   . LYS A 346  ? 1.9529 2.3993 1.6388 0.7921  -0.0814 0.0462  346  LYS A O   
2622  C CB  . LYS A 346  ? 1.9752 2.4002 1.5549 0.7676  -0.1537 0.1026  346  LYS A CB  
2623  C CG  . LYS A 346  ? 2.0100 2.4681 1.5980 0.7808  -0.1315 0.1342  346  LYS A CG  
2624  C CD  . LYS A 346  ? 1.9853 2.5100 1.6053 0.7636  -0.1521 0.1718  346  LYS A CD  
2625  C CE  . LYS A 346  ? 2.0503 2.5748 1.6211 0.7390  -0.2069 0.1959  346  LYS A CE  
2626  N NZ  . LYS A 346  ? 2.0139 2.6062 1.6161 0.7268  -0.2204 0.2350  346  LYS A NZ  
2627  N N   . TYR A 347  ? 1.6302 2.0271 1.2865 0.8305  -0.0234 0.0351  347  TYR A N   
2628  C CA  . TYR A 347  ? 1.5763 2.0122 1.3031 0.8450  0.0254  0.0247  347  TYR A CA  
2629  C C   . TYR A 347  ? 1.5462 2.0461 1.3134 0.8384  0.0267  0.0609  347  TYR A C   
2630  O O   . TYR A 347  ? 1.5176 2.0249 1.2547 0.8316  0.0031  0.0937  347  TYR A O   
2631  C CB  . TYR A 347  ? 1.6336 2.0462 1.3636 0.8732  0.0787  0.0132  347  TYR A CB  
2632  C CG  . TYR A 347  ? 1.6438 2.0114 1.3682 0.8854  0.1001  -0.0308 347  TYR A CG  
2633  C CD1 . TYR A 347  ? 1.6346 2.0094 1.4075 0.9053  0.1558  -0.0549 347  TYR A CD1 
2634  C CD2 . TYR A 347  ? 1.7268 2.0448 1.3988 0.8768  0.0649  -0.0493 347  TYR A CD2 
2635  C CE1 . TYR A 347  ? 1.6974 2.0330 1.4662 0.9164  0.1752  -0.0964 347  TYR A CE1 
2636  C CE2 . TYR A 347  ? 1.7861 2.0636 1.4530 0.8886  0.0836  -0.0896 347  TYR A CE2 
2637  C CZ  . TYR A 347  ? 1.7831 2.0707 1.4986 0.9084  0.1383  -0.1133 347  TYR A CZ  
2638  O OH  . TYR A 347  ? 1.8448 2.0940 1.5559 0.9198  0.1559  -0.1548 347  TYR A OH  
2639  N N   . VAL A 348  ? 1.2801 1.8280 1.1155 0.8410  0.0552  0.0552  348  VAL A N   
2640  C CA  . VAL A 348  ? 1.2493 1.8573 1.1277 0.8400  0.0674  0.0890  348  VAL A CA  
2641  C C   . VAL A 348  ? 1.2049 1.8397 1.1483 0.8599  0.1280  0.0754  348  VAL A C   
2642  O O   . VAL A 348  ? 1.1825 1.8061 1.1518 0.8685  0.1559  0.0384  348  VAL A O   
2643  C CB  . VAL A 348  ? 1.2210 1.8802 1.1204 0.8134  0.0272  0.1104  348  VAL A CB  
2644  C CG1 . VAL A 348  ? 1.1895 1.9094 1.1358 0.8156  0.0454  0.1427  348  VAL A CG1 
2645  C CG2 . VAL A 348  ? 1.2666 1.9040 1.1050 0.7918  -0.0319 0.1285  348  VAL A CG2 
2646  N N   . LEU A 349  ? 1.3140 1.9851 1.2844 0.8677  0.1491  0.1057  349  LEU A N   
2647  C CA  . LEU A 349  ? 1.2884 1.9894 1.3243 0.8843  0.2058  0.0967  349  LEU A CA  
2648  C C   . LEU A 349  ? 1.1660 1.9265 1.2595 0.8678  0.1988  0.0941  349  LEU A C   
2649  O O   . LEU A 349  ? 1.1167 1.8839 1.2454 0.8681  0.2174  0.0593  349  LEU A O   
2650  C CB  . LEU A 349  ? 1.3609 2.0775 1.4007 0.8987  0.2274  0.1340  349  LEU A CB  
2651  C CG  . LEU A 349  ? 1.3717 2.1064 1.4713 0.9211  0.2933  0.1285  349  LEU A CG  
2652  C CD1 . LEU A 349  ? 1.3227 2.1189 1.4658 0.9189  0.2982  0.1665  349  LEU A CD1 
2653  C CD2 . LEU A 349  ? 1.3565 2.0942 1.5025 0.9217  0.3222  0.0820  349  LEU A CD2 
2654  N N   . SER A 350  ? 2.0397 1.6529 1.6312 0.8260  0.3082  0.1469  350  SER A N   
2655  C CA  . SER A 350  ? 1.9999 1.5833 1.6136 0.7908  0.3091  0.1504  350  SER A CA  
2656  C C   . SER A 350  ? 2.0243 1.5815 1.5899 0.7620  0.2615  0.1376  350  SER A C   
2657  O O   . SER A 350  ? 2.0757 1.6693 1.6247 0.7620  0.2458  0.1521  350  SER A O   
2658  C CB  . SER A 350  ? 1.9932 1.6275 1.6673 0.7886  0.3490  0.1920  350  SER A CB  
2659  O OG  . SER A 350  ? 1.9862 1.5984 1.6791 0.7551  0.3486  0.1975  350  SER A OG  
2660  N N   . PRO A 351  ? 1.7819 1.2757 1.3254 0.7357  0.2385  0.1114  351  PRO A N   
2661  C CA  . PRO A 351  ? 1.8209 1.2737 1.3054 0.7097  0.1875  0.0894  351  PRO A CA  
2662  C C   . PRO A 351  ? 1.8662 1.3458 1.3587 0.6811  0.1784  0.1131  351  PRO A C   
2663  O O   . PRO A 351  ? 1.9312 1.3791 1.3779 0.6549  0.1372  0.0982  351  PRO A O   
2664  C CB  . PRO A 351  ? 1.7859 1.1655 1.2585 0.6902  0.1768  0.0599  351  PRO A CB  
2665  C CG  . PRO A 351  ? 1.7349 1.1184 1.2495 0.7150  0.2168  0.0601  351  PRO A CG  
2666  C CD  . PRO A 351  ? 1.7248 1.1785 1.2967 0.7297  0.2603  0.1002  351  PRO A CD  
2667  N N   . TYR A 352  ? 2.0233 1.5618 1.5733 0.6868  0.2165  0.1502  352  TYR A N   
2668  C CA  . TYR A 352  ? 2.0542 1.6305 1.6207 0.6643  0.2133  0.1769  352  TYR A CA  
2669  C C   . TYR A 352  ? 2.0618 1.7118 1.6432 0.6895  0.2259  0.2066  352  TYR A C   
2670  O O   . TYR A 352  ? 2.0178 1.6943 1.6174 0.7228  0.2526  0.2145  352  TYR A O   
2671  C CB  . TYR A 352  ? 2.0564 1.6392 1.6832 0.6469  0.2498  0.1980  352  TYR A CB  
2672  C CG  . TYR A 352  ? 2.0639 1.5792 1.6878 0.6202  0.2462  0.1754  352  TYR A CG  
2673  C CD1 . TYR A 352  ? 2.0997 1.5927 1.7140 0.5808  0.2261  0.1736  352  TYR A CD1 
2674  C CD2 . TYR A 352  ? 2.0523 1.5297 1.6865 0.6336  0.2651  0.1582  352  TYR A CD2 
2675  C CE1 . TYR A 352  ? 2.0987 1.5305 1.7090 0.5560  0.2231  0.1543  352  TYR A CE1 
2676  C CE2 . TYR A 352  ? 2.0669 1.4832 1.6983 0.6092  0.2615  0.1388  352  TYR A CE2 
2677  C CZ  . TYR A 352  ? 2.0885 1.4810 1.7067 0.5704  0.2404  0.1368  352  TYR A CZ  
2678  O OH  . TYR A 352  ? 2.0916 1.4214 1.7040 0.5451  0.2360  0.1175  352  TYR A OH  
2679  N N   . LYS A 353  ? 1.7569 1.4419 1.3338 0.6730  0.2085  0.2247  353  LYS A N   
2680  C CA  . LYS A 353  ? 1.8018 1.5550 1.3892 0.6955  0.2166  0.2524  353  LYS A CA  
2681  C C   . LYS A 353  ? 1.7438 1.5461 1.3655 0.6758  0.2221  0.2847  353  LYS A C   
2682  O O   . LYS A 353  ? 1.7161 1.5128 1.3090 0.6478  0.1868  0.2802  353  LYS A O   
2683  C CB  . LYS A 353  ? 1.9241 1.6694 1.4441 0.7040  0.1733  0.2332  353  LYS A CB  
2684  C CG  . LYS A 353  ? 2.0395 1.7361 1.5041 0.6694  0.1228  0.2079  353  LYS A CG  
2685  C CD  . LYS A 353  ? 2.1412 1.7925 1.5347 0.6827  0.0861  0.1723  353  LYS A CD  
2686  C CE  . LYS A 353  ? 2.2304 1.9175 1.5841 0.6976  0.0609  0.1786  353  LYS A CE  
2687  N NZ  . LYS A 353  ? 2.2746 1.9165 1.5593 0.7154  0.0288  0.1431  353  LYS A NZ  
2688  N N   . LEU A 354  ? 1.8114 1.6631 1.4940 0.6910  0.2660  0.3177  354  LEU A N   
2689  C CA  . LEU A 354  ? 1.8288 1.7289 1.5502 0.6743  0.2752  0.3492  354  LEU A CA  
2690  C C   . LEU A 354  ? 1.8554 1.8075 1.5562 0.6800  0.2512  0.3650  354  LEU A C   
2691  O O   . LEU A 354  ? 1.8788 1.8457 1.5555 0.7075  0.2463  0.3633  354  LEU A O   
2692  C CB  . LEU A 354  ? 1.8242 1.7635 1.6140 0.6938  0.3291  0.3810  354  LEU A CB  
2693  C CG  . LEU A 354  ? 1.7682 1.6725 1.5888 0.7042  0.3669  0.3745  354  LEU A CG  
2694  C CD1 . LEU A 354  ? 1.7695 1.6497 1.6243 0.6754  0.3826  0.3771  354  LEU A CD1 
2695  C CD2 . LEU A 354  ? 1.7441 1.5938 1.5207 0.7147  0.3512  0.3381  354  LEU A CD2 
2696  N N   . ASN A 355  ? 1.7392 1.7218 1.4510 0.6544  0.2374  0.3815  355  ASN A N   
2697  C CA  . ASN A 355  ? 1.6768 1.7208 1.3833 0.6613  0.2223  0.4044  355  ASN A CA  
2698  C C   . ASN A 355  ? 1.6792 1.7692 1.4259 0.6380  0.2265  0.4317  355  ASN A C   
2699  O O   . ASN A 355  ? 1.7695 1.8376 1.5014 0.6014  0.2010  0.4206  355  ASN A O   
2700  C CB  . ASN A 355  ? 1.7689 1.7905 1.4021 0.6545  0.1703  0.3802  355  ASN A CB  
2701  C CG  . ASN A 355  ? 1.8575 1.8297 1.4523 0.6124  0.1306  0.3554  355  ASN A CG  
2702  O OD1 . ASN A 355  ? 1.8677 1.7733 1.4374 0.6026  0.1225  0.3249  355  ASN A OD1 
2703  N ND2 . ASN A 355  ? 1.9282 1.9324 1.5159 0.5869  0.1038  0.3680  355  ASN A ND2 
2704  N N   . LEU A 356  ? 1.3146 1.4689 1.1124 0.6595  0.2592  0.4678  356  LEU A N   
2705  C CA  . LEU A 356  ? 1.2986 1.5052 1.1399 0.6421  0.2664  0.4966  356  LEU A CA  
2706  C C   . LEU A 356  ? 1.3376 1.5449 1.1406 0.6059  0.2173  0.4868  356  LEU A C   
2707  O O   . LEU A 356  ? 1.4043 1.5889 1.1480 0.6038  0.1789  0.4662  356  LEU A O   
2708  C CB  . LEU A 356  ? 1.3186 1.5994 1.1947 0.6731  0.2883  0.5335  356  LEU A CB  
2709  C CG  . LEU A 356  ? 1.2662 1.5619 1.1906 0.7075  0.3407  0.5535  356  LEU A CG  
2710  C CD1 . LEU A 356  ? 1.2918 1.6620 1.2430 0.7332  0.3533  0.5902  356  LEU A CD1 
2711  C CD2 . LEU A 356  ? 1.2480 1.5313 1.2209 0.6921  0.3711  0.5599  356  LEU A CD2 
2712  N N   . VAL A 357  ? 1.3737 1.6070 1.2084 0.5773  0.2177  0.5014  357  VAL A N   
2713  C CA  . VAL A 357  ? 1.4484 1.6854 1.2470 0.5406  0.1706  0.4936  357  VAL A CA  
2714  C C   . VAL A 357  ? 1.3475 1.6587 1.1875 0.5256  0.1711  0.5260  357  VAL A C   
2715  O O   . VAL A 357  ? 1.4666 1.8003 1.3619 0.5200  0.2028  0.5436  357  VAL A O   
2716  C CB  . VAL A 357  ? 1.3877 1.5556 1.1574 0.5031  0.1509  0.4629  357  VAL A CB  
2717  C CG1 . VAL A 357  ? 1.4604 1.6262 1.1813 0.4671  0.0978  0.4524  357  VAL A CG1 
2718  C CG2 . VAL A 357  ? 1.3758 1.4704 1.1081 0.5173  0.1508  0.4305  357  VAL A CG2 
2719  N N   . ALA A 358  ? 1.8669 2.2153 1.6789 0.5184  0.1349  0.5330  358  ALA A N   
2720  C CA  . ALA A 358  ? 1.9414 2.3691 1.7939 0.5085  0.1344  0.5659  358  ALA A CA  
2721  C C   . ALA A 358  ? 1.9037 2.3820 1.8345 0.5328  0.1882  0.5988  358  ALA A C   
2722  O O   . ALA A 358  ? 1.8336 2.3448 1.8088 0.5131  0.2008  0.6150  358  ALA A O   
2723  C CB  . ALA A 358  ? 2.0222 2.4420 1.8619 0.4582  0.1033  0.5568  358  ALA A CB  
2724  N N   . THR A 359  ? 1.6673 2.1509 1.6128 0.5755  0.2193  0.6083  359  THR A N   
2725  C CA  . THR A 359  ? 1.6313 2.1550 1.6450 0.6037  0.2714  0.6387  359  THR A CA  
2726  C C   . THR A 359  ? 1.6012 2.1794 1.6301 0.6462  0.2870  0.6663  359  THR A C   
2727  O O   . THR A 359  ? 1.5393 2.0928 1.5596 0.6770  0.3072  0.6617  359  THR A O   
2728  C CB  . THR A 359  ? 1.3979 1.8611 1.4262 0.6128  0.3081  0.6235  359  THR A CB  
2729  O OG1 . THR A 359  ? 1.4221 1.8240 1.3974 0.6225  0.2942  0.5932  359  THR A OG1 
2730  C CG2 . THR A 359  ? 1.3730 1.8030 1.4123 0.5749  0.3081  0.6102  359  THR A CG2 
2731  N N   . PRO A 360  ? 1.7248 2.3780 1.7772 0.6474  0.2781  0.6957  360  PRO A N   
2732  C CA  . PRO A 360  ? 1.7301 2.4416 1.7978 0.6845  0.2891  0.7251  360  PRO A CA  
2733  C C   . PRO A 360  ? 1.6789 2.3877 1.7850 0.7235  0.3412  0.7406  360  PRO A C   
2734  O O   . PRO A 360  ? 1.5328 2.2237 1.6778 0.7187  0.3733  0.7419  360  PRO A O   
2735  C CB  . PRO A 360  ? 1.7423 2.5312 1.8538 0.6726  0.2851  0.7558  360  PRO A CB  
2736  C CG  . PRO A 360  ? 1.7735 2.5452 1.8604 0.6250  0.2473  0.7357  360  PRO A CG  
2737  C CD  . PRO A 360  ? 1.7411 2.4273 1.8031 0.6092  0.2523  0.7010  360  PRO A CD  
2738  N N   . LEU A 361  ? 1.2486 1.9739 1.3433 0.7596  0.3494  0.7522  361  LEU A N   
2739  C CA  . LEU A 361  ? 1.2236 1.9438 1.3499 0.7966  0.3979  0.7669  361  LEU A CA  
2740  C C   . LEU A 361  ? 1.2110 2.0013 1.3867 0.8266  0.4257  0.8098  361  LEU A C   
2741  O O   . LEU A 361  ? 1.2067 2.0009 1.3895 0.8613  0.4530  0.8236  361  LEU A O   
2742  C CB  . LEU A 361  ? 1.2392 1.9132 1.3189 0.8170  0.3964  0.7459  361  LEU A CB  
2743  C CG  . LEU A 361  ? 1.2470 1.8438 1.2835 0.7957  0.3795  0.7035  361  LEU A CG  
2744  C CD1 . LEU A 361  ? 1.2770 1.8599 1.2688 0.7582  0.3273  0.6806  361  LEU A CD1 
2745  C CD2 . LEU A 361  ? 1.2591 1.8230 1.2599 0.8234  0.3858  0.6890  361  LEU A CD2 
2746  N N   . PHE A 362  ? 1.9831 2.8280 2.1931 0.8121  0.4185  0.8303  362  PHE A N   
2747  C CA  . PHE A 362  ? 2.0462 2.9546 2.3129 0.8370  0.4486  0.8703  362  PHE A CA  
2748  C C   . PHE A 362  ? 1.8916 2.8157 2.2120 0.8192  0.4688  0.8802  362  PHE A C   
2749  O O   . PHE A 362  ? 1.8517 2.8049 2.1791 0.7890  0.4436  0.8799  362  PHE A O   
2750  C CB  . PHE A 362  ? 2.2735 3.2494 2.5330 0.8434  0.4197  0.8918  362  PHE A CB  
2751  C CG  . PHE A 362  ? 2.4816 3.4385 2.6784 0.8470  0.3868  0.8747  362  PHE A CG  
2752  C CD1 . PHE A 362  ? 2.5763 3.5224 2.7278 0.8145  0.3385  0.8520  362  PHE A CD1 
2753  C CD2 . PHE A 362  ? 2.5554 3.5006 2.7355 0.8824  0.4044  0.8797  362  PHE A CD2 
2754  C CE1 . PHE A 362  ? 2.6959 3.6207 2.7862 0.8189  0.3080  0.8350  362  PHE A CE1 
2755  C CE2 . PHE A 362  ? 2.6643 3.5913 2.7849 0.8869  0.3751  0.8631  362  PHE A CE2 
2756  C CZ  . PHE A 362  ? 2.7158 3.6317 2.7906 0.8559  0.3266  0.8402  362  PHE A CZ  
2757  N N   . LEU A 363  ? 1.3572 2.2622 1.7150 0.8378  0.5149  0.8895  363  LEU A N   
2758  C CA  . LEU A 363  ? 1.2621 2.1785 1.6701 0.8250  0.5383  0.8990  363  LEU A CA  
2759  C C   . LEU A 363  ? 1.2250 2.2226 1.6809 0.8433  0.5492  0.9381  363  LEU A C   
2760  O O   . LEU A 363  ? 1.2137 2.2314 1.6910 0.8800  0.5775  0.9627  363  LEU A O   
2761  C CB  . LEU A 363  ? 1.1723 2.0344 1.5985 0.8399  0.5833  0.8942  363  LEU A CB  
2762  C CG  . LEU A 363  ? 1.1856 2.0342 1.5994 0.8785  0.6041  0.9026  363  LEU A CG  
2763  C CD1 . LEU A 363  ? 1.2008 2.0973 1.6664 0.9103  0.6407  0.9415  363  LEU A CD1 
2764  C CD2 . LEU A 363  ? 1.1388 1.9091 1.5341 0.8786  0.6240  0.8767  363  LEU A CD2 
2765  N N   . LYS A 364  ? 1.4198 2.4652 1.8911 0.8177  0.5252  0.9441  364  LYS A N   
2766  C CA  . LYS A 364  ? 1.3286 2.4504 1.8563 0.8322  0.5412  0.9803  364  LYS A CA  
2767  C C   . LYS A 364  ? 1.3176 2.4187 1.8921 0.8491  0.5937  0.9907  364  LYS A C   
2768  O O   . LYS A 364  ? 1.2558 2.2886 1.8182 0.8369  0.6083  0.9666  364  LYS A O   
2769  C CB  . LYS A 364  ? 1.3720 2.5411 1.9106 0.7955  0.5093  0.9803  364  LYS A CB  
2770  C CG  . LYS A 364  ? 1.4832 2.6595 1.9693 0.7719  0.4551  0.9648  364  LYS A CG  
2771  C CD  . LYS A 364  ? 1.5035 2.5964 1.9278 0.7559  0.4371  0.9262  364  LYS A CD  
2772  C CE  . LYS A 364  ? 1.5902 2.6875 1.9664 0.7229  0.3824  0.9086  364  LYS A CE  
2773  N NZ  . LYS A 364  ? 1.6682 2.8496 2.0602 0.7307  0.3624  0.9374  364  LYS A NZ  
2774  N N   . PRO A 365  ? 1.9567 3.1130 2.5816 0.8792  0.6222  1.0263  365  PRO A N   
2775  C CA  . PRO A 365  ? 1.9316 3.0653 2.5972 0.8993  0.6729  1.0375  365  PRO A CA  
2776  C C   . PRO A 365  ? 1.9487 3.0985 2.6563 0.8777  0.6859  1.0394  365  PRO A C   
2777  O O   . PRO A 365  ? 1.9993 3.2074 2.7232 0.8583  0.6625  1.0468  365  PRO A O   
2778  C CB  . PRO A 365  ? 1.9464 3.1325 2.6414 0.9443  0.6942  1.0757  365  PRO A CB  
2779  C CG  . PRO A 365  ? 1.9923 3.2151 2.6544 0.9493  0.6564  1.0805  365  PRO A CG  
2780  C CD  . PRO A 365  ? 2.0062 3.2361 2.6434 0.9047  0.6113  1.0573  365  PRO A CD  
2781  N N   . GLY A 366  ? 2.1210 3.2209 2.8463 0.8814  0.7239  1.0334  366  GLY A N   
2782  C CA  . GLY A 366  ? 2.1977 3.3049 2.9593 0.8604  0.7388  1.0327  366  GLY A CA  
2783  C C   . GLY A 366  ? 2.1098 3.1802 2.8420 0.8115  0.7100  0.9988  366  GLY A C   
2784  O O   . GLY A 366  ? 2.0852 3.1170 2.8291 0.7935  0.7290  0.9858  366  GLY A O   
2785  N N   . ILE A 367  ? 1.7181 2.7984 2.4102 0.7896  0.6638  0.9845  367  ILE A N   
2786  C CA  . ILE A 367  ? 1.6684 2.7024 2.3227 0.7438  0.6337  0.9498  367  ILE A CA  
2787  C C   . ILE A 367  ? 1.6128 2.5527 2.2329 0.7445  0.6476  0.9218  367  ILE A C   
2788  O O   . ILE A 367  ? 1.6110 2.5297 2.2271 0.7784  0.6694  0.9286  367  ILE A O   
2789  C CB  . ILE A 367  ? 1.7288 2.7928 2.3441 0.7217  0.5795  0.9414  367  ILE A CB  
2790  C CG1 . ILE A 367  ? 1.7451 2.8961 2.3972 0.7084  0.5650  0.9638  367  ILE A CG1 
2791  C CG2 . ILE A 367  ? 1.7224 2.7210 2.2846 0.6809  0.5475  0.9024  367  ILE A CG2 
2792  C CD1 . ILE A 367  ? 1.8038 2.9770 2.4181 0.6758  0.5112  0.9520  367  ILE A CD1 
2793  N N   . PRO A 368  ? 1.4013 2.2854 1.9993 0.7077  0.6373  0.8917  368  PRO A N   
2794  C CA  . PRO A 368  ? 1.3593 2.1556 1.9209 0.7060  0.6441  0.8630  368  PRO A CA  
2795  C C   . PRO A 368  ? 1.3438 2.1153 1.8453 0.6936  0.6000  0.8390  368  PRO A C   
2796  O O   . PRO A 368  ? 1.4018 2.1997 1.8824 0.6666  0.5600  0.8325  368  PRO A O   
2797  C CB  . PRO A 368  ? 1.2909 2.0438 1.8561 0.6702  0.6497  0.8427  368  PRO A CB  
2798  C CG  . PRO A 368  ? 1.3171 2.1356 1.9148 0.6498  0.6411  0.8585  368  PRO A CG  
2799  C CD  . PRO A 368  ? 1.3829 2.2817 1.9908 0.6669  0.6221  0.8839  368  PRO A CD  
2800  N N   . TYR A 369  ? 1.1862 1.9067 1.6589 0.7128  0.6072  0.8257  369  TYR A N   
2801  C CA  . TYR A 369  ? 1.1969 1.8934 1.6120 0.7056  0.5677  0.8032  369  TYR A CA  
2802  C C   . TYR A 369  ? 1.2503 1.8726 1.6214 0.6691  0.5440  0.7630  369  TYR A C   
2803  O O   . TYR A 369  ? 1.2077 1.7723 1.5826 0.6658  0.5679  0.7482  369  TYR A O   
2804  C CB  . TYR A 369  ? 1.2670 1.9539 1.6724 0.7458  0.5853  0.8105  369  TYR A CB  
2805  C CG  . TYR A 369  ? 1.2730 1.9491 1.6228 0.7475  0.5481  0.7938  369  TYR A CG  
2806  C CD1 . TYR A 369  ? 1.3820 2.0978 1.7078 0.7299  0.5044  0.7936  369  TYR A CD1 
2807  C CD2 . TYR A 369  ? 1.3080 1.9353 1.6290 0.7674  0.5570  0.7786  369  TYR A CD2 
2808  C CE1 . TYR A 369  ? 1.4310 2.1334 1.7032 0.7322  0.4706  0.7777  369  TYR A CE1 
2809  C CE2 . TYR A 369  ? 1.3755 1.9921 1.6454 0.7701  0.5246  0.7626  369  TYR A CE2 
2810  C CZ  . TYR A 369  ? 1.4553 2.1077 1.6998 0.7530  0.4816  0.7619  369  TYR A CZ  
2811  O OH  . TYR A 369  ? 1.5436 2.1820 1.7337 0.7565  0.4490  0.7451  369  TYR A OH  
2812  N N   . PRO A 370  ? 1.2609 1.8848 1.5898 0.6407  0.4960  0.7458  370  PRO A N   
2813  C CA  . PRO A 370  ? 1.2635 1.8209 1.5439 0.6038  0.4651  0.7079  370  PRO A CA  
2814  C C   . PRO A 370  ? 1.4002 1.8968 1.6247 0.6127  0.4475  0.6793  370  PRO A C   
2815  O O   . PRO A 370  ? 1.4567 1.9620 1.6392 0.6091  0.4096  0.6710  370  PRO A O   
2816  C CB  . PRO A 370  ? 1.3194 1.9175 1.5818 0.5719  0.4206  0.7083  370  PRO A CB  
2817  C CG  . PRO A 370  ? 1.3717 2.0610 1.6844 0.5900  0.4340  0.7479  370  PRO A CG  
2818  C CD  . PRO A 370  ? 1.3160 2.0160 1.6514 0.6377  0.4701  0.7670  370  PRO A CD  
2819  N N   . ILE A 371  ? 1.8171 2.2524 2.0387 0.6223  0.4723  0.6631  371  ILE A N   
2820  C CA  . ILE A 371  ? 1.8351 2.2163 2.0060 0.6322  0.4564  0.6358  371  ILE A CA  
2821  C C   . ILE A 371  ? 1.8833 2.1917 2.0043 0.5974  0.4244  0.5957  371  ILE A C   
2822  O O   . ILE A 371  ? 1.8318 2.0868 1.9592 0.5867  0.4421  0.5801  371  ILE A O   
2823  C CB  . ILE A 371  ? 1.8156 2.1729 2.0071 0.6665  0.4994  0.6405  371  ILE A CB  
2824  C CG1 . ILE A 371  ? 1.7804 2.2005 2.0266 0.6969  0.5367  0.6806  371  ILE A CG1 
2825  C CG2 . ILE A 371  ? 1.8137 2.1447 1.9602 0.6861  0.4843  0.6229  371  ILE A CG2 
2826  C CD1 . ILE A 371  ? 1.7490 2.1505 2.0092 0.7322  0.5747  0.6875  371  ILE A CD1 
2827  N N   . LYS A 372  ? 1.4827 1.7860 1.5520 0.5807  0.3770  0.5787  372  LYS A N   
2828  C CA  . LYS A 372  ? 1.4836 1.7178 1.5010 0.5474  0.3426  0.5411  372  LYS A CA  
2829  C C   . LYS A 372  ? 1.5062 1.6895 1.4689 0.5623  0.3230  0.5127  372  LYS A C   
2830  O O   . LYS A 372  ? 1.6128 1.8019 1.5299 0.5599  0.2847  0.5036  372  LYS A O   
2831  C CB  . LYS A 372  ? 1.5399 1.7940 1.5320 0.5102  0.2989  0.5381  372  LYS A CB  
2832  C CG  . LYS A 372  ? 1.6048 1.9108 1.6461 0.4897  0.3117  0.5630  372  LYS A CG  
2833  C CD  . LYS A 372  ? 1.7021 2.0412 1.7184 0.4585  0.2672  0.5644  372  LYS A CD  
2834  C CE  . LYS A 372  ? 1.8027 2.2364 1.8676 0.4712  0.2786  0.6035  372  LYS A CE  
2835  N NZ  . LYS A 372  ? 1.7916 2.2593 1.8864 0.4359  0.2760  0.6150  372  LYS A NZ  
2836  N N   . VAL A 373  ? 1.4850 1.6191 1.4519 0.5776  0.3490  0.4988  373  VAL A N   
2837  C CA  . VAL A 373  ? 1.5339 1.6150 1.4505 0.5901  0.3318  0.4687  373  VAL A CA  
2838  C C   . VAL A 373  ? 1.4894 1.5051 1.3533 0.5542  0.2914  0.4325  373  VAL A C   
2839  O O   . VAL A 373  ? 1.5059 1.5153 1.3776 0.5205  0.2835  0.4322  373  VAL A O   
2840  C CB  . VAL A 373  ? 1.4201 1.4754 1.3617 0.6189  0.3737  0.4674  373  VAL A CB  
2841  C CG1 . VAL A 373  ? 1.4048 1.4869 1.4120 0.6228  0.4196  0.4953  373  VAL A CG1 
2842  C CG2 . VAL A 373  ? 1.4124 1.3865 1.3174 0.6078  0.3618  0.4289  373  VAL A CG2 
2843  N N   . GLN A 374  ? 1.6384 1.6060 1.4479 0.5613  0.2658  0.4025  374  GLN A N   
2844  C CA  . GLN A 374  ? 1.6305 1.5371 1.3812 0.5288  0.2210  0.3683  374  GLN A CA  
2845  C C   . GLN A 374  ? 1.7050 1.5506 1.4096 0.5451  0.2084  0.3349  374  GLN A C   
2846  O O   . GLN A 374  ? 1.7932 1.6482 1.4646 0.5674  0.1916  0.3293  374  GLN A O   
2847  C CB  . GLN A 374  ? 1.7177 1.6549 1.4340 0.5091  0.1776  0.3723  374  GLN A CB  
2848  C CG  . GLN A 374  ? 1.7533 1.6317 1.3924 0.4903  0.1254  0.3366  374  GLN A CG  
2849  C CD  . GLN A 374  ? 1.8917 1.8028 1.4991 0.4693  0.0839  0.3433  374  GLN A CD  
2850  O OE1 . GLN A 374  ? 1.9347 1.8665 1.5113 0.4881  0.0643  0.3442  374  GLN A OE1 
2851  N NE2 . GLN A 374  ? 1.9414 1.8576 1.5560 0.4296  0.0706  0.3484  374  GLN A NE2 
2852  N N   . VAL A 375  ? 1.7069 1.4909 1.4101 0.5348  0.2172  0.3131  375  VAL A N   
2853  C CA  . VAL A 375  ? 1.6561 1.3840 1.3239 0.5522  0.2105  0.2823  375  VAL A CA  
2854  C C   . VAL A 375  ? 1.7317 1.4078 1.3251 0.5342  0.1568  0.2486  375  VAL A C   
2855  O O   . VAL A 375  ? 1.7693 1.4286 1.3392 0.4980  0.1271  0.2424  375  VAL A O   
2856  C CB  . VAL A 375  ? 1.6094 1.2889 1.3031 0.5481  0.2391  0.2710  375  VAL A CB  
2857  C CG1 . VAL A 375  ? 1.6168 1.2281 1.2637 0.5550  0.2196  0.2330  375  VAL A CG1 
2858  C CG2 . VAL A 375  ? 1.5859 1.3064 1.3429 0.5768  0.2925  0.2988  375  VAL A CG2 
2859  N N   . LYS A 376  ? 1.7191 1.3709 1.2750 0.5604  0.1450  0.2274  376  LYS A N   
2860  C CA  . LYS A 376  ? 1.7299 1.3245 1.2118 0.5496  0.0959  0.1919  376  LYS A CA  
2861  C C   . LYS A 376  ? 1.6427 1.1925 1.1071 0.5764  0.1024  0.1653  376  LYS A C   
2862  O O   . LYS A 376  ? 1.5721 1.1425 1.0792 0.6040  0.1427  0.1762  376  LYS A O   
2863  C CB  . LYS A 376  ? 1.8003 1.4277 1.2414 0.5576  0.0636  0.1959  376  LYS A CB  
2864  C CG  . LYS A 376  ? 1.8761 1.5552 1.3286 0.5330  0.0509  0.2224  376  LYS A CG  
2865  C CD  . LYS A 376  ? 1.9380 1.6608 1.3598 0.5516  0.0288  0.2316  376  LYS A CD  
2866  C CE  . LYS A 376  ? 1.9977 1.7597 1.4131 0.5221  0.0022  0.2499  376  LYS A CE  
2867  N NZ  . LYS A 376  ? 2.0294 1.8770 1.4878 0.5439  0.0251  0.2878  376  LYS A NZ  
2868  N N   . ASP A 377  ? 1.9562 1.4448 1.3552 0.5681  0.0608  0.1301  377  ASP A N   
2869  C CA  . ASP A 377  ? 1.9836 1.4233 1.3597 0.5902  0.0603  0.1004  377  ASP A CA  
2870  C C   . ASP A 377  ? 2.0780 1.5259 1.4064 0.6191  0.0373  0.0881  377  ASP A C   
2871  O O   . ASP A 377  ? 2.1403 1.6231 1.4472 0.6177  0.0172  0.1001  377  ASP A O   
2872  C CB  . ASP A 377  ? 2.0054 1.3644 1.3336 0.5602  0.0246  0.0668  377  ASP A CB  
2873  C CG  . ASP A 377  ? 2.1073 1.4475 1.3709 0.5378  -0.0275 0.0548  377  ASP A CG  
2874  O OD1 . ASP A 377  ? 2.1509 1.5389 1.4274 0.5213  -0.0312 0.0802  377  ASP A OD1 
2875  O OD2 . ASP A 377  ? 2.1678 1.4466 1.3680 0.5381  -0.0644 0.0204  377  ASP A OD2 
2876  N N   . SER A 378  ? 2.3384 1.7504 1.6465 0.6440  0.0377  0.0619  378  SER A N   
2877  C CA  . SER A 378  ? 2.3902 1.8042 1.6511 0.6749  0.0179  0.0461  378  SER A CA  
2878  C C   . SER A 378  ? 2.1562 1.5411 1.3429 0.6579  -0.0374 0.0284  378  SER A C   
2879  O O   . SER A 378  ? 2.1916 1.5830 1.3357 0.6815  -0.0564 0.0186  378  SER A O   
2880  C CB  . SER A 378  ? 2.3975 1.7648 1.6461 0.6966  0.0225  0.0155  378  SER A CB  
2881  O OG  . SER A 378  ? 2.3563 1.6844 1.6344 0.6751  0.0368  0.0092  378  SER A OG  
2882  N N   . LEU A 379  ? 2.2037 1.5560 1.3738 0.6165  -0.0629 0.0246  379  LEU A N   
2883  C CA  . LEU A 379  ? 2.3246 1.6406 1.4211 0.5951  -0.1176 0.0063  379  LEU A CA  
2884  C C   . LEU A 379  ? 2.4581 1.8160 1.5615 0.5651  -0.1299 0.0333  379  LEU A C   
2885  O O   . LEU A 379  ? 2.5592 1.8887 1.6051 0.5400  -0.1754 0.0215  379  LEU A O   
2886  C CB  . LEU A 379  ? 2.3234 1.5523 1.3776 0.5699  -0.1472 -0.0281 379  LEU A CB  
2887  C CG  . LEU A 379  ? 2.3497 1.5265 1.3416 0.5966  -0.1741 -0.0653 379  LEU A CG  
2888  C CD1 . LEU A 379  ? 2.3439 1.4383 1.3127 0.5868  -0.1869 -0.0996 379  LEU A CD1 
2889  C CD2 . LEU A 379  ? 2.4440 1.6094 1.3619 0.5914  -0.2233 -0.0754 379  LEU A CD2 
2890  N N   . ASP A 380  ? 2.6183 2.0436 1.7931 0.5675  -0.0887 0.0697  380  ASP A N   
2891  C CA  . ASP A 380  ? 2.7093 2.1908 1.9037 0.5461  -0.0922 0.1007  380  ASP A CA  
2892  C C   . ASP A 380  ? 2.7731 2.2252 1.9533 0.4962  -0.1186 0.0978  380  ASP A C   
2893  O O   . ASP A 380  ? 2.8393 2.3035 1.9869 0.4740  -0.1523 0.1029  380  ASP A O   
2894  C CB  . ASP A 380  ? 2.8384 2.3535 1.9932 0.5626  -0.1172 0.1060  380  ASP A CB  
2895  C CG  . ASP A 380  ? 2.8929 2.4675 2.0842 0.6073  -0.0802 0.1260  380  ASP A CG  
2896  O OD1 . ASP A 380  ? 2.8702 2.5080 2.1268 0.6118  -0.0430 0.1609  380  ASP A OD1 
2897  O OD2 . ASP A 380  ? 2.9670 2.5245 2.1205 0.6383  -0.0884 0.1068  380  ASP A OD2 
2898  N N   . GLN A 381  ? 2.8086 2.2211 2.0118 0.4783  -0.1034 0.0891  381  GLN A N   
2899  C CA  . GLN A 381  ? 2.8441 2.2490 2.0613 0.4330  -0.1096 0.0975  381  GLN A CA  
2900  C C   . GLN A 381  ? 2.7498 2.2055 2.0518 0.4379  -0.0557 0.1282  381  GLN A C   
2901  O O   . GLN A 381  ? 2.6768 2.1501 2.0173 0.4721  -0.0178 0.1345  381  GLN A O   
2902  C CB  . GLN A 381  ? 2.9101 2.2259 2.0864 0.4063  -0.1334 0.0639  381  GLN A CB  
2903  C CG  . GLN A 381  ? 3.0364 2.2881 2.1244 0.4009  -0.1875 0.0295  381  GLN A CG  
2904  C CD  . GLN A 381  ? 3.0812 2.2634 2.1417 0.4207  -0.1901 -0.0049 381  GLN A CD  
2905  O OE1 . GLN A 381  ? 3.1337 2.2421 2.1558 0.3958  -0.2148 -0.0311 381  GLN A OE1 
2906  N NE2 . GLN A 381  ? 3.0521 2.2584 2.1331 0.4657  -0.1639 -0.0047 381  GLN A NE2 
2907  N N   . LEU A 382  ? 2.3365 1.8148 1.6662 0.4032  -0.0525 0.1471  382  LEU A N   
2908  C CA  . LEU A 382  ? 2.2450 1.7645 1.6519 0.4035  -0.0034 0.1748  382  LEU A CA  
2909  C C   . LEU A 382  ? 2.2216 1.6785 1.6367 0.3995  0.0139  0.1546  382  LEU A C   
2910  O O   . LEU A 382  ? 2.2963 1.6813 1.6591 0.3788  -0.0185 0.1236  382  LEU A O   
2911  C CB  . LEU A 382  ? 2.2691 1.8210 1.6948 0.3641  -0.0101 0.1952  382  LEU A CB  
2912  C CG  . LEU A 382  ? 2.2957 1.9311 1.7417 0.3739  -0.0099 0.2263  382  LEU A CG  
2913  C CD1 . LEU A 382  ? 2.3530 2.0229 1.8173 0.3337  -0.0188 0.2456  382  LEU A CD1 
2914  C CD2 . LEU A 382  ? 2.2169 1.9101 1.7278 0.4145  0.0412  0.2533  382  LEU A CD2 
2915  N N   . VAL A 383  ? 2.0107 1.4917 1.4888 0.4185  0.0634  0.1717  383  VAL A N   
2916  C CA  . VAL A 383  ? 1.9396 1.3622 1.4285 0.4129  0.0812  0.1542  383  VAL A CA  
2917  C C   . VAL A 383  ? 1.9219 1.3804 1.4820 0.4067  0.1274  0.1827  383  VAL A C   
2918  O O   . VAL A 383  ? 1.8984 1.4133 1.5103 0.4353  0.1660  0.2091  383  VAL A O   
2919  C CB  . VAL A 383  ? 1.8414 1.2361 1.3226 0.4506  0.0929  0.1353  383  VAL A CB  
2920  C CG1 . VAL A 383  ? 1.8536 1.3080 1.3441 0.4886  0.1028  0.1514  383  VAL A CG1 
2921  C CG2 . VAL A 383  ? 1.7210 1.1017 1.2534 0.4585  0.1375  0.1393  383  VAL A CG2 
2922  N N   . GLY A 384  ? 1.7137 1.1377 1.2735 0.3689  0.1226  0.1773  384  GLY A N   
2923  C CA  . GLY A 384  ? 1.7058 1.1642 1.3281 0.3582  0.1621  0.2044  384  GLY A CA  
2924  C C   . GLY A 384  ? 1.6916 1.1094 1.3421 0.3666  0.1965  0.1968  384  GLY A C   
2925  O O   . GLY A 384  ? 1.7044 1.0590 1.3207 0.3720  0.1833  0.1670  384  GLY A O   
2926  N N   . GLY A 385  ? 2.1327 1.5870 1.8452 0.3683  0.2400  0.2239  385  GLY A N   
2927  C CA  . GLY A 385  ? 2.0956 1.5117 1.8376 0.3708  0.2742  0.2196  385  GLY A CA  
2928  C C   . GLY A 385  ? 2.0416 1.4667 1.8083 0.4132  0.3046  0.2227  385  GLY A C   
2929  O O   . GLY A 385  ? 2.0300 1.4008 1.7888 0.4197  0.3112  0.2018  385  GLY A O   
2930  N N   . VAL A 386  ? 1.6277 1.1227 1.4251 0.4417  0.3234  0.2497  386  VAL A N   
2931  C CA  . VAL A 386  ? 1.5713 1.0791 1.3873 0.4818  0.3490  0.2534  386  VAL A CA  
2932  C C   . VAL A 386  ? 1.4888 1.0639 1.3672 0.5024  0.3937  0.2924  386  VAL A C   
2933  O O   . VAL A 386  ? 1.5063 1.1367 1.3996 0.4974  0.3915  0.3157  386  VAL A O   
2934  C CB  . VAL A 386  ? 1.4567 0.9736 1.2281 0.5023  0.3171  0.2400  386  VAL A CB  
2935  C CG1 . VAL A 386  ? 1.4155 0.8968 1.1758 0.5296  0.3247  0.2191  386  VAL A CG1 
2936  C CG2 . VAL A 386  ? 1.4961 0.9785 1.2050 0.4728  0.2630  0.2157  386  VAL A CG2 
2937  N N   . PRO A 387  ? 1.4738 1.0431 1.3876 0.5255  0.4334  0.2991  387  PRO A N   
2938  C CA  . PRO A 387  ? 1.4931 1.1129 1.4663 0.5489  0.4815  0.3338  387  PRO A CA  
2939  C C   . PRO A 387  ? 1.5482 1.2357 1.5294 0.5808  0.4850  0.3561  387  PRO A C   
2940  O O   . PRO A 387  ? 1.5747 1.2575 1.5176 0.5933  0.4592  0.3397  387  PRO A O   
2941  C CB  . PRO A 387  ? 1.4603 1.0363 1.4486 0.5628  0.5103  0.3233  387  PRO A CB  
2942  C CG  . PRO A 387  ? 1.3624 0.8754 1.2990 0.5540  0.4758  0.2837  387  PRO A CG  
2943  C CD  . PRO A 387  ? 1.4016 0.9133 1.2896 0.5355  0.4276  0.2692  387  PRO A CD  
2944  N N   . VAL A 388  ? 1.4804 1.2273 1.5089 0.5951  0.5168  0.3921  388  VAL A N   
2945  C CA  . VAL A 388  ? 1.4892 1.3031 1.5220 0.6179  0.5136  0.4148  388  VAL A CA  
2946  C C   . VAL A 388  ? 1.4799 1.3458 1.5687 0.6449  0.5601  0.4525  388  VAL A C   
2947  O O   . VAL A 388  ? 1.4844 1.4042 1.5979 0.6445  0.5653  0.4792  388  VAL A O   
2948  C CB  . VAL A 388  ? 1.5272 1.3713 1.5445 0.5927  0.4805  0.4200  388  VAL A CB  
2949  C CG1 . VAL A 388  ? 1.5585 1.4746 1.5842 0.6139  0.4779  0.4462  388  VAL A CG1 
2950  C CG2 . VAL A 388  ? 1.5331 1.3277 1.4893 0.5679  0.4315  0.3843  388  VAL A CG2 
2951  N N   . THR A 389  ? 1.8284 1.6792 1.9368 0.6685  0.5932  0.4553  389  THR A N   
2952  C CA  . THR A 389  ? 1.8215 1.7124 1.9819 0.6925  0.6393  0.4905  389  THR A CA  
2953  C C   . THR A 389  ? 1.8499 1.8126 2.0199 0.7176  0.6406  0.5193  389  THR A C   
2954  O O   . THR A 389  ? 1.9272 1.9015 2.0707 0.7363  0.6266  0.5132  389  THR A O   
2955  C CB  . THR A 389  ? 1.9811 1.8400 2.1556 0.7126  0.6722  0.4869  389  THR A CB  
2956  O OG1 . THR A 389  ? 2.0019 1.8038 2.1377 0.7032  0.6491  0.4499  389  THR A OG1 
2957  C CG2 . THR A 389  ? 1.9513 1.7909 2.1678 0.7065  0.7110  0.5002  389  THR A CG2 
2958  N N   . LEU A 390  ? 1.2885 1.2993 1.4970 0.7193  0.6590  0.5508  390  LEU A N   
2959  C CA  . LEU A 390  ? 1.2761 1.3580 1.4963 0.7414  0.6593  0.5804  390  LEU A CA  
2960  C C   . LEU A 390  ? 1.3239 1.4391 1.5889 0.7732  0.7053  0.6146  390  LEU A C   
2961  O O   . LEU A 390  ? 1.3717 1.5229 1.6739 0.7743  0.7239  0.6412  390  LEU A O   
2962  C CB  . LEU A 390  ? 1.3242 1.4475 1.5509 0.7203  0.6381  0.5923  390  LEU A CB  
2963  C CG  . LEU A 390  ? 1.3094 1.5080 1.5503 0.7423  0.6375  0.6239  390  LEU A CG  
2964  C CD1 . LEU A 390  ? 1.3891 1.5892 1.5881 0.7587  0.6140  0.6117  390  LEU A CD1 
2965  C CD2 . LEU A 390  ? 1.3434 1.5867 1.5902 0.7209  0.6137  0.6350  390  LEU A CD2 
2966  N N   . ASN A 391  ? 1.5874 1.6922 1.8485 0.7990  0.7233  0.6146  391  ASN A N   
2967  C CA  . ASN A 391  ? 1.6367 1.7739 1.9348 0.8299  0.7643  0.6482  391  ASN A CA  
2968  C C   . ASN A 391  ? 1.6984 1.9044 1.9986 0.8495  0.7557  0.6748  391  ASN A C   
2969  O O   . ASN A 391  ? 1.7550 1.9761 2.0191 0.8526  0.7243  0.6644  391  ASN A O   
2970  C CB  . ASN A 391  ? 1.6964 1.8026 1.9867 0.8490  0.7837  0.6395  391  ASN A CB  
2971  C CG  . ASN A 391  ? 1.7196 1.7610 2.0116 0.8321  0.7949  0.6163  391  ASN A CG  
2972  O OD1 . ASN A 391  ? 1.7051 1.7085 1.9707 0.8065  0.7667  0.5862  391  ASN A OD1 
2973  N ND2 . ASN A 391  ? 1.7441 1.7699 2.0661 0.8454  0.8358  0.6303  391  ASN A ND2 
2974  N N   . ALA A 392  ? 1.6066 1.8536 1.9475 0.8641  0.7833  0.7095  392  ALA A N   
2975  C CA  . ALA A 392  ? 1.6220 1.9360 1.9669 0.8820  0.7742  0.7361  392  ALA A CA  
2976  C C   . ALA A 392  ? 1.6171 1.9544 1.9917 0.9164  0.8149  0.7686  392  ALA A C   
2977  O O   . ALA A 392  ? 1.6172 1.9176 2.0086 0.9236  0.8484  0.7693  392  ALA A O   
2978  C CB  . ALA A 392  ? 1.6155 1.9670 1.9802 0.8637  0.7608  0.7483  392  ALA A CB  
2979  N N   . GLN A 393  ? 1.6254 2.0219 2.0041 0.9372  0.8106  0.7950  393  GLN A N   
2980  C CA  . GLN A 393  ? 1.7138 2.1384 2.1181 0.9711  0.8459  0.8292  393  GLN A CA  
2981  C C   . GLN A 393  ? 1.7456 2.2408 2.1594 0.9834  0.8322  0.8574  393  GLN A C   
2982  O O   . GLN A 393  ? 1.7343 2.2551 2.1218 0.9721  0.7932  0.8479  393  GLN A O   
2983  C CB  . GLN A 393  ? 1.7630 2.1685 2.1419 0.9912  0.8544  0.8228  393  GLN A CB  
2984  C CG  . GLN A 393  ? 1.7983 2.2180 2.2010 1.0236  0.8953  0.8551  393  GLN A CG  
2985  C CD  . GLN A 393  ? 1.8495 2.3219 2.2376 1.0496  0.8864  0.8770  393  GLN A CD  
2986  O OE1 . GLN A 393  ? 1.8822 2.3844 2.2938 1.0742  0.9119  0.9108  393  GLN A OE1 
2987  N NE2 . GLN A 393  ? 1.8581 2.3399 2.2051 1.0444  0.8497  0.8577  393  GLN A NE2 
2988  N N   . THR A 394  ? 2.2556 2.7810 2.7065 1.0062  0.8637  0.8921  394  THR A N   
2989  C CA  . THR A 394  ? 2.3120 2.9054 2.7780 1.0184  0.8533  0.9207  394  THR A CA  
2990  C C   . THR A 394  ? 2.4687 3.0849 2.9615 1.0540  0.8904  0.9572  394  THR A C   
2991  O O   . THR A 394  ? 2.5244 3.1011 3.0266 1.0652  0.9248  0.9597  394  THR A O   
2992  C CB  . THR A 394  ? 2.2013 2.8170 2.6948 0.9957  0.8434  0.9232  394  THR A CB  
2993  O OG1 . THR A 394  ? 2.2003 2.8541 2.6713 0.9800  0.7990  0.9158  394  THR A OG1 
2994  C CG2 . THR A 394  ? 2.2126 2.8684 2.7546 1.0168  0.8744  0.9608  394  THR A CG2 
2995  N N   . ILE A 395  ? 1.7749 2.4533 2.2779 1.0714  0.8821  0.9853  395  ILE A N   
2996  C CA  . ILE A 395  ? 1.8571 2.5603 2.3836 1.1061  0.9141  1.0218  395  ILE A CA  
2997  C C   . ILE A 395  ? 1.9231 2.6901 2.4829 1.1136  0.9096  1.0505  395  ILE A C   
2998  O O   . ILE A 395  ? 1.9360 2.7409 2.4896 1.0973  0.8744  1.0450  395  ILE A O   
2999  C CB  . ILE A 395  ? 1.9040 2.6153 2.3973 1.1281  0.9094  1.0273  395  ILE A CB  
3000  C CG1 . ILE A 395  ? 1.9137 2.6818 2.3870 1.1287  0.8697  1.0328  395  ILE A CG1 
3001  C CG2 . ILE A 395  ? 1.9029 2.5569 2.3611 1.1166  0.9067  0.9941  395  ILE A CG2 
3002  C CD1 . ILE A 395  ? 1.9789 2.8002 2.4672 1.1615  0.8806  1.0727  395  ILE A CD1 
3003  N N   . ASP A 396  ? 1.9446 2.7214 2.5405 1.1376  0.9456  1.0805  396  ASP A N   
3004  C CA  . ASP A 396  ? 1.9689 2.8046 2.6018 1.1477  0.9467  1.1089  396  ASP A CA  
3005  C C   . ASP A 396  ? 2.0157 2.9074 2.6322 1.1660  0.9231  1.1273  396  ASP A C   
3006  O O   . ASP A 396  ? 2.0585 2.9363 2.6394 1.1752  0.9166  1.1217  396  ASP A O   
3007  C CB  . ASP A 396  ? 2.0405 2.8660 2.7092 1.1744  0.9928  1.1367  396  ASP A CB  
3008  C CG  . ASP A 396  ? 2.0953 2.9509 2.8092 1.1711  1.0024  1.1506  396  ASP A CG  
3009  O OD1 . ASP A 396  ? 2.1604 3.0045 2.9036 1.1917  1.0399  1.1714  396  ASP A OD1 
3010  O OD2 . ASP A 396  ? 2.0693 2.9592 2.7888 1.1477  0.9730  1.1406  396  ASP A OD2 
3011  N N   . VAL A 397  ? 2.2865 3.2425 2.9287 1.1714  0.9103  1.1492  397  VAL A N   
3012  C CA  . VAL A 397  ? 2.3855 3.3971 3.0210 1.1972  0.8976  1.1762  397  VAL A CA  
3013  C C   . VAL A 397  ? 2.4371 3.4330 3.0838 1.2338  0.9387  1.2035  397  VAL A C   
3014  O O   . VAL A 397  ? 2.4933 3.5065 3.1208 1.2582  0.9375  1.2210  397  VAL A O   
3015  C CB  . VAL A 397  ? 2.4149 3.5007 3.0828 1.1970  0.8791  1.1968  397  VAL A CB  
3016  C CG1 . VAL A 397  ? 2.4111 3.5159 3.1290 1.2224  0.9162  1.2284  397  VAL A CG1 
3017  C CG2 . VAL A 397  ? 2.4973 3.6370 3.1422 1.2093  0.8472  1.2108  397  VAL A CG2 
3018  N N   . ASN A 398  ? 2.7283 3.6876 3.4039 1.2361  0.9751  1.2061  398  ASN A N   
3019  C CA  . ASN A 398  ? 2.7948 3.7273 3.4810 1.2669  1.0170  1.2292  398  ASN A CA  
3020  C C   . ASN A 398  ? 2.8025 3.6826 3.4498 1.2701  1.0263  1.2157  398  ASN A C   
3021  O O   . ASN A 398  ? 2.8101 3.6533 3.4616 1.2884  1.0623  1.2281  398  ASN A O   
3022  C CB  . ASN A 398  ? 2.8019 3.7008 3.5240 1.2628  1.0505  1.2295  398  ASN A CB  
3023  C CG  . ASN A 398  ? 2.8969 3.8100 3.6503 1.2985  1.0848  1.2672  398  ASN A CG  
3024  O OD1 . ASN A 398  ? 2.9778 3.9368 3.7322 1.3249  1.0799  1.2949  398  ASN A OD1 
3025  N ND2 . ASN A 398  ? 2.8858 3.7578 3.6635 1.2996  1.1193  1.2684  398  ASN A ND2 
3026  N N   . GLN A 399  ? 2.4577 3.3352 3.0667 1.2521  0.9938  1.1902  399  GLN A N   
3027  C CA  . GLN A 399  ? 2.4950 3.3221 3.0668 1.2496  0.9994  1.1704  399  GLN A CA  
3028  C C   . GLN A 399  ? 2.4771 3.2386 3.0615 1.2426  1.0348  1.1588  399  GLN A C   
3029  O O   . GLN A 399  ? 2.5030 3.2299 3.0766 1.2577  1.0616  1.1648  399  GLN A O   
3030  C CB  . GLN A 399  ? 2.5934 3.4361 3.1424 1.2799  1.0060  1.1930  399  GLN A CB  
3031  C CG  . GLN A 399  ? 2.6381 3.5344 3.1607 1.2831  0.9665  1.1964  399  GLN A CG  
3032  C CD  . GLN A 399  ? 2.6116 3.4915 3.0934 1.2574  0.9323  1.1589  399  GLN A CD  
3033  O OE1 . GLN A 399  ? 2.6290 3.4677 3.0821 1.2560  0.9397  1.1412  399  GLN A OE1 
3034  N NE2 . GLN A 399  ? 2.5735 3.4863 3.0520 1.2370  0.8944  1.1470  399  GLN A NE2 
3035  N N   . GLU A 400  ? 2.4631 3.2088 3.0699 1.2188  1.0343  1.1429  400  GLU A N   
3036  C CA  . GLU A 400  ? 2.4320 3.1136 3.0490 1.2056  1.0619  1.1264  400  GLU A CA  
3037  C C   . GLU A 400  ? 2.3135 2.9622 2.9084 1.1696  1.0361  1.0845  400  GLU A C   
3038  O O   . GLU A 400  ? 2.2634 2.9404 2.8558 1.1499  1.0034  1.0721  400  GLU A O   
3039  C CB  . GLU A 400  ? 2.4520 3.1369 3.1134 1.2095  1.0869  1.1439  400  GLU A CB  
3040  C CG  . GLU A 400  ? 2.5189 3.1394 3.1919 1.2111  1.1274  1.1420  400  GLU A CG  
3041  C CD  . GLU A 400  ? 2.5975 3.2253 3.3117 1.2262  1.1571  1.1678  400  GLU A CD  
3042  O OE1 . GLU A 400  ? 2.6667 3.2823 3.3890 1.2538  1.1889  1.1937  400  GLU A OE1 
3043  O OE2 . GLU A 400  ? 2.5869 3.2319 3.3242 1.2107  1.1490  1.1623  400  GLU A OE2 
3044  N N   . THR A 401  ? 2.8160 3.4052 3.3940 1.1610  1.0498  1.0631  401  THR A N   
3045  C CA  . THR A 401  ? 2.7057 3.2602 3.2591 1.1295  1.0248  1.0228  401  THR A CA  
3046  C C   . THR A 401  ? 2.6046 3.1241 3.1793 1.1045  1.0323  1.0065  401  THR A C   
3047  O O   . THR A 401  ? 2.6362 3.1504 3.2446 1.1122  1.0619  1.0250  401  THR A O   
3048  C CB  . THR A 401  ? 2.7135 3.2195 3.2385 1.1297  1.0338  1.0036  401  THR A CB  
3049  O OG1 . THR A 401  ? 2.7142 3.1726 3.2597 1.1333  1.0738  1.0086  401  THR A OG1 
3050  C CG2 . THR A 401  ? 2.7863 3.3201 3.2879 1.1548  1.0313  1.0188  401  THR A CG2 
3051  N N   . SER A 402  ? 2.3402 2.8323 2.8923 1.0749  1.0056  0.9710  402  SER A N   
3052  C CA  . SER A 402  ? 2.2249 2.6804 2.7906 1.0474  1.0079  0.9515  402  SER A CA  
3053  C C   . SER A 402  ? 2.1258 2.5341 2.6574 1.0214  0.9851  0.9111  402  SER A C   
3054  O O   . SER A 402  ? 2.0705 2.4952 2.5723 1.0098  0.9472  0.8937  402  SER A O   
3055  C CB  . SER A 402  ? 2.2098 2.7105 2.7953 1.0343  0.9887  0.9583  402  SER A CB  
3056  O OG  . SER A 402  ? 2.2083 2.7471 2.7675 1.0252  0.9462  0.9490  402  SER A OG  
3057  N N   . ASP A 403  ? 2.2824 2.6306 2.8169 1.0131  1.0079  0.8964  403  ASP A N   
3058  C CA  . ASP A 403  ? 2.2409 2.5395 2.7484 0.9858  0.9878  0.8571  403  ASP A CA  
3059  C C   . ASP A 403  ? 2.1645 2.4410 2.6843 0.9560  0.9809  0.8419  403  ASP A C   
3060  O O   . ASP A 403  ? 2.1698 2.4160 2.7148 0.9528  1.0102  0.8471  403  ASP A O   
3061  C CB  . ASP A 403  ? 2.3061 2.5515 2.8056 0.9914  1.0119  0.8462  403  ASP A CB  
3062  C CG  . ASP A 403  ? 2.3785 2.6255 2.8417 0.9989  0.9930  0.8313  403  ASP A CG  
3063  O OD1 . ASP A 403  ? 2.3464 2.6017 2.7804 0.9844  0.9542  0.8087  403  ASP A OD1 
3064  O OD2 . ASP A 403  ? 2.4545 2.6941 2.9174 1.0194  1.0173  0.8424  403  ASP A OD2 
3065  N N   . LEU A 404  ? 1.3966 1.6872 1.8960 0.9337  0.9414  0.8230  404  LEU A N   
3066  C CA  . LEU A 404  ? 1.3208 1.5923 1.8269 0.9029  0.9307  0.8072  404  LEU A CA  
3067  C C   . LEU A 404  ? 1.3166 1.5145 1.8100 0.8821  0.9360  0.7766  404  LEU A C   
3068  O O   . LEU A 404  ? 1.3500 1.5098 1.8334 0.8919  0.9514  0.7681  404  LEU A O   
3069  C CB  . LEU A 404  ? 1.2316 1.5336 1.7142 0.8820  0.8845  0.7935  404  LEU A CB  
3070  C CG  . LEU A 404  ? 1.1957 1.5703 1.6986 0.8892  0.8751  0.8209  404  LEU A CG  
3071  C CD1 . LEU A 404  ? 1.2619 1.6503 1.7384 0.8602  0.8291  0.8009  404  LEU A CD1 
3072  C CD2 . LEU A 404  ? 1.1612 1.5476 1.7095 0.8911  0.9062  0.8428  404  LEU A CD2 
3073  N N   . ASP A 405  ? 1.7661 1.9471 2.2601 0.8519  0.9216  0.7607  405  ASP A N   
3074  C CA  . ASP A 405  ? 1.7239 1.8373 2.2095 0.8278  0.9252  0.7334  405  ASP A CA  
3075  C C   . ASP A 405  ? 1.6488 1.7441 2.0974 0.7975  0.8811  0.7007  405  ASP A C   
3076  O O   . ASP A 405  ? 1.6261 1.7581 2.0702 0.7834  0.8543  0.7021  405  ASP A O   
3077  C CB  . ASP A 405  ? 1.7704 1.8734 2.2911 0.8196  0.9535  0.7458  405  ASP A CB  
3078  C CG  . ASP A 405  ? 1.9931 2.0822 2.5415 0.8452  0.9995  0.7681  405  ASP A CG  
3079  O OD1 . ASP A 405  ? 2.0318 2.0835 2.5661 0.8540  1.0092  0.7581  405  ASP A OD1 
3080  O OD2 . ASP A 405  ? 1.9743 2.0901 2.5573 0.8567  1.0251  0.7952  405  ASP A OD2 
3081  N N   . PRO A 406  ? 1.4399 1.4763 1.8620 0.7868  0.8739  0.6709  406  PRO A N   
3082  C CA  . PRO A 406  ? 1.4228 1.4327 1.8002 0.7660  0.8318  0.6365  406  PRO A CA  
3083  C C   . PRO A 406  ? 1.4621 1.4618 1.8333 0.7317  0.8092  0.6232  406  PRO A C   
3084  O O   . PRO A 406  ? 1.5096 1.4685 1.8935 0.7153  0.8256  0.6162  406  PRO A O   
3085  C CB  . PRO A 406  ? 1.4213 1.3648 1.7865 0.7639  0.8434  0.6129  406  PRO A CB  
3086  C CG  . PRO A 406  ? 1.4464 1.3917 1.8466 0.7894  0.8902  0.6383  406  PRO A CG  
3087  C CD  . PRO A 406  ? 1.4355 1.4226 1.8720 0.7942  0.9097  0.6695  406  PRO A CD  
3088  N N   . SER A 407  ? 1.6044 1.6395 1.9560 0.7201  0.7730  0.6204  407  SER A N   
3089  C CA  . SER A 407  ? 1.6424 1.6601 1.9804 0.6835  0.7473  0.6031  407  SER A CA  
3090  C C   . SER A 407  ? 1.6629 1.6280 1.9503 0.6657  0.7116  0.5648  407  SER A C   
3091  O O   . SER A 407  ? 1.6922 1.6563 1.9557 0.6838  0.7006  0.5565  407  SER A O   
3092  C CB  . SER A 407  ? 1.6735 1.7563 2.0177 0.6771  0.7266  0.6206  407  SER A CB  
3093  O OG  . SER A 407  ? 1.7031 1.8351 2.0958 0.6968  0.7612  0.6565  407  SER A OG  
3094  N N   . LYS A 408  ? 1.7794 1.7000 2.0500 0.6314  0.6944  0.5418  408  LYS A N   
3095  C CA  . LYS A 408  ? 1.7430 1.6092 1.9625 0.6114  0.6570  0.5040  408  LYS A CA  
3096  C C   . LYS A 408  ? 1.6871 1.5425 1.8893 0.5731  0.6283  0.4917  408  LYS A C   
3097  O O   . LYS A 408  ? 1.6883 1.5285 1.9128 0.5553  0.6460  0.4956  408  LYS A O   
3098  C CB  . LYS A 408  ? 1.7485 1.5447 1.9633 0.6098  0.6735  0.4827  408  LYS A CB  
3099  C CG  . LYS A 408  ? 1.8092 1.5430 1.9758 0.5812  0.6360  0.4437  408  LYS A CG  
3100  C CD  . LYS A 408  ? 1.8697 1.5370 2.0354 0.5804  0.6536  0.4244  408  LYS A CD  
3101  C CE  . LYS A 408  ? 1.8854 1.5648 2.0764 0.6160  0.6884  0.4386  408  LYS A CE  
3102  N NZ  . LYS A 408  ? 1.8843 1.4999 2.0646 0.6162  0.6959  0.4145  408  LYS A NZ  
3103  N N   . SER A 409  ? 1.3532 1.2162 1.5148 0.5598  0.5843  0.4773  409  SER A N   
3104  C CA  . SER A 409  ? 1.4132 1.2544 1.5492 0.5197  0.5524  0.4605  409  SER A CA  
3105  C C   . SER A 409  ? 1.5245 1.2989 1.6072 0.5088  0.5210  0.4228  409  SER A C   
3106  O O   . SER A 409  ? 1.4629 1.2097 1.5388 0.5313  0.5313  0.4120  409  SER A O   
3107  C CB  . SER A 409  ? 1.5058 1.4055 1.6323 0.5093  0.5222  0.4728  409  SER A CB  
3108  O OG  . SER A 409  ? 1.5350 1.4082 1.6326 0.4674  0.4897  0.4546  409  SER A OG  
3109  N N   . VAL A 410  ? 1.6529 1.4028 1.6976 0.4741  0.4822  0.4031  410  VAL A N   
3110  C CA  . VAL A 410  ? 1.7392 1.4299 1.7249 0.4624  0.4430  0.3668  410  VAL A CA  
3111  C C   . VAL A 410  ? 1.8585 1.5672 1.8066 0.4378  0.3972  0.3613  410  VAL A C   
3112  O O   . VAL A 410  ? 1.8847 1.6303 1.8509 0.4165  0.3957  0.3784  410  VAL A O   
3113  C CB  . VAL A 410  ? 1.7350 1.3487 1.7085 0.4397  0.4458  0.3419  410  VAL A CB  
3114  C CG1 . VAL A 410  ? 1.7998 1.3506 1.7092 0.4271  0.4018  0.3034  410  VAL A CG1 
3115  C CG2 . VAL A 410  ? 1.6612 1.2603 1.6733 0.4649  0.4918  0.3492  410  VAL A CG2 
3116  N N   . THR A 411  ? 1.4483 1.1329 1.3443 0.4425  0.3608  0.3382  411  THR A N   
3117  C CA  . THR A 411  ? 1.4682 1.1689 1.3224 0.4249  0.3153  0.3325  411  THR A CA  
3118  C C   . THR A 411  ? 1.4821 1.1416 1.3078 0.3783  0.2872  0.3156  411  THR A C   
3119  O O   . THR A 411  ? 1.4257 1.0142 1.2268 0.3632  0.2805  0.2891  411  THR A O   
3120  C CB  . THR A 411  ? 1.4845 1.1541 1.2856 0.4422  0.2853  0.3069  411  THR A CB  
3121  O OG1 . THR A 411  ? 1.5742 1.2202 1.3173 0.4138  0.2338  0.2870  411  THR A OG1 
3122  C CG2 . THR A 411  ? 1.4199 1.0217 1.2099 0.4479  0.2946  0.2815  411  THR A CG2 
3123  N N   . ARG A 412  ? 1.7591 1.4635 1.5862 0.3556  0.2694  0.3308  412  ARG A N   
3124  C CA  . ARG A 412  ? 1.9200 1.5928 1.7174 0.3083  0.2392  0.3171  412  ARG A CA  
3125  C C   . ARG A 412  ? 1.9535 1.5475 1.6760 0.2903  0.1926  0.2776  412  ARG A C   
3126  O O   . ARG A 412  ? 1.9550 1.5301 1.6453 0.3149  0.1774  0.2621  412  ARG A O   
3127  C CB  . ARG A 412  ? 2.0912 1.8336 1.8988 0.2905  0.2232  0.3405  412  ARG A CB  
3128  C CG  . ARG A 412  ? 2.2633 1.9883 2.0575 0.2402  0.2036  0.3349  412  ARG A CG  
3129  C CD  . ARG A 412  ? 2.4301 2.2269 2.2335 0.2213  0.1851  0.3574  412  ARG A CD  
3130  N NE  . ARG A 412  ? 2.4768 2.3284 2.3421 0.2113  0.2191  0.3860  412  ARG A NE  
3131  C CZ  . ARG A 412  ? 2.5649 2.4861 2.4509 0.1945  0.2107  0.4090  412  ARG A CZ  
3132  N NH1 . ARG A 412  ? 2.6483 2.5910 2.4969 0.1843  0.1686  0.4070  412  ARG A NH1 
3133  N NH2 . ARG A 412  ? 2.5499 2.5196 2.4939 0.1881  0.2442  0.4339  412  ARG A NH2 
3134  N N   . VAL A 413  ? 1.8432 1.3918 1.5376 0.2474  0.1701  0.2618  413  VAL A N   
3135  C CA  . VAL A 413  ? 1.8796 1.3442 1.5029 0.2266  0.1274  0.2237  413  VAL A CA  
3136  C C   . VAL A 413  ? 1.9493 1.4174 1.5173 0.2057  0.0756  0.2153  413  VAL A C   
3137  O O   . VAL A 413  ? 1.9604 1.3755 1.4666 0.2072  0.0386  0.1870  413  VAL A O   
3138  C CB  . VAL A 413  ? 1.9284 1.3367 1.5449 0.1875  0.1279  0.2107  413  VAL A CB  
3139  C CG1 . VAL A 413  ? 1.9396 1.2524 1.4905 0.1772  0.0945  0.1705  413  VAL A CG1 
3140  C CG2 . VAL A 413  ? 1.8820 1.3030 1.5630 0.1989  0.1823  0.2279  413  VAL A CG2 
3141  N N   . ASP A 414  ? 2.5592 2.0889 2.1495 0.1850  0.0731  0.2400  414  ASP A N   
3142  C CA  . ASP A 414  ? 2.6379 2.1826 2.1832 0.1621  0.0265  0.2378  414  ASP A CA  
3143  C C   . ASP A 414  ? 2.5904 2.2068 2.1507 0.1958  0.0277  0.2585  414  ASP A C   
3144  O O   . ASP A 414  ? 2.6396 2.2637 2.1553 0.1876  -0.0126 0.2536  414  ASP A O   
3145  C CB  . ASP A 414  ? 2.7432 2.3213 2.3085 0.1189  0.0241  0.2550  414  ASP A CB  
3146  C CG  . ASP A 414  ? 2.7626 2.4221 2.4114 0.1334  0.0740  0.2924  414  ASP A CG  
3147  O OD1 . ASP A 414  ? 2.7341 2.3777 2.4217 0.1427  0.1138  0.2952  414  ASP A OD1 
3148  O OD2 . ASP A 414  ? 2.7973 2.5352 2.4716 0.1356  0.0726  0.3188  414  ASP A OD2 
3149  N N   . ASP A 415  ? 2.2893 1.9555 1.9107 0.2333  0.0740  0.2819  415  ASP A N   
3150  C CA  . ASP A 415  ? 2.2736 2.0212 1.9246 0.2632  0.0842  0.3099  415  ASP A CA  
3151  C C   . ASP A 415  ? 2.1323 1.8729 1.7719 0.3090  0.0913  0.3026  415  ASP A C   
3152  O O   . ASP A 415  ? 2.1141 1.8906 1.7361 0.3269  0.0737  0.3093  415  ASP A O   
3153  C CB  . ASP A 415  ? 2.3417 2.1576 2.0728 0.2735  0.1332  0.3457  415  ASP A CB  
3154  C CG  . ASP A 415  ? 2.4395 2.3442 2.2013 0.2955  0.1390  0.3774  415  ASP A CG  
3155  O OD1 . ASP A 415  ? 2.5072 2.4183 2.2291 0.3076  0.1090  0.3712  415  ASP A OD1 
3156  O OD2 . ASP A 415  ? 2.4409 2.4078 2.2653 0.3012  0.1734  0.4083  415  ASP A OD2 
3157  N N   . GLY A 416  ? 1.8638 1.5594 1.5144 0.3275  0.1179  0.2894  416  GLY A N   
3158  C CA  . GLY A 416  ? 1.8132 1.5045 1.4607 0.3711  0.1312  0.2837  416  GLY A CA  
3159  C C   . GLY A 416  ? 1.8242 1.5936 1.5367 0.4033  0.1743  0.3206  416  GLY A C   
3160  O O   . GLY A 416  ? 1.8285 1.6110 1.5501 0.4418  0.1928  0.3243  416  GLY A O   
3161  N N   . VAL A 417  ? 1.8045 1.6262 1.5617 0.3869  0.1902  0.3481  417  VAL A N   
3162  C CA  . VAL A 417  ? 1.7833 1.6814 1.6031 0.4149  0.2296  0.3852  417  VAL A CA  
3163  C C   . VAL A 417  ? 1.7226 1.6169 1.5989 0.4238  0.2799  0.3974  417  VAL A C   
3164  O O   . VAL A 417  ? 1.7220 1.5917 1.6100 0.3949  0.2864  0.3934  417  VAL A O   
3165  C CB  . VAL A 417  ? 1.8782 1.8450 1.7182 0.3955  0.2188  0.4112  417  VAL A CB  
3166  C CG1 . VAL A 417  ? 1.8635 1.9030 1.7758 0.4205  0.2650  0.4499  417  VAL A CG1 
3167  C CG2 . VAL A 417  ? 1.9442 1.9313 1.7371 0.3958  0.1753  0.4074  417  VAL A CG2 
3168  N N   . ALA A 418  ? 1.8016 1.7201 1.7111 0.4638  0.3155  0.4128  418  ALA A N   
3169  C CA  . ALA A 418  ? 1.7808 1.7072 1.7484 0.4771  0.3663  0.4308  418  ALA A CA  
3170  C C   . ALA A 418  ? 1.7638 1.7753 1.7864 0.4929  0.3927  0.4718  418  ALA A C   
3171  O O   . ALA A 418  ? 1.7501 1.7986 1.7955 0.5295  0.4156  0.4908  418  ALA A O   
3172  C CB  . ALA A 418  ? 1.7553 1.6480 1.7242 0.5098  0.3904  0.4210  418  ALA A CB  
3173  N N   . SER A 419  ? 1.6101 1.6528 1.6548 0.4658  0.3906  0.4857  419  SER A N   
3174  C CA  . SER A 419  ? 1.6199 1.7459 1.7165 0.4790  0.4123  0.5240  419  SER A CA  
3175  C C   . SER A 419  ? 1.5181 1.6604 1.6710 0.5103  0.4668  0.5470  419  SER A C   
3176  O O   . SER A 419  ? 1.4924 1.5881 1.6585 0.5048  0.4915  0.5378  419  SER A O   
3177  C CB  . SER A 419  ? 1.6860 1.8361 1.7956 0.4408  0.4008  0.5311  419  SER A CB  
3178  O OG  . SER A 419  ? 1.7525 1.8527 1.8062 0.4035  0.3567  0.5007  419  SER A OG  
3179  N N   . PHE A 420  ? 1.5235 1.7301 1.7077 0.5425  0.4848  0.5770  420  PHE A N   
3180  C CA  . PHE A 420  ? 1.5477 1.7765 1.7866 0.5720  0.5359  0.6031  420  PHE A CA  
3181  C C   . PHE A 420  ? 1.3721 1.6847 1.6564 0.5811  0.5482  0.6399  420  PHE A C   
3182  O O   . PHE A 420  ? 1.4922 1.8474 1.7646 0.5663  0.5163  0.6450  420  PHE A O   
3183  C CB  . PHE A 420  ? 1.5291 1.7557 1.7625 0.6110  0.5501  0.6067  420  PHE A CB  
3184  C CG  . PHE A 420  ? 1.3455 1.4986 1.5504 0.6130  0.5525  0.5777  420  PHE A CG  
3185  C CD1 . PHE A 420  ? 1.3144 1.4420 1.5489 0.6321  0.5950  0.5832  420  PHE A CD1 
3186  C CD2 . PHE A 420  ? 1.4013 1.5115 1.5494 0.5979  0.5122  0.5453  420  PHE A CD2 
3187  C CE1 . PHE A 420  ? 1.3183 1.3819 1.5288 0.6349  0.5976  0.5573  420  PHE A CE1 
3188  C CE2 . PHE A 420  ? 1.4386 1.4834 1.5618 0.6023  0.5145  0.5184  420  PHE A CE2 
3189  C CZ  . PHE A 420  ? 1.3772 1.4001 1.5327 0.6205  0.5572  0.5245  420  PHE A CZ  
3190  N N   . VAL A 421  ? 1.7138 2.0498 2.0489 0.6064  0.5937  0.6658  421  VAL A N   
3191  C CA  . VAL A 421  ? 1.6547 2.0723 2.0344 0.6254  0.6091  0.7032  421  VAL A CA  
3192  C C   . VAL A 421  ? 1.6161 2.0358 2.0374 0.6614  0.6598  0.7249  421  VAL A C   
3193  O O   . VAL A 421  ? 1.5981 1.9738 2.0354 0.6567  0.6881  0.7186  421  VAL A O   
3194  C CB  . VAL A 421  ? 1.6120 2.0677 2.0195 0.5963  0.6053  0.7136  421  VAL A CB  
3195  C CG1 . VAL A 421  ? 1.5758 2.0865 2.0455 0.6207  0.6471  0.7497  421  VAL A CG1 
3196  C CG2 . VAL A 421  ? 1.6370 2.1375 2.0208 0.5747  0.5589  0.7131  421  VAL A CG2 
3197  N N   . LEU A 422  ? 1.2129 1.6783 1.6469 0.6969  0.6698  0.7491  422  LEU A N   
3198  C CA  . LEU A 422  ? 1.1918 1.6754 1.6699 0.7322  0.7168  0.7776  422  LEU A CA  
3199  C C   . LEU A 422  ? 1.2682 1.8361 1.7855 0.7443  0.7209  0.8125  422  LEU A C   
3200  O O   . LEU A 422  ? 1.3063 1.9229 1.8100 0.7431  0.6895  0.8191  422  LEU A O   
3201  C CB  . LEU A 422  ? 1.1811 1.6454 1.6435 0.7655  0.7296  0.7787  422  LEU A CB  
3202  C CG  . LEU A 422  ? 1.1122 1.5444 1.5196 0.7625  0.6966  0.7517  422  LEU A CG  
3203  C CD1 . LEU A 422  ? 1.1692 1.6601 1.5599 0.7670  0.6632  0.7624  422  LEU A CD1 
3204  C CD2 . LEU A 422  ? 1.0987 1.4933 1.4970 0.7905  0.7207  0.7478  422  LEU A CD2 
3205  N N   . ASN A 423  ? 2.0701 2.6542 2.6351 0.7547  0.7585  0.8339  423  ASN A N   
3206  C CA  . ASN A 423  ? 2.0924 2.7560 2.6997 0.7679  0.7664  0.8674  423  ASN A CA  
3207  C C   . ASN A 423  ? 2.0887 2.7746 2.7119 0.8130  0.7923  0.8939  423  ASN A C   
3208  O O   . ASN A 423  ? 2.0396 2.6803 2.6683 0.8313  0.8257  0.8940  423  ASN A O   
3209  C CB  . ASN A 423  ? 2.0584 2.7232 2.7067 0.7571  0.7950  0.8751  423  ASN A CB  
3210  C CG  . ASN A 423  ? 2.0300 2.6265 2.6555 0.7196  0.7880  0.8419  423  ASN A CG  
3211  O OD1 . ASN A 423  ? 2.0646 2.6717 2.6834 0.6847  0.7630  0.8305  423  ASN A OD1 
3212  N ND2 . ASN A 423  ? 1.9771 2.5023 2.5889 0.7257  0.8089  0.8261  423  ASN A ND2 
3213  N N   . LEU A 424  ? 1.2836 2.0361 1.9116 0.8303  0.7765  0.9160  424  LEU A N   
3214  C CA  . LEU A 424  ? 1.3173 2.0847 1.9491 0.8720  0.7954  0.9380  424  LEU A CA  
3215  C C   . LEU A 424  ? 1.3567 2.1872 2.0359 0.9041  0.8215  0.9781  424  LEU A C   
3216  O O   . LEU A 424  ? 1.3788 2.2768 2.0773 0.9008  0.8043  0.9947  424  LEU A O   
3217  C CB  . LEU A 424  ? 1.3440 2.1206 1.9311 0.8753  0.7594  0.9292  424  LEU A CB  
3218  C CG  . LEU A 424  ? 1.3241 2.0243 1.8649 0.8631  0.7502  0.8940  424  LEU A CG  
3219  C CD1 . LEU A 424  ? 1.3831 2.0860 1.8793 0.8753  0.7233  0.8867  424  LEU A CD1 
3220  C CD2 . LEU A 424  ? 1.2817 1.9273 1.8381 0.8786  0.7945  0.8933  424  LEU A CD2 
3221  N N   . PRO A 425  ? 1.6190 2.4266 2.3152 0.9359  0.8622  0.9936  425  PRO A N   
3222  C CA  . PRO A 425  ? 1.6825 2.5365 2.4215 0.9712  0.8930  1.0315  425  PRO A CA  
3223  C C   . PRO A 425  ? 1.8034 2.7290 2.5417 0.9906  0.8707  1.0548  425  PRO A C   
3224  O O   . PRO A 425  ? 1.8860 2.8079 2.6094 1.0184  0.8779  1.0659  425  PRO A O   
3225  C CB  . PRO A 425  ? 1.6595 2.4594 2.3936 0.9981  0.9297  1.0354  425  PRO A CB  
3226  C CG  . PRO A 425  ? 1.6012 2.3249 2.3058 0.9719  0.9273  0.9996  425  PRO A CG  
3227  C CD  . PRO A 425  ? 1.5687 2.2990 2.2402 0.9387  0.8799  0.9737  425  PRO A CD  
3228  N N   . SER A 426  ? 2.0071 2.9961 2.7615 0.9760  0.8452  1.0627  426  SER A N   
3229  C CA  . SER A 426  ? 2.1049 3.1649 2.8565 0.9884  0.8171  1.0823  426  SER A CA  
3230  C C   . SER A 426  ? 2.2404 3.3036 2.9715 1.0238  0.8209  1.0977  426  SER A C   
3231  O O   . SER A 426  ? 2.2527 3.3407 2.9528 1.0220  0.7867  1.0952  426  SER A O   
3232  C CB  . SER A 426  ? 2.1629 3.2997 2.9659 0.9963  0.8230  1.1115  426  SER A CB  
3233  O OG  . SER A 426  ? 2.1516 3.2832 2.9945 1.0247  0.8693  1.1330  426  SER A OG  
3234  N N   . GLY A 427  ? 1.5247 2.5623 2.2716 1.0554  0.8622  1.1139  427  GLY A N   
3235  C CA  . GLY A 427  ? 1.5748 2.6066 2.3017 1.0881  0.8711  1.1280  427  GLY A CA  
3236  C C   . GLY A 427  ? 1.5426 2.5172 2.2176 1.0779  0.8574  1.0991  427  GLY A C   
3237  O O   . GLY A 427  ? 1.5649 2.5247 2.2199 1.1027  0.8680  1.1069  427  GLY A O   
3238  N N   . VAL A 428  ? 1.5463 2.4878 2.1983 1.0413  0.8339  1.0653  428  VAL A N   
3239  C CA  . VAL A 428  ? 1.4999 2.3926 2.1013 1.0309  0.8157  1.0363  428  VAL A CA  
3240  C C   . VAL A 428  ? 1.5266 2.4643 2.0987 1.0395  0.7813  1.0433  428  VAL A C   
3241  O O   . VAL A 428  ? 1.5617 2.5647 2.1554 1.0512  0.7730  1.0697  428  VAL A O   
3242  C CB  . VAL A 428  ? 1.4489 2.2978 2.0298 0.9897  0.7941  0.9987  428  VAL A CB  
3243  C CG1 . VAL A 428  ? 1.4771 2.3718 2.0481 0.9635  0.7496  0.9927  428  VAL A CG1 
3244  C CG2 . VAL A 428  ? 1.4328 2.2171 1.9678 0.9852  0.7886  0.9690  428  VAL A CG2 
3245  N N   . THR A 429  ? 1.0707 1.9741 1.5934 1.0332  0.7602  1.0190  429  THR A N   
3246  C CA  . THR A 429  ? 1.0957 2.0266 1.5865 1.0525  0.7409  1.0279  429  THR A CA  
3247  C C   . THR A 429  ? 1.1346 2.0352 1.5698 1.0314  0.7031  0.9935  429  THR A C   
3248  O O   . THR A 429  ? 1.2086 2.1352 1.6217 1.0115  0.6619  0.9841  429  THR A O   
3249  C CB  . THR A 429  ? 1.1823 2.0900 1.6734 1.0878  0.7789  1.0433  429  THR A CB  
3250  O OG1 . THR A 429  ? 1.1675 2.0051 1.6353 1.0790  0.7906  1.0145  429  THR A OG1 
3251  C CG2 . THR A 429  ? 1.1977 2.1212 1.7410 1.1087  0.8197  1.0744  429  THR A CG2 
3252  N N   . VAL A 430  ? 1.7309 2.5748 2.1433 1.0375  0.7192  0.9756  430  VAL A N   
3253  C CA  . VAL A 430  ? 1.6851 2.4846 2.0485 1.0191  0.6928  0.9392  430  VAL A CA  
3254  C C   . VAL A 430  ? 1.6478 2.3858 2.0208 1.0018  0.7127  0.9163  430  VAL A C   
3255  O O   . VAL A 430  ? 1.6154 2.3369 2.0218 1.0154  0.7532  0.9297  430  VAL A O   
3256  C CB  . VAL A 430  ? 1.6576 2.4431 1.9908 1.0449  0.7012  0.9394  430  VAL A CB  
3257  C CG1 . VAL A 430  ? 1.6377 2.3797 1.9170 1.0287  0.6719  0.9009  430  VAL A CG1 
3258  C CG2 . VAL A 430  ? 1.7225 2.5677 2.0530 1.0674  0.6912  0.9682  430  VAL A CG2 
3259  N N   . LEU A 431  ? 1.6486 2.3495 1.9893 0.9721  0.6833  0.8813  431  LEU A N   
3260  C CA  . LEU A 431  ? 1.5297 2.1717 1.8763 0.9517  0.6964  0.8571  431  LEU A CA  
3261  C C   . LEU A 431  ? 1.5427 2.1368 1.8383 0.9453  0.6760  0.8232  431  LEU A C   
3262  O O   . LEU A 431  ? 1.4452 2.0407 1.7023 0.9282  0.6348  0.8039  431  LEU A O   
3263  C CB  . LEU A 431  ? 1.4379 2.0866 1.7956 0.9174  0.6752  0.8480  431  LEU A CB  
3264  C CG  . LEU A 431  ? 1.3483 1.9444 1.7249 0.8983  0.6965  0.8318  431  LEU A CG  
3265  C CD1 . LEU A 431  ? 1.3025 1.8858 1.6686 0.8572  0.6652  0.8092  431  LEU A CD1 
3266  C CD2 . LEU A 431  ? 1.3269 1.8599 1.6787 0.9054  0.7097  0.8089  431  LEU A CD2 
3267  N N   . GLU A 432  ? 2.2106 2.7634 2.5052 0.9599  0.7046  0.8163  432  GLU A N   
3268  C CA  . GLU A 432  ? 2.2226 2.7244 2.4735 0.9520  0.6883  0.7809  432  GLU A CA  
3269  C C   . GLU A 432  ? 2.1813 2.6250 2.4406 0.9257  0.6953  0.7557  432  GLU A C   
3270  O O   . GLU A 432  ? 2.1759 2.6102 2.4761 0.9265  0.7292  0.7691  432  GLU A O   
3271  C CB  . GLU A 432  ? 2.2474 2.7411 2.4891 0.9829  0.7129  0.7869  432  GLU A CB  
3272  C CG  . GLU A 432  ? 2.3624 2.9133 2.6082 1.0121  0.7189  0.8201  432  GLU A CG  
3273  C CD  . GLU A 432  ? 2.4616 3.0236 2.6565 1.0210  0.6881  0.8082  432  GLU A CD  
3274  O OE1 . GLU A 432  ? 2.4182 2.9489 2.5742 1.0022  0.6564  0.7745  432  GLU A OE1 
3275  O OE2 . GLU A 432  ? 2.5551 3.1556 2.7473 1.0475  0.6957  0.8326  432  GLU A OE2 
3276  N N   . PHE A 433  ? 1.3449 1.7480 1.5643 0.9027  0.6630  0.7195  433  PHE A N   
3277  C CA  . PHE A 433  ? 1.2700 1.6150 1.4925 0.8775  0.6667  0.6940  433  PHE A CA  
3278  C C   . PHE A 433  ? 1.1782 1.4699 1.3513 0.8672  0.6407  0.6540  433  PHE A C   
3279  O O   . PHE A 433  ? 1.2510 1.5521 1.3823 0.8680  0.6065  0.6416  433  PHE A O   
3280  C CB  . PHE A 433  ? 1.2069 1.5626 1.4486 0.8479  0.6543  0.6967  433  PHE A CB  
3281  C CG  . PHE A 433  ? 1.2478 1.6317 1.4589 0.8286  0.6069  0.6895  433  PHE A CG  
3282  C CD1 . PHE A 433  ? 1.2493 1.6866 1.4876 0.8199  0.6014  0.7133  433  PHE A CD1 
3283  C CD2 . PHE A 433  ? 1.3916 1.7465 1.5477 0.8172  0.5678  0.6585  433  PHE A CD2 
3284  C CE1 . PHE A 433  ? 1.2797 1.7426 1.4917 0.7993  0.5582  0.7073  433  PHE A CE1 
3285  C CE2 . PHE A 433  ? 1.2672 1.6441 1.3943 0.7974  0.5244  0.6524  433  PHE A CE2 
3286  C CZ  . PHE A 433  ? 1.2828 1.7138 1.4382 0.7875  0.5196  0.6770  433  PHE A CZ  
3287  N N   . ASN A 434  ? 1.7076 1.9433 1.8851 0.8592  0.6574  0.6342  434  ASN A N   
3288  C CA  . ASN A 434  ? 1.6919 1.8736 1.8255 0.8482  0.6330  0.5949  434  ASN A CA  
3289  C C   . ASN A 434  ? 1.7151 1.8475 1.8390 0.8119  0.6137  0.5679  434  ASN A C   
3290  O O   . ASN A 434  ? 1.7024 1.8082 1.8571 0.8010  0.6386  0.5694  434  ASN A O   
3291  C CB  . ASN A 434  ? 1.6492 1.8025 1.7867 0.8695  0.6626  0.5888  434  ASN A CB  
3292  C CG  . ASN A 434  ? 1.6399 1.8386 1.7886 0.9039  0.6855  0.6168  434  ASN A CG  
3293  O OD1 . ASN A 434  ? 1.6468 1.8566 1.7619 0.9194  0.6697  0.6090  434  ASN A OD1 
3294  N ND2 . ASN A 434  ? 1.6403 1.8657 1.8343 0.9163  0.7220  0.6500  434  ASN A ND2 
3295  N N   . VAL A 435  ? 1.2699 1.3873 1.3480 0.7931  0.5689  0.5428  435  VAL A N   
3296  C CA  . VAL A 435  ? 1.2645 1.3272 1.3229 0.7596  0.5466  0.5128  435  VAL A CA  
3297  C C   . VAL A 435  ? 1.2455 1.2500 1.2731 0.7637  0.5414  0.4796  435  VAL A C   
3298  O O   . VAL A 435  ? 1.2387 1.2517 1.2527 0.7900  0.5462  0.4780  435  VAL A O   
3299  C CB  . VAL A 435  ? 1.3799 1.4519 1.4001 0.7367  0.4989  0.5017  435  VAL A CB  
3300  C CG1 . VAL A 435  ? 1.3665 1.3737 1.3486 0.7065  0.4684  0.4642  435  VAL A CG1 
3301  C CG2 . VAL A 435  ? 1.3800 1.5024 1.4354 0.7247  0.5040  0.5308  435  VAL A CG2 
3302  N N   . LYS A 436  ? 1.9720 1.9187 1.9891 0.7382  0.5321  0.4535  436  LYS A N   
3303  C CA  . LYS A 436  ? 1.9203 1.8094 1.9067 0.7399  0.5231  0.4196  436  LYS A CA  
3304  C C   . LYS A 436  ? 1.9516 1.7800 1.9300 0.7068  0.5116  0.3951  436  LYS A C   
3305  O O   . LYS A 436  ? 1.9445 1.7710 1.9578 0.6908  0.5318  0.4086  436  LYS A O   
3306  C CB  . LYS A 436  ? 1.8520 1.7410 1.8651 0.7691  0.5634  0.4277  436  LYS A CB  
3307  C CG  . LYS A 436  ? 1.7882 1.6652 1.8517 0.7668  0.6066  0.4436  436  LYS A CG  
3308  C CD  . LYS A 436  ? 2.0024 1.8194 2.0602 0.7646  0.6152  0.4168  436  LYS A CD  
3309  C CE  . LYS A 436  ? 2.0597 1.8791 2.1635 0.7814  0.6649  0.4371  436  LYS A CE  
3310  N NZ  . LYS A 436  ? 2.0547 1.9171 2.1647 0.8154  0.6830  0.4552  436  LYS A NZ  
3311  N N   . THR A 437  ? 1.7007 1.4785 1.6314 0.6967  0.4785  0.3590  437  THR A N   
3312  C CA  . THR A 437  ? 1.7713 1.4856 1.6913 0.6675  0.4682  0.3340  437  THR A CA  
3313  C C   . THR A 437  ? 1.6892 1.3752 1.6417 0.6784  0.5067  0.3329  437  THR A C   
3314  O O   . THR A 437  ? 1.6058 1.3071 1.5685 0.7080  0.5275  0.3379  437  THR A O   
3315  C CB  . THR A 437  ? 1.6539 1.3204 1.5121 0.6576  0.4225  0.2957  437  THR A CB  
3316  O OG1 . THR A 437  ? 1.6502 1.3211 1.4921 0.6894  0.4241  0.2861  437  THR A OG1 
3317  C CG2 . THR A 437  ? 1.6852 1.3703 1.5081 0.6395  0.3815  0.2951  437  THR A CG2 
3318  N N   . ASP A 438  ? 1.8218 1.4676 1.7902 0.6539  0.5166  0.3272  438  ASP A N   
3319  C CA  . ASP A 438  ? 1.9017 1.5083 1.8930 0.6588  0.5467  0.3202  438  ASP A CA  
3320  C C   . ASP A 438  ? 1.8794 1.4141 1.8381 0.6323  0.5209  0.2847  438  ASP A C   
3321  O O   . ASP A 438  ? 1.8280 1.3236 1.8059 0.6183  0.5394  0.2805  438  ASP A O   
3322  C CB  . ASP A 438  ? 1.9711 1.5967 2.0183 0.6592  0.5917  0.3509  438  ASP A CB  
3323  C CG  . ASP A 438  ? 2.0431 1.6720 2.1218 0.6864  0.6321  0.3618  438  ASP A CG  
3324  O OD1 . ASP A 438  ? 2.0607 1.6607 2.1193 0.6969  0.6253  0.3390  438  ASP A OD1 
3325  O OD2 . ASP A 438  ? 2.0696 1.7302 2.1922 0.6974  0.6699  0.3932  438  ASP A OD2 
3326  N N   . ALA A 439  ? 2.3906 1.9066 2.2968 0.6259  0.4766  0.2590  439  ALA A N   
3327  C CA  . ALA A 439  ? 2.4279 1.8731 2.2958 0.6070  0.4486  0.2220  439  ALA A CA  
3328  C C   . ALA A 439  ? 2.4305 1.8459 2.3277 0.6163  0.4819  0.2180  439  ALA A C   
3329  O O   . ALA A 439  ? 2.4495 1.8952 2.3760 0.6446  0.5129  0.2329  439  ALA A O   
3330  C CB  . ALA A 439  ? 2.4567 1.8894 2.2711 0.6187  0.4099  0.1953  439  ALA A CB  
3331  N N   . PRO A 440  ? 2.0228 1.3783 1.9126 0.5912  0.4762  0.1990  440  PRO A N   
3332  C CA  . PRO A 440  ? 1.9431 1.2719 1.8665 0.5962  0.5112  0.1997  440  PRO A CA  
3333  C C   . PRO A 440  ? 1.8994 1.1949 1.7987 0.6119  0.4986  0.1706  440  PRO A C   
3334  O O   . PRO A 440  ? 1.8801 1.1736 1.8073 0.6255  0.5288  0.1746  440  PRO A O   
3335  C CB  . PRO A 440  ? 1.9312 1.2074 1.8503 0.5600  0.5051  0.1895  440  PRO A CB  
3336  C CG  . PRO A 440  ? 2.0469 1.3195 1.9240 0.5354  0.4619  0.1798  440  PRO A CG  
3337  C CD  . PRO A 440  ? 2.0618 1.3686 1.9102 0.5571  0.4374  0.1756  440  PRO A CD  
3338  N N   . ASP A 441  ? 2.1163 1.3880 1.9624 0.6074  0.4537  0.1425  441  ASP A N   
3339  C CA  . ASP A 441  ? 2.1492 1.3858 1.9643 0.6217  0.4341  0.1104  441  ASP A CA  
3340  C C   . ASP A 441  ? 2.1176 1.4002 1.9279 0.6593  0.4364  0.1124  441  ASP A C   
3341  O O   . ASP A 441  ? 2.1087 1.3710 1.9045 0.6763  0.4299  0.0895  441  ASP A O   
3342  C CB  . ASP A 441  ? 2.2914 1.4691 2.0478 0.5980  0.3839  0.0761  441  ASP A CB  
3343  C CG  . ASP A 441  ? 2.4062 1.6008 2.1361 0.5786  0.3561  0.0835  441  ASP A CG  
3344  O OD1 . ASP A 441  ? 2.4902 1.6529 2.1648 0.5693  0.3116  0.0579  441  ASP A OD1 
3345  O OD2 . ASP A 441  ? 2.3903 1.6296 2.1535 0.5726  0.3778  0.1148  441  ASP A OD2 
3346  N N   . LEU A 442  ? 1.4438 0.7889 1.2661 0.6731  0.4457  0.1394  442  LEU A N   
3347  C CA  . LEU A 442  ? 1.4015 0.7860 1.2103 0.7058  0.4421  0.1390  442  LEU A CA  
3348  C C   . LEU A 442  ? 1.4215 0.8434 1.2765 0.7331  0.4875  0.1597  442  LEU A C   
3349  O O   . LEU A 442  ? 1.4245 0.8611 1.3253 0.7294  0.5239  0.1852  442  LEU A O   
3350  C CB  . LEU A 442  ? 1.5309 0.9593 1.3209 0.7061  0.4231  0.1544  442  LEU A CB  
3351  C CG  . LEU A 442  ? 1.4816 0.8658 1.2183 0.6781  0.3737  0.1291  442  LEU A CG  
3352  C CD1 . LEU A 442  ? 1.4856 0.9076 1.2021 0.6704  0.3509  0.1438  442  LEU A CD1 
3353  C CD2 . LEU A 442  ? 1.5736 0.9083 1.2592 0.6856  0.3395  0.0885  442  LEU A CD2 
3354  N N   . PRO A 443  ? 3.7476 3.1824 3.5895 0.7606  0.4858  0.1477  443  PRO A N   
3355  C CA  . PRO A 443  ? 3.7781 3.2575 3.6650 0.7837  0.5307  0.1742  443  PRO A CA  
3356  C C   . PRO A 443  ? 3.8829 3.4158 3.7942 0.7862  0.5485  0.2117  443  PRO A C   
3357  O O   . PRO A 443  ? 3.9138 3.4628 3.7968 0.7805  0.5206  0.2132  443  PRO A O   
3358  C CB  . PRO A 443  ? 3.7268 3.2270 3.5877 0.8132  0.5202  0.1597  443  PRO A CB  
3359  C CG  . PRO A 443  ? 3.7131 3.1578 3.5262 0.8047  0.4780  0.1179  443  PRO A CG  
3360  C CD  . PRO A 443  ? 3.7152 3.1232 3.5087 0.7716  0.4509  0.1120  443  PRO A CD  
3361  N N   . GLU A 444  ? 2.3038 1.8617 2.2651 0.7926  0.5926  0.2416  444  GLU A N   
3362  C CA  . GLU A 444  ? 2.3530 1.9681 2.3368 0.8020  0.6112  0.2781  444  GLU A CA  
3363  C C   . GLU A 444  ? 2.2587 1.9105 2.2085 0.8245  0.5896  0.2742  444  GLU A C   
3364  O O   . GLU A 444  ? 2.1975 1.8689 2.1231 0.8190  0.5635  0.2781  444  GLU A O   
3365  C CB  . GLU A 444  ? 2.5320 2.1708 2.5611 0.8108  0.6597  0.3085  444  GLU A CB  
3366  C CG  . GLU A 444  ? 2.6924 2.3704 2.7598 0.8155  0.6851  0.3451  444  GLU A CG  
3367  C CD  . GLU A 444  ? 2.8413 2.5784 2.8972 0.8351  0.6771  0.3639  444  GLU A CD  
3368  O OE1 . GLU A 444  ? 2.8836 2.6335 2.9101 0.8535  0.6613  0.3503  444  GLU A OE1 
3369  O OE2 . GLU A 444  ? 2.8818 2.6533 2.9578 0.8327  0.6867  0.3925  444  GLU A OE2 
3370  N N   . GLU A 445  ? 2.1572 1.8164 2.1030 0.8489  0.5992  0.2648  445  GLU A N   
3371  C CA  . GLU A 445  ? 2.1747 1.8660 2.0860 0.8724  0.5805  0.2587  445  GLU A CA  
3372  C C   . GLU A 445  ? 2.1004 1.7877 1.9673 0.8595  0.5360  0.2476  445  GLU A C   
3373  O O   . GLU A 445  ? 2.1120 1.8428 1.9706 0.8682  0.5302  0.2664  445  GLU A O   
3374  C CB  . GLU A 445  ? 2.2528 1.9189 2.1408 0.8864  0.5703  0.2261  445  GLU A CB  
3375  C CG  . GLU A 445  ? 2.3681 2.0595 2.2826 0.9051  0.6069  0.2391  445  GLU A CG  
3376  C CD  . GLU A 445  ? 2.4768 2.1519 2.3580 0.9149  0.5891  0.2080  445  GLU A CD  
3377  O OE1 . GLU A 445  ? 2.4900 2.1234 2.3360 0.9092  0.5523  0.1733  445  GLU A OE1 
3378  O OE2 . GLU A 445  ? 2.5382 2.2410 2.4275 0.9288  0.6112  0.2181  445  GLU A OE2 
3379  N N   . ASN A 446  ? 1.4653 1.0980 1.3030 0.8373  0.5042  0.2171  446  ASN A N   
3380  C CA  . ASN A 446  ? 1.4717 1.0903 1.2552 0.8277  0.4564  0.1971  446  ASN A CA  
3381  C C   . ASN A 446  ? 1.5975 1.2164 1.3809 0.7991  0.4415  0.2100  446  ASN A C   
3382  O O   . ASN A 446  ? 1.5912 1.1783 1.3324 0.7798  0.4013  0.1889  446  ASN A O   
3383  C CB  . ASN A 446  ? 1.4330 0.9910 1.1787 0.8224  0.4276  0.1550  446  ASN A CB  
3384  C CG  . ASN A 446  ? 1.4812 1.0456 1.2289 0.8528  0.4429  0.1424  446  ASN A CG  
3385  O OD1 . ASN A 446  ? 1.4824 1.0136 1.2450 0.8517  0.4546  0.1266  446  ASN A OD1 
3386  N ND2 . ASN A 446  ? 1.5329 1.1431 1.2670 0.8801  0.4441  0.1507  446  ASN A ND2 
3387  N N   . GLN A 447  ? 1.8427 1.4993 1.6734 0.7971  0.4744  0.2453  447  GLN A N   
3388  C CA  . GLN A 447  ? 1.8991 1.5653 1.7376 0.7717  0.4656  0.2616  447  GLN A CA  
3389  C C   . GLN A 447  ? 1.9053 1.6271 1.7305 0.7824  0.4526  0.2813  447  GLN A C   
3390  O O   . GLN A 447  ? 1.8798 1.6524 1.7304 0.8073  0.4799  0.3079  447  GLN A O   
3391  C CB  . GLN A 447  ? 1.9192 1.5982 1.8172 0.7660  0.5093  0.2902  447  GLN A CB  
3392  C CG  . GLN A 447  ? 1.9482 1.5703 1.8609 0.7490  0.5213  0.2735  447  GLN A CG  
3393  C CD  . GLN A 447  ? 1.9719 1.5585 1.8733 0.7125  0.4989  0.2640  447  GLN A CD  
3394  O OE1 . GLN A 447  ? 1.9818 1.5779 1.8535 0.6990  0.4662  0.2615  447  GLN A OE1 
3395  N NE2 . GLN A 447  ? 1.9804 1.5258 1.9045 0.6954  0.5166  0.2593  447  GLN A NE2 
3396  N N   . ALA A 448  ? 1.6536 1.3654 1.4385 0.7624  0.4108  0.2695  448  ALA A N   
3397  C CA  . ALA A 448  ? 1.6845 1.4475 1.4538 0.7689  0.3939  0.2875  448  ALA A CA  
3398  C C   . ALA A 448  ? 1.8175 1.6378 1.6392 0.7713  0.4261  0.3296  448  ALA A C   
3399  O O   . ALA A 448  ? 1.7775 1.5899 1.6331 0.7509  0.4420  0.3404  448  ALA A O   
3400  C CB  . ALA A 448  ? 1.7070 1.4448 1.4271 0.7411  0.3442  0.2683  448  ALA A CB  
3401  N N   . ARG A 449  ? 1.5466 1.4235 1.3726 0.7962  0.4342  0.3528  449  ARG A N   
3402  C CA  . ARG A 449  ? 1.5686 1.5035 1.4409 0.8015  0.4617  0.3937  449  ARG A CA  
3403  C C   . ARG A 449  ? 1.6173 1.6113 1.4765 0.8171  0.4490  0.4149  449  ARG A C   
3404  O O   . ARG A 449  ? 1.6320 1.6257 1.4441 0.8272  0.4202  0.3993  449  ARG A O   
3405  C CB  . ARG A 449  ? 1.5595 1.5051 1.4821 0.8216  0.5130  0.4136  449  ARG A CB  
3406  C CG  . ARG A 449  ? 1.5239 1.4846 1.4390 0.8545  0.5277  0.4139  449  ARG A CG  
3407  C CD  . ARG A 449  ? 1.5721 1.5201 1.5300 0.8637  0.5718  0.4225  449  ARG A CD  
3408  N NE  . ARG A 449  ? 1.5934 1.4888 1.5321 0.8621  0.5663  0.3887  449  ARG A NE  
3409  C CZ  . ARG A 449  ? 1.6230 1.4950 1.5927 0.8654  0.5991  0.3882  449  ARG A CZ  
3410  N NH1 . ARG A 449  ? 1.6391 1.5326 1.6582 0.8700  0.6395  0.4195  449  ARG A NH1 
3411  N NH2 . ARG A 449  ? 1.6081 1.4347 1.5585 0.8642  0.5906  0.3564  449  ARG A NH2 
3412  N N   . GLU A 450  ? 1.6925 1.7365 1.5937 0.8194  0.4709  0.4509  450  GLU A N   
3413  C CA  . GLU A 450  ? 1.7407 1.8444 1.6367 0.8328  0.4614  0.4753  450  GLU A CA  
3414  C C   . GLU A 450  ? 1.7311 1.8826 1.6842 0.8489  0.5040  0.5152  450  GLU A C   
3415  O O   . GLU A 450  ? 1.7155 1.8514 1.7086 0.8500  0.5399  0.5226  450  GLU A O   
3416  C CB  . GLU A 450  ? 1.6080 1.7218 1.4836 0.8041  0.4223  0.4737  450  GLU A CB  
3417  C CG  . GLU A 450  ? 1.7046 1.7755 1.5170 0.7883  0.3747  0.4371  450  GLU A CG  
3418  C CD  . GLU A 450  ? 1.8177 1.9098 1.5878 0.8115  0.3545  0.4340  450  GLU A CD  
3419  O OE1 . GLU A 450  ? 1.8828 2.0333 1.6709 0.8281  0.3653  0.4647  450  GLU A OE1 
3420  O OE2 . GLU A 450  ? 1.8341 1.8848 1.5532 0.8140  0.3286  0.4016  450  GLU A OE2 
3421  N N   . GLY A 451  ? 1.3707 1.5791 1.3258 0.8612  0.4988  0.5411  451  GLY A N   
3422  C CA  . GLY A 451  ? 1.3560 1.6138 1.3618 0.8785  0.5357  0.5809  451  GLY A CA  
3423  C C   . GLY A 451  ? 1.6302 1.9404 1.6232 0.8774  0.5085  0.5981  451  GLY A C   
3424  O O   . GLY A 451  ? 1.3994 1.7026 1.3420 0.8721  0.4695  0.5785  451  GLY A O   
3425  N N   . TYR A 452  ? 1.2537 1.6135 1.2900 0.8812  0.5269  0.6330  452  TYR A N   
3426  C CA  . TYR A 452  ? 1.2951 1.7119 1.3251 0.8813  0.5028  0.6534  452  TYR A CA  
3427  C C   . TYR A 452  ? 1.3327 1.8090 1.4107 0.9052  0.5357  0.6969  452  TYR A C   
3428  O O   . TYR A 452  ? 1.3111 1.7864 1.4114 0.9305  0.5734  0.7104  452  TYR A O   
3429  C CB  . TYR A 452  ? 1.2877 1.7017 1.3093 0.8440  0.4683  0.6426  452  TYR A CB  
3430  C CG  . TYR A 452  ? 1.2859 1.6419 1.2546 0.8204  0.4314  0.6011  452  TYR A CG  
3431  C CD1 . TYR A 452  ? 1.3373 1.6980 1.2558 0.8080  0.3843  0.5876  452  TYR A CD1 
3432  C CD2 . TYR A 452  ? 1.2505 1.5449 1.2176 0.8110  0.4429  0.5755  452  TYR A CD2 
3433  C CE1 . TYR A 452  ? 1.3559 1.6600 1.2233 0.7875  0.3501  0.5495  452  TYR A CE1 
3434  C CE2 . TYR A 452  ? 1.2597 1.4994 1.1776 0.7912  0.4090  0.5376  452  TYR A CE2 
3435  C CZ  . TYR A 452  ? 1.2859 1.5296 1.1536 0.7798  0.3628  0.5247  452  TYR A CZ  
3436  O OH  . TYR A 452  ? 1.2927 1.4774 1.1091 0.7610  0.3289  0.4865  452  TYR A OH  
3437  N N   . ARG A 453  ? 1.5552 2.0829 1.6477 0.8972  0.5204  0.7185  453  ARG A N   
3438  C CA  . ARG A 453  ? 1.5304 2.1171 1.6682 0.9194  0.5478  0.7600  453  ARG A CA  
3439  C C   . ARG A 453  ? 1.5528 2.1924 1.7097 0.9023  0.5267  0.7786  453  ARG A C   
3440  O O   . ARG A 453  ? 1.6080 2.2605 1.7292 0.8864  0.4846  0.7682  453  ARG A O   
3441  C CB  . ARG A 453  ? 1.5902 2.2033 1.7072 0.9531  0.5515  0.7742  453  ARG A CB  
3442  C CG  . ARG A 453  ? 1.6116 2.2756 1.7712 0.9822  0.5852  0.8162  453  ARG A CG  
3443  C CD  . ARG A 453  ? 1.7122 2.4065 1.8427 1.0108  0.5787  0.8293  453  ARG A CD  
3444  N NE  . ARG A 453  ? 1.7467 2.4235 1.8838 1.0390  0.6172  0.8368  453  ARG A NE  
3445  C CZ  . ARG A 453  ? 1.7954 2.4307 1.8979 1.0447  0.6179  0.8117  453  ARG A CZ  
3446  N NH1 . ARG A 453  ? 1.7980 2.4031 1.8547 1.0263  0.5816  0.7770  453  ARG A NH1 
3447  N NH2 . ARG A 453  ? 1.8116 2.4359 1.9244 1.0691  0.6548  0.8214  453  ARG A NH2 
3448  N N   . ALA A 454  ? 1.5315 2.2024 1.7436 0.9053  0.5551  0.8060  454  ALA A N   
3449  C CA  . ALA A 454  ? 1.5202 2.2488 1.7547 0.8917  0.5372  0.8259  454  ALA A CA  
3450  C C   . ALA A 454  ? 1.5831 2.3732 1.8570 0.9231  0.5622  0.8674  454  ALA A C   
3451  O O   . ALA A 454  ? 1.5876 2.3691 1.8846 0.9499  0.6018  0.8821  454  ALA A O   
3452  C CB  . ALA A 454  ? 1.5265 2.2419 1.7909 0.8622  0.5423  0.8195  454  ALA A CB  
3453  N N   . ILE A 455  ? 2.0297 2.8814 2.3121 0.9196  0.5395  0.8871  455  ILE A N   
3454  C CA  . ILE A 455  ? 2.0808 2.9911 2.3943 0.9522  0.5593  0.9261  455  ILE A CA  
3455  C C   . ILE A 455  ? 2.0658 3.0428 2.4167 0.9433  0.5489  0.9507  455  ILE A C   
3456  O O   . ILE A 455  ? 2.0781 3.0714 2.4133 0.9138  0.5110  0.9395  455  ILE A O   
3457  C CB  . ILE A 455  ? 2.0275 2.9527 2.2987 0.9730  0.5402  0.9295  455  ILE A CB  
3458  C CG1 . ILE A 455  ? 2.0186 2.8913 2.2659 0.9931  0.5633  0.9159  455  ILE A CG1 
3459  C CG2 . ILE A 455  ? 2.0798 3.0737 2.3789 1.0003  0.5489  0.9697  455  ILE A CG2 
3460  C CD1 . ILE A 455  ? 2.1225 3.0007 2.3183 1.0099  0.5411  0.9118  455  ILE A CD1 
3461  N N   . ALA A 456  ? 1.2957 2.3122 1.6952 0.9697  0.5825  0.9850  456  ALA A N   
3462  C CA  . ALA A 456  ? 1.2804 2.3630 1.7247 0.9648  0.5794  1.0105  456  ALA A CA  
3463  C C   . ALA A 456  ? 1.3802 2.5300 1.8131 0.9689  0.5441  1.0286  456  ALA A C   
3464  O O   . ALA A 456  ? 1.4214 2.5973 1.8496 1.0010  0.5505  1.0504  456  ALA A O   
3465  C CB  . ALA A 456  ? 1.2510 2.3497 1.7500 0.9929  0.6273  1.0400  456  ALA A CB  
3466  N N   . TYR A 457  ? 1.2807 2.4566 1.7084 0.9351  0.5070  1.0194  457  TYR A N   
3467  C CA  . TYR A 457  ? 1.3799 2.6264 1.8060 0.9329  0.4728  1.0381  457  TYR A CA  
3468  C C   . TYR A 457  ? 1.4129 2.7204 1.8925 0.9667  0.5018  1.0793  457  TYR A C   
3469  O O   . TYR A 457  ? 1.3669 2.7186 1.8960 0.9601  0.5107  1.0959  457  TYR A O   
3470  C CB  . TYR A 457  ? 1.4312 2.6985 1.8613 0.8889  0.4395  1.0259  457  TYR A CB  
3471  C CG  . TYR A 457  ? 1.3212 2.6705 1.7640 0.8822  0.4074  1.0483  457  TYR A CG  
3472  C CD1 . TYR A 457  ? 1.3731 2.7398 1.8051 0.8394  0.3679  1.0348  457  TYR A CD1 
3473  C CD2 . TYR A 457  ? 1.3969 2.8056 1.8615 0.9174  0.4155  1.0831  457  TYR A CD2 
3474  C CE1 . TYR A 457  ? 1.4418 2.8857 1.8864 0.8318  0.3378  1.0557  457  TYR A CE1 
3475  C CE2 . TYR A 457  ? 1.4700 2.9553 1.9471 0.9117  0.3853  1.1040  457  TYR A CE2 
3476  C CZ  . TYR A 457  ? 1.4788 2.9830 1.9470 0.8688  0.3466  1.0904  457  TYR A CZ  
3477  O OH  . TYR A 457  ? 1.5313 3.1147 2.0134 0.8636  0.3168  1.1126  457  TYR A OH  
3478  N N   . SER A 458  ? 1.8838 3.1925 2.3525 1.0038  0.5172  1.0956  458  SER A N   
3479  C CA  . SER A 458  ? 1.9623 3.3228 2.4758 1.0397  0.5447  1.1351  458  SER A CA  
3480  C C   . SER A 458  ? 2.0245 3.4669 2.5545 1.0334  0.5124  1.1561  458  SER A C   
3481  O O   . SER A 458  ? 2.0371 3.4926 2.5277 1.0141  0.4686  1.1445  458  SER A O   
3482  C CB  . SER A 458  ? 2.0301 3.3708 2.5183 1.0772  0.5623  1.1457  458  SER A CB  
3483  O OG  . SER A 458  ? 1.9931 3.2564 2.4514 1.0743  0.5788  1.1181  458  SER A OG  
3484  N N   . SER A 459  ? 1.8643 3.3610 2.4529 1.0488  0.5338  1.1864  459  SER A N   
3485  C CA  . SER A 459  ? 1.9373 3.5188 2.5528 1.0445  0.5079  1.2095  459  SER A CA  
3486  C C   . SER A 459  ? 1.9661 3.5930 2.6447 1.0769  0.5454  1.2451  459  SER A C   
3487  O O   . SER A 459  ? 1.8914 3.5015 2.6077 1.0749  0.5777  1.2440  459  SER A O   
3488  C CB  . SER A 459  ? 1.8962 3.4914 2.5167 0.9972  0.4783  1.1900  459  SER A CB  
3489  O OG  . SER A 459  ? 1.9441 3.6218 2.5832 0.9894  0.4469  1.2099  459  SER A OG  
3490  N N   . LEU A 460  ? 2.2171 3.8998 2.9054 1.1076  0.5410  1.2765  460  LEU A N   
3491  C CA  . LEU A 460  ? 2.3308 4.0491 3.0725 1.1450  0.5782  1.3111  460  LEU A CA  
3492  C C   . LEU A 460  ? 2.3767 4.1515 3.1801 1.1334  0.5844  1.3234  460  LEU A C   
3493  O O   . LEU A 460  ? 2.3757 4.1528 3.2238 1.1560  0.6244  1.3400  460  LEU A O   
3494  C CB  . LEU A 460  ? 2.4887 4.2516 3.2233 1.1815  0.5707  1.3422  460  LEU A CB  
3495  C CG  . LEU A 460  ? 2.5649 4.3182 3.3281 1.2270  0.6183  1.3693  460  LEU A CG  
3496  C CD1 . LEU A 460  ? 2.5557 4.2246 3.2776 1.2378  0.6422  1.3530  460  LEU A CD1 
3497  C CD2 . LEU A 460  ? 2.6958 4.5155 3.4734 1.2626  0.6119  1.4076  460  LEU A CD2 
3498  N N   . SER A 461  ? 2.9921 3.6152 2.8604 1.2618  0.2846  0.7255  461  SER A N   
3499  C CA  . SER A 461  ? 3.0158 3.6940 2.8922 1.2586  0.2616  0.6849  461  SER A CA  
3500  C C   . SER A 461  ? 2.9511 3.5865 2.8723 1.2218  0.2564  0.6846  461  SER A C   
3501  O O   . SER A 461  ? 2.9296 3.6048 2.8637 1.2099  0.2393  0.6509  461  SER A O   
3502  C CB  . SER A 461  ? 2.9978 3.7636 2.8680 1.2398  0.2557  0.6392  461  SER A CB  
3503  O OG  . SER A 461  ? 3.0819 3.9105 2.9100 1.2827  0.2463  0.6231  461  SER A OG  
3504  N N   . GLN A 462  ? 2.1376 2.6921 2.0820 1.2033  0.2715  0.7220  462  GLN A N   
3505  C CA  . GLN A 462  ? 2.0463 2.5525 2.0343 1.1642  0.2687  0.7256  462  GLN A CA  
3506  C C   . GLN A 462  ? 1.8890 2.4382 1.9033 1.1130  0.2650  0.6884  462  GLN A C   
3507  O O   . GLN A 462  ? 1.8442 2.3619 1.8951 1.0738  0.2618  0.6859  462  GLN A O   
3508  C CB  . GLN A 462  ? 2.0913 2.5888 2.0812 1.1854  0.2503  0.7213  462  GLN A CB  
3509  C CG  . GLN A 462  ? 2.1476 2.5686 2.1307 1.2180  0.2551  0.7671  462  GLN A CG  
3510  C CD  . GLN A 462  ? 2.0974 2.4316 2.1157 1.1849  0.2695  0.8027  462  GLN A CD  
3511  O OE1 . GLN A 462  ? 1.9925 2.3221 2.0400 1.1380  0.2767  0.7946  462  GLN A OE1 
3512  N NE2 . GLN A 462  ? 2.1806 2.4450 2.1963 1.2096  0.2730  0.8425  462  GLN A NE2 
3513  N N   . SER A 463  ? 2.8329 3.4532 2.8270 1.1135  0.2649  0.6602  463  SER A N   
3514  C CA  . SER A 463  ? 2.7154 3.3892 2.7280 1.0693  0.2590  0.6202  463  SER A CA  
3515  C C   . SER A 463  ? 2.5868 3.2286 2.6255 1.0251  0.2757  0.6311  463  SER A C   
3516  O O   . SER A 463  ? 2.6233 3.2481 2.6480 1.0367  0.2929  0.6533  463  SER A O   
3517  C CB  . SER A 463  ? 2.7469 3.5122 2.7251 1.0916  0.2507  0.5850  463  SER A CB  
3518  O OG  . SER A 463  ? 2.6943 3.5079 2.6844 1.0510  0.2505  0.5529  463  SER A OG  
3519  N N   . TYR A 464  ? 1.9114 2.5451 1.9877 0.9745  0.2706  0.6152  464  TYR A N   
3520  C CA  . TYR A 464  ? 1.7988 2.4066 1.9030 0.9295  0.2838  0.6211  464  TYR A CA  
3521  C C   . TYR A 464  ? 1.7175 2.3828 1.8372 0.8860  0.2727  0.5776  464  TYR A C   
3522  O O   . TYR A 464  ? 1.7107 2.4424 1.8161 0.8925  0.2565  0.5420  464  TYR A O   
3523  C CB  . TYR A 464  ? 1.7767 2.2942 1.9186 0.9048  0.2910  0.6557  464  TYR A CB  
3524  C CG  . TYR A 464  ? 1.8677 2.3310 1.9968 0.9462  0.2951  0.6932  464  TYR A CG  
3525  C CD1 . TYR A 464  ? 1.9390 2.3985 2.0343 0.9901  0.3078  0.7167  464  TYR A CD1 
3526  C CD2 . TYR A 464  ? 1.8902 2.3068 2.0387 0.9425  0.2857  0.7047  464  TYR A CD2 
3527  C CE1 . TYR A 464  ? 2.0297 2.4392 2.1112 1.0289  0.3107  0.7518  464  TYR A CE1 
3528  C CE2 . TYR A 464  ? 1.9867 2.3528 2.1226 0.9815  0.2886  0.7393  464  TYR A CE2 
3529  C CZ  . TYR A 464  ? 2.0583 2.4207 2.1608 1.0246  0.3009  0.7631  464  TYR A CZ  
3530  O OH  . TYR A 464  ? 2.1376 2.4488 2.2265 1.0631  0.3032  0.7983  464  TYR A OH  
3531  N N   . LEU A 465  ? 1.4734 2.1128 1.6231 0.8413  0.2814  0.5809  465  LEU A N   
3532  C CA  . LEU A 465  ? 1.4392 2.1239 1.6072 0.7946  0.2709  0.5427  465  LEU A CA  
3533  C C   . LEU A 465  ? 1.4015 2.0221 1.6133 0.7456  0.2788  0.5604  465  LEU A C   
3534  O O   . LEU A 465  ? 1.4207 1.9792 1.6422 0.7514  0.2961  0.5979  465  LEU A O   
3535  C CB  . LEU A 465  ? 1.4466 2.2049 1.5889 0.7999  0.2730  0.5152  465  LEU A CB  
3536  C CG  . LEU A 465  ? 1.4246 2.2527 1.5730 0.7639  0.2575  0.4677  465  LEU A CG  
3537  C CD1 . LEU A 465  ? 1.4779 2.3684 1.6019 0.7907  0.2402  0.4395  465  LEU A CD1 
3538  C CD2 . LEU A 465  ? 1.4205 2.2935 1.5566 0.7551  0.2647  0.4509  465  LEU A CD2 
3539  N N   . TYR A 466  ? 1.6050 2.2400 1.8431 0.6978  0.2656  0.5338  466  TYR A N   
3540  C CA  . TYR A 466  ? 1.7111 2.2958 1.9918 0.6452  0.2691  0.5430  466  TYR A CA  
3541  C C   . TYR A 466  ? 1.6687 2.3108 1.9582 0.6030  0.2548  0.5002  466  TYR A C   
3542  O O   . TYR A 466  ? 1.7084 2.3901 1.9923 0.5973  0.2379  0.4726  466  TYR A O   
3543  C CB  . TYR A 466  ? 1.6848 2.1979 1.9952 0.6288  0.2644  0.5659  466  TYR A CB  
3544  C CG  . TYR A 466  ? 1.5889 2.0494 1.9449 0.5727  0.2655  0.5747  466  TYR A CG  
3545  C CD1 . TYR A 466  ? 1.5499 2.0239 1.9192 0.5424  0.2718  0.5649  466  TYR A CD1 
3546  C CD2 . TYR A 466  ? 1.5563 1.9516 1.9421 0.5506  0.2599  0.5935  466  TYR A CD2 
3547  C CE1 . TYR A 466  ? 1.4970 1.9212 1.9095 0.4917  0.2719  0.5735  466  TYR A CE1 
3548  C CE2 . TYR A 466  ? 1.5598 1.9048 1.9878 0.4993  0.2598  0.6026  466  TYR A CE2 
3549  C CZ  . TYR A 466  ? 1.5155 1.8754 1.9574 0.4700  0.2655  0.5925  466  TYR A CZ  
3550  O OH  . TYR A 466  ? 1.5524 1.8628 2.0370 0.4197  0.2643  0.6011  466  TYR A OH  
3551  N N   . ILE A 467  ? 1.5543 2.2005 1.8579 0.5728  0.2616  0.4945  467  ILE A N   
3552  C CA  . ILE A 467  ? 1.4998 2.1899 1.8168 0.5264  0.2476  0.4571  467  ILE A CA  
3553  C C   . ILE A 467  ? 1.4641 2.0936 1.8260 0.4745  0.2500  0.4708  467  ILE A C   
3554  O O   . ILE A 467  ? 1.4507 2.0264 1.8276 0.4771  0.2668  0.5023  467  ILE A O   
3555  C CB  . ILE A 467  ? 1.4676 2.2349 1.7579 0.5340  0.2483  0.4270  467  ILE A CB  
3556  C CG1 . ILE A 467  ? 1.4078 2.1516 1.7112 0.5194  0.2644  0.4403  467  ILE A CG1 
3557  C CG2 . ILE A 467  ? 1.5357 2.3476 1.7819 0.5927  0.2508  0.4249  467  ILE A CG2 
3558  C CD1 . ILE A 467  ? 1.3837 2.2021 1.6670 0.5144  0.2622  0.4061  467  ILE A CD1 
3559  N N   . ASP A 468  ? 1.2670 1.9057 1.6499 0.4279  0.2328  0.4471  468  ASP A N   
3560  C CA  . ASP A 468  ? 1.2240 1.8097 1.6505 0.3729  0.2301  0.4550  468  ASP A CA  
3561  C C   . ASP A 468  ? 1.1973 1.8366 1.6300 0.3262  0.2132  0.4134  468  ASP A C   
3562  O O   . ASP A 468  ? 1.1876 1.9043 1.5918 0.3376  0.2072  0.3807  468  ASP A O   
3563  C CB  . ASP A 468  ? 1.3264 1.8417 1.7773 0.3615  0.2252  0.4797  468  ASP A CB  
3564  C CG  . ASP A 468  ? 1.3677 1.8033 1.8629 0.3243  0.2315  0.5084  468  ASP A CG  
3565  O OD1 . ASP A 468  ? 1.3720 1.7896 1.8769 0.3252  0.2466  0.5234  468  ASP A OD1 
3566  O OD2 . ASP A 468  ? 1.3877 1.7773 1.9085 0.2940  0.2212  0.5161  468  ASP A OD2 
3567  N N   . TRP A 469  ? 2.0772 2.6738 2.5471 0.2737  0.2053  0.4157  469  TRP A N   
3568  C CA  . TRP A 469  ? 2.1614 2.7970 2.6415 0.2232  0.1884  0.3801  469  TRP A CA  
3569  C C   . TRP A 469  ? 2.3021 2.8643 2.8267 0.1732  0.1835  0.3979  469  TRP A C   
3570  O O   . TRP A 469  ? 2.2995 2.7892 2.8456 0.1808  0.1955  0.4359  469  TRP A O   
3571  C CB  . TRP A 469  ? 2.1127 2.8024 2.5810 0.2202  0.1926  0.3583  469  TRP A CB  
3572  C CG  . TRP A 469  ? 2.0565 2.7014 2.5513 0.2045  0.2064  0.3789  469  TRP A CG  
3573  C CD1 . TRP A 469  ? 2.0205 2.6818 2.5309 0.1649  0.2017  0.3599  469  TRP A CD1 
3574  C CD2 . TRP A 469  ? 2.0567 2.6374 2.5641 0.2290  0.2270  0.4202  469  TRP A CD2 
3575  N NE1 . TRP A 469  ? 1.9818 2.5937 2.5151 0.1636  0.2179  0.3859  469  TRP A NE1 
3576  C CE2 . TRP A 469  ? 2.0114 2.5740 2.5435 0.2020  0.2340  0.4230  469  TRP A CE2 
3577  C CE3 . TRP A 469  ? 2.0979 2.6347 2.5989 0.2703  0.2399  0.4548  469  TRP A CE3 
3578  C CZ2 . TRP A 469  ? 2.0108 2.5152 2.5615 0.2154  0.2542  0.4584  469  TRP A CZ2 
3579  C CZ3 . TRP A 469  ? 2.0821 2.5603 2.6005 0.2826  0.2598  0.4909  469  TRP A CZ3 
3580  C CH2 . TRP A 469  ? 2.0373 2.5008 2.5806 0.2553  0.2672  0.4920  469  TRP A CH2 
3581  N N   . THR A 470  ? 2.3132 2.8906 2.8524 0.1217  0.1654  0.3723  470  THR A N   
3582  C CA  . THR A 470  ? 2.4312 2.9384 3.0138 0.0732  0.1612  0.3901  470  THR A CA  
3583  C C   . THR A 470  ? 2.5971 3.1251 3.1968 0.0196  0.1487  0.3645  470  THR A C   
3584  O O   . THR A 470  ? 2.6305 3.2215 3.2136 0.0007  0.1341  0.3277  470  THR A O   
3585  C CB  . THR A 470  ? 2.4046 2.8585 3.0032 0.0574  0.1517  0.4050  470  THR A CB  
3586  O OG1 . THR A 470  ? 2.4232 2.8639 3.0024 0.1097  0.1620  0.4258  470  THR A OG1 
3587  C CG2 . THR A 470  ? 2.3379 2.7053 2.9821 0.0212  0.1532  0.4356  470  THR A CG2 
3588  N N   . ASP A 471  ? 2.0756 2.5480 2.7095 -0.0030 0.1553  0.3860  471  ASP A N   
3589  C CA  . ASP A 471  ? 2.2642 2.7312 2.9252 -0.0579 0.1438  0.3716  471  ASP A CA  
3590  C C   . ASP A 471  ? 2.4101 2.7835 3.1178 -0.0851 0.1463  0.4071  471  ASP A C   
3591  O O   . ASP A 471  ? 2.4064 2.7339 3.1250 -0.0554 0.1650  0.4404  471  ASP A O   
3592  C CB  . ASP A 471  ? 2.3303 2.8415 2.9815 -0.0480 0.1530  0.3571  471  ASP A CB  
3593  C CG  . ASP A 471  ? 2.4135 2.9366 3.0864 -0.1052 0.1379  0.3331  471  ASP A CG  
3594  O OD1 . ASP A 471  ? 2.4633 3.0320 3.1263 -0.1378 0.1183  0.3000  471  ASP A OD1 
3595  O OD2 . ASP A 471  ? 2.4333 2.9284 3.1301 -0.1143 0.1469  0.3446  471  ASP A OD2 
3596  N N   . ASN A 472  ? 4.0217 4.3686 4.7567 -0.1419 0.1274  0.3996  472  ASN A N   
3597  C CA  . ASN A 472  ? 4.0418 4.3018 4.8235 -0.1750 0.1255  0.4297  472  ASN A CA  
3598  C C   . ASN A 472  ? 4.0782 4.3122 4.8918 -0.1923 0.1329  0.4388  472  ASN A C   
3599  O O   . ASN A 472  ? 3.9966 4.1574 4.8493 -0.2084 0.1362  0.4685  472  ASN A O   
3600  C CB  . ASN A 472  ? 3.9849 4.2212 4.7822 -0.2284 0.1013  0.4205  472  ASN A CB  
3601  C CG  . ASN A 472  ? 3.9806 4.2819 4.7630 -0.2658 0.0820  0.3774  472  ASN A CG  
3602  O OD1 . ASN A 472  ? 4.0186 4.3788 4.7839 -0.2567 0.0855  0.3545  472  ASN A OD1 
3603  N ND2 . ASN A 472  ? 3.9337 4.2236 4.7222 -0.3092 0.0614  0.3664  472  ASN A ND2 
3604  N N   . HIS A 473  ? 3.4166 3.7109 4.2138 -0.1881 0.1355  0.4130  473  HIS A N   
3605  C CA  . HIS A 473  ? 3.4814 3.7599 4.3050 -0.2004 0.1436  0.4175  473  HIS A CA  
3606  C C   . HIS A 473  ? 3.3524 3.6402 4.1621 -0.1468 0.1706  0.4330  473  HIS A C   
3607  O O   . HIS A 473  ? 3.3808 3.7226 4.1488 -0.1037 0.1792  0.4226  473  HIS A O   
3608  C CB  . HIS A 473  ? 3.7619 4.0934 4.5818 -0.2386 0.1272  0.3789  473  HIS A CB  
3609  C CG  . HIS A 473  ? 4.0863 4.4578 4.8873 -0.2686 0.1039  0.3492  473  HIS A CG  
3610  N ND1 . HIS A 473  ? 4.2268 4.6673 4.9829 -0.2396 0.1030  0.3264  473  HIS A ND1 
3611  C CD2 . HIS A 473  ? 4.1875 4.5426 5.0077 -0.3253 0.0806  0.3372  473  HIS A CD2 
3612  C CE1 . HIS A 473  ? 4.4320 4.8966 5.1816 -0.2773 0.0812  0.3018  473  HIS A CE1 
3613  N NE2 . HIS A 473  ? 4.3288 4.7423 5.1154 -0.3297 0.0673  0.3080  473  HIS A NE2 
3614  N N   . LYS A 474  ? 3.4768 3.7128 4.3223 -0.1518 0.1831  0.4567  474  LYS A N   
3615  C CA  . LYS A 474  ? 3.3662 3.5917 4.2066 -0.1045 0.2105  0.4799  474  LYS A CA  
3616  C C   . LYS A 474  ? 3.2255 3.5254 4.0298 -0.0774 0.2198  0.4540  474  LYS A C   
3617  O O   . LYS A 474  ? 3.2477 3.5512 4.0379 -0.0345 0.2426  0.4688  474  LYS A O   
3618  C CB  . LYS A 474  ? 3.3203 3.4760 4.2120 -0.1239 0.2197  0.5070  474  LYS A CB  
3619  C CG  . LYS A 474  ? 3.2883 3.4441 4.2107 -0.1768 0.2037  0.4862  474  LYS A CG  
3620  C CD  . LYS A 474  ? 3.2378 3.3305 4.2103 -0.1905 0.2147  0.5113  474  LYS A CD  
3621  C CE  . LYS A 474  ? 3.2990 3.4128 4.2602 -0.1505 0.2413  0.5158  474  LYS A CE  
3622  N NZ  . LYS A 474  ? 3.2397 3.2954 4.2514 -0.1638 0.2531  0.5382  474  LYS A NZ  
3623  N N   . ALA A 475  ? 2.9455 3.3041 3.7342 -0.1033 0.2017  0.4157  475  ALA A N   
3624  C CA  . ALA A 475  ? 2.7277 3.1617 3.4803 -0.0816 0.2068  0.3872  475  ALA A CA  
3625  C C   . ALA A 475  ? 2.5501 3.0530 3.2710 -0.0953 0.1859  0.3492  475  ALA A C   
3626  O O   . ALA A 475  ? 2.5258 3.0140 3.2596 -0.1317 0.1664  0.3431  475  ALA A O   
3627  C CB  . ALA A 475  ? 2.7031 3.1335 3.4806 -0.1045 0.2106  0.3792  475  ALA A CB  
3628  N N   . LEU A 476  ? 1.9488 2.5253 2.6289 -0.0661 0.1904  0.3247  476  LEU A N   
3629  C CA  . LEU A 476  ? 1.8099 2.4559 2.4568 -0.0698 0.1737  0.2907  476  LEU A CA  
3630  C C   . LEU A 476  ? 1.7373 2.4436 2.3723 -0.0866 0.1670  0.2559  476  LEU A C   
3631  O O   . LEU A 476  ? 1.7583 2.5172 2.3606 -0.0512 0.1773  0.2436  476  LEU A O   
3632  C CB  . LEU A 476  ? 1.7304 2.4101 2.3359 -0.0132 0.1841  0.2952  476  LEU A CB  
3633  C CG  . LEU A 476  ? 1.6533 2.2706 2.2652 0.0261  0.2039  0.3388  476  LEU A CG  
3634  C CD1 . LEU A 476  ? 1.6588 2.3141 2.2282 0.0791  0.2106  0.3394  476  LEU A CD1 
3635  C CD2 . LEU A 476  ? 1.6472 2.1883 2.2954 0.0011  0.1986  0.3656  476  LEU A CD2 
3636  N N   . LEU A 477  ? 2.1168 2.8097 2.7803 -0.1422 0.1490  0.2422  477  LEU A N   
3637  C CA  . LEU A 477  ? 2.0425 2.7830 2.7025 -0.1711 0.1377  0.2088  477  LEU A CA  
3638  C C   . LEU A 477  ? 1.9629 2.7924 2.5737 -0.1404 0.1376  0.1785  477  LEU A C   
3639  O O   . LEU A 477  ? 1.9752 2.8330 2.5569 -0.1084 0.1393  0.1778  477  LEU A O   
3640  C CB  . LEU A 477  ? 2.0979 2.8284 2.7803 -0.2332 0.1110  0.1924  477  LEU A CB  
3641  C CG  . LEU A 477  ? 2.1624 2.8060 2.8861 -0.2586 0.1076  0.2243  477  LEU A CG  
3642  C CD1 . LEU A 477  ? 2.2179 2.8543 2.9570 -0.3176 0.0803  0.2081  477  LEU A CD1 
3643  C CD2 . LEU A 477  ? 2.1533 2.7311 2.9171 -0.2623 0.1211  0.2519  477  LEU A CD2 
3644  N N   . VAL A 478  ? 1.3026 2.1753 1.9048 -0.1484 0.1362  0.1542  478  VAL A N   
3645  C CA  . VAL A 478  ? 1.3318 2.2909 1.8894 -0.1243 0.1342  0.1229  478  VAL A CA  
3646  C C   . VAL A 478  ? 1.3535 2.3587 1.9022 -0.1616 0.1090  0.0904  478  VAL A C   
3647  O O   . VAL A 478  ? 1.3258 2.3107 1.9016 -0.2145 0.0923  0.0814  478  VAL A O   
3648  C CB  . VAL A 478  ? 1.3287 2.3175 1.8815 -0.1255 0.1394  0.1059  478  VAL A CB  
3649  C CG1 . VAL A 478  ? 1.3389 2.3340 1.9140 -0.1858 0.1176  0.0809  478  VAL A CG1 
3650  C CG2 . VAL A 478  ? 1.3455 2.4157 1.8489 -0.0851 0.1440  0.0827  478  VAL A CG2 
3651  N N   . GLY A 479  ? 1.2110 2.2808 1.7214 -0.1347 0.1057  0.0715  479  GLY A N   
3652  C CA  . GLY A 479  ? 1.2744 2.3954 1.7736 -0.1674 0.0829  0.0387  479  GLY A CA  
3653  C C   . GLY A 479  ? 1.3041 2.4114 1.8005 -0.1611 0.0784  0.0483  479  GLY A C   
3654  O O   . GLY A 479  ? 1.3698 2.5370 1.8409 -0.1583 0.0676  0.0230  479  GLY A O   
3655  N N   . GLU A 480  ? 1.7592 2.7872 2.2828 -0.1592 0.0867  0.0846  480  GLU A N   
3656  C CA  . GLU A 480  ? 1.7662 2.7690 2.2888 -0.1465 0.0860  0.1004  480  GLU A CA  
3657  C C   . GLU A 480  ? 1.7795 2.8390 2.2619 -0.0932 0.0930  0.0921  480  GLU A C   
3658  O O   . GLU A 480  ? 1.7724 2.8963 2.2262 -0.0697 0.0961  0.0709  480  GLU A O   
3659  C CB  . GLU A 480  ? 1.7890 2.7025 2.3414 -0.1378 0.0995  0.1437  480  GLU A CB  
3660  C CG  . GLU A 480  ? 1.8850 2.7372 2.4769 -0.1953 0.0844  0.1525  480  GLU A CG  
3661  C CD  . GLU A 480  ? 1.9842 2.7454 2.6074 -0.1868 0.0968  0.1967  480  GLU A CD  
3662  O OE1 . GLU A 480  ? 2.0132 2.7204 2.6605 -0.2153 0.0876  0.2117  480  GLU A OE1 
3663  O OE2 . GLU A 480  ? 2.0214 2.7613 2.6459 -0.1501 0.1174  0.2190  480  GLU A OE2 
3664  N N   . HIS A 481  ? 1.8503 2.8826 2.3308 -0.0713 0.0963  0.1108  481  HIS A N   
3665  C CA  . HIS A 481  ? 1.9079 2.9884 2.3518 -0.0169 0.1035  0.1060  481  HIS A CA  
3666  C C   . HIS A 481  ? 1.8684 2.8899 2.3169 0.0195  0.1171  0.1437  481  HIS A C   
3667  O O   . HIS A 481  ? 1.8490 2.8074 2.3248 -0.0040 0.1136  0.1638  481  HIS A O   
3668  C CB  . HIS A 481  ? 2.0277 3.1753 2.4517 -0.0293 0.0858  0.0705  481  HIS A CB  
3669  C CG  . HIS A 481  ? 2.1046 3.3331 2.5087 -0.0417 0.0766  0.0314  481  HIS A CG  
3670  N ND1 . HIS A 481  ? 2.1605 3.4597 2.5283 0.0024  0.0816  0.0139  481  HIS A ND1 
3671  C CD2 . HIS A 481  ? 2.1223 3.3711 2.5375 -0.0933 0.0621  0.0068  481  HIS A CD2 
3672  C CE1 . HIS A 481  ? 2.1790 3.5394 2.5367 -0.0217 0.0708  -0.0201 481  HIS A CE1 
3673  N NE2 . HIS A 481  ? 2.1579 3.4892 2.5437 -0.0799 0.0589  -0.0251 481  HIS A NE2 
3674  N N   . LEU A 482  ? 1.7810 2.8208 2.2028 0.0765  0.1325  0.1542  482  LEU A N   
3675  C CA  . LEU A 482  ? 1.7885 2.7711 2.2132 0.1136  0.1463  0.1918  482  LEU A CA  
3676  C C   . LEU A 482  ? 1.8365 2.8448 2.2384 0.1448  0.1414  0.1870  482  LEU A C   
3677  O O   . LEU A 482  ? 1.8815 2.9507 2.2487 0.1856  0.1435  0.1720  482  LEU A O   
3678  C CB  . LEU A 482  ? 1.7644 2.7318 2.1783 0.1567  0.1683  0.2153  482  LEU A CB  
3679  C CG  . LEU A 482  ? 1.7315 2.6095 2.1691 0.1702  0.1835  0.2616  482  LEU A CG  
3680  C CD1 . LEU A 482  ? 1.6839 2.5334 2.1266 0.1880  0.2042  0.2838  482  LEU A CD1 
3681  C CD2 . LEU A 482  ? 1.7721 2.6383 2.1921 0.2132  0.1872  0.2791  482  LEU A CD2 
3682  N N   . ASN A 483  ? 2.0979 3.0582 2.5199 0.1255  0.1345  0.1999  483  ASN A N   
3683  C CA  . ASN A 483  ? 2.1210 3.0879 2.5262 0.1588  0.1327  0.2035  483  ASN A CA  
3684  C C   . ASN A 483  ? 2.1058 3.0107 2.5123 0.2022  0.1500  0.2459  483  ASN A C   
3685  O O   . ASN A 483  ? 2.1009 2.9272 2.5374 0.1850  0.1544  0.2766  483  ASN A O   
3686  C CB  . ASN A 483  ? 2.1669 3.1181 2.5889 0.1191  0.1161  0.1938  483  ASN A CB  
3687  C CG  . ASN A 483  ? 2.2388 3.2267 2.6370 0.1509  0.1107  0.1817  483  ASN A CG  
3688  O OD1 . ASN A 483  ? 2.2635 3.3254 2.6312 0.1814  0.1093  0.1572  483  ASN A OD1 
3689  N ND2 . ASN A 483  ? 2.2649 3.2014 2.6777 0.1442  0.1072  0.1984  483  ASN A ND2 
3690  N N   . ILE A 484  ? 1.2824 2.2242 1.6556 0.2579  0.1587  0.2468  484  ILE A N   
3691  C CA  . ILE A 484  ? 1.2399 2.1331 1.6067 0.3056  0.1747  0.2848  484  ILE A CA  
3692  C C   . ILE A 484  ? 1.2332 2.1479 1.5763 0.3459  0.1701  0.2824  484  ILE A C   
3693  O O   . ILE A 484  ? 1.2532 2.2430 1.5685 0.3646  0.1620  0.2517  484  ILE A O   
3694  C CB  . ILE A 484  ? 1.2224 2.1281 1.5707 0.3399  0.1919  0.2955  484  ILE A CB  
3695  C CG1 . ILE A 484  ? 1.2379 2.1256 1.5630 0.4003  0.2045  0.3230  484  ILE A CG1 
3696  C CG2 . ILE A 484  ? 1.2231 2.2170 1.5469 0.3379  0.1852  0.2556  484  ILE A CG2 
3697  C CD1 . ILE A 484  ? 1.2132 2.1480 1.5027 0.4439  0.2155  0.3192  484  ILE A CD1 
3698  N N   . ILE A 485  ? 1.1950 2.0416 1.5512 0.3579  0.1747  0.3147  485  ILE A N   
3699  C CA  . ILE A 485  ? 1.2296 2.0820 1.5696 0.3922  0.1698  0.3164  485  ILE A CA  
3700  C C   . ILE A 485  ? 1.2375 2.0845 1.5522 0.4520  0.1848  0.3403  485  ILE A C   
3701  O O   . ILE A 485  ? 1.2485 2.0405 1.5731 0.4599  0.2003  0.3736  485  ILE A O   
3702  C CB  . ILE A 485  ? 1.2158 1.9891 1.5842 0.3735  0.1676  0.3425  485  ILE A CB  
3703  C CG1 . ILE A 485  ? 1.2845 2.0707 1.6705 0.3207  0.1492  0.3150  485  ILE A CG1 
3704  C CG2 . ILE A 485  ? 1.2754 2.0294 1.6275 0.4228  0.1706  0.3615  485  ILE A CG2 
3705  C CD1 . ILE A 485  ? 1.1727 1.9366 1.5890 0.2606  0.1457  0.3109  485  ILE A CD1 
3706  N N   . VAL A 486  ? 1.2637 2.1672 1.5461 0.4935  0.1799  0.3237  486  VAL A N   
3707  C CA  . VAL A 486  ? 1.2803 2.1926 1.5325 0.5517  0.1918  0.3408  486  VAL A CA  
3708  C C   . VAL A 486  ? 1.2222 2.1107 1.4647 0.5905  0.1894  0.3571  486  VAL A C   
3709  O O   . VAL A 486  ? 1.2342 2.1794 1.4525 0.6191  0.1799  0.3346  486  VAL A O   
3710  C CB  . VAL A 486  ? 1.1979 2.2043 1.4172 0.5711  0.1867  0.3051  486  VAL A CB  
3711  C CG1 . VAL A 486  ? 1.2403 2.2607 1.4247 0.6339  0.1953  0.3199  486  VAL A CG1 
3712  C CG2 . VAL A 486  ? 1.2242 2.2528 1.4502 0.5375  0.1905  0.2911  486  VAL A CG2 
3713  N N   . THR A 487  ? 1.7688 2.5733 2.0310 0.5914  0.1974  0.3957  487  THR A N   
3714  C CA  . THR A 487  ? 1.8141 2.5876 2.0705 0.6239  0.1941  0.4126  487  THR A CA  
3715  C C   . THR A 487  ? 1.8702 2.6329 2.0980 0.6844  0.2060  0.4395  487  THR A C   
3716  O O   . THR A 487  ? 1.8534 2.5505 2.0895 0.6929  0.2209  0.4783  487  THR A O   
3717  C CB  . THR A 487  ? 1.8340 2.5178 2.1255 0.5959  0.1960  0.4429  487  THR A CB  
3718  O OG1 . THR A 487  ? 1.8190 2.4422 2.1247 0.5925  0.2134  0.4790  487  THR A OG1 
3719  C CG2 . THR A 487  ? 1.7820 2.4702 2.1010 0.5363  0.1828  0.4186  487  THR A CG2 
3720  N N   . PRO A 488  ? 1.3562 2.1818 1.5506 0.7265  0.1990  0.4198  488  PRO A N   
3721  C CA  . PRO A 488  ? 1.4387 2.2565 1.6029 0.7845  0.2088  0.4447  488  PRO A CA  
3722  C C   . PRO A 488  ? 1.4243 2.1725 1.5922 0.8121  0.2111  0.4804  488  PRO A C   
3723  O O   . PRO A 488  ? 1.5415 2.2785 1.6842 0.8600  0.2184  0.5029  488  PRO A O   
3724  C CB  . PRO A 488  ? 1.4485 2.3572 1.5795 0.8161  0.1967  0.4085  488  PRO A CB  
3725  C CG  . PRO A 488  ? 1.3969 2.3648 1.5398 0.7714  0.1853  0.3658  488  PRO A CG  
3726  C CD  . PRO A 488  ? 1.3598 2.2720 1.5415 0.7216  0.1825  0.3725  488  PRO A CD  
3727  N N   . LYS A 489  ? 1.7582 2.4601 1.9561 0.7813  0.2047  0.4853  489  LYS A N   
3728  C CA  . LYS A 489  ? 1.9636 2.5978 2.1688 0.8014  0.2046  0.5163  489  LYS A CA  
3729  C C   . LYS A 489  ? 2.1309 2.7347 2.3108 0.8573  0.2154  0.5515  489  LYS A C   
3730  O O   . LYS A 489  ? 2.1412 2.7256 2.3142 0.8659  0.2312  0.5744  489  LYS A O   
3731  C CB  . LYS A 489  ? 1.9564 2.5110 2.2020 0.7553  0.2090  0.5399  489  LYS A CB  
3732  C CG  . LYS A 489  ? 2.0197 2.4998 2.2779 0.7670  0.2072  0.5703  489  LYS A CG  
3733  C CD  . LYS A 489  ? 2.0206 2.4401 2.3202 0.7119  0.2053  0.5798  489  LYS A CD  
3734  C CE  . LYS A 489  ? 2.0829 2.4315 2.3957 0.7195  0.2015  0.6061  489  LYS A CE  
3735  N NZ  . LYS A 489  ? 2.1468 2.5312 2.4492 0.7308  0.1844  0.5781  489  LYS A NZ  
3736  N N   . SER A 490  ? 2.8558 3.4566 3.0216 0.8946  0.2064  0.5547  490  SER A N   
3737  C CA  . SER A 490  ? 2.9830 3.5449 3.1267 0.9469  0.2140  0.5906  490  SER A CA  
3738  C C   . SER A 490  ? 3.0719 3.6975 3.1735 1.0008  0.2089  0.5769  490  SER A C   
3739  O O   . SER A 490  ? 3.1541 3.7807 3.2423 1.0370  0.1987  0.5776  490  SER A O   
3740  C CB  . SER A 490  ? 3.0052 3.4973 3.1589 0.9407  0.2344  0.6339  490  SER A CB  
3741  O OG  . SER A 490  ? 2.9866 3.4141 3.1802 0.8961  0.2367  0.6492  490  SER A OG  
3742  N N   . PRO A 491  ? 2.5889 3.2674 2.6697 1.0065  0.2152  0.5638  491  PRO A N   
3743  C CA  . PRO A 491  ? 2.5939 3.3294 2.6340 1.0583  0.2098  0.5529  491  PRO A CA  
3744  C C   . PRO A 491  ? 2.5139 3.2670 2.5452 1.0906  0.1924  0.5403  491  PRO A C   
3745  O O   . PRO A 491  ? 2.4486 3.2380 2.4948 1.0691  0.1784  0.5067  491  PRO A O   
3746  C CB  . PRO A 491  ? 2.6147 3.4343 2.6474 1.0379  0.2059  0.5115  491  PRO A CB  
3747  C CG  . PRO A 491  ? 2.5754 3.3602 2.6342 0.9890  0.2202  0.5221  491  PRO A CG  
3748  C CD  . PRO A 491  ? 2.5522 3.2477 2.6447 0.9665  0.2248  0.5537  491  PRO A CD  
3749  N N   . TYR A 492  ? 2.3814 3.1080 2.3887 1.1413  0.1933  0.5672  492  TYR A N   
3750  C CA  . TYR A 492  ? 2.3981 3.1294 2.3996 1.1732  0.1774  0.5603  492  TYR A CA  
3751  C C   . TYR A 492  ? 2.3892 3.2076 2.3910 1.1641  0.1607  0.5082  492  TYR A C   
3752  O O   . TYR A 492  ? 2.4367 3.2616 2.4484 1.1685  0.1469  0.4923  492  TYR A O   
3753  C CB  . TYR A 492  ? 2.4707 3.1950 2.4361 1.2350  0.1768  0.5834  492  TYR A CB  
3754  C CG  . TYR A 492  ? 2.4726 3.2745 2.4017 1.2660  0.1732  0.5623  492  TYR A CG  
3755  C CD1 . TYR A 492  ? 2.5416 3.3440 2.4356 1.3228  0.1698  0.5797  492  TYR A CD1 
3756  C CD2 . TYR A 492  ? 2.3919 3.2645 2.3208 1.2388  0.1726  0.5263  492  TYR A CD2 
3757  C CE1 . TYR A 492  ? 2.5600 3.4312 2.4193 1.3520  0.1659  0.5619  492  TYR A CE1 
3758  C CE2 . TYR A 492  ? 2.4104 3.3532 2.3053 1.2677  0.1689  0.5076  492  TYR A CE2 
3759  C CZ  . TYR A 492  ? 2.5039 3.4456 2.3638 1.3245  0.1655  0.5257  492  TYR A CZ  
3760  O OH  . TYR A 492  ? 2.5561 3.5655 2.3812 1.3536  0.1611  0.5083  492  TYR A OH  
3761  N N   . ILE A 493  ? 2.4162 3.3015 2.4078 1.1502  0.1619  0.4808  493  ILE A N   
3762  C CA  . ILE A 493  ? 2.4589 3.4311 2.4516 1.1387  0.1463  0.4297  493  ILE A CA  
3763  C C   . ILE A 493  ? 2.4398 3.4609 2.4436 1.0903  0.1489  0.4000  493  ILE A C   
3764  O O   . ILE A 493  ? 2.4177 3.4157 2.4237 1.0698  0.1633  0.4163  493  ILE A O   
3765  C CB  . ILE A 493  ? 3.3989 4.4355 3.3587 1.1942  0.1329  0.4111  493  ILE A CB  
3766  C CG1 . ILE A 493  ? 3.4359 4.4726 3.4054 1.2113  0.1172  0.3987  493  ILE A CG1 
3767  C CG2 . ILE A 493  ? 3.3891 4.5221 3.3358 1.1867  0.1263  0.3682  493  ILE A CG2 
3768  C CD1 . ILE A 493  ? 3.5143 4.6177 3.4576 1.2625  0.1016  0.3757  493  ILE A CD1 
3769  N N   . ASP A 494  ? 2.8150 3.9031 2.8264 1.0727  0.1343  0.3557  494  ASP A N   
3770  C CA  . ASP A 494  ? 2.7533 3.8892 2.7795 1.0222  0.1326  0.3223  494  ASP A CA  
3771  C C   . ASP A 494  ? 2.7780 4.0120 2.7799 1.0362  0.1246  0.2844  494  ASP A C   
3772  O O   . ASP A 494  ? 2.7433 4.0310 2.7560 0.9983  0.1187  0.2489  494  ASP A O   
3773  C CB  . ASP A 494  ? 2.7454 3.8837 2.8006 0.9853  0.1215  0.2986  494  ASP A CB  
3774  C CG  . ASP A 494  ? 2.7263 3.9162 2.7723 1.0176  0.1050  0.2710  494  ASP A CG  
3775  O OD1 . ASP A 494  ? 2.7696 3.9495 2.7955 1.0708  0.1029  0.2876  494  ASP A OD1 
3776  O OD2 . ASP A 494  ? 2.7156 3.9556 2.7748 0.9897  0.0939  0.2325  494  ASP A OD2 
3777  N N   . LYS A 495  ? 2.2657 3.5232 2.2350 1.0897  0.1237  0.2918  495  LYS A N   
3778  C CA  . LYS A 495  ? 2.2719 3.6246 2.2171 1.1093  0.1134  0.2551  495  LYS A CA  
3779  C C   . LYS A 495  ? 2.1608 3.5500 2.1000 1.0808  0.1207  0.2419  495  LYS A C   
3780  O O   . LYS A 495  ? 2.1623 3.6103 2.0735 1.1054  0.1181  0.2274  495  LYS A O   
3781  C CB  . LYS A 495  ? 2.3902 3.7556 2.3015 1.1749  0.1089  0.2676  495  LYS A CB  
3782  C CG  . LYS A 495  ? 2.4669 3.8429 2.3812 1.2057  0.0935  0.2569  495  LYS A CG  
3783  C CD  . LYS A 495  ? 2.4305 3.8622 2.3686 1.1717  0.0806  0.2116  495  LYS A CD  
3784  C CE  . LYS A 495  ? 2.3624 3.7298 2.3352 1.1310  0.0839  0.2223  495  LYS A CE  
3785  N NZ  . LYS A 495  ? 2.2767 3.6873 2.2737 1.0766  0.0780  0.1836  495  LYS A NZ  
3786  N N   . ILE A 496  ? 2.1052 3.4591 2.0717 1.0277  0.1288  0.2458  496  ILE A N   
3787  C CA  . ILE A 496  ? 2.0275 3.3977 1.9927 0.9971  0.1380  0.2401  496  ILE A CA  
3788  C C   . ILE A 496  ? 2.0456 3.5102 2.0054 0.9786  0.1262  0.1916  496  ILE A C   
3789  O O   . ILE A 496  ? 2.0291 3.5246 2.0091 0.9463  0.1152  0.1615  496  ILE A O   
3790  C CB  . ILE A 496  ? 1.9067 3.2117 1.9057 0.9441  0.1482  0.2570  496  ILE A CB  
3791  C CG1 . ILE A 496  ? 1.8495 3.0602 1.8614 0.9561  0.1567  0.3013  496  ILE A CG1 
3792  C CG2 . ILE A 496  ? 1.9021 3.2090 1.8963 0.9235  0.1610  0.2616  496  ILE A CG2 
3793  C CD1 . ILE A 496  ? 1.8038 2.9851 1.8459 0.9296  0.1479  0.2961  496  ILE A CD1 
3794  N N   . THR A 497  ? 1.5774 3.0868 1.5092 0.9984  0.1290  0.1848  497  THR A N   
3795  C CA  . THR A 497  ? 1.6222 3.2170 1.5478 0.9781  0.1200  0.1420  497  THR A CA  
3796  C C   . THR A 497  ? 1.5615 3.1432 1.5134 0.9157  0.1253  0.1335  497  THR A C   
3797  O O   . THR A 497  ? 1.5507 3.1459 1.5277 0.8760  0.1165  0.1105  497  THR A O   
3798  C CB  . THR A 497  ? 1.7259 3.3631 1.6141 1.0134  0.1231  0.1408  497  THR A CB  
3799  O OG1 . THR A 497  ? 1.7174 3.4177 1.6049 0.9803  0.1193  0.1066  497  THR A OG1 
3800  C CG2 . THR A 497  ? 1.7379 3.3035 1.6142 1.0293  0.1426  0.1863  497  THR A CG2 
3801  N N   . HIS A 498  ? 2.2424 3.7953 2.1888 0.9070  0.1398  0.1530  498  HIS A N   
3802  C CA  . HIS A 498  ? 2.1494 3.7017 2.1166 0.8514  0.1436  0.1409  498  HIS A CA  
3803  C C   . HIS A 498  ? 2.0542 3.5167 2.0402 0.8319  0.1615  0.1808  498  HIS A C   
3804  O O   . HIS A 498  ? 2.0834 3.4981 2.0557 0.8665  0.1743  0.2165  498  HIS A O   
3805  C CB  . HIS A 498  ? 2.1929 3.8165 2.1360 0.8530  0.1420  0.1149  498  HIS A CB  
3806  C CG  . HIS A 498  ? 2.2761 3.9936 2.2059 0.8619  0.1237  0.0710  498  HIS A CG  
3807  N ND1 . HIS A 498  ? 2.3558 4.1300 2.2503 0.9084  0.1188  0.0606  498  HIS A ND1 
3808  C CD2 . HIS A 498  ? 2.2683 4.0325 2.2159 0.8290  0.1091  0.0350  498  HIS A CD2 
3809  C CE1 . HIS A 498  ? 2.3873 4.2408 2.2801 0.9046  0.1019  0.0195  498  HIS A CE1 
3810  N NE2 . HIS A 498  ? 2.3348 4.1842 2.2591 0.8568  0.0963  0.0033  498  HIS A NE2 
3811  N N   . TYR A 499  ? 1.7308 3.1703 1.7489 0.7762  0.1618  0.1747  499  TYR A N   
3812  C CA  . TYR A 499  ? 1.5915 2.9593 1.6281 0.7525  0.1782  0.2058  499  TYR A CA  
3813  C C   . TYR A 499  ? 1.4971 2.9023 1.5216 0.7400  0.1837  0.1914  499  TYR A C   
3814  O O   . TYR A 499  ? 1.4615 2.9387 1.4800 0.7221  0.1717  0.1525  499  TYR A O   
3815  C CB  . TYR A 499  ? 1.5191 2.8392 1.5971 0.6991  0.1753  0.2083  499  TYR A CB  
3816  C CG  . TYR A 499  ? 1.5360 2.8076 1.6264 0.7116  0.1723  0.2277  499  TYR A CG  
3817  C CD1 . TYR A 499  ? 1.5471 2.7439 1.6380 0.7394  0.1858  0.2719  499  TYR A CD1 
3818  C CD2 . TYR A 499  ? 1.5669 2.8683 1.6674 0.6962  0.1560  0.2014  499  TYR A CD2 
3819  C CE1 . TYR A 499  ? 1.5758 2.7269 1.6779 0.7511  0.1823  0.2897  499  TYR A CE1 
3820  C CE2 . TYR A 499  ? 1.5944 2.8516 1.7059 0.7076  0.1529  0.2178  499  TYR A CE2 
3821  C CZ  . TYR A 499  ? 1.5992 2.7806 1.7116 0.7352  0.1656  0.2621  499  TYR A CZ  
3822  O OH  . TYR A 499  ? 1.6153 2.7529 1.7385 0.7461  0.1615  0.2774  499  TYR A OH  
3823  N N   . ASN A 500  ? 1.8178 3.1738 1.8384 0.7503  0.2021  0.2231  500  ASN A N   
3824  C CA  . ASN A 500  ? 1.7729 3.1542 1.7795 0.7446  0.2109  0.2157  500  ASN A CA  
3825  C C   . ASN A 500  ? 1.6637 2.9729 1.6975 0.7143  0.2278  0.2434  500  ASN A C   
3826  O O   . ASN A 500  ? 1.6762 2.9140 1.7183 0.7289  0.2414  0.2825  500  ASN A O   
3827  C CB  . ASN A 500  ? 1.8413 3.2498 1.8039 0.8012  0.2175  0.2243  500  ASN A CB  
3828  C CG  . ASN A 500  ? 1.9176 3.3766 1.8558 0.8414  0.2026  0.2091  500  ASN A CG  
3829  O OD1 . ASN A 500  ? 1.9323 3.4314 1.8818 0.8249  0.1858  0.1801  500  ASN A OD1 
3830  N ND2 . ASN A 500  ? 1.9642 3.4220 1.8686 0.8945  0.2087  0.2284  500  ASN A ND2 
3831  N N   . TYR A 501  ? 1.9122 3.2401 1.9605 0.6720  0.2267  0.2230  501  TYR A N   
3832  C CA  . TYR A 501  ? 1.8402 3.1024 1.9182 0.6405  0.2409  0.2461  501  TYR A CA  
3833  C C   . TYR A 501  ? 1.8262 3.1039 1.8907 0.6408  0.2533  0.2433  501  TYR A C   
3834  O O   . TYR A 501  ? 1.8441 3.1882 1.8756 0.6607  0.2495  0.2199  501  TYR A O   
3835  C CB  . TYR A 501  ? 1.8229 3.0698 1.9414 0.5816  0.2297  0.2316  501  TYR A CB  
3836  C CG  . TYR A 501  ? 1.8472 3.1655 1.9647 0.5472  0.2144  0.1867  501  TYR A CG  
3837  C CD1 . TYR A 501  ? 1.8285 3.1499 1.9572 0.5145  0.2187  0.1770  501  TYR A CD1 
3838  C CD2 . TYR A 501  ? 1.8949 3.2756 2.0027 0.5450  0.1952  0.1539  501  TYR A CD2 
3839  C CE1 . TYR A 501  ? 1.8382 3.2224 1.9666 0.4810  0.2038  0.1365  501  TYR A CE1 
3840  C CE2 . TYR A 501  ? 1.9056 3.3511 2.0137 0.5109  0.1809  0.1130  501  TYR A CE2 
3841  C CZ  . TYR A 501  ? 1.8801 3.3263 1.9979 0.4790  0.1850  0.1050  501  TYR A CZ  
3842  O OH  . TYR A 501  ? 1.8859 3.3946 2.0033 0.4449  0.1703  0.0653  501  TYR A OH  
3843  N N   . LEU A 502  ? 1.4602 2.6756 1.5519 0.6172  0.2679  0.2667  502  LEU A N   
3844  C CA  . LEU A 502  ? 1.4268 2.6451 1.5082 0.6192  0.2829  0.2693  502  LEU A CA  
3845  C C   . LEU A 502  ? 1.3882 2.5450 1.5136 0.5746  0.2917  0.2837  502  LEU A C   
3846  O O   . LEU A 502  ? 1.3597 2.4449 1.5096 0.5729  0.3011  0.3174  502  LEU A O   
3847  C CB  . LEU A 502  ? 1.4236 2.6201 1.4741 0.6724  0.3009  0.3005  502  LEU A CB  
3848  C CG  . LEU A 502  ? 1.4052 2.6512 1.4160 0.6988  0.3087  0.2887  502  LEU A CG  
3849  C CD1 . LEU A 502  ? 1.3775 2.7108 1.3717 0.6865  0.2897  0.2417  502  LEU A CD1 
3850  C CD2 . LEU A 502  ? 1.4508 2.6922 1.4223 0.7577  0.3177  0.3130  502  LEU A CD2 
3851  N N   . ILE A 503  ? 1.4023 2.5864 1.5385 0.5387  0.2881  0.2584  503  ILE A N   
3852  C CA  . ILE A 503  ? 1.3647 2.4939 1.5447 0.4938  0.2942  0.2688  503  ILE A CA  
3853  C C   . ILE A 503  ? 1.3546 2.4864 1.5308 0.4908  0.3096  0.2675  503  ILE A C   
3854  O O   . ILE A 503  ? 1.3500 2.5375 1.5157 0.4745  0.3014  0.2344  503  ILE A O   
3855  C CB  . ILE A 503  ? 1.3276 2.4734 1.5367 0.4397  0.2731  0.2401  503  ILE A CB  
3856  C CG1 . ILE A 503  ? 1.3508 2.5008 1.5626 0.4396  0.2570  0.2364  503  ILE A CG1 
3857  C CG2 . ILE A 503  ? 1.2748 2.3551 1.5314 0.3956  0.2786  0.2554  503  ILE A CG2 
3858  C CD1 . ILE A 503  ? 1.3063 2.4967 1.5327 0.3932  0.2340  0.1998  503  ILE A CD1 
3859  N N   . LEU A 504  ? 1.3931 2.4641 1.5784 0.5063  0.3319  0.3035  504  LEU A N   
3860  C CA  . LEU A 504  ? 1.3936 2.4545 1.5797 0.5046  0.3502  0.3081  504  LEU A CA  
3861  C C   . LEU A 504  ? 1.3990 2.4145 1.6366 0.4528  0.3500  0.3095  504  LEU A C   
3862  O O   . LEU A 504  ? 1.4050 2.3777 1.6781 0.4257  0.3415  0.3200  504  LEU A O   
3863  C CB  . LEU A 504  ? 1.3608 2.3738 1.5347 0.5449  0.3754  0.3481  504  LEU A CB  
3864  C CG  . LEU A 504  ? 1.3821 2.4317 1.5015 0.6010  0.3816  0.3527  504  LEU A CG  
3865  C CD1 . LEU A 504  ? 1.3990 2.5030 1.4952 0.6134  0.3593  0.3300  504  LEU A CD1 
3866  C CD2 . LEU A 504  ? 1.5036 2.4896 1.6215 0.6331  0.4011  0.3979  504  LEU A CD2 
3867  N N   . SER A 505  ? 2.5531 3.5752 2.7953 0.4399  0.3598  0.3002  505  SER A N   
3868  C CA  . SER A 505  ? 2.5249 3.5081 2.8161 0.3904  0.3584  0.2986  505  SER A CA  
3869  C C   . SER A 505  ? 2.5592 3.5444 2.8476 0.3931  0.3762  0.2966  505  SER A C   
3870  O O   . SER A 505  ? 2.5536 3.5998 2.8123 0.3986  0.3725  0.2675  505  SER A O   
3871  C CB  . SER A 505  ? 2.4899 3.5158 2.7923 0.3475  0.3319  0.2607  505  SER A CB  
3872  O OG  . SER A 505  ? 2.4407 3.4417 2.7825 0.3024  0.3306  0.2533  505  SER A OG  
3873  N N   . LYS A 506  ? 1.7288 2.6478 2.0489 0.3881  0.3954  0.3264  506  LYS A N   
3874  C CA  . LYS A 506  ? 1.7480 2.6662 2.0642 0.3953  0.4155  0.3270  506  LYS A CA  
3875  C C   . LYS A 506  ? 1.8328 2.7879 2.0924 0.4489  0.4295  0.3312  506  LYS A C   
3876  O O   . LYS A 506  ? 1.8660 2.8736 2.0954 0.4574  0.4307  0.3065  506  LYS A O   
3877  C CB  . LYS A 506  ? 1.7096 2.6721 2.0320 0.3604  0.4023  0.2878  506  LYS A CB  
3878  C CG  . LYS A 506  ? 1.6299 2.5663 2.0022 0.3056  0.3833  0.2782  506  LYS A CG  
3879  C CD  . LYS A 506  ? 1.5905 2.5786 1.9616 0.2738  0.3672  0.2371  506  LYS A CD  
3880  C CE  . LYS A 506  ? 1.6022 2.6648 1.9325 0.2830  0.3473  0.2068  506  LYS A CE  
3881  N NZ  . LYS A 506  ? 1.5793 2.6313 1.9264 0.2624  0.3273  0.2076  506  LYS A NZ  
3882  N N   . GLY A 507  ? 2.2247 3.1527 2.4687 0.4845  0.4385  0.3618  507  GLY A N   
3883  C CA  . GLY A 507  ? 2.3011 3.2555 2.4918 0.5369  0.4524  0.3710  507  GLY A CA  
3884  C C   . GLY A 507  ? 2.3682 3.4046 2.5100 0.5566  0.4360  0.3383  507  GLY A C   
3885  O O   . GLY A 507  ? 2.4101 3.4731 2.5049 0.5999  0.4454  0.3433  507  GLY A O   
3886  N N   . LYS A 508  ? 2.4594 3.5354 2.6121 0.5244  0.4112  0.3050  508  LYS A N   
3887  C CA  . LYS A 508  ? 2.4855 3.6431 2.5966 0.5373  0.3938  0.2701  508  LYS A CA  
3888  C C   . LYS A 508  ? 2.4174 3.5963 2.5295 0.5326  0.3702  0.2595  508  LYS A C   
3889  O O   . LYS A 508  ? 2.3638 3.5207 2.5151 0.4928  0.3568  0.2546  508  LYS A O   
3890  C CB  . LYS A 508  ? 2.4798 3.6803 2.5967 0.5033  0.3849  0.2330  508  LYS A CB  
3891  C CG  . LYS A 508  ? 2.5286 3.7886 2.5971 0.5309  0.3904  0.2133  508  LYS A CG  
3892  C CD  . LYS A 508  ? 2.5018 3.7838 2.5846 0.4949  0.3871  0.1844  508  LYS A CD  
3893  C CE  . LYS A 508  ? 2.5316 3.8291 2.5818 0.5213  0.4072  0.1842  508  LYS A CE  
3894  N NZ  . LYS A 508  ? 2.4969 3.7871 2.5740 0.4853  0.4114  0.1682  508  LYS A NZ  
3895  N N   . ILE A 509  ? 1.5234 2.7452 1.5921 0.5733  0.3649  0.2555  509  ILE A N   
3896  C CA  . ILE A 509  ? 1.4687 2.7252 1.5340 0.5700  0.3415  0.2379  509  ILE A CA  
3897  C C   . ILE A 509  ? 1.4070 2.7205 1.4790 0.5311  0.3221  0.1946  509  ILE A C   
3898  O O   . ILE A 509  ? 1.4184 2.7681 1.4743 0.5281  0.3253  0.1749  509  ILE A O   
3899  C CB  . ILE A 509  ? 1.4988 2.7996 1.5141 0.6225  0.3384  0.2372  509  ILE A CB  
3900  C CG1 . ILE A 509  ? 1.5147 2.7650 1.5144 0.6649  0.3601  0.2790  509  ILE A CG1 
3901  C CG2 . ILE A 509  ? 1.5198 2.8433 1.5382 0.6210  0.3169  0.2253  509  ILE A CG2 
3902  C CD1 . ILE A 509  ? 1.5626 2.8220 1.5374 0.7045  0.3523  0.2898  509  ILE A CD1 
3903  N N   . ILE A 510  ? 1.7533 3.0741 1.8485 0.5004  0.3020  0.1798  510  ILE A N   
3904  C CA  . ILE A 510  ? 1.7192 3.0938 1.8211 0.4613  0.2821  0.1390  510  ILE A CA  
3905  C C   . ILE A 510  ? 1.7377 3.1454 1.8402 0.4528  0.2600  0.1210  510  ILE A C   
3906  O O   . ILE A 510  ? 1.7110 3.1781 1.8086 0.4297  0.2418  0.0847  510  ILE A O   
3907  C CB  . ILE A 510  ? 1.7756 3.1075 1.9238 0.4084  0.2820  0.1384  510  ILE A CB  
3908  C CG1 . ILE A 510  ? 1.7501 2.9968 1.9362 0.3997  0.2912  0.1762  510  ILE A CG1 
3909  C CG2 . ILE A 510  ? 1.7669 3.0997 1.9100 0.4076  0.2968  0.1354  510  ILE A CG2 
3910  C CD1 . ILE A 510  ? 1.6912 2.8907 1.9270 0.3465  0.2892  0.1777  510  ILE A CD1 
3911  N N   . HIS A 511  ? 1.7534 3.1233 1.8617 0.4715  0.2616  0.1461  511  HIS A N   
3912  C CA  . HIS A 511  ? 1.8308 3.2342 1.9361 0.4695  0.2421  0.1293  511  HIS A CA  
3913  C C   . HIS A 511  ? 1.9053 3.3046 1.9857 0.5210  0.2462  0.1494  511  HIS A C   
3914  O O   . HIS A 511  ? 1.9228 3.2669 2.0019 0.5485  0.2638  0.1857  511  HIS A O   
3915  C CB  . HIS A 511  ? 1.8354 3.1981 1.9857 0.4192  0.2314  0.1300  511  HIS A CB  
3916  C CG  . HIS A 511  ? 1.8150 3.1839 1.9896 0.3670  0.2244  0.1084  511  HIS A CG  
3917  N ND1 . HIS A 511  ? 1.8201 3.2583 1.9861 0.3418  0.2057  0.0672  511  HIS A ND1 
3918  C CD2 . HIS A 511  ? 1.7800 3.0950 1.9874 0.3359  0.2333  0.1220  511  HIS A CD2 
3919  C CE1 . HIS A 511  ? 1.7727 3.1979 1.9643 0.2968  0.2028  0.0569  511  HIS A CE1 
3920  N NE2 . HIS A 511  ? 1.7476 3.0986 1.9652 0.2927  0.2191  0.0893  511  HIS A NE2 
3921  N N   . PHE A 512  ? 1.6398 3.0994 1.7003 0.5335  0.2293  0.1246  512  PHE A N   
3922  C CA  . PHE A 512  ? 1.7240 3.1906 1.7594 0.5825  0.2291  0.1374  512  PHE A CA  
3923  C C   . PHE A 512  ? 1.7179 3.2587 1.7419 0.5796  0.2067  0.1000  512  PHE A C   
3924  O O   . PHE A 512  ? 1.6723 3.2668 1.6971 0.5494  0.1948  0.0653  512  PHE A O   
3925  C CB  . PHE A 512  ? 1.8437 3.3264 1.8381 0.6331  0.2429  0.1493  512  PHE A CB  
3926  C CG  . PHE A 512  ? 1.9270 3.4965 1.8879 0.6438  0.2327  0.1128  512  PHE A CG  
3927  C CD1 . PHE A 512  ? 2.0024 3.6229 1.9258 0.6896  0.2256  0.1045  512  PHE A CD1 
3928  C CD2 . PHE A 512  ? 1.9018 3.5028 1.8701 0.6063  0.2284  0.0857  512  PHE A CD2 
3929  C CE1 . PHE A 512  ? 2.0379 3.7396 1.9317 0.6982  0.2152  0.0702  512  PHE A CE1 
3930  C CE2 . PHE A 512  ? 1.9305 3.6117 1.8687 0.6143  0.2182  0.0515  512  PHE A CE2 
3931  C CZ  . PHE A 512  ? 1.9960 3.7283 1.8969 0.6602  0.2116  0.0436  512  PHE A CZ  
3932  N N   . GLY A 513  ? 1.6258 3.1699 1.6400 0.6105  0.2010  0.1067  513  GLY A N   
3933  C CA  . GLY A 513  ? 1.6606 3.2748 1.6649 0.6116  0.1808  0.0722  513  GLY A CA  
3934  C C   . GLY A 513  ? 1.7057 3.3049 1.7055 0.6457  0.1772  0.0868  513  GLY A C   
3935  O O   . GLY A 513  ? 1.7071 3.2526 1.7007 0.6792  0.1905  0.1229  513  GLY A O   
3936  N N   . THR A 514  ? 1.7284 3.3743 1.7316 0.6372  0.1595  0.0589  514  THR A N   
3937  C CA  . THR A 514  ? 1.7863 3.4135 1.7911 0.6637  0.1550  0.0712  514  THR A CA  
3938  C C   . THR A 514  ? 1.7560 3.4047 1.7835 0.6303  0.1382  0.0458  514  THR A C   
3939  O O   . THR A 514  ? 1.7505 3.4688 1.7755 0.6080  0.1245  0.0069  514  THR A O   
3940  C CB  . THR A 514  ? 1.8767 3.5475 1.8433 0.7244  0.1529  0.0697  514  THR A CB  
3941  O OG1 . THR A 514  ? 1.9013 3.5315 1.8484 0.7591  0.1703  0.1033  514  THR A OG1 
3942  C CG2 . THR A 514  ? 1.9394 3.5988 1.9103 0.7475  0.1451  0.0758  514  THR A CG2 
3943  N N   . ARG A 515  ? 2.2914 3.8793 2.3402 0.6269  0.1397  0.0685  515  ARG A N   
3944  C CA  . ARG A 515  ? 2.3351 3.9364 2.4033 0.6003  0.1252  0.0483  515  ARG A CA  
3945  C C   . ARG A 515  ? 2.3752 3.9874 2.4280 0.6490  0.1207  0.0525  515  ARG A C   
3946  O O   . ARG A 515  ? 2.3957 3.9486 2.4458 0.6814  0.1308  0.0885  515  ARG A O   
3947  C CB  . ARG A 515  ? 2.3587 3.8788 2.4641 0.5578  0.1293  0.0709  515  ARG A CB  
3948  C CG  . ARG A 515  ? 2.3624 3.8497 2.4855 0.5171  0.1373  0.0787  515  ARG A CG  
3949  C CD  . ARG A 515  ? 2.4054 3.9587 2.5300 0.4760  0.1250  0.0376  515  ARG A CD  
3950  N NE  . ARG A 515  ? 2.4041 3.9172 2.5530 0.4292  0.1298  0.0448  515  ARG A NE  
3951  C CZ  . ARG A 515  ? 2.4259 3.8848 2.6091 0.3831  0.1267  0.0537  515  ARG A CZ  
3952  N NH1 . ARG A 515  ? 2.4557 3.8931 2.6517 0.3769  0.1195  0.0568  515  ARG A NH1 
3953  N NH2 . ARG A 515  ? 2.4009 3.8257 2.6059 0.3429  0.1305  0.0596  515  ARG A NH2 
3954  N N   . GLU A 516  ? 2.2578 3.9453 2.3011 0.6542  0.1053  0.0158  516  GLU A N   
3955  C CA  . GLU A 516  ? 2.2835 3.9855 2.3150 0.6989  0.0992  0.0159  516  GLU A CA  
3956  C C   . GLU A 516  ? 2.2450 3.8732 2.3015 0.6896  0.1011  0.0403  516  GLU A C   
3957  O O   . GLU A 516  ? 2.1765 3.7851 2.2601 0.6404  0.0966  0.0321  516  GLU A O   
3958  C CB  . GLU A 516  ? 2.3353 4.1325 2.3581 0.6992  0.0819  -0.0309 516  GLU A CB  
3959  C CG  . GLU A 516  ? 2.4117 4.2225 2.4305 0.7366  0.0736  -0.0351 516  GLU A CG  
3960  C CD  . GLU A 516  ? 2.4795 4.3825 2.4721 0.7752  0.0624  -0.0666 516  GLU A CD  
3961  O OE1 . GLU A 516  ? 2.5204 4.4562 2.5153 0.7912  0.0516  -0.0850 516  GLU A OE1 
3962  O OE2 . GLU A 516  ? 2.4970 4.4391 2.4668 0.7900  0.0642  -0.0729 516  GLU A OE2 
3963  N N   . LYS A 517  ? 1.7477 3.3338 1.7940 0.7366  0.1072  0.0706  517  LYS A N   
3964  C CA  . LYS A 517  ? 1.7628 3.2744 1.8307 0.7325  0.1097  0.0970  517  LYS A CA  
3965  C C   . LYS A 517  ? 1.8617 3.4019 1.9435 0.7165  0.0949  0.0692  517  LYS A C   
3966  O O   . LYS A 517  ? 1.9337 3.5485 2.0007 0.7371  0.0834  0.0374  517  LYS A O   
3967  C CB  . LYS A 517  ? 1.7553 3.2208 1.8064 0.7890  0.1183  0.1340  517  LYS A CB  
3968  C CG  . LYS A 517  ? 1.7119 3.0840 1.7866 0.7807  0.1251  0.1703  517  LYS A CG  
3969  C CD  . LYS A 517  ? 1.7375 3.1054 1.8113 0.8101  0.1160  0.1698  517  LYS A CD  
3970  C CE  . LYS A 517  ? 1.7072 2.9789 1.8031 0.8030  0.1230  0.2079  517  LYS A CE  
3971  N NZ  . LYS A 517  ? 1.7605 3.0118 1.8419 0.8573  0.1213  0.2262  517  LYS A NZ  
3972  N N   . PHE A 518  ? 2.4908 3.9703 2.6014 0.6795  0.0954  0.0818  518  PHE A N   
3973  C CA  . PHE A 518  ? 2.5693 4.0629 2.6953 0.6591  0.0830  0.0594  518  PHE A CA  
3974  C C   . PHE A 518  ? 2.6616 4.1424 2.7795 0.7077  0.0802  0.0697  518  PHE A C   
3975  O O   . PHE A 518  ? 2.6344 4.0368 2.7622 0.7179  0.0868  0.1049  518  PHE A O   
3976  C CB  . PHE A 518  ? 2.5690 3.9983 2.7272 0.6019  0.0844  0.0709  518  PHE A CB  
3977  C CG  . PHE A 518  ? 2.5865 4.0607 2.7565 0.5446  0.0759  0.0366  518  PHE A CG  
3978  C CD1 . PHE A 518  ? 2.6152 4.1768 2.7674 0.5464  0.0700  0.0019  518  PHE A CD1 
3979  C CD2 . PHE A 518  ? 2.5740 4.0029 2.7722 0.4884  0.0731  0.0390  518  PHE A CD2 
3980  C CE1 . PHE A 518  ? 2.5994 4.2029 2.7617 0.4933  0.0616  -0.0298 518  PHE A CE1 
3981  C CE2 . PHE A 518  ? 2.5597 4.0294 2.7675 0.4346  0.0643  0.0076  518  PHE A CE2 
3982  C CZ  . PHE A 518  ? 2.5671 4.1243 2.7569 0.4370  0.0587  -0.0268 518  PHE A CZ  
3983  N N   . SER A 519  ? 1.6664 3.2258 1.7672 0.7362  0.0695  0.0376  519  SER A N   
3984  C CA  . SER A 519  ? 1.7847 3.3464 1.8730 0.7908  0.0655  0.0434  519  SER A CA  
3985  C C   . SER A 519  ? 1.8347 3.3151 1.9424 0.7867  0.0678  0.0703  519  SER A C   
3986  O O   . SER A 519  ? 1.8845 3.2882 1.9935 0.8015  0.0787  0.1124  519  SER A O   
3987  C CB  . SER A 519  ? 1.8199 3.4757 1.9009 0.8007  0.0506  -0.0034 519  SER A CB  
3988  O OG  . SER A 519  ? 1.7974 3.5292 1.8626 0.7980  0.0477  -0.0301 519  SER A OG  
3989  N N   . ASP A 520  ? 3.0402 4.5380 3.1631 0.7652  0.0577  0.0456  520  ASP A N   
3990  C CA  . ASP A 520  ? 3.0861 4.5122 3.2272 0.7601  0.0580  0.0665  520  ASP A CA  
3991  C C   . ASP A 520  ? 3.0198 4.3463 3.1727 0.7480  0.0711  0.1143  520  ASP A C   
3992  O O   . ASP A 520  ? 3.0438 4.3258 3.1853 0.7897  0.0792  0.1489  520  ASP A O   
3993  C CB  . ASP A 520  ? 3.1794 4.6240 3.3416 0.7077  0.0490  0.0357  520  ASP A CB  
3994  C CG  . ASP A 520  ? 3.2529 4.7051 3.4274 0.6468  0.0505  0.0247  520  ASP A CG  
3995  O OD1 . ASP A 520  ? 3.2650 4.7261 3.4298 0.6487  0.0572  0.0330  520  ASP A OD1 
3996  O OD2 . ASP A 520  ? 3.2741 4.7226 3.4675 0.5971  0.0446  0.0079  520  ASP A OD2 
3997  N N   . ALA A 521  ? 2.2984 3.5912 2.4746 0.6898  0.0728  0.1157  521  ALA A N   
3998  C CA  . ALA A 521  ? 2.1853 3.3796 2.3801 0.6711  0.0831  0.1583  521  ALA A CA  
3999  C C   . ALA A 521  ? 2.0093 3.1686 2.1952 0.6896  0.0973  0.1921  521  ALA A C   
4000  O O   . ALA A 521  ? 1.9856 3.1978 2.1502 0.7116  0.0997  0.1817  521  ALA A O   
4001  C CB  . ALA A 521  ? 2.1697 3.3408 2.3921 0.6017  0.0796  0.1490  521  ALA A CB  
4002  N N   . SER A 522  ? 2.6237 3.6921 2.8271 0.6788  0.1068  0.2324  522  SER A N   
4003  C CA  . SER A 522  ? 2.5113 3.5292 2.7117 0.6930  0.1222  0.2705  522  SER A CA  
4004  C C   . SER A 522  ? 2.3885 3.4365 2.5902 0.6617  0.1270  0.2588  522  SER A C   
4005  O O   . SER A 522  ? 2.3910 3.5165 2.5727 0.6718  0.1231  0.2296  522  SER A O   
4006  C CB  . SER A 522  ? 2.4801 3.3960 2.7067 0.6739  0.1292  0.3105  522  SER A CB  
4007  O OG  . SER A 522  ? 2.4561 3.3192 2.6836 0.6839  0.1452  0.3484  522  SER A OG  
4008  N N   . TYR A 523  ? 1.7081 2.6920 1.9348 0.6229  0.1349  0.2821  523  TYR A N   
4009  C CA  . TYR A 523  ? 1.5735 2.5669 1.8063 0.5920  0.1414  0.2789  523  TYR A CA  
4010  C C   . TYR A 523  ? 1.5010 2.5718 1.7330 0.5559  0.1295  0.2329  523  TYR A C   
4011  O O   . TYR A 523  ? 1.4922 2.6186 1.7164 0.5575  0.1166  0.2008  523  TYR A O   
4012  C CB  . TYR A 523  ? 1.5279 2.4357 1.7942 0.5513  0.1485  0.3091  523  TYR A CB  
4013  C CG  . TYR A 523  ? 1.5101 2.3867 1.8019 0.5108  0.1373  0.3029  523  TYR A CG  
4014  C CD1 . TYR A 523  ? 1.4731 2.3730 1.7819 0.4538  0.1272  0.2752  523  TYR A CD1 
4015  C CD2 . TYR A 523  ? 1.5180 2.3394 1.8161 0.5284  0.1365  0.3256  523  TYR A CD2 
4016  C CE1 . TYR A 523  ? 1.4590 2.3288 1.7894 0.4154  0.1170  0.2703  523  TYR A CE1 
4017  C CE2 . TYR A 523  ? 1.4950 2.2863 1.8153 0.4907  0.1264  0.3202  523  TYR A CE2 
4018  C CZ  . TYR A 523  ? 1.4775 2.2934 1.8133 0.4340  0.1168  0.2925  523  TYR A CZ  
4019  O OH  . TYR A 523  ? 1.4994 2.2860 1.8552 0.3946  0.1065  0.2865  523  TYR A OH  
4020  N N   . GLN A 524  ? 1.4117 2.4859 1.6523 0.5232  0.1341  0.2299  524  GLN A N   
4021  C CA  . GLN A 524  ? 1.4277 2.5613 1.6735 0.4784  0.1227  0.1901  524  GLN A CA  
4022  C C   . GLN A 524  ? 1.4119 2.5333 1.6692 0.4453  0.1297  0.1946  524  GLN A C   
4023  O O   . GLN A 524  ? 1.4006 2.4889 1.6542 0.4666  0.1442  0.2222  524  GLN A O   
4024  C CB  . GLN A 524  ? 1.4618 2.6926 1.6782 0.5054  0.1141  0.1523  524  GLN A CB  
4025  C CG  . GLN A 524  ? 1.4572 2.7259 1.6502 0.5324  0.1223  0.1512  524  GLN A CG  
4026  C CD  . GLN A 524  ? 1.5345 2.8627 1.6949 0.5889  0.1191  0.1383  524  GLN A CD  
4027  O OE1 . GLN A 524  ? 1.5798 2.8856 1.7349 0.6243  0.1187  0.1528  524  GLN A OE1 
4028  N NE2 . GLN A 524  ? 1.5483 2.9525 1.6871 0.5980  0.1159  0.1107  524  GLN A NE2 
4029  N N   . SER A 525  ? 2.2393 3.3887 2.5107 0.3926  0.1189  0.1663  525  SER A N   
4030  C CA  . SER A 525  ? 2.1979 3.3332 2.4851 0.3534  0.1227  0.1678  525  SER A CA  
4031  C C   . SER A 525  ? 2.2029 3.4032 2.4652 0.3727  0.1268  0.1498  525  SER A C   
4032  O O   . SER A 525  ? 2.2027 3.4799 2.4390 0.3961  0.1197  0.1205  525  SER A O   
4033  C CB  . SER A 525  ? 2.2177 3.3585 2.5278 0.2891  0.1081  0.1439  525  SER A CB  
4034  O OG  . SER A 525  ? 2.2487 3.3426 2.5759 0.2748  0.1022  0.1544  525  SER A OG  
4035  N N   . ILE A 526  ? 1.7910 2.9592 2.0619 0.3637  0.1384  0.1679  526  ILE A N   
4036  C CA  . ILE A 526  ? 1.7365 2.9607 1.9891 0.3685  0.1412  0.1490  526  ILE A CA  
4037  C C   . ILE A 526  ? 1.6701 2.8778 1.9492 0.3104  0.1383  0.1416  526  ILE A C   
4038  O O   . ILE A 526  ? 1.5676 2.7002 1.8765 0.2855  0.1442  0.1689  526  ILE A O   
4039  C CB  . ILE A 526  ? 1.6670 2.8736 1.8998 0.4186  0.1597  0.1767  526  ILE A CB  
4040  C CG1 . ILE A 526  ? 1.6399 2.8564 1.8472 0.4760  0.1616  0.1868  526  ILE A CG1 
4041  C CG2 . ILE A 526  ? 1.6639 2.9326 1.8752 0.4239  0.1616  0.1543  526  ILE A CG2 
4042  C CD1 . ILE A 526  ? 1.6590 2.8725 1.8400 0.5263  0.1773  0.2083  526  ILE A CD1 
4043  N N   . ASN A 527  ? 2.3426 3.6196 2.6119 0.2882  0.1283  0.1046  527  ASN A N   
4044  C CA  . ASN A 527  ? 2.3757 3.6393 2.6697 0.2320  0.1234  0.0955  527  ASN A CA  
4045  C C   . ASN A 527  ? 2.4151 3.7188 2.6972 0.2298  0.1273  0.0804  527  ASN A C   
4046  O O   . ASN A 527  ? 2.4405 3.8199 2.7051 0.2214  0.1164  0.0439  527  ASN A O   
4047  C CB  . ASN A 527  ? 2.4052 3.6934 2.7124 0.1819  0.1038  0.0663  527  ASN A CB  
4048  C CG  . ASN A 527  ? 2.3942 3.6323 2.7362 0.1224  0.0992  0.0719  527  ASN A CG  
4049  O OD1 . ASN A 527  ? 2.3609 3.6002 2.7086 0.1062  0.1027  0.0693  527  ASN A OD1 
4050  N ND2 . ASN A 527  ? 2.4293 3.6208 2.7951 0.0900  0.0911  0.0802  527  ASN A ND2 
4051  N N   . ILE A 528  ? 1.6149 2.8646 1.9089 0.2347  0.1429  0.1090  528  ILE A N   
4052  C CA  . ILE A 528  ? 1.6267 2.9016 1.9118 0.2346  0.1497  0.1003  528  ILE A CA  
4053  C C   . ILE A 528  ? 1.6116 2.8534 1.9307 0.1769  0.1451  0.0975  528  ILE A C   
4054  O O   . ILE A 528  ? 1.5902 2.7549 1.9413 0.1580  0.1513  0.1266  528  ILE A O   
4055  C CB  . ILE A 528  ? 1.6750 2.9193 1.9461 0.2837  0.1717  0.1320  528  ILE A CB  
4056  C CG1 . ILE A 528  ? 1.7246 2.9544 1.9792 0.3323  0.1772  0.1530  528  ILE A CG1 
4057  C CG2 . ILE A 528  ? 1.6795 2.9866 1.9199 0.3049  0.1761  0.1119  528  ILE A CG2 
4058  C CD1 . ILE A 528  ? 1.7345 2.8829 2.0195 0.3205  0.1795  0.1848  528  ILE A CD1 
4059  N N   . PRO A 529  ? 2.0993 3.4004 2.4120 0.1480  0.1329  0.0617  529  PRO A N   
4060  C CA  . PRO A 529  ? 2.0883 3.3736 2.4267 0.0965  0.1273  0.0527  529  PRO A CA  
4061  C C   . PRO A 529  ? 2.0667 3.3023 2.4165 0.1090  0.1463  0.0798  529  PRO A C   
4062  O O   . PRO A 529  ? 2.0933 3.3617 2.4168 0.1447  0.1576  0.0770  529  PRO A O   
4063  C CB  . PRO A 529  ? 2.0813 3.4555 2.3941 0.0895  0.1159  0.0106  529  PRO A CB  
4064  C CG  . PRO A 529  ? 2.1246 3.5549 2.4121 0.1123  0.1070  -0.0077 529  PRO A CG  
4065  C CD  . PRO A 529  ? 2.1382 3.5297 2.4183 0.1618  0.1211  0.0250  529  PRO A CD  
4066  N N   . VAL A 530  ? 1.6502 2.8083 2.0385 0.0803  0.1499  0.1055  530  VAL A N   
4067  C CA  . VAL A 530  ? 1.6070 2.7201 2.0108 0.0855  0.1671  0.1278  530  VAL A CA  
4068  C C   . VAL A 530  ? 1.5717 2.7339 1.9684 0.0649  0.1618  0.0975  530  VAL A C   
4069  O O   . VAL A 530  ? 1.5538 2.7392 1.9617 0.0189  0.1432  0.0712  530  VAL A O   
4070  C CB  . VAL A 530  ? 1.2840 2.3087 1.7347 0.0515  0.1688  0.1568  530  VAL A CB  
4071  C CG1 . VAL A 530  ? 1.2523 2.2733 1.7314 -0.0107 0.1510  0.1367  530  VAL A CG1 
4072  C CG2 . VAL A 530  ? 1.2689 2.2412 1.7318 0.0750  0.1919  0.1890  530  VAL A CG2 
4073  N N   . THR A 531  ? 1.9465 3.1274 2.3223 0.0994  0.1777  0.1001  531  THR A N   
4074  C CA  . THR A 531  ? 1.9481 3.1769 2.3152 0.0821  0.1726  0.0707  531  THR A CA  
4075  C C   . THR A 531  ? 1.9250 3.1033 2.3185 0.0699  0.1862  0.0874  531  THR A C   
4076  O O   . THR A 531  ? 1.9117 3.0376 2.3135 0.0968  0.2065  0.1208  531  THR A O   
4077  C CB  . THR A 531  ? 1.9872 3.2914 2.3058 0.1265  0.1770  0.0515  531  THR A CB  
4078  O OG1 . THR A 531  ? 1.9788 3.3339 2.2896 0.1032  0.1681  0.0186  531  THR A OG1 
4079  C CG2 . THR A 531  ? 2.0035 3.2824 2.3061 0.1779  0.2021  0.0806  531  THR A CG2 
4080  N N   . GLN A 532  ? 1.6200 2.8155 2.0269 0.0289  0.1749  0.0631  532  GLN A N   
4081  C CA  . GLN A 532  ? 1.6237 2.7824 2.0538 0.0171  0.1865  0.0723  532  GLN A CA  
4082  C C   . GLN A 532  ? 1.6471 2.8000 2.0547 0.0717  0.2132  0.0931  532  GLN A C   
4083  O O   . GLN A 532  ? 1.6408 2.7376 2.0727 0.0741  0.2301  0.1179  532  GLN A O   
4084  C CB  . GLN A 532  ? 1.6284 2.8357 2.0561 -0.0180 0.1712  0.0349  532  GLN A CB  
4085  C CG  . GLN A 532  ? 1.6188 2.8011 2.0656 -0.0283 0.1820  0.0373  532  GLN A CG  
4086  C CD  . GLN A 532  ? 1.5848 2.6869 2.0852 -0.0666 0.1815  0.0591  532  GLN A CD  
4087  O OE1 . GLN A 532  ? 1.5937 2.6502 2.1162 -0.0785 0.1772  0.0793  532  GLN A OE1 
4088  N NE2 . GLN A 532  ? 1.5381 2.6223 2.0603 -0.0859 0.1854  0.0550  532  GLN A NE2 
4089  N N   . ASN A 533  ? 1.9351 3.1446 2.2969 0.1154  0.2168  0.0840  533  ASN A N   
4090  C CA  . ASN A 533  ? 1.9534 3.1666 2.2863 0.1680  0.2402  0.1002  533  ASN A CA  
4091  C C   . ASN A 533  ? 1.9410 3.0874 2.2849 0.1972  0.2596  0.1436  533  ASN A C   
4092  O O   . ASN A 533  ? 1.9616 3.1080 2.2799 0.2423  0.2792  0.1600  533  ASN A O   
4093  C CB  . ASN A 533  ? 2.0231 3.3136 2.3040 0.2068  0.2363  0.0797  533  ASN A CB  
4094  C CG  . ASN A 533  ? 2.0664 3.4284 2.3285 0.1889  0.2223  0.0383  533  ASN A CG  
4095  O OD1 . ASN A 533  ? 2.1074 3.5274 2.3514 0.1830  0.2040  0.0114  533  ASN A OD1 
4096  N ND2 . ASN A 533  ? 2.0553 3.4146 2.3218 0.1804  0.2310  0.0323  533  ASN A ND2 
4097  N N   . MET A 534  ? 1.4969 2.5866 1.8772 0.1719  0.2539  0.1623  534  MET A N   
4098  C CA  . MET A 534  ? 1.4572 2.4805 1.8508 0.1966  0.2714  0.2041  534  MET A CA  
4099  C C   . MET A 534  ? 1.3947 2.3470 1.8400 0.1592  0.2759  0.2223  534  MET A C   
4100  O O   . MET A 534  ? 1.3743 2.2601 1.8443 0.1650  0.2874  0.2571  534  MET A O   
4101  C CB  . MET A 534  ? 1.4643 2.4829 1.8539 0.2027  0.2601  0.2109  534  MET A CB  
4102  C CG  . MET A 534  ? 1.4856 2.5862 1.8360 0.2146  0.2445  0.1772  534  MET A CG  
4103  S SD  . MET A 534  ? 1.4507 2.5535 1.8090 0.1959  0.2228  0.1708  534  MET A SD  
4104  C CE  . MET A 534  ? 1.2946 2.3332 1.6534 0.2396  0.2402  0.2173  534  MET A CE  
4105  N N   . VAL A 535  ? 1.5569 2.5256 2.0185 0.1210  0.2664  0.1978  535  VAL A N   
4106  C CA  . VAL A 535  ? 1.5189 2.4279 2.0328 0.0763  0.2639  0.2074  535  VAL A CA  
4107  C C   . VAL A 535  ? 1.5082 2.3357 2.0541 0.0871  0.2837  0.2506  535  VAL A C   
4108  O O   . VAL A 535  ? 1.5135 2.2861 2.0969 0.0591  0.2762  0.2675  535  VAL A O   
4109  C CB  . VAL A 535  ? 1.5085 2.4414 2.0295 0.0526  0.2623  0.1825  535  VAL A CB  
4110  C CG1 . VAL A 535  ? 1.5096 2.4780 2.0379 0.0039  0.2337  0.1476  535  VAL A CG1 
4111  C CG2 . VAL A 535  ? 1.5769 2.5654 2.0521 0.0953  0.2770  0.1701  535  VAL A CG2 
4112  N N   . PRO A 536  ? 1.2562 2.0746 1.7879 0.1268  0.3090  0.2689  536  PRO A N   
4113  C CA  . PRO A 536  ? 1.2128 1.9494 1.7873 0.1214  0.3239  0.3061  536  PRO A CA  
4114  C C   . PRO A 536  ? 1.1804 1.8782 1.7534 0.1448  0.3284  0.3378  536  PRO A C   
4115  O O   . PRO A 536  ? 1.1719 1.8099 1.7846 0.1198  0.3235  0.3582  536  PRO A O   
4116  C CB  . PRO A 536  ? 1.2538 1.9886 1.8189 0.1509  0.3506  0.3155  536  PRO A CB  
4117  C CG  . PRO A 536  ? 1.2860 2.0974 1.8162 0.1522  0.3436  0.2760  536  PRO A CG  
4118  C CD  . PRO A 536  ? 1.2936 2.1584 1.7893 0.1587  0.3238  0.2562  536  PRO A CD  
4119  N N   . SER A 537  ? 1.3430 2.0735 1.8704 0.1926  0.3372  0.3421  537  SER A N   
4120  C CA  . SER A 537  ? 1.3322 2.0337 1.8531 0.2163  0.3386  0.3681  537  SER A CA  
4121  C C   . SER A 537  ? 1.3821 2.1527 1.8480 0.2533  0.3332  0.3497  537  SER A C   
4122  O O   . SER A 537  ? 1.4023 2.2388 1.8452 0.2462  0.3215  0.3141  537  SER A O   
4123  C CB  . SER A 537  ? 1.2932 1.9313 1.8272 0.2440  0.3646  0.4110  537  SER A CB  
4124  O OG  . SER A 537  ? 1.3032 1.9702 1.7958 0.2920  0.3844  0.4159  537  SER A OG  
4125  N N   . SER A 538  ? 1.4397 2.1953 1.8858 0.2918  0.3406  0.3734  538  SER A N   
4126  C CA  . SER A 538  ? 1.4084 2.2251 1.8043 0.3296  0.3348  0.3586  538  SER A CA  
4127  C C   . SER A 538  ? 1.4336 2.2124 1.8211 0.3642  0.3416  0.3912  538  SER A C   
4128  O O   . SER A 538  ? 1.4237 2.1385 1.8462 0.3472  0.3415  0.4161  538  SER A O   
4129  C CB  . SER A 538  ? 1.3884 2.2614 1.7775 0.3019  0.3074  0.3202  538  SER A CB  
4130  O OG  . SER A 538  ? 1.3280 2.2561 1.7081 0.2825  0.3005  0.2854  538  SER A OG  
4131  N N   . ARG A 539  ? 1.1656 1.9819 1.5068 0.4131  0.3476  0.3921  539  ARG A N   
4132  C CA  . ARG A 539  ? 1.1840 1.9822 1.5113 0.4442  0.3462  0.4126  539  ARG A CA  
4133  C C   . ARG A 539  ? 1.1911 2.0657 1.4756 0.4674  0.3310  0.3829  539  ARG A C   
4134  O O   . ARG A 539  ? 1.1949 2.1340 1.4555 0.4683  0.3263  0.3521  539  ARG A O   
4135  C CB  . ARG A 539  ? 1.2238 1.9766 1.5389 0.4873  0.3704  0.4529  539  ARG A CB  
4136  C CG  . ARG A 539  ? 1.2395 1.9780 1.5560 0.4933  0.3933  0.4643  539  ARG A CG  
4137  C CD  . ARG A 539  ? 1.2839 1.9858 1.5798 0.5405  0.4164  0.5029  539  ARG A CD  
4138  N NE  . ARG A 539  ? 1.2848 1.9064 1.6152 0.5353  0.4241  0.5414  539  ARG A NE  
4139  C CZ  . ARG A 539  ? 1.2805 1.8429 1.6491 0.5164  0.4404  0.5652  539  ARG A CZ  
4140  N NH1 . ARG A 539  ? 1.2749 1.8479 1.6531 0.5008  0.4512  0.5542  539  ARG A NH1 
4141  N NH2 . ARG A 539  ? 1.2818 1.7741 1.6804 0.5128  0.4456  0.5996  539  ARG A NH2 
4142  N N   . LEU A 540  ? 1.1978 2.0644 1.4752 0.4848  0.3225  0.3917  540  LEU A N   
4143  C CA  . LEU A 540  ? 1.2104 2.1433 1.4475 0.5149  0.3101  0.3691  540  LEU A CA  
4144  C C   . LEU A 540  ? 1.2406 2.1405 1.4638 0.5563  0.3152  0.3989  540  LEU A C   
4145  O O   . LEU A 540  ? 1.2449 2.0721 1.4948 0.5521  0.3237  0.4327  540  LEU A O   
4146  C CB  . LEU A 540  ? 1.2043 2.1800 1.4510 0.4794  0.2852  0.3331  540  LEU A CB  
4147  C CG  . LEU A 540  ? 1.2461 2.1838 1.5236 0.4512  0.2715  0.3383  540  LEU A CG  
4148  C CD1 . LEU A 540  ? 1.3030 2.1748 1.5871 0.4774  0.2802  0.3780  540  LEU A CD1 
4149  C CD2 . LEU A 540  ? 1.2646 2.2719 1.5244 0.4466  0.2499  0.3008  540  LEU A CD2 
4150  N N   . LEU A 541  ? 1.5731 2.5276 1.7553 0.5957  0.3087  0.3856  541  LEU A N   
4151  C CA  . LEU A 541  ? 1.6296 2.5618 1.7923 0.6404  0.3121  0.4108  541  LEU A CA  
4152  C C   . LEU A 541  ? 1.7181 2.7218 1.8514 0.6600  0.2932  0.3798  541  LEU A C   
4153  O O   . LEU A 541  ? 1.7080 2.7793 1.8305 0.6454  0.2817  0.3423  541  LEU A O   
4154  C CB  . LEU A 541  ? 1.6320 2.5476 1.7677 0.6819  0.3338  0.4378  541  LEU A CB  
4155  C CG  . LEU A 541  ? 1.7358 2.6752 1.8257 0.7402  0.3354  0.4469  541  LEU A CG  
4156  C CD1 . LEU A 541  ? 1.7186 2.6084 1.7960 0.7705  0.3601  0.4866  541  LEU A CD1 
4157  C CD2 . LEU A 541  ? 1.7550 2.7850 1.8074 0.7552  0.3243  0.4083  541  LEU A CD2 
4158  N N   . VAL A 542  ? 1.3209 2.3104 1.4420 0.6931  0.2894  0.3948  542  VAL A N   
4159  C CA  . VAL A 542  ? 1.3249 2.3737 1.4299 0.7029  0.2692  0.3649  542  VAL A CA  
4160  C C   . VAL A 542  ? 1.4565 2.4972 1.5346 0.7564  0.2697  0.3843  542  VAL A C   
4161  O O   . VAL A 542  ? 1.4651 2.4427 1.5588 0.7630  0.2733  0.4141  542  VAL A O   
4162  C CB  . VAL A 542  ? 1.2776 2.3100 1.4191 0.6580  0.2547  0.3527  542  VAL A CB  
4163  C CG1 . VAL A 542  ? 1.3043 2.3726 1.4323 0.6775  0.2379  0.3358  542  VAL A CG1 
4164  C CG2 . VAL A 542  ? 1.2384 2.3057 1.3976 0.6074  0.2471  0.3207  542  VAL A CG2 
4165  N N   . TYR A 543  ? 1.7369 2.8416 1.7745 0.7944  0.2652  0.3671  543  TYR A N   
4166  C CA  . TYR A 543  ? 1.8514 2.9528 1.8589 0.8493  0.2654  0.3851  543  TYR A CA  
4167  C C   . TYR A 543  ? 1.9058 3.0746 1.8964 0.8667  0.2444  0.3525  543  TYR A C   
4168  O O   . TYR A 543  ? 1.8961 3.1367 1.8787 0.8527  0.2331  0.3139  543  TYR A O   
4169  C CB  . TYR A 543  ? 1.9094 3.0193 1.8801 0.8874  0.2804  0.4003  543  TYR A CB  
4170  C CG  . TYR A 543  ? 1.9354 3.1271 1.8792 0.8888  0.2754  0.3646  543  TYR A CG  
4171  C CD1 . TYR A 543  ? 1.9055 3.1055 1.8609 0.8536  0.2833  0.3531  543  TYR A CD1 
4172  C CD2 . TYR A 543  ? 1.9928 3.2524 1.8998 0.9263  0.2625  0.3430  543  TYR A CD2 
4173  C CE1 . TYR A 543  ? 1.9124 3.1854 1.8426 0.8550  0.2786  0.3209  543  TYR A CE1 
4174  C CE2 . TYR A 543  ? 1.9971 3.3306 1.8794 0.9277  0.2576  0.3110  543  TYR A CE2 
4175  C CZ  . TYR A 543  ? 1.9439 3.2834 1.8375 0.8917  0.2657  0.3002  543  TYR A CZ  
4176  O OH  . TYR A 543  ? 1.9218 3.3333 1.7910 0.8922  0.2604  0.2684  543  TYR A OH  
4177  N N   . TYR A 544  ? 2.1361 3.2808 2.1228 0.8965  0.2390  0.3681  544  TYR A N   
4178  C CA  . TYR A 544  ? 2.1987 3.4045 2.1649 0.9252  0.2208  0.3421  544  TYR A CA  
4179  C C   . TYR A 544  ? 2.2692 3.4725 2.1967 0.9863  0.2255  0.3644  544  TYR A C   
4180  O O   . TYR A 544  ? 2.2899 3.4234 2.2177 1.0054  0.2379  0.4051  544  TYR A O   
4181  C CB  . TYR A 544  ? 2.2065 3.3896 2.1995 0.9105  0.2086  0.3387  544  TYR A CB  
4182  C CG  . TYR A 544  ? 2.2269 3.3223 2.2312 0.9263  0.2178  0.3830  544  TYR A CG  
4183  C CD1 . TYR A 544  ? 2.1891 3.2128 2.2098 0.9107  0.2361  0.4182  544  TYR A CD1 
4184  C CD2 . TYR A 544  ? 2.2665 3.3509 2.2663 0.9567  0.2080  0.3892  544  TYR A CD2 
4185  C CE1 . TYR A 544  ? 2.2080 3.1522 2.2397 0.9240  0.2445  0.4587  544  TYR A CE1 
4186  C CE2 . TYR A 544  ? 2.2805 3.2834 2.2906 0.9705  0.2159  0.4300  544  TYR A CE2 
4187  C CZ  . TYR A 544  ? 2.2558 3.1891 2.2815 0.9537  0.2342  0.4649  544  TYR A CZ  
4188  O OH  . TYR A 544  ? 2.2787 3.1312 2.3154 0.9661  0.2422  0.5057  544  TYR A OH  
4189  N N   . ILE A 545  ? 1.7398 3.0189 1.6341 1.0157  0.2153  0.3381  545  ILE A N   
4190  C CA  . ILE A 545  ? 1.7964 3.0831 1.6503 1.0741  0.2170  0.3549  545  ILE A CA  
4191  C C   . ILE A 545  ? 1.8624 3.1384 1.7140 1.1076  0.2042  0.3612  545  ILE A C   
4192  O O   . ILE A 545  ? 1.8529 3.1861 1.7056 1.1104  0.1859  0.3279  545  ILE A O   
4193  C CB  . ILE A 545  ? 1.7650 3.1374 1.5837 1.0917  0.2105  0.3240  545  ILE A CB  
4194  C CG1 . ILE A 545  ? 1.6721 3.0658 1.5008 1.0483  0.2181  0.3063  545  ILE A CG1 
4195  C CG2 . ILE A 545  ? 1.8593 3.2244 1.6357 1.1446  0.2181  0.3492  545  ILE A CG2 
4196  C CD1 . ILE A 545  ? 1.5503 3.0350 1.3524 1.0540  0.2081  0.2675  545  ILE A CD1 
4197  N N   . VAL A 546  ? 2.2434 3.4453 2.0933 1.1316  0.2142  0.4040  546  VAL A N   
4198  C CA  . VAL A 546  ? 2.3654 3.5409 2.2154 1.1631  0.2043  0.4173  546  VAL A CA  
4199  C C   . VAL A 546  ? 2.5910 3.7872 2.3981 1.2242  0.1995  0.4270  546  VAL A C   
4200  O O   . VAL A 546  ? 2.6351 3.7975 2.4182 1.2489  0.2133  0.4588  546  VAL A O   
4201  C CB  . VAL A 546  ? 2.2779 3.3538 2.1529 1.1531  0.2169  0.4606  546  VAL A CB  
4202  C CG1 . VAL A 546  ? 2.3313 3.3725 2.1923 1.2004  0.2110  0.4852  546  VAL A CG1 
4203  C CG2 . VAL A 546  ? 2.1996 3.2539 2.1193 1.0999  0.2137  0.4488  546  VAL A CG2 
4204  N N   . THR A 547  ? 2.3228 3.5744 2.1210 1.2480  0.1797  0.3995  547  THR A N   
4205  C CA  . THR A 547  ? 2.5765 3.8500 2.3369 1.3065  0.1711  0.4058  547  THR A CA  
4206  C C   . THR A 547  ? 2.8119 4.0199 2.5760 1.3361  0.1688  0.4383  547  THR A C   
4207  O O   . THR A 547  ? 2.8643 4.0932 2.6341 1.3535  0.1518  0.4222  547  THR A O   
4208  C CB  . THR A 547  ? 2.5978 3.9674 2.3478 1.3200  0.1496  0.3585  547  THR A CB  
4209  O OG1 . THR A 547  ? 2.5389 3.9695 2.2829 1.2942  0.1513  0.3293  547  THR A OG1 
4210  C CG2 . THR A 547  ? 2.7001 4.0921 2.4123 1.3814  0.1390  0.3650  547  THR A CG2 
4211  N N   . GLY A 548  ? 3.8521 4.9806 3.6141 1.3411  0.1860  0.4837  548  GLY A N   
4212  C CA  . GLY A 548  ? 4.0922 5.1595 3.8492 1.3763  0.1842  0.5180  548  GLY A CA  
4213  C C   . GLY A 548  ? 4.3802 5.4910 4.0962 1.4329  0.1709  0.5131  548  GLY A C   
4214  O O   . GLY A 548  ? 4.4282 5.5888 4.1145 1.4457  0.1720  0.5016  548  GLY A O   
4215  N N   . GLU A 549  ? 4.2968 5.3897 4.0109 1.4668  0.1574  0.5211  549  GLU A N   
4216  C CA  . GLU A 549  ? 4.5216 5.6571 4.1991 1.5213  0.1420  0.5147  549  GLU A CA  
4217  C C   . GLU A 549  ? 4.5900 5.7036 4.2262 1.5518  0.1538  0.5475  549  GLU A C   
4218  O O   . GLU A 549  ? 4.6389 5.7794 4.2574 1.5590  0.1369  0.5273  549  GLU A O   
4219  C CB  . GLU A 549  ? 4.6853 5.7845 4.3769 1.5408  0.1237  0.5182  549  GLU A CB  
4220  C CG  . GLU A 549  ? 4.7786 5.7513 4.4948 1.5142  0.1233  0.5546  549  GLU A CG  
4221  C CD  . GLU A 549  ? 4.7947 5.7316 4.5292 1.5044  0.1454  0.5815  549  GLU A CD  
4222  O OE1 . GLU A 549  ? 4.7572 5.7384 4.5118 1.4787  0.1475  0.5556  549  GLU A OE1 
4223  O OE2 . GLU A 549  ? 4.8297 5.6821 4.5698 1.5041  0.1553  0.6226  549  GLU A OE2 
4224  N N   . GLN A 550  ? 4.3660 5.4053 4.0071 1.5358  0.1751  0.5867  550  GLN A N   
4225  C CA  . GLN A 550  ? 4.3865 5.3967 3.9893 1.5623  0.1888  0.6215  550  GLN A CA  
4226  C C   . GLN A 550  ? 4.2447 5.2969 3.8311 1.5432  0.2014  0.6082  550  GLN A C   
4227  O O   . GLN A 550  ? 4.3271 5.4028 3.8716 1.5743  0.2022  0.6142  550  GLN A O   
4228  C CB  . GLN A 550  ? 4.4356 5.3457 4.0486 1.5582  0.2066  0.6722  550  GLN A CB  
4229  C CG  . GLN A 550  ? 4.3592 5.2298 4.0102 1.5035  0.2258  0.6792  550  GLN A CG  
4230  C CD  . GLN A 550  ? 4.3133 5.1641 4.0103 1.4733  0.2178  0.6670  550  GLN A CD  
4231  O OE1 . GLN A 550  ? 4.3611 5.2196 4.0619 1.4949  0.1995  0.6573  550  GLN A OE1 
4232  N NE2 . GLN A 550  ? 4.2151 5.0395 3.9474 1.4231  0.2311  0.6672  550  GLN A NE2 
4233  N N   . THR A 551  ? 4.2234 5.2847 3.8419 1.4921  0.2105  0.5899  551  THR A N   
4234  C CA  . THR A 551  ? 4.0653 5.1564 3.6719 1.4704  0.2245  0.5804  551  THR A CA  
4235  C C   . THR A 551  ? 3.8048 4.9257 3.4490 1.4152  0.2261  0.5476  551  THR A C   
4236  O O   . THR A 551  ? 3.7392 4.8255 3.4236 1.3840  0.2261  0.5481  551  THR A O   
4237  C CB  . THR A 551  ? 4.0961 5.1157 3.6925 1.4690  0.2500  0.6259  551  THR A CB  
4238  O OG1 . THR A 551  ? 4.2281 5.2219 3.7848 1.5198  0.2490  0.6570  551  THR A OG1 
4239  C CG2 . THR A 551  ? 4.0552 5.1056 3.6406 1.4458  0.2650  0.6145  551  THR A CG2 
4240  N N   . ALA A 552  ? 4.1508 5.3348 3.7808 1.4030  0.2269  0.5193  552  ALA A N   
4241  C CA  . ALA A 552  ? 3.9038 5.1180 3.5654 1.3503  0.2289  0.4884  552  ALA A CA  
4242  C C   . ALA A 552  ? 3.6806 4.8214 3.3724 1.3119  0.2508  0.5164  552  ALA A C   
4243  O O   . ALA A 552  ? 3.6740 4.7865 3.3497 1.3140  0.2697  0.5403  552  ALA A O   
4244  C CB  . ALA A 552  ? 3.9012 5.1899 3.5364 1.3489  0.2277  0.4588  552  ALA A CB  
4245  N N   . GLU A 553  ? 2.7286 3.8386 2.4639 1.2768  0.2481  0.5134  553  GLU A N   
4246  C CA  . GLU A 553  ? 2.5174 3.5554 2.2854 1.2394  0.2670  0.5401  553  GLU A CA  
4247  C C   . GLU A 553  ? 2.3274 3.3875 2.1300 1.1826  0.2680  0.5115  553  GLU A C   
4248  O O   . GLU A 553  ? 2.2687 3.3564 2.0954 1.1591  0.2529  0.4830  553  GLU A O   
4249  C CB  . GLU A 553  ? 2.4585 3.4219 2.2503 1.2429  0.2668  0.5706  553  GLU A CB  
4250  C CG  . GLU A 553  ? 2.4177 3.2958 2.2210 1.2336  0.2901  0.6163  553  GLU A CG  
4251  C CD  . GLU A 553  ? 2.3421 3.1533 2.1903 1.2030  0.2917  0.6332  553  GLU A CD  
4252  O OE1 . GLU A 553  ? 2.2744 3.1021 2.1557 1.1604  0.2849  0.6072  553  GLU A OE1 
4253  O OE2 . GLU A 553  ? 2.3585 3.0998 2.2084 1.2205  0.2996  0.6731  553  GLU A OE2 
4254  N N   . LEU A 554  ? 2.0814 3.1296 1.8855 1.1607  0.2857  0.5189  554  LEU A N   
4255  C CA  . LEU A 554  ? 1.9539 3.0081 1.7939 1.1051  0.2884  0.4986  554  LEU A CA  
4256  C C   . LEU A 554  ? 1.8862 2.8565 1.7681 1.0764  0.2977  0.5281  554  LEU A C   
4257  O O   . LEU A 554  ? 1.9203 2.8251 1.7993 1.0968  0.3104  0.5689  554  LEU A O   
4258  C CB  . LEU A 554  ? 1.9345 3.0113 1.7613 1.0922  0.3029  0.4924  554  LEU A CB  
4259  C CG  . LEU A 554  ? 1.9484 3.1147 1.7584 1.0829  0.2922  0.4470  554  LEU A CG  
4260  C CD1 . LEU A 554  ? 1.9003 3.0695 1.7128 1.0552  0.3082  0.4434  554  LEU A CD1 
4261  C CD2 . LEU A 554  ? 1.9290 3.1394 1.7646 1.0527  0.2715  0.4086  554  LEU A CD2 
4262  N N   . VAL A 555  ? 2.6226 3.5954 2.5430 1.0284  0.2908  0.5072  555  VAL A N   
4263  C CA  . VAL A 555  ? 2.5537 3.4507 2.5168 0.9950  0.2979  0.5313  555  VAL A CA  
4264  C C   . VAL A 555  ? 2.4146 3.3230 2.4127 0.9370  0.2966  0.5074  555  VAL A C   
4265  O O   . VAL A 555  ? 2.3776 3.3519 2.3750 0.9196  0.2816  0.4669  555  VAL A O   
4266  C CB  . VAL A 555  ? 2.6007 3.4718 2.5775 1.0032  0.2840  0.5367  555  VAL A CB  
4267  C CG1 . VAL A 555  ? 2.5606 3.3688 2.5849 0.9579  0.2866  0.5496  555  VAL A CG1 
4268  C CG2 . VAL A 555  ? 2.6770 3.5102 2.6279 1.0551  0.2887  0.5717  555  VAL A CG2 
4269  N N   . SER A 556  ? 1.5329 2.3771 1.5620 0.9069  0.3118  0.5323  556  SER A N   
4270  C CA  . SER A 556  ? 1.4590 2.3067 1.5241 0.8507  0.3097  0.5121  556  SER A CA  
4271  C C   . SER A 556  ? 1.5705 2.3363 1.6799 0.8143  0.3216  0.5412  556  SER A C   
4272  O O   . SER A 556  ? 1.4863 2.1839 1.6029 0.8301  0.3331  0.5807  556  SER A O   
4273  C CB  . SER A 556  ? 1.5562 2.4635 1.6042 0.8423  0.3135  0.4859  556  SER A CB  
4274  O OG  . SER A 556  ? 1.5145 2.3876 1.5933 0.8019  0.3259  0.4928  556  SER A OG  
4275  N N   . ASP A 557  ? 2.1218 2.8970 2.2614 0.7641  0.3171  0.5197  557  ASP A N   
4276  C CA  . ASP A 557  ? 2.0003 2.7092 2.1825 0.7248  0.3278  0.5409  557  ASP A CA  
4277  C C   . ASP A 557  ? 1.8871 2.6318 2.0854 0.6813  0.3250  0.5108  557  ASP A C   
4278  O O   . ASP A 557  ? 1.8503 2.6692 2.0264 0.6819  0.3147  0.4746  557  ASP A O   
4279  C CB  . ASP A 557  ? 2.0068 2.6611 2.2231 0.7024  0.3184  0.5540  557  ASP A CB  
4280  C CG  . ASP A 557  ? 1.9873 2.5650 2.2477 0.6666  0.3303  0.5819  557  ASP A CG  
4281  O OD1 . ASP A 557  ? 2.0081 2.5582 2.2682 0.6763  0.3502  0.6052  557  ASP A OD1 
4282  O OD2 . ASP A 557  ? 1.9457 2.4914 2.2411 0.6289  0.3197  0.5804  557  ASP A OD2 
4283  N N   . SER A 558  ? 1.6269 2.3181 1.8647 0.6434  0.3337  0.5259  558  SER A N   
4284  C CA  . SER A 558  ? 1.5874 2.3032 1.8408 0.6055  0.3344  0.5032  558  SER A CA  
4285  C C   . SER A 558  ? 1.5367 2.1846 1.8412 0.5602  0.3381  0.5207  558  SER A C   
4286  O O   . SER A 558  ? 1.5292 2.1084 1.8534 0.5647  0.3456  0.5556  558  SER A O   
4287  C CB  . SER A 558  ? 1.6118 2.3407 1.8410 0.6309  0.3540  0.5112  558  SER A CB  
4288  O OG  . SER A 558  ? 1.6286 2.2837 1.8740 0.6403  0.3747  0.5539  558  SER A OG  
4289  N N   . VAL A 559  ? 2.0124 2.6782 2.3390 0.5168  0.3327  0.4972  559  VAL A N   
4290  C CA  . VAL A 559  ? 1.9504 2.5526 2.3270 0.4724  0.3354  0.5128  559  VAL A CA  
4291  C C   . VAL A 559  ? 1.9459 2.5575 2.3370 0.4471  0.3439  0.5020  559  VAL A C   
4292  O O   . VAL A 559  ? 1.9900 2.6661 2.3550 0.4528  0.3420  0.4732  559  VAL A O   
4293  C CB  . VAL A 559  ? 1.8564 2.4550 2.2592 0.4299  0.3129  0.4952  559  VAL A CB  
4294  C CG1 . VAL A 559  ? 1.8339 2.3939 2.2373 0.4473  0.3078  0.5165  559  VAL A CG1 
4295  C CG2 . VAL A 559  ? 1.7880 2.4705 2.1681 0.4192  0.2949  0.4490  559  VAL A CG2 
4296  N N   . TRP A 560  ? 2.0512 2.5972 2.4851 0.4195  0.3532  0.5253  560  TRP A N   
4297  C CA  . TRP A 560  ? 2.0103 2.5598 2.4661 0.3885  0.3587  0.5135  560  TRP A CA  
4298  C C   . TRP A 560  ? 1.9261 2.4766 2.4156 0.3322  0.3368  0.4900  560  TRP A C   
4299  O O   . TRP A 560  ? 1.9286 2.4397 2.4417 0.3121  0.3254  0.5002  560  TRP A O   
4300  C CB  . TRP A 560  ? 2.0832 2.5652 2.5667 0.3915  0.3823  0.5506  560  TRP A CB  
4301  C CG  . TRP A 560  ? 2.1268 2.6161 2.6307 0.3640  0.3888  0.5371  560  TRP A CG  
4302  C CD1 . TRP A 560  ? 2.1793 2.7089 2.6578 0.3830  0.4023  0.5253  560  TRP A CD1 
4303  C CD2 . TRP A 560  ? 2.1178 2.5741 2.6715 0.3117  0.3807  0.5324  560  TRP A CD2 
4304  N NE1 . TRP A 560  ? 2.1559 2.6793 2.6664 0.3460  0.4036  0.5131  560  TRP A NE1 
4305  C CE2 . TRP A 560  ? 2.1111 2.5897 2.6686 0.3018  0.3900  0.5174  560  TRP A CE2 
4306  C CE3 . TRP A 560  ? 2.1237 2.5328 2.7190 0.2719  0.3658  0.5395  560  TRP A CE3 
4307  C CZ2 . TRP A 560  ? 2.0779 2.5326 2.6807 0.2542  0.3845  0.5094  560  TRP A CZ2 
4308  C CZ3 . TRP A 560  ? 2.0994 2.4842 2.7389 0.2242  0.3602  0.5325  560  TRP A CZ3 
4309  C CH2 . TRP A 560  ? 2.0664 2.4739 2.7101 0.2159  0.3693  0.5176  560  TRP A CH2 
4310  N N   . LEU A 561  ? 1.0972 1.6912 1.5881 0.3063  0.3307  0.4589  561  LEU A N   
4311  C CA  . LEU A 561  ? 1.0591 1.6736 1.5698 0.2559  0.3064  0.4285  561  LEU A CA  
4312  C C   . LEU A 561  ? 1.0313 1.6299 1.5803 0.2072  0.3030  0.4178  561  LEU A C   
4313  O O   . LEU A 561  ? 1.0170 1.6719 1.5549 0.1892  0.2927  0.3831  561  LEU A O   
4314  C CB  . LEU A 561  ? 1.0567 1.7592 1.5270 0.2644  0.2923  0.3882  561  LEU A CB  
4315  C CG  . LEU A 561  ? 1.0745 1.8197 1.5046 0.3019  0.2856  0.3805  561  LEU A CG  
4316  C CD1 . LEU A 561  ? 1.0563 1.8833 1.4650 0.2855  0.2659  0.3343  561  LEU A CD1 
4317  C CD2 . LEU A 561  ? 1.0723 1.7679 1.5190 0.2990  0.2787  0.4016  561  LEU A CD2 
4318  N N   . ASN A 562  ? 1.3260 1.8502 1.9205 0.1842  0.3096  0.4457  562  ASN A N   
4319  C CA  . ASN A 562  ? 1.2988 1.8066 1.9304 0.1419  0.3077  0.4369  562  ASN A CA  
4320  C C   . ASN A 562  ? 1.2573 1.8054 1.8924 0.0982  0.2815  0.3998  562  ASN A C   
4321  O O   . ASN A 562  ? 1.2727 1.8292 1.9024 0.0865  0.2642  0.3915  562  ASN A O   
4322  C CB  . ASN A 562  ? 1.2379 1.6594 1.9230 0.1171  0.3136  0.4700  562  ASN A CB  
4323  C CG  . ASN A 562  ? 1.3987 1.8044 2.1192 0.0856  0.3178  0.4642  562  ASN A CG  
4324  O OD1 . ASN A 562  ? 1.3646 1.8088 2.0868 0.0539  0.3024  0.4316  562  ASN A OD1 
4325  N ND2 . ASN A 562  ? 1.3951 1.7447 2.1440 0.0944  0.3388  0.4955  562  ASN A ND2 
4326  N N   . ILE A 563  ? 1.1723 1.7480 1.8141 0.0751  0.2788  0.3764  563  ILE A N   
4327  C CA  . ILE A 563  ? 1.1617 1.7729 1.8083 0.0309  0.2535  0.3421  563  ILE A CA  
4328  C C   . ILE A 563  ? 1.1767 1.7709 1.8603 -0.0132 0.2486  0.3316  563  ILE A C   
4329  O O   . ILE A 563  ? 1.1767 1.7346 1.8822 -0.0070 0.2664  0.3498  563  ILE A O   
4330  C CB  . ILE A 563  ? 1.1554 1.8541 1.7518 0.0508  0.2450  0.3078  563  ILE A CB  
4331  C CG1 . ILE A 563  ? 1.1457 1.8939 1.7343 0.0356  0.2419  0.2766  563  ILE A CG1 
4332  C CG2 . ILE A 563  ? 1.2526 1.9716 1.8085 0.1116  0.2623  0.3215  563  ILE A CG2 
4333  C CD1 . ILE A 563  ? 1.1769 2.0117 1.7197 0.0494  0.2308  0.2411  563  ILE A CD1 
4334  N N   . GLU A 564  ? 1.7478 2.3684 2.4381 -0.0580 0.2240  0.3019  564  GLU A N   
4335  C CA  . GLU A 564  ? 1.7493 2.3514 2.4768 -0.1066 0.2136  0.2902  564  GLU A CA  
4336  C C   . GLU A 564  ? 1.7846 2.4194 2.5030 -0.0949 0.2258  0.2755  564  GLU A C   
4337  O O   . GLU A 564  ? 1.8129 2.5170 2.4897 -0.0733 0.2261  0.2502  564  GLU A O   
4338  C CB  . GLU A 564  ? 1.7656 2.3979 2.4939 -0.1546 0.1838  0.2591  564  GLU A CB  
4339  C CG  . GLU A 564  ? 1.8055 2.5287 2.4878 -0.1456 0.1745  0.2197  564  GLU A CG  
4340  C CD  . GLU A 564  ? 1.8424 2.5913 2.5353 -0.2012 0.1482  0.1871  564  GLU A CD  
4341  O OE1 . GLU A 564  ? 1.8703 2.6879 2.5299 -0.2034 0.1352  0.1555  564  GLU A OE1 
4342  O OE2 . GLU A 564  ? 1.8374 2.5378 2.5725 -0.2432 0.1401  0.1929  564  GLU A OE2 
4343  N N   . GLU A 565  ? 1.2126 1.7976 1.9710 -0.1100 0.2353  0.2904  565  GLU A N   
4344  C CA  . GLU A 565  ? 1.2720 1.8821 2.0245 -0.0980 0.2490  0.2783  565  GLU A CA  
4345  C C   . GLU A 565  ? 1.2505 1.9050 2.0028 -0.1374 0.2279  0.2392  565  GLU A C   
4346  O O   . GLU A 565  ? 1.2107 1.8475 1.9925 -0.1610 0.2284  0.2337  565  GLU A O   
4347  C CB  . GLU A 565  ? 1.3377 1.8798 2.1332 -0.0969 0.2686  0.3085  565  GLU A CB  
4348  C CG  . GLU A 565  ? 1.4207 1.9195 2.2150 -0.0591 0.2884  0.3475  565  GLU A CG  
4349  C CD  . GLU A 565  ? 1.4578 1.8878 2.2976 -0.0605 0.3071  0.3783  565  GLU A CD  
4350  O OE1 . GLU A 565  ? 1.4477 1.8624 2.3222 -0.0920 0.3034  0.3689  565  GLU A OE1 
4351  O OE2 . GLU A 565  ? 1.4823 1.8737 2.3237 -0.0302 0.3251  0.4117  565  GLU A OE2 
4352  N N   . LYS A 566  ? 1.3225 2.0348 2.0421 -0.1444 0.2092  0.2120  566  LYS A N   
4353  C CA  . LYS A 566  ? 1.3433 2.1090 2.0534 -0.1767 0.1895  0.1726  566  LYS A CA  
4354  C C   . LYS A 566  ? 1.3648 2.1793 2.0459 -0.1462 0.2046  0.1563  566  LYS A C   
4355  O O   . LYS A 566  ? 1.3670 2.2223 2.0057 -0.0999 0.2177  0.1559  566  LYS A O   
4356  C CB  . LYS A 566  ? 1.3601 2.1791 2.0386 -0.1853 0.1688  0.1493  566  LYS A CB  
4357  C CG  . LYS A 566  ? 1.3623 2.2303 2.0360 -0.2286 0.1438  0.1096  566  LYS A CG  
4358  C CD  . LYS A 566  ? 1.3996 2.2989 2.0561 -0.2470 0.1224  0.0941  566  LYS A CD  
4359  C CE  . LYS A 566  ? 1.4253 2.3694 2.0788 -0.2950 0.0962  0.0562  566  LYS A CE  
4360  N NZ  . LYS A 566  ? 1.4352 2.4688 2.0412 -0.2743 0.0934  0.0228  566  LYS A NZ  
4361  N N   . CYS A 567  ? 1.8990 2.9216 2.4288 0.4397  -0.0076 0.2821  567  CYS A N   
4362  C CA  . CYS A 567  ? 1.9166 2.9869 2.4339 0.4299  -0.0115 0.2873  567  CYS A CA  
4363  C C   . CYS A 567  ? 1.9373 3.0426 2.4477 0.4214  -0.0119 0.2901  567  CYS A C   
4364  O O   . CYS A 567  ? 1.9438 3.0343 2.4560 0.4219  -0.0093 0.2851  567  CYS A O   
4365  C CB  . CYS A 567  ? 1.9379 2.9904 2.4223 0.4191  -0.0170 0.2642  567  CYS A CB  
4366  S SG  . CYS A 567  ? 2.7416 3.7667 3.2321 0.4268  -0.0175 0.2623  567  CYS A SG  
4367  N N   . GLY A 568  ? 1.7981 2.9509 2.3007 0.4131  -0.0150 0.2982  568  GLY A N   
4368  C CA  . GLY A 568  ? 1.8199 3.0092 2.3149 0.4040  -0.0162 0.3015  568  GLY A CA  
4369  C C   . GLY A 568  ? 1.8384 3.0046 2.2963 0.3897  -0.0205 0.2737  568  GLY A C   
4370  O O   . GLY A 568  ? 1.8513 2.9987 2.3040 0.3873  -0.0192 0.2644  568  GLY A O   
4371  N N   . ASN A 569  ? 2.0984 3.2659 2.5304 0.3799  -0.0259 0.2600  569  ASN A N   
4372  C CA  . ASN A 569  ? 2.1135 3.2543 2.5100 0.3665  -0.0312 0.2324  569  ASN A CA  
4373  C C   . ASN A 569  ? 2.0884 3.1694 2.4758 0.3697  -0.0322 0.2123  569  ASN A C   
4374  O O   . ASN A 569  ? 2.1012 3.1712 2.4901 0.3739  -0.0330 0.2101  569  ASN A O   
4375  C CB  . ASN A 569  ? 2.1396 3.3120 2.5120 0.3537  -0.0373 0.2259  569  ASN A CB  
4376  C CG  . ASN A 569  ? 2.1685 3.3800 2.5308 0.3427  -0.0396 0.2302  569  ASN A CG  
4377  O OD1 . ASN A 569  ? 2.1778 3.3837 2.5434 0.3419  -0.0377 0.2306  569  ASN A OD1 
4378  N ND2 . ASN A 569  ? 2.1762 3.4282 2.5261 0.3338  -0.0435 0.2331  569  ASN A ND2 
4379  N N   . GLN A 570  ? 3.1108 4.1538 3.4893 0.3673  -0.0320 0.1980  570  GLN A N   
4380  C CA  . GLN A 570  ? 3.0988 4.0836 3.4652 0.3680  -0.0341 0.1773  570  GLN A CA  
4381  C C   . GLN A 570  ? 3.1610 4.1360 3.4947 0.3551  -0.0425 0.1553  570  GLN A C   
4382  O O   . GLN A 570  ? 3.1769 4.1470 3.4850 0.3418  -0.0479 0.1398  570  GLN A O   
4383  C CB  . GLN A 570  ? 3.0562 4.0049 3.4184 0.3666  -0.0325 0.1670  570  GLN A CB  
4384  C CG  . GLN A 570  ? 3.4922 4.4022 3.8764 0.3805  -0.0268 0.1707  570  GLN A CG  
4385  C CD  . GLN A 570  ? 3.4628 4.3959 3.8792 0.3919  -0.0188 0.1929  570  GLN A CD  
4386  O OE1 . GLN A 570  ? 3.4417 4.4240 3.8735 0.3943  -0.0169 0.2124  570  GLN A OE1 
4387  N NE2 . GLN A 570  ? 3.4551 4.3530 3.8821 0.3988  -0.0142 0.1898  570  GLN A NE2 
4388  N N   . LEU A 571  ? 1.9816 2.9553 2.3169 0.3589  -0.0439 0.1542  571  LEU A N   
4389  C CA  . LEU A 571  ? 2.0060 2.9662 2.3130 0.3485  -0.0516 0.1318  571  LEU A CA  
4390  C C   . LEU A 571  ? 2.0544 2.9550 2.3548 0.3510  -0.0542 0.1132  571  LEU A C   
4391  O O   . LEU A 571  ? 2.0623 2.9467 2.3815 0.3627  -0.0504 0.1200  571  LEU A O   
4392  C CB  . LEU A 571  ? 1.9079 2.9036 2.2194 0.3504  -0.0517 0.1396  571  LEU A CB  
4393  C CG  . LEU A 571  ? 1.8311 2.8019 2.1200 0.3441  -0.0585 0.1153  571  LEU A CG  
4394  C CD1 . LEU A 571  ? 1.7680 2.7141 2.0251 0.3297  -0.0667 0.0904  571  LEU A CD1 
4395  C CD2 . LEU A 571  ? 1.7638 2.7777 2.0512 0.3422  -0.0590 0.1201  571  LEU A CD2 
4396  N N   . GLN A 572  ? 2.3465 3.2146 2.6198 0.3395  -0.0612 0.0900  572  GLN A N   
4397  C CA  . GLN A 572  ? 2.3807 3.1915 2.6452 0.3401  -0.0653 0.0709  572  GLN A CA  
4398  C C   . GLN A 572  ? 2.3487 3.1470 2.5833 0.3275  -0.0756 0.0465  572  GLN A C   
4399  O O   . GLN A 572  ? 2.3341 3.1543 2.5492 0.3153  -0.0805 0.0399  572  GLN A O   
4400  C CB  . GLN A 572  ? 2.5185 3.2911 2.7824 0.3397  -0.0640 0.0666  572  GLN A CB  
4401  C CG  . GLN A 572  ? 2.6560 3.3673 2.9159 0.3423  -0.0669 0.0510  572  GLN A CG  
4402  C CD  . GLN A 572  ? 2.7482 3.4486 3.0347 0.3582  -0.0609 0.0630  572  GLN A CD  
4403  O OE1 . GLN A 572  ? 2.7624 3.4933 3.0747 0.3689  -0.0530 0.0855  572  GLN A OE1 
4404  N NE2 . GLN A 572  ? 2.8012 3.4573 3.0819 0.3594  -0.0653 0.0482  572  GLN A NE2 
4405  N N   . VAL A 573  ? 1.8748 2.6387 2.1073 0.3307  -0.0789 0.0334  573  VAL A N   
4406  C CA  . VAL A 573  ? 1.8490 2.5939 2.0560 0.3204  -0.0891 0.0085  573  VAL A CA  
4407  C C   . VAL A 573  ? 1.8862 2.5673 2.0817 0.3175  -0.0956 -0.0113 573  VAL A C   
4408  O O   . VAL A 573  ? 1.8934 2.5436 2.1038 0.3276  -0.0925 -0.0092 573  VAL A O   
4409  C CB  . VAL A 573  ? 1.7242 2.4849 1.9392 0.3267  -0.0882 0.0088  573  VAL A CB  
4410  C CG1 . VAL A 573  ? 1.6943 2.5069 1.8999 0.3198  -0.0895 0.0109  573  VAL A CG1 
4411  C CG2 . VAL A 573  ? 1.6521 2.4207 1.8988 0.3426  -0.0783 0.0312  573  VAL A CG2 
4412  N N   . HIS A 574  ? 2.3587 3.0195 2.5275 0.3033  -0.1051 -0.0304 574  HIS A N   
4413  C CA  . HIS A 574  ? 2.3869 2.9873 2.5434 0.2989  -0.1125 -0.0491 574  HIS A CA  
4414  C C   . HIS A 574  ? 2.4589 3.0391 2.5914 0.2882  -0.1253 -0.0743 574  HIS A C   
4415  O O   . HIS A 574  ? 2.4545 3.0603 2.5699 0.2778  -0.1308 -0.0813 574  HIS A O   
4416  C CB  . HIS A 574  ? 2.4271 3.0088 2.5751 0.2916  -0.1128 -0.0489 574  HIS A CB  
4417  C CG  . HIS A 574  ? 2.4516 3.0354 2.6239 0.3033  -0.1013 -0.0290 574  HIS A CG  
4418  N ND1 . HIS A 574  ? 2.4495 3.0102 2.6429 0.3169  -0.0959 -0.0224 574  HIS A ND1 
4419  C CD2 . HIS A 574  ? 2.4628 3.0684 2.6423 0.3034  -0.0946 -0.0149 574  HIS A CD2 
4420  C CE1 . HIS A 574  ? 2.4418 3.0098 2.6541 0.3250  -0.0864 -0.0052 574  HIS A CE1 
4421  N NE2 . HIS A 574  ? 2.4524 3.0478 2.6573 0.3173  -0.0853 -0.0006 574  HIS A NE2 
4422  N N   . LEU A 575  ? 1.8817 2.4149 2.0138 0.2908  -0.1303 -0.0880 575  LEU A N   
4423  C CA  . LEU A 575  ? 2.0069 2.5146 2.1191 0.2819  -0.1431 -0.1128 575  LEU A CA  
4424  C C   . LEU A 575  ? 2.1691 2.6387 2.2564 0.2668  -0.1546 -0.1295 575  LEU A C   
4425  O O   . LEU A 575  ? 2.2237 2.6561 2.3121 0.2666  -0.1544 -0.1289 575  LEU A O   
4426  C CB  . LEU A 575  ? 1.9421 2.4163 2.0667 0.2917  -0.1438 -0.1194 575  LEU A CB  
4427  C CG  . LEU A 575  ? 1.8448 2.3606 1.9887 0.3033  -0.1353 -0.1074 575  LEU A CG  
4428  C CD1 . LEU A 575  ? 1.8116 2.2966 1.9692 0.3132  -0.1354 -0.1126 575  LEU A CD1 
4429  C CD2 . LEU A 575  ? 1.8539 2.4037 1.9823 0.2951  -0.1407 -0.1183 575  LEU A CD2 
4430  N N   . SER A 576  ? 3.1133 3.5910 3.1781 0.2538  -0.1649 -0.1448 576  SER A N   
4431  C CA  . SER A 576  ? 3.2392 3.6856 3.2789 0.2375  -0.1768 -0.1595 576  SER A CA  
4432  C C   . SER A 576  ? 3.2768 3.6602 3.3129 0.2358  -0.1839 -0.1716 576  SER A C   
4433  O O   . SER A 576  ? 3.2789 3.6396 3.3107 0.2311  -0.1834 -0.1679 576  SER A O   
4434  C CB  . SER A 576  ? 3.3275 3.7859 3.3448 0.2248  -0.1888 -0.1769 576  SER A CB  
4435  O OG  . SER A 576  ? 3.3721 3.8762 3.3821 0.2181  -0.1858 -0.1671 576  SER A OG  
4436  N N   . PRO A 577  ? 2.3622 2.7174 2.3994 0.2390  -0.1910 -0.1868 577  PRO A N   
4437  C CA  . PRO A 577  ? 2.3807 2.6801 2.4221 0.2417  -0.1946 -0.1929 577  PRO A CA  
4438  C C   . PRO A 577  ? 2.3369 2.6396 2.4059 0.2588  -0.1803 -0.1742 577  PRO A C   
4439  O O   . PRO A 577  ? 2.3373 2.6565 2.4228 0.2704  -0.1752 -0.1706 577  PRO A O   
4440  C CB  . PRO A 577  ? 2.4391 2.7140 2.4751 0.2405  -0.2064 -0.2144 577  PRO A CB  
4441  C CG  . PRO A 577  ? 2.4593 2.7652 2.4785 0.2308  -0.2134 -0.2245 577  PRO A CG  
4442  C CD  . PRO A 577  ? 2.3989 2.7634 2.4266 0.2354  -0.2001 -0.2039 577  PRO A CD  
4443  N N   . ASP A 578  ? 2.6351 2.9225 2.7091 0.2599  -0.1742 -0.1629 578  ASP A N   
4444  C CA  . ASP A 578  ? 2.5583 2.8497 2.6588 0.2759  -0.1608 -0.1443 578  ASP A CA  
4445  C C   . ASP A 578  ? 2.5232 2.7667 2.6330 0.2829  -0.1637 -0.1511 578  ASP A C   
4446  O O   . ASP A 578  ? 2.4646 2.7034 2.5957 0.2955  -0.1541 -0.1373 578  ASP A O   
4447  C CB  . ASP A 578  ? 2.5760 2.8723 2.6800 0.2754  -0.1524 -0.1296 578  ASP A CB  
4448  C CG  . ASP A 578  ? 2.5761 2.9027 2.7089 0.2920  -0.1370 -0.1063 578  ASP A CG  
4449  O OD1 . ASP A 578  ? 2.5653 2.8916 2.7157 0.3041  -0.1335 -0.1022 578  ASP A OD1 
4450  O OD2 . ASP A 578  ? 2.5803 2.9318 2.7188 0.2929  -0.1287 -0.0919 578  ASP A OD2 
4451  N N   . ALA A 579  ? 2.6382 2.8458 2.7323 0.2743  -0.1777 -0.1724 579  ALA A N   
4452  C CA  . ALA A 579  ? 2.6374 2.8009 2.7395 0.2800  -0.1824 -0.1811 579  ALA A CA  
4453  C C   . ALA A 579  ? 2.5472 2.7356 2.6757 0.2971  -0.1718 -0.1687 579  ALA A C   
4454  O O   . ALA A 579  ? 2.5447 2.7822 2.6797 0.3016  -0.1657 -0.1614 579  ALA A O   
4455  C CB  . ALA A 579  ? 2.7002 2.8377 2.7849 0.2699  -0.1987 -0.2054 579  ALA A CB  
4456  N N   . ASP A 580  ? 2.6114 2.7658 2.7547 0.3060  -0.1699 -0.1662 580  ASP A N   
4457  C CA  . ASP A 580  ? 2.5593 2.7332 2.7289 0.3222  -0.1598 -0.1528 580  ASP A CA  
4458  C C   . ASP A 580  ? 2.5404 2.7058 2.7133 0.3252  -0.1666 -0.1672 580  ASP A C   
4459  O O   . ASP A 580  ? 2.5223 2.6775 2.7144 0.3365  -0.1627 -0.1623 580  ASP A O   
4460  C CB  . ASP A 580  ? 2.6038 2.7482 2.7892 0.3309  -0.1531 -0.1402 580  ASP A CB  
4461  C CG  . ASP A 580  ? 2.7220 2.8035 2.8960 0.3237  -0.1640 -0.1554 580  ASP A CG  
4462  O OD1 . ASP A 580  ? 2.7782 2.8359 2.9465 0.3205  -0.1747 -0.1725 580  ASP A OD1 
4463  O OD2 . ASP A 580  ? 2.7585 2.8149 2.9295 0.3209  -0.1621 -0.1505 580  ASP A OD2 
4464  N N   . ALA A 581  ? 2.5825 2.7524 2.7371 0.3150  -0.1769 -0.1854 581  ALA A N   
4465  C CA  . ALA A 581  ? 2.5650 2.7306 2.7216 0.3170  -0.1839 -0.2016 581  ALA A CA  
4466  C C   . ALA A 581  ? 2.5732 2.7484 2.7068 0.3040  -0.1949 -0.2203 581  ALA A C   
4467  O O   . ALA A 581  ? 2.5932 2.7529 2.7072 0.2914  -0.2020 -0.2257 581  ALA A O   
4468  C CB  . ALA A 581  ? 2.6036 2.7112 2.7638 0.3183  -0.1921 -0.2125 581  ALA A CB  
4469  N N   . TYR A 582  ? 2.1441 2.3452 2.2802 0.3066  -0.1965 -0.2302 582  TYR A N   
4470  C CA  . TYR A 582  ? 2.1188 2.3341 2.2342 0.2949  -0.2063 -0.2476 582  TYR A CA  
4471  C C   . TYR A 582  ? 2.0949 2.2896 2.2071 0.2935  -0.2182 -0.2723 582  TYR A C   
4472  O O   . TYR A 582  ? 2.0917 2.2838 2.2216 0.3040  -0.2153 -0.2742 582  TYR A O   
4473  C CB  . TYR A 582  ? 2.0703 2.3502 2.1866 0.2966  -0.1965 -0.2360 582  TYR A CB  
4474  C CG  . TYR A 582  ? 2.0277 2.3292 2.1425 0.2947  -0.1877 -0.2151 582  TYR A CG  
4475  C CD1 . TYR A 582  ? 2.0486 2.3546 2.1416 0.2811  -0.1936 -0.2191 582  TYR A CD1 
4476  C CD2 . TYR A 582  ? 1.9704 2.2876 2.1065 0.3066  -0.1738 -0.1914 582  TYR A CD2 
4477  C CE1 . TYR A 582  ? 2.0270 2.3538 2.1199 0.2796  -0.1854 -0.2003 582  TYR A CE1 
4478  C CE2 . TYR A 582  ? 1.9469 2.2841 2.0836 0.3056  -0.1659 -0.1728 582  TYR A CE2 
4479  C CZ  . TYR A 582  ? 1.9769 2.3193 2.0921 0.2922  -0.1714 -0.1775 582  TYR A CZ  
4480  O OH  . TYR A 582  ? 1.9571 2.3206 2.0741 0.2915  -0.1633 -0.1594 582  TYR A OH  
4481  N N   . SER A 583  ? 2.9755 3.1558 3.0657 0.2800  -0.2321 -0.2912 583  SER A N   
4482  C CA  . SER A 583  ? 2.9819 3.1470 3.0674 0.2773  -0.2447 -0.3164 583  SER A CA  
4483  C C   . SER A 583  ? 2.9562 3.1771 3.0458 0.2819  -0.2381 -0.3186 583  SER A C   
4484  O O   . SER A 583  ? 2.8922 3.1534 2.9714 0.2767  -0.2339 -0.3118 583  SER A O   
4485  C CB  . SER A 583  ? 3.0922 3.2269 3.1523 0.2605  -0.2618 -0.3340 583  SER A CB  
4486  O OG  . SER A 583  ? 3.1146 3.2777 3.1597 0.2519  -0.2583 -0.3233 583  SER A OG  
4487  N N   . PRO A 584  ? 1.9792 2.2029 2.0836 0.2911  -0.2375 -0.3287 584  PRO A N   
4488  C CA  . PRO A 584  ? 1.9751 2.2546 2.0876 0.2978  -0.2282 -0.3278 584  PRO A CA  
4489  C C   . PRO A 584  ? 1.9584 2.2606 2.0507 0.2871  -0.2363 -0.3450 584  PRO A C   
4490  O O   . PRO A 584  ? 2.0017 2.2859 2.0900 0.2847  -0.2476 -0.3694 584  PRO A O   
4491  C CB  . PRO A 584  ? 1.9763 2.2398 2.1071 0.3080  -0.2293 -0.3397 584  PRO A CB  
4492  C CG  . PRO A 584  ? 2.0031 2.2042 2.1383 0.3083  -0.2367 -0.3411 584  PRO A CG  
4493  C CD  . PRO A 584  ? 2.0385 2.2115 2.1510 0.2943  -0.2471 -0.3441 584  PRO A CD  
4494  N N   . GLY A 585  ? 2.7107 3.0516 2.7915 0.2811  -0.2310 -0.3328 585  GLY A N   
4495  C CA  . GLY A 585  ? 2.7547 3.1175 2.8152 0.2702  -0.2388 -0.3479 585  GLY A CA  
4496  C C   . GLY A 585  ? 2.7780 3.1295 2.8170 0.2564  -0.2457 -0.3441 585  GLY A C   
4497  O O   . GLY A 585  ? 2.8036 3.1774 2.8247 0.2463  -0.2511 -0.3519 585  GLY A O   
4498  N N   . GLN A 586  ? 2.4501 2.7669 2.4909 0.2556  -0.2456 -0.3324 586  GLN A N   
4499  C CA  . GLN A 586  ? 2.4972 2.8041 2.5196 0.2430  -0.2503 -0.3262 586  GLN A CA  
4500  C C   . GLN A 586  ? 2.5075 2.8726 2.5245 0.2405  -0.2407 -0.3111 586  GLN A C   
4501  O O   . GLN A 586  ? 2.4613 2.8668 2.4944 0.2508  -0.2258 -0.2926 586  GLN A O   
4502  C CB  . GLN A 586  ? 2.4672 2.7417 2.4981 0.2463  -0.2455 -0.3100 586  GLN A CB  
4503  C CG  . GLN A 586  ? 2.5014 2.7697 2.5161 0.2347  -0.2473 -0.3004 586  GLN A CG  
4504  C CD  . GLN A 586  ? 2.5157 2.7556 2.5407 0.2394  -0.2408 -0.2845 586  GLN A CD  
4505  O OE1 . GLN A 586  ? 2.5021 2.7222 2.5453 0.2506  -0.2365 -0.2815 586  GLN A OE1 
4506  N NE2 . GLN A 586  ? 2.5406 2.7792 2.5543 0.2306  -0.2400 -0.2744 586  GLN A NE2 
4507  N N   . THR A 587  ? 2.3277 2.6973 2.3221 0.2262  -0.2500 -0.3186 587  THR A N   
4508  C CA  . THR A 587  ? 2.3791 2.7985 2.3672 0.2221  -0.2418 -0.3021 587  THR A CA  
4509  C C   . THR A 587  ? 2.3763 2.7871 2.3697 0.2231  -0.2338 -0.2799 587  THR A C   
4510  O O   . THR A 587  ? 2.3610 2.7247 2.3475 0.2171  -0.2417 -0.2845 587  THR A O   
4511  C CB  . THR A 587  ? 2.4726 2.8962 2.4347 0.2058  -0.2550 -0.3173 587  THR A CB  
4512  O OG1 . THR A 587  ? 2.5223 2.8895 2.4705 0.1954  -0.2704 -0.3316 587  THR A OG1 
4513  C CG2 . THR A 587  ? 2.5203 2.9639 2.4791 0.2063  -0.2599 -0.3367 587  THR A CG2 
4514  N N   . VAL A 588  ? 2.1865 2.6424 2.1931 0.2307  -0.2185 -0.2562 588  VAL A N   
4515  C CA  . VAL A 588  ? 2.1772 2.6297 2.1928 0.2339  -0.2093 -0.2343 588  VAL A CA  
4516  C C   . VAL A 588  ? 2.1491 2.6589 2.1691 0.2351  -0.1976 -0.2123 588  VAL A C   
4517  O O   . VAL A 588  ? 2.1541 2.7060 2.1874 0.2439  -0.1881 -0.2022 588  VAL A O   
4518  C CB  . VAL A 588  ? 2.1474 2.5808 2.1876 0.2491  -0.2002 -0.2240 588  VAL A CB  
4519  C CG1 . VAL A 588  ? 2.1221 2.5755 2.1764 0.2598  -0.1961 -0.2281 588  VAL A CG1 
4520  C CG2 . VAL A 588  ? 2.1043 2.5619 2.1597 0.2564  -0.1858 -0.1964 588  VAL A CG2 
4521  N N   . SER A 589  ? 2.8135 3.3247 2.8229 0.2261  -0.1982 -0.2042 589  SER A N   
4522  C CA  . SER A 589  ? 2.8007 3.3657 2.8129 0.2256  -0.1888 -0.1844 589  SER A CA  
4523  C C   . SER A 589  ? 2.7214 3.3060 2.7603 0.2401  -0.1728 -0.1585 589  SER A C   
4524  O O   . SER A 589  ? 2.6898 3.2398 2.7393 0.2462  -0.1698 -0.1537 589  SER A O   
4525  C CB  . SER A 589  ? 2.8787 3.4390 2.8702 0.2102  -0.1957 -0.1861 589  SER A CB  
4526  O OG  . SER A 589  ? 2.9633 3.4834 2.9327 0.1977  -0.2120 -0.2106 589  SER A OG  
4527  N N   . LEU A 590  ? 2.0504 2.6902 2.1000 0.2454  -0.1632 -0.1417 590  LEU A N   
4528  C CA  . LEU A 590  ? 1.9577 2.6207 2.0336 0.2589  -0.1489 -0.1159 590  LEU A CA  
4529  C C   . LEU A 590  ? 1.9265 2.6285 2.0033 0.2551  -0.1429 -0.0969 590  LEU A C   
4530  O O   . LEU A 590  ? 1.9773 2.7118 2.0392 0.2452  -0.1467 -0.0991 590  LEU A O   
4531  C CB  . LEU A 590  ? 1.8752 2.5710 1.9677 0.2698  -0.1419 -0.1091 590  LEU A CB  
4532  C CG  . LEU A 590  ? 1.7466 2.4862 1.8629 0.2804  -0.1282 -0.0799 590  LEU A CG  
4533  C CD1 . LEU A 590  ? 1.6871 2.3976 1.8240 0.2915  -0.1212 -0.0668 590  LEU A CD1 
4534  C CD2 . LEU A 590  ? 1.6944 2.4729 1.8217 0.2872  -0.1232 -0.0747 590  LEU A CD2 
4535  N N   . ASN A 591  ? 2.3296 3.0288 2.4246 0.2633  -0.1337 -0.0783 591  ASN A N   
4536  C CA  . ASN A 591  ? 2.2913 3.0235 2.3895 0.2605  -0.1279 -0.0606 591  ASN A CA  
4537  C C   . ASN A 591  ? 2.2300 3.0078 2.3553 0.2732  -0.1151 -0.0336 591  ASN A C   
4538  O O   . ASN A 591  ? 2.1989 2.9675 2.3461 0.2867  -0.1081 -0.0239 591  ASN A O   
4539  C CB  . ASN A 591  ? 2.3039 2.9986 2.3993 0.2574  -0.1283 -0.0612 591  ASN A CB  
4540  C CG  . ASN A 591  ? 2.3838 3.0506 2.4494 0.2401  -0.1412 -0.0822 591  ASN A CG  
4541  O OD1 . ASN A 591  ? 2.4186 3.1107 2.4703 0.2289  -0.1442 -0.0811 591  ASN A OD1 
4542  N ND2 . ASN A 591  ? 2.4152 3.0293 2.4710 0.2375  -0.1496 -0.1009 591  ASN A ND2 
4543  N N   . MET A 592  ? 2.3979 3.2244 2.5216 0.2684  -0.1127 -0.0212 592  MET A N   
4544  C CA  . MET A 592  ? 2.3316 3.2010 2.4810 0.2787  -0.1014 0.0063  592  MET A CA  
4545  C C   . MET A 592  ? 2.3429 3.2198 2.4969 0.2765  -0.0975 0.0187  592  MET A C   
4546  O O   . MET A 592  ? 2.3700 3.2300 2.5035 0.2643  -0.1039 0.0064  592  MET A O   
4547  C CB  . MET A 592  ? 2.3209 3.2467 2.4697 0.2766  -0.1005 0.0146  592  MET A CB  
4548  C CG  . MET A 592  ? 2.2874 3.2220 2.4475 0.2856  -0.0977 0.0157  592  MET A CG  
4549  S SD  . MET A 592  ? 2.5791 3.4896 2.7129 0.2768  -0.1090 -0.0162 592  MET A SD  
4550  C CE  . MET A 592  ? 2.4565 3.4058 2.5647 0.2598  -0.1159 -0.0218 592  MET A CE  
4551  N N   . ALA A 593  ? 1.8348 2.7378 2.0163 0.2882  -0.0872 0.0431  593  ALA A N   
4552  C CA  . ALA A 593  ? 1.8625 2.7778 2.0527 0.2879  -0.0822 0.0564  593  ALA A CA  
4553  C C   . ALA A 593  ? 1.8811 2.8375 2.1033 0.3007  -0.0718 0.0852  593  ALA A C   
4554  O O   . ALA A 593  ? 1.8392 2.7975 2.0824 0.3134  -0.0667 0.0960  593  ALA A O   
4555  C CB  . ALA A 593  ? 1.8390 2.7016 2.0269 0.2883  -0.0824 0.0464  593  ALA A CB  
4556  N N   . THR A 594  ? 1.6079 2.5968 1.8342 0.2971  -0.0691 0.0977  594  THR A N   
4557  C CA  . THR A 594  ? 1.6441 2.6733 1.9009 0.3081  -0.0602 0.1253  594  THR A CA  
4558  C C   . THR A 594  ? 1.6975 2.7486 1.9587 0.3041  -0.0574 0.1348  594  THR A C   
4559  O O   . THR A 594  ? 1.7558 2.8207 1.9950 0.2900  -0.0630 0.1266  594  THR A O   
4560  C CB  . THR A 594  ? 1.6568 2.7361 1.9180 0.3081  -0.0605 0.1379  594  THR A CB  
4561  O OG1 . THR A 594  ? 1.6711 2.7371 1.9114 0.3022  -0.0671 0.1196  594  THR A OG1 
4562  C CG2 . THR A 594  ? 1.6185 2.7174 1.9145 0.3242  -0.0522 0.1626  594  THR A CG2 
4563  N N   . GLY A 595  ? 2.7282 3.7833 3.0188 0.3167  -0.0489 0.1524  595  GLY A N   
4564  C CA  . GLY A 595  ? 2.7847 3.8650 3.0853 0.3154  -0.0449 0.1639  595  GLY A CA  
4565  C C   . GLY A 595  ? 2.8824 4.0222 3.1836 0.3094  -0.0464 0.1784  595  GLY A C   
4566  O O   . GLY A 595  ? 2.8827 4.0471 3.1852 0.3042  -0.0454 0.1849  595  GLY A O   
4567  N N   . MET A 596  ? 2.0023 3.1654 2.3021 0.3097  -0.0489 0.1834  596  MET A N   
4568  C CA  . MET A 596  ? 2.0620 3.2823 2.3608 0.3034  -0.0510 0.1971  596  MET A CA  
4569  C C   . MET A 596  ? 2.0783 3.3043 2.3518 0.2940  -0.0583 0.1838  596  MET A C   
4570  O O   . MET A 596  ? 2.0943 3.2896 2.3636 0.2981  -0.0593 0.1724  596  MET A O   
4571  C CB  . MET A 596  ? 2.0429 3.3003 2.3778 0.3171  -0.0443 0.2263  596  MET A CB  
4572  C CG  . MET A 596  ? 2.0336 3.2975 2.3972 0.3268  -0.0373 0.2427  596  MET A CG  
4573  S SD  . MET A 596  ? 2.3648 3.6771 2.7238 0.3153  -0.0390 0.2517  596  MET A SD  
4574  C CE  . MET A 596  ? 1.7456 3.1101 2.0951 0.3073  -0.0445 0.2619  596  MET A CE  
4575  N N   . ASP A 597  ? 2.4373 3.7028 2.6947 0.2816  -0.0632 0.1849  597  ASP A N   
4576  C CA  . ASP A 597  ? 2.4367 3.7129 2.6719 0.2732  -0.0695 0.1733  597  ASP A CA  
4577  C C   . ASP A 597  ? 2.3194 3.6015 2.5733 0.2852  -0.0652 0.1836  597  ASP A C   
4578  O O   . ASP A 597  ? 2.2655 3.5734 2.5489 0.2960  -0.0589 0.2083  597  ASP A O   
4579  C CB  . ASP A 597  ? 2.5371 3.8675 2.7622 0.2617  -0.0732 0.1820  597  ASP A CB  
4580  C CG  . ASP A 597  ? 2.6537 3.9840 2.8604 0.2488  -0.0778 0.1736  597  ASP A CG  
4581  O OD1 . ASP A 597  ? 2.7027 3.9894 2.8887 0.2423  -0.0824 0.1509  597  ASP A OD1 
4582  O OD2 . ASP A 597  ? 2.6853 4.0598 2.8984 0.2445  -0.0772 0.1900  597  ASP A OD2 
4583  N N   . SER A 598  ? 1.8182 3.0779 2.0560 0.2833  -0.0691 0.1654  598  SER A N   
4584  C CA  . SER A 598  ? 1.7054 2.9694 1.9604 0.2943  -0.0650 0.1741  598  SER A CA  
4585  C C   . SER A 598  ? 1.6106 2.8692 1.8457 0.2893  -0.0696 0.1556  598  SER A C   
4586  O O   . SER A 598  ? 1.6275 2.8622 1.8350 0.2790  -0.0767 0.1305  598  SER A O   
4587  C CB  . SER A 598  ? 1.6594 2.8835 1.9379 0.3092  -0.0590 0.1789  598  SER A CB  
4588  O OG  . SER A 598  ? 1.6146 2.8542 1.9172 0.3208  -0.0539 0.1963  598  SER A OG  
4589  N N   . TRP A 599  ? 2.1478 3.4301 2.3989 0.2967  -0.0656 0.1691  599  TRP A N   
4590  C CA  . TRP A 599  ? 2.0973 3.3811 2.3352 0.2940  -0.0682 0.1549  599  TRP A CA  
4591  C C   . TRP A 599  ? 2.0284 3.2659 2.2750 0.3045  -0.0662 0.1452  599  TRP A C   
4592  O O   . TRP A 599  ? 2.0138 3.2530 2.2871 0.3169  -0.0599 0.1636  599  TRP A O   
4593  C CB  . TRP A 599  ? 2.1135 3.4539 2.3641 0.2953  -0.0647 0.1766  599  TRP A CB  
4594  C CG  . TRP A 599  ? 2.2040 3.5912 2.4376 0.2820  -0.0686 0.1790  599  TRP A CG  
4595  C CD1 . TRP A 599  ? 2.2295 3.6659 2.4758 0.2804  -0.0666 0.2045  599  TRP A CD1 
4596  C CD2 . TRP A 599  ? 2.2660 3.6551 2.4669 0.2680  -0.0759 0.1548  599  TRP A CD2 
4597  N NE1 . TRP A 599  ? 2.2689 3.7380 2.4915 0.2659  -0.0720 0.1979  599  TRP A NE1 
4598  C CE2 . TRP A 599  ? 2.2850 3.7257 2.4793 0.2582  -0.0777 0.1673  599  TRP A CE2 
4599  C CE3 . TRP A 599  ? 2.2968 3.6484 2.4740 0.2630  -0.0817 0.1238  599  TRP A CE3 
4600  C CZ2 . TRP A 599  ? 2.3145 3.7701 2.4787 0.2434  -0.0848 0.1494  599  TRP A CZ2 
4601  C CZ3 . TRP A 599  ? 2.3280 3.6942 2.4763 0.2487  -0.0889 0.1060  599  TRP A CZ3 
4602  C CH2 . TRP A 599  ? 2.3367 3.7542 2.4782 0.2390  -0.0903 0.1186  599  TRP A CH2 
4603  N N   . VAL A 600  ? 1.6915 2.8880 1.9162 0.2995  -0.0720 0.1168  600  VAL A N   
4604  C CA  . VAL A 600  ? 1.6011 2.7510 1.8331 0.3088  -0.0709 0.1061  600  VAL A CA  
4605  C C   . VAL A 600  ? 1.5630 2.7281 1.7931 0.3099  -0.0708 0.1000  600  VAL A C   
4606  O O   . VAL A 600  ? 1.5865 2.7955 1.8068 0.3024  -0.0719 0.1016  600  VAL A O   
4607  C CB  . VAL A 600  ? 1.6090 2.7010 1.8210 0.3036  -0.0777 0.0791  600  VAL A CB  
4608  C CG1 . VAL A 600  ? 1.5873 2.6285 1.8143 0.3153  -0.0750 0.0761  600  VAL A CG1 
4609  C CG2 . VAL A 600  ? 1.6087 2.6991 1.8117 0.2959  -0.0800 0.0804  600  VAL A CG2 
4610  N N   . ALA A 601  ? 1.4211 2.5508 1.6606 0.3189  -0.0692 0.0931  601  ALA A N   
4611  C CA  . ALA A 601  ? 1.4096 2.5496 1.6481 0.3205  -0.0688 0.0853  601  ALA A CA  
4612  C C   . ALA A 601  ? 1.4106 2.4964 1.6506 0.3271  -0.0704 0.0671  601  ALA A C   
4613  O O   . ALA A 601  ? 1.4082 2.4830 1.6705 0.3386  -0.0651 0.0790  601  ALA A O   
4614  C CB  . ALA A 601  ? 1.3668 2.5531 1.6290 0.3276  -0.0613 0.1132  601  ALA A CB  
4615  N N   . LEU A 602  ? 1.7420 2.7946 1.9583 0.3193  -0.0784 0.0384  602  LEU A N   
4616  C CA  . LEU A 602  ? 1.7344 2.7326 1.9499 0.3240  -0.0816 0.0190  602  LEU A CA  
4617  C C   . LEU A 602  ? 1.7593 2.7672 1.9850 0.3305  -0.0785 0.0167  602  LEU A C   
4618  O O   . LEU A 602  ? 1.7657 2.8223 1.9920 0.3284  -0.0755 0.0238  602  LEU A O   
4619  C CB  . LEU A 602  ? 1.7377 2.7030 1.9248 0.3127  -0.0922 -0.0107 602  LEU A CB  
4620  C CG  . LEU A 602  ? 1.7265 2.6934 1.8987 0.3027  -0.0962 -0.0099 602  LEU A CG  
4621  C CD1 . LEU A 602  ? 1.7249 2.6487 1.8709 0.2922  -0.1076 -0.0391 602  LEU A CD1 
4622  C CD2 . LEU A 602  ? 1.6719 2.6303 1.8625 0.3096  -0.0901 0.0119  602  LEU A CD2 
4623  N N   . ALA A 603  ? 2.0106 2.9730 2.2443 0.3381  -0.0792 0.0071  603  ALA A N   
4624  C CA  . ALA A 603  ? 1.9464 2.9144 2.1923 0.3453  -0.0759 0.0055  603  ALA A CA  
4625  C C   . ALA A 603  ? 1.9262 2.8352 2.1769 0.3518  -0.0789 -0.0096 603  ALA A C   
4626  O O   . ALA A 603  ? 1.8859 2.7727 2.1565 0.3615  -0.0746 0.0049  603  ALA A O   
4627  C CB  . ALA A 603  ? 1.8980 2.9041 2.1698 0.3540  -0.0664 0.0370  603  ALA A CB  
4628  N N   . ALA A 604  ? 2.0483 2.9327 2.2820 0.3466  -0.0865 -0.0383 604  ALA A N   
4629  C CA  . ALA A 604  ? 2.0430 2.8678 2.2785 0.3509  -0.0914 -0.0550 604  ALA A CA  
4630  C C   . ALA A 604  ? 2.0334 2.8560 2.2846 0.3597  -0.0881 -0.0576 604  ALA A C   
4631  O O   . ALA A 604  ? 2.0696 2.8947 2.3114 0.3566  -0.0921 -0.0786 604  ALA A O   
4632  C CB  . ALA A 604  ? 2.0501 2.8426 2.2597 0.3404  -0.1029 -0.0850 604  ALA A CB  
4633  N N   . VAL A 605  ? 1.3564 2.1733 1.6318 0.3706  -0.0811 -0.0367 605  VAL A N   
4634  C CA  . VAL A 605  ? 1.3663 2.1790 1.6590 0.3795  -0.0777 -0.0363 605  VAL A CA  
4635  C C   . VAL A 605  ? 1.3666 2.1182 1.6572 0.3819  -0.0846 -0.0584 605  VAL A C   
4636  O O   . VAL A 605  ? 1.3861 2.0944 1.6662 0.3784  -0.0910 -0.0681 605  VAL A O   
4637  C CB  . VAL A 605  ? 1.3140 2.1383 1.6341 0.3903  -0.0687 -0.0051 605  VAL A CB  
4638  C CG1 . VAL A 605  ? 1.3120 2.1364 1.6499 0.3986  -0.0651 -0.0034 605  VAL A CG1 
4639  C CG2 . VAL A 605  ? 1.3078 2.1903 1.6327 0.3884  -0.0624 0.0195  605  VAL A CG2 
4640  N N   . ASP A 606  ? 1.8717 2.6207 2.1723 0.3873  -0.0837 -0.0662 606  ASP A N   
4641  C CA  . ASP A 606  ? 1.8845 2.5766 2.1914 0.3925  -0.0884 -0.0787 606  ASP A CA  
4642  C C   . ASP A 606  ? 1.8372 2.5180 2.1681 0.4030  -0.0816 -0.0532 606  ASP A C   
4643  O O   . ASP A 606  ? 1.8378 2.5455 2.1878 0.4102  -0.0745 -0.0379 606  ASP A O   
4644  C CB  . ASP A 606  ? 1.9321 2.6240 2.2418 0.3945  -0.0904 -0.0978 606  ASP A CB  
4645  C CG  . ASP A 606  ? 1.9250 2.5579 2.2432 0.4003  -0.0955 -0.1089 606  ASP A CG  
4646  O OD1 . ASP A 606  ? 1.9290 2.5161 2.2437 0.3997  -0.1001 -0.1089 606  ASP A OD1 
4647  O OD2 . ASP A 606  ? 1.9222 2.5550 2.2507 0.4051  -0.0949 -0.1177 606  ASP A OD2 
4648  N N   . SER A 607  ? 1.8814 2.1661 2.5180 0.3760  -0.9949 -0.4812 607  SER A N   
4649  C CA  . SER A 607  ? 1.7903 2.1361 2.5038 0.3858  -0.9521 -0.4781 607  SER A CA  
4650  C C   . SER A 607  ? 1.7154 2.0439 2.5096 0.4155  -0.8951 -0.5153 607  SER A C   
4651  O O   . SER A 607  ? 1.6259 1.9961 2.4847 0.4289  -0.8487 -0.5162 607  SER A O   
4652  C CB  . SER A 607  ? 1.8201 2.2220 2.5690 0.3586  -0.9949 -0.4736 607  SER A CB  
4653  O OG  . SER A 607  ? 1.8761 2.2515 2.6566 0.3521  -1.0255 -0.5072 607  SER A OG  
4654  N N   . ALA A 608  ? 1.5873 1.8540 2.3775 0.4253  -0.8989 -0.5465 608  ALA A N   
4655  C CA  . ALA A 608  ? 1.5384 1.7858 2.4047 0.4518  -0.8496 -0.5853 608  ALA A CA  
4656  C C   . ALA A 608  ? 1.4689 1.7242 2.3540 0.4788  -0.7771 -0.5783 608  ALA A C   
4657  O O   . ALA A 608  ? 1.3802 1.6709 2.3427 0.4923  -0.7331 -0.5901 608  ALA A O   
4658  C CB  . ALA A 608  ? 1.6702 1.8439 2.5118 0.4596  -0.8627 -0.6149 608  ALA A CB  
4659  N N   . VAL A 609  ? 1.5139 1.7354 2.3249 0.4858  -0.7657 -0.5584 609  VAL A N   
4660  C CA  . VAL A 609  ? 1.4675 1.6849 2.2804 0.5117  -0.6992 -0.5502 609  VAL A CA  
4661  C C   . VAL A 609  ? 1.3650 1.6451 2.2499 0.5212  -0.6540 -0.5438 609  VAL A C   
4662  O O   . VAL A 609  ? 1.3162 1.5972 2.2771 0.5404  -0.6086 -0.5738 609  VAL A O   
4663  C CB  . VAL A 609  ? 1.4992 1.7021 2.2145 0.5056  -0.7120 -0.5121 609  VAL A CB  
4664  C CG1 . VAL A 609  ? 1.6297 1.7747 2.2756 0.4929  -0.7611 -0.5182 609  VAL A CG1 
4665  C CG2 . VAL A 609  ? 1.4475 1.7137 2.1406 0.4829  -0.7441 -0.4727 609  VAL A CG2 
4666  N N   . TYR A 610  ? 1.7852 2.1173 2.6461 0.5078  -0.6659 -0.5053 610  TYR A N   
4667  C CA  . TYR A 610  ? 1.6625 2.0580 2.5868 0.5136  -0.6291 -0.4955 610  TYR A CA  
4668  C C   . TYR A 610  ? 2.3092 2.7243 3.3300 0.5152  -0.6210 -0.5317 610  TYR A C   
4669  O O   . TYR A 610  ? 2.2223 2.6160 3.2973 0.5393  -0.5699 -0.5621 610  TYR A O   
4670  C CB  . TYR A 610  ? 1.6022 2.0559 2.4934 0.4882  -0.6694 -0.4547 610  TYR A CB  
4671  C CG  . TYR A 610  ? 1.7188 2.1517 2.5057 0.4751  -0.7069 -0.4218 610  TYR A CG  
4672  C CD1 . TYR A 610  ? 1.7770 2.2047 2.5166 0.4894  -0.6736 -0.3949 610  TYR A CD1 
4673  C CD2 . TYR A 610  ? 1.7417 2.1617 2.4771 0.4475  -0.7764 -0.4172 610  TYR A CD2 
4674  C CE1 . TYR A 610  ? 1.9001 2.3107 2.5445 0.4768  -0.7083 -0.3646 610  TYR A CE1 
4675  C CE2 . TYR A 610  ? 1.8696 2.2716 2.5092 0.4344  -0.8108 -0.3873 610  TYR A CE2 
4676  C CZ  . TYR A 610  ? 1.9338 2.3320 2.5286 0.4491  -0.7765 -0.3611 610  TYR A CZ  
4677  O OH  . TYR A 610  ? 1.9774 2.3592 2.4775 0.4362  -0.8097 -0.3313 610  TYR A OH  
4678  N N   . GLY A 611  ? 2.2686 2.7249 3.3092 0.4891  -0.6712 -0.5279 611  GLY A N   
4679  C CA  . GLY A 611  ? 2.3054 2.7706 3.4200 0.4837  -0.6848 -0.5624 611  GLY A CA  
4680  C C   . GLY A 611  ? 2.2967 2.8049 3.5134 0.4952  -0.6402 -0.5826 611  GLY A C   
4681  O O   . GLY A 611  ? 2.2370 2.8074 3.4865 0.4821  -0.6448 -0.5658 611  GLY A O   
4682  N N   . VAL A 612  ? 1.8667 2.3403 3.1333 0.5186  -0.5986 -0.6203 612  VAL A N   
4683  C CA  . VAL A 612  ? 1.8768 2.3814 3.2417 0.5324  -0.5516 -0.6460 612  VAL A CA  
4684  C C   . VAL A 612  ? 1.9386 2.4968 3.3257 0.5388  -0.5076 -0.6199 612  VAL A C   
4685  O O   . VAL A 612  ? 1.9754 2.5183 3.3472 0.5607  -0.4554 -0.6118 612  VAL A O   
4686  C CB  . VAL A 612  ? 2.9315 3.3841 4.3303 0.5620  -0.5002 -0.6850 612  VAL A CB  
4687  C CG1 . VAL A 612  ? 2.9830 3.3957 4.3949 0.5571  -0.5381 -0.7207 612  VAL A CG1 
4688  C CG2 . VAL A 612  ? 3.0137 3.4193 4.3457 0.5803  -0.4681 -0.6718 612  VAL A CG2 
4689  N N   . GLN A 613  ? 2.7754 3.3959 4.1994 0.5194  -0.5284 -0.6074 613  GLN A N   
4690  C CA  . GLN A 613  ? 2.8349 3.5110 4.2721 0.5207  -0.4974 -0.5776 613  GLN A CA  
4691  C C   . GLN A 613  ? 3.0148 3.6760 4.3651 0.5241  -0.4961 -0.5407 613  GLN A C   
4692  O O   . GLN A 613  ? 3.0245 3.6632 4.3641 0.5490  -0.4422 -0.5379 613  GLN A O   
4693  C CB  . GLN A 613  ? 2.7818 3.4734 4.2993 0.5460  -0.4229 -0.5980 613  GLN A CB  
4694  C CG  . GLN A 613  ? 2.6838 3.4345 4.2183 0.5474  -0.3905 -0.5674 613  GLN A CG  
4695  C CD  . GLN A 613  ? 2.5658 3.3552 4.1975 0.5578  -0.3407 -0.5881 613  GLN A CD  
4696  O OE1 . GLN A 613  ? 2.5261 3.3168 4.2185 0.5543  -0.3472 -0.6212 613  GLN A OE1 
4697  N NE2 . GLN A 613  ? 2.5093 3.3310 4.1557 0.5705  -0.2910 -0.5683 613  GLN A NE2 
4698  N N   . ARG A 614  ? 2.2655 2.9376 3.5520 0.4984  -0.5568 -0.5128 614  ARG A N   
4699  C CA  . ARG A 614  ? 2.3930 3.0612 3.5979 0.4978  -0.5616 -0.4743 614  ARG A CA  
4700  C C   . ARG A 614  ? 2.3735 3.1039 3.6030 0.5008  -0.5290 -0.4463 614  ARG A C   
4701  O O   . ARG A 614  ? 2.3521 3.1349 3.5766 0.4773  -0.5650 -0.4223 614  ARG A O   
4702  C CB  . ARG A 614  ? 2.4557 3.1209 3.5893 0.4675  -0.6376 -0.4546 614  ARG A CB  
4703  C CG  . ARG A 614  ? 2.5068 3.1635 3.5506 0.4654  -0.6481 -0.4166 614  ARG A CG  
4704  C CD  . ARG A 614  ? 2.5933 3.2122 3.5611 0.4442  -0.7133 -0.4123 614  ARG A CD  
4705  N NE  . ARG A 614  ? 2.6310 3.2756 3.5267 0.4254  -0.7485 -0.3706 614  ARG A NE  
4706  C CZ  . ARG A 614  ? 2.7031 3.3538 3.5520 0.3948  -0.8158 -0.3588 614  ARG A CZ  
4707  N NH1 . ARG A 614  ? 2.7290 3.3600 3.5951 0.3803  -0.8552 -0.3850 614  ARG A NH1 
4708  N NH2 . ARG A 614  ? 2.7594 3.4358 3.5444 0.3789  -0.8435 -0.3210 614  ARG A NH2 
4709  N N   . GLY A 615  ? 4.6970 5.4204 5.9525 0.5295  -0.4604 -0.4501 615  GLY A N   
4710  C CA  . GLY A 615  ? 4.6435 5.4230 5.9386 0.5371  -0.4189 -0.4309 615  GLY A CA  
4711  C C   . GLY A 615  ? 4.6588 5.4991 5.9308 0.5123  -0.4588 -0.3933 615  GLY A C   
4712  O O   . GLY A 615  ? 4.7410 5.5736 5.9355 0.4981  -0.5017 -0.3669 615  GLY A O   
4713  N N   . ALA A 616  ? 2.7077 3.6087 4.0470 0.5067  -0.4440 -0.3913 616  ALA A N   
4714  C CA  . ALA A 616  ? 2.6961 3.6597 4.0218 0.4844  -0.4752 -0.3565 616  ALA A CA  
4715  C C   . ALA A 616  ? 2.7628 3.7229 4.0091 0.4900  -0.4742 -0.3178 616  ALA A C   
4716  O O   . ALA A 616  ? 2.8388 3.7956 4.0166 0.4697  -0.5287 -0.2971 616  ALA A O   
4717  C CB  . ALA A 616  ? 2.5864 3.6106 3.9955 0.4875  -0.4371 -0.3580 616  ALA A CB  
4718  N N   . LYS A 617  ? 2.9272 3.8856 4.1812 0.5176  -0.4124 -0.3089 617  LYS A N   
4719  C CA  . LYS A 617  ? 2.9574 3.9138 4.1405 0.5260  -0.4056 -0.2720 617  LYS A CA  
4720  C C   . LYS A 617  ? 2.9204 3.9179 4.0537 0.4961  -0.4681 -0.2388 617  LYS A C   
4721  O O   . LYS A 617  ? 2.8571 3.9175 4.0284 0.4811  -0.4783 -0.2266 617  LYS A O   
4722  C CB  . LYS A 617  ? 3.0860 3.9677 4.2053 0.5429  -0.3960 -0.2782 617  LYS A CB  
4723  C CG  . LYS A 617  ? 3.1552 4.0300 4.2168 0.5606  -0.3673 -0.2456 617  LYS A CG  
4724  C CD  . LYS A 617  ? 3.0829 3.9967 4.2003 0.5808  -0.3057 -0.2383 617  LYS A CD  
4725  C CE  . LYS A 617  ? 3.1566 4.0475 4.2237 0.6057  -0.2643 -0.2148 617  LYS A CE  
4726  N NZ  . LYS A 617  ? 3.0812 4.0123 4.2017 0.6242  -0.2067 -0.2061 617  LYS A NZ  
4727  N N   . LYS A 618  ? 2.6014 3.5632 3.6501 0.4870  -0.5091 -0.2251 618  LYS A N   
4728  C CA  . LYS A 618  ? 2.5665 3.5590 3.5623 0.4552  -0.5761 -0.1986 618  LYS A CA  
4729  C C   . LYS A 618  ? 2.5383 3.4758 3.4429 0.4475  -0.6175 -0.1926 618  LYS A C   
4730  O O   . LYS A 618  ? 2.5660 3.4494 3.4346 0.4698  -0.5882 -0.1963 618  LYS A O   
4731  C CB  . LYS A 618  ? 2.6169 3.6687 3.5997 0.4536  -0.5688 -0.1592 618  LYS A CB  
4732  C CG  . LYS A 618  ? 2.5600 3.6776 3.6251 0.4527  -0.5426 -0.1589 618  LYS A CG  
4733  C CD  . LYS A 618  ? 2.5693 3.7381 3.6555 0.4173  -0.5973 -0.1563 618  LYS A CD  
4734  C CE  . LYS A 618  ? 2.4735 3.7137 3.6264 0.4167  -0.5702 -0.1454 618  LYS A CE  
4735  N NZ  . LYS A 618  ? 2.3921 3.6268 3.6135 0.4475  -0.4973 -0.1639 618  LYS A NZ  
4736  N N   . PRO A 619  ? 4.1920 5.1424 5.0583 0.4149  -0.6856 -0.1836 619  PRO A N   
4737  C CA  . PRO A 619  ? 4.2461 5.1510 5.0221 0.4029  -0.7314 -0.1748 619  PRO A CA  
4738  C C   . PRO A 619  ? 4.2410 5.1581 4.9433 0.4045  -0.7348 -0.1343 619  PRO A C   
4739  O O   . PRO A 619  ? 4.2901 5.1607 4.9470 0.4254  -0.7083 -0.1298 619  PRO A O   
4740  C CB  . PRO A 619  ? 4.2953 5.2222 5.0668 0.3657  -0.8004 -0.1781 619  PRO A CB  
4741  C CG  . PRO A 619  ? 4.1961 5.1659 5.0623 0.3620  -0.7862 -0.1978 619  PRO A CG  
4742  C CD  . PRO A 619  ? 4.1182 5.1229 5.0296 0.3868  -0.7229 -0.1865 619  PRO A CD  
4743  N N   . LEU A 620  ? 3.3644 4.3431 4.0549 0.3823  -0.7674 -0.1058 620  LEU A N   
4744  C CA  . LEU A 620  ? 3.3615 4.3603 3.9850 0.3816  -0.7749 -0.0662 620  LEU A CA  
4745  C C   . LEU A 620  ? 3.2968 4.3181 3.9471 0.4118  -0.7109 -0.0506 620  LEU A C   
4746  O O   . LEU A 620  ? 3.3667 4.3865 3.9600 0.4214  -0.7028 -0.0221 620  LEU A O   
4747  C CB  . LEU A 620  ? 3.3189 4.3781 3.9234 0.3466  -0.8321 -0.0426 620  LEU A CB  
4748  C CG  . LEU A 620  ? 3.3136 4.4159 3.8710 0.3452  -0.8357 -0.0007 620  LEU A CG  
4749  C CD1 . LEU A 620  ? 3.4428 4.4994 3.9025 0.3458  -0.8565 0.0163  620  LEU A CD1 
4750  C CD2 . LEU A 620  ? 3.2825 4.4545 3.8481 0.3122  -0.8821 0.0163  620  LEU A CD2 
4751  N N   . GLU A 621  ? 2.4252 3.4671 3.1616 0.4263  -0.6661 -0.0694 621  GLU A N   
4752  C CA  . GLU A 621  ? 2.3691 3.4299 3.1398 0.4559  -0.6011 -0.0591 621  GLU A CA  
4753  C C   . GLU A 621  ? 2.3716 3.3643 3.1151 0.4879  -0.5537 -0.0686 621  GLU A C   
4754  O O   . GLU A 621  ? 2.3885 3.3828 3.1114 0.5097  -0.5153 -0.0473 621  GLU A O   
4755  C CB  . GLU A 621  ? 2.3129 3.4152 3.1843 0.4590  -0.5700 -0.0785 621  GLU A CB  
4756  C CG  . GLU A 621  ? 2.3274 3.4372 3.2490 0.4924  -0.4948 -0.0794 621  GLU A CG  
4757  C CD  . GLU A 621  ? 2.2464 3.3945 3.2676 0.4925  -0.4678 -0.1018 621  GLU A CD  
4758  O OE1 . GLU A 621  ? 2.2007 3.4065 3.2510 0.4678  -0.5002 -0.0944 621  GLU A OE1 
4759  O OE2 . GLU A 621  ? 2.2186 3.3390 3.2891 0.5164  -0.4141 -0.1275 621  GLU A OE2 
4760  N N   . ARG A 622  ? 2.2104 3.1429 2.9518 0.4899  -0.5581 -0.1004 622  ARG A N   
4761  C CA  . ARG A 622  ? 2.2062 3.0677 2.9149 0.5161  -0.5209 -0.1123 622  ARG A CA  
4762  C C   . ARG A 622  ? 2.2151 3.0699 2.8435 0.5241  -0.5191 -0.0757 622  ARG A C   
4763  O O   . ARG A 622  ? 2.2325 3.0716 2.8576 0.5520  -0.4654 -0.0682 622  ARG A O   
4764  C CB  . ARG A 622  ? 2.2787 3.0812 2.9606 0.5048  -0.5564 -0.1395 622  ARG A CB  
4765  C CG  . ARG A 622  ? 2.3209 3.0522 3.0055 0.5315  -0.5113 -0.1679 622  ARG A CG  
4766  C CD  . ARG A 622  ? 2.1561 2.8385 2.8321 0.5185  -0.5481 -0.1989 622  ARG A CD  
4767  N NE  . ARG A 622  ? 2.2833 2.9378 2.8681 0.5001  -0.6021 -0.1819 622  ARG A NE  
4768  C CZ  . ARG A 622  ? 2.3476 2.9483 2.9021 0.4911  -0.6337 -0.2033 622  ARG A CZ  
4769  N NH1 . ARG A 622  ? 2.3167 2.8862 2.9260 0.4994  -0.6176 -0.2429 622  ARG A NH1 
4770  N NH2 . ARG A 622  ? 2.4404 3.0183 2.9096 0.4739  -0.6814 -0.1853 622  ARG A NH2 
4771  N N   . VAL A 623  ? 2.7292 3.5976 3.2929 0.4986  -0.5786 -0.0525 623  VAL A N   
4772  C CA  . VAL A 623  ? 2.7584 3.6298 3.2457 0.5019  -0.5849 -0.0153 623  VAL A CA  
4773  C C   . VAL A 623  ? 2.6375 3.5766 3.1512 0.5091  -0.5615 0.0138  623  VAL A C   
4774  O O   . VAL A 623  ? 2.6606 3.5916 3.1590 0.5346  -0.5171 0.0296  623  VAL A O   
4775  C CB  . VAL A 623  ? 2.2925 3.1613 2.7045 0.4707  -0.6568 -0.0001 623  VAL A CB  
4776  C CG1 . VAL A 623  ? 2.3379 3.2382 2.6863 0.4679  -0.6702 0.0428  623  VAL A CG1 
4777  C CG2 . VAL A 623  ? 2.3624 3.1514 2.7254 0.4713  -0.6700 -0.0215 623  VAL A CG2 
4778  N N   . PHE A 624  ? 2.6699 3.6745 3.2243 0.4871  -0.5901 0.0200  624  PHE A N   
4779  C CA  . PHE A 624  ? 2.5521 3.6247 3.1330 0.4917  -0.5719 0.0476  624  PHE A CA  
4780  C C   . PHE A 624  ? 2.5537 3.6238 3.1873 0.5270  -0.4960 0.0423  624  PHE A C   
4781  O O   . PHE A 624  ? 2.5584 3.6643 3.1889 0.5398  -0.4720 0.0697  624  PHE A O   
4782  C CB  . PHE A 624  ? 2.3315 3.4720 2.9627 0.4632  -0.6079 0.0477  624  PHE A CB  
4783  C CG  . PHE A 624  ? 2.2534 3.4403 2.8306 0.4356  -0.6649 0.0806  624  PHE A CG  
4784  C CD1 . PHE A 624  ? 2.2165 3.4215 2.7861 0.3997  -0.7272 0.0748  624  PHE A CD1 
4785  C CD2 . PHE A 624  ? 2.2342 3.4469 2.7684 0.4455  -0.6562 0.1167  624  PHE A CD2 
4786  C CE1 . PHE A 624  ? 2.2417 3.4896 2.7617 0.3734  -0.7788 0.1038  624  PHE A CE1 
4787  C CE2 . PHE A 624  ? 2.2547 3.5118 2.7405 0.4201  -0.7083 0.1459  624  PHE A CE2 
4788  C CZ  . PHE A 624  ? 2.2668 3.5417 2.7456 0.3836  -0.7691 0.1392  624  PHE A CZ  
4789  N N   . GLN A 625  ? 2.2565 3.2849 2.9382 0.5427  -0.4584 0.0070  625  GLN A N   
4790  C CA  . GLN A 625  ? 2.2903 3.3078 3.0156 0.5765  -0.3847 0.0000  625  GLN A CA  
4791  C C   . GLN A 625  ? 2.3780 3.3540 3.0322 0.5986  -0.3605 0.0204  625  GLN A C   
4792  O O   . GLN A 625  ? 2.3926 3.4006 3.0217 0.6065  -0.3512 0.0535  625  GLN A O   
4793  C CB  . GLN A 625  ? 2.3606 3.3332 3.1408 0.5880  -0.3523 -0.0434 625  GLN A CB  
4794  C CG  . GLN A 625  ? 2.3630 3.3708 3.2172 0.5683  -0.3721 -0.0673 625  GLN A CG  
4795  C CD  . GLN A 625  ? 2.4091 3.3863 3.3337 0.5865  -0.3230 -0.1072 625  GLN A CD  
4796  O OE1 . GLN A 625  ? 2.4572 3.4038 3.3897 0.6158  -0.2638 -0.1128 625  GLN A OE1 
4797  N NE2 . GLN A 625  ? 2.3876 3.3727 3.3632 0.5690  -0.3471 -0.1355 625  GLN A NE2 
4798  N N   . PHE A 626  ? 2.0873 2.9907 2.7088 0.6085  -0.3510 0.0001  626  PHE A N   
4799  C CA  . PHE A 626  ? 2.1764 3.0321 2.7206 0.6254  -0.3362 0.0175  626  PHE A CA  
4800  C C   . PHE A 626  ? 2.1019 3.0002 2.5861 0.6151  -0.3696 0.0619  626  PHE A C   
4801  O O   . PHE A 626  ? 2.0696 2.9870 2.5456 0.6342  -0.3361 0.0866  626  PHE A O   
4802  C CB  . PHE A 626  ? 2.3337 3.1202 2.8294 0.6177  -0.3625 -0.0035 626  PHE A CB  
4803  C CG  . PHE A 626  ? 2.5447 3.2823 2.9502 0.6281  -0.3606 0.0160  626  PHE A CG  
4804  C CD1 . PHE A 626  ? 2.6355 3.3124 3.0307 0.6567  -0.3057 0.0030  626  PHE A CD1 
4805  C CD2 . PHE A 626  ? 2.6471 3.3986 2.9768 0.6084  -0.4142 0.0467  626  PHE A CD2 
4806  C CE1 . PHE A 626  ? 2.7815 3.4119 3.0917 0.6655  -0.3041 0.0210  626  PHE A CE1 
4807  C CE2 . PHE A 626  ? 2.7938 3.5005 3.0391 0.6173  -0.4132 0.0648  626  PHE A CE2 
4808  C CZ  . PHE A 626  ? 2.8586 3.5041 3.0937 0.6458  -0.3583 0.0522  626  PHE A CZ  
4809  N N   . LEU A 627  ? 1.6794 2.5953 2.1252 0.5842  -0.4361 0.0712  627  LEU A N   
4810  C CA  . LEU A 627  ? 1.6778 2.6232 2.0533 0.5713  -0.4755 0.1104  627  LEU A CA  
4811  C C   . LEU A 627  ? 1.6229 2.6303 2.0136 0.5824  -0.4535 0.1427  627  LEU A C   
4812  O O   . LEU A 627  ? 1.7331 2.7552 2.0618 0.5812  -0.4713 0.1758  627  LEU A O   
4813  C CB  . LEU A 627  ? 1.6126 2.5830 1.9694 0.5331  -0.5484 0.1108  627  LEU A CB  
4814  C CG  . LEU A 627  ? 1.5974 2.6087 1.8901 0.5103  -0.6023 0.1469  627  LEU A CG  
4815  C CD1 . LEU A 627  ? 1.6424 2.6347 1.8932 0.4776  -0.6679 0.1370  627  LEU A CD1 
4816  C CD2 . LEU A 627  ? 1.4738 2.5699 1.8161 0.5026  -0.6051 0.1656  627  LEU A CD2 
4817  N N   . GLU A 628  ? 2.2135 3.2582 2.6861 0.5931  -0.4153 0.1334  628  GLU A N   
4818  C CA  . GLU A 628  ? 2.1646 3.2656 2.6530 0.6053  -0.3917 0.1631  628  GLU A CA  
4819  C C   . GLU A 628  ? 2.1289 3.2073 2.6574 0.6414  -0.3161 0.1543  628  GLU A C   
4820  O O   . GLU A 628  ? 2.0411 3.1619 2.6399 0.6498  -0.2833 0.1517  628  GLU A O   
4821  C CB  . GLU A 628  ? 2.1009 3.2814 2.6476 0.5831  -0.4175 0.1680  628  GLU A CB  
4822  C CG  . GLU A 628  ? 2.3620 3.5540 3.0041 0.5844  -0.3891 0.1349  628  GLU A CG  
4823  C CD  . GLU A 628  ? 2.2897 3.5640 2.9937 0.5728  -0.3932 0.1462  628  GLU A CD  
4824  O OE1 . GLU A 628  ? 2.3104 3.6231 3.0121 0.5864  -0.3715 0.1746  628  GLU A OE1 
4825  O OE2 . GLU A 628  ? 2.2058 3.5054 2.9605 0.5503  -0.4176 0.1263  628  GLU A OE2 
4826  N N   . LYS A 629  ? 1.6653 2.6748 2.1483 0.6620  -0.2876 0.1488  629  LYS A N   
4827  C CA  . LYS A 629  ? 1.6441 2.6293 2.1487 0.6973  -0.2161 0.1466  629  LYS A CA  
4828  C C   . LYS A 629  ? 1.6960 2.6860 2.1327 0.7108  -0.2120 0.1863  629  LYS A C   
4829  O O   . LYS A 629  ? 1.6741 2.6399 2.1048 0.7404  -0.1583 0.1933  629  LYS A O   
4830  C CB  . LYS A 629  ? 1.6875 2.5944 2.1941 0.7118  -0.1824 0.1117  629  LYS A CB  
4831  C CG  . LYS A 629  ? 1.5930 2.5022 2.1698 0.6969  -0.1915 0.0731  629  LYS A CG  
4832  C CD  . LYS A 629  ? 1.7780 2.7677 2.4249 0.6836  -0.2013 0.0788  629  LYS A CD  
4833  C CE  . LYS A 629  ? 1.4955 2.4948 2.2122 0.6662  -0.2152 0.0433  629  LYS A CE  
4834  N NZ  . LYS A 629  ? 1.3701 2.4499 2.1437 0.6502  -0.2310 0.0540  629  LYS A NZ  
4835  N N   . SER A 630  ? 1.1997 2.2232 1.5861 0.6872  -0.2717 0.2118  630  SER A N   
4836  C CA  . SER A 630  ? 1.2719 2.3177 1.5968 0.6928  -0.2825 0.2526  630  SER A CA  
4837  C C   . SER A 630  ? 1.2188 2.3411 1.5937 0.6973  -0.2693 0.2734  630  SER A C   
4838  O O   . SER A 630  ? 1.3187 2.4766 1.6562 0.7002  -0.2811 0.3085  630  SER A O   
4839  C CB  . SER A 630  ? 1.2972 2.3507 1.5517 0.6628  -0.3545 0.2686  630  SER A CB  
4840  O OG  . SER A 630  ? 1.1757 2.2849 1.4671 0.6318  -0.4016 0.2640  630  SER A OG  
4841  N N   . ASP A 631  ? 1.9892 3.1386 2.4503 0.6969  -0.2462 0.2514  631  ASP A N   
4842  C CA  . ASP A 631  ? 1.9253 3.1412 2.4394 0.7051  -0.2233 0.2683  631  ASP A CA  
4843  C C   . ASP A 631  ? 1.9758 3.1582 2.4836 0.7434  -0.1568 0.2758  631  ASP A C   
4844  O O   . ASP A 631  ? 1.9358 3.0766 2.4823 0.7623  -0.1056 0.2491  631  ASP A O   
4845  C CB  . ASP A 631  ? 1.8611 3.1131 2.4691 0.6932  -0.2160 0.2414  631  ASP A CB  
4846  C CG  . ASP A 631  ? 1.9379 3.2769 2.5874 0.6817  -0.2306 0.2626  631  ASP A CG  
4847  O OD1 . ASP A 631  ? 1.9374 3.3011 2.6290 0.7039  -0.1820 0.2708  631  ASP A OD1 
4848  O OD2 . ASP A 631  ? 1.9636 3.3450 2.6031 0.6503  -0.2898 0.2707  631  ASP A OD2 
4849  N N   . LEU A 632  ? 1.7788 2.9767 2.2327 0.7543  -0.1598 0.3124  632  LEU A N   
4850  C CA  . LEU A 632  ? 1.8392 3.0043 2.2729 0.7902  -0.1024 0.3250  632  LEU A CA  
4851  C C   . LEU A 632  ? 1.7256 2.9170 2.2428 0.8102  -0.0436 0.3158  632  LEU A C   
4852  O O   . LEU A 632  ? 1.7478 2.8905 2.2821 0.8356  0.0144  0.2987  632  LEU A O   
4853  C CB  . LEU A 632  ? 1.9546 3.1430 2.3179 0.7950  -0.1244 0.3685  632  LEU A CB  
4854  C CG  . LEU A 632  ? 2.0474 3.2163 2.3232 0.7747  -0.1838 0.3825  632  LEU A CG  
4855  C CD1 . LEU A 632  ? 2.0796 3.2998 2.3075 0.7721  -0.2148 0.4253  632  LEU A CD1 
4856  C CD2 . LEU A 632  ? 2.1606 3.2409 2.3770 0.7894  -0.1634 0.3714  632  LEU A CD2 
4857  N N   . GLY A 633  ? 2.1050 3.3725 2.6744 0.7976  -0.0587 0.3258  633  GLY A N   
4858  C CA  . GLY A 633  ? 1.9646 3.2636 2.6116 0.8150  -0.0060 0.3204  633  GLY A CA  
4859  C C   . GLY A 633  ? 1.8070 3.0831 2.5259 0.8143  0.0253  0.2784  633  GLY A C   
4860  O O   . GLY A 633  ? 1.8363 3.0548 2.5397 0.8100  0.0217  0.2521  633  GLY A O   
4861  N N   . CYS A 634  ? 1.5634 2.8856 2.3614 0.8183  0.0558  0.2721  634  CYS A N   
4862  C CA  . CYS A 634  ? 1.4924 2.7999 2.3653 0.8179  0.0880  0.2327  634  CYS A CA  
4863  C C   . CYS A 634  ? 1.3951 2.7683 2.3564 0.8141  0.1078  0.2287  634  CYS A C   
4864  O O   . CYS A 634  ? 1.4350 2.8609 2.4039 0.8198  0.1127  0.2570  634  CYS A O   
4865  C CB  . CYS A 634  ? 1.5622 2.7974 2.4295 0.8490  0.1522  0.2148  634  CYS A CB  
4866  S SG  . CYS A 634  ? 1.9275 3.1457 2.8888 0.8519  0.1988  0.1667  634  CYS A SG  
4867  N N   . GLY A 635  ? 1.4781 2.8478 2.5058 0.8041  0.1185  0.1928  635  GLY A N   
4868  C CA  . GLY A 635  ? 1.3422 2.7638 2.4580 0.8024  0.1461  0.1829  635  GLY A CA  
4869  C C   . GLY A 635  ? 1.2600 2.7456 2.4210 0.7675  0.0961  0.1784  635  GLY A C   
4870  O O   . GLY A 635  ? 1.2654 2.7536 2.3948 0.7402  0.0347  0.1771  635  GLY A O   
4871  N N   . ALA A 636  ? 1.1508 2.6860 2.3874 0.7685  0.1252  0.1745  636  ALA A N   
4872  C CA  . ALA A 636  ? 1.0694 2.6766 2.3504 0.7386  0.0851  0.1780  636  ALA A CA  
4873  C C   . ALA A 636  ? 1.0714 2.7306 2.3146 0.7365  0.0596  0.2203  636  ALA A C   
4874  O O   . ALA A 636  ? 1.0327 2.7524 2.2888 0.7095  0.0139  0.2319  636  ALA A O   
4875  C CB  . ALA A 636  ? 1.0312 2.6686 2.4050 0.7431  0.1315  0.1588  636  ALA A CB  
4876  N N   . GLY A 637  ? 1.0476 2.6819 2.2444 0.7658  0.0911  0.2428  637  GLY A N   
4877  C CA  . GLY A 637  ? 1.1114 2.7845 2.2610 0.7686  0.0690  0.2838  637  GLY A CA  
4878  C C   . GLY A 637  ? 1.2044 2.8848 2.3655 0.8029  0.1290  0.3030  637  GLY A C   
4879  O O   . GLY A 637  ? 1.1499 2.8121 2.3631 0.8218  0.1878  0.2838  637  GLY A O   
4880  N N   . GLY A 638  ? 1.1355 2.8402 2.2459 0.8113  0.1143  0.3404  638  GLY A N   
4881  C CA  . GLY A 638  ? 1.1698 2.9030 2.2961 0.8381  0.1588  0.3644  638  GLY A CA  
4882  C C   . GLY A 638  ? 1.1944 2.8756 2.3344 0.8749  0.2345  0.3543  638  GLY A C   
4883  O O   . GLY A 638  ? 1.2177 2.8655 2.4021 0.8775  0.2680  0.3210  638  GLY A O   
4884  N N   . GLY A 639  ? 1.6908 3.3676 2.7946 0.9032  0.2622  0.3833  639  GLY A N   
4885  C CA  . GLY A 639  ? 1.7203 3.3369 2.8166 0.9390  0.3299  0.3771  639  GLY A CA  
4886  C C   . GLY A 639  ? 1.7120 3.3461 2.8660 0.9642  0.3960  0.3788  639  GLY A C   
4887  O O   . GLY A 639  ? 1.5807 3.2451 2.8129 0.9555  0.4161  0.3581  639  GLY A O   
4888  N N   . LEU A 640  ? 0.7774 2.3903 1.8894 0.9958  0.4297  0.4040  640  LEU A N   
4889  C CA  . LEU A 640  ? 0.7993 2.4019 1.9473 1.0273  0.5027  0.4041  640  LEU A CA  
4890  C C   . LEU A 640  ? 0.8488 2.4756 1.9554 1.0495  0.5068  0.4467  640  LEU A C   
4891  O O   . LEU A 640  ? 0.8416 2.4875 1.9824 1.0712  0.5538  0.4566  640  LEU A O   
4892  C CB  . LEU A 640  ? 0.8475 2.3620 1.9787 1.0484  0.5542  0.3782  640  LEU A CB  
4893  C CG  . LEU A 640  ? 0.7527 2.2272 1.9179 1.0789  0.6366  0.3628  640  LEU A CG  
4894  C CD1 . LEU A 640  ? 0.6937 2.2269 1.9279 1.0865  0.6703  0.3708  640  LEU A CD1 
4895  C CD2 . LEU A 640  ? 0.7657 2.1853 1.9596 1.0735  0.6614  0.3179  640  LEU A CD2 
4896  N N   . ASN A 641  ? 1.3671 2.9928 2.3994 1.0432  0.4559  0.4711  641  ASN A N   
4897  C CA  . ASN A 641  ? 1.4110 3.0708 2.3997 1.0569  0.4411  0.5133  641  ASN A CA  
4898  C C   . ASN A 641  ? 1.4364 3.1273 2.3802 1.0281  0.3637  0.5277  641  ASN A C   
4899  O O   . ASN A 641  ? 1.4652 3.1199 2.3805 1.0095  0.3326  0.5096  641  ASN A O   
4900  C CB  . ASN A 641  ? 1.5712 3.1640 2.4896 1.0901  0.4743  0.5281  641  ASN A CB  
4901  C CG  . ASN A 641  ? 1.6412 3.1589 2.5718 1.1069  0.5330  0.4968  641  ASN A CG  
4902  O OD1 . ASN A 641  ? 1.6147 3.1379 2.6124 1.1156  0.5826  0.4788  641  ASN A OD1 
4903  N ND2 . ASN A 641  ? 1.7465 3.1934 2.6131 1.1106  0.5284  0.4889  641  ASN A ND2 
4904  N N   . ASN A 642  ? 1.6807 3.4371 2.6161 1.0244  0.3324  0.5601  642  ASN A N   
4905  C CA  . ASN A 642  ? 1.7085 3.4986 2.6007 0.9957  0.2578  0.5746  642  ASN A CA  
4906  C C   . ASN A 642  ? 1.7951 3.5140 2.6058 0.9974  0.2400  0.5724  642  ASN A C   
4907  O O   . ASN A 642  ? 1.7569 3.4753 2.5356 0.9694  0.1844  0.5672  642  ASN A O   
4908  C CB  . ASN A 642  ? 1.8099 3.6631 2.6816 1.0015  0.2344  0.6147  642  ASN A CB  
4909  C CG  . ASN A 642  ? 1.9072 3.7881 2.7236 0.9739  0.1591  0.6309  642  ASN A CG  
4910  O OD1 . ASN A 642  ? 2.0314 3.9273 2.7919 0.9837  0.1381  0.6633  642  ASN A OD1 
4911  N ND2 . ASN A 642  ? 1.8574 3.7434 2.6876 0.9390  0.1179  0.6077  642  ASN A ND2 
4912  N N   . ALA A 643  ? 1.4889 3.1458 2.2655 1.0308  0.2896  0.5761  643  ALA A N   
4913  C CA  . ALA A 643  ? 1.6081 3.1875 2.3138 1.0357  0.2858  0.5693  643  ALA A CA  
4914  C C   . ALA A 643  ? 1.4771 3.0181 2.2135 1.0162  0.2858  0.5272  643  ALA A C   
4915  O O   . ALA A 643  ? 1.4479 2.9769 2.1505 0.9910  0.2356  0.5190  643  ALA A O   
4916  C CB  . ALA A 643  ? 1.7715 3.2930 2.4445 1.0759  0.3463  0.5789  643  ALA A CB  
4917  N N   . ASN A 644  ? 1.3253 2.8481 2.1260 1.0274  0.3413  0.5003  644  ASN A N   
4918  C CA  . ASN A 644  ? 1.2610 2.7470 2.0955 1.0115  0.3459  0.4591  644  ASN A CA  
4919  C C   . ASN A 644  ? 1.2071 2.7379 2.0592 0.9710  0.2792  0.4495  644  ASN A C   
4920  O O   . ASN A 644  ? 1.2710 2.7632 2.0971 0.9537  0.2505  0.4299  644  ASN A O   
4921  C CB  . ASN A 644  ? 1.1451 2.6268 2.0600 1.0260  0.4114  0.4340  644  ASN A CB  
4922  C CG  . ASN A 644  ? 1.0874 2.5257 2.0378 1.0134  0.4228  0.3895  644  ASN A CG  
4923  O OD1 . ASN A 644  ? 1.0304 2.4505 2.0371 1.0261  0.4784  0.3651  644  ASN A OD1 
4924  N ND2 . ASN A 644  ? 1.1207 2.5428 2.0385 0.9883  0.3702  0.3787  644  ASN A ND2 
4925  N N   . VAL A 645  ? 1.9436 3.5546 2.8380 0.9559  0.2547  0.4636  645  VAL A N   
4926  C CA  . VAL A 645  ? 1.8640 3.5235 2.7790 0.9165  0.1924  0.4558  645  VAL A CA  
4927  C C   . VAL A 645  ? 1.9566 3.6010 2.7913 0.8978  0.1293  0.4681  645  VAL A C   
4928  O O   . VAL A 645  ? 1.9200 3.5541 2.7524 0.8700  0.0892  0.4475  645  VAL A O   
4929  C CB  . VAL A 645  ? 1.8144 3.5637 2.7748 0.9061  0.1761  0.4761  645  VAL A CB  
4930  C CG1 . VAL A 645  ? 1.7436 3.5396 2.7325 0.8647  0.1177  0.4637  645  VAL A CG1 
4931  C CG2 . VAL A 645  ? 1.7301 3.4956 2.7647 0.9268  0.2403  0.4684  645  VAL A CG2 
4932  N N   . PHE A 646  ? 1.1665 2.8102 1.9355 0.9134  0.1210  0.5021  646  PHE A N   
4933  C CA  . PHE A 646  ? 1.2341 2.8581 1.9172 0.9015  0.0683  0.5181  646  PHE A CA  
4934  C C   . PHE A 646  ? 1.3365 2.8719 1.9728 0.9079  0.0799  0.4975  646  PHE A C   
4935  O O   . PHE A 646  ? 1.3770 2.8899 1.9591 0.8880  0.0322  0.4957  646  PHE A O   
4936  C CB  . PHE A 646  ? 1.3021 2.9432 1.9327 0.9231  0.0697  0.5587  646  PHE A CB  
4937  C CG  . PHE A 646  ? 1.2215 2.9440 1.8507 0.9030  0.0180  0.5851  646  PHE A CG  
4938  C CD1 . PHE A 646  ? 1.1364 2.9207 1.8074 0.9154  0.0371  0.6052  646  PHE A CD1 
4939  C CD2 . PHE A 646  ? 1.2090 2.9467 1.7954 0.8709  -0.0500 0.5889  646  PHE A CD2 
4940  C CE1 . PHE A 646  ? 1.0944 2.9556 1.7647 0.8961  -0.0113 0.6288  646  PHE A CE1 
4941  C CE2 . PHE A 646  ? 1.1638 2.9771 1.7477 0.8510  -0.0984 0.6123  646  PHE A CE2 
4942  C CZ  . PHE A 646  ? 1.1080 2.9840 1.7346 0.8635  -0.0792 0.6320  646  PHE A CZ  
4943  N N   . HIS A 647  ? 1.8152 3.2998 2.4712 0.9362  0.1449  0.4823  647  HIS A N   
4944  C CA  . HIS A 647  ? 1.9079 3.3089 2.5299 0.9429  0.1625  0.4587  647  HIS A CA  
4945  C C   . HIS A 647  ? 1.7041 3.1026 2.3655 0.9129  0.1348  0.4236  647  HIS A C   
4946  O O   . HIS A 647  ? 1.7016 3.0911 2.3199 0.8889  0.0806  0.4219  647  HIS A O   
4947  C CB  . HIS A 647  ? 2.0589 3.4103 2.7021 0.9777  0.2401  0.4470  647  HIS A CB  
4948  C CG  . HIS A 647  ? 2.3163 3.5795 2.8993 0.9920  0.2603  0.4359  647  HIS A CG  
4949  N ND1 . HIS A 647  ? 2.3925 3.6149 2.9400 0.9713  0.2232  0.4170  647  HIS A ND1 
4950  C CD2 . HIS A 647  ? 2.4881 3.6928 3.0378 1.0241  0.3133  0.4401  647  HIS A CD2 
4951  C CE1 . HIS A 647  ? 2.5265 3.6725 3.0242 0.9898  0.2527  0.4102  647  HIS A CE1 
4952  N NE2 . HIS A 647  ? 2.5935 3.7260 3.0903 1.0220  0.3081  0.4240  647  HIS A NE2 
4953  N N   . LEU A 648  ? 1.3393 2.7485 2.0830 0.9136  0.1703  0.3965  648  LEU A N   
4954  C CA  . LEU A 648  ? 1.2318 2.6335 2.0188 0.8882  0.1511  0.3599  648  LEU A CA  
4955  C C   . LEU A 648  ? 1.1781 2.6192 1.9443 0.8514  0.0742  0.3663  648  LEU A C   
4956  O O   . LEU A 648  ? 1.1415 2.5677 1.9214 0.8285  0.0463  0.3395  648  LEU A O   
4957  C CB  . LEU A 648  ? 1.0691 2.5043 1.9531 0.8895  0.1895  0.3386  648  LEU A CB  
4958  C CG  . LEU A 648  ? 1.0470 2.4192 1.9578 0.9149  0.2580  0.3101  648  LEU A CG  
4959  C CD1 . LEU A 648  ? 0.9528 2.3559 1.9337 0.9338  0.3159  0.3091  648  LEU A CD1 
4960  C CD2 . LEU A 648  ? 0.9986 2.3355 1.9360 0.8969  0.2473  0.2692  648  LEU A CD2 
4961  N N   . ALA A 649  ? 1.1722 2.6637 1.9047 0.8464  0.0407  0.4020  649  ALA A N   
4962  C CA  . ALA A 649  ? 1.1428 2.6722 1.8440 0.8126  -0.0328 0.4132  649  ALA A CA  
4963  C C   . ALA A 649  ? 1.2181 2.6878 1.8377 0.8053  -0.0659 0.4114  649  ALA A C   
4964  O O   . ALA A 649  ? 1.1973 2.6849 1.7846 0.7760  -0.1272 0.4158  649  ALA A O   
4965  C CB  . ALA A 649  ? 1.2001 2.7952 1.8832 0.8134  -0.0534 0.4526  649  ALA A CB  
4966  N N   . GLY A 650  ? 1.7884 3.1862 2.3734 0.8312  -0.0250 0.4049  650  GLY A N   
4967  C CA  . GLY A 650  ? 1.9250 3.2661 2.4253 0.8276  -0.0526 0.4084  650  GLY A CA  
4968  C C   . GLY A 650  ? 2.0424 3.4064 2.4716 0.8314  -0.0802 0.4500  650  GLY A C   
4969  O O   . GLY A 650  ? 2.1136 3.4488 2.4680 0.8211  -0.1185 0.4594  650  GLY A O   
4970  N N   . LEU A 651  ? 1.4781 2.8951 1.9315 0.8462  -0.0607 0.4748  651  LEU A N   
4971  C CA  . LEU A 651  ? 1.6111 3.0495 2.0018 0.8554  -0.0784 0.5146  651  LEU A CA  
4972  C C   . LEU A 651  ? 1.7116 3.1121 2.0809 0.8956  -0.0190 0.5289  651  LEU A C   
4973  O O   . LEU A 651  ? 1.6828 3.0483 2.0939 0.9169  0.0396  0.5087  651  LEU A O   
4974  C CB  . LEU A 651  ? 1.5273 3.0587 1.9542 0.8427  -0.1050 0.5369  651  LEU A CB  
4975  C CG  . LEU A 651  ? 1.4558 3.0372 1.8847 0.8017  -0.1744 0.5355  651  LEU A CG  
4976  C CD1 . LEU A 651  ? 1.3824 3.0528 1.8417 0.7951  -0.1920 0.5612  651  LEU A CD1 
4977  C CD2 . LEU A 651  ? 1.5771 3.1266 1.9157 0.7870  -0.2240 0.5461  651  LEU A CD2 
4978  N N   . THR A 652  ? 1.4600 2.8663 1.7606 0.9050  -0.0363 0.5636  652  THR A N   
4979  C CA  . THR A 652  ? 1.4857 2.9109 1.7857 0.9366  0.0023  0.5915  652  THR A CA  
4980  C C   . THR A 652  ? 1.4928 2.9772 1.7468 0.9267  -0.0493 0.6299  652  THR A C   
4981  O O   . THR A 652  ? 1.5260 3.0095 1.7247 0.9034  -0.1041 0.6364  652  THR A O   
4982  C CB  . THR A 652  ? 1.5715 2.9175 1.8386 0.9727  0.0633  0.5892  652  THR A CB  
4983  O OG1 . THR A 652  ? 1.5515 2.9182 1.8604 1.0022  0.1169  0.6005  652  THR A OG1 
4984  C CG2 . THR A 652  ? 1.7315 3.0390 1.8998 0.9796  0.0422  0.6137  652  THR A CG2 
4985  N N   . PHE A 653  ? 1.5984 3.1366 1.8794 0.9434  -0.0316 0.6540  653  PHE A N   
4986  C CA  . PHE A 653  ? 1.6454 3.2613 1.9146 0.9299  -0.0790 0.6847  653  PHE A CA  
4987  C C   . PHE A 653  ? 1.8104 3.4218 2.0290 0.9614  -0.0596 0.7196  653  PHE A C   
4988  O O   . PHE A 653  ? 1.8376 3.3988 2.0536 0.9939  -0.0023 0.7180  653  PHE A O   
4989  C CB  . PHE A 653  ? 1.5446 3.2306 1.9032 0.9255  -0.0663 0.6804  653  PHE A CB  
4990  C CG  . PHE A 653  ? 1.5680 3.2330 1.9776 0.9587  0.0071  0.6722  653  PHE A CG  
4991  C CD1 . PHE A 653  ? 1.5759 3.2917 2.0187 0.9788  0.0325  0.6944  653  PHE A CD1 
4992  C CD2 . PHE A 653  ? 1.5723 3.1641 1.9932 0.9706  0.0518  0.6424  653  PHE A CD2 
4993  C CE1 . PHE A 653  ? 1.5584 3.2522 2.0456 1.0092  0.1010  0.6867  653  PHE A CE1 
4994  C CE2 . PHE A 653  ? 1.5548 3.1255 2.0201 1.0005  0.1201  0.6342  653  PHE A CE2 
4995  C CZ  . PHE A 653  ? 1.5449 3.1662 2.0432 1.0195  0.1449  0.6564  653  PHE A CZ  
4996  N N   . LEU A 654  ? 1.9565 3.6214 2.1368 0.9526  -0.1056 0.7511  654  LEU A N   
4997  C CA  . LEU A 654  ? 2.1600 3.8194 2.2821 0.9809  -0.0950 0.7861  654  LEU A CA  
4998  C C   . LEU A 654  ? 2.2558 3.9971 2.4136 0.9908  -0.0954 0.8134  654  LEU A C   
4999  O O   . LEU A 654  ? 2.3247 4.1275 2.4647 0.9715  -0.1479 0.8335  654  LEU A O   
5000  C CB  . LEU A 654  ? 2.2143 3.8570 2.2453 0.9656  -0.1485 0.8025  654  LEU A CB  
5001  C CG  . LEU A 654  ? 2.3530 3.9357 2.3117 0.9975  -0.1210 0.8221  654  LEU A CG  
5002  C CD1 . LEU A 654  ? 2.3471 3.8679 2.3375 1.0277  -0.0478 0.8028  654  LEU A CD1 
5003  C CD2 . LEU A 654  ? 2.4497 3.9820 2.3231 0.9811  -0.1599 0.8220  654  LEU A CD2 
5004  N N   . THR A 655  ? 2.1680 3.9100 2.3750 1.0208  -0.0367 0.8140  655  THR A N   
5005  C CA  . THR A 655  ? 2.1693 3.9901 2.4207 1.0302  -0.0330 0.8366  655  THR A CA  
5006  C C   . THR A 655  ? 2.3309 4.1322 2.5837 1.0742  0.0267  0.8539  655  THR A C   
5007  O O   . THR A 655  ? 2.2867 4.0370 2.5680 1.0952  0.0854  0.8354  655  THR A O   
5008  C CB  . THR A 655  ? 2.3191 4.1990 2.6655 1.0086  -0.0337 0.8155  655  THR A CB  
5009  O OG1 . THR A 655  ? 2.2403 4.1579 2.5826 0.9667  -0.0985 0.8080  655  THR A OG1 
5010  C CG2 . THR A 655  ? 2.2682 4.2204 2.6641 1.0243  -0.0168 0.8373  655  THR A CG2 
5011  N N   . ASN A 656  ? 2.3063 4.1488 2.5263 1.0878  0.0102  0.8899  656  ASN A N   
5012  C CA  . ASN A 656  ? 2.4837 4.3264 2.7149 1.1274  0.0607  0.9094  656  ASN A CA  
5013  C C   . ASN A 656  ? 2.3673 4.2836 2.6882 1.1261  0.0754  0.9076  656  ASN A C   
5014  O O   . ASN A 656  ? 2.3435 4.3399 2.6846 1.1074  0.0329  0.9217  656  ASN A O   
5015  C CB  . ASN A 656  ? 2.6948 4.5433 2.8500 1.1459  0.0405  0.9485  656  ASN A CB  
5016  C CG  . ASN A 656  ? 2.8240 4.5809 2.8966 1.1619  0.0547  0.9499  656  ASN A CG  
5017  O OD1 . ASN A 656  ? 2.9618 4.7089 2.9659 1.1785  0.0429  0.9793  656  ASN A OD1 
5018  N ND2 . ASN A 656  ? 2.7702 4.4593 2.8497 1.1567  0.0808  0.9174  656  ASN A ND2 
5019  N N   . ALA A 657  ? 2.8843 4.7697 3.2588 1.1446  0.1371  0.8880  657  ALA A N   
5020  C CA  . ALA A 657  ? 2.7437 4.6840 3.2056 1.1492  0.1665  0.8832  657  ALA A CA  
5021  C C   . ALA A 657  ? 2.6837 4.5617 3.1862 1.1617  0.2286  0.8512  657  ALA A C   
5022  O O   . ALA A 657  ? 2.6987 4.5618 3.2285 1.1927  0.2866  0.8542  657  ALA A O   
5023  C CB  . ALA A 657  ? 2.5876 4.6048 3.1000 1.1096  0.1171  0.8741  657  ALA A CB  
5024  N N   . ASN A 658  ? 2.8370 4.6763 3.3407 1.1376  0.2164  0.8203  658  ASN A N   
5025  C CA  . ASN A 658  ? 2.7779 4.5560 3.3176 1.1467  0.2716  0.7871  658  ASN A CA  
5026  C C   . ASN A 658  ? 2.8619 4.5489 3.3333 1.1532  0.2799  0.7760  658  ASN A C   
5027  O O   . ASN A 658  ? 2.9344 4.6090 3.3353 1.1425  0.2342  0.7895  658  ASN A O   
5028  C CB  . ASN A 658  ? 2.5917 4.4008 3.2051 1.1139  0.2584  0.7548  658  ASN A CB  
5029  C CG  . ASN A 658  ? 2.4242 4.3002 3.1222 1.1160  0.2812  0.7552  658  ASN A CG  
5030  O OD1 . ASN A 658  ? 2.2725 4.1785 3.0362 1.0916  0.2753  0.7307  658  ASN A OD1 
5031  N ND2 . ASN A 658  ? 2.4518 4.3511 3.1489 1.1453  0.3079  0.7832  658  ASN A ND2 
5032  N N   . ALA A 659  ? 2.2912 3.9152 2.7848 1.1701  0.3389  0.7508  659  ALA A N   
5033  C CA  . ALA A 659  ? 2.3845 3.9178 2.8231 1.1754  0.3537  0.7340  659  ALA A CA  
5034  C C   . ALA A 659  ? 2.3112 3.8322 2.7499 1.1391  0.3110  0.7060  659  ALA A C   
5035  O O   . ALA A 659  ? 2.2309 3.7350 2.7249 1.1291  0.3332  0.6715  659  ALA A O   
5036  C CB  . ALA A 659  ? 2.3976 3.8708 2.8650 1.2033  0.4312  0.7136  659  ALA A CB  
5037  N N   . ASP A 660  ? 2.0834 3.6115 2.4590 1.1199  0.2504  0.7208  660  ASP A N   
5038  C CA  . ASP A 660  ? 2.0228 3.5368 2.3884 1.0853  0.2053  0.6971  660  ASP A CA  
5039  C C   . ASP A 660  ? 2.0429 3.4644 2.3833 1.0905  0.2344  0.6678  660  ASP A C   
5040  O O   . ASP A 660  ? 2.0070 3.4008 2.3134 1.0673  0.1966  0.6538  660  ASP A O   
5041  C CB  . ASP A 660  ? 2.1102 3.6603 2.4165 1.0612  0.1312  0.7204  660  ASP A CB  
5042  C CG  . ASP A 660  ? 2.3237 3.8533 2.5463 1.0830  0.1262  0.7553  660  ASP A CG  
5043  O OD1 . ASP A 660  ? 2.4382 3.8904 2.6110 1.1027  0.1569  0.7518  660  ASP A OD1 
5044  O OD2 . ASP A 660  ? 2.3696 3.9612 2.5751 1.0792  0.0896  0.7859  660  ASP A OD2 
5045  N N   . ASP A 661  ? 1.9414 3.3166 2.3016 1.1204  0.3027  0.6575  661  ASP A N   
5046  C CA  . ASP A 661  ? 1.9800 3.2649 2.3153 1.1303  0.3390  0.6314  661  ASP A CA  
5047  C C   . ASP A 661  ? 1.9089 3.1768 2.2850 1.1032  0.3273  0.5904  661  ASP A C   
5048  O O   . ASP A 661  ? 1.8181 3.1351 2.2177 1.0719  0.2758  0.5849  661  ASP A O   
5049  C CB  . ASP A 661  ? 1.9383 3.1840 2.2939 1.1672  0.4169  0.6282  661  ASP A CB  
5050  C CG  . ASP A 661  ? 1.6753 2.9526 2.1288 1.1670  0.4546  0.6048  661  ASP A CG  
5051  O OD1 . ASP A 661  ? 1.5478 2.8857 2.0429 1.1756  0.4644  0.6228  661  ASP A OD1 
5052  O OD2 . ASP A 661  ? 1.6021 2.8429 2.0906 1.1583  0.4748  0.5678  661  ASP A OD2 
5053  N N   . SER A 662  ? 2.7845 3.9809 3.1666 1.1157  0.3752  0.5616  662  SER A N   
5054  C CA  . SER A 662  ? 2.7375 3.9095 3.1555 1.0937  0.3690  0.5213  662  SER A CA  
5055  C C   . SER A 662  ? 2.8478 3.9331 3.2574 1.1148  0.4290  0.4953  662  SER A C   
5056  O O   . SER A 662  ? 2.8768 3.9011 3.2377 1.1089  0.4187  0.4810  662  SER A O   
5057  C CB  . SER A 662  ? 2.7855 3.9589 3.1558 1.0622  0.2982  0.5214  662  SER A CB  
5058  O OG  . SER A 662  ? 2.9392 4.0745 3.2166 1.0714  0.2821  0.5461  662  SER A OG  
5059  N N   . GLN A 663  ? 1.7372 2.8195 2.1966 1.1386  0.4918  0.4886  663  GLN A N   
5060  C CA  . GLN A 663  ? 1.8893 2.8944 2.3393 1.1653  0.5590  0.4708  663  GLN A CA  
5061  C C   . GLN A 663  ? 2.0944 3.0159 2.4967 1.1618  0.5622  0.4459  663  GLN A C   
5062  O O   . GLN A 663  ? 2.0140 2.9213 2.4476 1.1423  0.5514  0.4123  663  GLN A O   
5063  C CB  . GLN A 663  ? 1.7054 2.7256 2.2446 1.1754  0.6153  0.4477  663  GLN A CB  
5064  C CG  . GLN A 663  ? 1.5352 2.6438 2.1322 1.1722  0.6057  0.4668  663  GLN A CG  
5065  C CD  . GLN A 663  ? 1.5671 2.7041 2.1199 1.1922  0.6018  0.5125  663  GLN A CD  
5066  O OE1 . GLN A 663  ? 1.6859 2.7737 2.1650 1.2110  0.6114  0.5303  663  GLN A OE1 
5067  N NE2 . GLN A 663  ? 1.4711 2.6871 2.0697 1.1880  0.5881  0.5306  663  GLN A NE2 
5068  N N   . GLU A 664  ? 3.6837 4.5505 4.0081 1.1823  0.5781  0.4645  664  GLU A N   
5069  C CA  . GLU A 664  ? 3.9334 4.7106 4.2034 1.1882  0.5974  0.4457  664  GLU A CA  
5070  C C   . GLU A 664  ? 4.0209 4.7803 4.2458 1.1607  0.5381  0.4378  664  GLU A C   
5071  O O   . GLU A 664  ? 4.0000 4.7333 4.1432 1.1609  0.5104  0.4598  664  GLU A O   
5072  C CB  . GLU A 664  ? 3.9728 4.7071 4.3004 1.1974  0.6590  0.4045  664  GLU A CB  
5073  C CG  . GLU A 664  ? 3.9169 4.6685 4.2938 1.2234  0.7202  0.4095  664  GLU A CG  
5074  C CD  . GLU A 664  ? 4.0324 4.7113 4.4214 1.2443  0.7933  0.3798  664  GLU A CD  
5075  O OE1 . GLU A 664  ? 4.1380 4.7476 4.4863 1.2424  0.7993  0.3596  664  GLU A OE1 
5076  O OE2 . GLU A 664  ? 4.0206 4.7118 4.4598 1.2625  0.8457  0.3766  664  GLU A OE2 
5077  N N   . ASN A 665  ? 2.1272 2.9030 2.4078 1.1368  0.5188  0.4063  665  ASN A N   
5078  C CA  . ASN A 665  ? 2.2159 2.9551 2.4658 1.1141  0.4805  0.3857  665  ASN A CA  
5079  C C   . ASN A 665  ? 2.1594 2.9701 2.4416 1.0817  0.4152  0.3877  665  ASN A C   
5080  O O   . ASN A 665  ? 2.1778 3.0437 2.4369 1.0740  0.3729  0.4211  665  ASN A O   
5081  C CB  . ASN A 665  ? 2.1983 2.8808 2.4909 1.1187  0.5286  0.3399  665  ASN A CB  
5082  C CG  . ASN A 665  ? 2.1919 2.8281 2.4564 1.0982  0.4971  0.3141  665  ASN A CG  
5083  O OD1 . ASN A 665  ? 2.0693 2.7177 2.3902 1.0793  0.4839  0.2828  665  ASN A OD1 
5084  N ND2 . ASN A 665  ? 2.3287 2.9095 2.5074 1.1022  0.4867  0.3258  665  ASN A ND2 
5085  N N   . ASP A 666  ? 3.9403 4.7500 4.2773 1.0630  0.4083  0.3511  666  ASP A N   
5086  C CA  . ASP A 666  ? 3.8387 4.7180 4.2262 1.0335  0.3576  0.3467  666  ASP A CA  
5087  C C   . ASP A 666  ? 3.6722 4.5403 4.1262 1.0182  0.3634  0.3019  666  ASP A C   
5088  O O   . ASP A 666  ? 3.6578 4.5058 4.0943 0.9963  0.3231  0.2847  666  ASP A O   
5089  C CB  . ASP A 666  ? 3.9844 4.8893 4.3106 1.0092  0.2825  0.3710  666  ASP A CB  
5090  C CG  . ASP A 666  ? 4.1648 5.0066 4.4352 0.9959  0.2560  0.3538  666  ASP A CG  
5091  O OD1 . ASP A 666  ? 4.2663 5.0367 4.5256 1.0112  0.2992  0.3311  666  ASP A OD1 
5092  O OD2 . ASP A 666  ? 4.1949 5.0583 4.4320 0.9695  0.1921  0.3627  666  ASP A OD2 
5093  N N   . GLU A 667  ? 4.3835 5.2618 4.9123 1.0313  0.4159  0.2829  667  GLU A N   
5094  C CA  . GLU A 667  ? 4.1783 5.0800 4.7906 1.0145  0.4157  0.2477  667  GLU A CA  
5095  C C   . GLU A 667  ? 4.1580 5.0311 4.7647 0.9896  0.3755  0.2184  667  GLU A C   
5096  O O   . GLU A 667  ? 4.1213 5.0335 4.7201 0.9623  0.3124  0.2260  667  GLU A O   
5097  C CB  . GLU A 667  ? 3.9698 4.9622 4.6340 0.9994  0.3865  0.2646  667  GLU A CB  
5098  C CG  . GLU A 667  ? 3.9395 4.9734 4.5572 1.0059  0.3657  0.3113  667  GLU A CG  
5099  C CD  . GLU A 667  ? 3.9252 4.9420 4.5349 1.0414  0.4283  0.3284  667  GLU A CD  
5100  O OE1 . GLU A 667  ? 3.9309 4.8880 4.5481 1.0616  0.4854  0.3063  667  GLU A OE1 
5101  O OE2 . GLU A 667  ? 3.9178 4.9805 4.5134 1.0492  0.4206  0.3638  667  GLU A OE2 
5102  N N   . PRO A 668  ? 3.7700 4.5754 4.3827 0.9987  0.4125  0.1839  668  PRO A N   
5103  C CA  . PRO A 668  ? 3.7374 4.5130 4.3585 0.9779  0.3837  0.1498  668  PRO A CA  
5104  C C   . PRO A 668  ? 3.5744 4.4034 4.2806 0.9560  0.3631  0.1268  668  PRO A C   
5105  O O   . PRO A 668  ? 3.5317 4.3316 4.2756 0.9497  0.3715  0.0886  668  PRO A O   
5106  C CB  . PRO A 668  ? 3.7930 4.4903 4.4139 0.9994  0.4445  0.1193  668  PRO A CB  
5107  C CG  . PRO A 668  ? 3.9087 4.5804 4.4802 1.0278  0.4866  0.1464  668  PRO A CG  
5108  C CD  . PRO A 668  ? 3.8534 4.5996 4.4500 1.0306  0.4821  0.1788  668  PRO A CD  
5109  N N   . CYS A 669  ? 3.4064 4.3118 4.1410 0.9445  0.3360  0.1499  669  CYS A N   
5110  C CA  . CYS A 669  ? 3.2650 4.2284 4.0778 0.9224  0.3139  0.1332  669  CYS A CA  
5111  C C   . CYS A 669  ? 3.2320 4.1679 4.0651 0.9020  0.2871  0.0954  669  CYS A C   
5112  O O   . CYS A 669  ? 3.3073 4.2024 4.0806 0.8922  0.2517  0.0933  669  CYS A O   
5113  C CB  . CYS A 669  ? 3.2273 4.2648 4.0296 0.9023  0.2577  0.1671  669  CYS A CB  
5114  S SG  . CYS A 669  ? 3.7012 4.8071 4.5802 0.8676  0.2118  0.1498  669  CYS A SG  
5115  N N   . LYS A 670  ? 2.8818 3.8403 3.7990 0.8955  0.3035  0.0657  670  LYS A N   
5116  C CA  . LYS A 670  ? 2.8282 3.7589 3.7720 0.8791  0.2845  0.0269  670  LYS A CA  
5117  C C   . LYS A 670  ? 2.6424 3.6263 3.6776 0.8626  0.2790  0.0053  670  LYS A C   
5118  O O   . LYS A 670  ? 2.5825 3.5593 3.6819 0.8753  0.3306  -0.0213 670  LYS A O   
5119  C CB  . LYS A 670  ? 2.9157 3.7681 3.8545 0.9011  0.3380  -0.0034 670  LYS A CB  
5120  C CG  . LYS A 670  ? 2.8948 3.7145 3.8646 0.8877  0.3248  -0.0463 670  LYS A CG  
5121  C CD  . LYS A 670  ? 2.9607 3.7595 3.8675 0.8658  0.2578  -0.0424 670  LYS A CD  
5122  C CE  . LYS A 670  ? 2.9293 3.6992 3.8696 0.8519  0.2411  -0.0846 670  LYS A CE  
5123  N NZ  . LYS A 670  ? 2.9951 3.6934 3.9385 0.8730  0.2942  -0.1167 670  LYS A NZ  
5124  N N   . GLU A 671  ? 3.0564 4.0934 4.0955 0.8339  0.2166  0.0172  671  GLU A N   
5125  C CA  . GLU A 671  ? 2.8864 3.9695 4.0028 0.8119  0.1969  -0.0047 671  GLU A CA  
5126  C C   . GLU A 671  ? 2.5161 3.6604 3.7124 0.8164  0.2325  -0.0026 671  GLU A C   
5127  O O   . GLU A 671  ? 2.4772 3.6269 3.7463 0.8144  0.2563  -0.0343 671  GLU A O   
5128  C CB  . GLU A 671  ? 2.8735 3.9079 4.0189 0.8079  0.2016  -0.0498 671  GLU A CB  
5129  C CG  . GLU A 671  ? 2.9320 3.9198 4.0112 0.7936  0.1505  -0.0552 671  GLU A CG  
5130  C CD  . GLU A 671  ? 2.8937 3.8364 4.0065 0.7903  0.1554  -0.1004 671  GLU A CD  
5131  O OE1 . GLU A 671  ? 2.7946 3.7538 3.9871 0.7925  0.1860  -0.1273 671  GLU A OE1 
5132  O OE2 . GLU A 671  ? 2.9621 3.8530 4.0217 0.7855  0.1286  -0.1092 671  GLU A OE2 
5133  N N   . ILE A 672  ? 2.3249 3.5156 3.5081 0.8217  0.2347  0.0340  672  ILE A N   
5134  C CA  . ILE A 672  ? 2.1373 3.3899 3.3908 0.8248  0.2643  0.0403  672  ILE A CA  
5135  C C   . ILE A 672  ? 1.9592 3.2860 3.2292 0.7942  0.2055  0.0577  672  ILE A C   
5136  O O   . ILE A 672  ? 1.8617 3.2467 3.1875 0.7917  0.2199  0.0653  672  ILE A O   
5137  C CB  . ILE A 672  ? 2.4293 3.6846 3.6620 0.8550  0.3146  0.0697  672  ILE A CB  
5138  C CG1 . ILE A 672  ? 2.3433 3.6444 3.6553 0.8647  0.3634  0.0669  672  ILE A CG1 
5139  C CG2 . ILE A 672  ? 2.4693 3.7569 3.6381 0.8493  0.2721  0.1133  672  ILE A CG2 
5140  C CD1 . ILE A 672  ? 2.3979 3.7074 3.6888 0.8926  0.4068  0.0985  672  ILE A CD1 
5141  N N   . LEU A 673  ? 1.1026 2.4257 2.3236 0.7702  0.1398  0.0631  673  LEU A N   
5142  C CA  . LEU A 673  ? 0.9551 2.3409 2.1584 0.7453  0.0818  0.0919  673  LEU A CA  
5143  C C   . LEU A 673  ? 0.8055 2.2512 2.0777 0.7178  0.0550  0.0800  673  LEU A C   
5144  O O   . LEU A 673  ? 0.7618 2.2597 2.0203 0.6948  0.0053  0.1020  673  LEU A O   
5145  C CB  . LEU A 673  ? 0.9499 2.3107 2.0690 0.7294  0.0211  0.1050  673  LEU A CB  
5146  C CG  . LEU A 673  ? 0.8161 2.1742 1.9337 0.6967  -0.0396 0.0854  673  LEU A CG  
5147  C CD1 . LEU A 673  ? 0.8515 2.2175 1.8885 0.6790  -0.1012 0.1143  673  LEU A CD1 
5148  C CD2 . LEU A 673  ? 0.8119 2.1002 1.9349 0.7019  -0.0257 0.0467  673  LEU A CD2 
5149  N N   . LEU A 679  ? 4.3214 4.3386 4.1139 -0.5023 0.7825  -0.3242 679  LEU A N   
5150  C CA  . LEU A 679  ? 4.3238 4.3314 4.0786 -0.5108 0.7554  -0.3906 679  LEU A CA  
5151  C C   . LEU A 679  ? 4.3275 4.3617 4.1242 -0.5013 0.7002  -0.3924 679  LEU A C   
5152  O O   . LEU A 679  ? 4.3433 4.3701 4.0951 -0.5018 0.6865  -0.4395 679  LEU A O   
5153  C CB  . LEU A 679  ? 4.2997 4.3109 4.0808 -0.5324 0.7260  -0.4358 679  LEU A CB  
5154  C CG  . LEU A 679  ? 4.2923 4.2773 4.0152 -0.5436 0.7824  -0.4478 679  LEU A CG  
5155  C CD1 . LEU A 679  ? 4.2424 4.2412 4.0202 -0.5608 0.7489  -0.4695 679  LEU A CD1 
5156  C CD2 . LEU A 679  ? 4.3141 4.2665 3.9226 -0.5474 0.8255  -0.4970 679  LEU A CD2 
5157  N N   . GLN A 680  ? 3.6922 3.7609 3.5745 -0.4940 0.6687  -0.3412 680  GLN A N   
5158  C CA  . GLN A 680  ? 3.6975 3.7943 3.6154 -0.4825 0.6257  -0.3316 680  GLN A CA  
5159  C C   . GLN A 680  ? 3.6837 3.7743 3.5500 -0.4569 0.6716  -0.2918 680  GLN A C   
5160  O O   . GLN A 680  ? 3.6863 3.8006 3.5711 -0.4435 0.6452  -0.2792 680  GLN A O   
5161  C CB  . GLN A 680  ? 3.7163 3.8564 3.7512 -0.4900 0.5650  -0.2987 680  GLN A CB  
5162  C CG  . GLN A 680  ? 3.7398 3.9149 3.8191 -0.4734 0.5692  -0.2302 680  GLN A CG  
5163  C CD  . GLN A 680  ? 3.7516 3.9243 3.8261 -0.4669 0.6239  -0.1783 680  GLN A CD  
5164  O OE1 . GLN A 680  ? 3.7571 3.9048 3.8091 -0.4785 0.6526  -0.1901 680  GLN A OE1 
5165  N NE2 . GLN A 680  ? 3.7567 3.9592 3.8526 -0.4473 0.6385  -0.1209 680  GLN A NE2 
5166  N N   . LYS A 681  ? 4.5968 4.6547 4.3977 -0.4495 0.7397  -0.2724 681  LYS A N   
5167  C CA  . LYS A 681  ? 4.5728 4.6113 4.3073 -0.4232 0.7912  -0.2388 681  LYS A CA  
5168  C C   . LYS A 681  ? 4.6029 4.5997 4.2319 -0.4207 0.8145  -0.2850 681  LYS A C   
5169  O O   . LYS A 681  ? 4.6266 4.6144 4.2112 -0.3989 0.8308  -0.2682 681  LYS A O   
5170  C CB  . LYS A 681  ? 4.5361 4.5498 4.2362 -0.4164 0.8561  -0.2022 681  LYS A CB  
5171  C CG  . LYS A 681  ? 4.4655 4.5139 4.2544 -0.4245 0.8449  -0.1622 681  LYS A CG  
5172  C CD  . LYS A 681  ? 4.4442 4.4640 4.1838 -0.4173 0.9141  -0.1339 681  LYS A CD  
5173  C CE  . LYS A 681  ? 4.3997 4.4438 4.2095 -0.4353 0.9060  -0.1155 681  LYS A CE  
5174  N NZ  . LYS A 681  ? 4.4155 4.4279 4.1682 -0.4322 0.9744  -0.0995 681  LYS A NZ  
5175  N N   . LYS A 682  ? 4.4522 4.4251 4.0389 -0.4433 0.8176  -0.3424 682  LYS A N   
5176  C CA  . LYS A 682  ? 4.4844 4.4221 3.9708 -0.4475 0.8378  -0.3919 682  LYS A CA  
5177  C C   . LYS A 682  ? 4.5292 4.4923 4.0313 -0.4396 0.7894  -0.4091 682  LYS A C   
5178  O O   . LYS A 682  ? 4.5414 4.4796 3.9614 -0.4343 0.8088  -0.4304 682  LYS A O   
5179  C CB  . LYS A 682  ? 4.4501 4.3748 3.9079 -0.4752 0.8384  -0.4524 682  LYS A CB  
5180  C CG  . LYS A 682  ? 4.4439 4.3602 3.8377 -0.4855 0.8258  -0.5154 682  LYS A CG  
5181  C CD  . LYS A 682  ? 4.4663 4.3353 3.7424 -0.4780 0.8834  -0.5146 682  LYS A CD  
5182  C CE  . LYS A 682  ? 4.4655 4.3357 3.6869 -0.4869 0.8640  -0.5708 682  LYS A CE  
5183  N NZ  . LYS A 682  ? 4.5023 4.3235 3.6069 -0.4810 0.9171  -0.5674 682  LYS A NZ  
5184  N N   . ILE A 683  ? 5.3798 5.3919 4.9863 -0.4404 0.7263  -0.3993 683  ILE A N   
5185  C CA  . ILE A 683  ? 5.4386 5.4813 5.0726 -0.4337 0.6748  -0.4134 683  ILE A CA  
5186  C C   . ILE A 683  ? 5.4970 5.5582 5.1471 -0.4060 0.6801  -0.3548 683  ILE A C   
5187  O O   . ILE A 683  ? 5.5429 5.6071 5.1579 -0.3935 0.6723  -0.3629 683  ILE A O   
5188  C CB  . ILE A 683  ? 4.9305 5.0147 4.6665 -0.4495 0.5998  -0.4358 683  ILE A CB  
5189  C CG1 . ILE A 683  ? 4.8923 4.9621 4.6330 -0.4722 0.5986  -0.4738 683  ILE A CG1 
5190  C CG2 . ILE A 683  ? 4.9532 5.0581 4.6901 -0.4496 0.5509  -0.4778 683  ILE A CG2 
5191  C CD1 . ILE A 683  ? 4.8467 4.9486 4.6897 -0.4857 0.5288  -0.4858 683  ILE A CD1 
5192  N N   . GLU A 684  ? 4.5153 4.5921 4.2170 -0.3959 0.6938  -0.2962 684  GLU A N   
5193  C CA  . GLU A 684  ? 4.5412 4.6468 4.2699 -0.3682 0.6958  -0.2373 684  GLU A CA  
5194  C C   . GLU A 684  ? 4.5383 4.6035 4.1645 -0.3412 0.7555  -0.2188 684  GLU A C   
5195  O O   . GLU A 684  ? 4.5376 4.6251 4.1738 -0.3139 0.7571  -0.1755 684  GLU A O   
5196  C CB  . GLU A 684  ? 4.5810 4.7214 4.3952 -0.3661 0.6931  -0.1807 684  GLU A CB  
5197  C CG  . GLU A 684  ? 4.6111 4.7993 4.5385 -0.3885 0.6236  -0.1848 684  GLU A CG  
5198  C CD  . GLU A 684  ? 4.6396 4.8764 4.6545 -0.3831 0.6135  -0.1199 684  GLU A CD  
5199  O OE1 . GLU A 684  ? 4.6616 4.8970 4.6506 -0.3606 0.6627  -0.0732 684  GLU A OE1 
5200  O OE2 . GLU A 684  ? 4.6383 4.9148 4.7461 -0.4016 0.5560  -0.1156 684  GLU A OE2 
5201  N N   . GLU A 685  ? 3.8769 3.8824 3.4033 -0.3490 0.8036  -0.2513 685  GLU A N   
5202  C CA  . GLU A 685  ? 3.9000 3.8542 3.3152 -0.3282 0.8587  -0.2427 685  GLU A CA  
5203  C C   . GLU A 685  ? 3.8705 3.8316 3.2543 -0.3217 0.8309  -0.2680 685  GLU A C   
5204  O O   . GLU A 685  ? 3.9045 3.8527 3.2406 -0.2943 0.8511  -0.2404 685  GLU A O   
5205  C CB  . GLU A 685  ? 3.9439 3.8335 3.2617 -0.3463 0.9122  -0.2773 685  GLU A CB  
5206  C CG  . GLU A 685  ? 3.9470 3.8335 3.2444 -0.3780 0.8863  -0.3486 685  GLU A CG  
5207  C CD  . GLU A 685  ? 3.9781 3.8133 3.1938 -0.4001 0.9358  -0.3819 685  GLU A CD  
5208  O OE1 . GLU A 685  ? 3.9958 3.7979 3.1801 -0.3933 0.9874  -0.3498 685  GLU A OE1 
5209  O OE2 . GLU A 685  ? 3.9842 3.8155 3.1671 -0.4244 0.9226  -0.4413 685  GLU A OE2 
5210  N N   . ILE A 686  ? 3.4057 3.3882 2.8165 -0.3463 0.7836  -0.3216 686  ILE A N   
5211  C CA  . ILE A 686  ? 3.3779 3.3711 2.7611 -0.3449 0.7537  -0.3541 686  ILE A CA  
5212  C C   . ILE A 686  ? 3.3179 3.3688 2.7801 -0.3240 0.7082  -0.3171 686  ILE A C   
5213  O O   . ILE A 686  ? 3.3312 3.4110 2.8073 -0.3259 0.6647  -0.3437 686  ILE A O   
5214  C CB  . ILE A 686  ? 3.3623 3.3663 2.7552 -0.3760 0.7152  -0.4239 686  ILE A CB  
5215  C CG1 . ILE A 686  ? 3.3603 3.3210 2.6984 -0.3980 0.7566  -0.4538 686  ILE A CG1 
5216  C CG2 . ILE A 686  ? 3.3954 3.3981 2.7287 -0.3766 0.7008  -0.4639 686  ILE A CG2 
5217  C CD1 . ILE A 686  ? 3.4041 3.3007 2.6119 -0.3952 0.8245  -0.4576 686  ILE A CD1 
5218  N N   . ALA A 687  ? 3.8311 3.9029 3.3457 -0.3047 0.7184  -0.2563 687  ALA A N   
5219  C CA  . ALA A 687  ? 3.7511 3.8731 3.3176 -0.2787 0.6922  -0.2118 687  ALA A CA  
5220  C C   . ALA A 687  ? 3.7347 3.8179 3.1975 -0.2516 0.7329  -0.2021 687  ALA A C   
5221  O O   . ALA A 687  ? 3.7239 3.8378 3.1997 -0.2238 0.7226  -0.1669 687  ALA A O   
5222  C CB  . ALA A 687  ? 3.7202 3.8728 3.3555 -0.2646 0.7016  -0.1500 687  ALA A CB  
5223  N N   . ALA A 688  ? 3.8786 3.8932 3.2364 -0.2613 0.7796  -0.2337 688  ALA A N   
5224  C CA  . ALA A 688  ? 3.8885 3.8494 3.1285 -0.2444 0.8205  -0.2367 688  ALA A CA  
5225  C C   . ALA A 688  ? 3.8693 3.8545 3.0969 -0.2450 0.7802  -0.2674 688  ALA A C   
5226  O O   . ALA A 688  ? 3.8929 3.8472 3.0379 -0.2253 0.8041  -0.2590 688  ALA A O   
5227  C CB  . ALA A 688  ? 3.9160 3.8025 3.0541 -0.2652 0.8730  -0.2711 688  ALA A CB  
5228  N N   . LYS A 689  ? 3.4062 3.4439 2.7124 -0.2676 0.7191  -0.3038 689  LYS A N   
5229  C CA  . LYS A 689  ? 3.4275 3.4984 2.7355 -0.2685 0.6748  -0.3330 689  LYS A CA  
5230  C C   . LYS A 689  ? 3.4921 3.6311 2.8877 -0.2458 0.6310  -0.2919 689  LYS A C   
5231  O O   . LYS A 689  ? 3.5055 3.6893 2.9377 -0.2514 0.5794  -0.3169 689  LYS A O   
5232  C CB  . LYS A 689  ? 3.3196 3.4072 2.6514 -0.3040 0.6324  -0.4022 689  LYS A CB  
5233  C CG  . LYS A 689  ? 3.1987 3.3148 2.6295 -0.3241 0.5999  -0.4097 689  LYS A CG  
5234  C CD  . LYS A 689  ? 3.1312 3.2500 2.5619 -0.3554 0.5691  -0.4817 689  LYS A CD  
5235  C CE  . LYS A 689  ? 3.1191 3.1808 2.4299 -0.3677 0.6196  -0.5199 689  LYS A CE  
5236  N NZ  . LYS A 689  ? 3.0802 3.1533 2.3891 -0.3960 0.5889  -0.5922 689  LYS A NZ  
5237  N N   . TYR A 690  ? 4.3766 4.5272 3.8056 -0.2207 0.6514  -0.2300 690  TYR A N   
5238  C CA  . TYR A 690  ? 4.4670 4.6858 3.9721 -0.1974 0.6158  -0.1865 690  TYR A CA  
5239  C C   . TYR A 690  ? 4.5412 4.7614 3.9855 -0.1737 0.6152  -0.1850 690  TYR A C   
5240  O O   . TYR A 690  ? 4.5793 4.7389 3.9154 -0.1576 0.6648  -0.1818 690  TYR A O   
5241  C CB  . TYR A 690  ? 4.5417 4.7736 4.0816 -0.1716 0.6448  -0.1195 690  TYR A CB  
5242  C CG  . TYR A 690  ? 4.6466 4.9361 4.2214 -0.1370 0.6278  -0.0712 690  TYR A CG  
5243  C CD1 . TYR A 690  ? 4.6523 5.0237 4.3317 -0.1450 0.5637  -0.0666 690  TYR A CD1 
5244  C CD2 . TYR A 690  ? 4.7302 4.9914 4.2304 -0.0960 0.6752  -0.0313 690  TYR A CD2 
5245  C CE1 . TYR A 690  ? 4.6987 5.1290 4.4099 -0.1144 0.5480  -0.0235 690  TYR A CE1 
5246  C CE2 . TYR A 690  ? 4.7770 5.0952 4.3080 -0.0618 0.6594  0.0122  690  TYR A CE2 
5247  C CZ  . TYR A 690  ? 4.7595 5.1655 4.3972 -0.0718 0.5960  0.0159  690  TYR A CZ  
5248  O OH  . TYR A 690  ? 4.7935 5.2625 4.4624 -0.0387 0.5803  0.0588  690  TYR A OH  
5249  N N   . LYS A 691  ? 3.9232 4.2120 3.4371 -0.1727 0.5580  -0.1869 691  LYS A N   
5250  C CA  . LYS A 691  ? 3.9805 4.2835 3.4505 -0.1522 0.5479  -0.1872 691  LYS A CA  
5251  C C   . LYS A 691  ? 3.9793 4.3729 3.5620 -0.1528 0.4825  -0.1752 691  LYS A C   
5252  O O   . LYS A 691  ? 4.0057 4.4369 3.5866 -0.1378 0.4576  -0.1723 691  LYS A O   
5253  C CB  . LYS A 691  ? 4.0006 4.2651 3.3919 -0.1742 0.5461  -0.2514 691  LYS A CB  
5254  C CG  . LYS A 691  ? 3.9364 4.2123 3.3765 -0.2157 0.5069  -0.3108 691  LYS A CG  
5255  C CD  . LYS A 691  ? 3.9376 4.1657 3.2827 -0.2367 0.5223  -0.3722 691  LYS A CD  
5256  C CE  . LYS A 691  ? 3.8805 4.1154 3.2694 -0.2738 0.4910  -0.4289 691  LYS A CE  
5257  N NZ  . LYS A 691  ? 3.8938 4.0835 3.1869 -0.2949 0.5139  -0.4868 691  LYS A NZ  
5258  N N   . HIS A 692  ? 3.2916 3.7189 2.9718 -0.1722 0.4552  -0.1677 692  HIS A N   
5259  C CA  . HIS A 692  ? 3.2652 3.7757 3.0601 -0.1787 0.3937  -0.1526 692  HIS A CA  
5260  C C   . HIS A 692  ? 3.1534 3.6730 3.0307 -0.2058 0.3768  -0.1503 692  HIS A C   
5261  O O   . HIS A 692  ? 3.1117 3.5787 2.9608 -0.2265 0.3960  -0.1818 692  HIS A O   
5262  C CB  . HIS A 692  ? 3.3355 3.8764 3.1469 -0.1966 0.3373  -0.2039 692  HIS A CB  
5263  C CG  . HIS A 692  ? 3.3954 4.0201 3.3192 -0.2045 0.2726  -0.1898 692  HIS A CG  
5264  N ND1 . HIS A 692  ? 3.4474 4.1321 3.4068 -0.1774 0.2664  -0.1360 692  HIS A ND1 
5265  C CD2 . HIS A 692  ? 3.4099 4.0676 3.4155 -0.2368 0.2108  -0.2236 692  HIS A CD2 
5266  C CE1 . HIS A 692  ? 3.4570 4.2104 3.5163 -0.1957 0.2040  -0.1366 692  HIS A CE1 
5267  N NE2 . HIS A 692  ? 3.4355 4.1703 3.5235 -0.2318 0.1690  -0.1892 692  HIS A NE2 
5268  N N   . SER A 693  ? 3.5897 4.1780 3.5677 -0.2067 0.3404  -0.1123 693  SER A N   
5269  C CA  . SER A 693  ? 3.4928 4.0951 3.5553 -0.2340 0.3187  -0.1054 693  SER A CA  
5270  C C   . SER A 693  ? 3.3933 3.9742 3.4758 -0.2718 0.2770  -0.1706 693  SER A C   
5271  O O   . SER A 693  ? 3.3658 3.9025 3.4401 -0.2902 0.2931  -0.1902 693  SER A O   
5272  C CB  . SER A 693  ? 3.4931 4.1807 3.6608 -0.2335 0.2764  -0.0593 693  SER A CB  
5273  O OG  . SER A 693  ? 3.4574 4.1585 3.7097 -0.2662 0.2450  -0.0585 693  SER A OG  
5274  N N   . VAL A 694  ? 4.7389 5.3528 4.8459 -0.2814 0.2234  -0.2048 694  VAL A N   
5275  C CA  . VAL A 694  ? 4.6691 5.2743 4.8086 -0.3148 0.1729  -0.2658 694  VAL A CA  
5276  C C   . VAL A 694  ? 4.6139 5.1483 4.6749 -0.3251 0.2053  -0.3171 694  VAL A C   
5277  O O   . VAL A 694  ? 4.5946 5.1123 4.6859 -0.3514 0.1778  -0.3566 694  VAL A O   
5278  C CB  . VAL A 694  ? 4.6147 5.2624 4.7737 -0.3185 0.1169  -0.2991 694  VAL A CB  
5279  C CG1 . VAL A 694  ? 4.6037 5.2444 4.8051 -0.3513 0.0606  -0.3599 694  VAL A CG1 
5280  C CG2 . VAL A 694  ? 4.6254 5.3482 4.8585 -0.3088 0.0858  -0.2486 694  VAL A CG2 
5281  N N   . VAL A 695  ? 2.9546 3.4474 2.9133 -0.3049 0.2630  -0.3170 695  VAL A N   
5282  C CA  . VAL A 695  ? 2.9139 3.3428 2.7936 -0.3168 0.2973  -0.3637 695  VAL A CA  
5283  C C   . VAL A 695  ? 2.8556 3.2548 2.7545 -0.3268 0.3261  -0.3442 695  VAL A C   
5284  O O   . VAL A 695  ? 2.8288 3.1961 2.7168 -0.3486 0.3249  -0.3874 695  VAL A O   
5285  C CB  . VAL A 695  ? 2.9540 3.3402 2.7135 -0.2962 0.3537  -0.3666 695  VAL A CB  
5286  C CG1 . VAL A 695  ? 2.9437 3.2659 2.6246 -0.3125 0.3929  -0.4100 695  VAL A CG1 
5287  C CG2 . VAL A 695  ? 2.9835 3.3979 2.7193 -0.2899 0.3230  -0.3937 695  VAL A CG2 
5288  N N   . LYS A 696  ? 4.4160 4.8303 4.3444 -0.3099 0.3509  -0.2794 696  LYS A N   
5289  C CA  . LYS A 696  ? 4.3716 4.7704 4.3346 -0.3200 0.3715  -0.2545 696  LYS A CA  
5290  C C   . LYS A 696  ? 4.3426 4.7649 4.3987 -0.3514 0.3102  -0.2791 696  LYS A C   
5291  O O   . LYS A 696  ? 4.3224 4.7134 4.3834 -0.3699 0.3182  -0.2970 696  LYS A O   
5292  C CB  . LYS A 696  ? 4.3727 4.8008 4.3661 -0.2961 0.3979  -0.1797 696  LYS A CB  
5293  C CG  . LYS A 696  ? 4.3492 4.7898 4.4164 -0.3108 0.3963  -0.1473 696  LYS A CG  
5294  C CD  . LYS A 696  ? 4.2800 4.6591 4.2889 -0.3145 0.4539  -0.1525 696  LYS A CD  
5295  C CE  . LYS A 696  ? 4.2379 4.6368 4.3216 -0.3260 0.4541  -0.1125 696  LYS A CE  
5296  N NZ  . LYS A 696  ? 4.2066 4.5505 4.2359 -0.3284 0.5118  -0.1135 696  LYS A NZ  
5297  N N   . LYS A 697  ? 2.3923 2.8675 2.5189 -0.3574 0.2486  -0.2808 697  LYS A N   
5298  C CA  . LYS A 697  ? 2.3668 2.8585 2.5760 -0.3874 0.1836  -0.3100 697  LYS A CA  
5299  C C   . LYS A 697  ? 2.3550 2.8109 2.5227 -0.4028 0.1651  -0.3875 697  LYS A C   
5300  O O   . LYS A 697  ? 2.3547 2.7998 2.5660 -0.4257 0.1294  -0.4181 697  LYS A O   
5301  C CB  . LYS A 697  ? 2.3814 2.9381 2.6727 -0.3908 0.1226  -0.2918 697  LYS A CB  
5302  C CG  . LYS A 697  ? 2.3794 2.9487 2.7574 -0.4227 0.0526  -0.3177 697  LYS A CG  
5303  C CD  . LYS A 697  ? 2.3503 2.9222 2.7935 -0.4378 0.0536  -0.2740 697  LYS A CD  
5304  C CE  . LYS A 697  ? 2.3027 2.8789 2.8283 -0.4702 -0.0161 -0.2965 697  LYS A CE  
5305  N NZ  . LYS A 697  ? 2.2696 2.8566 2.8637 -0.4864 -0.0181 -0.2452 697  LYS A NZ  
5306  N N   . CYS A 698  ? 2.8028 3.2419 2.8853 -0.3898 0.1887  -0.4188 698  CYS A N   
5307  C CA  . CYS A 698  ? 2.7946 3.2066 2.8294 -0.4028 0.1757  -0.4931 698  CYS A CA  
5308  C C   . CYS A 698  ? 2.7556 3.1166 2.7486 -0.4135 0.2155  -0.5130 698  CYS A C   
5309  O O   . CYS A 698  ? 2.7248 3.0705 2.7180 -0.4309 0.1917  -0.5684 698  CYS A O   
5310  C CB  . CYS A 698  ? 2.8124 3.2214 2.7607 -0.3873 0.1964  -0.5159 698  CYS A CB  
5311  S SG  . CYS A 698  ? 3.2481 3.7157 3.2360 -0.3853 0.1276  -0.5402 698  CYS A SG  
5312  N N   . CYS A 699  ? 3.2325 3.5693 3.1893 -0.4017 0.2765  -0.4668 699  CYS A N   
5313  C CA  . CYS A 699  ? 3.2641 3.5535 3.1758 -0.4106 0.3218  -0.4788 699  CYS A CA  
5314  C C   . CYS A 699  ? 3.2844 3.5789 3.2778 -0.4246 0.3054  -0.4536 699  CYS A C   
5315  O O   . CYS A 699  ? 3.2715 3.5441 3.2687 -0.4423 0.2975  -0.4903 699  CYS A O   
5316  C CB  . CYS A 699  ? 3.2949 3.5505 3.1210 -0.3910 0.3973  -0.4431 699  CYS A CB  
5317  S SG  . CYS A 699  ? 3.2910 3.4830 3.0092 -0.4023 0.4562  -0.4870 699  CYS A SG  
5318  N N   . TYR A 700  ? 2.4272 2.7534 2.4846 -0.4166 0.3000  -0.3906 700  TYR A N   
5319  C CA  . TYR A 700  ? 2.5016 2.8349 2.6332 -0.4298 0.2906  -0.3566 700  TYR A CA  
5320  C C   . TYR A 700  ? 2.5458 2.8791 2.7359 -0.4556 0.2291  -0.4017 700  TYR A C   
5321  O O   . TYR A 700  ? 2.5444 2.8425 2.7047 -0.4671 0.2390  -0.4423 700  TYR A O   
5322  C CB  . TYR A 700  ? 2.5789 2.9614 2.7797 -0.4196 0.2809  -0.2864 700  TYR A CB  
5323  C CG  . TYR A 700  ? 2.6569 3.0386 2.8844 -0.4193 0.3173  -0.2313 700  TYR A CG  
5324  C CD1 . TYR A 700  ? 2.6950 3.1081 3.0191 -0.4380 0.2784  -0.2010 700  TYR A CD1 
5325  C CD2 . TYR A 700  ? 2.6957 3.0443 2.8489 -0.4014 0.3906  -0.2097 700  TYR A CD2 
5326  C CE1 . TYR A 700  ? 2.7139 3.1307 3.0621 -0.4386 0.3118  -0.1509 700  TYR A CE1 
5327  C CE2 . TYR A 700  ? 2.7175 3.0679 2.8944 -0.4004 0.4242  -0.1610 700  TYR A CE2 
5328  C CZ  . TYR A 700  ? 2.7234 3.1108 2.9988 -0.4189 0.3847  -0.1316 700  TYR A CZ  
5329  O OH  . TYR A 700  ? 2.7238 3.1177 3.0229 -0.4187 0.4176  -0.0834 700  TYR A OH  
5330  N N   . ASP A 701  ? 2.9564 3.3284 3.2265 -0.4643 0.1649  -0.3965 701  ASP A N   
5331  C CA  . ASP A 701  ? 2.9251 3.2917 3.2435 -0.4860 0.1019  -0.4445 701  ASP A CA  
5332  C C   . ASP A 701  ? 2.9099 3.2448 3.1543 -0.4855 0.1082  -0.5182 701  ASP A C   
5333  O O   . ASP A 701  ? 2.8845 3.2024 3.1455 -0.4997 0.0728  -0.5658 701  ASP A O   
5334  C CB  . ASP A 701  ? 2.9257 3.3355 3.3162 -0.4923 0.0333  -0.4414 701  ASP A CB  
5335  C CG  . ASP A 701  ? 2.9672 3.3976 3.3131 -0.4763 0.0291  -0.4655 701  ASP A CG  
5336  O OD1 . ASP A 701  ? 3.0035 3.4083 3.2629 -0.4653 0.0666  -0.5019 701  ASP A OD1 
5337  O OD2 . ASP A 701  ? 2.9629 3.4369 3.3599 -0.4763 -0.0126 -0.4481 701  ASP A OD2 
5338  N N   . GLY A 702  ? 3.3822 3.7105 3.5432 -0.4686 0.1533  -0.5262 702  GLY A N   
5339  C CA  . GLY A 702  ? 3.3480 3.6543 3.4316 -0.4686 0.1629  -0.5931 702  GLY A CA  
5340  C C   . GLY A 702  ? 3.2766 3.5519 3.3519 -0.4836 0.1632  -0.6351 702  GLY A C   
5341  O O   . GLY A 702  ? 3.2281 3.5065 3.3294 -0.4936 0.1116  -0.6875 702  GLY A O   
5342  N N   . ALA A 703  ? 2.0812 2.3275 2.1207 -0.4839 0.2203  -0.6125 703  ALA A N   
5343  C CA  . ALA A 703  ? 2.1209 2.3406 2.1504 -0.4974 0.2248  -0.6493 703  ALA A CA  
5344  C C   . ALA A 703  ? 2.0328 2.2601 2.1601 -0.5108 0.1670  -0.6425 703  ALA A C   
5345  O O   . ALA A 703  ? 2.0257 2.2397 2.1608 -0.5207 0.1388  -0.6913 703  ALA A O   
5346  C CB  . ALA A 703  ? 2.1634 2.3534 2.1370 -0.4954 0.2986  -0.6208 703  ALA A CB  
5347  N N   . CYS A 704  ? 2.5800 2.8298 2.7791 -0.5109 0.1478  -0.5828 704  CYS A N   
5348  C CA  . CYS A 704  ? 2.5028 2.7566 2.7925 -0.5260 0.1078  -0.5540 704  CYS A CA  
5349  C C   . CYS A 704  ? 2.4687 2.6918 2.7636 -0.5389 0.0974  -0.5896 704  CYS A C   
5350  O O   . CYS A 704  ? 2.4745 2.6778 2.7398 -0.5401 0.1471  -0.5737 704  CYS A O   
5351  C CB  . CYS A 704  ? 2.4602 2.7451 2.8306 -0.5327 0.0361  -0.5450 704  CYS A CB  
5352  S SG  . CYS A 704  ? 2.1108 2.4149 2.5854 -0.5489 0.0103  -0.4702 704  CYS A SG  
5353  N N   . VAL A 705  ? 2.6355 2.8544 2.9671 -0.5475 0.0330  -0.6369 705  VAL A N   
5354  C CA  . VAL A 705  ? 2.6154 2.8059 2.9522 -0.5566 0.0194  -0.6716 705  VAL A CA  
5355  C C   . VAL A 705  ? 2.6289 2.8141 2.9762 -0.5576 -0.0448 -0.7423 705  VAL A C   
5356  O O   . VAL A 705  ? 2.6299 2.8041 3.0420 -0.5676 -0.1029 -0.7468 705  VAL A O   
5357  C CB  . VAL A 705  ? 2.5517 2.7346 2.9633 -0.5712 0.0035  -0.6192 705  VAL A CB  
5358  C CG1 . VAL A 705  ? 2.5699 2.7410 2.9478 -0.5709 0.0735  -0.5835 705  VAL A CG1 
5359  C CG2 . VAL A 705  ? 2.5255 2.7369 3.0100 -0.5778 -0.0290 -0.5626 705  VAL A CG2 
5360  N N   . ASN A 706  ? 3.5094 3.7013 3.7914 -0.5472 -0.0353 -0.7978 706  ASN A N   
5361  C CA  . ASN A 706  ? 3.5161 3.7087 3.8059 -0.5453 -0.0961 -0.8673 706  ASN A CA  
5362  C C   . ASN A 706  ? 3.4924 3.6742 3.7166 -0.5402 -0.0784 -0.9351 706  ASN A C   
5363  O O   . ASN A 706  ? 3.5214 3.7127 3.6674 -0.5340 -0.0320 -0.9596 706  ASN A O   
5364  C CB  . ASN A 706  ? 3.5767 3.7980 3.8655 -0.5389 -0.1239 -0.8813 706  ASN A CB  
5365  C CG  . ASN A 706  ? 3.5900 3.8139 3.9504 -0.5442 -0.2084 -0.9033 706  ASN A CG  
5366  O OD1 . ASN A 706  ? 3.5784 3.7776 3.9768 -0.5502 -0.2488 -0.9231 706  ASN A OD1 
5367  N ND2 . ASN A 706  ? 3.6191 3.8710 3.9967 -0.5418 -0.2362 -0.8997 706  ASN A ND2 
5368  N N   . ASN A 707  ? 3.2205 3.3827 3.4772 -0.5433 -0.1176 -0.9643 707  ASN A N   
5369  C CA  . ASN A 707  ? 3.2010 3.3566 3.4058 -0.5378 -0.1077 -1.0288 707  ASN A CA  
5370  C C   . ASN A 707  ? 3.1437 3.3040 3.3600 -0.5295 -0.1755 -1.1026 707  ASN A C   
5371  O O   . ASN A 707  ? 3.1062 3.2683 3.2804 -0.5224 -0.1730 -1.1622 707  ASN A O   
5372  C CB  . ASN A 707  ? 3.2129 3.3433 3.4309 -0.5441 -0.0875 -1.0075 707  ASN A CB  
5373  C CG  . ASN A 707  ? 3.1949 3.3063 3.5017 -0.5546 -0.1251 -0.9499 707  ASN A CG  
5374  O OD1 . ASN A 707  ? 3.1880 3.3066 3.5464 -0.5588 -0.1619 -0.9207 707  ASN A OD1 
5375  N ND2 . ASN A 707  ? 3.1816 3.2711 3.5051 -0.5605 -0.1152 -0.9327 707  ASN A ND2 
5376  N N   . ASP A 708  ? 2.9190 3.0833 3.1912 -0.5298 -0.2359 -1.0999 708  ASP A N   
5377  C CA  . ASP A 708  ? 2.8725 3.0388 3.1588 -0.5207 -0.3045 -1.1695 708  ASP A CA  
5378  C C   . ASP A 708  ? 2.8880 3.0907 3.1224 -0.5113 -0.3030 -1.2188 708  ASP A C   
5379  O O   . ASP A 708  ? 2.8690 3.0802 3.1090 -0.5022 -0.3567 -1.2797 708  ASP A O   
5380  C CB  . ASP A 708  ? 2.7900 2.9366 3.1642 -0.5278 -0.3776 -1.1471 708  ASP A CB  
5381  C CG  . ASP A 708  ? 2.6741 2.7798 3.0905 -0.5302 -0.4150 -1.1517 708  ASP A CG  
5382  O OD1 . ASP A 708  ? 2.6126 2.7083 2.9958 -0.5265 -0.3793 -1.1621 708  ASP A OD1 
5383  O OD2 . ASP A 708  ? 2.6314 2.7138 3.1127 -0.5364 -0.4809 -1.1448 708  ASP A OD2 
5384  N N   . GLU A 709  ? 2.7273 2.9503 2.9095 -0.5131 -0.2420 -1.1925 709  GLU A N   
5385  C CA  . GLU A 709  ? 2.7800 3.0371 2.9099 -0.5062 -0.2370 -1.2329 709  GLU A CA  
5386  C C   . GLU A 709  ? 2.8301 3.0968 2.8877 -0.5090 -0.1569 -1.2024 709  GLU A C   
5387  O O   . GLU A 709  ? 2.8766 3.1290 2.9460 -0.5147 -0.1184 -1.1340 709  GLU A O   
5388  C CB  . GLU A 709  ? 2.8050 3.0770 2.9883 -0.5058 -0.2922 -1.2229 709  GLU A CB  
5389  C CG  . GLU A 709  ? 2.8091 3.0714 3.0554 -0.5157 -0.2927 -1.1397 709  GLU A CG  
5390  C CD  . GLU A 709  ? 2.8096 3.0940 3.1040 -0.5168 -0.3451 -1.1315 709  GLU A CD  
5391  O OE1 . GLU A 709  ? 2.8159 3.1281 3.0785 -0.5089 -0.3613 -1.1794 709  GLU A OE1 
5392  O OE2 . GLU A 709  ? 2.7937 3.0710 3.1574 -0.5268 -0.3697 -1.0765 709  GLU A OE2 
5393  N N   . THR A 710  ? 2.9323 3.2226 2.9130 -0.5050 -0.1326 -1.2536 710  THR A N   
5394  C CA  . THR A 710  ? 2.9924 3.2845 2.8911 -0.5091 -0.0552 -1.2335 710  THR A CA  
5395  C C   . THR A 710  ? 3.0617 3.3527 2.9693 -0.5092 -0.0316 -1.1647 710  THR A C   
5396  O O   . THR A 710  ? 3.0426 3.3375 3.0215 -0.5074 -0.0744 -1.1323 710  THR A O   
5397  C CB  . THR A 710  ? 3.2839 3.6062 3.1006 -0.5075 -0.0412 -1.2993 710  THR A CB  
5398  O OG1 . THR A 710  ? 3.3046 3.6488 3.1113 -0.5040 -0.0498 -1.2905 710  THR A OG1 
5399  C CG2 . THR A 710  ? 3.2611 3.6015 3.0897 -0.5013 -0.0942 -1.3780 710  THR A CG2 
5400  N N   . CYS A 711  ? 2.8888 3.1743 2.7210 -0.5112 0.0371  -1.1424 711  CYS A N   
5401  C CA  . CYS A 711  ? 2.9622 3.2449 2.7958 -0.5074 0.0645  -1.0758 711  CYS A CA  
5402  C C   . CYS A 711  ? 2.9961 3.3084 2.8051 -0.5009 0.0477  -1.0927 711  CYS A C   
5403  O O   . CYS A 711  ? 3.0313 3.3503 2.8625 -0.4947 0.0489  -1.0419 711  CYS A O   
5404  C CB  . CYS A 711  ? 3.0285 3.2831 2.7972 -0.5103 0.1456  -1.0340 711  CYS A CB  
5405  S SG  . CYS A 711  ? 2.9940 3.2224 2.8296 -0.5111 0.1641  -0.9510 711  CYS A SG  
5406  N N   . GLU A 712  ? 2.9763 3.3107 2.7410 -0.5017 0.0311  -1.1634 712  GLU A N   
5407  C CA  . GLU A 712  ? 2.9995 3.3666 2.7464 -0.4961 0.0082  -1.1835 712  GLU A CA  
5408  C C   . GLU A 712  ? 2.8987 3.2929 2.7182 -0.4922 -0.0742 -1.2233 712  GLU A C   
5409  O O   . GLU A 712  ? 2.8906 3.3159 2.7089 -0.4874 -0.1033 -1.2417 712  GLU A O   
5410  C CB  . GLU A 712  ? 3.1288 3.5072 2.7713 -0.5005 0.0474  -1.2303 712  GLU A CB  
5411  C CG  . GLU A 712  ? 3.1972 3.5643 2.7949 -0.5098 0.0748  -1.2720 712  GLU A CG  
5412  C CD  . GLU A 712  ? 3.3116 3.6889 2.8008 -0.5184 0.1216  -1.3082 712  GLU A CD  
5413  O OE1 . GLU A 712  ? 3.3660 3.7140 2.7913 -0.5244 0.1870  -1.2697 712  GLU A OE1 
5414  O OE2 . GLU A 712  ? 3.3268 3.7414 2.7932 -0.5195 0.0924  -1.3748 712  GLU A OE2 
5415  N N   . GLN A 713  ? 3.4178 3.7974 3.2980 -0.4942 -0.1114 -1.2364 713  GLN A N   
5416  C CA  . GLN A 713  ? 3.3479 3.7384 3.3105 -0.4913 -0.1910 -1.2577 713  GLN A CA  
5417  C C   . GLN A 713  ? 3.2951 3.6834 3.3283 -0.4924 -0.2089 -1.1864 713  GLN A C   
5418  O O   . GLN A 713  ? 3.3021 3.7158 3.3712 -0.4899 -0.2545 -1.1908 713  GLN A O   
5419  C CB  . GLN A 713  ? 3.3121 3.6794 3.3131 -0.4928 -0.2217 -1.2876 713  GLN A CB  
5420  C CG  . GLN A 713  ? 3.3139 3.6932 3.2575 -0.4892 -0.2194 -1.3673 713  GLN A CG  
5421  C CD  . GLN A 713  ? 3.2775 3.6328 3.2598 -0.4874 -0.2498 -1.3930 713  GLN A CD  
5422  O OE1 . GLN A 713  ? 3.2560 3.5785 3.2826 -0.4926 -0.2440 -1.3438 713  GLN A OE1 
5423  N NE2 . GLN A 713  ? 3.2725 3.6462 3.2359 -0.4790 -0.2819 -1.4708 713  GLN A NE2 
5424  N N   . ARG A 714  ? 3.3914 3.7536 3.4437 -0.4968 -0.1721 -1.1216 714  ARG A N   
5425  C CA  . ARG A 714  ? 3.3521 3.7179 3.4645 -0.4981 -0.1783 -1.0482 714  ARG A CA  
5426  C C   . ARG A 714  ? 3.3389 3.7314 3.4108 -0.4898 -0.1503 -1.0229 714  ARG A C   
5427  O O   . ARG A 714  ? 3.3168 3.7307 3.4386 -0.4880 -0.1745 -0.9824 714  ARG A O   
5428  C CB  . ARG A 714  ? 3.3624 3.6987 3.4881 -0.5029 -0.1334 -0.9869 714  ARG A CB  
5429  C CG  . ARG A 714  ? 3.3516 3.6589 3.5148 -0.5111 -0.1542 -1.0026 714  ARG A CG  
5430  C CD  . ARG A 714  ? 3.3929 3.6729 3.5219 -0.5139 -0.0875 -0.9679 714  ARG A CD  
5431  N NE  . ARG A 714  ? 3.4421 3.7199 3.6075 -0.5157 -0.0616 -0.8861 714  ARG A NE  
5432  C CZ  . ARG A 714  ? 3.4870 3.7430 3.6412 -0.5185 -0.0106 -0.8444 714  ARG A CZ  
5433  N NH1 . ARG A 714  ? 3.4905 3.7235 3.5985 -0.5214 0.0205  -0.8756 714  ARG A NH1 
5434  N NH2 . ARG A 714  ? 3.5068 3.7680 3.6970 -0.5184 0.0088  -0.7718 714  ARG A NH2 
5435  N N   . ALA A 715  ? 2.6007 2.9918 2.5798 -0.4854 -0.0990 -1.0466 715  ALA A N   
5436  C CA  . ALA A 715  ? 2.6169 3.0245 2.5393 -0.4767 -0.0630 -1.0241 715  ALA A CA  
5437  C C   . ALA A 715  ? 2.5982 3.0458 2.5234 -0.4730 -0.1112 -1.0669 715  ALA A C   
5438  O O   . ALA A 715  ? 2.6541 3.1218 2.5429 -0.4651 -0.0943 -1.0498 715  ALA A O   
5439  C CB  . ALA A 715  ? 2.6111 2.9968 2.4293 -0.4772 0.0074  -1.0365 715  ALA A CB  
5440  N N   . ALA A 716  ? 2.6816 3.1399 2.6480 -0.4775 -0.1718 -1.1236 716  ALA A N   
5441  C CA  . ALA A 716  ? 2.7086 3.2059 2.6901 -0.4743 -0.2261 -1.1659 716  ALA A CA  
5442  C C   . ALA A 716  ? 2.7010 3.2166 2.7668 -0.4741 -0.2697 -1.1187 716  ALA A C   
5443  O O   . ALA A 716  ? 2.7290 3.2759 2.7873 -0.4678 -0.2704 -1.0987 716  ALA A O   
5444  C CB  . ALA A 716  ? 2.6836 3.1835 2.6793 -0.4770 -0.2761 -1.2435 716  ALA A CB  
5445  N N   . ARG A 717  ? 2.4178 2.9142 2.5615 -0.4820 -0.3042 -1.0993 717  ARG A N   
5446  C CA  . ARG A 717  ? 2.4296 2.9416 2.6607 -0.4873 -0.3510 -1.0568 717  ARG A CA  
5447  C C   . ARG A 717  ? 2.4478 2.9797 2.6775 -0.4812 -0.3126 -0.9824 717  ARG A C   
5448  O O   . ARG A 717  ? 2.4302 2.9844 2.7282 -0.4854 -0.3451 -0.9409 717  ARG A O   
5449  C CB  . ARG A 717  ? 2.3436 2.8215 2.6420 -0.4992 -0.3750 -1.0377 717  ARG A CB  
5450  C CG  . ARG A 717  ? 2.3592 2.8450 2.7483 -0.5105 -0.4502 -1.0337 717  ARG A CG  
5451  C CD  . ARG A 717  ? 2.3419 2.7848 2.7800 -0.5224 -0.4711 -1.0270 717  ARG A CD  
5452  N NE  . ARG A 717  ? 2.3215 2.7338 2.7090 -0.5169 -0.4509 -1.0784 717  ARG A NE  
5453  C CZ  . ARG A 717  ? 2.2923 2.6816 2.6398 -0.5151 -0.3895 -1.0563 717  ARG A CZ  
5454  N NH1 . ARG A 717  ? 2.2825 2.6726 2.6336 -0.5169 -0.3414 -0.9837 717  ARG A NH1 
5455  N NH2 . ARG A 717  ? 2.2863 2.6540 2.5892 -0.5110 -0.3759 -1.1078 717  ARG A NH2 
5456  N N   . ILE A 718  ? 2.7901 3.3132 2.9402 -0.4712 -0.2435 -0.9659 718  ILE A N   
5457  C CA  . ILE A 718  ? 2.8581 3.3939 2.9939 -0.4605 -0.1996 -0.8964 718  ILE A CA  
5458  C C   . ILE A 718  ? 2.9579 3.5375 3.0748 -0.4502 -0.2130 -0.8994 718  ILE A C   
5459  O O   . ILE A 718  ? 2.9629 3.5493 3.0103 -0.4452 -0.2015 -0.9448 718  ILE A O   
5460  C CB  . ILE A 718  ? 2.8536 3.3532 2.9102 -0.4535 -0.1186 -0.8720 718  ILE A CB  
5461  C CG1 . ILE A 718  ? 2.8398 3.3083 2.9380 -0.4609 -0.1013 -0.8317 718  ILE A CG1 
5462  C CG2 . ILE A 718  ? 2.8939 3.4067 2.9044 -0.4367 -0.0732 -0.8221 718  ILE A CG2 
5463  C CD1 . ILE A 718  ? 2.8867 3.3239 2.9197 -0.4527 -0.0225 -0.7919 718  ILE A CD1 
5464  N N   . SER A 719  ? 2.2312 2.8434 2.4117 -0.4482 -0.2371 -0.8489 719  SER A N   
5465  C CA  . SER A 719  ? 2.2500 2.9113 2.4330 -0.4391 -0.2587 -0.8429 719  SER A CA  
5466  C C   . SER A 719  ? 2.2609 2.9311 2.3982 -0.4195 -0.2008 -0.7815 719  SER A C   
5467  O O   . SER A 719  ? 2.2800 2.9413 2.3302 -0.4075 -0.1594 -0.7946 719  SER A O   
5468  C CB  . SER A 719  ? 2.2457 2.9414 2.5318 -0.4506 -0.3246 -0.8245 719  SER A CB  
5469  O OG  . SER A 719  ? 2.2629 3.0117 2.5574 -0.4428 -0.3482 -0.8169 719  SER A OG  
5470  N N   . LEU A 720  ? 2.6673 3.3550 2.8639 -0.4166 -0.1998 -0.7146 720  LEU A N   
5471  C CA  . LEU A 720  ? 2.8182 3.5215 2.9885 -0.3948 -0.1524 -0.6485 720  LEU A CA  
5472  C C   . LEU A 720  ? 2.9370 3.6241 2.9985 -0.3751 -0.0987 -0.6561 720  LEU A C   
5473  O O   . LEU A 720  ? 2.9440 3.6635 2.9866 -0.3567 -0.0902 -0.6267 720  LEU A O   
5474  C CB  . LEU A 720  ? 2.8611 3.5404 3.0554 -0.3937 -0.1145 -0.5898 720  LEU A CB  
5475  C CG  . LEU A 720  ? 2.8878 3.5710 3.1799 -0.4149 -0.1538 -0.5723 720  LEU A CG  
5476  C CD1 . LEU A 720  ? 2.9107 3.5652 3.2016 -0.4107 -0.1011 -0.5182 720  LEU A CD1 
5477  C CD2 . LEU A 720  ? 2.9169 3.6615 3.2961 -0.4214 -0.2100 -0.5450 720  LEU A CD2 
5478  N N   . GLY A 721  ? 3.7512 4.3883 3.7397 -0.3794 -0.0615 -0.6929 721  GLY A N   
5479  C CA  . GLY A 721  ? 3.8510 4.4684 3.7318 -0.3661 -0.0133 -0.7050 721  GLY A CA  
5480  C C   . GLY A 721  ? 3.8856 4.4436 3.6882 -0.3733 0.0380  -0.7314 721  GLY A C   
5481  O O   . GLY A 721  ? 3.8850 4.4095 3.7010 -0.3775 0.0649  -0.7078 721  GLY A O   
5482  N N   . PRO A 722  ? 3.3033 3.8515 3.0225 -0.3762 0.0516  -0.7813 722  PRO A N   
5483  C CA  . PRO A 722  ? 3.2735 3.7703 2.9014 -0.3842 0.1041  -0.8094 722  PRO A CA  
5484  C C   . PRO A 722  ? 3.2333 3.6827 2.8047 -0.3705 0.1758  -0.7498 722  PRO A C   
5485  O O   . PRO A 722  ? 3.2073 3.6088 2.7175 -0.3791 0.2222  -0.7615 722  PRO A O   
5486  C CB  . PRO A 722  ? 3.3147 3.8262 2.8662 -0.3857 0.1023  -0.8572 722  PRO A CB  
5487  C CG  . PRO A 722  ? 3.3150 3.8860 2.9401 -0.3870 0.0304  -0.8827 722  PRO A CG  
5488  C CD  . PRO A 722  ? 3.3154 3.9089 3.0293 -0.3755 0.0096  -0.8200 722  PRO A CD  
5489  N N   . ARG A 723  ? 3.5544 4.0190 3.1462 -0.3487 0.1843  -0.6871 723  ARG A N   
5490  C CA  . ARG A 723  ? 3.5231 3.9453 3.0672 -0.3312 0.2485  -0.6280 723  ARG A CA  
5491  C C   . ARG A 723  ? 3.4693 3.8604 3.0469 -0.3422 0.2673  -0.6159 723  ARG A C   
5492  O O   . ARG A 723  ? 3.4852 3.8240 2.9976 -0.3390 0.3269  -0.5977 723  ARG A O   
5493  C CB  . ARG A 723  ? 3.4901 3.9480 3.0779 -0.3049 0.2416  -0.5630 723  ARG A CB  
5494  C CG  . ARG A 723  ? 3.4555 3.9699 3.0625 -0.2984 0.1945  -0.5768 723  ARG A CG  
5495  C CD  . ARG A 723  ? 3.4156 3.9746 3.0802 -0.2741 0.1830  -0.5119 723  ARG A CD  
5496  N NE  . ARG A 723  ? 3.4007 4.0198 3.0922 -0.2695 0.1342  -0.5252 723  ARG A NE  
5497  C CZ  . ARG A 723  ? 3.3758 4.0511 3.1647 -0.2831 0.0686  -0.5404 723  ARG A CZ  
5498  N NH1 . ARG A 723  ? 3.3424 4.0185 3.2104 -0.3021 0.0433  -0.5429 723  ARG A NH1 
5499  N NH2 . ARG A 723  ? 3.3947 4.1236 3.1997 -0.2784 0.0281  -0.5528 723  ARG A NH2 
5500  N N   . CYS A 724  ? 3.2609 3.6828 2.9391 -0.3559 0.2153  -0.6261 724  CYS A N   
5501  C CA  . CYS A 724  ? 3.2002 3.5987 2.9214 -0.3663 0.2267  -0.6101 724  CYS A CA  
5502  C C   . CYS A 724  ? 3.1838 3.5576 2.8907 -0.3905 0.2193  -0.6737 724  CYS A C   
5503  O O   . CYS A 724  ? 3.1493 3.4878 2.8490 -0.3981 0.2510  -0.6666 724  CYS A O   
5504  C CB  . CYS A 724  ? 3.1634 3.6049 3.0025 -0.3664 0.1806  -0.5704 724  CYS A CB  
5505  S SG  . CYS A 724  ? 2.7508 3.2376 2.6877 -0.3882 0.0884  -0.6204 724  CYS A SG  
5506  N N   . ILE A 725  ? 3.3544 3.7497 3.0557 -0.4011 0.1782  -0.7364 725  ILE A N   
5507  C CA  . ILE A 725  ? 3.3415 3.7224 3.0336 -0.4212 0.1650  -0.8006 725  ILE A CA  
5508  C C   . ILE A 725  ? 3.3550 3.6836 2.9635 -0.4267 0.2329  -0.8029 725  ILE A C   
5509  O O   . ILE A 725  ? 3.3473 3.6578 2.9703 -0.4403 0.2346  -0.8250 725  ILE A O   
5510  C CB  . ILE A 725  ? 3.3392 3.7493 3.0069 -0.4278 0.1257  -0.8701 725  ILE A CB  
5511  C CG1 . ILE A 725  ? 3.3314 3.7922 3.0891 -0.4251 0.0536  -0.8721 725  ILE A CG1 
5512  C CG2 . ILE A 725  ? 3.3269 3.7244 2.9751 -0.4454 0.1180  -0.9377 725  ILE A CG2 
5513  C CD1 . ILE A 725  ? 3.3458 3.8385 3.0967 -0.4325 0.0049  -0.9457 725  ILE A CD1 
5514  N N   . LYS A 726  ? 3.7877 4.0904 3.3077 -0.4161 0.2886  -0.7787 726  LYS A N   
5515  C CA  . LYS A 726  ? 3.8011 4.0503 3.2374 -0.4217 0.3561  -0.7749 726  LYS A CA  
5516  C C   . LYS A 726  ? 3.6983 3.9258 3.1824 -0.4194 0.3778  -0.7265 726  LYS A C   
5517  O O   . LYS A 726  ? 3.6505 3.8515 3.1193 -0.4338 0.3999  -0.7456 726  LYS A O   
5518  C CB  . LYS A 726  ? 3.9377 4.1570 3.2722 -0.4087 0.4096  -0.7496 726  LYS A CB  
5519  C CG  . LYS A 726  ? 4.0650 4.2756 3.3028 -0.4229 0.4234  -0.8073 726  LYS A CG  
5520  C CD  . LYS A 726  ? 4.1783 4.3323 3.2989 -0.4182 0.4950  -0.7816 726  LYS A CD  
5521  C CE  . LYS A 726  ? 4.2519 4.3953 3.2717 -0.4388 0.5122  -0.8404 726  LYS A CE  
5522  N NZ  . LYS A 726  ? 4.3126 4.3909 3.2121 -0.4395 0.5841  -0.8174 726  LYS A NZ  
5523  N N   . ALA A 727  ? 4.0589 4.3025 3.6009 -0.4015 0.3713  -0.6641 727  ALA A N   
5524  C CA  . ALA A 727  ? 4.0052 4.2356 3.5956 -0.3976 0.3920  -0.6114 727  ALA A CA  
5525  C C   . ALA A 727  ? 3.9003 4.1464 3.5779 -0.4162 0.3474  -0.6330 727  ALA A C   
5526  O O   . ALA A 727  ? 3.8692 4.1007 3.5802 -0.4197 0.3648  -0.6029 727  ALA A O   
5527  C CB  . ALA A 727  ? 4.0166 4.2737 3.6542 -0.3743 0.3877  -0.5439 727  ALA A CB  
5528  N N   . PHE A 728  ? 2.8182 3.0938 2.5316 -0.4272 0.2885  -0.6854 728  PHE A N   
5529  C CA  . PHE A 728  ? 2.7364 3.0200 2.5208 -0.4443 0.2430  -0.7159 728  PHE A CA  
5530  C C   . PHE A 728  ? 2.7682 3.0181 2.4949 -0.4589 0.2724  -0.7640 728  PHE A C   
5531  O O   . PHE A 728  ? 2.7781 3.0012 2.5067 -0.4638 0.3054  -0.7417 728  PHE A O   
5532  C CB  . PHE A 728  ? 2.6271 2.9511 2.4642 -0.4485 0.1696  -0.7574 728  PHE A CB  
5533  C CG  . PHE A 728  ? 2.5853 2.9170 2.5084 -0.4624 0.1141  -0.7775 728  PHE A CG  
5534  C CD1 . PHE A 728  ? 2.5527 2.8847 2.5526 -0.4654 0.1044  -0.7249 728  PHE A CD1 
5535  C CD2 . PHE A 728  ? 2.6243 2.9625 2.5495 -0.4721 0.0711  -0.8488 728  PHE A CD2 
5536  C CE1 . PHE A 728  ? 2.5466 2.8797 2.6222 -0.4794 0.0523  -0.7416 728  PHE A CE1 
5537  C CE2 . PHE A 728  ? 2.5490 2.8875 2.5496 -0.4828 0.0186  -0.8673 728  PHE A CE2 
5538  C CZ  . PHE A 728  ? 2.5178 2.8509 2.5929 -0.4873 0.0090  -0.8128 728  PHE A CZ  
5539  N N   . THR A 729  ? 3.2624 3.5182 2.9362 -0.4657 0.2614  -0.8294 729  THR A N   
5540  C CA  . THR A 729  ? 3.2596 3.4962 2.8790 -0.4806 0.2810  -0.8855 729  THR A CA  
5541  C C   . THR A 729  ? 3.2803 3.4731 2.8173 -0.4842 0.3588  -0.8655 729  THR A C   
5542  O O   . THR A 729  ? 3.2699 3.4466 2.7827 -0.4974 0.3770  -0.8964 729  THR A O   
5543  C CB  . THR A 729  ? 3.6271 3.8856 3.1928 -0.4855 0.2612  -0.9551 729  THR A CB  
5544  O OG1 . THR A 729  ? 3.6396 3.9185 3.1945 -0.4735 0.2510  -0.9378 729  THR A OG1 
5545  C CG2 . THR A 729  ? 3.6243 3.9114 3.2524 -0.4921 0.1932  -1.0129 729  THR A CG2 
5546  N N   . GLU A 730  ? 3.8765 4.0499 3.3678 -0.4717 0.4038  -0.8155 730  GLU A N   
5547  C CA  . GLU A 730  ? 3.9172 4.0435 3.3329 -0.4726 0.4776  -0.7879 730  GLU A CA  
5548  C C   . GLU A 730  ? 3.9056 4.0206 3.3814 -0.4748 0.4858  -0.7528 730  GLU A C   
5549  O O   . GLU A 730  ? 3.8989 3.9870 3.3383 -0.4871 0.5223  -0.7659 730  GLU A O   
5550  C CB  . GLU A 730  ? 3.9508 4.0597 3.3236 -0.4527 0.5141  -0.7328 730  GLU A CB  
5551  C CG  . GLU A 730  ? 3.9782 4.0758 3.2511 -0.4530 0.5354  -0.7602 730  GLU A CG  
5552  C CD  . GLU A 730  ? 3.9860 4.0303 3.1467 -0.4648 0.6047  -0.7701 730  GLU A CD  
5553  O OE1 . GLU A 730  ? 3.9602 3.9699 3.1143 -0.4629 0.6471  -0.7331 730  GLU A OE1 
5554  O OE2 . GLU A 730  ? 4.0123 4.0506 3.0907 -0.4772 0.6164  -0.8146 730  GLU A OE2 
5555  N N   . CYS A 731  ? 5.5350 5.6743 5.1040 -0.4639 0.4504  -0.7077 731  CYS A N   
5556  C CA  . CYS A 731  ? 5.5411 5.6732 5.1690 -0.4629 0.4615  -0.6583 731  CYS A CA  
5557  C C   . CYS A 731  ? 5.5508 5.6964 5.2533 -0.4788 0.4158  -0.6862 731  CYS A C   
5558  O O   . CYS A 731  ? 5.5436 5.6756 5.2735 -0.4843 0.4336  -0.6612 731  CYS A O   
5559  C CB  . CYS A 731  ? 5.5266 5.6819 5.2127 -0.4442 0.4491  -0.5929 731  CYS A CB  
5560  S SG  . CYS A 731  ? 6.1226 6.2519 5.7302 -0.3769 0.4551  -0.5314 731  CYS A SG  
5561  N N   . CYS A 732  ? 4.1342 4.3054 3.8673 -0.4852 0.3568  -0.7382 732  CYS A N   
5562  C CA  . CYS A 732  ? 4.1446 4.3221 3.9351 -0.4984 0.3129  -0.7740 732  CYS A CA  
5563  C C   . CYS A 732  ? 4.1536 4.3069 3.8754 -0.5100 0.3513  -0.8181 732  CYS A C   
5564  O O   . CYS A 732  ? 4.1546 4.2955 3.9035 -0.5179 0.3573  -0.8123 732  CYS A O   
5565  C CB  . CYS A 732  ? 4.1276 4.3363 3.9627 -0.4996 0.2396  -0.8215 732  CYS A CB  
5566  S SG  . CYS A 732  ? 3.9642 4.1775 3.8886 -0.5111 0.1724  -0.8531 732  CYS A SG  
5567  N N   . VAL A 733  ? 3.6249 3.7738 3.2565 -0.5122 0.3778  -0.8609 733  VAL A N   
5568  C CA  . VAL A 733  ? 3.6104 3.7422 3.1685 -0.5255 0.4162  -0.9057 733  VAL A CA  
5569  C C   . VAL A 733  ? 3.5778 3.6760 3.1155 -0.5289 0.4757  -0.8611 733  VAL A C   
5570  O O   . VAL A 733  ? 3.5286 3.6199 3.0690 -0.5396 0.4845  -0.8802 733  VAL A O   
5571  C CB  . VAL A 733  ? 3.6260 3.7547 3.0786 -0.5293 0.4489  -0.9431 733  VAL A CB  
5572  C CG1 . VAL A 733  ? 3.6386 3.7471 3.0093 -0.5459 0.5005  -0.9770 733  VAL A CG1 
5573  C CG2 . VAL A 733  ? 3.6219 3.7890 3.0881 -0.5281 0.3907  -0.9990 733  VAL A CG2 
5574  N N   . VAL A 734  ? 4.6368 4.7159 4.1545 -0.5181 0.5154  -0.8018 734  VAL A N   
5575  C CA  . VAL A 734  ? 4.6381 4.6855 4.1366 -0.5182 0.5727  -0.7546 734  VAL A CA  
5576  C C   . VAL A 734  ? 4.6316 4.6882 4.2201 -0.5225 0.5477  -0.7337 734  VAL A C   
5577  O O   . VAL A 734  ? 4.6519 4.6900 4.2214 -0.5322 0.5827  -0.7331 734  VAL A O   
5578  C CB  . VAL A 734  ? 4.6341 4.6671 4.1183 -0.4996 0.6051  -0.6895 734  VAL A CB  
5579  C CG1 . VAL A 734  ? 4.6191 4.6217 4.0899 -0.4974 0.6617  -0.6396 734  VAL A CG1 
5580  C CG2 . VAL A 734  ? 4.6636 4.6799 4.0500 -0.4955 0.6338  -0.7075 734  VAL A CG2 
5581  N N   . ALA A 735  ? 4.6813 4.7664 4.3661 -0.5170 0.4866  -0.7168 735  ALA A N   
5582  C CA  . ALA A 735  ? 4.6595 4.7524 4.4339 -0.5219 0.4586  -0.6893 735  ALA A CA  
5583  C C   . ALA A 735  ? 4.6336 4.7322 4.4329 -0.5347 0.4186  -0.7464 735  ALA A C   
5584  O O   . ALA A 735  ? 4.6070 4.7027 4.4592 -0.5415 0.4069  -0.7316 735  ALA A O   
5585  C CB  . ALA A 735  ? 4.6419 4.7618 4.5062 -0.5136 0.4105  -0.6447 735  ALA A CB  
5586  N N   . SER A 736  ? 3.5242 3.6322 3.2836 -0.5368 0.3977  -0.8116 736  SER A N   
5587  C CA  . SER A 736  ? 3.5067 3.6232 3.2822 -0.5449 0.3592  -0.8724 736  SER A CA  
5588  C C   . SER A 736  ? 3.4941 3.5956 3.2007 -0.5553 0.4094  -0.9027 736  SER A C   
5589  O O   . SER A 736  ? 3.4720 3.5728 3.2110 -0.5610 0.3941  -0.9174 736  SER A O   
5590  C CB  . SER A 736  ? 3.5118 3.6522 3.2806 -0.5412 0.3105  -0.9310 736  SER A CB  
5591  O OG  . SER A 736  ? 3.5047 3.6603 3.3425 -0.5333 0.2617  -0.9025 736  SER A OG  
5592  N N   . GLN A 737  ? 3.1828 3.2716 2.7930 -0.5586 0.4690  -0.9112 737  GLN A N   
5593  C CA  . GLN A 737  ? 3.1608 3.2341 2.7007 -0.5713 0.5242  -0.9320 737  GLN A CA  
5594  C C   . GLN A 737  ? 3.1455 3.1998 2.7218 -0.5731 0.5521  -0.8767 737  GLN A C   
5595  O O   . GLN A 737  ? 3.1034 3.1519 2.6590 -0.5835 0.5773  -0.8927 737  GLN A O   
5596  C CB  . GLN A 737  ? 3.1890 3.2436 2.6183 -0.5764 0.5867  -0.9376 737  GLN A CB  
5597  C CG  . GLN A 737  ? 3.2165 3.2841 2.6175 -0.5699 0.5664  -0.9577 737  GLN A CG  
5598  C CD  . GLN A 737  ? 3.2055 3.3071 2.5946 -0.5753 0.5242  -1.0355 737  GLN A CD  
5599  O OE1 . GLN A 737  ? 3.2134 3.3202 2.5355 -0.5892 0.5500  -1.0842 737  GLN A OE1 
5600  N NE2 . GLN A 737  ? 3.1885 3.3162 2.6411 -0.5646 0.4593  -1.0482 737  GLN A NE2 
5601  N N   . LEU A 738  ? 4.0708 4.1204 3.7027 -0.5630 0.5461  -0.8121 738  LEU A N   
5602  C CA  . LEU A 738  ? 4.1080 4.1439 3.7758 -0.5632 0.5743  -0.7515 738  LEU A CA  
5603  C C   . LEU A 738  ? 4.1485 4.1952 3.8987 -0.5692 0.5329  -0.7505 738  LEU A C   
5604  O O   . LEU A 738  ? 4.1522 4.1881 3.9011 -0.5761 0.5659  -0.7307 738  LEU A O   
5605  C CB  . LEU A 738  ? 4.1051 4.1417 3.8094 -0.5493 0.5767  -0.6842 738  LEU A CB  
5606  C CG  . LEU A 738  ? 4.0692 4.0967 3.8055 -0.5470 0.6108  -0.6164 738  LEU A CG  
5607  C CD1 . LEU A 738  ? 4.0821 4.0771 3.7239 -0.5469 0.6921  -0.6034 738  LEU A CD1 
5608  C CD2 . LEU A 738  ? 4.0647 4.1109 3.8691 -0.5336 0.5861  -0.5573 738  LEU A CD2 
5609  N N   . ARG A 739  ? 3.5829 3.6486 3.4034 -0.5667 0.4606  -0.7702 739  ARG A N   
5610  C CA  . ARG A 739  ? 3.6425 3.7121 3.5399 -0.5721 0.4163  -0.7688 739  ARG A CA  
5611  C C   . ARG A 739  ? 3.6395 3.7077 3.4993 -0.5792 0.4217  -0.8279 739  ARG A C   
5612  O O   . ARG A 739  ? 3.6231 3.6905 3.5322 -0.5831 0.3941  -0.8301 739  ARG A O   
5613  C CB  . ARG A 739  ? 3.7127 3.7967 3.6902 -0.5681 0.3359  -0.7760 739  ARG A CB  
5614  C CG  . ARG A 739  ? 3.7945 3.8899 3.7484 -0.5645 0.2953  -0.8510 739  ARG A CG  
5615  C CD  . ARG A 739  ? 3.8432 3.9487 3.8776 -0.5608 0.2164  -0.8535 739  ARG A CD  
5616  N NE  . ARG A 739  ? 3.9213 4.0410 3.9314 -0.5547 0.1784  -0.9226 739  ARG A NE  
5617  C CZ  . ARG A 739  ? 3.9457 4.0753 4.0101 -0.5505 0.1111  -0.9371 739  ARG A CZ  
5618  N NH1 . ARG A 739  ? 3.9331 4.0595 4.0787 -0.5539 0.0744  -0.8862 739  ARG A NH1 
5619  N NH2 . ARG A 739  ? 3.9652 4.1103 4.0020 -0.5440 0.0805  -1.0028 739  ARG A NH2 
5620  N N   . ALA A 740  ? 3.8689 3.9388 3.6401 -0.5811 0.4561  -0.8758 740  ALA A N   
5621  C CA  . ALA A 740  ? 3.8638 3.9391 3.5880 -0.5887 0.4709  -0.9318 740  ALA A CA  
5622  C C   . ALA A 740  ? 3.8458 3.9047 3.5269 -0.5987 0.5406  -0.9031 740  ALA A C   
5623  O O   . ALA A 740  ? 3.8687 3.9334 3.5133 -0.6069 0.5594  -0.9410 740  ALA A O   
5624  C CB  . ALA A 740  ? 3.8799 3.9699 3.5264 -0.5898 0.4775  -0.9968 740  ALA A CB  
5625  N N   . ASN A 741  ? 4.5093 4.5504 4.1950 -0.5973 0.5784  -0.8370 741  ASN A N   
5626  C CA  . ASN A 741  ? 4.4598 4.4825 4.0970 -0.6056 0.6494  -0.8078 741  ASN A CA  
5627  C C   . ASN A 741  ? 4.5735 4.5891 4.2756 -0.6039 0.6582  -0.7364 741  ASN A C   
5628  O O   . ASN A 741  ? 4.5795 4.5864 4.2601 -0.6120 0.7030  -0.7210 741  ASN A O   
5629  C CB  . ASN A 741  ? 4.3361 4.3387 3.8760 -0.6069 0.7107  -0.8057 741  ASN A CB  
5630  C CG  . ASN A 741  ? 4.2287 4.2380 3.6830 -0.6172 0.7242  -0.8776 741  ASN A CG  
5631  O OD1 . ASN A 741  ? 4.2170 4.2300 3.6362 -0.6139 0.7136  -0.9023 741  ASN A OD1 
5632  N ND2 . ASN A 741  ? 4.1472 4.1626 3.5681 -0.6305 0.7470  -0.9116 741  ASN A ND2 
5633  N N   . ILE A 742  ? 4.2403 4.2633 4.0203 -0.5949 0.6165  -0.6935 742  ILE A N   
5634  C CA  . ILE A 742  ? 4.3425 4.3674 4.1937 -0.5952 0.6154  -0.6276 742  ILE A CA  
5635  C C   . ILE A 742  ? 4.3691 4.4009 4.2720 -0.6042 0.5813  -0.6427 742  ILE A C   
5636  O O   . ILE A 742  ? 4.3631 4.3958 4.3100 -0.6091 0.5902  -0.5971 742  ILE A O   
5637  C CB  . ILE A 742  ? 4.3827 4.4213 4.3118 -0.5864 0.5696  -0.5822 742  ILE A CB  
5638  C CG1 . ILE A 742  ? 4.4202 4.4562 4.3034 -0.5743 0.5887  -0.5760 742  ILE A CG1 
5639  C CG2 . ILE A 742  ? 4.3844 4.4298 4.3763 -0.5883 0.5793  -0.5103 742  ILE A CG2 
5640  C CD1 . ILE A 742  ? 4.4285 4.4839 4.3854 -0.5655 0.5472  -0.5304 742  ILE A CD1 
5641  N N   . SER A 743  ? 4.3624 4.4001 4.2580 -0.6052 0.5417  -0.7074 743  SER A N   
5642  C CA  . SER A 743  ? 4.3632 4.4056 4.3071 -0.6097 0.4996  -0.7287 743  SER A CA  
5643  C C   . SER A 743  ? 4.3577 4.4082 4.2540 -0.6084 0.4837  -0.8101 743  SER A C   
5644  O O   . SER A 743  ? 4.3562 4.4137 4.2299 -0.6022 0.4606  -0.8502 743  SER A O   
5645  C CB  . SER A 743  ? 4.3757 4.4207 4.4182 -0.6072 0.4260  -0.7032 743  SER A CB  
5646  O OG  . SER A 743  ? 4.3843 4.4348 4.4307 -0.5992 0.3817  -0.7363 743  SER A OG  
5647  N N   . GLY A 750  ? 2.9594 2.9208 3.3561 -0.6066 0.0232  -0.7847 750  GLY A N   
5648  C CA  . GLY A 750  ? 2.9999 2.9662 3.3899 -0.5979 -0.0082 -0.8200 750  GLY A CA  
5649  C C   . GLY A 750  ? 3.0220 2.9942 3.4512 -0.6086 -0.0117 -0.7641 750  GLY A C   
5650  O O   . GLY A 750  ? 3.0144 2.9839 3.4656 -0.6049 -0.0598 -0.7818 750  GLY A O   
5651  N N   . ARG A 751  ? 3.7452 3.7286 4.1832 -0.6209 0.0388  -0.6973 751  ARG A N   
5652  C CA  . ARG A 751  ? 3.7599 3.7566 4.2340 -0.6296 0.0420  -0.6391 751  ARG A CA  
5653  C C   . ARG A 751  ? 3.8750 3.8960 4.2882 -0.6230 0.1103  -0.6324 751  ARG A C   
5654  O O   . ARG A 751  ? 3.8926 3.9214 4.2708 -0.6252 0.1760  -0.6054 751  ARG A O   
5655  C CB  . ARG A 751  ? 3.6610 3.6568 4.1955 -0.6474 0.0456  -0.5621 751  ARG A CB  
5656  C CG  . ARG A 751  ? 3.5560 3.5251 4.1628 -0.6591 -0.0293 -0.5510 751  ARG A CG  
5657  C CD  . ARG A 751  ? 3.4133 3.3872 4.0749 -0.6796 -0.0201 -0.4724 751  ARG A CD  
5658  N NE  . ARG A 751  ? 3.3258 3.2680 4.0499 -0.6933 -0.0909 -0.4622 751  ARG A NE  
5659  C CZ  . ARG A 751  ? 3.2694 3.2009 4.0497 -0.7050 -0.1539 -0.4471 751  ARG A CZ  
5660  N NH1 . ARG A 751  ? 3.2633 3.2189 4.0473 -0.7034 -0.1544 -0.4407 751  ARG A NH1 
5661  N NH2 . ARG A 751  ? 3.2445 3.1398 4.0748 -0.7188 -0.2168 -0.4385 751  ARG A NH2 
5662  N N   . LEU A 752  ? 5.1275 5.1582 5.5266 -0.6150 0.0942  -0.6561 752  LEU A N   
5663  C CA  . LEU A 752  ? 5.2066 5.2564 5.5522 -0.6085 0.1522  -0.6435 752  LEU A CA  
5664  C C   . LEU A 752  ? 5.1971 5.2598 5.5748 -0.6059 0.1141  -0.6327 752  LEU A C   
5665  O O   . LEU A 752  ? 5.1989 5.2569 5.5956 -0.6027 0.0546  -0.6758 752  LEU A O   
5666  C CB  . LEU A 752  ? 5.2924 5.3434 5.5471 -0.5983 0.1913  -0.7075 752  LEU A CB  
5667  C CG  . LEU A 752  ? 5.3738 5.4370 5.5633 -0.5916 0.2466  -0.7025 752  LEU A CG  
5668  C CD1 . LEU A 752  ? 5.4123 5.4756 5.5810 -0.5951 0.3172  -0.6424 752  LEU A CD1 
5669  C CD2 . LEU A 752  ? 5.4160 5.4811 5.5226 -0.5851 0.2665  -0.7749 752  LEU A CD2 
5670  N N   . HIS A 753  ? 5.3758 5.4565 5.7582 -0.6060 0.1487  -0.5762 753  HIS A N   
5671  C CA  . HIS A 753  ? 5.3248 5.4238 5.7450 -0.6046 0.1138  -0.5563 753  HIS A CA  
5672  C C   . HIS A 753  ? 5.2198 5.3401 5.6102 -0.5964 0.1723  -0.5092 753  HIS A C   
5673  O O   . HIS A 753  ? 5.1949 5.3304 5.6256 -0.6015 0.1868  -0.4448 753  HIS A O   
5674  C CB  . HIS A 753  ? 5.3770 5.4767 5.8921 -0.6202 0.0506  -0.5188 753  HIS A CB  
5675  C CG  . HIS A 753  ? 5.4289 5.5064 5.9762 -0.6327 0.0373  -0.5100 753  HIS A CG  
5676  N ND1 . HIS A 753  ? 5.4576 5.5391 6.0012 -0.6382 0.0901  -0.4628 753  HIS A ND1 
5677  C CD2 . HIS A 753  ? 5.4410 5.4915 6.0222 -0.6393 -0.0224 -0.5418 753  HIS A CD2 
5678  C CE1 . HIS A 753  ? 5.4535 5.5137 6.0310 -0.6495 0.0617  -0.4638 753  HIS A CE1 
5679  N NE2 . HIS A 753  ? 5.4447 5.4839 6.0426 -0.6494 -0.0047 -0.5111 753  HIS A NE2 
5680  N N   . MET A 754  ? 3.5977 3.7196 3.9154 -0.5830 0.2045  -0.5424 754  MET A N   
5681  C CA  . MET A 754  ? 3.5315 3.6662 3.8080 -0.5716 0.2609  -0.5041 754  MET A CA  
5682  C C   . MET A 754  ? 3.4560 3.6203 3.7993 -0.5710 0.2298  -0.4515 754  MET A C   
5683  O O   . MET A 754  ? 3.4276 3.6008 3.8388 -0.5806 0.1626  -0.4558 754  MET A O   
5684  C CB  . MET A 754  ? 3.5260 3.6556 3.7176 -0.5593 0.2847  -0.5543 754  MET A CB  
5685  C CG  . MET A 754  ? 3.5137 3.6218 3.6365 -0.5616 0.3078  -0.6165 754  MET A CG  
5686  S SD  . MET A 754  ? 3.2409 3.3518 3.2809 -0.5516 0.3146  -0.6781 754  MET A SD  
5687  C CE  . MET A 754  ? 2.4818 2.6096 2.5285 -0.5389 0.3290  -0.6195 754  MET A CE  
5688  N N   . LYS A 755  ? 3.4150 3.5948 3.7377 -0.5595 0.2784  -0.4023 755  LYS A N   
5689  C CA  . LYS A 755  ? 3.3804 3.5965 3.7563 -0.5553 0.2568  -0.3522 755  LYS A CA  
5690  C C   . LYS A 755  ? 3.4567 3.6833 3.7831 -0.5353 0.3222  -0.3103 755  LYS A C   
5691  O O   . LYS A 755  ? 3.4653 3.6676 3.7239 -0.5278 0.3847  -0.3115 755  LYS A O   
5692  C CB  . LYS A 755  ? 3.3024 3.5388 3.7735 -0.5728 0.2204  -0.3017 755  LYS A CB  
5693  C CG  . LYS A 755  ? 3.2297 3.4612 3.7671 -0.5917 0.1397  -0.3293 755  LYS A CG  
5694  C CD  . LYS A 755  ? 3.2122 3.4513 3.7474 -0.5864 0.0929  -0.3720 755  LYS A CD  
5695  C CE  . LYS A 755  ? 3.2154 3.4977 3.7773 -0.5790 0.0885  -0.3278 755  LYS A CE  
5696  N NZ  . LYS A 755  ? 3.2045 3.4974 3.7717 -0.5762 0.0375  -0.3679 755  LYS A NZ  
5697  N N   . THR A 756  ? 3.1505 3.4130 3.5100 -0.5262 0.3061  -0.2740 756  THR A N   
5698  C CA  . THR A 756  ? 3.2497 3.5287 3.5779 -0.5045 0.3599  -0.2241 756  THR A CA  
5699  C C   . THR A 756  ? 3.3180 3.6506 3.7240 -0.5035 0.3198  -0.1768 756  THR A C   
5700  O O   . THR A 756  ? 3.3457 3.6969 3.7534 -0.4962 0.2899  -0.1911 756  THR A O   
5701  C CB  . THR A 756  ? 3.2558 3.5120 3.4867 -0.4841 0.3984  -0.2563 756  THR A CB  
5702  O OG1 . THR A 756  ? 3.2434 3.4534 3.3986 -0.4875 0.4412  -0.2961 756  THR A OG1 
5703  C CG2 . THR A 756  ? 3.2417 3.5142 3.4449 -0.4585 0.4456  -0.2027 756  THR A CG2 
5704  N N   . LEU A 757  ? 2.5290 2.8901 2.9992 -0.5122 0.3190  -0.1207 757  LEU A N   
5705  C CA  . LEU A 757  ? 2.5889 3.0051 3.1476 -0.5211 0.2700  -0.0782 757  LEU A CA  
5706  C C   . LEU A 757  ? 2.6749 3.1325 3.2241 -0.4967 0.2792  -0.0500 757  LEU A C   
5707  O O   . LEU A 757  ? 2.6963 3.1441 3.1758 -0.4693 0.3367  -0.0404 757  LEU A O   
5708  C CB  . LEU A 757  ? 2.6127 3.0541 3.2367 -0.5370 0.2731  -0.0216 757  LEU A CB  
5709  C CG  . LEU A 757  ? 2.6420 3.1392 3.3668 -0.5573 0.2172  0.0227  757  LEU A CG  
5710  C CD1 . LEU A 757  ? 2.6115 3.0890 3.3910 -0.5896 0.1452  -0.0102 757  LEU A CD1 
5711  C CD2 . LEU A 757  ? 2.6536 3.1872 3.4171 -0.5609 0.2477  0.0898  757  LEU A CD2 
5712  N N   . LEU A 758  ? 4.0864 4.5882 4.7047 -0.5075 0.2200  -0.0386 758  LEU A N   
5713  C CA  . LEU A 758  ? 4.1735 4.7291 4.8039 -0.4883 0.2177  -0.0045 758  LEU A CA  
5714  C C   . LEU A 758  ? 4.3077 4.9030 5.0221 -0.5123 0.1397  -0.0052 758  LEU A C   
5715  O O   . LEU A 758  ? 4.3110 4.8907 5.0169 -0.5175 0.0990  -0.0557 758  LEU A O   
5716  C CB  . LEU A 758  ? 4.0954 4.6290 4.6386 -0.4597 0.2466  -0.0380 758  LEU A CB  
5717  C CG  . LEU A 758  ? 3.9776 4.5508 4.4963 -0.4264 0.2791  0.0039  758  LEU A CG  
5718  C CD1 . LEU A 758  ? 3.9459 4.4989 4.3923 -0.4064 0.2843  -0.0374 758  LEU A CD1 
5719  C CD2 . LEU A 758  ? 3.9366 4.5876 4.5453 -0.4324 0.2381  0.0537  758  LEU A CD2 
5720  N N   . PRO A 759  ? 5.0155 5.6628 5.8103 -0.5287 0.1180  0.0498  759  PRO A N   
5721  C CA  . PRO A 759  ? 5.0901 5.7772 5.9670 -0.5557 0.0440  0.0550  759  PRO A CA  
5722  C C   . PRO A 759  ? 5.2090 5.9328 6.0783 -0.5395 0.0229  0.0449  759  PRO A C   
5723  O O   . PRO A 759  ? 5.2375 6.0085 6.1739 -0.5582 -0.0315 0.0597  759  PRO A O   
5724  C CB  . PRO A 759  ? 5.0592 5.8052 6.0061 -0.5690 0.0460  0.1269  759  PRO A CB  
5725  C CG  . PRO A 759  ? 5.0339 5.7500 5.9466 -0.5610 0.1055  0.1437  759  PRO A CG  
5726  C CD  . PRO A 759  ? 5.0425 5.7127 5.8550 -0.5263 0.1611  0.1083  759  PRO A CD  
5727  N N   . VAL A 760  ? 4.2158 5.4096 4.9223 0.4751  0.0242  0.1718  760  VAL A N   
5728  C CA  . VAL A 760  ? 4.2842 5.5501 4.9874 0.4659  0.0305  0.1907  760  VAL A CA  
5729  C C   . VAL A 760  ? 4.1459 5.4169 4.8381 0.4631  0.0283  0.2077  760  VAL A C   
5730  O O   . VAL A 760  ? 4.1649 5.4922 4.8493 0.4546  0.0322  0.2203  760  VAL A O   
5731  C CB  . VAL A 760  ? 4.5490 5.8624 5.2376 0.4587  0.0363  0.1631  760  VAL A CB  
5732  C CG1 . VAL A 760  ? 4.6426 6.0325 5.3324 0.4489  0.0434  0.1855  760  VAL A CG1 
5733  C CG2 . VAL A 760  ? 4.6262 5.9218 5.3243 0.4633  0.0372  0.1386  760  VAL A CG2 
5734  N N   . SER A 761  ? 3.5224 4.7343 4.2143 0.4700  0.0219  0.2079  761  SER A N   
5735  C CA  . SER A 761  ? 3.3341 4.5418 4.0176 0.4689  0.0191  0.2228  761  SER A CA  
5736  C C   . SER A 761  ? 3.1367 4.3515 3.7928 0.4633  0.0185  0.1965  761  SER A C   
5737  O O   . SER A 761  ? 3.1122 4.3416 3.7590 0.4597  0.0177  0.2084  761  SER A O   
5738  C CB  . SER A 761  ? 3.3710 4.6307 4.0658 0.4642  0.0222  0.2615  761  SER A CB  
5739  O OG  . SER A 761  ? 3.3471 4.5997 4.0377 0.4644  0.0191  0.2779  761  SER A OG  
5740  N N   . LYS A 762  ? 2.3541 3.5578 2.9982 0.4627  0.0184  0.1609  762  LYS A N   
5741  C CA  . LYS A 762  ? 2.1223 3.3349 2.7404 0.4568  0.0174  0.1337  762  LYS A CA  
5742  C C   . LYS A 762  ? 1.9875 3.1404 2.5935 0.4606  0.0101  0.1195  762  LYS A C   
5743  O O   . LYS A 762  ? 1.9847 3.0803 2.5966 0.4677  0.0053  0.1075  762  LYS A O   
5744  C CB  . LYS A 762  ? 2.0273 3.2555 2.6376 0.4543  0.0200  0.1002  762  LYS A CB  
5745  C CG  . LYS A 762  ? 1.9273 3.2302 2.5378 0.4463  0.0283  0.1056  762  LYS A CG  
5746  C CD  . LYS A 762  ? 1.8440 3.1570 2.4464 0.4447  0.0305  0.0681  762  LYS A CD  
5747  C CE  . LYS A 762  ? 1.7956 3.1694 2.4075 0.4400  0.0390  0.0738  762  LYS A CE  
5748  N NZ  . LYS A 762  ? 1.7829 3.1486 2.3962 0.4428  0.0402  0.0391  762  LYS A NZ  
5749  N N   . PRO A 763  ? 2.5330 3.7003 3.1216 0.4551  0.0090  0.1209  763  PRO A N   
5750  C CA  . PRO A 763  ? 2.4344 3.5524 3.0084 0.4567  0.0023  0.1066  763  PRO A CA  
5751  C C   . PRO A 763  ? 2.3449 3.4321 2.9033 0.4562  -0.0020 0.0661  763  PRO A C   
5752  O O   . PRO A 763  ? 2.3647 3.4789 2.9036 0.4490  -0.0016 0.0466  763  PRO A O   
5753  C CB  . PRO A 763  ? 2.4089 3.5674 2.9681 0.4489  0.0037  0.1176  763  PRO A CB  
5754  C CG  . PRO A 763  ? 2.4340 3.6504 3.0069 0.4459  0.0099  0.1490  763  PRO A CG  
5755  C CD  . PRO A 763  ? 2.5026 3.7353 3.0862 0.4469  0.0139  0.1409  763  PRO A CD  
5756  N N   . GLU A 764  ? 2.2790 3.3105 2.8463 0.4634  -0.0065 0.0539  764  GLU A N   
5757  C CA  . GLU A 764  ? 2.1763 3.1675 2.7297 0.4635  -0.0128 0.0171  764  GLU A CA  
5758  C C   . GLU A 764  ? 2.0449 2.9706 2.5936 0.4672  -0.0206 0.0138  764  GLU A C   
5759  O O   . GLU A 764  ? 2.0106 2.9143 2.5716 0.4720  -0.0209 0.0379  764  GLU A O   
5760  C CB  . GLU A 764  ? 2.1969 3.1787 2.7622 0.4676  -0.0124 -0.0008 764  GLU A CB  
5761  C CG  . GLU A 764  ? 2.1908 3.1439 2.7807 0.4757  -0.0122 0.0176  764  GLU A CG  
5762  C CD  . GLU A 764  ? 2.2261 3.1997 2.8303 0.4777  -0.0082 0.0090  764  GLU A CD  
5763  O OE1 . GLU A 764  ? 2.2403 3.2123 2.8363 0.4763  -0.0100 -0.0228 764  GLU A OE1 
5764  O OE2 . GLU A 764  ? 2.2331 3.2253 2.8573 0.4806  -0.0035 0.0340  764  GLU A OE2 
5765  N N   . ILE A 765  ? 1.8481 2.7429 2.3791 0.4646  -0.0273 -0.0169 765  ILE A N   
5766  C CA  . ILE A 765  ? 1.7706 2.6140 2.2905 0.4647  -0.0346 -0.0214 765  ILE A CA  
5767  C C   . ILE A 765  ? 1.7846 2.5912 2.2898 0.4627  -0.0427 -0.0581 765  ILE A C   
5768  O O   . ILE A 765  ? 1.8298 2.6620 2.3189 0.4564  -0.0435 -0.0787 765  ILE A O   
5769  C CB  . ILE A 765  ? 1.6919 2.5646 2.1967 0.4584  -0.0331 -0.0096 765  ILE A CB  
5770  C CG1 . ILE A 765  ? 1.6705 2.4917 2.1614 0.4573  -0.0408 -0.0180 765  ILE A CG1 
5771  C CG2 . ILE A 765  ? 1.6955 2.6181 2.1833 0.4501  -0.0309 -0.0262 765  ILE A CG2 
5772  C CD1 . ILE A 765  ? 1.6390 2.4807 2.1235 0.4540  -0.0386 0.0036  765  ILE A CD1 
5773  N N   . ARG A 766  ? 1.9367 2.6826 2.4476 0.4676  -0.0494 -0.0666 766  ARG A N   
5774  C CA  . ARG A 766  ? 1.9289 2.6387 2.4300 0.4663  -0.0579 -0.1009 766  ARG A CA  
5775  C C   . ARG A 766  ? 1.9553 2.6341 2.4331 0.4602  -0.0662 -0.1162 766  ARG A C   
5776  O O   . ARG A 766  ? 1.9634 2.5870 2.4365 0.4606  -0.0755 -0.1341 766  ARG A O   
5777  C CB  . ARG A 766  ? 1.8913 2.5512 2.4097 0.4737  -0.0620 -0.1035 766  ARG A CB  
5778  C CG  . ARG A 766  ? 1.8632 2.5523 2.4055 0.4795  -0.0537 -0.0835 766  ARG A CG  
5779  C CD  . ARG A 766  ? 1.8903 2.6332 2.4328 0.4770  -0.0483 -0.0967 766  ARG A CD  
5780  N NE  . ARG A 766  ? 1.9254 2.6954 2.4910 0.4820  -0.0411 -0.0814 766  ARG A NE  
5781  C CZ  . ARG A 766  ? 1.9996 2.7774 2.5751 0.4843  -0.0403 -0.0992 766  ARG A CZ  
5782  N NH1 . ARG A 766  ? 2.0638 2.8233 2.6291 0.4827  -0.0467 -0.1333 766  ARG A NH1 
5783  N NH2 . ARG A 766  ? 1.9972 2.8018 2.5937 0.4882  -0.0334 -0.0827 766  ARG A NH2 
5784  N N   . SER A 767  ? 1.5557 2.2704 2.0188 0.4539  -0.0633 -0.1088 767  SER A N   
5785  C CA  . SER A 767  ? 1.6190 2.3087 2.0593 0.4472  -0.0709 -0.1219 767  SER A CA  
5786  C C   . SER A 767  ? 1.6467 2.3878 2.0693 0.4389  -0.0679 -0.1226 767  SER A C   
5787  O O   . SER A 767  ? 1.6321 2.4231 2.0599 0.4385  -0.0593 -0.0997 767  SER A O   
5788  C CB  . SER A 767  ? 1.6391 2.2861 2.0814 0.4494  -0.0734 -0.1043 767  SER A CB  
5789  O OG  . SER A 767  ? 1.6198 2.2810 2.0831 0.4562  -0.0655 -0.0735 767  SER A OG  
5790  N N   . TYR A 768  ? 2.7543 3.4826 3.1559 0.4320  -0.0758 -0.1492 768  TYR A N   
5791  C CA  . TYR A 768  ? 2.8030 3.5737 3.1851 0.4233  -0.0746 -0.1526 768  TYR A CA  
5792  C C   . TYR A 768  ? 2.7102 3.4647 3.0818 0.4196  -0.0769 -0.1380 768  TYR A C   
5793  O O   . TYR A 768  ? 2.7119 3.4153 3.0866 0.4225  -0.0816 -0.1347 768  TYR A O   
5794  C CB  . TYR A 768  ? 2.9549 3.7185 3.3197 0.4174  -0.0827 -0.1886 768  TYR A CB  
5795  C CG  . TYR A 768  ? 3.0531 3.8570 3.3959 0.4076  -0.0827 -0.1950 768  TYR A CG  
5796  C CD1 . TYR A 768  ? 3.1188 3.9851 3.4606 0.4050  -0.0750 -0.1946 768  TYR A CD1 
5797  C CD2 . TYR A 768  ? 3.0953 3.8750 3.4178 0.4003  -0.0908 -0.2020 768  TYR A CD2 
5798  C CE1 . TYR A 768  ? 3.1698 4.0727 3.4910 0.3956  -0.0755 -0.2006 768  TYR A CE1 
5799  C CE2 . TYR A 768  ? 3.1483 3.9643 3.4507 0.3910  -0.0914 -0.2078 768  TYR A CE2 
5800  C CZ  . TYR A 768  ? 3.1903 4.0674 3.4921 0.3888  -0.0838 -0.2070 768  TYR A CZ  
5801  O OH  . TYR A 768  ? 3.2262 4.1392 3.5075 0.3791  -0.0846 -0.2126 768  TYR A OH  
5802  N N   . PHE A 769  ? 1.7975 2.5960 2.1566 0.4129  -0.0736 -0.1297 769  PHE A N   
5803  C CA  . PHE A 769  ? 1.7288 2.5211 2.0797 0.4095  -0.0744 -0.1134 769  PHE A CA  
5804  C C   . PHE A 769  ? 1.7369 2.5584 2.0640 0.3989  -0.0771 -0.1241 769  PHE A C   
5805  O O   . PHE A 769  ? 1.7553 2.6309 2.0812 0.3957  -0.0704 -0.1083 769  PHE A O   
5806  C CB  . PHE A 769  ? 1.6678 2.4953 2.0360 0.4142  -0.0644 -0.0778 769  PHE A CB  
5807  C CG  . PHE A 769  ? 1.6159 2.4091 2.0063 0.4241  -0.0624 -0.0609 769  PHE A CG  
5808  C CD1 . PHE A 769  ? 1.8260 2.5700 2.2161 0.4260  -0.0666 -0.0561 769  PHE A CD1 
5809  C CD2 . PHE A 769  ? 1.8080 2.6208 2.2196 0.4309  -0.0559 -0.0483 769  PHE A CD2 
5810  C CE1 . PHE A 769  ? 1.5871 2.3008 1.9974 0.4349  -0.0646 -0.0401 769  PHE A CE1 
5811  C CE2 . PHE A 769  ? 1.7339 2.5159 2.1661 0.4398  -0.0542 -0.0317 769  PHE A CE2 
5812  C CZ  . PHE A 769  ? 1.7945 2.5268 2.2260 0.4419  -0.0586 -0.0278 769  PHE A CZ  
5813  N N   . PRO A 770  ? 1.8290 2.6146 2.1372 0.3928  -0.0875 -0.1499 770  PRO A N   
5814  C CA  . PRO A 770  ? 1.9008 2.7083 2.1849 0.3822  -0.0922 -0.1668 770  PRO A CA  
5815  C C   . PRO A 770  ? 1.9584 2.8169 2.2356 0.3766  -0.0863 -0.1456 770  PRO A C   
5816  O O   . PRO A 770  ? 1.9544 2.8170 2.2410 0.3796  -0.0814 -0.1187 770  PRO A O   
5817  C CB  . PRO A 770  ? 1.9012 2.6505 2.1704 0.3775  -0.1042 -0.1841 770  PRO A CB  
5818  C CG  . PRO A 770  ? 1.8901 2.5879 2.1743 0.3856  -0.1073 -0.1900 770  PRO A CG  
5819  C CD  . PRO A 770  ? 1.8401 2.5580 2.1492 0.3955  -0.0962 -0.1633 770  PRO A CD  
5820  N N   . GLU A 771  ? 2.2543 3.1522 2.5154 0.3686  -0.0869 -0.1581 771  GLU A N   
5821  C CA  . GLU A 771  ? 2.3008 3.2441 2.5523 0.3618  -0.0832 -0.1412 771  GLU A CA  
5822  C C   . GLU A 771  ? 2.2583 3.1672 2.4987 0.3575  -0.0896 -0.1378 771  GLU A C   
5823  O O   . GLU A 771  ? 2.2576 3.1207 2.4851 0.3540  -0.0995 -0.1603 771  GLU A O   
5824  C CB  . GLU A 771  ? 2.4272 3.4088 2.6597 0.3527  -0.0852 -0.1609 771  GLU A CB  
5825  C CG  . GLU A 771  ? 2.5109 3.5405 2.7314 0.3443  -0.0823 -0.1452 771  GLU A CG  
5826  C CD  . GLU A 771  ? 2.6160 3.6752 2.8145 0.3343  -0.0862 -0.1685 771  GLU A CD  
5827  O OE1 . GLU A 771  ? 2.6315 3.7488 2.8271 0.3298  -0.0798 -0.1573 771  GLU A OE1 
5828  O OE2 . GLU A 771  ? 2.6743 3.6985 2.8586 0.3306  -0.0960 -0.1979 771  GLU A OE2 
5829  N N   . SER A 772  ? 1.9819 2.9131 2.2280 0.3578  -0.0840 -0.1095 772  SER A N   
5830  C CA  . SER A 772  ? 1.9438 2.8466 2.1826 0.3546  -0.0881 -0.1025 772  SER A CA  
5831  C C   . SER A 772  ? 1.9263 2.8374 2.1383 0.3420  -0.0955 -0.1180 772  SER A C   
5832  O O   . SER A 772  ? 1.9550 2.8770 2.1531 0.3364  -0.0999 -0.1409 772  SER A O   
5833  C CB  . SER A 772  ? 1.9145 2.8425 2.1702 0.3596  -0.0794 -0.0674 772  SER A CB  
5834  O OG  . SER A 772  ? 1.8929 2.8172 2.1733 0.3707  -0.0729 -0.0529 772  SER A OG  
5835  N N   . TRP A 773  ? 1.8779 2.7835 2.0830 0.3376  -0.0971 -0.1064 773  TRP A N   
5836  C CA  . TRP A 773  ? 1.9261 2.8408 2.1059 0.3250  -0.1042 -0.1188 773  TRP A CA  
5837  C C   . TRP A 773  ? 1.9652 2.8820 2.1420 0.3213  -0.1037 -0.1003 773  TRP A C   
5838  O O   . TRP A 773  ? 1.9758 2.8916 2.1711 0.3289  -0.0969 -0.0764 773  TRP A O   
5839  C CB  . TRP A 773  ? 1.9495 2.8168 2.1118 0.3194  -0.1164 -0.1515 773  TRP A CB  
5840  C CG  . TRP A 773  ? 1.9385 2.7446 2.1081 0.3247  -0.1203 -0.1548 773  TRP A CG  
5841  C CD1 . TRP A 773  ? 1.9279 2.7058 2.1154 0.3350  -0.1181 -0.1557 773  TRP A CD1 
5842  C CD2 . TRP A 773  ? 1.9606 2.7256 2.1192 0.3193  -0.1274 -0.1576 773  TRP A CD2 
5843  N NE1 . TRP A 773  ? 1.9219 2.6432 2.1099 0.3362  -0.1235 -0.1590 773  TRP A NE1 
5844  C CE2 . TRP A 773  ? 1.9419 2.6546 2.1120 0.3265  -0.1292 -0.1604 773  TRP A CE2 
5845  C CE3 . TRP A 773  ? 1.9728 2.7410 2.1125 0.3084  -0.1325 -0.1580 773  TRP A CE3 
5846  C CZ2 . TRP A 773  ? 1.9534 2.6173 2.1162 0.3229  -0.1357 -0.1637 773  TRP A CZ2 
5847  C CZ3 . TRP A 773  ? 1.9787 2.6988 2.1117 0.3049  -0.1388 -0.1613 773  TRP A CZ3 
5848  C CH2 . TRP A 773  ? 1.9711 2.6401 2.1152 0.3120  -0.1403 -0.1642 773  TRP A CH2 
5849  N N   . LEU A 774  ? 2.7185 3.6380 2.8722 0.3095  -0.1110 -0.1120 774  LEU A N   
5850  C CA  . LEU A 774  ? 2.7289 3.6607 2.8776 0.3041  -0.1104 -0.0954 774  LEU A CA  
5851  C C   . LEU A 774  ? 2.6783 3.6653 2.8428 0.3080  -0.0998 -0.0643 774  LEU A C   
5852  O O   . LEU A 774  ? 2.6231 3.6105 2.7993 0.3116  -0.0954 -0.0426 774  LEU A O   
5853  C CB  . LEU A 774  ? 2.7506 3.6298 2.9030 0.3067  -0.1130 -0.0931 774  LEU A CB  
5854  C CG  . LEU A 774  ? 2.8307 3.6776 2.9585 0.2948  -0.1244 -0.1126 774  LEU A CG  
5855  C CD1 . LEU A 774  ? 2.8222 3.6177 2.9546 0.2974  -0.1262 -0.1100 774  LEU A CD1 
5856  C CD2 . LEU A 774  ? 2.8666 3.7549 2.9800 0.2842  -0.1251 -0.1053 774  LEU A CD2 
5857  N N   . TRP A 775  ? 1.7687 2.8027 1.9335 0.3070  -0.0960 -0.0627 775  TRP A N   
5858  C CA  . TRP A 775  ? 1.7176 2.8041 1.8996 0.3112  -0.0863 -0.0335 775  TRP A CA  
5859  C C   . TRP A 775  ? 1.7477 2.8784 1.9180 0.3013  -0.0866 -0.0220 775  TRP A C   
5860  O O   . TRP A 775  ? 1.7243 2.9008 1.9073 0.3032  -0.0798 0.0033  775  TRP A O   
5861  C CB  . TRP A 775  ? 1.6889 2.8040 1.8774 0.3145  -0.0819 -0.0370 775  TRP A CB  
5862  C CG  . TRP A 775  ? 1.6672 2.8319 1.8752 0.3193  -0.0723 -0.0069 775  TRP A CG  
5863  C CD1 . TRP A 775  ? 1.7088 2.9325 1.9117 0.3126  -0.0694 0.0042  775  TRP A CD1 
5864  C CD2 . TRP A 775  ? 1.6298 2.7901 1.8657 0.3313  -0.0651 0.0166  775  TRP A CD2 
5865  N NE1 . TRP A 775  ? 1.6798 2.9368 1.9057 0.3193  -0.0611 0.0338  775  TRP A NE1 
5866  C CE2 . TRP A 775  ? 1.6242 2.8429 1.8710 0.3310  -0.0584 0.0417  775  TRP A CE2 
5867  C CE3 . TRP A 775  ? 1.6016 2.7142 1.8541 0.3419  -0.0642 0.0190  775  TRP A CE3 
5868  C CZ2 . TRP A 775  ? 1.5810 2.8112 1.8551 0.3409  -0.0513 0.0692  775  TRP A CZ2 
5869  C CZ3 . TRP A 775  ? 1.5662 2.6906 1.8457 0.3520  -0.0566 0.0459  775  TRP A CZ3 
5870  C CH2 . TRP A 775  ? 1.5588 2.7412 1.8490 0.3515  -0.0506 0.0706  775  TRP A CH2 
5871  N N   . GLU A 776  ? 2.6002 3.7164 2.7466 0.2906  -0.0953 -0.0404 776  GLU A N   
5872  C CA  . GLU A 776  ? 2.6661 3.8194 2.7989 0.2799  -0.0971 -0.0322 776  GLU A CA  
5873  C C   . GLU A 776  ? 2.6423 3.8063 2.7912 0.2837  -0.0918 -0.0027 776  GLU A C   
5874  O O   . GLU A 776  ? 2.6057 3.7325 2.7689 0.2920  -0.0899 0.0037  776  GLU A O   
5875  C CB  . GLU A 776  ? 2.7680 3.8927 2.8732 0.2682  -0.1085 -0.0589 776  GLU A CB  
5876  C CG  . GLU A 776  ? 2.8237 3.8822 2.9281 0.2712  -0.1140 -0.0728 776  GLU A CG  
5877  C CD  . GLU A 776  ? 2.9407 3.9686 3.0177 0.2594  -0.1266 -0.1020 776  GLU A CD  
5878  O OE1 . GLU A 776  ? 2.9622 3.9406 3.0360 0.2614  -0.1326 -0.1224 776  GLU A OE1 
5879  O OE2 . GLU A 776  ? 3.0064 4.0595 3.0654 0.2479  -0.1311 -0.1043 776  GLU A OE2 
5880  N N   . VAL A 777  ? 1.4682 2.6829 1.6155 0.2777  -0.0896 0.0149  777  VAL A N   
5881  C CA  . VAL A 777  ? 1.4296 2.6552 1.5904 0.2800  -0.0859 0.0406  777  VAL A CA  
5882  C C   . VAL A 777  ? 1.3225 2.5320 1.4626 0.2692  -0.0934 0.0297  777  VAL A C   
5883  O O   . VAL A 777  ? 1.3341 2.5322 1.4493 0.2591  -0.1015 0.0048  777  VAL A O   
5884  C CB  . VAL A 777  ? 1.3119 2.6009 1.4862 0.2804  -0.0795 0.0690  777  VAL A CB  
5885  C CG1 . VAL A 777  ? 1.3326 2.6355 1.5187 0.2811  -0.0771 0.0930  777  VAL A CG1 
5886  C CG2 . VAL A 777  ? 1.3454 2.6445 1.5431 0.2918  -0.0720 0.0830  777  VAL A CG2 
5887  N N   . HIS A 778  ? 1.8340 3.0411 1.9844 0.2710  -0.0911 0.0470  778  HIS A N   
5888  C CA  . HIS A 778  ? 1.9427 3.1384 2.0738 0.2599  -0.0979 0.0379  778  HIS A CA  
5889  C C   . HIS A 778  ? 2.0819 3.3049 2.2241 0.2593  -0.0941 0.0625  778  HIS A C   
5890  O O   . HIS A 778  ? 2.0429 3.2765 2.2117 0.2702  -0.0862 0.0863  778  HIS A O   
5891  C CB  . HIS A 778  ? 1.9182 3.0494 2.0397 0.2597  -0.1036 0.0162  778  HIS A CB  
5892  C CG  . HIS A 778  ? 1.9279 3.0345 2.0251 0.2519  -0.1129 -0.0149 778  HIS A CG  
5893  N ND1 . HIS A 778  ? 1.9620 3.0707 2.0321 0.2372  -0.1223 -0.0318 778  HIS A ND1 
5894  C CD2 . HIS A 778  ? 1.9125 2.9914 2.0094 0.2567  -0.1146 -0.0324 778  HIS A CD2 
5895  C CE1 . HIS A 778  ? 1.9777 3.0606 2.0322 0.2337  -0.1297 -0.0585 778  HIS A CE1 
5896  N NE2 . HIS A 778  ? 1.9474 3.0122 2.0181 0.2455  -0.1250 -0.0596 778  HIS A NE2 
5897  N N   . LEU A 779  ? 2.1733 3.4075 2.2951 0.2464  -0.1003 0.0561  779  LEU A N   
5898  C CA  . LEU A 779  ? 2.3009 3.5555 2.4299 0.2441  -0.0982 0.0749  779  LEU A CA  
5899  C C   . LEU A 779  ? 2.4037 3.6093 2.5257 0.2420  -0.1017 0.0631  779  LEU A C   
5900  O O   . LEU A 779  ? 2.4696 3.6527 2.5655 0.2303  -0.1107 0.0408  779  LEU A O   
5901  C CB  . LEU A 779  ? 2.3593 3.6591 2.4696 0.2300  -0.1031 0.0758  779  LEU A CB  
5902  C CG  . LEU A 779  ? 2.3645 3.6918 2.4815 0.2262  -0.1015 0.0954  779  LEU A CG  
5903  C CD1 . LEU A 779  ? 2.3262 3.6743 2.4779 0.2401  -0.0915 0.1253  779  LEU A CD1 
5904  C CD2 . LEU A 779  ? 2.4109 3.7860 2.5099 0.2123  -0.1064 0.0972  779  LEU A CD2 
5905  N N   . VAL A 780  ? 2.5915 3.7805 2.7365 0.2528  -0.0950 0.0778  780  VAL A N   
5906  C CA  . VAL A 780  ? 2.6746 3.8172 2.8141 0.2511  -0.0973 0.0674  780  VAL A CA  
5907  C C   . VAL A 780  ? 2.6375 3.7974 2.7911 0.2523  -0.0924 0.0869  780  VAL A C   
5908  O O   . VAL A 780  ? 2.5810 3.7459 2.7627 0.2652  -0.0838 0.1066  780  VAL A O   
5909  C CB  . VAL A 780  ? 2.7298 3.8211 2.8806 0.2625  -0.0948 0.0598  780  VAL A CB  
5910  C CG1 . VAL A 780  ? 2.8009 3.8474 2.9471 0.2605  -0.0965 0.0514  780  VAL A CG1 
5911  C CG2 . VAL A 780  ? 2.7921 3.8611 2.9274 0.2603  -0.1008 0.0372  780  VAL A CG2 
5912  N N   . PRO A 781  ? 2.3705 3.5405 2.5050 0.2388  -0.0980 0.0814  781  PRO A N   
5913  C CA  . PRO A 781  ? 2.3617 3.5449 2.5065 0.2381  -0.0942 0.0960  781  PRO A CA  
5914  C C   . PRO A 781  ? 2.3523 3.4839 2.4982 0.2407  -0.0933 0.0867  781  PRO A C   
5915  O O   . PRO A 781  ? 2.3976 3.5142 2.5248 0.2291  -0.0987 0.0753  781  PRO A O   
5916  C CB  . PRO A 781  ? 2.4344 3.6425 2.5534 0.2206  -0.1023 0.0890  781  PRO A CB  
5917  C CG  . PRO A 781  ? 2.4684 3.6907 2.5701 0.2147  -0.1082 0.0774  781  PRO A CG  
5918  C CD  . PRO A 781  ? 2.4400 3.6197 2.5438 0.2232  -0.1080 0.0635  781  PRO A CD  
5919  N N   . ARG A 782  ? 2.6796 3.7849 2.8466 0.2552  -0.0868 0.0915  782  ARG A N   
5920  C CA  . ARG A 782  ? 2.6813 3.7387 2.8522 0.2591  -0.0848 0.0846  782  ARG A CA  
5921  C C   . ARG A 782  ? 2.6549 3.6567 2.8026 0.2529  -0.0930 0.0572  782  ARG A C   
5922  O O   . ARG A 782  ? 2.6528 3.6114 2.8075 0.2598  -0.0907 0.0520  782  ARG A O   
5923  C CB  . ARG A 782  ? 2.7690 3.8365 2.9389 0.2526  -0.0834 0.0902  782  ARG A CB  
5924  C CG  . ARG A 782  ? 2.8315 3.9517 3.0266 0.2590  -0.0756 0.1172  782  ARG A CG  
5925  C CD  . ARG A 782  ? 2.9274 4.0538 3.1224 0.2531  -0.0740 0.1207  782  ARG A CD  
5926  N NE  . ARG A 782  ? 3.0354 4.1705 3.1997 0.2344  -0.0832 0.1076  782  ARG A NE  
5927  C CZ  . ARG A 782  ? 3.1033 4.2436 3.2602 0.2251  -0.0840 0.1069  782  ARG A CZ  
5928  N NH1 . ARG A 782  ? 3.1017 4.2400 3.2801 0.2332  -0.0755 0.1176  782  ARG A NH1 
5929  N NH2 . ARG A 782  ? 3.1605 4.3084 3.2888 0.2076  -0.0933 0.0950  782  ARG A NH2 
5930  N N   . ARG A 783  ? 2.4087 3.4105 2.5290 0.2398  -0.1029 0.0396  783  ARG A N   
5931  C CA  . ARG A 783  ? 2.3880 3.3381 2.4870 0.2339  -0.1120 0.0135  783  ARG A CA  
5932  C C   . ARG A 783  ? 2.3487 3.3104 2.4290 0.2266  -0.1201 -0.0008 783  ARG A C   
5933  O O   . ARG A 783  ? 2.3643 3.3663 2.4340 0.2178  -0.1230 0.0023  783  ARG A O   
5934  C CB  . ARG A 783  ? 2.4449 3.3639 2.5230 0.2206  -0.1189 -0.0003 783  ARG A CB  
5935  C CG  . ARG A 783  ? 2.4438 3.3303 2.5349 0.2269  -0.1129 0.0041  783  ARG A CG  
5936  C CD  . ARG A 783  ? 2.4998 3.3702 2.5702 0.2118  -0.1188 -0.0056 783  ARG A CD  
5937  N NE  . ARG A 783  ? 2.5023 3.3846 2.5903 0.2166  -0.1093 0.0105  783  ARG A NE  
5938  C CZ  . ARG A 783  ? 2.5288 3.4399 2.6116 0.2074  -0.1090 0.0171  783  ARG A CZ  
5939  N NH1 . ARG A 783  ? 2.5612 3.4914 2.6205 0.1922  -0.1182 0.0094  783  ARG A NH1 
5940  N NH2 . ARG A 783  ? 2.5065 3.4274 2.6080 0.2133  -0.0996 0.0310  783  ARG A NH2 
5941  N N   . LYS A 784  ? 1.8705 2.7969 1.9470 0.2303  -0.1238 -0.0167 784  LYS A N   
5942  C CA  . LYS A 784  ? 1.8455 2.7759 1.9041 0.2239  -0.1320 -0.0342 784  LYS A CA  
5943  C C   . LYS A 784  ? 1.8186 2.6954 1.8729 0.2273  -0.1372 -0.0545 784  LYS A C   
5944  O O   . LYS A 784  ? 1.7902 2.6511 1.8645 0.2406  -0.1306 -0.0485 784  LYS A O   
5945  C CB  . LYS A 784  ? 1.8091 2.7926 1.8802 0.2301  -0.1259 -0.0200 784  LYS A CB  
5946  C CG  . LYS A 784  ? 1.8260 2.8226 1.8770 0.2219  -0.1339 -0.0381 784  LYS A CG  
5947  C CD  . LYS A 784  ? 1.7866 2.8446 1.8454 0.2239  -0.1284 -0.0224 784  LYS A CD  
5948  C CE  . LYS A 784  ? 1.7853 2.8580 1.8199 0.2129  -0.1372 -0.0422 784  LYS A CE  
5949  N NZ  . LYS A 784  ? 1.7543 2.8870 1.7929 0.2127  -0.1326 -0.0290 784  LYS A NZ  
5950  N N   . GLN A 785  ? 2.3253 3.1736 2.3539 0.2147  -0.1497 -0.0784 785  GLN A N   
5951  C CA  . GLN A 785  ? 2.2998 3.0977 2.3223 0.2160  -0.1567 -0.0996 785  GLN A CA  
5952  C C   . GLN A 785  ? 2.2851 3.0968 2.2951 0.2121  -0.1635 -0.1159 785  GLN A C   
5953  O O   . GLN A 785  ? 2.2780 3.1191 2.2713 0.2011  -0.1687 -0.1201 785  GLN A O   
5954  C CB  . GLN A 785  ? 2.3506 3.1009 2.3536 0.2042  -0.1671 -0.1151 785  GLN A CB  
5955  C CG  . GLN A 785  ? 2.3972 3.0897 2.3963 0.2058  -0.1745 -0.1347 785  GLN A CG  
5956  C CD  . GLN A 785  ? 2.4618 3.1101 2.4418 0.1929  -0.1847 -0.1474 785  GLN A CD  
5957  O OE1 . GLN A 785  ? 2.4866 3.1482 2.4501 0.1799  -0.1896 -0.1477 785  GLN A OE1 
5958  N NE2 . GLN A 785  ? 2.4804 3.0765 2.4623 0.1959  -0.1884 -0.1576 785  GLN A NE2 
5959  N N   . LEU A 786  ? 2.0673 2.8590 2.0861 0.2211  -0.1631 -0.1251 786  LEU A N   
5960  C CA  . LEU A 786  ? 2.0940 2.8950 2.1025 0.2186  -0.1692 -0.1431 786  LEU A CA  
5961  C C   . LEU A 786  ? 2.1292 2.8789 2.1377 0.2225  -0.1756 -0.1638 786  LEU A C   
5962  O O   . LEU A 786  ? 2.1208 2.8633 2.1489 0.2356  -0.1686 -0.1587 786  LEU A O   
5963  C CB  . LEU A 786  ? 2.0309 2.8871 2.0542 0.2267  -0.1590 -0.1282 786  LEU A CB  
5964  C CG  . LEU A 786  ? 1.9342 2.8035 1.9871 0.2429  -0.1455 -0.1058 786  LEU A CG  
5965  C CD1 . LEU A 786  ? 1.8964 2.8213 1.9574 0.2467  -0.1387 -0.0952 786  LEU A CD1 
5966  C CD2 . LEU A 786  ? 1.8945 2.7687 1.9595 0.2456  -0.1386 -0.0832 786  LEU A CD2 
5967  N N   . GLN A 787  ? 2.6991 3.4127 2.6856 0.2108  -0.1896 -0.1869 787  GLN A N   
5968  C CA  . GLN A 787  ? 2.7115 3.3730 2.6968 0.2130  -0.1978 -0.2077 787  GLN A CA  
5969  C C   . GLN A 787  ? 2.6631 3.3385 2.6533 0.2193  -0.1978 -0.2204 787  GLN A C   
5970  O O   . GLN A 787  ? 2.6541 3.3761 2.6404 0.2173  -0.1953 -0.2191 787  GLN A O   
5971  C CB  . GLN A 787  ? 2.8056 3.4252 2.7662 0.1979  -0.2141 -0.2282 787  GLN A CB  
5972  C CG  . GLN A 787  ? 2.8842 3.5316 2.8222 0.1832  -0.2220 -0.2351 787  GLN A CG  
5973  C CD  . GLN A 787  ? 2.9777 3.5841 2.8926 0.1675  -0.2375 -0.2506 787  GLN A CD  
5974  O OE1 . GLN A 787  ? 3.0296 3.6410 2.9241 0.1552  -0.2489 -0.2657 787  GLN A OE1 
5975  N NE2 . GLN A 787  ? 2.9938 3.5595 2.9115 0.1674  -0.2382 -0.2468 787  GLN A NE2 
5976  N N   . PHE A 788  ? 2.7286 3.3639 2.7277 0.2267  -0.2005 -0.2324 788  PHE A N   
5977  C CA  . PHE A 788  ? 2.6759 3.3190 2.6823 0.2338  -0.2001 -0.2456 788  PHE A CA  
5978  C C   . PHE A 788  ? 2.6347 3.2247 2.6516 0.2412  -0.2039 -0.2571 788  PHE A C   
5979  O O   . PHE A 788  ? 2.6393 3.1996 2.6660 0.2458  -0.2007 -0.2461 788  PHE A O   
5980  C CB  . PHE A 788  ? 2.5979 3.2952 2.6232 0.2446  -0.1848 -0.2250 788  PHE A CB  
5981  C CG  . PHE A 788  ? 2.5079 3.2021 2.5565 0.2565  -0.1729 -0.2003 788  PHE A CG  
5982  C CD1 . PHE A 788  ? 2.4682 3.1409 2.5362 0.2688  -0.1684 -0.2000 788  PHE A CD1 
5983  C CD2 . PHE A 788  ? 2.4574 3.1704 2.5092 0.2553  -0.1663 -0.1776 788  PHE A CD2 
5984  C CE1 . PHE A 788  ? 2.3958 3.0650 2.4851 0.2796  -0.1580 -0.1775 788  PHE A CE1 
5985  C CE2 . PHE A 788  ? 2.3887 3.0986 2.4627 0.2665  -0.1557 -0.1557 788  PHE A CE2 
5986  C CZ  . PHE A 788  ? 2.3589 3.0462 2.4513 0.2785  -0.1518 -0.1557 788  PHE A CZ  
5987  N N   . ALA A 789  ? 2.6427 3.2209 2.6578 0.2424  -0.2108 -0.2796 789  ALA A N   
5988  C CA  . ALA A 789  ? 2.5756 3.1053 2.6017 0.2496  -0.2149 -0.2912 789  ALA A CA  
5989  C C   . ALA A 789  ? 2.4966 3.0472 2.5482 0.2652  -0.2015 -0.2790 789  ALA A C   
5990  O O   . ALA A 789  ? 2.4787 3.0789 2.5354 0.2689  -0.1936 -0.2740 789  ALA A O   
5991  C CB  . ALA A 789  ? 2.6341 3.1367 2.6471 0.2431  -0.2302 -0.3224 789  ALA A CB  
5992  N N   . LEU A 790  ? 2.1681 2.6811 2.2353 0.2738  -0.1994 -0.2739 790  LEU A N   
5993  C CA  . LEU A 790  ? 2.1290 2.6573 2.2211 0.2884  -0.1874 -0.2614 790  LEU A CA  
5994  C C   . LEU A 790  ? 2.1757 2.6939 2.2732 0.2928  -0.1921 -0.2834 790  LEU A C   
5995  O O   . LEU A 790  ? 2.1845 2.6616 2.2718 0.2874  -0.2055 -0.3069 790  LEU A O   
5996  C CB  . LEU A 790  ? 2.0550 2.5482 2.1622 0.2958  -0.1829 -0.2459 790  LEU A CB  
5997  C CG  . LEU A 790  ? 2.0209 2.4983 2.1168 0.2879  -0.1848 -0.2357 790  LEU A CG  
5998  C CD1 . LEU A 790  ? 2.0498 2.4655 2.1320 0.2796  -0.1992 -0.2544 790  LEU A CD1 
5999  C CD2 . LEU A 790  ? 1.9417 2.4252 2.0574 0.2979  -0.1720 -0.2087 790  LEU A CD2 
6000  N N   . PRO A 791  ? 1.9800 2.5355 2.0947 0.3029  -0.1811 -0.2751 791  PRO A N   
6001  C CA  . PRO A 791  ? 2.0795 2.6417 2.1990 0.3068  -0.1833 -0.2954 791  PRO A CA  
6002  C C   . PRO A 791  ? 2.1908 2.6967 2.3195 0.3117  -0.1906 -0.3090 791  PRO A C   
6003  O O   . PRO A 791  ? 2.2096 2.6913 2.3521 0.3184  -0.1861 -0.2935 791  PRO A O   
6004  C CB  . PRO A 791  ? 2.0181 2.6292 2.1576 0.3174  -0.1676 -0.2756 791  PRO A CB  
6005  C CG  . PRO A 791  ? 1.9583 2.5917 2.1019 0.3180  -0.1583 -0.2452 791  PRO A CG  
6006  C CD  . PRO A 791  ? 1.9379 2.5226 2.0723 0.3126  -0.1661 -0.2453 791  PRO A CD  
6007  N N   . ASP A 792  ? 2.5696 3.0544 2.6915 0.3086  -0.2020 -0.3373 792  ASP A N   
6008  C CA  . ASP A 792  ? 2.6577 3.0950 2.7923 0.3150  -0.2078 -0.3497 792  ASP A CA  
6009  C C   . ASP A 792  ? 2.5577 3.0213 2.7175 0.3286  -0.1930 -0.3321 792  ASP A C   
6010  O O   . ASP A 792  ? 2.5381 3.0540 2.7029 0.3319  -0.1837 -0.3281 792  ASP A O   
6011  C CB  . ASP A 792  ? 2.8858 3.3096 3.0138 0.3118  -0.2201 -0.3824 792  ASP A CB  
6012  C CG  . ASP A 792  ? 3.1311 3.4932 3.2669 0.3145  -0.2314 -0.3981 792  ASP A CG  
6013  O OD1 . ASP A 792  ? 3.2057 3.5426 3.3563 0.3215  -0.2270 -0.3835 792  ASP A OD1 
6014  O OD2 . ASP A 792  ? 3.2922 3.6307 3.4197 0.3094  -0.2453 -0.4253 792  ASP A OD2 
6015  N N   . SER A 793  ? 2.5196 2.9480 2.6943 0.3357  -0.1909 -0.3203 793  SER A N   
6016  C CA  . SER A 793  ? 2.4126 2.8576 2.6124 0.3486  -0.1785 -0.3041 793  SER A CA  
6017  C C   . SER A 793  ? 2.2984 2.7026 2.5104 0.3541  -0.1767 -0.2872 793  SER A C   
6018  O O   . SER A 793  ? 2.2863 2.6690 2.4886 0.3487  -0.1791 -0.2779 793  SER A O   
6019  C CB  . SER A 793  ? 2.3730 2.8841 2.5781 0.3515  -0.1640 -0.2830 793  SER A CB  
6020  O OG  . SER A 793  ? 2.3131 2.8374 2.5426 0.3633  -0.1529 -0.2654 793  SER A OG  
6021  N N   . LEU A 794  ? 2.6560 3.0504 2.8896 0.3647  -0.1721 -0.2834 794  LEU A N   
6022  C CA  . LEU A 794  ? 2.5519 2.9102 2.7986 0.3706  -0.1696 -0.2668 794  LEU A CA  
6023  C C   . LEU A 794  ? 2.4974 2.8946 2.7593 0.3782  -0.1543 -0.2359 794  LEU A C   
6024  O O   . LEU A 794  ? 2.5175 2.9441 2.7973 0.3868  -0.1456 -0.2276 794  LEU A O   
6025  C CB  . LEU A 794  ? 2.5390 2.8596 2.8011 0.3776  -0.1744 -0.2788 794  LEU A CB  
6026  C CG  . LEU A 794  ? 2.5863 2.8465 2.8361 0.3704  -0.1910 -0.3018 794  LEU A CG  
6027  C CD1 . LEU A 794  ? 2.6325 2.9022 2.8641 0.3614  -0.2010 -0.3274 794  LEU A CD1 
6028  C CD2 . LEU A 794  ? 2.5983 2.8203 2.8661 0.3781  -0.1949 -0.3092 794  LEU A CD2 
6029  N N   . THR A 795  ? 2.2938 2.6912 2.5490 0.3748  -0.1514 -0.2187 795  THR A N   
6030  C CA  . THR A 795  ? 2.1999 2.6322 2.4697 0.3817  -0.1380 -0.1887 795  THR A CA  
6031  C C   . THR A 795  ? 2.1512 2.5655 2.4142 0.3781  -0.1376 -0.1746 795  THR A C   
6032  O O   . THR A 795  ? 2.1274 2.5065 2.3725 0.3692  -0.1473 -0.1878 795  THR A O   
6033  C CB  . THR A 795  ? 2.9116 3.4113 3.1793 0.3803  -0.1300 -0.1808 795  THR A CB  
6034  O OG1 . THR A 795  ? 2.9479 3.4559 3.1916 0.3689  -0.1379 -0.1992 795  THR A OG1 
6035  C CG2 . THR A 795  ? 2.9066 3.4368 3.1896 0.3874  -0.1244 -0.1829 795  THR A CG2 
6036  N N   . THR A 796  ? 2.2609 2.6999 2.5390 0.3850  -0.1264 -0.1474 796  THR A N   
6037  C CA  . THR A 796  ? 2.2387 2.6742 2.5114 0.3819  -0.1240 -0.1324 796  THR A CA  
6038  C C   . THR A 796  ? 2.2676 2.7650 2.5415 0.3814  -0.1151 -0.1145 796  THR A C   
6039  O O   . THR A 796  ? 2.2646 2.7968 2.5576 0.3898  -0.1054 -0.0950 796  THR A O   
6040  C CB  . THR A 796  ? 2.1798 2.5830 2.4697 0.3903  -0.1196 -0.1156 796  THR A CB  
6041  O OG1 . THR A 796  ? 2.2030 2.5476 2.4903 0.3897  -0.1286 -0.1326 796  THR A OG1 
6042  C CG2 . THR A 796  ? 2.1411 2.5429 2.4254 0.3870  -0.1168 -0.1018 796  THR A CG2 
6043  N N   . TRP A 797  ? 2.0505 2.5618 2.3038 0.3709  -0.1191 -0.1213 797  TRP A N   
6044  C CA  . TRP A 797  ? 2.0131 2.5830 2.2645 0.3684  -0.1124 -0.1067 797  TRP A CA  
6045  C C   . TRP A 797  ? 1.9195 2.4995 2.1817 0.3723  -0.1045 -0.0801 797  TRP A C   
6046  O O   . TRP A 797  ? 1.9136 2.4605 2.1686 0.3688  -0.1077 -0.0810 797  TRP A O   
6047  C CB  . TRP A 797  ? 2.0881 2.6674 2.3127 0.3551  -0.1206 -0.1250 797  TRP A CB  
6048  C CG  . TRP A 797  ? 2.1862 2.7662 2.4008 0.3513  -0.1277 -0.1505 797  TRP A CG  
6049  C CD1 . TRP A 797  ? 2.2601 2.8077 2.4545 0.3420  -0.1403 -0.1773 797  TRP A CD1 
6050  C CD2 . TRP A 797  ? 2.2235 2.8388 2.4486 0.3567  -0.1227 -0.1517 797  TRP A CD2 
6051  N NE1 . TRP A 797  ? 2.3171 2.8775 2.5098 0.3421  -0.1434 -0.1957 797  TRP A NE1 
6052  C CE2 . TRP A 797  ? 2.2984 2.9009 2.5094 0.3509  -0.1323 -0.1806 797  TRP A CE2 
6053  C CE3 . TRP A 797  ? 2.2086 2.8654 2.4538 0.3654  -0.1113 -0.1309 797  TRP A CE3 
6054  C CZ2 . TRP A 797  ? 2.3215 2.9523 2.5382 0.3541  -0.1299 -0.1902 797  TRP A CZ2 
6055  C CZ3 . TRP A 797  ? 2.2364 2.9213 2.4860 0.3677  -0.1092 -0.1395 797  TRP A CZ3 
6056  C CH2 . TRP A 797  ? 2.2897 2.9621 2.5252 0.3623  -0.1180 -0.1694 797  TRP A CH2 
6057  N N   . GLU A 798  ? 1.8840 2.5099 2.1640 0.3793  -0.0944 -0.0567 798  GLU A N   
6058  C CA  . GLU A 798  ? 1.8402 2.4831 2.1309 0.3826  -0.0873 -0.0315 798  GLU A CA  
6059  C C   . GLU A 798  ? 1.8303 2.5277 2.1127 0.3760  -0.0846 -0.0221 798  GLU A C   
6060  O O   . GLU A 798  ? 1.8094 2.5546 2.1045 0.3800  -0.0777 -0.0045 798  GLU A O   
6061  C CB  . GLU A 798  ? 1.8105 2.4616 2.1300 0.3957  -0.0784 -0.0076 798  GLU A CB  
6062  C CG  . GLU A 798  ? 1.7980 2.4722 2.1302 0.3993  -0.0713 0.0186  798  GLU A CG  
6063  C CD  . GLU A 798  ? 1.8014 2.4794 2.1627 0.4122  -0.0637 0.0422  798  GLU A CD  
6064  O OE1 . GLU A 798  ? 1.8174 2.4760 2.1886 0.4181  -0.0640 0.0381  798  GLU A OE1 
6065  O OE2 . GLU A 798  ? 1.7952 2.4956 2.1704 0.4164  -0.0578 0.0651  798  GLU A OE2 
6066  N N   . ILE A 799  ? 1.3378 2.0278 1.5989 0.3654  -0.0905 -0.0333 799  ILE A N   
6067  C CA  . ILE A 799  ? 1.3711 2.1100 1.6218 0.3578  -0.0893 -0.0270 799  ILE A CA  
6068  C C   . ILE A 799  ? 1.3620 2.1247 1.6283 0.3625  -0.0813 0.0009  799  ILE A C   
6069  O O   . ILE A 799  ? 1.3738 2.1122 1.6371 0.3608  -0.0822 0.0026  799  ILE A O   
6070  C CB  . ILE A 799  ? 1.3022 2.0254 1.5230 0.3438  -0.0998 -0.0516 799  ILE A CB  
6071  C CG1 . ILE A 799  ? 1.3038 2.0253 1.5150 0.3369  -0.1008 -0.0455 799  ILE A CG1 
6072  C CG2 . ILE A 799  ? 1.3105 1.9760 1.5224 0.3423  -0.1086 -0.0760 799  ILE A CG2 
6073  C CD1 . ILE A 799  ? 1.3181 2.0171 1.5001 0.3228  -0.1125 -0.0706 799  ILE A CD1 
6074  N N   . GLN A 800  ? 1.5036 2.3132 1.7881 0.3688  -0.0735 0.0230  800  GLN A N   
6075  C CA  . GLN A 800  ? 1.4981 2.3373 1.7997 0.3735  -0.0662 0.0510  800  GLN A CA  
6076  C C   . GLN A 800  ? 1.5119 2.4061 1.8040 0.3652  -0.0657 0.0585  800  GLN A C   
6077  O O   . GLN A 800  ? 1.5301 2.4574 1.8137 0.3604  -0.0667 0.0530  800  GLN A O   
6078  C CB  . GLN A 800  ? 1.4927 2.3463 1.8241 0.3865  -0.0584 0.0744  800  GLN A CB  
6079  C CG  . GLN A 800  ? 1.5155 2.4276 1.8542 0.3866  -0.0544 0.0879  800  GLN A CG  
6080  C CD  . GLN A 800  ? 1.5241 2.4309 1.8702 0.3917  -0.0537 0.0818  800  GLN A CD  
6081  O OE1 . GLN A 800  ? 1.5405 2.3996 1.8876 0.3958  -0.0563 0.0684  800  GLN A OE1 
6082  N NE2 . GLN A 800  ? 1.5108 2.4672 1.8620 0.3911  -0.0502 0.0919  800  GLN A NE2 
6083  N N   . GLY A 801  ? 1.2766 2.1820 1.5706 0.3634  -0.0638 0.0713  801  GLY A N   
6084  C CA  . GLY A 801  ? 1.2853 2.2397 1.5684 0.3543  -0.0644 0.0770  801  GLY A CA  
6085  C C   . GLY A 801  ? 1.2627 2.2517 1.5666 0.3595  -0.0576 0.1065  801  GLY A C   
6086  O O   . GLY A 801  ? 1.2532 2.2244 1.5620 0.3612  -0.0564 0.1118  801  GLY A O   
6087  N N   . ILE A 802  ? 1.6547 2.6936 1.9717 0.3621  -0.0533 0.1256  802  ILE A N   
6088  C CA  . ILE A 802  ? 1.6431 2.7221 1.9796 0.3658  -0.0481 0.1544  802  ILE A CA  
6089  C C   . ILE A 802  ? 1.6657 2.7804 1.9847 0.3536  -0.0511 0.1539  802  ILE A C   
6090  O O   . ILE A 802  ? 1.7386 2.8668 2.0338 0.3429  -0.0560 0.1373  802  ILE A O   
6091  C CB  . ILE A 802  ? 1.6573 2.7741 2.0170 0.3734  -0.0428 0.1777  802  ILE A CB  
6092  C CG1 . ILE A 802  ? 1.6534 2.8318 2.0184 0.3690  -0.0411 0.1995  802  ILE A CG1 
6093  C CG2 . ILE A 802  ? 1.6691 2.7854 2.0198 0.3718  -0.0443 0.1631  802  ILE A CG2 
6094  C CD1 . ILE A 802  ? 1.6389 2.8270 2.0275 0.3759  -0.0372 0.2243  802  ILE A CD1 
6095  N N   . GLY A 803  ? 1.7818 2.9106 2.1130 0.3555  -0.0483 0.1715  803  GLY A N   
6096  C CA  . GLY A 803  ? 1.7726 2.9372 2.0906 0.3447  -0.0507 0.1744  803  GLY A CA  
6097  C C   . GLY A 803  ? 1.8014 3.0121 2.1446 0.3499  -0.0456 0.2061  803  GLY A C   
6098  O O   . GLY A 803  ? 1.7483 2.9495 2.1187 0.3621  -0.0406 0.2234  803  GLY A O   
6099  N N   . ILE A 804  ? 1.2772 2.5377 1.6118 0.3406  -0.0474 0.2139  804  ILE A N   
6100  C CA  . ILE A 804  ? 1.2658 2.5735 1.6241 0.3445  -0.0436 0.2447  804  ILE A CA  
6101  C C   . ILE A 804  ? 1.3033 2.6473 1.6480 0.3327  -0.0467 0.2475  804  ILE A C   
6102  O O   . ILE A 804  ? 1.2779 2.6314 1.5944 0.3201  -0.0519 0.2301  804  ILE A O   
6103  C CB  . ILE A 804  ? 1.2619 2.6067 1.6340 0.3480  -0.0413 0.2620  804  ILE A CB  
6104  C CG1 . ILE A 804  ? 1.2479 2.6073 1.5929 0.3370  -0.0452 0.2435  804  ILE A CG1 
6105  C CG2 . ILE A 804  ? 1.2262 2.5405 1.6206 0.3617  -0.0373 0.2678  804  ILE A CG2 
6106  C CD1 . ILE A 804  ? 1.2387 2.6113 1.5947 0.3422  -0.0425 0.2508  804  ILE A CD1 
6107  N N   . SER A 805  ? 2.1940 3.5574 2.5602 0.3374  -0.0437 0.2694  805  SER A N   
6108  C CA  . SER A 805  ? 2.3011 3.7001 2.6604 0.3281  -0.0460 0.2763  805  SER A CA  
6109  C C   . SER A 805  ? 2.3043 3.7397 2.6972 0.3364  -0.0418 0.3090  805  SER A C   
6110  O O   . SER A 805  ? 2.3055 3.7522 2.7224 0.3461  -0.0386 0.3276  805  SER A O   
6111  C CB  . SER A 805  ? 2.2903 3.6551 2.6347 0.3233  -0.0479 0.2584  805  SER A CB  
6112  O OG  . SER A 805  ? 2.3296 3.6787 2.6387 0.3103  -0.0543 0.2310  805  SER A OG  
6113  N N   . ASN A 806  ? 2.3659 3.8189 2.7610 0.3325  -0.0423 0.3159  806  ASN A N   
6114  C CA  . ASN A 806  ? 2.4515 3.9448 2.8773 0.3387  -0.0396 0.3467  806  ASN A CA  
6115  C C   . ASN A 806  ? 2.4624 3.9309 2.9225 0.3556  -0.0339 0.3601  806  ASN A C   
6116  O O   . ASN A 806  ? 2.4535 3.9517 2.9443 0.3635  -0.0317 0.3871  806  ASN A O   
6117  C CB  . ASN A 806  ? 2.5427 4.0666 2.9592 0.3281  -0.0424 0.3494  806  ASN A CB  
6118  C CG  . ASN A 806  ? 2.6447 4.2004 3.0306 0.3118  -0.0484 0.3406  806  ASN A CG  
6119  O OD1 . ASN A 806  ? 2.6958 4.2362 3.0516 0.3004  -0.0525 0.3175  806  ASN A OD1 
6120  N ND2 . ASN A 806  ? 2.6768 4.2764 3.0699 0.3102  -0.0492 0.3586  806  ASN A ND2 
6121  N N   . THR A 807  ? 2.3745 3.7881 2.8299 0.3611  -0.0320 0.3413  807  THR A N   
6122  C CA  . THR A 807  ? 2.3451 3.7318 2.8317 0.3774  -0.0266 0.3521  807  THR A CA  
6123  C C   . THR A 807  ? 2.2633 3.6528 2.7680 0.3865  -0.0253 0.3658  807  THR A C   
6124  O O   . THR A 807  ? 2.2828 3.6806 2.8210 0.3987  -0.0222 0.3887  807  THR A O   
6125  C CB  . THR A 807  ? 2.3748 3.7021 2.8513 0.3799  -0.0249 0.3286  807  THR A CB  
6126  O OG1 . THR A 807  ? 2.3999 3.6980 2.8436 0.3710  -0.0289 0.3019  807  THR A OG1 
6127  C CG2 . THR A 807  ? 2.3920 3.7223 2.8640 0.3748  -0.0245 0.3245  807  THR A CG2 
6128  N N   . GLY A 808  ? 1.7628 3.1472 2.2459 0.3802  -0.0279 0.3521  808  GLY A N   
6129  C CA  . GLY A 808  ? 1.6650 3.0507 2.1616 0.3874  -0.0267 0.3621  808  GLY A CA  
6130  C C   . GLY A 808  ? 1.6398 2.9907 2.1119 0.3837  -0.0284 0.3362  808  GLY A C   
6131  O O   . GLY A 808  ? 1.6321 2.9876 2.0736 0.3712  -0.0322 0.3168  808  GLY A O   
6132  N N   . ILE A 809  ? 1.2048 2.5205 1.6911 0.3946  -0.0258 0.3357  809  ILE A N   
6133  C CA  . ILE A 809  ? 1.2082 2.4869 1.6755 0.3930  -0.0272 0.3119  809  ILE A CA  
6134  C C   . ILE A 809  ? 1.2071 2.4252 1.6788 0.4014  -0.0253 0.2988  809  ILE A C   
6135  O O   . ILE A 809  ? 1.2016 2.4109 1.7012 0.4130  -0.0216 0.3156  809  ILE A O   
6136  C CB  . ILE A 809  ? 1.2052 2.5008 1.6862 0.3980  -0.0259 0.3251  809  ILE A CB  
6137  C CG1 . ILE A 809  ? 1.2090 2.4717 1.6707 0.3959  -0.0274 0.3004  809  ILE A CG1 
6138  C CG2 . ILE A 809  ? 1.1977 2.4856 1.7155 0.4130  -0.0220 0.3493  809  ILE A CG2 
6139  C CD1 . ILE A 809  ? 1.2045 2.4652 1.6863 0.4050  -0.0249 0.3126  809  ILE A CD1 
6140  N N   . CYS A 810  ? 2.3470 3.5239 2.7921 0.3954  -0.0283 0.2695  810  CYS A N   
6141  C CA  . CYS A 810  ? 2.3141 3.4305 2.7602 0.4019  -0.0273 0.2550  810  CYS A CA  
6142  C C   . CYS A 810  ? 2.3286 3.4005 2.7500 0.3971  -0.0313 0.2258  810  CYS A C   
6143  O O   . CYS A 810  ? 2.3334 3.4000 2.7261 0.3852  -0.0362 0.2049  810  CYS A O   
6144  C CB  . CYS A 810  ? 2.2910 3.3955 2.7345 0.3998  -0.0266 0.2514  810  CYS A CB  
6145  S SG  . CYS A 810  ? 2.6839 3.7163 3.1262 0.4058  -0.0254 0.2333  810  CYS A SG  
6146  N N   . VAL A 811  ? 1.8365 2.8748 2.2699 0.4065  -0.0297 0.2245  811  VAL A N   
6147  C CA  . VAL A 811  ? 1.8418 2.8379 2.2556 0.4033  -0.0337 0.1986  811  VAL A CA  
6148  C C   . VAL A 811  ? 1.8546 2.7996 2.2527 0.3999  -0.0363 0.1776  811  VAL A C   
6149  O O   . VAL A 811  ? 1.8531 2.7756 2.2658 0.4070  -0.0329 0.1845  811  VAL A O   
6150  C CB  . VAL A 811  ? 1.8344 2.8094 2.2679 0.4147  -0.0311 0.2051  811  VAL A CB  
6151  C CG1 . VAL A 811  ? 1.8581 2.7896 2.2725 0.4114  -0.0356 0.1781  811  VAL A CG1 
6152  C CG2 . VAL A 811  ? 1.8097 2.8344 2.2595 0.4177  -0.0286 0.2269  811  VAL A CG2 
6153  N N   . ALA A 812  ? 2.7376 3.6635 3.1062 0.3888  -0.0427 0.1517  812  ALA A N   
6154  C CA  . ALA A 812  ? 2.7317 3.6048 3.0847 0.3849  -0.0463 0.1310  812  ALA A CA  
6155  C C   . ALA A 812  ? 2.7124 3.5363 3.0720 0.3928  -0.0467 0.1224  812  ALA A C   
6156  O O   . ALA A 812  ? 2.7026 3.5319 3.0696 0.3974  -0.0463 0.1243  812  ALA A O   
6157  C CB  . ALA A 812  ? 2.7875 3.6569 3.1069 0.3697  -0.0543 0.1070  812  ALA A CB  
6158  N N   . ASP A 813  ? 2.0852 2.8620 2.4424 0.3939  -0.0472 0.1133  813  ASP A N   
6159  C CA  . ASP A 813  ? 2.0612 2.7862 2.4203 0.3991  -0.0490 0.1020  813  ASP A CA  
6160  C C   . ASP A 813  ? 2.0259 2.7389 2.3615 0.3902  -0.0568 0.0789  813  ASP A C   
6161  O O   . ASP A 813  ? 2.0175 2.7347 2.3286 0.3778  -0.0626 0.0637  813  ASP A O   
6162  C CB  . ASP A 813  ? 2.1205 2.7992 2.4741 0.3978  -0.0496 0.0927  813  ASP A CB  
6163  C CG  . ASP A 813  ? 2.1431 2.8329 2.5201 0.4067  -0.0417 0.1135  813  ASP A CG  
6164  O OD1 . ASP A 813  ? 2.1297 2.8175 2.5329 0.4196  -0.0365 0.1297  813  ASP A OD1 
6165  O OD2 . ASP A 813  ? 2.1640 2.8646 2.5337 0.4007  -0.0410 0.1136  813  ASP A OD2 
6166  N N   . THR A 814  ? 1.3586 2.0570 1.7022 0.3964  -0.0572 0.0761  814  THR A N   
6167  C CA  . THR A 814  ? 1.3596 2.0456 1.6842 0.3896  -0.0644 0.0536  814  THR A CA  
6168  C C   . THR A 814  ? 1.3719 2.0112 1.6714 0.3795  -0.0728 0.0284  814  THR A C   
6169  O O   . THR A 814  ? 1.3762 1.9975 1.6719 0.3769  -0.0725 0.0291  814  THR A O   
6170  C CB  . THR A 814  ? 1.3239 1.9948 1.6637 0.3990  -0.0632 0.0544  814  THR A CB  
6171  O OG1 . THR A 814  ? 1.3456 1.9789 1.6675 0.3934  -0.0713 0.0280  814  THR A OG1 
6172  C CG2 . THR A 814  ? 1.3072 1.9510 1.6710 0.4111  -0.0578 0.0696  814  THR A CG2 
6173  N N   . VAL A 815  ? 2.0760 2.6976 2.3586 0.3734  -0.0806 0.0063  815  VAL A N   
6174  C CA  . VAL A 815  ? 2.1342 2.7059 2.3947 0.3642  -0.0901 -0.0181 815  VAL A CA  
6175  C C   . VAL A 815  ? 2.1617 2.7110 2.4164 0.3638  -0.0967 -0.0374 815  VAL A C   
6176  O O   . VAL A 815  ? 2.2217 2.7866 2.4600 0.3558  -0.1026 -0.0523 815  VAL A O   
6177  C CB  . VAL A 815  ? 2.1837 2.7681 2.4189 0.3497  -0.0960 -0.0288 815  VAL A CB  
6178  C CG1 . VAL A 815  ? 2.2168 2.7513 2.4284 0.3392  -0.1076 -0.0551 815  VAL A CG1 
6179  C CG2 . VAL A 815  ? 2.1743 2.7737 2.4146 0.3495  -0.0901 -0.0123 815  VAL A CG2 
6180  N N   . LYS A 816  ? 2.2888 2.8023 2.5577 0.3726  -0.0958 -0.0370 816  LYS A N   
6181  C CA  . LYS A 816  ? 2.3374 2.8245 2.6029 0.3730  -0.1023 -0.0556 816  LYS A CA  
6182  C C   . LYS A 816  ? 2.4157 2.8715 2.6539 0.3598  -0.1144 -0.0819 816  LYS A C   
6183  O O   . LYS A 816  ? 2.4031 2.8504 2.6266 0.3513  -0.1174 -0.0843 816  LYS A O   
6184  C CB  . LYS A 816  ? 2.6354 3.0798 2.9180 0.3828  -0.1008 -0.0521 816  LYS A CB  
6185  C CG  . LYS A 816  ? 2.8284 3.2984 3.1395 0.3963  -0.0906 -0.0285 816  LYS A CG  
6186  C CD  . LYS A 816  ? 2.7911 3.2782 3.1153 0.4012  -0.0822 -0.0049 816  LYS A CD  
6187  C CE  . LYS A 816  ? 2.7308 3.2390 3.0842 0.4146  -0.0734 0.0189  816  LYS A CE  
6188  N NZ  . LYS A 816  ? 2.6850 3.2091 3.0537 0.4202  -0.0658 0.0419  816  LYS A NZ  
6189  N N   . ALA A 817  ? 2.0987 2.5373 2.3306 0.3581  -0.1218 -0.1015 817  ALA A N   
6190  C CA  . ALA A 817  ? 2.2187 2.6287 2.4255 0.3454  -0.1346 -0.1269 817  ALA A CA  
6191  C C   . ALA A 817  ? 2.2426 2.6347 2.4480 0.3460  -0.1421 -0.1475 817  ALA A C   
6192  O O   . ALA A 817  ? 2.2767 2.6865 2.4686 0.3394  -0.1479 -0.1631 817  ALA A O   
6193  C CB  . ALA A 817  ? 2.2792 2.7274 2.4680 0.3349  -0.1364 -0.1290 817  ALA A CB  
6194  N N   . LYS A 818  ? 2.6337 2.9904 2.8537 0.3543  -0.1419 -0.1476 818  LYS A N   
6195  C CA  . LYS A 818  ? 2.6583 2.9928 2.8800 0.3559  -0.1491 -0.1668 818  LYS A CA  
6196  C C   . LYS A 818  ? 2.6684 2.9763 2.8658 0.3432  -0.1636 -0.1937 818  LYS A C   
6197  O O   . LYS A 818  ? 2.6516 2.9274 2.8335 0.3340  -0.1708 -0.1992 818  LYS A O   
6198  C CB  . LYS A 818  ? 2.6941 2.9828 2.9317 0.3642  -0.1490 -0.1638 818  LYS A CB  
6199  C CG  . LYS A 818  ? 2.7786 3.0116 3.0046 0.3575  -0.1566 -0.1695 818  LYS A CG  
6200  C CD  . LYS A 818  ? 2.8373 3.0269 3.0797 0.3658  -0.1558 -0.1646 818  LYS A CD  
6201  C CE  . LYS A 818  ? 2.9104 3.0458 3.1396 0.3580  -0.1634 -0.1707 818  LYS A CE  
6202  N NZ  . LYS A 818  ? 2.9262 3.0139 3.1679 0.3641  -0.1655 -0.1707 818  LYS A NZ  
6203  N N   . VAL A 819  ? 2.2810 2.6038 2.4755 0.3423  -0.1681 -0.2103 819  VAL A N   
6204  C CA  . VAL A 819  ? 2.3211 2.6150 2.4962 0.3317  -0.1830 -0.2375 819  VAL A CA  
6205  C C   . VAL A 819  ? 2.3401 2.5999 2.5269 0.3379  -0.1884 -0.2514 819  VAL A C   
6206  O O   . VAL A 819  ? 2.3191 2.5979 2.5262 0.3491  -0.1799 -0.2434 819  VAL A O   
6207  C CB  . VAL A 819  ? 2.3204 2.6579 2.4831 0.3258  -0.1849 -0.2486 819  VAL A CB  
6208  C CG1 . VAL A 819  ? 2.3054 2.6845 2.4594 0.3209  -0.1780 -0.2320 819  VAL A CG1 
6209  C CG2 . VAL A 819  ? 2.2908 2.6630 2.4697 0.3355  -0.1780 -0.2497 819  VAL A CG2 
6210  N N   . PHE A 820  ? 2.5075 2.7172 2.6822 0.3303  -0.2029 -0.2718 820  PHE A N   
6211  C CA  . PHE A 820  ? 2.5810 2.7551 2.7675 0.3358  -0.2092 -0.2852 820  PHE A CA  
6212  C C   . PHE A 820  ? 2.6262 2.7423 2.7977 0.3256  -0.2270 -0.3071 820  PHE A C   
6213  O O   . PHE A 820  ? 2.6020 2.6895 2.7592 0.3166  -0.2325 -0.3047 820  PHE A O   
6214  C CB  . PHE A 820  ? 2.6604 2.8218 2.8687 0.3473  -0.1996 -0.2659 820  PHE A CB  
6215  C CG  . PHE A 820  ? 2.8281 2.9355 3.0439 0.3496  -0.2086 -0.2776 820  PHE A CG  
6216  C CD1 . PHE A 820  ? 2.9173 2.9718 3.1245 0.3433  -0.2168 -0.2789 820  PHE A CD1 
6217  C CD2 . PHE A 820  ? 2.9022 3.0119 3.1331 0.3573  -0.2096 -0.2883 820  PHE A CD2 
6218  C CE1 . PHE A 820  ? 2.9904 2.9942 3.2040 0.3446  -0.2260 -0.2895 820  PHE A CE1 
6219  C CE2 . PHE A 820  ? 2.9650 3.0245 3.2035 0.3592  -0.2186 -0.2993 820  PHE A CE2 
6220  C CZ  . PHE A 820  ? 3.0034 3.0093 3.2331 0.3527  -0.2271 -0.2996 820  PHE A CZ  
6221  N N   . LYS A 821  ? 3.0311 3.1308 3.2069 0.3271  -0.2361 -0.3282 821  LYS A N   
6222  C CA  . LYS A 821  ? 3.1049 3.1505 3.2686 0.3178  -0.2545 -0.3505 821  LYS A CA  
6223  C C   . LYS A 821  ? 3.1203 3.1158 3.2986 0.3234  -0.2582 -0.3498 821  LYS A C   
6224  O O   . LYS A 821  ? 3.1237 3.1284 3.3235 0.3356  -0.2507 -0.3453 821  LYS A O   
6225  C CB  . LYS A 821  ? 3.1198 3.1775 3.2800 0.3159  -0.2634 -0.3756 821  LYS A CB  
6226  C CG  . LYS A 821  ? 3.1272 3.1323 3.2759 0.3062  -0.2840 -0.4004 821  LYS A CG  
6227  C CD  . LYS A 821  ? 3.1280 3.1428 3.2524 0.2927  -0.2942 -0.4145 821  LYS A CD  
6228  C CE  . LYS A 821  ? 3.1681 3.1386 3.2854 0.2852  -0.3151 -0.4424 821  LYS A CE  
6229  N NZ  . LYS A 821  ? 3.2043 3.1798 3.2973 0.2712  -0.3267 -0.4562 821  LYS A NZ  
6230  N N   . ASP A 822  ? 3.2116 3.1554 3.4065 0.3331  -0.4960 -0.0904 822  ASP A N   
6231  C CA  . ASP A 822  ? 3.2187 3.1115 3.4302 0.3311  -0.4961 -0.1023 822  ASP A CA  
6232  C C   . ASP A 822  ? 3.1916 3.1005 3.4459 0.3686  -0.5151 -0.1562 822  ASP A C   
6233  O O   . ASP A 822  ? 3.0621 3.0177 3.3702 0.3856  -0.4705 -0.1600 822  ASP A O   
6234  C CB  . ASP A 822  ? 3.4066 3.1834 3.5621 0.3008  -0.5486 -0.1009 822  ASP A CB  
6235  C CG  . ASP A 822  ? 3.5142 3.2654 3.6344 0.2612  -0.5210 -0.0446 822  ASP A CG  
6236  O OD1 . ASP A 822  ? 3.5021 3.3151 3.6233 0.2542  -0.4828 -0.0109 822  ASP A OD1 
6237  O OD2 . ASP A 822  ? 3.6098 3.2794 3.7001 0.2382  -0.5383 -0.0345 822  ASP A OD2 
6238  N N   . VAL A 823  ? 2.2564 2.1246 2.4883 0.3808  -0.5811 -0.1982 823  VAL A N   
6239  C CA  . VAL A 823  ? 2.2633 2.1410 2.5307 0.4162  -0.6071 -0.2523 823  VAL A CA  
6240  C C   . VAL A 823  ? 2.3400 2.2519 2.6041 0.4406  -0.6419 -0.2844 823  VAL A C   
6241  O O   . VAL A 823  ? 2.4664 2.3476 2.6859 0.4261  -0.6791 -0.2809 823  VAL A O   
6242  C CB  . VAL A 823  ? 2.3001 2.0783 2.5447 0.4106  -0.6633 -0.2823 823  VAL A CB  
6243  C CG1 . VAL A 823  ? 2.2839 2.0694 2.5586 0.4475  -0.6994 -0.3410 823  VAL A CG1 
6244  C CG2 . VAL A 823  ? 2.2472 2.0020 2.5059 0.3947  -0.6290 -0.2614 823  VAL A CG2 
6245  N N   . PHE A 824  ? 2.2708 2.2454 2.5841 0.4783  -0.6306 -0.3177 824  PHE A N   
6246  C CA  . PHE A 824  ? 2.2659 2.2901 2.5820 0.5047  -0.6535 -0.3455 824  PHE A CA  
6247  C C   . PHE A 824  ? 2.1632 2.2314 2.5319 0.5460  -0.6521 -0.3900 824  PHE A C   
6248  O O   . PHE A 824  ? 2.0459 2.1552 2.4640 0.5584  -0.6025 -0.3846 824  PHE A O   
6249  C CB  . PHE A 824  ? 2.2349 2.3464 2.5533 0.5042  -0.6037 -0.3067 824  PHE A CB  
6250  C CG  . PHE A 824  ? 2.1480 2.3376 2.5150 0.5131  -0.5218 -0.2735 824  PHE A CG  
6251  C CD1 . PHE A 824  ? 2.1116 2.3869 2.5329 0.5529  -0.4873 -0.2913 824  PHE A CD1 
6252  C CD2 . PHE A 824  ? 2.1252 2.3029 2.4847 0.4821  -0.4775 -0.2234 824  PHE A CD2 
6253  C CE1 . PHE A 824  ? 2.0141 2.3603 2.4829 0.5619  -0.4089 -0.2593 824  PHE A CE1 
6254  C CE2 . PHE A 824  ? 2.0280 2.2772 2.4352 0.4905  -0.4000 -0.1924 824  PHE A CE2 
6255  C CZ  . PHE A 824  ? 1.9690 2.3015 2.4316 0.5304  -0.3653 -0.2102 824  PHE A CZ  
6256  N N   . LEU A 825  ? 2.3289 2.3869 2.6889 0.5668  -0.7067 -0.4350 825  LEU A N   
6257  C CA  . LEU A 825  ? 2.2251 2.3242 2.6326 0.6072  -0.7105 -0.4800 825  LEU A CA  
6258  C C   . LEU A 825  ? 2.1641 2.3731 2.6001 0.6379  -0.6745 -0.4791 825  LEU A C   
6259  O O   . LEU A 825  ? 2.1967 2.4338 2.6036 0.6322  -0.6790 -0.4638 825  LEU A O   
6260  C CB  . LEU A 825  ? 2.2559 2.2851 2.6399 0.6161  -0.7902 -0.5319 825  LEU A CB  
6261  C CG  . LEU A 825  ? 2.1362 2.2277 2.5571 0.6598  -0.8003 -0.5771 825  LEU A CG  
6262  C CD1 . LEU A 825  ? 2.0230 2.1323 2.5003 0.6834  -0.7770 -0.6000 825  LEU A CD1 
6263  C CD2 . LEU A 825  ? 2.2249 2.2630 2.6130 0.6664  -0.8778 -0.6209 825  LEU A CD2 
6264  N N   . GLU A 826  ? 2.6719 2.9441 3.1658 0.6717  -0.6389 -0.4964 826  GLU A N   
6265  C CA  . GLU A 826  ? 2.6220 2.9925 3.1430 0.7094  -0.6167 -0.5077 826  GLU A CA  
6266  C C   . GLU A 826  ? 2.6254 2.9960 3.1777 0.7448  -0.6512 -0.5659 826  GLU A C   
6267  O O   . GLU A 826  ? 2.6002 2.9206 3.1733 0.7448  -0.6656 -0.5892 826  GLU A O   
6268  C CB  . GLU A 826  ? 2.5140 2.9778 3.0804 0.7221  -0.5288 -0.4676 826  GLU A CB  
6269  C CG  . GLU A 826  ? 2.4732 2.9738 3.1074 0.7529  -0.4940 -0.4893 826  GLU A CG  
6270  C CD  . GLU A 826  ? 2.3999 3.0108 3.0803 0.7792  -0.4130 -0.4590 826  GLU A CD  
6271  O OE1 . GLU A 826  ? 2.3499 3.0106 3.0851 0.8151  -0.3885 -0.4828 826  GLU A OE1 
6272  O OE2 . GLU A 826  ? 2.3842 3.0321 3.0461 0.7649  -0.3732 -0.4109 826  GLU A OE2 
6273  N N   . MET A 827  ? 1.7715 2.2002 2.3274 0.7759  -0.6651 -0.5907 827  MET A N   
6274  C CA  . MET A 827  ? 1.7706 2.2023 2.3545 0.8103  -0.6990 -0.6462 827  MET A CA  
6275  C C   . MET A 827  ? 1.6510 2.1973 2.2813 0.8523  -0.6461 -0.6458 827  MET A C   
6276  O O   . MET A 827  ? 1.6674 2.2776 2.2818 0.8622  -0.6320 -0.6301 827  MET A O   
6277  C CB  . MET A 827  ? 1.9010 2.2815 2.4398 0.8090  -0.7793 -0.6846 827  MET A CB  
6278  C CG  . MET A 827  ? 2.0013 2.2610 2.4933 0.7715  -0.8372 -0.6891 827  MET A CG  
6279  S SD  . MET A 827  ? 1.8724 2.0520 2.3865 0.7754  -0.8696 -0.7273 827  MET A SD  
6280  C CE  . MET A 827  ? 1.7095 1.9188 2.2514 0.8223  -0.9107 -0.7930 827  MET A CE  
6281  N N   . ASN A 828  ? 2.2024 2.7774 2.8910 0.8779  -0.6145 -0.6623 828  ASN A N   
6282  C CA  . ASN A 828  ? 2.1082 2.7900 2.8426 0.9218  -0.5657 -0.6648 828  ASN A CA  
6283  C C   . ASN A 828  ? 2.0915 2.7864 2.8292 0.9574  -0.6170 -0.7215 828  ASN A C   
6284  O O   . ASN A 828  ? 2.0752 2.7615 2.8536 0.9789  -0.6256 -0.7586 828  ASN A O   
6285  C CB  . ASN A 828  ? 2.1032 2.8203 2.9062 0.9342  -0.4969 -0.6513 828  ASN A CB  
6286  C CG  . ASN A 828  ? 2.1147 2.9491 2.9617 0.9739  -0.4259 -0.6323 828  ASN A CG  
6287  O OD1 . ASN A 828  ? 2.1133 3.0019 2.9534 0.9690  -0.3731 -0.5833 828  ASN A OD1 
6288  N ND2 . ASN A 828  ? 2.1255 2.9995 3.0182 1.0144  -0.4232 -0.6700 828  ASN A ND2 
6289  N N   . ILE A 829  ? 1.5411 2.2560 2.2372 0.9628  -0.6517 -0.7296 829  ILE A N   
6290  C CA  . ILE A 829  ? 1.4785 2.2186 2.1764 0.9984  -0.6961 -0.7808 829  ILE A CA  
6291  C C   . ILE A 829  ? 1.3758 2.2275 2.1251 1.0462  -0.6365 -0.7793 829  ILE A C   
6292  O O   . ILE A 829  ? 1.3330 2.2501 2.1012 1.0499  -0.5656 -0.7333 829  ILE A O   
6293  C CB  . ILE A 829  ? 1.5196 2.2595 2.1621 0.9903  -0.7429 -0.7870 829  ILE A CB  
6294  C CG1 . ILE A 829  ? 1.5599 2.2071 2.1520 0.9393  -0.7772 -0.7666 829  ILE A CG1 
6295  C CG2 . ILE A 829  ? 1.5749 2.3049 2.2126 1.0165  -0.8077 -0.8478 829  ILE A CG2 
6296  C CD1 . ILE A 829  ? 1.6673 2.2031 2.2477 0.9209  -0.8384 -0.8006 829  ILE A CD1 
6297  N N   . PRO A 830  ? 1.7785 2.6516 2.5516 1.0836  -0.6630 -0.8285 830  PRO A N   
6298  C CA  . PRO A 830  ? 1.7504 2.7299 2.5705 1.1327  -0.6094 -0.8297 830  PRO A CA  
6299  C C   . PRO A 830  ? 1.9475 3.0096 2.7404 1.1565  -0.6059 -0.8234 830  PRO A C   
6300  O O   . PRO A 830  ? 2.1739 3.2064 2.9143 1.1357  -0.6544 -0.8280 830  PRO A O   
6301  C CB  . PRO A 830  ? 1.6815 2.6387 2.5300 1.1599  -0.6519 -0.8899 830  PRO A CB  
6302  C CG  . PRO A 830  ? 1.7214 2.5601 2.5444 1.1241  -0.7178 -0.9148 830  PRO A CG  
6303  C CD  . PRO A 830  ? 1.7900 2.5825 2.5538 1.0819  -0.7391 -0.8841 830  PRO A CD  
6304  N N   . TYR A 831  ? 2.1738 3.3394 3.0030 1.2008  -0.5494 -0.8140 831  TYR A N   
6305  C CA  . TYR A 831  ? 2.2008 3.4474 3.0046 1.2302  -0.5542 -0.8181 831  TYR A CA  
6306  C C   . TYR A 831  ? 2.2524 3.4596 3.0361 1.2401  -0.6377 -0.8816 831  TYR A C   
6307  O O   . TYR A 831  ? 2.3469 3.5108 3.0816 1.2163  -0.6957 -0.8952 831  TYR A O   
6308  C CB  . TYR A 831  ? 2.1579 3.5239 3.0041 1.2817  -0.4793 -0.7989 831  TYR A CB  
6309  C CG  . TYR A 831  ? 2.2292 3.6854 3.0466 1.3158  -0.4845 -0.8038 831  TYR A CG  
6310  C CD1 . TYR A 831  ? 2.2113 3.7516 3.0564 1.3718  -0.4666 -0.8266 831  TYR A CD1 
6311  C CD2 . TYR A 831  ? 2.2859 3.7432 3.0490 1.2924  -0.5088 -0.7877 831  TYR A CD2 
6312  C CE1 . TYR A 831  ? 2.2506 3.8753 3.0682 1.4045  -0.4733 -0.8333 831  TYR A CE1 
6313  C CE2 . TYR A 831  ? 2.3274 3.8690 3.0656 1.3238  -0.5159 -0.7959 831  TYR A CE2 
6314  C CZ  . TYR A 831  ? 2.3112 3.9368 3.0758 1.3803  -0.4987 -0.8190 831  TYR A CZ  
6315  O OH  . TYR A 831  ? 2.3533 4.0659 3.0921 1.4134  -0.5068 -0.8288 831  TYR A OH  
6316  N N   . SER A 832  ? 1.3903 2.6061 2.2142 1.2731  -0.6443 -0.9210 832  SER A N   
6317  C CA  . SER A 832  ? 1.4958 2.6892 2.3049 1.2900  -0.7175 -0.9815 832  SER A CA  
6318  C C   . SER A 832  ? 1.5013 2.6186 2.3393 1.2873  -0.7523 -1.0221 832  SER A C   
6319  O O   . SER A 832  ? 1.4345 2.5374 2.3143 1.2831  -0.7114 -1.0069 832  SER A O   
6320  C CB  . SER A 832  ? 1.5127 2.8156 2.3389 1.3462  -0.6963 -0.9979 832  SER A CB  
6321  O OG  . SER A 832  ? 1.4705 2.8064 2.3562 1.3799  -0.6549 -1.0067 832  SER A OG  
6322  N N   . VAL A 833  ? 1.5928 2.6661 2.4103 1.2922  -0.8275 -1.0756 833  VAL A N   
6323  C CA  . VAL A 833  ? 1.6023 2.5987 2.4389 1.2910  -0.8741 -1.1211 833  VAL A CA  
6324  C C   . VAL A 833  ? 1.6315 2.6466 2.4652 1.3257  -0.9269 -1.1784 833  VAL A C   
6325  O O   . VAL A 833  ? 1.6975 2.7139 2.4892 1.3224  -0.9707 -1.1935 833  VAL A O   
6326  C CB  . VAL A 833  ? 1.6786 2.5563 2.4743 1.2416  -0.9324 -1.1252 833  VAL A CB  
6327  C CG1 . VAL A 833  ? 1.6958 2.4987 2.5145 1.2419  -0.9711 -1.1660 833  VAL A CG1 
6328  C CG2 . VAL A 833  ? 1.6529 2.5101 2.4360 1.2025  -0.8901 -1.0674 833  VAL A CG2 
6329  N N   . VAL A 834  ? 1.7430 2.7721 2.6229 1.3584  -0.9232 -1.2118 834  VAL A N   
6330  C CA  . VAL A 834  ? 1.8045 2.8440 2.6859 1.3916  -0.9747 -1.2695 834  VAL A CA  
6331  C C   . VAL A 834  ? 1.9646 2.8910 2.8146 1.3644  -1.0612 -1.3107 834  VAL A C   
6332  O O   . VAL A 834  ? 1.9813 2.8281 2.8412 1.3410  -1.0747 -1.3136 834  VAL A O   
6333  C CB  . VAL A 834  ? 1.7231 2.8094 2.6680 1.4342  -0.9402 -1.2907 834  VAL A CB  
6334  C CG1 . VAL A 834  ? 1.7967 2.8769 2.7451 1.4644  -0.9989 -1.3537 834  VAL A CG1 
6335  C CG2 . VAL A 834  ? 1.6039 2.8076 2.5796 1.4680  -0.8556 -1.2528 834  VAL A CG2 
6336  N N   . ARG A 835  ? 1.9093 2.8287 2.7228 1.3681  -1.1189 -1.3428 835  ARG A N   
6337  C CA  . ARG A 835  ? 2.0859 2.9028 2.8750 1.3497  -1.2005 -1.3865 835  ARG A CA  
6338  C C   . ARG A 835  ? 2.0786 2.8504 2.9077 1.3594  -1.2069 -1.4121 835  ARG A C   
6339  O O   . ARG A 835  ? 2.0107 2.8469 2.8879 1.3958  -1.1671 -1.4204 835  ARG A O   
6340  C CB  . ARG A 835  ? 2.2004 3.0418 2.9715 1.3742  -1.2536 -1.4344 835  ARG A CB  
6341  C CG  . ARG A 835  ? 2.3338 3.0965 3.1046 1.3789  -1.3275 -1.4935 835  ARG A CG  
6342  C CD  . ARG A 835  ? 2.4728 3.2350 3.2138 1.3869  -1.3886 -1.5350 835  ARG A CD  
6343  N NE  . ARG A 835  ? 2.4396 3.3173 3.1927 1.4289  -1.3647 -1.5461 835  ARG A NE  
6344  C CZ  . ARG A 835  ? 2.3469 3.3036 3.1419 1.4725  -1.3232 -1.5531 835  ARG A CZ  
6345  N NH1 . ARG A 835  ? 2.2695 3.2029 3.1023 1.4788  -1.3009 -1.5522 835  ARG A NH1 
6346  N NH2 . ARG A 835  ? 2.3233 3.3838 3.1234 1.5110  -1.3035 -1.5618 835  ARG A NH2 
6347  N N   . GLY A 836  ? 2.3595 3.0223 3.1699 1.3273  -1.2540 -1.4230 836  GLY A N   
6348  C CA  . GLY A 836  ? 2.3852 2.9982 3.2283 1.3374  -1.2743 -1.4566 836  GLY A CA  
6349  C C   . GLY A 836  ? 2.3017 2.9204 3.1886 1.3334  -1.2176 -1.4302 836  GLY A C   
6350  O O   . GLY A 836  ? 2.2931 2.8630 3.2060 1.3366  -1.2361 -1.4567 836  GLY A O   
6351  N N   . GLU A 837  ? 2.2900 2.9705 3.1885 1.3279  -1.1478 -1.3797 837  GLU A N   
6352  C CA  . GLU A 837  ? 2.2130 2.8889 3.1511 1.3170  -1.0953 -1.3520 837  GLU A CA  
6353  C C   . GLU A 837  ? 2.3106 2.8882 3.2093 1.2678  -1.1216 -1.3302 837  GLU A C   
6354  O O   . GLU A 837  ? 2.3888 2.9286 3.2321 1.2419  -1.1553 -1.3178 837  GLU A O   
6355  C CB  . GLU A 837  ? 2.0812 2.8563 3.0471 1.3290  -1.0088 -1.3041 837  GLU A CB  
6356  C CG  . GLU A 837  ? 1.8589 2.7331 2.8747 1.3809  -0.9696 -1.3210 837  GLU A CG  
6357  C CD  . GLU A 837  ? 1.6958 2.6654 2.7391 1.3933  -0.8798 -1.2691 837  GLU A CD  
6358  O OE1 . GLU A 837  ? 1.6939 2.6856 2.6987 1.3755  -0.8622 -1.2289 837  GLU A OE1 
6359  O OE2 . GLU A 837  ? 1.5720 2.5955 2.6767 1.4215  -0.8252 -1.2678 837  GLU A OE2 
6360  N N   . GLN A 838  ? 2.1231 2.6589 3.0515 1.2560  -1.1077 -1.3279 838  GLN A N   
6361  C CA  . GLN A 838  ? 2.1667 2.6148 3.0619 1.2119  -1.1248 -1.3045 838  GLN A CA  
6362  C C   . GLN A 838  ? 2.0564 2.5482 2.9662 1.1937  -1.0489 -1.2461 838  GLN A C   
6363  O O   . GLN A 838  ? 1.9221 2.4665 2.8901 1.2097  -0.9903 -1.2373 838  GLN A O   
6364  C CB  . GLN A 838  ? 2.2157 2.5956 3.1354 1.2119  -1.1557 -1.3392 838  GLN A CB  
6365  C CG  . GLN A 838  ? 2.3287 2.6081 3.2111 1.1704  -1.1846 -1.3234 838  GLN A CG  
6366  C CD  . GLN A 838  ? 2.4644 2.6875 3.3768 1.1754  -1.2099 -1.3592 838  GLN A CD  
6367  O OE1 . GLN A 838  ? 2.6000 2.7537 3.4877 1.1784  -1.2779 -1.3978 838  GLN A OE1 
6368  N NE2 . GLN A 838  ? 2.3827 2.6368 3.3495 1.1766  -1.1545 -1.3465 838  GLN A NE2 
6369  N N   . ILE A 839  ? 2.5913 3.0635 3.4512 1.1609  -1.0477 -1.2060 839  ILE A N   
6370  C CA  . ILE A 839  ? 2.5048 3.0219 3.3762 1.1442  -0.9749 -1.1488 839  ILE A CA  
6371  C C   . ILE A 839  ? 2.5511 2.9918 3.4089 1.1034  -0.9731 -1.1229 839  ILE A C   
6372  O O   . ILE A 839  ? 2.6762 3.0245 3.4942 1.0815  -1.0341 -1.1397 839  ILE A O   
6373  C CB  . ILE A 839  ? 2.5094 3.0718 3.3395 1.1363  -0.9614 -1.1145 839  ILE A CB  
6374  C CG1 . ILE A 839  ? 2.3895 3.0254 3.2449 1.1333  -0.8752 -1.0591 839  ILE A CG1 
6375  C CG2 . ILE A 839  ? 2.6098 3.0854 3.3733 1.0957  -1.0151 -1.1048 839  ILE A CG2 
6376  C CD1 . ILE A 839  ? 2.2917 3.0245 3.2120 1.1766  -0.8152 -1.0632 839  ILE A CD1 
6377  N N   . GLN A 840  ? 1.8624 2.3415 2.7529 1.0941  -0.9025 -1.0817 840  GLN A N   
6378  C CA  . GLN A 840  ? 1.8633 2.2776 2.7368 1.0538  -0.8959 -1.0514 840  GLN A CA  
6379  C C   . GLN A 840  ? 1.7463 2.1864 2.5894 1.0270  -0.8531 -0.9915 840  GLN A C   
6380  O O   . GLN A 840  ? 1.6199 2.1282 2.5000 1.0315  -0.7797 -0.9558 840  GLN A O   
6381  C CB  . GLN A 840  ? 1.8664 2.2847 2.8039 1.0588  -0.8562 -1.0571 840  GLN A CB  
6382  C CG  . GLN A 840  ? 2.0414 2.3579 2.9619 1.0334  -0.9028 -1.0746 840  GLN A CG  
6383  C CD  . GLN A 840  ? 2.0778 2.3725 3.0029 0.9994  -0.8598 -1.0318 840  GLN A CD  
6384  O OE1 . GLN A 840  ? 2.1551 2.3802 3.0760 0.9829  -0.8868 -1.0451 840  GLN A OE1 
6385  N NE2 . GLN A 840  ? 2.0075 2.3628 2.9406 0.9903  -0.7937 -0.9814 840  GLN A NE2 
6386  N N   . LEU A 841  ? 2.4118 2.7948 3.1884 0.9993  -0.8998 -0.9813 841  LEU A N   
6387  C CA  . LEU A 841  ? 2.3459 2.7431 3.0857 0.9710  -0.8704 -0.9277 841  LEU A CA  
6388  C C   . LEU A 841  ? 2.2860 2.6445 3.0263 0.9362  -0.8364 -0.8878 841  LEU A C   
6389  O O   . LEU A 841  ? 2.3421 2.6100 3.0418 0.9056  -0.8789 -0.8868 841  LEU A O   
6390  C CB  . LEU A 841  ? 2.4313 2.7716 3.1031 0.9509  -0.9351 -0.9337 841  LEU A CB  
6391  C CG  . LEU A 841  ? 2.4098 2.7889 3.0701 0.9786  -0.9704 -0.9671 841  LEU A CG  
6392  C CD1 . LEU A 841  ? 2.5042 2.8230 3.1003 0.9508  -1.0257 -0.9651 841  LEU A CD1 
6393  C CD2 . LEU A 841  ? 2.2810 2.7791 2.9699 1.0063  -0.9086 -0.9464 841  LEU A CD2 
6394  N N   . LYS A 842  ? 2.1153 2.5418 2.8999 0.9409  -0.7592 -0.8534 842  LYS A N   
6395  C CA  . LYS A 842  ? 2.0876 2.4834 2.8780 0.9090  -0.7224 -0.8160 842  LYS A CA  
6396  C C   . LYS A 842  ? 2.1210 2.5080 2.8604 0.8741  -0.7075 -0.7630 842  LYS A C   
6397  O O   . LYS A 842  ? 2.1710 2.5630 2.8654 0.8710  -0.7352 -0.7586 842  LYS A O   
6398  C CB  . LYS A 842  ? 1.9556 2.4225 2.8217 0.9275  -0.6441 -0.8031 842  LYS A CB  
6399  C CG  . LYS A 842  ? 1.9464 2.4112 2.8692 0.9553  -0.6547 -0.8533 842  LYS A CG  
6400  C CD  . LYS A 842  ? 1.8452 2.3587 2.8426 0.9619  -0.5778 -0.8367 842  LYS A CD  
6401  C CE  . LYS A 842  ? 1.8498 2.3525 2.9054 0.9852  -0.5915 -0.8890 842  LYS A CE  
6402  N NZ  . LYS A 842  ? 1.7685 2.3156 2.9028 0.9900  -0.5165 -0.8758 842  LYS A NZ  
6403  N N   . GLY A 843  ? 1.6723 2.0464 2.4214 0.8478  -0.6635 -0.7245 843  GLY A N   
6404  C CA  . GLY A 843  ? 1.7134 2.0760 2.4185 0.8126  -0.6444 -0.6719 843  GLY A CA  
6405  C C   . GLY A 843  ? 1.7265 2.0315 2.4344 0.7805  -0.6279 -0.6498 843  GLY A C   
6406  O O   . GLY A 843  ? 1.7330 2.0080 2.4753 0.7869  -0.6358 -0.6788 843  GLY A O   
6407  N N   . THR A 844  ? 2.2514 2.5421 2.9241 0.7466  -0.6055 -0.6002 844  THR A N   
6408  C CA  . THR A 844  ? 2.2854 2.5206 2.9559 0.7146  -0.5904 -0.5771 844  THR A CA  
6409  C C   . THR A 844  ? 2.3113 2.4991 2.9157 0.6743  -0.6017 -0.5340 844  THR A C   
6410  O O   . THR A 844  ? 2.2727 2.5120 2.8629 0.6689  -0.5689 -0.4970 844  THR A O   
6411  C CB  . THR A 844  ? 1.9313 2.2328 2.6694 0.7209  -0.5055 -0.5514 844  THR A CB  
6412  O OG1 . THR A 844  ? 1.8672 2.2264 2.5967 0.7102  -0.4494 -0.4969 844  THR A OG1 
6413  C CG2 . THR A 844  ? 1.7821 2.1518 2.5902 0.7642  -0.4806 -0.5861 844  THR A CG2 
6414  N N   . VAL A 845  ? 1.9466 2.0378 2.5110 0.6473  -0.6476 -0.5387 845  VAL A N   
6415  C CA  . VAL A 845  ? 2.0217 2.0593 2.5229 0.6082  -0.6610 -0.4990 845  VAL A CA  
6416  C C   . VAL A 845  ? 1.9434 1.9903 2.4551 0.5816  -0.5997 -0.4489 845  VAL A C   
6417  O O   . VAL A 845  ? 1.8779 1.9134 2.4256 0.5808  -0.5781 -0.4546 845  VAL A O   
6418  C CB  . VAL A 845  ? 1.7020 1.6279 2.1503 0.5912  -0.7371 -0.5222 845  VAL A CB  
6419  C CG1 . VAL A 845  ? 1.6982 1.5866 2.1775 0.6034  -0.7536 -0.5591 845  VAL A CG1 
6420  C CG2 . VAL A 845  ? 1.7493 1.6171 2.1425 0.5489  -0.7377 -0.4761 845  VAL A CG2 
6421  N N   . TYR A 846  ? 2.5630 2.6307 3.0447 0.5595  -0.5721 -0.4011 846  TYR A N   
6422  C CA  . TYR A 846  ? 2.4896 2.5808 2.9885 0.5382  -0.5056 -0.3522 846  TYR A CA  
6423  C C   . TYR A 846  ? 2.6260 2.6340 3.0756 0.4967  -0.5210 -0.3229 846  TYR A C   
6424  O O   . TYR A 846  ? 2.6939 2.6607 3.0850 0.4741  -0.5525 -0.3046 846  TYR A O   
6425  C CB  . TYR A 846  ? 2.3310 2.5167 2.8440 0.5445  -0.4450 -0.3125 846  TYR A CB  
6426  C CG  . TYR A 846  ? 2.1582 2.4371 2.7388 0.5851  -0.3996 -0.3286 846  TYR A CG  
6427  C CD1 . TYR A 846  ? 2.0893 2.4545 2.6770 0.6071  -0.3711 -0.3153 846  TYR A CD1 
6428  C CD2 . TYR A 846  ? 2.0822 2.3634 2.7202 0.6028  -0.3855 -0.3582 846  TYR A CD2 
6429  C CE1 . TYR A 846  ? 1.9759 2.4263 2.6244 0.6465  -0.3277 -0.3283 846  TYR A CE1 
6430  C CE2 . TYR A 846  ? 1.9616 2.3266 2.6643 0.6405  -0.3421 -0.3727 846  TYR A CE2 
6431  C CZ  . TYR A 846  ? 1.9088 2.3576 2.6156 0.6627  -0.3125 -0.3564 846  TYR A CZ  
6432  O OH  . TYR A 846  ? 1.8085 2.3404 2.5788 0.7022  -0.2672 -0.3689 846  TYR A OH  
6433  N N   . ASN A 847  ? 2.2256 2.2112 2.7024 0.4878  -0.4972 -0.3200 847  ASN A N   
6434  C CA  . ASN A 847  ? 2.3560 2.2756 2.7949 0.4500  -0.4966 -0.2868 847  ASN A CA  
6435  C C   . ASN A 847  ? 2.2902 2.2654 2.7539 0.4338  -0.4176 -0.2340 847  ASN A C   
6436  O O   . ASN A 847  ? 2.1541 2.1860 2.6823 0.4480  -0.3621 -0.2339 847  ASN A O   
6437  C CB  . ASN A 847  ? 2.4358 2.2900 2.8839 0.4490  -0.5246 -0.3179 847  ASN A CB  
6438  C CG  . ASN A 847  ? 2.4995 2.2758 2.8975 0.4118  -0.5358 -0.2875 847  ASN A CG  
6439  O OD1 . ASN A 847  ? 2.5048 2.2988 2.8960 0.3873  -0.4886 -0.2386 847  ASN A OD1 
6440  N ND2 . ASN A 847  ? 2.5137 2.2036 2.8755 0.4089  -0.5982 -0.3159 847  ASN A ND2 
6441  N N   . TYR A 848  ? 3.1081 3.0658 3.5221 0.4038  -0.4119 -0.1890 848  TYR A N   
6442  C CA  . TYR A 848  ? 3.0740 3.0720 3.5030 0.3840  -0.3414 -0.1358 848  TYR A CA  
6443  C C   . TYR A 848  ? 3.1653 3.0854 3.5377 0.3428  -0.3561 -0.1023 848  TYR A C   
6444  O O   . TYR A 848  ? 3.1091 3.0507 3.4797 0.3207  -0.3055 -0.0540 848  TYR A O   
6445  C CB  . TYR A 848  ? 3.0336 3.1191 3.4702 0.3937  -0.2993 -0.1060 848  TYR A CB  
6446  C CG  . TYR A 848  ? 2.9355 3.1114 3.4388 0.4342  -0.2611 -0.1268 848  TYR A CG  
6447  C CD1 . TYR A 848  ? 2.8587 3.0489 3.4249 0.4511  -0.2347 -0.1507 848  TYR A CD1 
6448  C CD2 . TYR A 848  ? 2.9048 3.1535 3.4095 0.4564  -0.2499 -0.1226 848  TYR A CD2 
6449  C CE1 . TYR A 848  ? 2.7720 3.0433 3.4012 0.4884  -0.1975 -0.1684 848  TYR A CE1 
6450  C CE2 . TYR A 848  ? 2.8180 3.1493 3.3817 0.4952  -0.2134 -0.1394 848  TYR A CE2 
6451  C CZ  . TYR A 848  ? 2.7657 3.1068 3.3919 0.5108  -0.1864 -0.1614 848  TYR A CZ  
6452  O OH  . TYR A 848  ? 2.7142 3.1367 3.4012 0.5499  -0.1479 -0.1772 848  TYR A OH  
6453  N N   . ARG A 849  ? 2.7899 2.6190 3.1155 0.3338  -0.4249 -0.1273 849  ARG A N   
6454  C CA  . ARG A 849  ? 2.8776 2.6256 3.1545 0.2988  -0.4401 -0.1015 849  ARG A CA  
6455  C C   . ARG A 849  ? 2.7855 2.5280 3.1045 0.2985  -0.4096 -0.1079 849  ARG A C   
6456  O O   . ARG A 849  ? 2.7336 2.5012 3.1043 0.3263  -0.4093 -0.1492 849  ARG A O   
6457  C CB  . ARG A 849  ? 2.9789 2.6337 3.1946 0.2938  -0.5222 -0.1271 849  ARG A CB  
6458  C CG  . ARG A 849  ? 3.0309 2.5941 3.1902 0.2611  -0.5451 -0.1029 849  ARG A CG  
6459  C CD  . ARG A 849  ? 3.1149 2.6842 3.2430 0.2276  -0.5095 -0.0438 849  ARG A CD  
6460  N NE  . ARG A 849  ? 3.1414 2.6250 3.2211 0.1981  -0.5257 -0.0208 849  ARG A NE  
6461  C CZ  . ARG A 849  ? 3.1497 2.6303 3.2108 0.1673  -0.4862 0.0305  849  ARG A CZ  
6462  N NH1 . ARG A 849  ? 3.1613 2.7202 3.2484 0.1616  -0.4275 0.0650  849  ARG A NH1 
6463  N NH2 . ARG A 849  ? 3.1334 2.5334 3.1492 0.1435  -0.5048 0.0480  849  ARG A NH2 
6464  N N   . THR A 850  ? 2.6497 2.3629 2.9498 0.2677  -0.3827 -0.0685 850  THR A N   
6465  C CA  . THR A 850  ? 2.5519 2.2676 2.8948 0.2640  -0.3451 -0.0694 850  THR A CA  
6466  C C   . THR A 850  ? 2.5206 2.1869 2.8746 0.2813  -0.3923 -0.1235 850  THR A C   
6467  O O   . THR A 850  ? 2.4875 2.1946 2.9081 0.3021  -0.3673 -0.1531 850  THR A O   
6468  C CB  . THR A 850  ? 2.4979 2.1734 2.8047 0.2254  -0.3211 -0.0198 850  THR A CB  
6469  O OG1 . THR A 850  ? 2.5267 2.1063 2.7569 0.2072  -0.3842 -0.0185 850  THR A OG1 
6470  C CG2 . THR A 850  ? 2.5106 2.2435 2.8173 0.2082  -0.2628 0.0359  850  THR A CG2 
6471  N N   . SER A 851  ? 2.7004 2.2782 2.9892 0.2725  -0.4595 -0.1351 851  SER A N   
6472  C CA  . SER A 851  ? 2.6964 2.2202 2.9830 0.2904  -0.5143 -0.1862 851  SER A CA  
6473  C C   . SER A 851  ? 2.7563 2.3023 3.0617 0.3234  -0.5504 -0.2321 851  SER A C   
6474  O O   . SER A 851  ? 2.7808 2.3730 3.0884 0.3294  -0.5400 -0.2219 851  SER A O   
6475  C CB  . SER A 851  ? 2.7498 2.1712 2.9540 0.2705  -0.5722 -0.1765 851  SER A CB  
6476  O OG  . SER A 851  ? 2.8600 2.2632 3.0145 0.2618  -0.5993 -0.1584 851  SER A OG  
6477  N N   . GLY A 852  ? 2.2296 1.7429 2.5470 0.3455  -0.5940 -0.2833 852  GLY A N   
6478  C CA  . GLY A 852  ? 2.2660 1.7854 2.5925 0.3763  -0.6386 -0.3298 852  GLY A CA  
6479  C C   . GLY A 852  ? 2.2820 1.7292 2.5336 0.3706  -0.7060 -0.3317 852  GLY A C   
6480  O O   . GLY A 852  ? 2.3136 1.7080 2.5063 0.3418  -0.7152 -0.2936 852  GLY A O   
6481  N N   . MET A 853  ? 2.0418 1.4862 2.2974 0.3977  -0.7517 -0.3754 853  MET A N   
6482  C CA  . MET A 853  ? 2.0564 1.4275 2.2459 0.3948  -0.8191 -0.3833 853  MET A CA  
6483  C C   . MET A 853  ? 2.0452 1.4067 2.2429 0.4276  -0.8738 -0.4389 853  MET A C   
6484  O O   . MET A 853  ? 1.9989 1.4101 2.2546 0.4559  -0.8643 -0.4768 853  MET A O   
6485  C CB  . MET A 853  ? 2.1290 1.5067 2.2799 0.3707  -0.8076 -0.3391 853  MET A CB  
6486  C CG  . MET A 853  ? 2.1608 1.6373 2.3541 0.3805  -0.7621 -0.3299 853  MET A CG  
6487  S SD  . MET A 853  ? 2.5550 2.0355 2.7019 0.3448  -0.7382 -0.2686 853  MET A SD  
6488  C CE  . MET A 853  ? 2.6109 2.0873 2.7614 0.3155  -0.6808 -0.2208 853  MET A CE  
6489  N N   . GLN A 854  ? 3.5141 2.8086 3.6538 0.4230  -0.9309 -0.4430 854  GLN A N   
6490  C CA  . GLN A 854  ? 3.5387 2.8118 3.6781 0.4516  -0.9878 -0.4936 854  GLN A CA  
6491  C C   . GLN A 854  ? 3.5970 2.9016 3.7300 0.4555  -0.9980 -0.4945 854  GLN A C   
6492  O O   . GLN A 854  ? 3.6435 2.9319 3.7370 0.4302  -0.9947 -0.4576 854  GLN A O   
6493  C CB  . GLN A 854  ? 3.5701 2.7353 3.6506 0.4482  -1.0511 -0.5050 854  GLN A CB  
6494  C CG  . GLN A 854  ? 3.4979 2.6298 3.5776 0.4440  -1.0438 -0.5029 854  GLN A CG  
6495  C CD  . GLN A 854  ? 3.5283 2.5541 3.5453 0.4435  -1.1059 -0.5117 854  GLN A CD  
6496  O OE1 . GLN A 854  ? 3.6000 2.5723 3.5712 0.4409  -1.1498 -0.5116 854  GLN A OE1 
6497  N NE2 . GLN A 854  ? 3.4685 2.4638 3.4838 0.4471  -1.1096 -0.5198 854  GLN A NE2 
6498  N N   . PHE A 855  ? 2.5424 1.8927 2.7155 0.4879  -1.0109 -0.5384 855  PHE A N   
6499  C CA  . PHE A 855  ? 2.5768 1.9672 2.7511 0.4976  -1.0210 -0.5471 855  PHE A CA  
6500  C C   . PHE A 855  ? 2.6429 1.9946 2.8089 0.5233  -1.0864 -0.5990 855  PHE A C   
6501  O O   . PHE A 855  ? 2.6443 1.9303 2.7957 0.5316  -1.1272 -0.6245 855  PHE A O   
6502  C CB  . PHE A 855  ? 2.5041 2.0078 2.7414 0.5154  -0.9630 -0.5471 855  PHE A CB  
6503  C CG  . PHE A 855  ? 2.3976 1.9405 2.6950 0.5495  -0.9573 -0.5916 855  PHE A CG  
6504  C CD1 . PHE A 855  ? 2.4222 1.9490 2.7262 0.5786  -1.0094 -0.6442 855  PHE A CD1 
6505  C CD2 . PHE A 855  ? 2.2824 1.8813 2.6337 0.5526  -0.8973 -0.5809 855  PHE A CD2 
6506  C CE1 . PHE A 855  ? 2.3662 1.9314 2.7278 0.6096  -1.0023 -0.6848 855  PHE A CE1 
6507  C CE2 . PHE A 855  ? 2.2249 1.8620 2.6367 0.5831  -0.8888 -0.6219 855  PHE A CE2 
6508  C CZ  . PHE A 855  ? 2.2644 1.8857 2.6813 0.6117  -0.9412 -0.6737 855  PHE A CZ  
6509  N N   . CYS A 856  ? 3.0686 2.4656 3.2460 0.5380  -1.0953 -0.6160 856  CYS A N   
6510  C CA  . CYS A 856  ? 3.1356 2.4947 3.3026 0.5603  -1.1581 -0.6635 856  CYS A CA  
6511  C C   . CYS A 856  ? 3.2287 2.6606 3.4168 0.5761  -1.1531 -0.6774 856  CYS A C   
6512  O O   . CYS A 856  ? 3.3009 2.7171 3.4552 0.5610  -1.1711 -0.6644 856  CYS A O   
6513  C CB  . CYS A 856  ? 3.1820 2.4322 3.2816 0.5385  -1.2115 -0.6537 856  CYS A CB  
6514  S SG  . CYS A 856  ? 3.7134 2.8784 3.7918 0.5632  -1.2932 -0.7087 856  CYS A SG  
6515  N N   . VAL A 857  ? 2.4212 1.9350 2.6666 0.6068  -1.1268 -0.7034 857  VAL A N   
6516  C CA  . VAL A 857  ? 2.4741 2.0636 2.7416 0.6270  -1.1210 -0.7194 857  VAL A CA  
6517  C C   . VAL A 857  ? 2.5404 2.1016 2.8078 0.6543  -1.1829 -0.7753 857  VAL A C   
6518  O O   . VAL A 857  ? 2.5181 2.0587 2.8070 0.6752  -1.2028 -0.8103 857  VAL A O   
6519  C CB  . VAL A 857  ? 2.4035 2.1036 2.7335 0.6479  -1.0545 -0.7143 857  VAL A CB  
6520  C CG1 . VAL A 857  ? 2.3588 2.0980 2.6885 0.6216  -0.9903 -0.6562 857  VAL A CG1 
6521  C CG2 . VAL A 857  ? 2.3217 2.0261 2.6981 0.6713  -1.0491 -0.7462 857  VAL A CG2 
6522  N N   . LYS A 858  ? 3.0781 2.6384 3.3223 0.6539  -1.2134 -0.7845 858  LYS A N   
6523  C CA  . LYS A 858  ? 3.1508 2.6921 3.3972 0.6803  -1.2698 -0.8375 858  LYS A CA  
6524  C C   . LYS A 858  ? 3.1949 2.8178 3.4588 0.6972  -1.2626 -0.8507 858  LYS A C   
6525  O O   . LYS A 858  ? 3.2393 2.8903 3.4856 0.6783  -1.2433 -0.8201 858  LYS A O   
6526  C CB  . LYS A 858  ? 3.2562 2.6833 3.4486 0.6630  -1.3339 -0.8452 858  LYS A CB  
6527  C CG  . LYS A 858  ? 3.3655 2.7578 3.5125 0.6256  -1.3323 -0.8030 858  LYS A CG  
6528  C CD  . LYS A 858  ? 3.4652 2.7418 3.5623 0.6107  -1.3936 -0.8106 858  LYS A CD  
6529  C CE  . LYS A 858  ? 3.5588 2.8052 3.6163 0.5742  -1.3908 -0.7708 858  LYS A CE  
6530  N NZ  . LYS A 858  ? 3.6170 2.7465 3.6267 0.5585  -1.4449 -0.7729 858  LYS A NZ  
6531  N N   . MET A 859  ? 3.1835 2.8467 3.4825 0.7341  -1.2780 -0.8973 859  MET A N   
6532  C CA  . MET A 859  ? 3.1972 2.9415 3.5151 0.7562  -1.2737 -0.9160 859  MET A CA  
6533  C C   . MET A 859  ? 3.2761 2.9697 3.5646 0.7578  -1.3400 -0.9502 859  MET A C   
6534  O O   . MET A 859  ? 3.2801 2.9010 3.5585 0.7655  -1.3916 -0.9840 859  MET A O   
6535  C CB  . MET A 859  ? 3.0780 2.8990 3.4525 0.7969  -1.2504 -0.9472 859  MET A CB  
6536  C CG  . MET A 859  ? 3.0856 2.9618 3.4754 0.8282  -1.2726 -0.9872 859  MET A CG  
6537  S SD  . MET A 859  ? 2.5072 2.4577 2.9626 0.8767  -1.2508 -1.0267 859  MET A SD  
6538  C CE  . MET A 859  ? 3.2741 3.3425 3.7663 0.8822  -1.1588 -0.9807 859  MET A CE  
6539  N N   . SER A 860  ? 3.5503 3.2842 3.8269 0.7511  -1.3379 -0.9421 860  SER A N   
6540  C CA  . SER A 860  ? 3.6880 3.3828 3.9422 0.7515  -1.3966 -0.9748 860  SER A CA  
6541  C C   . SER A 860  ? 3.6976 3.4388 3.9845 0.7935  -1.4209 -1.0303 860  SER A C   
6542  O O   . SER A 860  ? 3.6135 3.4561 3.9351 0.8194  -1.3839 -1.0354 860  SER A O   
6543  C CB  . SER A 860  ? 3.7178 3.4483 3.9535 0.7308  -1.3837 -0.9496 860  SER A CB  
6544  O OG  . SER A 860  ? 3.8145 3.5539 4.0492 0.7442  -1.4273 -0.9904 860  SER A OG  
6545  N N   . ALA A 861  ? 2.9196 2.5862 3.1949 0.8012  -1.4821 -1.0710 861  ALA A N   
6546  C CA  . ALA A 861  ? 2.9348 2.6355 3.2382 0.8400  -1.5117 -1.1265 861  ALA A CA  
6547  C C   . ALA A 861  ? 2.9537 2.7024 3.2556 0.8468  -1.5290 -1.1469 861  ALA A C   
6548  O O   . ALA A 861  ? 3.0456 2.7294 3.3202 0.8309  -1.5763 -1.1606 861  ALA A O   
6549  C CB  . ALA A 861  ? 2.9338 2.5358 3.2247 0.8459  -1.5711 -1.1619 861  ALA A CB  
6550  N N   . VAL A 862  ? 3.2991 3.1617 3.6317 0.8716  -1.4904 -1.1497 862  VAL A N   
6551  C CA  . VAL A 862  ? 3.3331 3.2557 3.6685 0.8843  -1.5052 -1.1739 862  VAL A CA  
6552  C C   . VAL A 862  ? 3.3593 3.3019 3.7194 0.9241  -1.5439 -1.2353 862  VAL A C   
6553  O O   . VAL A 862  ? 3.3081 3.2953 3.7013 0.9557  -1.5250 -1.2514 862  VAL A O   
6554  C CB  . VAL A 862  ? 3.2357 3.2759 3.5860 0.8911  -1.4433 -1.1424 862  VAL A CB  
6555  C CG1 . VAL A 862  ? 3.2718 3.3818 3.6275 0.9106  -1.4605 -1.1736 862  VAL A CG1 
6556  C CG2 . VAL A 862  ? 3.2088 3.2284 3.5319 0.8500  -1.4101 -1.0838 862  VAL A CG2 
6557  N N   . GLU A 863  ? 3.3717 3.2809 3.7174 0.9216  -1.5969 -1.2695 863  GLU A N   
6558  C CA  . GLU A 863  ? 3.3936 3.3115 3.7585 0.9557  -1.6412 -1.3301 863  GLU A CA  
6559  C C   . GLU A 863  ? 3.2594 3.2228 3.6612 0.9953  -1.6251 -1.3531 863  GLU A C   
6560  O O   . GLU A 863  ? 3.2681 3.1648 3.6731 1.0006  -1.6500 -1.3704 863  GLU A O   
6561  C CB  . GLU A 863  ? 3.4913 3.4878 3.8629 0.9691  -1.6487 -1.3540 863  GLU A CB  
6562  C CG  . GLU A 863  ? 3.7684 3.7006 4.1159 0.9450  -1.7020 -1.3738 863  GLU A CG  
6563  C CD  . GLU A 863  ? 3.9359 3.8043 4.2884 0.9612  -1.7657 -1.4303 863  GLU A CD  
6564  O OE1 . GLU A 863  ? 3.9443 3.7615 4.3017 0.9724  -1.7785 -1.4408 863  GLU A OE1 
6565  O OE2 . GLU A 863  ? 4.0245 3.8966 4.3733 0.9539  -1.7912 -1.4549 863  GLU A OE2 
6566  N N   . GLY A 864  ? 2.7450 2.8241 3.1753 1.0242  -1.5828 -1.3534 864  GLY A N   
6567  C CA  . GLY A 864  ? 2.6786 2.8128 3.1480 1.0676  -1.5736 -1.3857 864  GLY A CA  
6568  C C   . GLY A 864  ? 2.5294 2.6839 3.0241 1.0741  -1.5220 -1.3580 864  GLY A C   
6569  O O   . GLY A 864  ? 2.4761 2.6823 3.0083 1.1098  -1.5056 -1.3804 864  GLY A O   
6570  N N   . ILE A 865  ? 2.6997 2.8155 3.1764 1.0398  -1.4942 -1.3094 865  ILE A N   
6571  C CA  . ILE A 865  ? 2.5567 2.6807 3.0593 1.0432  -1.4492 -1.2862 865  ILE A CA  
6572  C C   . ILE A 865  ? 2.6284 2.6478 3.1250 1.0353  -1.4906 -1.3057 865  ILE A C   
6573  O O   . ILE A 865  ? 2.7219 2.6483 3.1817 1.0121  -1.5416 -1.3128 865  ILE A O   
6574  C CB  . ILE A 865  ? 2.4325 2.5794 2.9254 1.0148  -1.3915 -1.2245 865  ILE A CB  
6575  C CG1 . ILE A 865  ? 2.3901 2.6129 2.8710 1.0136  -1.3708 -1.2071 865  ILE A CG1 
6576  C CG2 . ILE A 865  ? 2.2947 2.4992 2.8308 1.0319  -1.3292 -1.2054 865  ILE A CG2 
6577  C CD1 . ILE A 865  ? 2.2862 2.5564 2.7660 0.9949  -1.3044 -1.1475 865  ILE A CD1 
6578  N N   . CYS A 866  ? 2.6630 2.7001 3.1979 1.0567  -1.4682 -1.3157 866  CYS A N   
6579  C CA  . CYS A 866  ? 2.7845 2.7350 3.3195 1.0556  -1.5049 -1.3382 866  CYS A CA  
6580  C C   . CYS A 866  ? 2.8476 2.7563 3.3759 1.0270  -1.4744 -1.2963 866  CYS A C   
6581  O O   . CYS A 866  ? 2.6967 2.6649 3.2409 1.0195  -1.4128 -1.2563 866  CYS A O   
6582  C CB  . CYS A 866  ? 2.7167 2.7119 3.3017 1.0977  -1.5023 -1.3803 866  CYS A CB  
6583  S SG  . CYS A 866  ? 2.8949 2.7970 3.4699 1.1108  -1.5831 -1.4379 866  CYS A SG  
6584  N N   . THR A 867  ? 3.4304 3.2382 3.9353 1.0125  -1.5168 -1.3054 867  THR A N   
6585  C CA  . THR A 867  ? 3.4806 3.2448 3.9776 0.9870  -1.4925 -1.2696 867  THR A CA  
6586  C C   . THR A 867  ? 3.6020 3.2726 4.0881 0.9871  -1.5382 -1.2936 867  THR A C   
6587  O O   . THR A 867  ? 3.6425 3.2856 4.1345 1.0108  -1.5859 -1.3406 867  THR A O   
6588  C CB  . THR A 867  ? 3.3477 3.0795 3.7985 0.9454  -1.4804 -1.2185 867  THR A CB  
6589  O OG1 . THR A 867  ? 3.4254 3.1702 3.8524 0.9417  -1.5027 -1.2233 867  THR A OG1 
6590  C CG2 . THR A 867  ? 3.2707 3.0714 3.7431 0.9342  -1.4055 -1.1711 867  THR A CG2 
6591  N N   . SER A 868  ? 3.1993 2.8226 3.6686 0.9611  -1.5225 -1.2601 868  SER A N   
6592  C CA  . SER A 868  ? 3.3216 2.8675 3.7843 0.9627  -1.5556 -1.2782 868  SER A CA  
6593  C C   . SER A 868  ? 3.5259 2.9599 3.9240 0.9352  -1.6049 -1.2643 868  SER A C   
6594  O O   . SER A 868  ? 3.5135 2.8734 3.8966 0.9420  -1.6487 -1.2874 868  SER A O   
6595  C CB  . SER A 868  ? 3.2231 2.8006 3.7211 0.9592  -1.5024 -1.2574 868  SER A CB  
6596  O OG  . SER A 868  ? 3.2044 2.8889 3.7601 0.9805  -1.4480 -1.2599 868  SER A OG  
6597  N N   . GLU A 869  ? 4.2582 3.6809 4.6190 0.9056  -1.5967 -1.2265 869  GLU A N   
6598  C CA  . GLU A 869  ? 4.4611 3.7814 4.7622 0.8806  -1.6431 -1.2140 869  GLU A CA  
6599  C C   . GLU A 869  ? 4.5556 3.8921 4.8209 0.8343  -1.5985 -1.1848 869  GLU A C   
6600  O O   . GLU A 869  ? 4.5684 3.9881 4.8539 0.8317  -1.5558 -1.1820 869  GLU A O   
6601  C CB  . GLU A 869  ? 4.5002 3.8254 4.7712 0.8435  -1.6118 -1.1607 869  GLU A CB  
6602  C CG  . GLU A 869  ? 4.5476 3.7653 4.7582 0.8124  -1.6472 -1.1364 869  GLU A CG  
6603  C CD  . GLU A 869  ? 4.6219 3.8270 4.8024 0.7891  -1.6572 -1.1302 869  GLU A CD  
6604  O OE1 . GLU A 869  ? 4.6373 3.9318 4.8366 0.7832  -1.6163 -1.1269 869  GLU A OE1 
6605  O OE2 . GLU A 869  ? 4.6486 3.7635 4.7841 0.7668  -1.6876 -1.1175 869  GLU A OE2 
6606  N N   . SER A 870  ? 3.6039 2.7920 3.8522 0.8889  -1.7546 -1.2640 870  SER A N   
6607  C CA  . SER A 870  ? 3.7442 2.8982 3.9846 0.9049  -1.8104 -1.3057 870  SER A CA  
6608  C C   . SER A 870  ? 3.8458 3.0418 4.0829 0.8931  -1.8038 -1.2988 870  SER A C   
6609  O O   . SER A 870  ? 3.8810 3.0553 4.0879 0.8602  -1.7901 -1.2587 870  SER A O   
6610  C CB  . SER A 870  ? 3.8041 2.8347 3.9969 0.8955  -1.8649 -1.3078 870  SER A CB  
6611  O OG  . SER A 870  ? 3.8665 2.8468 4.0173 0.8611  -1.8692 -1.2721 870  SER A OG  
6612  N N   . LYS A 882  ? 3.8585 3.1282 4.0390 0.7230  -1.4942 -0.9748 882  LYS A N   
6613  C CA  . LYS A 882  ? 3.8229 3.0100 3.9781 0.7144  -1.5112 -0.9666 882  LYS A CA  
6614  C C   . LYS A 882  ? 3.7129 2.9156 3.8671 0.6898  -1.4566 -0.9178 882  LYS A C   
6615  O O   . LYS A 882  ? 3.6673 2.9575 3.8577 0.6899  -1.4009 -0.9004 882  LYS A O   
6616  C CB  . LYS A 882  ? 3.8142 2.9964 3.9992 0.7493  -1.5365 -1.0152 882  LYS A CB  
6617  C CG  . LYS A 882  ? 3.7629 3.0379 4.0096 0.7691  -1.4861 -1.0243 882  LYS A CG  
6618  C CD  . LYS A 882  ? 3.7511 3.0153 4.0273 0.8025  -1.5148 -1.0744 882  LYS A CD  
6619  C CE  . LYS A 882  ? 3.8462 3.1058 4.1269 0.8293  -1.5641 -1.1222 882  LYS A CE  
6620  N NZ  . LYS A 882  ? 3.8231 3.0702 4.1316 0.8622  -1.5940 -1.1716 882  LYS A NZ  
6621  N N   . CYS A 883  ? 4.5897 3.7076 4.7024 0.6702  -1.4721 -0.8956 883  CYS A N   
6622  C CA  . CYS A 883  ? 4.4968 3.6187 4.6017 0.6438  -1.4246 -0.8477 883  CYS A CA  
6623  C C   . CYS A 883  ? 4.3668 3.4960 4.5003 0.6572  -1.4077 -0.8588 883  CYS A C   
6624  O O   . CYS A 883  ? 4.3483 3.4013 4.4521 0.6558  -1.4378 -0.8620 883  CYS A O   
6625  C CB  . CYS A 883  ? 4.5299 3.5588 4.5700 0.6108  -1.4453 -0.8100 883  CYS A CB  
6626  S SG  . CYS A 883  ? 5.1421 4.1749 5.1665 0.5743  -1.3872 -0.7463 883  CYS A SG  
6627  N N   . VAL A 884  ? 3.9692 3.1919 4.1616 0.6708  -1.3580 -0.8644 884  VAL A N   
6628  C CA  . VAL A 884  ? 3.8597 3.1030 4.0916 0.6834  -1.3344 -0.8770 884  VAL A CA  
6629  C C   . VAL A 884  ? 3.8115 3.0763 4.0467 0.6558  -1.2761 -0.8280 884  VAL A C   
6630  O O   . VAL A 884  ? 3.7676 3.1174 4.0541 0.6593  -1.2181 -0.8179 884  VAL A O   
6631  C CB  . VAL A 884  ? 3.3861 2.7200 3.6885 0.7167  -1.3114 -0.9143 884  VAL A CB  
6632  C CG1 . VAL A 884  ? 3.4306 2.7374 3.7351 0.7475  -1.3710 -0.9693 884  VAL A CG1 
6633  C CG2 . VAL A 884  ? 3.4172 2.8371 3.7415 0.7131  -1.2657 -0.8920 884  VAL A CG2 
6634  N N   . ARG A 885  ? 3.6407 2.8285 3.8222 0.6295  -1.2897 -0.7970 885  ARG A N   
6635  C CA  . ARG A 885  ? 3.5811 2.7854 3.7582 0.5994  -1.2358 -0.7456 885  ARG A CA  
6636  C C   . ARG A 885  ? 3.4664 2.7188 3.6974 0.6071  -1.1908 -0.7506 885  ARG A C   
6637  O O   . ARG A 885  ? 3.4122 2.6404 3.6581 0.6258  -1.2144 -0.7855 885  ARG A O   
6638  C CB  . ARG A 885  ? 3.6030 2.7146 3.7086 0.5685  -1.2585 -0.7082 885  ARG A CB  
6639  C CG  . ARG A 885  ? 3.5819 2.6071 3.6546 0.5748  -1.3029 -0.7247 885  ARG A CG  
6640  C CD  . ARG A 885  ? 3.5975 2.5436 3.6037 0.5420  -1.3088 -0.6773 885  ARG A CD  
6641  N NE  . ARG A 885  ? 3.6872 2.6062 3.6525 0.5205  -1.3204 -0.6495 885  ARG A NE  
6642  C CZ  . ARG A 885  ? 3.7281 2.5784 3.6357 0.4915  -1.3274 -0.6081 885  ARG A CZ  
6643  N NH1 . ARG A 885  ? 3.6905 2.4908 3.5697 0.4811  -1.3248 -0.5879 885  ARG A NH1 
6644  N NH2 . ARG A 885  ? 3.8044 2.6369 3.6838 0.4733  -1.3368 -0.5877 885  ARG A NH2 
6645  N N   . GLN A 886  ? 3.0243 2.3466 3.2861 0.5926  -1.1249 -0.7157 886  GLN A N   
6646  C CA  . GLN A 886  ? 2.9529 2.3326 3.2757 0.5989  -1.0725 -0.7180 886  GLN A CA  
6647  C C   . GLN A 886  ? 2.8515 2.2324 3.1596 0.5645  -1.0233 -0.6624 886  GLN A C   
6648  O O   . GLN A 886  ? 2.8898 2.2236 3.1391 0.5374  -1.0340 -0.6249 886  GLN A O   
6649  C CB  . GLN A 886  ? 3.0285 2.5095 3.4191 0.6224  -1.0319 -0.7343 886  GLN A CB  
6650  C CG  . GLN A 886  ? 3.0331 2.5703 3.4994 0.6422  -0.9934 -0.7594 886  GLN A CG  
6651  C CD  . GLN A 886  ? 3.0908 2.6246 3.5858 0.6778  -1.0362 -0.8206 886  GLN A CD  
6652  O OE1 . GLN A 886  ? 3.0700 2.6569 3.6334 0.6989  -1.0081 -0.8482 886  GLN A OE1 
6653  N NE2 . GLN A 886  ? 3.1572 2.6284 3.6023 0.6848  -1.1037 -0.8425 886  GLN A NE2 
6654  N N   . LYS A 887  ? 3.1646 2.5985 3.5282 0.5652  -0.9687 -0.6576 887  LYS A N   
6655  C CA  . LYS A 887  ? 3.0962 2.5328 3.4512 0.5340  -0.9203 -0.6076 887  LYS A CA  
6656  C C   . LYS A 887  ? 3.0151 2.5526 3.4384 0.5364  -0.8426 -0.5897 887  LYS A C   
6657  O O   . LYS A 887  ? 2.9329 2.5281 3.4236 0.5629  -0.8216 -0.6229 887  LYS A O   
6658  C CB  . LYS A 887  ? 3.0452 2.4270 3.3918 0.5282  -0.9336 -0.6163 887  LYS A CB  
6659  C CG  . LYS A 887  ? 3.0895 2.3823 3.3874 0.5406  -1.0118 -0.6511 887  LYS A CG  
6660  C CD  . LYS A 887  ? 3.0859 2.4004 3.4355 0.5784  -1.0360 -0.7139 887  LYS A CD  
6661  C CE  . LYS A 887  ? 3.1215 2.3508 3.4234 0.5943  -1.1144 -0.7496 887  LYS A CE  
6662  N NZ  . LYS A 887  ? 3.0663 2.2449 3.3534 0.5931  -1.1313 -0.7589 887  LYS A NZ  
6663  N N   . VAL A 888  ? 2.3690 1.9270 2.7749 0.5092  -0.7990 -0.5360 888  VAL A N   
6664  C CA  . VAL A 888  ? 2.3298 1.9807 2.7944 0.5095  -0.7216 -0.5108 888  VAL A CA  
6665  C C   . VAL A 888  ? 2.2980 1.9477 2.7728 0.4838  -0.6729 -0.4748 888  VAL A C   
6666  O O   . VAL A 888  ? 2.3415 1.9452 2.7610 0.4532  -0.6759 -0.4347 888  VAL A O   
6667  C CB  . VAL A 888  ? 2.3458 2.0369 2.7882 0.5012  -0.7023 -0.4754 888  VAL A CB  
6668  C CG1 . VAL A 888  ? 2.3936 2.1247 2.8548 0.5333  -0.7253 -0.5118 888  VAL A CG1 
6669  C CG2 . VAL A 888  ? 2.3792 1.9948 2.7392 0.4699  -0.7387 -0.4433 888  VAL A CG2 
6670  N N   . GLU A 889  ? 2.2648 1.9660 2.8130 0.4961  -0.6266 -0.4894 889  GLU A N   
6671  C CA  . GLU A 889  ? 2.2619 1.9748 2.8313 0.4731  -0.5716 -0.4559 889  GLU A CA  
6672  C C   . GLU A 889  ? 2.2493 2.0022 2.8026 0.4513  -0.5211 -0.3964 889  GLU A C   
6673  O O   . GLU A 889  ? 2.2455 2.0573 2.8134 0.4647  -0.5016 -0.3891 889  GLU A O   
6674  C CB  . GLU A 889  ? 2.3277 2.1009 2.9903 0.4923  -0.5239 -0.4833 889  GLU A CB  
6675  C CG  . GLU A 889  ? 2.4878 2.3487 3.2151 0.5215  -0.4870 -0.4974 889  GLU A CG  
6676  C CD  . GLU A 889  ? 2.6462 2.4980 3.3814 0.5543  -0.5427 -0.5545 889  GLU A CD  
6677  O OE1 . GLU A 889  ? 2.7006 2.4787 3.3951 0.5556  -0.6095 -0.5854 889  GLU A OE1 
6678  O OE2 . GLU A 889  ? 2.7045 2.6240 3.4867 0.5801  -0.5185 -0.5679 889  GLU A OE2 
6679  N N   . GLY A 890  ? 2.9697 2.6910 3.4915 0.4189  -0.5012 -0.3544 890  GLY A N   
6680  C CA  . GLY A 890  ? 2.9604 2.7064 3.4550 0.3946  -0.4615 -0.2962 890  GLY A CA  
6681  C C   . GLY A 890  ? 2.8485 2.6965 3.4066 0.4063  -0.3869 -0.2759 890  GLY A C   
6682  O O   . GLY A 890  ? 2.7775 2.6747 3.4089 0.4206  -0.3416 -0.2905 890  GLY A O   
6683  N N   . SER A 891  ? 2.9047 2.7863 3.4364 0.4013  -0.3731 -0.2426 891  SER A N   
6684  C CA  . SER A 891  ? 2.7229 2.7005 3.3068 0.4110  -0.2983 -0.2146 891  SER A CA  
6685  C C   . SER A 891  ? 2.6343 2.6735 3.2914 0.4503  -0.2820 -0.2567 891  SER A C   
6686  O O   . SER A 891  ? 2.5423 2.6373 3.2694 0.4591  -0.2191 -0.2519 891  SER A O   
6687  C CB  . SER A 891  ? 2.6081 2.5999 3.2202 0.3880  -0.2336 -0.1759 891  SER A CB  
6688  O OG  . SER A 891  ? 2.6901 2.5986 3.2463 0.3560  -0.2650 -0.1616 891  SER A OG  
6689  N N   . SER A 892  ? 2.3558 2.3841 2.9993 0.4740  -0.3375 -0.2982 892  SER A N   
6690  C CA  . SER A 892  ? 2.2807 2.3679 2.9912 0.5128  -0.3245 -0.3387 892  SER A CA  
6691  C C   . SER A 892  ? 2.3371 2.4265 3.0204 0.5364  -0.3783 -0.3695 892  SER A C   
6692  O O   . SER A 892  ? 2.3447 2.4434 2.9819 0.5301  -0.3889 -0.3457 892  SER A O   
6693  C CB  . SER A 892  ? 2.2773 2.3358 3.0340 0.5219  -0.3364 -0.3830 892  SER A CB  
6694  O OG  . SER A 892  ? 2.1972 2.2753 3.0008 0.5073  -0.2746 -0.3604 892  SER A OG  
6695  N N   . SER A 893  ? 2.2089 2.2912 2.9233 0.5639  -0.4120 -0.4242 893  SER A N   
6696  C CA  . SER A 893  ? 2.2763 2.3585 2.9691 0.5880  -0.4652 -0.4587 893  SER A CA  
6697  C C   . SER A 893  ? 2.3392 2.3902 3.0573 0.6128  -0.5138 -0.5216 893  SER A C   
6698  O O   . SER A 893  ? 2.2818 2.3597 3.0663 0.6278  -0.4841 -0.5439 893  SER A O   
6699  C CB  . SER A 893  ? 2.1876 2.3678 2.9122 0.6127  -0.4184 -0.4448 893  SER A CB  
6700  O OG  . SER A 893  ? 2.2430 2.4203 2.9294 0.6280  -0.4705 -0.4666 893  SER A OG  
6701  N N   . HIS A 894  ? 1.8523 1.8451 2.5180 0.6165  -0.5889 -0.5504 894  HIS A N   
6702  C CA  . HIS A 894  ? 2.0209 1.9840 2.7034 0.6421  -0.6412 -0.6104 894  HIS A CA  
6703  C C   . HIS A 894  ? 1.8214 1.8304 2.5108 0.6732  -0.6595 -0.6359 894  HIS A C   
6704  O O   . HIS A 894  ? 1.8506 1.8428 2.4858 0.6677  -0.6944 -0.6279 894  HIS A O   
6705  C CB  . HIS A 894  ? 2.5702 2.4261 3.1878 0.6247  -0.7150 -0.6259 894  HIS A CB  
6706  C CG  . HIS A 894  ? 3.1294 2.9482 3.7749 0.6403  -0.7468 -0.6749 894  HIS A CG  
6707  N ND1 . HIS A 894  ? 3.4971 3.2612 4.1158 0.6568  -0.8195 -0.7204 894  HIS A ND1 
6708  C CD2 . HIS A 894  ? 3.3200 3.1503 4.0195 0.6425  -0.7158 -0.6870 894  HIS A CD2 
6709  C CE1 . HIS A 894  ? 3.7313 3.4757 4.3843 0.6693  -0.8326 -0.7579 894  HIS A CE1 
6710  N NE2 . HIS A 894  ? 3.5193 3.3038 4.2227 0.6607  -0.7709 -0.7398 894  HIS A NE2 
6711  N N   . LEU A 895  ? 2.7633 2.8328 3.5224 0.7059  -0.6333 -0.6668 895  LEU A N   
6712  C CA  . LEU A 895  ? 2.6869 2.8057 3.4604 0.7396  -0.6470 -0.6948 895  LEU A CA  
6713  C C   . LEU A 895  ? 2.6966 2.7442 3.4112 0.7413  -0.7332 -0.7281 895  LEU A C   
6714  O O   . LEU A 895  ? 2.7762 2.7393 3.4553 0.7248  -0.7810 -0.7404 895  LEU A O   
6715  C CB  . LEU A 895  ? 2.6516 2.8206 3.5068 0.7736  -0.6212 -0.7335 895  LEU A CB  
6716  C CG  . LEU A 895  ? 2.5714 2.8469 3.4845 0.7972  -0.5474 -0.7148 895  LEU A CG  
6717  C CD1 . LEU A 895  ? 2.4860 2.8004 3.4852 0.8091  -0.4907 -0.7249 895  LEU A CD1 
6718  C CD2 . LEU A 895  ? 2.5923 2.9058 3.5051 0.8317  -0.5748 -0.7459 895  LEU A CD2 
6719  N N   . VAL A 896  ? 2.1079 2.1897 2.8122 0.7623  -0.7527 -0.7428 896  VAL A N   
6720  C CA  . VAL A 896  ? 2.1176 2.1361 2.7728 0.7666  -0.8328 -0.7777 896  VAL A CA  
6721  C C   . VAL A 896  ? 2.0803 2.1525 2.7738 0.8080  -0.8435 -0.8217 896  VAL A C   
6722  O O   . VAL A 896  ? 1.9902 2.1502 2.7369 0.8298  -0.7866 -0.8152 896  VAL A O   
6723  C CB  . VAL A 896  ? 2.1185 2.1123 2.7054 0.7423  -0.8553 -0.7463 896  VAL A CB  
6724  C CG1 . VAL A 896  ? 2.2495 2.1582 2.7839 0.7400  -0.9392 -0.7796 896  VAL A CG1 
6725  C CG2 . VAL A 896  ? 2.0670 2.0351 2.6264 0.7031  -0.8226 -0.6920 896  VAL A CG2 
6726  N N   . THR A 897  ? 2.1206 2.1401 2.7891 0.8203  -0.9143 -0.8661 897  THR A N   
6727  C CA  . THR A 897  ? 2.0731 2.1406 2.7694 0.8587  -0.9305 -0.9077 897  THR A CA  
6728  C C   . THR A 897  ? 2.2119 2.2136 2.8587 0.8624  -1.0127 -0.9436 897  THR A C   
6729  O O   . THR A 897  ? 2.3151 2.2255 2.9202 0.8430  -1.0620 -0.9502 897  THR A O   
6730  C CB  . THR A 897  ? 1.9715 2.0727 2.7407 0.8894  -0.9113 -0.9455 897  THR A CB  
6731  O OG1 . THR A 897  ? 2.0701 2.1004 2.8275 0.8987  -0.9800 -0.9950 897  THR A OG1 
6732  C CG2 . THR A 897  ? 1.8688 1.9889 2.6832 0.8766  -0.8491 -0.9196 897  THR A CG2 
6733  N N   . PHE A 898  ? 2.2400 2.2906 2.8929 0.8888  -1.0251 -0.9664 898  PHE A N   
6734  C CA  . PHE A 898  ? 2.3367 2.3393 2.9555 0.8994  -1.0989 -1.0073 898  PHE A CA  
6735  C C   . PHE A 898  ? 2.2923 2.3688 2.9548 0.9422  -1.0951 -1.0455 898  PHE A C   
6736  O O   . PHE A 898  ? 2.1868 2.3531 2.8732 0.9571  -1.0467 -1.0282 898  PHE A O   
6737  C CB  . PHE A 898  ? 2.4031 2.3836 2.9621 0.8766  -1.1232 -0.9841 898  PHE A CB  
6738  C CG  . PHE A 898  ? 2.4468 2.3452 2.9554 0.8349  -1.1367 -0.9495 898  PHE A CG  
6739  C CD1 . PHE A 898  ? 2.5564 2.3617 3.0121 0.8199  -1.2041 -0.9640 898  PHE A CD1 
6740  C CD2 . PHE A 898  ? 2.3646 2.2790 2.8792 0.8114  -1.0805 -0.9014 898  PHE A CD2 
6741  C CE1 . PHE A 898  ? 2.5470 2.2770 2.9560 0.7831  -1.2146 -0.9306 898  PHE A CE1 
6742  C CE2 . PHE A 898  ? 2.4189 2.2591 2.8869 0.7741  -1.0920 -0.8693 898  PHE A CE2 
6743  C CZ  . PHE A 898  ? 2.5014 2.2492 2.9157 0.7601  -1.1590 -0.8832 898  PHE A CZ  
6744  N N   . THR A 899  ? 1.9573 1.9967 2.6286 0.9634  -1.1464 -1.0971 899  THR A N   
6745  C CA  . THR A 899  ? 1.9031 2.0060 2.6124 1.0043  -1.1490 -1.1364 899  THR A CA  
6746  C C   . THR A 899  ? 1.9624 2.0415 2.6290 1.0104  -1.2101 -1.1625 899  THR A C   
6747  O O   . THR A 899  ? 2.0503 2.0404 2.6672 0.9887  -1.2660 -1.1682 899  THR A O   
6748  C CB  . THR A 899  ? 1.9213 2.0125 2.6787 1.0286  -1.1602 -1.1798 899  THR A CB  
6749  O OG1 . THR A 899  ? 2.0447 2.0315 2.7670 1.0123  -1.2204 -1.1987 899  THR A OG1 
6750  C CG2 . THR A 899  ? 1.7518 1.8940 2.5676 1.0300  -1.0883 -1.1578 899  THR A CG2 
6751  N N   . VAL A 900  ? 2.1731 2.3335 2.8607 1.0404  -1.1967 -1.1774 900  VAL A N   
6752  C CA  . VAL A 900  ? 2.2431 2.4005 2.8999 1.0511  -1.2474 -1.2053 900  VAL A CA  
6753  C C   . VAL A 900  ? 2.1689 2.4107 2.8689 1.0970  -1.2371 -1.2409 900  VAL A C   
6754  O O   . VAL A 900  ? 2.0742 2.3788 2.8278 1.1200  -1.1869 -1.2400 900  VAL A O   
6755  C CB  . VAL A 900  ? 2.0449 2.2235 2.6606 1.0285  -1.2363 -1.1676 900  VAL A CB  
6756  C CG1 . VAL A 900  ? 2.1544 2.2318 2.7140 0.9863  -1.2758 -1.1489 900  VAL A CG1 
6757  C CG2 . VAL A 900  ? 1.9173 2.1801 2.5575 1.0268  -1.1562 -1.1195 900  VAL A CG2 
6758  N N   . LEU A 901  ? 2.1692 2.4120 2.8468 1.1103  -1.2840 -1.2722 901  LEU A N   
6759  C CA  . LEU A 901  ? 2.2033 2.5222 2.9148 1.1545  -1.2824 -1.3093 901  LEU A CA  
6760  C C   . LEU A 901  ? 2.3523 2.6740 3.0286 1.1598  -1.3305 -1.3331 901  LEU A C   
6761  O O   . LEU A 901  ? 2.4986 2.7432 3.1490 1.1535  -1.3967 -1.3668 901  LEU A O   
6762  C CB  . LEU A 901  ? 2.1952 2.4861 2.9431 1.1789  -1.3074 -1.3555 901  LEU A CB  
6763  C CG  . LEU A 901  ? 2.2279 2.5574 2.9966 1.2204  -1.3369 -1.4081 901  LEU A CG  
6764  C CD1 . LEU A 901  ? 2.1331 2.5046 2.9649 1.2527  -1.3058 -1.4293 901  LEU A CD1 
6765  C CD2 . LEU A 901  ? 2.3753 2.6135 3.1078 1.2139  -1.4203 -1.4491 901  LEU A CD2 
6766  N N   . PRO A 902  ? 2.0255 2.4373 2.7017 1.1720  -1.2963 -1.3157 902  PRO A N   
6767  C CA  . PRO A 902  ? 2.1037 2.5375 2.7497 1.1764  -1.3305 -1.3325 902  PRO A CA  
6768  C C   . PRO A 902  ? 2.1618 2.6436 2.8305 1.2207  -1.3568 -1.3863 902  PRO A C   
6769  O O   . PRO A 902  ? 2.0777 2.6251 2.7908 1.2558  -1.3211 -1.3962 902  PRO A O   
6770  C CB  . PRO A 902  ? 2.0305 2.5533 2.6735 1.1738  -1.2691 -1.2851 902  PRO A CB  
6771  C CG  . PRO A 902  ? 1.8405 2.3744 2.5088 1.1628  -1.2047 -1.2402 902  PRO A CG  
6772  C CD  . PRO A 902  ? 1.8463 2.3458 2.5516 1.1795  -1.2154 -1.2717 902  PRO A CD  
6773  N N   . LEU A 903  ? 2.4343 2.8837 3.0739 1.2185  -1.4175 -1.4201 903  LEU A N   
6774  C CA  . LEU A 903  ? 2.5007 2.9881 3.1561 1.2576  -1.4507 -1.4742 903  LEU A CA  
6775  C C   . LEU A 903  ? 2.5451 3.0953 3.1795 1.2630  -1.4560 -1.4767 903  LEU A C   
6776  O O   . LEU A 903  ? 2.5642 3.1780 3.2125 1.2995  -1.4684 -1.5139 903  LEU A O   
6777  C CB  . LEU A 903  ? 2.6162 3.0008 3.2578 1.2509  -1.5258 -1.5197 903  LEU A CB  
6778  C CG  . LEU A 903  ? 2.6252 2.9196 3.2702 1.2322  -1.5346 -1.5131 903  LEU A CG  
6779  C CD1 . LEU A 903  ? 2.4917 2.8470 3.1847 1.2546  -1.4743 -1.4992 903  LEU A CD1 
6780  C CD2 . LEU A 903  ? 2.6505 2.8689 3.2556 1.1831  -1.5361 -1.4696 903  LEU A CD2 
6781  N N   . GLU A 904  ? 2.6960 3.2265 3.2966 1.2260  -1.4484 -1.4383 904  GLU A N   
6782  C CA  . GLU A 904  ? 2.7689 3.3626 3.3499 1.2266  -1.4464 -1.4336 904  GLU A CA  
6783  C C   . GLU A 904  ? 2.6092 3.3107 3.2033 1.2395  -1.3696 -1.3874 904  GLU A C   
6784  O O   . GLU A 904  ? 2.5302 3.2192 3.1152 1.2109  -1.3294 -1.3359 904  GLU A O   
6785  C CB  . GLU A 904  ? 2.9444 3.4550 3.4826 1.1798  -1.4856 -1.4222 904  GLU A CB  
6786  C CG  . GLU A 904  ? 3.1496 3.5536 3.6747 1.1690  -1.5606 -1.4670 904  GLU A CG  
6787  C CD  . GLU A 904  ? 3.3472 3.7038 3.8386 1.1394  -1.6060 -1.4755 904  GLU A CD  
6788  O OE1 . GLU A 904  ? 3.3504 3.7520 3.8268 1.1234  -1.5808 -1.4454 904  GLU A OE1 
6789  O OE2 . GLU A 904  ? 3.4851 3.7587 3.9670 1.1325  -1.6665 -1.5130 904  GLU A OE2 
6790  N N   . ILE A 905  ? 2.2750 3.0820 2.8902 1.2845  -1.3502 -1.4069 905  ILE A N   
6791  C CA  . ILE A 905  ? 2.0514 2.9728 2.6845 1.3092  -1.2758 -1.3689 905  ILE A CA  
6792  C C   . ILE A 905  ? 1.9800 2.9405 2.5815 1.2890  -1.2599 -1.3352 905  ILE A C   
6793  O O   . ILE A 905  ? 1.9583 2.9208 2.5364 1.2850  -1.3041 -1.3621 905  ILE A O   
6794  C CB  . ILE A 905  ? 1.8247 2.8473 2.4873 1.3676  -1.2638 -1.4031 905  ILE A CB  
6795  C CG1 . ILE A 905  ? 1.9256 2.9027 2.6175 1.3874  -1.2937 -1.4473 905  ILE A CG1 
6796  C CG2 . ILE A 905  ? 1.7386 2.8703 2.4247 1.3954  -1.1804 -1.3598 905  ILE A CG2 
6797  C CD1 . ILE A 905  ? 1.8179 2.8919 2.5501 1.4430  -1.2574 -1.4638 905  ILE A CD1 
6798  N N   . GLY A 906  ? 2.4020 3.3946 3.0053 1.2764  -1.1962 -1.2774 906  GLY A N   
6799  C CA  . GLY A 906  ? 2.4799 3.4985 3.0525 1.2516  -1.1794 -1.2402 906  GLY A CA  
6800  C C   . GLY A 906  ? 2.5863 3.4923 3.1279 1.1941  -1.2074 -1.2193 906  GLY A C   
6801  O O   . GLY A 906  ? 2.5433 3.4605 3.0655 1.1678  -1.1770 -1.1738 906  GLY A O   
6802  N N   . LEU A 907  ? 2.2627 3.0612 2.7993 1.1756  -1.2631 -1.2503 907  LEU A N   
6803  C CA  . LEU A 907  ? 2.3811 3.0670 2.8848 1.1230  -1.2957 -1.2336 907  LEU A CA  
6804  C C   . LEU A 907  ? 2.3344 3.0027 2.8336 1.0929  -1.2420 -1.1716 907  LEU A C   
6805  O O   . LEU A 907  ? 2.2427 2.9165 2.7688 1.1024  -1.2026 -1.1547 907  LEU A O   
6806  C CB  . LEU A 907  ? 2.5060 3.0798 3.0067 1.1127  -1.3581 -1.2733 907  LEU A CB  
6807  C CG  . LEU A 907  ? 2.6623 3.1184 3.1275 1.0606  -1.3894 -1.2533 907  LEU A CG  
6808  C CD1 . LEU A 907  ? 2.7453 3.2044 3.1794 1.0347  -1.4050 -1.2427 907  LEU A CD1 
6809  C CD2 . LEU A 907  ? 2.8115 3.1618 3.2718 1.0555  -1.4533 -1.2947 907  LEU A CD2 
6810  N N   . HIS A 908  ? 2.7019 3.3464 3.1684 1.0556  -1.2423 -1.1399 908  HIS A N   
6811  C CA  . HIS A 908  ? 2.6718 3.3170 3.1308 1.0278  -1.1874 -1.0780 908  HIS A CA  
6812  C C   . HIS A 908  ? 2.7523 3.2756 3.1795 0.9768  -1.2181 -1.0604 908  HIS A C   
6813  O O   . HIS A 908  ? 2.8735 3.3066 3.2912 0.9674  -1.2749 -1.0940 908  HIS A O   
6814  C CB  . HIS A 908  ? 2.6523 3.3887 3.0991 1.0291  -1.1523 -1.0487 908  HIS A CB  
6815  C CG  . HIS A 908  ? 2.5901 3.4335 3.0513 1.0754  -1.1526 -1.0816 908  HIS A CG  
6816  N ND1 . HIS A 908  ? 2.6517 3.4863 3.1048 1.0861  -1.2145 -1.1359 908  HIS A ND1 
6817  C CD2 . HIS A 908  ? 2.4586 3.4219 2.9404 1.1140  -1.0969 -1.0661 908  HIS A CD2 
6818  C CE1 . HIS A 908  ? 2.5963 3.5419 3.0640 1.1299  -1.1986 -1.1545 908  HIS A CE1 
6819  N NE2 . HIS A 908  ? 2.4764 3.5016 2.9606 1.1484  -1.1273 -1.1120 908  HIS A NE2 
6820  N N   . ASN A 909  ? 2.5769 3.1004 2.9869 0.9458  -1.1789 -1.0063 909  ASN A N   
6821  C CA  . ASN A 909  ? 2.6340 3.0520 3.0099 0.8959  -1.2002 -0.9810 909  ASN A CA  
6822  C C   . ASN A 909  ? 2.6008 2.9186 2.9776 0.8817  -1.2179 -0.9838 909  ASN A C   
6823  O O   . ASN A 909  ? 2.6372 2.9047 3.0193 0.8949  -1.2665 -1.0289 909  ASN A O   
6824  C CB  . ASN A 909  ? 2.8260 3.1962 3.1711 0.8754  -1.2599 -1.0055 909  ASN A CB  
6825  C CG  . ASN A 909  ? 2.9783 3.2258 3.2892 0.8269  -1.2881 -0.9846 909  ASN A CG  
6826  O OD1 . ASN A 909  ? 3.1181 3.2864 3.4112 0.8136  -1.3475 -1.0153 909  ASN A OD1 
6827  N ND2 . ASN A 909  ? 2.9426 3.1742 3.2451 0.8015  -1.2439 -0.9319 909  ASN A ND2 
6828  N N   . ILE A 910  ? 2.3888 2.6781 2.7593 0.8547  -1.1790 -0.9357 910  ILE A N   
6829  C CA  . ILE A 910  ? 2.3464 2.5338 2.7094 0.8341  -1.1972 -0.9325 910  ILE A CA  
6830  C C   . ILE A 910  ? 2.3609 2.5074 2.6957 0.7908  -1.1706 -0.8770 910  ILE A C   
6831  O O   . ILE A 910  ? 2.3239 2.5301 2.6713 0.7879  -1.1086 -0.8349 910  ILE A O   
6832  C CB  . ILE A 910  ? 2.1556 2.3688 2.5611 0.8612  -1.1660 -0.9405 910  ILE A CB  
6833  C CG1 . ILE A 910  ? 2.1270 2.3484 2.5550 0.8990  -1.2068 -1.0005 910  ILE A CG1 
6834  C CG2 . ILE A 910  ? 2.1450 2.2678 2.5424 0.8356  -1.1689 -0.9238 910  ILE A CG2 
6835  C CD1 . ILE A 910  ? 2.0134 2.2593 2.4867 0.9266  -1.1794 -1.0131 910  ILE A CD1 
6836  N N   . ASN A 911  ? 2.7960 2.8405 3.0922 0.7577  -1.2169 -0.8763 911  ASN A N   
6837  C CA  . ASN A 911  ? 2.7514 2.7452 3.0173 0.7152  -1.1973 -0.8253 911  ASN A CA  
6838  C C   . ASN A 911  ? 2.7450 2.6720 3.0125 0.7040  -1.1879 -0.8104 911  ASN A C   
6839  O O   . ASN A 911  ? 2.7990 2.6480 3.0596 0.7073  -1.2345 -0.8412 911  ASN A O   
6840  C CB  . ASN A 911  ? 2.8443 2.7613 3.0682 0.6843  -1.2481 -0.8284 911  ASN A CB  
6841  C CG  . ASN A 911  ? 2.8172 2.8005 3.0414 0.6932  -1.2591 -0.8456 911  ASN A CG  
6842  O OD1 . ASN A 911  ? 2.8427 2.8678 3.0868 0.7259  -1.2833 -0.8915 911  ASN A OD1 
6843  N ND2 . ASN A 911  ? 2.8235 2.8155 3.0256 0.6640  -1.2427 -0.8102 911  ASN A ND2 
6844  N N   . PHE A 912  ? 2.6330 2.5930 2.9107 0.6923  -1.1276 -0.7646 912  PHE A N   
6845  C CA  . PHE A 912  ? 2.5990 2.5017 2.8794 0.6795  -1.1142 -0.7481 912  PHE A CA  
6846  C C   . PHE A 912  ? 2.6927 2.5237 2.9302 0.6342  -1.1115 -0.7025 912  PHE A C   
6847  O O   . PHE A 912  ? 2.7102 2.5671 2.9288 0.6139  -1.0918 -0.6700 912  PHE A O   
6848  C CB  . PHE A 912  ? 2.3995 2.3846 2.7285 0.6998  -1.0473 -0.7324 912  PHE A CB  
6849  C CG  . PHE A 912  ? 2.2855 2.3188 2.6594 0.7434  -1.0518 -0.7785 912  PHE A CG  
6850  C CD1 . PHE A 912  ? 2.2931 2.2673 2.6784 0.7545  -1.0862 -0.8142 912  PHE A CD1 
6851  C CD2 . PHE A 912  ? 2.1870 2.3262 2.5915 0.7746  -1.0206 -0.7857 912  PHE A CD2 
6852  C CE1 . PHE A 912  ? 2.2254 2.2441 2.6535 0.7942  -1.0895 -0.8565 912  PHE A CE1 
6853  C CE2 . PHE A 912  ? 2.1203 2.3036 2.5664 0.8153  -1.0233 -0.8271 912  PHE A CE2 
6854  C CZ  . PHE A 912  ? 2.1338 2.2561 2.5926 0.8241  -1.0576 -0.8626 912  PHE A CZ  
6855  N N   . SER A 913  ? 2.7716 2.5151 2.9942 0.6199  -1.1305 -0.7008 913  SER A N   
6856  C CA  . SER A 913  ? 2.8409 2.5035 3.0190 0.5789  -1.1351 -0.6614 913  SER A CA  
6857  C C   . SER A 913  ? 2.8206 2.4333 3.0012 0.5708  -1.1219 -0.6485 913  SER A C   
6858  O O   . SER A 913  ? 2.7757 2.3628 2.9735 0.5925  -1.1465 -0.6848 913  SER A O   
6859  C CB  . SER A 913  ? 2.8973 2.4692 3.0322 0.5647  -1.2023 -0.6803 913  SER A CB  
6860  O OG  . SER A 913  ? 2.8803 2.3670 2.9720 0.5274  -1.2086 -0.6437 913  SER A OG  
6861  N N   . LEU A 914  ? 2.7632 2.3639 2.9273 0.5403  -1.0837 -0.5983 914  LEU A N   
6862  C CA  . LEU A 914  ? 2.7352 2.2863 2.8973 0.5289  -1.0709 -0.5830 914  LEU A CA  
6863  C C   . LEU A 914  ? 2.8593 2.3172 2.9648 0.4906  -1.0904 -0.5492 914  LEU A C   
6864  O O   . LEU A 914  ? 2.9398 2.3915 3.0160 0.4681  -1.0919 -0.5241 914  LEU A O   
6865  C CB  . LEU A 914  ? 2.5703 2.2015 2.7756 0.5316  -0.9969 -0.5545 914  LEU A CB  
6866  C CG  . LEU A 914  ? 2.4934 2.1927 2.6999 0.5140  -0.9397 -0.5055 914  LEU A CG  
6867  C CD1 . LEU A 914  ? 2.4850 2.1195 2.6405 0.4716  -0.9406 -0.4602 914  LEU A CD1 
6868  C CD2 . LEU A 914  ? 2.3360 2.1182 2.5963 0.5268  -0.8689 -0.4883 914  LEU A CD2 
6869  N N   . GLU A 915  ? 3.5803 2.9666 3.6709 0.4842  -1.1054 -0.5492 915  GLU A N   
6870  C CA  . GLU A 915  ? 3.6879 2.9809 3.7228 0.4510  -1.1257 -0.5181 915  GLU A CA  
6871  C C   . GLU A 915  ? 3.6574 2.9363 3.6915 0.4342  -1.0874 -0.4845 915  GLU A C   
6872  O O   . GLU A 915  ? 3.5653 2.8622 3.6332 0.4523  -1.0739 -0.5029 915  GLU A O   
6873  C CB  . GLU A 915  ? 3.7581 2.9530 3.7581 0.4577  -1.1972 -0.5511 915  GLU A CB  
6874  C CG  . GLU A 915  ? 3.9039 3.0805 3.8829 0.4556  -1.2374 -0.5657 915  GLU A CG  
6875  C CD  . GLU A 915  ? 3.9824 3.1800 3.9886 0.4918  -1.2751 -0.6233 915  GLU A CD  
6876  O OE1 . GLU A 915  ? 3.9510 3.1236 3.9694 0.5143  -1.2970 -0.6551 915  GLU A OE1 
6877  O OE2 . GLU A 915  ? 4.0735 3.3134 4.0890 0.4981  -1.2836 -0.6380 915  GLU A OE2 
6878  N N   . THR A 916  ? 3.4462 2.6937 3.4432 0.3993  -1.0698 -0.4362 916  THR A N   
6879  C CA  . THR A 916  ? 3.4648 2.6937 3.4548 0.3796  -1.0343 -0.4004 916  THR A CA  
6880  C C   . THR A 916  ? 3.6179 2.7548 3.5447 0.3463  -1.0567 -0.3659 916  THR A C   
6881  O O   . THR A 916  ? 3.7030 2.8144 3.6004 0.3332  -1.0806 -0.3585 916  THR A O   
6882  C CB  . THR A 916  ? 3.3963 2.7187 3.4225 0.3711  -0.9609 -0.3649 916  THR A CB  
6883  O OG1 . THR A 916  ? 3.3471 2.7551 3.4343 0.4037  -0.9364 -0.3954 916  THR A OG1 
6884  C CG2 . THR A 916  ? 3.3086 2.6088 3.3278 0.3491  -0.9245 -0.3282 916  THR A CG2 
6885  N N   . TRP A 917  ? 4.4356 3.5238 4.3436 0.3334  -1.0481 -0.3457 917  TRP A N   
6886  C CA  . TRP A 917  ? 4.5620 3.5591 4.4091 0.3038  -1.0672 -0.3115 917  TRP A CA  
6887  C C   . TRP A 917  ? 4.6831 3.6877 4.5076 0.2763  -1.0552 -0.2759 917  TRP A C   
6888  O O   . TRP A 917  ? 4.7365 3.6724 4.5200 0.2648  -1.0962 -0.2742 917  TRP A O   
6889  C CB  . TRP A 917  ? 4.5407 3.5240 4.3820 0.2885  -1.0320 -0.2803 917  TRP A CB  
6890  C CG  . TRP A 917  ? 4.6101 3.4854 4.3928 0.2761  -1.0692 -0.2682 917  TRP A CG  
6891  C CD1 . TRP A 917  ? 4.6392 3.4605 4.3738 0.2432  -1.0607 -0.2202 917  TRP A CD1 
6892  C CD2 . TRP A 917  ? 4.6352 3.4424 4.3995 0.2982  -1.1210 -0.3040 917  TRP A CD2 
6893  N NE1 . TRP A 917  ? 4.6618 3.3852 4.3484 0.2443  -1.1030 -0.2228 917  TRP A NE1 
6894  C CE2 . TRP A 917  ? 4.6583 3.3719 4.3614 0.2784  -1.1409 -0.2740 917  TRP A CE2 
6895  C CE3 . TRP A 917  ? 4.6426 3.4601 4.4363 0.3340  -1.1521 -0.3583 917  TRP A CE3 
6896  C CZ2 . TRP A 917  ? 4.6674 3.2987 4.3362 0.2948  -1.1904 -0.2957 917  TRP A CZ2 
6897  C CZ3 . TRP A 917  ? 4.6474 3.3835 4.4082 0.3491  -1.2021 -0.3810 917  TRP A CZ3 
6898  C CH2 . TRP A 917  ? 4.6619 3.3066 4.3601 0.3303  -1.2207 -0.3494 917  TRP A CH2 
6899  N N   . PHE A 918  ? 3.4625 2.5519 3.3161 0.2664  -0.9979 -0.2481 918  PHE A N   
6900  C CA  . PHE A 918  ? 3.5676 2.6728 3.4026 0.2400  -0.9818 -0.2129 918  PHE A CA  
6901  C C   . PHE A 918  ? 3.5425 2.7304 3.4096 0.2557  -0.9772 -0.2331 918  PHE A C   
6902  O O   . PHE A 918  ? 3.5856 2.8169 3.4511 0.2382  -0.9495 -0.2040 918  PHE A O   
6903  C CB  . PHE A 918  ? 3.6148 2.7426 3.4452 0.2112  -0.9232 -0.1573 918  PHE A CB  
6904  C CG  . PHE A 918  ? 3.6026 2.8238 3.4864 0.2242  -0.8639 -0.1525 918  PHE A CG  
6905  C CD1 . PHE A 918  ? 3.6518 2.9715 3.5698 0.2283  -0.8206 -0.1408 918  PHE A CD1 
6906  C CD2 . PHE A 918  ? 3.5400 2.7508 3.4405 0.2320  -0.8491 -0.1580 918  PHE A CD2 
6907  C CE1 . PHE A 918  ? 3.5985 3.0021 3.5668 0.2407  -0.7625 -0.1332 918  PHE A CE1 
6908  C CE2 . PHE A 918  ? 3.4843 2.7793 3.4387 0.2429  -0.7916 -0.1531 918  PHE A CE2 
6909  C CZ  . PHE A 918  ? 3.5131 2.9032 3.5014 0.2472  -0.7472 -0.1394 918  PHE A CZ  
6910  N N   . GLY A 919  ? 3.8775 3.0870 3.7723 0.2893  -1.0058 -0.2836 919  GLY A N   
6911  C CA  . GLY A 919  ? 3.8388 3.1292 3.7640 0.3076  -1.0024 -0.3055 919  GLY A CA  
6912  C C   . GLY A 919  ? 3.7930 3.0856 3.7378 0.3423  -1.0483 -0.3642 919  GLY A C   
6913  O O   . GLY A 919  ? 3.7397 2.9906 3.6884 0.3597  -1.0744 -0.3929 919  GLY A O   
6914  N N   . LYS A 920  ? 3.8802 3.2246 3.8378 0.3530  -1.0579 -0.3827 920  LYS A N   
6915  C CA  . LYS A 920  ? 3.8345 3.1971 3.8150 0.3873  -1.0966 -0.4383 920  LYS A CA  
6916  C C   . LYS A 920  ? 3.8101 3.2736 3.8174 0.3999  -1.0755 -0.4446 920  LYS A C   
6917  O O   . LYS A 920  ? 3.8985 3.3643 3.8859 0.3805  -1.0803 -0.4289 920  LYS A O   
6918  C CB  . LYS A 920  ? 3.8744 3.1352 3.8178 0.3827  -1.1655 -0.4639 920  LYS A CB  
6919  C CG  . LYS A 920  ? 3.8872 3.1549 3.8516 0.4176  -1.2103 -0.5231 920  LYS A CG  
6920  C CD  . LYS A 920  ? 3.9041 3.0588 3.8314 0.4134  -1.2752 -0.5446 920  LYS A CD  
6921  C CE  . LYS A 920  ? 3.9246 3.0859 3.8720 0.4464  -1.3210 -0.6031 920  LYS A CE  
6922  N NZ  . LYS A 920  ? 3.9410 2.9912 3.8564 0.4481  -1.3802 -0.6248 920  LYS A NZ  
6923  N N   . GLU A 921  ? 3.6643 3.2126 3.7180 0.4334  -1.0515 -0.4680 921  GLU A N   
6924  C CA  . GLU A 921  ? 3.5924 3.2517 3.6750 0.4494  -1.0175 -0.4669 921  GLU A CA  
6925  C C   . GLU A 921  ? 3.4822 3.1854 3.5944 0.4894  -1.0465 -0.5225 921  GLU A C   
6926  O O   . GLU A 921  ? 3.4727 3.1455 3.5990 0.5100  -1.0718 -0.5572 921  GLU A O   
6927  C CB  . GLU A 921  ? 3.4926 3.2296 3.6071 0.4526  -0.9438 -0.4313 921  GLU A CB  
6928  C CG  . GLU A 921  ? 3.4626 3.3029 3.5919 0.4559  -0.8968 -0.4061 921  GLU A CG  
6929  C CD  . GLU A 921  ? 3.5108 3.3419 3.6131 0.4177  -0.8622 -0.3489 921  GLU A CD  
6930  O OE1 . GLU A 921  ? 3.6267 3.3640 3.6905 0.3861  -0.8873 -0.3327 921  GLU A OE1 
6931  O OE2 . GLU A 921  ? 3.4330 3.3516 3.5523 0.4207  -0.8090 -0.3193 921  GLU A OE2 
6932  N N   . ILE A 922  ? 3.1453 2.9215 3.2669 0.5012  -1.0430 -0.5318 922  ILE A N   
6933  C CA  . ILE A 922  ? 3.0322 2.8547 3.1803 0.5394  -1.0701 -0.5842 922  ILE A CA  
6934  C C   . ILE A 922  ? 2.8309 2.7817 3.0142 0.5668  -1.0227 -0.5812 922  ILE A C   
6935  O O   . ILE A 922  ? 2.8123 2.8135 2.9870 0.5617  -1.0143 -0.5699 922  ILE A O   
6936  C CB  . ILE A 922  ? 3.1281 2.8992 3.2509 0.5343  -1.1353 -0.6179 922  ILE A CB  
6937  C CG1 . ILE A 922  ? 3.2108 2.8670 3.3132 0.5292  -1.1900 -0.6428 922  ILE A CG1 
6938  C CG2 . ILE A 922  ? 3.1124 2.9630 3.2634 0.5715  -1.1487 -0.6622 922  ILE A CG2 
6939  C CD1 . ILE A 922  ? 3.3060 2.9185 3.3969 0.5365  -1.2550 -0.6885 922  ILE A CD1 
6940  N N   . LEU A 923  ? 2.6055 2.6095 2.8294 0.5973  -0.9916 -0.5921 923  LEU A N   
6941  C CA  . LEU A 923  ? 2.4773 2.6031 2.7377 0.6296  -0.9451 -0.5912 923  LEU A CA  
6942  C C   . LEU A 923  ? 2.4957 2.6561 2.7747 0.6679  -0.9827 -0.6477 923  LEU A C   
6943  O O   . LEU A 923  ? 2.5310 2.6614 2.8285 0.6875  -1.0072 -0.6838 923  LEU A O   
6944  C CB  . LEU A 923  ? 2.3322 2.5010 2.6313 0.6415  -0.8826 -0.5680 923  LEU A CB  
6945  C CG  . LEU A 923  ? 2.2174 2.4897 2.5668 0.6872  -0.8457 -0.5860 923  LEU A CG  
6946  C CD1 . LEU A 923  ? 2.1809 2.5537 2.5316 0.7017  -0.8161 -0.5708 923  LEU A CD1 
6947  C CD2 . LEU A 923  ? 2.1014 2.3967 2.4895 0.6915  -0.7857 -0.5610 923  LEU A CD2 
6948  N N   . VAL A 924  ? 2.2250 2.4500 2.4996 0.6791  -0.9876 -0.6564 924  VAL A N   
6949  C CA  . VAL A 924  ? 2.2113 2.4766 2.5030 0.7164  -1.0222 -0.7102 924  VAL A CA  
6950  C C   . VAL A 924  ? 2.0223 2.4050 2.3570 0.7607  -0.9732 -0.7148 924  VAL A C   
6951  O O   . VAL A 924  ? 1.9005 2.3646 2.2447 0.7651  -0.9151 -0.6768 924  VAL A O   
6952  C CB  . VAL A 924  ? 2.2981 2.5639 2.5640 0.7087  -1.0660 -0.7302 924  VAL A CB  
6953  C CG1 . VAL A 924  ? 2.3801 2.6172 2.6522 0.7319  -1.1281 -0.7925 924  VAL A CG1 
6954  C CG2 . VAL A 924  ? 2.3957 2.5733 2.6204 0.6598  -1.0867 -0.7023 924  VAL A CG2 
6955  N N   . LYS A 925  ? 2.1503 2.5398 2.5107 0.7944  -0.9977 -0.7618 925  LYS A N   
6956  C CA  . LYS A 925  ? 1.9931 2.4823 2.3977 0.8387  -0.9541 -0.7702 925  LYS A CA  
6957  C C   . LYS A 925  ? 2.0028 2.5314 2.4181 0.8765  -0.9944 -0.8260 925  LYS A C   
6958  O O   . LYS A 925  ? 2.1702 2.6400 2.5618 0.8675  -1.0590 -0.8615 925  LYS A O   
6959  C CB  . LYS A 925  ? 1.9002 2.3613 2.3375 0.8452  -0.9313 -0.7697 925  LYS A CB  
6960  C CG  . LYS A 925  ? 1.7331 2.2827 2.2095 0.8640  -0.8512 -0.7347 925  LYS A CG  
6961  C CD  . LYS A 925  ? 1.6945 2.2480 2.1525 0.8307  -0.8060 -0.6749 925  LYS A CD  
6962  C CE  . LYS A 925  ? 1.5715 2.1897 2.0734 0.8448  -0.7265 -0.6399 925  LYS A CE  
6963  N NZ  . LYS A 925  ? 1.5387 2.1611 2.0243 0.8122  -0.6792 -0.5800 925  LYS A NZ  
6964  N N   . THR A 926  ? 2.0181 2.6452 2.4707 0.9195  -0.9551 -0.8336 926  THR A N   
6965  C CA  . THR A 926  ? 1.9667 2.6500 2.4296 0.9590  -0.9848 -0.8820 926  THR A CA  
6966  C C   . THR A 926  ? 1.8523 2.6020 2.3633 1.0061  -0.9533 -0.9014 926  THR A C   
6967  O O   . THR A 926  ? 1.7397 2.5638 2.2786 1.0232  -0.8846 -0.8675 926  THR A O   
6968  C CB  . THR A 926  ? 2.3174 3.0835 2.7626 0.9656  -0.9725 -0.8697 926  THR A CB  
6969  O OG1 . THR A 926  ? 2.2388 3.0470 2.6820 0.9505  -0.9071 -0.8090 926  THR A OG1 
6970  C CG2 . THR A 926  ? 2.4085 3.1086 2.8137 0.9348  -1.0370 -0.8893 926  THR A CG2 
6971  N N   . LEU A 927  ? 1.6341 2.3561 2.1555 1.0274  -1.0037 -0.9563 927  LEU A N   
6972  C CA  . LEU A 927  ? 1.6142 2.3742 2.1820 1.0673  -0.9840 -0.9804 927  LEU A CA  
6973  C C   . LEU A 927  ? 1.6152 2.4683 2.1975 1.1152  -0.9883 -1.0149 927  LEU A C   
6974  O O   . LEU A 927  ? 1.6575 2.4916 2.2203 1.1201  -1.0483 -1.0574 927  LEU A O   
6975  C CB  . LEU A 927  ? 1.6507 2.3077 2.2218 1.0581  -1.0384 -1.0190 927  LEU A CB  
6976  C CG  . LEU A 927  ? 1.6487 2.3097 2.2667 1.0895  -1.0322 -1.0498 927  LEU A CG  
6977  C CD1 . LEU A 927  ? 1.7376 2.2946 2.3425 1.0795  -1.1063 -1.0957 927  LEU A CD1 
6978  C CD2 . LEU A 927  ? 1.6217 2.3870 2.2722 1.1412  -1.0109 -1.0737 927  LEU A CD2 
6979  N N   . ARG A 928  ? 2.3009 3.2535 2.9190 1.1516  -0.9243 -0.9974 928  ARG A N   
6980  C CA  . ARG A 928  ? 2.2792 3.3277 2.9130 1.2021  -0.9217 -1.0276 928  ARG A CA  
6981  C C   . ARG A 928  ? 2.3070 3.3392 2.9746 1.2329  -0.9485 -1.0787 928  ARG A C   
6982  O O   . ARG A 928  ? 2.2467 3.2778 2.9542 1.2431  -0.9117 -1.0710 928  ARG A O   
6983  C CB  . ARG A 928  ? 2.1712 3.3382 2.8254 1.2307  -0.8390 -0.9834 928  ARG A CB  
6984  C CG  . ARG A 928  ? 2.2279 3.4454 2.8450 1.2174  -0.8231 -0.9482 928  ARG A CG  
6985  C CD  . ARG A 928  ? 2.2050 3.4855 2.8356 1.2170  -0.7365 -0.8822 928  ARG A CD  
6986  N NE  . ARG A 928  ? 2.2883 3.4885 2.9237 1.1742  -0.7165 -0.8473 928  ARG A NE  
6987  C CZ  . ARG A 928  ? 2.3377 3.5078 2.9445 1.1329  -0.7029 -0.8038 928  ARG A CZ  
6988  N NH1 . ARG A 928  ? 2.3772 3.5915 2.9497 1.1277  -0.7060 -0.7886 928  ARG A NH1 
6989  N NH2 . ARG A 928  ? 2.2946 3.3923 2.9082 1.0974  -0.6858 -0.7761 928  ARG A NH2 
6990  N N   . VAL A 929  ? 1.6257 2.6451 2.2795 1.2472  -1.0123 -1.1318 929  VAL A N   
6991  C CA  . VAL A 929  ? 1.6441 2.6427 2.3266 1.2752  -1.0447 -1.1836 929  VAL A CA  
6992  C C   . VAL A 929  ? 1.6393 2.7433 2.3421 1.3311  -1.0354 -1.2137 929  VAL A C   
6993  O O   . VAL A 929  ? 1.6573 2.8073 2.3349 1.3417  -1.0574 -1.2277 929  VAL A O   
6994  C CB  . VAL A 929  ? 1.7268 2.6098 2.3821 1.2476  -1.1296 -1.2254 929  VAL A CB  
6995  C CG1 . VAL A 929  ? 1.7422 2.5886 2.4285 1.2701  -1.1591 -1.2722 929  VAL A CG1 
6996  C CG2 . VAL A 929  ? 1.7407 2.5282 2.3695 1.1941  -1.1362 -1.1911 929  VAL A CG2 
6997  N N   . VAL A 930  ? 1.7779 2.9188 2.5273 1.3668  -1.0035 -1.2249 930  VAL A N   
6998  C CA  . VAL A 930  ? 1.7675 3.0178 2.5422 1.4235  -0.9769 -1.2428 930  VAL A CA  
6999  C C   . VAL A 930  ? 1.8611 3.0909 2.6649 1.4524  -1.0140 -1.2994 930  VAL A C   
7000  O O   . VAL A 930  ? 1.9513 3.0867 2.7604 1.4297  -1.0515 -1.3200 930  VAL A O   
7001  C CB  . VAL A 930  ? 1.6609 2.9904 2.4751 1.4459  -0.8853 -1.1954 930  VAL A CB  
7002  C CG1 . VAL A 930  ? 1.6122 3.0698 2.4382 1.5019  -0.8480 -1.1972 930  VAL A CG1 
7003  C CG2 . VAL A 930  ? 1.6300 2.9461 2.4270 1.4067  -0.8434 -1.1344 930  VAL A CG2 
7004  N N   . PRO A 931  ? 1.5708 2.8004 2.3975 1.1012  -0.5077 -1.5868 931  PRO A N   
7005  C CA  . PRO A 931  ? 1.5973 2.8567 2.4432 1.1054  -0.5172 -1.6211 931  PRO A CA  
7006  C C   . PRO A 931  ? 1.4962 2.7782 2.4179 1.0781  -0.5019 -1.6384 931  PRO A C   
7007  O O   . PRO A 931  ? 1.4909 2.7726 2.4539 1.0626  -0.4864 -1.6360 931  PRO A O   
7008  C CB  . PRO A 931  ? 1.5843 2.8199 2.3839 1.1028  -0.5213 -1.5904 931  PRO A CB  
7009  C CG  . PRO A 931  ? 1.5626 2.7569 2.3199 1.0966  -0.5140 -1.5410 931  PRO A CG  
7010  C CD  . PRO A 931  ? 1.5262 2.7204 2.3232 1.0831  -0.4988 -1.5363 931  PRO A CD  
7011  N N   . GLU A 932  ? 1.6261 2.9256 2.5651 1.0721  -0.5052 -1.6529 932  GLU A N   
7012  C CA  . GLU A 932  ? 1.6024 2.9358 2.6128 1.0565  -0.4976 -1.6862 932  GLU A CA  
7013  C C   . GLU A 932  ? 1.5033 2.8360 2.5432 1.0294  -0.4860 -1.6698 932  GLU A C   
7014  O O   . GLU A 932  ? 1.4643 2.8041 2.4848 1.0363  -0.4968 -1.6761 932  GLU A O   
7015  C CB  . GLU A 932  ? 1.6759 3.0465 2.6850 1.0826  -0.5174 -1.7359 932  GLU A CB  
7016  C CG  . GLU A 932  ? 1.7637 3.1338 2.7178 1.1175  -0.5358 -1.7469 932  GLU A CG  
7017  C CD  . GLU A 932  ? 1.7979 3.1402 2.6770 1.1350  -0.5477 -1.7175 932  GLU A CD  
7018  O OE1 . GLU A 932  ? 1.7627 3.0756 2.6254 1.1175  -0.5391 -1.6789 932  GLU A OE1 
7019  O OE2 . GLU A 932  ? 1.8615 3.2118 2.6978 1.1664  -0.5653 -1.7327 932  GLU A OE2 
7020  N N   . GLY A 933  ? 1.5592 2.8853 2.6468 0.9997  -0.4640 -1.6499 933  GLY A N   
7021  C CA  . GLY A 933  ? 1.5224 2.8488 2.6390 0.9735  -0.4518 -1.6315 933  GLY A CA  
7022  C C   . GLY A 933  ? 1.4738 2.7647 2.5609 0.9552  -0.4402 -1.5760 933  GLY A C   
7023  O O   . GLY A 933  ? 1.4386 2.7216 2.4995 0.9513  -0.4443 -1.5599 933  GLY A O   
7024  N N   . VAL A 934  ? 1.7917 3.0624 2.8834 0.9436  -0.4253 -1.5472 934  VAL A N   
7025  C CA  . VAL A 934  ? 1.8386 3.0766 2.9008 0.9267  -0.4139 -1.4932 934  VAL A CA  
7026  C C   . VAL A 934  ? 1.7495 2.9923 2.8534 0.8956  -0.3959 -1.4714 934  VAL A C   
7027  O O   . VAL A 934  ? 1.6847 2.9441 2.8532 0.8780  -0.3788 -1.4783 934  VAL A O   
7028  C CB  . VAL A 934  ? 1.9267 3.1454 2.9879 0.9229  -0.4014 -1.4690 934  VAL A CB  
7029  C CG1 . VAL A 934  ? 1.4556 2.6457 2.4951 0.9018  -0.3871 -1.4127 934  VAL A CG1 
7030  C CG2 . VAL A 934  ? 2.0415 3.2511 3.0536 0.9532  -0.4185 -1.4819 934  VAL A CG2 
7031  N N   . LYS A 935  ? 1.7589 2.9872 2.8255 0.8892  -0.3991 -1.4448 935  LYS A N   
7032  C CA  . LYS A 935  ? 1.7206 2.9496 2.8162 0.8594  -0.3817 -1.4153 935  LYS A CA  
7033  C C   . LYS A 935  ? 1.7609 2.9563 2.7989 0.8514  -0.3792 -1.3652 935  LYS A C   
7034  O O   . LYS A 935  ? 1.7870 2.9637 2.7611 0.8691  -0.3958 -1.3615 935  LYS A O   
7035  C CB  . LYS A 935  ? 1.7265 2.9792 2.8428 0.8573  -0.3882 -1.4398 935  LYS A CB  
7036  C CG  . LYS A 935  ? 1.2921 2.5714 2.4868 0.8322  -0.3696 -1.4452 935  LYS A CG  
7037  C CD  . LYS A 935  ? 1.3707 2.6644 2.6250 0.8273  -0.3561 -1.4624 935  LYS A CD  
7038  C CE  . LYS A 935  ? 1.3480 2.6573 2.6737 0.7973  -0.3310 -1.4483 935  LYS A CE  
7039  N NZ  . LYS A 935  ? 1.3759 2.7202 2.7632 0.7929  -0.3298 -1.4866 935  LYS A NZ  
7040  N N   . ARG A 936  ? 1.2776 2.4659 2.3375 0.8252  -0.3583 -1.3264 936  ARG A N   
7041  C CA  . ARG A 936  ? 1.2961 2.4566 2.3048 0.8145  -0.3552 -1.2791 936  ARG A CA  
7042  C C   . ARG A 936  ? 1.2756 2.4436 2.3041 0.7873  -0.3427 -1.2548 936  ARG A C   
7043  O O   . ARG A 936  ? 1.2646 2.4505 2.3528 0.7658  -0.3232 -1.2463 936  ARG A O   
7044  C CB  . ARG A 936  ? 1.2898 2.4310 2.2884 0.8094  -0.3434 -1.2462 936  ARG A CB  
7045  C CG  . ARG A 936  ? 1.2536 2.4103 2.3208 0.7891  -0.3195 -1.2375 936  ARG A CG  
7046  C CD  . ARG A 936  ? 1.3254 2.4669 2.3850 0.7955  -0.3131 -1.2238 936  ARG A CD  
7047  N NE  . ARG A 936  ? 1.3452 2.4713 2.3963 0.7748  -0.2952 -1.1711 936  ARG A NE  
7048  C CZ  . ARG A 936  ? 1.3923 2.5041 2.4369 0.7764  -0.2862 -1.1499 936  ARG A CZ  
7049  N NH1 . ARG A 936  ? 1.4347 2.5451 2.4803 0.7977  -0.2935 -1.1778 936  ARG A NH1 
7050  N NH2 . ARG A 936  ? 1.3713 2.4719 2.4084 0.7569  -0.2698 -1.1007 936  ARG A NH2 
7051  N N   . GLU A 937  ? 2.0083 3.1626 2.9860 0.7889  -0.3536 -1.2437 937  GLU A N   
7052  C CA  . GLU A 937  ? 2.0770 3.2360 3.0620 0.7649  -0.3442 -1.2198 937  GLU A CA  
7053  C C   . GLU A 937  ? 2.1301 3.2607 3.0604 0.7525  -0.3403 -1.1718 937  GLU A C   
7054  O O   . GLU A 937  ? 2.1013 3.2082 2.9671 0.7660  -0.3554 -1.1683 937  GLU A O   
7055  C CB  . GLU A 937  ? 2.2518 3.4218 3.2283 0.7748  -0.3589 -1.2496 937  GLU A CB  
7056  C CG  . GLU A 937  ? 2.9405 4.0857 3.8416 0.7984  -0.3803 -1.2560 937  GLU A CG  
7057  C CD  . GLU A 937  ? 3.1139 4.2745 4.0142 0.8155  -0.3960 -1.2956 937  GLU A CD  
7058  O OE1 . GLU A 937  ? 3.1249 4.3079 4.0595 0.8306  -0.4021 -1.3344 937  GLU A OE1 
7059  O OE2 . GLU A 937  ? 3.1246 4.2754 3.9896 0.8140  -0.4019 -1.2884 937  GLU A OE2 
7060  N N   . SER A 938  ? 1.0794 2.2140 2.0374 0.7263  -0.3192 -1.1351 938  SER A N   
7061  C CA  . SER A 938  ? 1.1253 2.2359 2.0392 0.7136  -0.3125 -1.0877 938  SER A CA  
7062  C C   . SER A 938  ? 1.2271 2.3410 2.1361 0.6865  -0.3020 -1.0541 938  SER A C   
7063  O O   . SER A 938  ? 1.3157 2.4135 2.1923 0.6726  -0.2948 -1.0131 938  SER A O   
7064  C CB  . SER A 938  ? 0.8833 1.9948 1.8269 0.7063  -0.2958 -1.0670 938  SER A CB  
7065  O OG  . SER A 938  ? 1.3442 2.4846 2.3614 0.6880  -0.2766 -1.0677 938  SER A OG  
7066  N N   . TYR A 939  ? 2.3412 3.4767 3.2809 0.6792  -0.3016 -1.0716 939  TYR A N   
7067  C CA  . TYR A 939  ? 2.4196 3.5678 3.3734 0.6510  -0.2879 -1.0426 939  TYR A CA  
7068  C C   . TYR A 939  ? 2.2814 3.4061 3.1695 0.6412  -0.2919 -1.0105 939  TYR A C   
7069  O O   . TYR A 939  ? 2.1506 3.2859 3.0467 0.6163  -0.2796 -0.9825 939  TYR A O   
7070  C CB  . TYR A 939  ? 2.7844 3.9611 3.7839 0.6476  -0.2881 -1.0709 939  TYR A CB  
7071  C CG  . TYR A 939  ? 3.0424 4.2104 4.0026 0.6662  -0.3095 -1.1015 939  TYR A CG  
7072  C CD1 . TYR A 939  ? 3.1280 4.2827 4.0412 0.6584  -0.3144 -1.0854 939  TYR A CD1 
7073  C CD2 . TYR A 939  ? 3.1562 4.3306 4.1272 0.6914  -0.3239 -1.1467 939  TYR A CD2 
7074  C CE1 . TYR A 939  ? 3.2028 4.3487 4.0806 0.6761  -0.3326 -1.1128 939  TYR A CE1 
7075  C CE2 . TYR A 939  ? 3.2306 4.3989 4.1668 0.7094  -0.3425 -1.1735 939  TYR A CE2 
7076  C CZ  . TYR A 939  ? 3.2515 4.4046 4.1412 0.7022  -0.3464 -1.1562 939  TYR A CZ  
7077  O OH  . TYR A 939  ? 3.3117 4.4578 4.1668 0.7212  -0.3639 -1.1829 939  TYR A OH  
7078  N N   . SER A 940  ? 2.0564 3.1504 2.8803 0.6607  -0.3088 -1.0152 940  SER A N   
7079  C CA  . SER A 940  ? 2.0026 3.0701 2.7627 0.6516  -0.3111 -0.9818 940  SER A CA  
7080  C C   . SER A 940  ? 1.8389 2.9063 2.6065 0.6311  -0.2931 -0.9374 940  SER A C   
7081  O O   . SER A 940  ? 1.8241 2.8945 2.6170 0.6367  -0.2867 -0.9356 940  SER A O   
7082  C CB  . SER A 940  ? 2.1065 3.1412 2.8018 0.6789  -0.3311 -0.9956 940  SER A CB  
7083  O OG  . SER A 940  ? 2.1261 3.1556 2.8280 0.6946  -0.3323 -1.0005 940  SER A OG  
7084  N N   . GLY A 941  ? 1.6657 2.7308 2.4115 0.6070  -0.2846 -0.9015 941  GLY A N   
7085  C CA  . GLY A 941  ? 1.5254 2.5927 2.2746 0.5859  -0.2674 -0.8562 941  GLY A CA  
7086  C C   . GLY A 941  ? 1.4302 2.4992 2.1542 0.5599  -0.2610 -0.8247 941  GLY A C   
7087  O O   . GLY A 941  ? 1.4075 2.4890 2.1409 0.5533  -0.2630 -0.8384 941  GLY A O   
7088  N N   . VAL A 942  ? 1.5170 2.5746 2.2087 0.5452  -0.2534 -0.7832 942  VAL A N   
7089  C CA  . VAL A 942  ? 1.3990 2.4608 2.0673 0.5178  -0.2455 -0.7496 942  VAL A CA  
7090  C C   . VAL A 942  ? 1.2960 2.3742 1.9839 0.4944  -0.2247 -0.7031 942  VAL A C   
7091  O O   . VAL A 942  ? 1.3091 2.3907 2.0234 0.5010  -0.2170 -0.6962 942  VAL A O   
7092  C CB  . VAL A 942  ? 1.4328 2.4573 2.0201 0.5228  -0.2608 -0.7438 942  VAL A CB  
7093  C CG1 . VAL A 942  ? 1.4331 2.4625 2.0009 0.5026  -0.2599 -0.7363 942  VAL A CG1 
7094  C CG2 . VAL A 942  ? 1.5015 2.4996 2.0602 0.5562  -0.2818 -0.7837 942  VAL A CG2 
7095  N N   . THR A 943  ? 0.6723 1.7628 1.3487 0.4671  -0.2150 -0.6717 943  THR A N   
7096  C CA  . THR A 943  ? 0.7152 1.8109 1.3807 0.4465  -0.2004 -0.6231 943  THR A CA  
7097  C C   . THR A 943  ? 0.7524 1.8231 1.3448 0.4369  -0.2097 -0.6058 943  THR A C   
7098  O O   . THR A 943  ? 0.7725 1.8448 1.3485 0.4276  -0.2144 -0.6142 943  THR A O   
7099  C CB  . THR A 943  ? 0.6213 1.7605 1.3433 0.4190  -0.1767 -0.5944 943  THR A CB  
7100  O OG1 . THR A 943  ? 0.5989 1.7626 1.3921 0.4270  -0.1690 -0.6183 943  THR A OG1 
7101  C CG2 . THR A 943  ? 0.6224 1.7684 1.3413 0.4038  -0.1606 -0.5462 943  THR A CG2 
7102  N N   . LEU A 944  ? 1.7008 2.7470 2.2480 0.4399  -0.2128 -0.5833 944  LEU A N   
7103  C CA  . LEU A 944  ? 1.7091 2.7354 2.1916 0.4257  -0.2179 -0.5612 944  LEU A CA  
7104  C C   . LEU A 944  ? 1.7066 2.7657 2.2066 0.3912  -0.1981 -0.5182 944  LEU A C   
7105  O O   . LEU A 944  ? 1.6848 2.7634 2.2148 0.3827  -0.1825 -0.4888 944  LEU A O   
7106  C CB  . LEU A 944  ? 1.7343 2.7236 2.1614 0.4403  -0.2281 -0.5510 944  LEU A CB  
7107  C CG  . LEU A 944  ? 1.7719 2.7276 2.1690 0.4729  -0.2498 -0.5936 944  LEU A CG  
7108  C CD1 . LEU A 944  ? 1.8314 2.7474 2.1618 0.4852  -0.2616 -0.5830 944  LEU A CD1 
7109  C CD2 . LEU A 944  ? 1.7637 2.7172 2.1489 0.4704  -0.2580 -0.6190 944  LEU A CD2 
7110  N N   . ASP A 945  ? 1.2533 2.3204 1.7367 0.3719  -0.1980 -0.5155 945  ASP A N   
7111  C CA  . ASP A 945  ? 1.1979 2.2973 1.6903 0.3378  -0.1806 -0.4751 945  ASP A CA  
7112  C C   . ASP A 945  ? 1.2075 2.2884 1.6361 0.3222  -0.1883 -0.4666 945  ASP A C   
7113  O O   . ASP A 945  ? 1.2239 2.3096 1.6495 0.3155  -0.1921 -0.4845 945  ASP A O   
7114  C CB  . ASP A 945  ? 1.1484 2.2919 1.7070 0.3253  -0.1670 -0.4798 945  ASP A CB  
7115  C CG  . ASP A 945  ? 1.0799 2.2642 1.6680 0.2964  -0.1444 -0.4337 945  ASP A CG  
7116  O OD1 . ASP A 945  ? 1.0898 2.2676 1.6454 0.2860  -0.1398 -0.3985 945  ASP A OD1 
7117  O OD2 . ASP A 945  ? 1.0031 2.2266 1.6474 0.2850  -0.1311 -0.4325 945  ASP A OD2 
7118  N N   . PRO A 946  ? 0.9636 2.0244 1.3419 0.3150  -0.1895 -0.4379 946  PRO A N   
7119  C CA  . PRO A 946  ? 1.0283 2.0663 1.3418 0.3012  -0.1975 -0.4321 946  PRO A CA  
7120  C C   . PRO A 946  ? 0.9940 2.0712 1.3228 0.2665  -0.1830 -0.4079 946  PRO A C   
7121  O O   . PRO A 946  ? 1.0116 2.0831 1.3128 0.2552  -0.1880 -0.4186 946  PRO A O   
7122  C CB  . PRO A 946  ? 1.0590 2.0744 1.3268 0.2996  -0.1985 -0.4010 946  PRO A CB  
7123  C CG  . PRO A 946  ? 1.0114 2.0432 1.3238 0.3098  -0.1888 -0.3870 946  PRO A CG  
7124  C CD  . PRO A 946  ? 0.9806 2.0513 1.3670 0.3092  -0.1776 -0.4000 946  PRO A CD  
7125  N N   . ARG A 947  ? 1.0555 2.1734 1.4296 0.2505  -0.1642 -0.3749 947  ARG A N   
7126  C CA  . ARG A 947  ? 1.0106 2.1724 1.4031 0.2170  -0.1478 -0.3449 947  ARG A CA  
7127  C C   . ARG A 947  ? 0.9436 2.1419 1.3987 0.2149  -0.1400 -0.3627 947  ARG A C   
7128  O O   . ARG A 947  ? 0.9177 2.1623 1.4146 0.1938  -0.1217 -0.3355 947  ARG A O   
7129  C CB  . ARG A 947  ? 0.9873 2.1777 1.3990 0.2017  -0.1300 -0.2978 947  ARG A CB  
7130  C CG  . ARG A 947  ? 1.0452 2.2022 1.4102 0.2102  -0.1364 -0.2809 947  ARG A CG  
7131  C CD  . ARG A 947  ? 1.0724 2.2271 1.3810 0.1834  -0.1351 -0.2479 947  ARG A CD  
7132  N NE  . ARG A 947  ? 1.0338 2.2284 1.3639 0.1614  -0.1153 -0.1989 947  ARG A NE  
7133  C CZ  . ARG A 947  ? 1.1011 2.2867 1.3915 0.1523  -0.1136 -0.1649 947  ARG A CZ  
7134  N NH1 . ARG A 947  ? 1.1802 2.3168 1.4080 0.1634  -0.1305 -0.1751 947  ARG A NH1 
7135  N NH2 . ARG A 947  ? 1.0790 2.3054 1.3923 0.1323  -0.0946 -0.1200 947  ARG A NH2 
7136  N N   . GLY A 948  ? 0.9629 2.1421 1.4260 0.2374  -0.1532 -0.4073 948  GLY A N   
7137  C CA  . GLY A 948  ? 0.8961 2.1080 1.4174 0.2369  -0.1471 -0.4270 948  GLY A CA  
7138  C C   . GLY A 948  ? 0.7883 2.0491 1.3838 0.2278  -0.1258 -0.4049 948  GLY A C   
7139  O O   . GLY A 948  ? 0.7289 2.0176 1.3780 0.2288  -0.1199 -0.4212 948  GLY A O   
7140  N N   . ILE A 949  ? 0.9498 2.2202 1.5484 0.2198  -0.1138 -0.3676 949  ILE A N   
7141  C CA  . ILE A 949  ? 0.7579 2.0756 1.4199 0.2072  -0.0906 -0.3372 949  ILE A CA  
7142  C C   . ILE A 949  ? 0.7057 2.0518 1.4426 0.2159  -0.0824 -0.3597 949  ILE A C   
7143  O O   . ILE A 949  ? 0.7062 2.0987 1.4921 0.1982  -0.0628 -0.3356 949  ILE A O   
7144  C CB  . ILE A 949  ? 0.8239 2.1333 1.4862 0.2141  -0.0834 -0.3105 949  ILE A CB  
7145  C CG1 . ILE A 949  ? 0.9267 2.2121 1.5165 0.2031  -0.0899 -0.2839 949  ILE A CG1 
7146  C CG2 . ILE A 949  ? 0.7483 2.1064 1.4761 0.2014  -0.0573 -0.2768 949  ILE A CG2 
7147  C CD1 . ILE A 949  ? 0.8847 2.1843 1.4783 0.1942  -0.0744 -0.2369 949  ILE A CD1 
7148  N N   . TYR A 950  ? 1.3222 2.6430 2.0690 0.2424  -0.0968 -0.4047 950  TYR A N   
7149  C CA  . TYR A 950  ? 1.3169 2.6629 2.1377 0.2524  -0.0886 -0.4265 950  TYR A CA  
7150  C C   . TYR A 950  ? 1.3122 2.6706 2.1521 0.2528  -0.0950 -0.4589 950  TYR A C   
7151  O O   . TYR A 950  ? 1.2950 2.6811 2.2001 0.2567  -0.0857 -0.4718 950  TYR A O   
7152  C CB  . TYR A 950  ? 1.2272 2.5490 2.0673 0.2807  -0.0939 -0.4495 950  TYR A CB  
7153  C CG  . TYR A 950  ? 1.1856 2.5232 2.0561 0.2761  -0.0747 -0.4136 950  TYR A CG  
7154  C CD1 . TYR A 950  ? 1.0764 2.4463 2.0230 0.2766  -0.0558 -0.4103 950  TYR A CD1 
7155  C CD2 . TYR A 950  ? 1.2082 2.5293 2.0315 0.2703  -0.0742 -0.3810 950  TYR A CD2 
7156  C CE1 . TYR A 950  ? 1.0511 2.4350 2.0253 0.2725  -0.0366 -0.3761 950  TYR A CE1 
7157  C CE2 . TYR A 950  ? 1.2052 2.5416 2.0554 0.2662  -0.0559 -0.3464 950  TYR A CE2 
7158  C CZ  . TYR A 950  ? 1.1563 2.5236 2.0816 0.2676  -0.0369 -0.3440 950  TYR A CZ  
7159  O OH  . TYR A 950  ? 1.1254 2.5066 2.0768 0.2642  -0.0175 -0.3091 950  TYR A OH  
7160  N N   . GLY A 951  ? 0.8583 2.1964 1.6424 0.2486  -0.1098 -0.4710 951  GLY A N   
7161  C CA  . GLY A 951  ? 0.8962 2.2394 1.6899 0.2521  -0.1182 -0.5042 951  GLY A CA  
7162  C C   . GLY A 951  ? 1.0083 2.3105 1.7302 0.2587  -0.1394 -0.5270 951  GLY A C   
7163  O O   . GLY A 951  ? 1.0288 2.3358 1.7474 0.2561  -0.1451 -0.5470 951  GLY A O   
7164  N N   . THR A 952  ? 0.8714 2.1323 1.5363 0.2684  -0.1507 -0.5245 952  THR A N   
7165  C CA  . THR A 952  ? 0.9200 2.1396 1.5107 0.2723  -0.1686 -0.5394 952  THR A CA  
7166  C C   . THR A 952  ? 0.9507 2.1306 1.4891 0.2824  -0.1771 -0.5293 952  THR A C   
7167  O O   . THR A 952  ? 0.9222 2.1055 1.4822 0.2887  -0.1706 -0.5144 952  THR A O   
7168  C CB  . THR A 952  ? 0.9442 2.1406 1.5279 0.2967  -0.1862 -0.5887 952  THR A CB  
7169  O OG1 . THR A 952  ? 1.0521 2.1978 1.5647 0.3111  -0.2037 -0.6021 952  THR A OG1 
7170  C CG2 . THR A 952  ? 0.8927 2.0973 1.5334 0.3208  -0.1873 -0.6159 952  THR A CG2 
7171  N N   . ILE A 953  ? 1.1324 2.2740 1.6021 0.2843  -0.1910 -0.5371 953  ILE A N   
7172  C CA  . ILE A 953  ? 1.2269 2.3272 1.6447 0.2973  -0.2009 -0.5315 953  ILE A CA  
7173  C C   . ILE A 953  ? 1.3894 2.4583 1.8045 0.3339  -0.2176 -0.5727 953  ILE A C   
7174  O O   . ILE A 953  ? 1.4474 2.5046 1.8562 0.3471  -0.2286 -0.6075 953  ILE A O   
7175  C CB  . ILE A 953  ? 1.3183 2.3909 1.6630 0.2822  -0.2069 -0.5181 953  ILE A CB  
7176  C CG1 . ILE A 953  ? 1.3852 2.4193 1.6877 0.3005  -0.2247 -0.5566 953  ILE A CG1 
7177  C CG2 . ILE A 953  ? 1.3256 2.4347 1.6775 0.2466  -0.1925 -0.4896 953  ILE A CG2 
7178  C CD1 . ILE A 953  ? 1.4343 2.4382 1.6651 0.2859  -0.2296 -0.5450 953  ILE A CD1 
7179  N N   . SER A 954  ? 1.7287 2.7858 2.1493 0.3504  -0.2188 -0.5681 954  SER A N   
7180  C CA  . SER A 954  ? 1.6920 2.7237 2.1136 0.3855  -0.2336 -0.6050 954  SER A CA  
7181  C C   . SER A 954  ? 1.7311 2.7220 2.0952 0.3993  -0.2440 -0.5970 954  SER A C   
7182  O O   . SER A 954  ? 1.7349 2.7282 2.1067 0.3995  -0.2375 -0.5738 954  SER A O   
7183  C CB  . SER A 954  ? 1.5743 2.6341 2.0670 0.3956  -0.2249 -0.6125 954  SER A CB  
7184  O OG  . SER A 954  ? 1.5792 2.6224 2.0798 0.4272  -0.2394 -0.6550 954  SER A OG  
7185  N N   . ARG A 955  ? 1.4197 2.3733 1.7264 0.4112  -0.2594 -0.6157 955  ARG A N   
7186  C CA  . ARG A 955  ? 1.4841 2.3972 1.7318 0.4241  -0.2695 -0.6079 955  ARG A CA  
7187  C C   . ARG A 955  ? 1.5873 2.4663 1.8080 0.4589  -0.2886 -0.6483 955  ARG A C   
7188  O O   . ARG A 955  ? 1.6812 2.5230 1.8468 0.4716  -0.2986 -0.6456 955  ARG A O   
7189  C CB  . ARG A 955  ? 1.5155 2.4112 1.7048 0.4002  -0.2678 -0.5804 955  ARG A CB  
7190  C CG  . ARG A 955  ? 1.4776 2.4025 1.6785 0.3660  -0.2504 -0.5352 955  ARG A CG  
7191  C CD  . ARG A 955  ? 1.5103 2.4117 1.6454 0.3460  -0.2522 -0.5159 955  ARG A CD  
7192  N NE  . ARG A 955  ? 1.4216 2.3558 1.5650 0.3085  -0.2369 -0.4829 955  ARG A NE  
7193  C CZ  . ARG A 955  ? 1.4376 2.3619 1.5377 0.2873  -0.2371 -0.4758 955  ARG A CZ  
7194  N NH1 . ARG A 955  ? 1.5158 2.3966 1.5626 0.3004  -0.2510 -0.4992 955  ARG A NH1 
7195  N NH2 . ARG A 955  ? 1.4536 2.4123 1.5638 0.2531  -0.2228 -0.4455 955  ARG A NH2 
7196  N N   . ARG A 956  ? 1.3418 2.2345 1.6004 0.4742  -0.2933 -0.6846 956  ARG A N   
7197  C CA  . ARG A 956  ? 1.3905 2.2586 1.6339 0.5101  -0.3108 -0.7248 956  ARG A CA  
7198  C C   . ARG A 956  ? 1.4311 2.3259 1.7334 0.5250  -0.3129 -0.7617 956  ARG A C   
7199  O O   . ARG A 956  ? 1.4001 2.3094 1.7180 0.5168  -0.3116 -0.7760 956  ARG A O   
7200  C CB  . ARG A 956  ? 1.4359 2.2646 1.6111 0.5174  -0.3229 -0.7355 956  ARG A CB  
7201  C CG  . ARG A 956  ? 1.5176 2.3093 1.6518 0.5520  -0.3389 -0.7545 956  ARG A CG  
7202  C CD  . ARG A 956  ? 1.6353 2.3866 1.7023 0.5597  -0.3491 -0.7631 956  ARG A CD  
7203  N NE  . ARG A 956  ? 1.6845 2.4345 1.7581 0.5806  -0.3587 -0.8032 956  ARG A NE  
7204  C CZ  . ARG A 956  ? 1.7849 2.5001 1.8084 0.6008  -0.3702 -0.8220 956  ARG A CZ  
7205  N NH1 . ARG A 956  ? 1.8514 2.5286 1.8144 0.6029  -0.3737 -0.8048 956  ARG A NH1 
7206  N NH2 . ARG A 956  ? 1.8030 2.5222 1.8378 0.6192  -0.3778 -0.8574 956  ARG A NH2 
7207  N N   . LYS A 957  ? 1.4459 2.3477 1.7808 0.5460  -0.3157 -0.7764 957  LYS A N   
7208  C CA  . LYS A 957  ? 1.4438 2.3664 1.8292 0.5649  -0.3203 -0.8153 957  LYS A CA  
7209  C C   . LYS A 957  ? 1.4754 2.3713 1.8309 0.6010  -0.3384 -0.8464 957  LYS A C   
7210  O O   . LYS A 957  ? 1.4768 2.3454 1.7899 0.6119  -0.3442 -0.8346 957  LYS A O   
7211  C CB  . LYS A 957  ? 1.3938 2.3514 1.8495 0.5588  -0.3071 -0.8098 957  LYS A CB  
7212  C CG  . LYS A 957  ? 1.4392 2.4174 1.9475 0.5789  -0.3122 -0.8520 957  LYS A CG  
7213  C CD  . LYS A 957  ? 1.4220 2.4426 2.0004 0.5589  -0.2971 -0.8512 957  LYS A CD  
7214  C CE  . LYS A 957  ? 1.4771 2.5117 2.0790 0.5691  -0.3049 -0.8904 957  LYS A CE  
7215  N NZ  . LYS A 957  ? 1.5494 2.5757 2.1527 0.6029  -0.3212 -0.9334 957  LYS A NZ  
7216  N N   . GLU A 958  ? 1.5420 2.4481 1.9207 0.6197  -0.3471 -0.8857 958  GLU A N   
7217  C CA  . GLU A 958  ? 1.6698 2.5534 2.0176 0.6545  -0.3649 -0.9175 958  GLU A CA  
7218  C C   . GLU A 958  ? 1.6634 2.5718 2.0642 0.6762  -0.3700 -0.9545 958  GLU A C   
7219  O O   . GLU A 958  ? 1.6457 2.5776 2.0841 0.6760  -0.3699 -0.9785 958  GLU A O   
7220  C CB  . GLU A 958  ? 1.7955 2.6588 2.0989 0.6593  -0.3737 -0.9310 958  GLU A CB  
7221  C CG  . GLU A 958  ? 1.9503 2.7896 2.2167 0.6952  -0.3913 -0.9612 958  GLU A CG  
7222  C CD  . GLU A 958  ? 2.0794 2.8980 2.3028 0.6991  -0.3979 -0.9725 958  GLU A CD  
7223  O OE1 . GLU A 958  ? 2.1207 2.9237 2.3117 0.6758  -0.3910 -0.9465 958  GLU A OE1 
7224  O OE2 . GLU A 958  ? 2.1277 2.9464 2.3497 0.7252  -0.4093 -1.0071 958  GLU A OE2 
7225  N N   . PHE A 959  ? 1.9552 2.8586 2.3584 0.6943  -0.3741 -0.9585 959  PHE A N   
7226  C CA  . PHE A 959  ? 1.9669 2.8881 2.4087 0.7192  -0.3816 -0.9959 959  PHE A CA  
7227  C C   . PHE A 959  ? 2.1028 3.0010 2.4975 0.7528  -0.4008 -1.0236 959  PHE A C   
7228  O O   . PHE A 959  ? 2.1695 3.0399 2.5166 0.7661  -0.4074 -1.0122 959  PHE A O   
7229  C CB  . PHE A 959  ? 1.8676 2.7944 2.3330 0.7213  -0.3756 -0.9844 959  PHE A CB  
7230  C CG  . PHE A 959  ? 1.7659 2.7008 2.2496 0.6902  -0.3572 -0.9432 959  PHE A CG  
7231  C CD1 . PHE A 959  ? 1.6914 2.6604 2.2424 0.6717  -0.3421 -0.9409 959  PHE A CD1 
7232  C CD2 . PHE A 959  ? 1.7563 2.6659 2.1903 0.6789  -0.3543 -0.9058 959  PHE A CD2 
7233  C CE1 . PHE A 959  ? 1.6295 2.6087 2.1988 0.6436  -0.3240 -0.9016 959  PHE A CE1 
7234  C CE2 . PHE A 959  ? 1.6985 2.6188 2.1496 0.6498  -0.3369 -0.8667 959  PHE A CE2 
7235  C CZ  . PHE A 959  ? 1.6342 2.5901 2.1533 0.6325  -0.3215 -0.8642 959  PHE A CZ  
7236  N N   . PRO A 960  ? 1.7647 2.6757 2.1732 0.7673  -0.4095 -1.0593 960  PRO A N   
7237  C CA  . PRO A 960  ? 1.9015 2.7953 2.2689 0.8006  -0.4271 -1.0877 960  PRO A CA  
7238  C C   . PRO A 960  ? 2.0106 2.9232 2.4078 0.8283  -0.4364 -1.1220 960  PRO A C   
7239  O O   . PRO A 960  ? 1.9716 2.9047 2.4156 0.8229  -0.4294 -1.1223 960  PRO A O   
7240  C CB  . PRO A 960  ? 1.8972 2.7994 2.2683 0.7980  -0.4295 -1.1062 960  PRO A CB  
7241  C CG  . PRO A 960  ? 1.6638 2.5895 2.0809 0.7627  -0.4130 -1.0874 960  PRO A CG  
7242  C CD  . PRO A 960  ? 1.6495 2.5904 2.1070 0.7508  -0.4021 -1.0705 960  PRO A CD  
7243  N N   . TYR A 961  ? 2.5163 3.4219 2.8850 0.8581  -0.4518 -1.1512 961  TYR A N   
7244  C CA  . TYR A 961  ? 2.6207 3.5483 3.0156 0.8861  -0.4625 -1.1899 961  TYR A CA  
7245  C C   . TYR A 961  ? 2.6289 3.5916 3.0771 0.8834  -0.4620 -1.2204 961  TYR A C   
7246  O O   . TYR A 961  ? 2.6580 3.6188 3.0943 0.8800  -0.4635 -1.2255 961  TYR A O   
7247  C CB  . TYR A 961  ? 2.7548 3.6606 3.0921 0.9203  -0.4790 -1.2056 961  TYR A CB  
7248  C CG  . TYR A 961  ? 2.8308 3.7293 3.1524 0.9417  -0.4857 -1.2067 961  TYR A CG  
7249  C CD1 . TYR A 961  ? 2.8761 3.7955 3.2132 0.9714  -0.4976 -1.2434 961  TYR A CD1 
7250  C CD2 . TYR A 961  ? 2.8515 3.7243 3.1438 0.9318  -0.4800 -1.1709 961  TYR A CD2 
7251  C CE1 . TYR A 961  ? 2.9188 3.8333 3.2418 0.9912  -0.5037 -1.2447 961  TYR A CE1 
7252  C CE2 . TYR A 961  ? 2.9037 3.7704 3.1818 0.9516  -0.4860 -1.1712 961  TYR A CE2 
7253  C CZ  . TYR A 961  ? 2.9417 3.8292 3.2352 0.9814  -0.4978 -1.2083 961  TYR A CZ  
7254  O OH  . TYR A 961  ? 2.9962 3.8789 3.2756 1.0014  -0.5037 -1.2088 961  TYR A OH  
7255  N N   . ARG A 962  ? 2.4961 3.4904 3.0029 0.8851  -0.4597 -1.2411 962  ARG A N   
7256  C CA  . ARG A 962  ? 2.5321 3.5615 3.0895 0.8877  -0.4616 -1.2754 962  ARG A CA  
7257  C C   . ARG A 962  ? 2.5012 3.5552 3.0909 0.9107  -0.4698 -1.3112 962  ARG A C   
7258  O O   . ARG A 962  ? 2.4217 3.4984 3.0674 0.8993  -0.4607 -1.3160 962  ARG A O   
7259  C CB  . ARG A 962  ? 2.5751 3.6261 3.1889 0.8541  -0.4447 -1.2622 962  ARG A CB  
7260  C CG  . ARG A 962  ? 2.6753 3.7665 3.3524 0.8565  -0.4452 -1.2984 962  ARG A CG  
7261  C CD  . ARG A 962  ? 2.7441 3.8483 3.4423 0.8366  -0.4382 -1.2949 962  ARG A CD  
7262  N NE  . ARG A 962  ? 2.7425 3.8721 3.5068 0.8091  -0.4208 -1.2839 962  ARG A NE  
7263  C CZ  . ARG A 962  ? 2.7508 3.9060 3.5590 0.7937  -0.4137 -1.2904 962  ARG A CZ  
7264  N NH1 . ARG A 962  ? 2.7978 3.9564 3.5900 0.8029  -0.4229 -1.3085 962  ARG A NH1 
7265  N NH2 . ARG A 962  ? 2.6946 3.8720 3.5629 0.7696  -0.3969 -1.2782 962  ARG A NH2 
7266  N N   . ILE A 963  ? 2.1830 3.2329 2.7371 0.9432  -0.4865 -1.3362 963  ILE A N   
7267  C CA  . ILE A 963  ? 2.1128 3.1882 2.6918 0.9679  -0.4964 -1.3734 963  ILE A CA  
7268  C C   . ILE A 963  ? 2.0868 3.2028 2.7267 0.9647  -0.4961 -1.4075 963  ILE A C   
7269  O O   . ILE A 963  ? 2.1066 3.2307 2.7373 0.9745  -0.5037 -1.4253 963  ILE A O   
7270  C CB  . ILE A 963  ? 2.0672 3.1292 2.5885 1.0045  -0.5143 -1.3893 963  ILE A CB  
7271  C CG1 . ILE A 963  ? 2.0369 3.0538 2.4884 1.0052  -0.5145 -1.3533 963  ILE A CG1 
7272  C CG2 . ILE A 963  ? 2.0807 3.1592 2.6153 1.0266  -0.5220 -1.4126 963  ILE A CG2 
7273  C CD1 . ILE A 963  ? 2.0904 3.0916 2.4830 1.0410  -0.5305 -1.3655 963  ILE A CD1 
7274  N N   . PRO A 964  ? 2.1835 3.3249 2.8863 0.9511  -0.4866 -1.4163 964  PRO A N   
7275  C CA  . PRO A 964  ? 2.1823 3.3632 2.9494 0.9451  -0.4843 -1.4472 964  PRO A CA  
7276  C C   . PRO A 964  ? 2.2913 3.4930 3.0515 0.9775  -0.5022 -1.4903 964  PRO A C   
7277  O O   . PRO A 964  ? 2.3338 3.5335 3.0747 0.9995  -0.5112 -1.5022 964  PRO A O   
7278  C CB  . PRO A 964  ? 2.1319 3.3285 2.9565 0.9300  -0.4715 -1.4471 964  PRO A CB  
7279  C CG  . PRO A 964  ? 2.0767 3.2406 2.8683 0.9214  -0.4641 -1.4079 964  PRO A CG  
7280  C CD  . PRO A 964  ? 2.1358 3.2701 2.8509 0.9443  -0.4785 -1.4003 964  PRO A CD  
7281  N N   . LEU A 965  ? 2.5475 3.7707 3.3229 0.9813  -0.5073 -1.5129 965  LEU A N   
7282  C CA  . LEU A 965  ? 2.6852 3.9293 3.4490 1.0136  -0.5248 -1.5521 965  LEU A CA  
7283  C C   . LEU A 965  ? 2.7248 4.0030 3.5343 1.0247  -0.5289 -1.5878 965  LEU A C   
7284  O O   . LEU A 965  ? 2.7865 4.0910 3.5979 1.0489  -0.5424 -1.6240 965  LEU A O   
7285  C CB  . LEU A 965  ? 2.7291 3.9894 3.4990 1.0150  -0.5288 -1.5673 965  LEU A CB  
7286  C CG  . LEU A 965  ? 2.9281 4.1557 3.6439 1.0117  -0.5283 -1.5400 965  LEU A CG  
7287  C CD1 . LEU A 965  ? 2.9591 4.2068 3.6797 1.0206  -0.5350 -1.5624 965  LEU A CD1 
7288  C CD2 . LEU A 965  ? 2.9951 4.1857 3.6361 1.0332  -0.5369 -1.5239 965  LEU A CD2 
7289  N N   . ASP A 966  ? 2.3557 3.6339 3.2013 1.0068  -0.5167 -1.5773 966  ASP A N   
7290  C CA  . ASP A 966  ? 2.3306 3.6361 3.2171 1.0152  -0.5186 -1.6081 966  ASP A CA  
7291  C C   . ASP A 966  ? 2.2552 3.5384 3.1066 1.0278  -0.5213 -1.5956 966  ASP A C   
7292  O O   . ASP A 966  ? 2.2525 3.5499 3.1381 1.0276  -0.5179 -1.6103 966  ASP A O   
7293  C CB  . ASP A 966  ? 2.3099 3.6349 3.2718 0.9856  -0.5010 -1.6093 966  ASP A CB  
7294  C CG  . ASP A 966  ? 2.3256 3.6890 3.3391 0.9813  -0.5020 -1.6414 966  ASP A CG  
7295  O OD1 . ASP A 966  ? 2.3819 3.7607 3.3749 1.0037  -0.5176 -1.6673 966  ASP A OD1 
7296  O OD2 . ASP A 966  ? 2.2716 3.6504 3.3465 0.9560  -0.4867 -1.6401 966  ASP A OD2 
7297  N N   . LEU A 967  ? 1.9722 3.2199 2.7561 1.0383  -0.5267 -1.5681 967  LEU A N   
7298  C CA  . LEU A 967  ? 1.9223 3.1464 2.6716 1.0484  -0.5280 -1.5510 967  LEU A CA  
7299  C C   . LEU A 967  ? 1.9161 3.1644 2.6670 1.0781  -0.5418 -1.5888 967  LEU A C   
7300  O O   . LEU A 967  ? 1.9702 3.2397 2.7110 1.1009  -0.5558 -1.6190 967  LEU A O   
7301  C CB  . LEU A 967  ? 1.9481 3.1310 2.6223 1.0568  -0.5327 -1.5176 967  LEU A CB  
7302  C CG  . LEU A 967  ? 1.9988 3.1583 2.6289 1.0738  -0.5376 -1.5028 967  LEU A CG  
7303  C CD1 . LEU A 967  ? 1.9693 3.1246 2.6320 1.0545  -0.5237 -1.4857 967  LEU A CD1 
7304  C CD2 . LEU A 967  ? 2.0259 3.1443 2.5842 1.0799  -0.5411 -1.4694 967  LEU A CD2 
7305  N N   . VAL A 968  ? 1.8800 3.1268 2.6438 1.0781  -0.5375 -1.5874 968  VAL A N   
7306  C CA  . VAL A 968  ? 1.8642 3.1313 2.6223 1.1072  -0.5508 -1.6201 968  VAL A CA  
7307  C C   . VAL A 968  ? 1.9172 3.1591 2.5999 1.1358  -0.5642 -1.6062 968  VAL A C   
7308  O O   . VAL A 968  ? 1.8977 3.1104 2.5512 1.1346  -0.5601 -1.5768 968  VAL A O   
7309  C CB  . VAL A 968  ? 1.7931 3.0665 2.5916 1.0968  -0.5406 -1.6235 968  VAL A CB  
7310  C CG1 . VAL A 968  ? 1.7143 3.0132 2.5880 1.0705  -0.5271 -1.6390 968  VAL A CG1 
7311  C CG2 . VAL A 968  ? 1.7705 3.0039 2.5422 1.0827  -0.5293 -1.5765 968  VAL A CG2 
7312  N N   . PRO A 969  ? 1.9137 3.1677 2.5653 1.1625  -0.5798 -1.6271 969  PRO A N   
7313  C CA  . PRO A 969  ? 2.0013 3.2265 2.5789 1.1861  -0.5900 -1.6078 969  PRO A CA  
7314  C C   . PRO A 969  ? 2.0880 3.2882 2.6281 1.1974  -0.5912 -1.5863 969  PRO A C   
7315  O O   . PRO A 969  ? 2.0825 3.2939 2.6519 1.1944  -0.5875 -1.5946 969  PRO A O   
7316  C CB  . PRO A 969  ? 2.0486 3.3063 2.6163 1.2182  -0.6069 -1.6465 969  PRO A CB  
7317  C CG  . PRO A 969  ? 1.9974 3.2910 2.6265 1.2026  -0.6033 -1.6750 969  PRO A CG  
7318  C CD  . PRO A 969  ? 1.9261 3.2246 2.6123 1.1737  -0.5885 -1.6718 969  PRO A CD  
7319  N N   . LYS A 970  ? 2.5418 3.7069 3.0173 1.2096  -0.5955 -1.5581 970  LYS A N   
7320  C CA  . LYS A 970  ? 2.6683 3.8066 3.1022 1.2211  -0.5970 -1.5339 970  LYS A CA  
7321  C C   . LYS A 970  ? 2.6578 3.7825 3.1180 1.1954  -0.5826 -1.5100 970  LYS A C   
7322  O O   . LYS A 970  ? 2.6727 3.7902 3.1168 1.2076  -0.5847 -1.5035 970  LYS A O   
7323  C CB  . LYS A 970  ? 2.8082 3.9703 3.2259 1.2588  -0.6125 -1.5635 970  LYS A CB  
7324  C CG  . LYS A 970  ? 2.9694 4.1267 3.3313 1.2910  -0.6264 -1.5678 970  LYS A CG  
7325  C CD  . LYS A 970  ? 3.1110 4.2814 3.4449 1.3275  -0.6395 -1.5826 970  LYS A CD  
7326  C CE  . LYS A 970  ? 3.2282 4.3924 3.5046 1.3610  -0.6519 -1.5833 970  LYS A CE  
7327  N NZ  . LYS A 970  ? 3.3065 4.4770 3.5480 1.3962  -0.6632 -1.5887 970  LYS A NZ  
7328  N N   . THR A 971  ? 2.4493 3.5714 2.9498 1.1610  -0.5676 -1.4965 971  THR A N   
7329  C CA  . THR A 971  ? 2.4417 3.5480 2.9637 1.1352  -0.5519 -1.4678 971  THR A CA  
7330  C C   . THR A 971  ? 2.3996 3.4727 2.9024 1.1080  -0.5401 -1.4243 971  THR A C   
7331  O O   . THR A 971  ? 2.3893 3.4695 2.9193 1.0873  -0.5330 -1.4243 971  THR A O   
7332  C CB  . THR A 971  ? 2.4214 3.5588 3.0193 1.1153  -0.5411 -1.4900 971  THR A CB  
7333  O OG1 . THR A 971  ? 2.3542 3.4970 2.9830 1.0900  -0.5320 -1.4861 971  THR A OG1 
7334  C CG2 . THR A 971  ? 2.4856 3.6625 3.1083 1.1394  -0.5533 -1.5400 971  THR A CG2 
7335  N N   . GLU A 972  ? 3.2408 4.2792 3.6976 1.1077  -0.5378 -1.3874 972  GLU A N   
7336  C CA  . GLU A 972  ? 3.1833 4.1895 3.6157 1.0825  -0.5273 -1.3444 972  GLU A CA  
7337  C C   . GLU A 972  ? 2.9900 4.0033 3.4767 1.0447  -0.5083 -1.3285 972  GLU A C   
7338  O O   . GLU A 972  ? 2.9095 3.9406 3.4443 1.0363  -0.4999 -1.3366 972  GLU A O   
7339  C CB  . GLU A 972  ? 3.3216 4.2930 3.6999 1.0893  -0.5279 -1.3092 972  GLU A CB  
7340  C CG  . GLU A 972  ? 3.4436 4.4241 3.8293 1.1069  -0.5313 -1.3192 972  GLU A CG  
7341  C CD  . GLU A 972  ? 3.5622 4.5095 3.8887 1.1192  -0.5348 -1.2874 972  GLU A CD  
7342  O OE1 . GLU A 972  ? 3.5759 4.4919 3.8662 1.1043  -0.5295 -1.2504 972  GLU A OE1 
7343  O OE2 . GLU A 972  ? 3.6314 4.5848 3.9478 1.1436  -0.5428 -1.2995 972  GLU A OE2 
7344  N N   . ILE A 973  ? 1.6822 2.6820 2.1606 1.0225  -0.5011 -1.3060 973  ILE A N   
7345  C CA  . ILE A 973  ? 1.5233 2.5280 2.0462 0.9860  -0.4823 -1.2844 973  ILE A CA  
7346  C C   . ILE A 973  ? 1.5547 2.5331 2.0588 0.9687  -0.4705 -1.2388 973  ILE A C   
7347  O O   . ILE A 973  ? 1.6034 2.5520 2.0564 0.9635  -0.4707 -1.2072 973  ILE A O   
7348  C CB  . ILE A 973  ? 1.3504 2.3538 1.8734 0.9676  -0.4786 -1.2774 973  ILE A CB  
7349  C CG1 . ILE A 973  ? 1.3617 2.3680 1.8554 0.9917  -0.4948 -1.3055 973  ILE A CG1 
7350  C CG2 . ILE A 973  ? 1.2285 2.2612 1.8227 0.9431  -0.4651 -1.2863 973  ILE A CG2 
7351  C CD1 . ILE A 973  ? 1.3134 2.3450 1.8486 0.9791  -0.4918 -1.3257 973  ILE A CD1 
7352  N N   . LYS A 974  ? 2.2997 3.2900 2.8461 0.9595  -0.4595 -1.2357 974  LYS A N   
7353  C CA  . LYS A 974  ? 2.2599 3.2299 2.7952 0.9441  -0.4472 -1.1940 974  LYS A CA  
7354  C C   . LYS A 974  ? 2.1154 3.0886 2.6849 0.9069  -0.4272 -1.1637 974  LYS A C   
7355  O O   . LYS A 974  ? 2.0642 3.0642 2.6945 0.8933  -0.4177 -1.1800 974  LYS A O   
7356  C CB  . LYS A 974  ? 2.3145 3.2960 2.8781 0.9551  -0.4448 -1.2068 974  LYS A CB  
7357  C CG  . LYS A 974  ? 2.3612 3.3299 2.9323 0.9358  -0.4281 -1.1670 974  LYS A CG  
7358  C CD  . LYS A 974  ? 2.4621 3.4402 3.0560 0.9506  -0.4273 -1.1830 974  LYS A CD  
7359  C CE  . LYS A 974  ? 2.4786 3.4452 3.0829 0.9321  -0.4094 -1.1434 974  LYS A CE  
7360  N NZ  . LYS A 974  ? 2.5046 3.4797 3.1313 0.9472  -0.4082 -1.1605 974  LYS A NZ  
7361  N N   . ARG A 975  ? 1.2114 2.1590 1.7430 0.8904  -0.4206 -1.1197 975  ARG A N   
7362  C CA  . ARG A 975  ? 1.2418 2.1936 1.8004 0.8550  -0.4018 -1.0877 975  ARG A CA  
7363  C C   . ARG A 975  ? 1.1703 2.1004 1.7023 0.8374  -0.3903 -1.0372 975  ARG A C   
7364  O O   . ARG A 975  ? 1.2247 2.1269 1.6965 0.8473  -0.3986 -1.0183 975  ARG A O   
7365  C CB  . ARG A 975  ? 1.2100 2.1625 1.7576 0.8453  -0.4051 -1.0913 975  ARG A CB  
7366  C CG  . ARG A 975  ? 1.2478 2.1744 1.7270 0.8656  -0.4222 -1.0945 975  ARG A CG  
7367  C CD  . ARG A 975  ? 1.2401 2.1742 1.7186 0.8658  -0.4286 -1.1158 975  ARG A CD  
7368  N NE  . ARG A 975  ? 1.2867 2.1894 1.6973 0.8710  -0.4371 -1.1002 975  ARG A NE  
7369  C CZ  . ARG A 975  ? 1.2659 2.1644 1.6615 0.8623  -0.4384 -1.1010 975  ARG A CZ  
7370  N NH1 . ARG A 975  ? 1.1944 2.1197 1.6384 0.8481  -0.4323 -1.1163 975  ARG A NH1 
7371  N NH2 . ARG A 975  ? 1.3191 2.1860 1.6510 0.8677  -0.4452 -1.0862 975  ARG A NH2 
7372  N N   . ILE A 976  ? 1.4514 2.3964 2.0306 0.8111  -0.3704 -1.0156 976  ILE A N   
7373  C CA  . ILE A 976  ? 1.3850 2.3166 1.9504 0.7927  -0.3567 -0.9679 976  ILE A CA  
7374  C C   . ILE A 976  ? 1.3161 2.2474 1.8760 0.7625  -0.3460 -0.9355 976  ILE A C   
7375  O O   . ILE A 976  ? 1.3098 2.2580 1.8965 0.7520  -0.3442 -0.9503 976  ILE A O   
7376  C CB  . ILE A 976  ? 1.3438 2.2935 1.9668 0.7840  -0.3395 -0.9626 976  ILE A CB  
7377  C CG1 . ILE A 976  ? 1.4138 2.3780 2.0677 0.8089  -0.3484 -1.0103 976  ILE A CG1 
7378  C CG2 . ILE A 976  ? 1.3319 2.2628 1.9270 0.7800  -0.3319 -0.9214 976  ILE A CG2 
7379  C CD1 . ILE A 976  ? 1.4145 2.4026 2.1396 0.7995  -0.3314 -1.0189 976  ILE A CD1 
7380  N N   . LEU A 977  ? 1.3596 2.2736 1.8865 0.7480  -0.3383 -0.8909 977  LEU A N   
7381  C CA  . LEU A 977  ? 1.2550 2.1639 1.7603 0.7207  -0.3305 -0.8562 977  LEU A CA  
7382  C C   . LEU A 977  ? 1.2139 2.1239 1.7258 0.6992  -0.3124 -0.8094 977  LEU A C   
7383  O O   . LEU A 977  ? 1.2701 2.1571 1.7355 0.7039  -0.3157 -0.7844 977  LEU A O   
7384  C CB  . LEU A 977  ? 1.2924 2.1695 1.7236 0.7327  -0.3471 -0.8530 977  LEU A CB  
7385  C CG  . LEU A 977  ? 1.3066 2.1688 1.6954 0.7106  -0.3443 -0.8210 977  LEU A CG  
7386  C CD1 . LEU A 977  ? 1.3029 2.1660 1.6843 0.7138  -0.3540 -0.8490 977  LEU A CD1 
7387  C CD2 . LEU A 977  ? 1.4047 2.2326 1.7261 0.7228  -0.3539 -0.8012 977  LEU A CD2 
7388  N N   . SER A 978  ? 1.1136 2.0512 1.6840 0.6767  -0.2931 -0.7974 978  SER A N   
7389  C CA  . SER A 978  ? 1.1117 2.0558 1.6986 0.6576  -0.2734 -0.7544 978  SER A CA  
7390  C C   . SER A 978  ? 1.1962 2.1447 1.7679 0.6261  -0.2620 -0.7126 978  SER A C   
7391  O O   . SER A 978  ? 1.2097 2.1827 1.8202 0.6062  -0.2511 -0.7110 978  SER A O   
7392  C CB  . SER A 978  ? 1.0521 2.0244 1.7151 0.6534  -0.2566 -0.7643 978  SER A CB  
7393  O OG  . SER A 978  ? 1.0070 1.9809 1.6817 0.6437  -0.2398 -0.7276 978  SER A OG  
7394  N N   . VAL A 979  ? 1.0946 2.0208 1.6103 0.6216  -0.2644 -0.6788 979  VAL A N   
7395  C CA  . VAL A 979  ? 1.0335 1.9625 1.5270 0.5924  -0.2553 -0.6393 979  VAL A CA  
7396  C C   . VAL A 979  ? 0.9994 1.9384 1.5058 0.5751  -0.2360 -0.5930 979  VAL A C   
7397  O O   . VAL A 979  ? 1.0666 1.9860 1.5388 0.5847  -0.2391 -0.5747 979  VAL A O   
7398  C CB  . VAL A 979  ? 1.0631 1.9589 1.4791 0.5972  -0.2719 -0.6334 979  VAL A CB  
7399  C CG1 . VAL A 979  ? 1.0217 1.9235 1.4262 0.5753  -0.2707 -0.6279 979  VAL A CG1 
7400  C CG2 . VAL A 979  ? 1.1171 1.9904 1.5064 0.6307  -0.2934 -0.6748 979  VAL A CG2 
7401  N N   . LYS A 980  ? 1.5784 2.5491 2.1343 0.5501  -0.2158 -0.5730 980  LYS A N   
7402  C CA  . LYS A 980  ? 1.5730 2.5575 2.1441 0.5319  -0.1953 -0.5262 980  LYS A CA  
7403  C C   . LYS A 980  ? 1.5140 2.5229 2.0924 0.4976  -0.1799 -0.4895 980  LYS A C   
7404  O O   . LYS A 980  ? 1.4954 2.5239 2.1014 0.4861  -0.1772 -0.5034 980  LYS A O   
7405  C CB  . LYS A 980  ? 1.5584 2.5612 2.1948 0.5393  -0.1806 -0.5341 980  LYS A CB  
7406  C CG  . LYS A 980  ? 1.5609 2.5711 2.2399 0.5565  -0.1877 -0.5863 980  LYS A CG  
7407  C CD  . LYS A 980  ? 1.6068 2.5889 2.2536 0.5892  -0.2092 -0.6215 980  LYS A CD  
7408  C CE  . LYS A 980  ? 1.5903 2.5600 2.2290 0.6009  -0.2043 -0.6032 980  LYS A CE  
7409  N NZ  . LYS A 980  ? 1.6396 2.5829 2.2440 0.6335  -0.2250 -0.6341 980  LYS A NZ  
7410  N N   . GLY A 981  ? 1.0920 2.1011 1.6452 0.4816  -0.1699 -0.4425 981  GLY A N   
7411  C CA  . GLY A 981  ? 1.0153 2.0533 1.5809 0.4489  -0.1525 -0.4040 981  GLY A CA  
7412  C C   . GLY A 981  ? 0.9249 2.0008 1.5664 0.4378  -0.1286 -0.3934 981  GLY A C   
7413  O O   . GLY A 981  ? 0.9281 2.0055 1.6037 0.4510  -0.1204 -0.3965 981  GLY A O   
7414  N N   . LEU A 982  ? 0.6171 1.7237 1.2847 0.4135  -0.1169 -0.3809 982  LEU A N   
7415  C CA  . LEU A 982  ? 0.6860 1.8321 1.4265 0.4003  -0.0926 -0.3675 982  LEU A CA  
7416  C C   . LEU A 982  ? 0.5728 1.7298 1.3704 0.4122  -0.0933 -0.4122 982  LEU A C   
7417  O O   . LEU A 982  ? 0.5899 1.7230 1.3786 0.4365  -0.1109 -0.4545 982  LEU A O   
7418  C CB  . LEU A 982  ? 0.6350 1.7867 1.3971 0.4022  -0.0749 -0.3361 982  LEU A CB  
7419  C CG  . LEU A 982  ? 0.6282 1.7792 1.3494 0.3877  -0.0672 -0.2835 982  LEU A CG  
7420  C CD1 . LEU A 982  ? 0.5768 1.7699 1.3474 0.3651  -0.0373 -0.2393 982  LEU A CD1 
7421  C CD2 . LEU A 982  ? 0.6521 1.7874 1.3025 0.3760  -0.0828 -0.2722 982  LEU A CD2 
7422  N N   . LEU A 983  ? 1.3918 2.5869 2.2479 0.3946  -0.0739 -0.4019 983  LEU A N   
7423  C CA  . LEU A 983  ? 1.3912 2.6014 2.3068 0.4024  -0.0719 -0.4403 983  LEU A CA  
7424  C C   . LEU A 983  ? 1.4744 2.6846 2.4364 0.4170  -0.0601 -0.4470 983  LEU A C   
7425  O O   . LEU A 983  ? 1.4537 2.6737 2.4697 0.4263  -0.0565 -0.4790 983  LEU A O   
7426  C CB  . LEU A 983  ? 1.2847 2.5371 2.2468 0.3774  -0.0534 -0.4222 983  LEU A CB  
7427  C CG  . LEU A 983  ? 1.2768 2.5346 2.2144 0.3662  -0.0657 -0.4349 983  LEU A CG  
7428  C CD1 . LEU A 983  ? 1.3193 2.5392 2.1753 0.3739  -0.0907 -0.4445 983  LEU A CD1 
7429  C CD2 . LEU A 983  ? 1.2512 2.5478 2.2064 0.3360  -0.0465 -0.3938 983  LEU A CD2 
7430  N N   . VAL A 984  ? 0.6377 2.0927 1.8038 0.2665  0.0966  -0.4098 984  VAL A N   
7431  C CA  . VAL A 984  ? 0.6861 2.1343 1.8264 0.2971  0.0868  -0.4045 984  VAL A CA  
7432  C C   . VAL A 984  ? 0.8859 2.3130 1.9766 0.3564  0.0847  -0.3854 984  VAL A C   
7433  O O   . VAL A 984  ? 0.9116 2.3254 1.9594 0.3837  0.0887  -0.3686 984  VAL A O   
7434  C CB  . VAL A 984  ? 0.6790 2.1290 1.7905 0.2601  0.1156  -0.3766 984  VAL A CB  
7435  C CG1 . VAL A 984  ? 0.7017 2.1410 1.7537 0.2558  0.1522  -0.3309 984  VAL A CG1 
7436  C CG2 . VAL A 984  ? 0.6730 2.1202 1.7750 0.2822  0.1023  -0.3805 984  VAL A CG2 
7437  N N   . GLY A 985  ? 1.3726 2.7935 2.4693 0.3764  0.0777  -0.3903 985  GLY A N   
7438  C CA  . GLY A 985  ? 1.4158 2.8100 2.4661 0.4347  0.0708  -0.3780 985  GLY A CA  
7439  C C   . GLY A 985  ? 1.4631 2.8193 2.5034 0.4821  0.0209  -0.4052 985  GLY A C   
7440  O O   . GLY A 985  ? 1.5938 2.8908 2.5489 0.5173  0.0098  -0.3910 985  GLY A O   
7441  N N   . GLU A 986  ? 0.9362 2.3113 2.0457 0.4761  -0.0119 -0.4447 986  GLU A N   
7442  C CA  . GLU A 986  ? 0.9838 2.3137 2.0727 0.5114  -0.0620 -0.4725 986  GLU A CA  
7443  C C   . GLU A 986  ? 0.9857 2.3010 2.0366 0.5204  -0.0634 -0.4672 986  GLU A C   
7444  O O   . GLU A 986  ? 1.1008 2.3609 2.0818 0.5558  -0.0842 -0.4628 986  GLU A O   
7445  C CB  . GLU A 986  ? 0.9536 2.3180 2.1333 0.4966  -0.0919 -0.5189 986  GLU A CB  
7446  C CG  . GLU A 986  ? 1.0578 2.3774 2.2263 0.5338  -0.1425 -0.5467 986  GLU A CG  
7447  C CD  . GLU A 986  ? 1.1728 2.4366 2.2707 0.5651  -0.1461 -0.5217 986  GLU A CD  
7448  O OE1 . GLU A 986  ? 1.2040 2.4455 2.3148 0.5842  -0.1791 -0.5413 986  GLU A OE1 
7449  O OE2 . GLU A 986  ? 1.2314 2.4724 2.2590 0.5702  -0.1166 -0.4832 986  GLU A OE2 
7450  N N   . ILE A 987  ? 0.8558 2.2222 1.9546 0.4855  -0.0400 -0.4673 987  ILE A N   
7451  C CA  . ILE A 987  ? 0.8456 2.2064 1.9165 0.4874  -0.0337 -0.4588 987  ILE A CA  
7452  C C   . ILE A 987  ? 0.9353 2.2645 1.9233 0.5032  -0.0049 -0.4160 987  ILE A C   
7453  O O   . ILE A 987  ? 0.9783 2.2855 1.9256 0.5167  -0.0057 -0.4086 987  ILE A O   
7454  C CB  . ILE A 987  ? 0.7299 2.1463 1.8672 0.4383  -0.0165 -0.4688 987  ILE A CB  
7455  C CG1 . ILE A 987  ? 0.7666 2.2022 1.9712 0.4179  -0.0471 -0.5161 987  ILE A CG1 
7456  C CG2 . ILE A 987  ? 0.6712 2.0838 1.7853 0.4416  -0.0109 -0.4608 987  ILE A CG2 
7457  C CD1 . ILE A 987  ? 0.7694 2.2292 2.0093 0.3524  -0.0300 -0.5262 987  ILE A CD1 
7458  N N   . LEU A 988  ? 0.5902 1.9172 1.5524 0.5012  0.0209  -0.3898 988  LEU A N   
7459  C CA  . LEU A 988  ? 0.6634 1.9541 1.5386 0.5193  0.0446  -0.3540 988  LEU A CA  
7460  C C   . LEU A 988  ? 0.8002 2.0176 1.5962 0.5628  0.0127  -0.3569 988  LEU A C   
7461  O O   . LEU A 988  ? 0.8931 2.0727 1.6292 0.5838  0.0072  -0.3492 988  LEU A O   
7462  C CB  . LEU A 988  ? 0.6408 1.9586 1.5120 0.4980  0.0885  -0.3247 988  LEU A CB  
7463  C CG  . LEU A 988  ? 0.5862 1.9423 1.4601 0.4677  0.1327  -0.2967 988  LEU A CG  
7464  C CD1 . LEU A 988  ? 0.6078 1.9621 1.4393 0.4478  0.1697  -0.2655 988  LEU A CD1 
7465  C CD2 . LEU A 988  ? 0.5944 1.9231 1.4156 0.4905  0.1331  -0.2857 988  LEU A CD2 
7466  N N   . SER A 989  ? 1.1613 2.3591 1.9597 0.5745  -0.0093 -0.3690 989  SER A N   
7467  C CA  . SER A 989  ? 1.2592 2.3866 1.9834 0.6129  -0.0413 -0.3707 989  SER A CA  
7468  C C   . SER A 989  ? 1.2757 2.3706 1.9804 0.6368  -0.0782 -0.3907 989  SER A C   
7469  O O   . SER A 989  ? 1.3459 2.3882 1.9712 0.6613  -0.0864 -0.3794 989  SER A O   
7470  C CB  . SER A 989  ? 1.3095 2.4284 2.0585 0.6188  -0.0636 -0.3855 989  SER A CB  
7471  O OG  . SER A 989  ? 1.4484 2.4990 2.1145 0.6505  -0.0837 -0.3762 989  SER A OG  
7472  N N   . ALA A 990  ? 1.6921 2.8200 2.4685 0.6271  -0.0985 -0.4217 990  ALA A N   
7473  C CA  . ALA A 990  ? 1.7453 2.8515 2.5100 0.6452  -0.1287 -0.4425 990  ALA A CA  
7474  C C   . ALA A 990  ? 1.7839 2.8639 2.4810 0.6544  -0.1099 -0.4186 990  ALA A C   
7475  O O   . ALA A 990  ? 1.9137 2.9409 2.5454 0.6821  -0.1304 -0.4176 990  ALA A O   
7476  C CB  . ALA A 990  ? 1.6719 2.8306 2.5233 0.6221  -0.1368 -0.4740 990  ALA A CB  
7477  N N   . VAL A 991  ? 1.0512 2.1685 1.7650 0.6301  -0.0710 -0.3994 991  VAL A N   
7478  C CA  . VAL A 991  ? 1.0943 2.1941 1.7567 0.6363  -0.0523 -0.3798 991  VAL A CA  
7479  C C   . VAL A 991  ? 1.1871 2.2505 1.7677 0.6476  -0.0293 -0.3477 991  VAL A C   
7480  O O   . VAL A 991  ? 1.2461 2.2890 1.7785 0.6555  -0.0167 -0.3340 991  VAL A O   
7481  C CB  . VAL A 991  ? 0.7014 1.8559 1.4200 0.6062  -0.0252 -0.3764 991  VAL A CB  
7482  C CG1 . VAL A 991  ? 0.7084 1.8573 1.3814 0.6052  0.0088  -0.3457 991  VAL A CG1 
7483  C CG2 . VAL A 991  ? 0.6885 1.8537 1.4496 0.6053  -0.0521 -0.4086 991  VAL A CG2 
7484  N N   . LEU A 992  ? 1.1212 2.1744 1.6831 0.6485  -0.0244 -0.3376 992  LEU A N   
7485  C CA  . LEU A 992  ? 1.2598 2.2762 1.7375 0.6578  -0.0027 -0.3101 992  LEU A CA  
7486  C C   . LEU A 992  ? 1.5468 2.5108 1.9696 0.6782  -0.0258 -0.3110 992  LEU A C   
7487  O O   . LEU A 992  ? 1.6192 2.5813 2.0191 0.6718  -0.0057 -0.2948 992  LEU A O   
7488  C CB  . LEU A 992  ? 1.0977 2.1577 1.5876 0.6315  0.0468  -0.2841 992  LEU A CB  
7489  C CG  . LEU A 992  ? 0.9505 2.0603 1.4837 0.6094  0.0759  -0.2753 992  LEU A CG  
7490  C CD1 . LEU A 992  ? 0.8445 2.0063 1.4064 0.5795  0.1206  -0.2528 992  LEU A CD1 
7491  C CD2 . LEU A 992  ? 1.0001 2.0820 1.4787 0.6232  0.0825  -0.2658 992  LEU A CD2 
7492  N N   . SER A 993  ? 2.3147 3.2356 2.7148 0.7022  -0.0682 -0.3299 993  SER A N   
7493  C CA  . SER A 993  ? 2.5156 3.3801 2.8609 0.7236  -0.0975 -0.3322 993  SER A CA  
7494  C C   . SER A 993  ? 2.7176 3.5372 3.0284 0.7474  -0.1368 -0.3483 993  SER A C   
7495  O O   . SER A 993  ? 2.8453 3.6055 3.0811 0.7656  -0.1567 -0.3436 993  SER A O   
7496  C CB  . SER A 993  ? 2.4655 3.3503 2.8725 0.7202  -0.1156 -0.3477 993  SER A CB  
7497  O OG  . SER A 993  ? 2.3824 3.3116 2.8236 0.6952  -0.0768 -0.3327 993  SER A OG  
7498  N N   . GLN A 994  ? 1.7618 2.6104 2.1274 0.7452  -0.1483 -0.3683 994  GLN A N   
7499  C CA  . GLN A 994  ? 1.9346 2.7497 2.2665 0.7629  -0.1735 -0.3803 994  GLN A CA  
7500  C C   . GLN A 994  ? 1.9296 2.7606 2.2498 0.7522  -0.1401 -0.3670 994  GLN A C   
7501  O O   . GLN A 994  ? 1.8108 2.6852 2.1648 0.7315  -0.1043 -0.3537 994  GLN A O   
7502  C CB  . GLN A 994  ? 1.9728 2.8076 2.3683 0.7685  -0.2084 -0.4138 994  GLN A CB  
7503  C CG  . GLN A 994  ? 1.9038 2.8036 2.3835 0.7458  -0.1904 -0.4262 994  GLN A CG  
7504  C CD  . GLN A 994  ? 1.9433 2.8503 2.4506 0.7522  -0.2149 -0.4550 994  GLN A CD  
7505  O OE1 . GLN A 994  ? 2.0504 2.9171 2.5183 0.7741  -0.2457 -0.4665 994  GLN A OE1 
7506  N NE2 . GLN A 994  ? 1.8453 2.8040 2.4184 0.7311  -0.2004 -0.4669 994  GLN A NE2 
7507  N N   . GLU A 995  ? 2.0305 2.8261 2.3024 0.7655  -0.1515 -0.3699 995  GLU A N   
7508  C CA  . GLU A 995  ? 2.0749 2.8877 2.3483 0.7571  -0.1253 -0.3633 995  GLU A CA  
7509  C C   . GLU A 995  ? 2.0638 2.8918 2.3825 0.7613  -0.1481 -0.3897 995  GLU A C   
7510  O O   . GLU A 995  ? 2.0453 2.8779 2.3990 0.7677  -0.1795 -0.4121 995  GLU A O   
7511  C CB  . GLU A 995  ? 2.2322 2.9968 2.4182 0.7654  -0.1158 -0.3477 995  GLU A CB  
7512  C CG  . GLU A 995  ? 2.2697 3.0383 2.4211 0.7533  -0.0760 -0.3209 995  GLU A CG  
7513  C CD  . GLU A 995  ? 2.3949 3.1083 2.4603 0.7618  -0.0822 -0.3100 995  GLU A CD  
7514  O OE1 . GLU A 995  ? 2.4801 3.1526 2.5176 0.7768  -0.1197 -0.3213 995  GLU A OE1 
7515  O OE2 . GLU A 995  ? 2.4056 3.1163 2.4297 0.7526  -0.0498 -0.2905 995  GLU A OE2 
7516  N N   . GLY A 996  ? 2.2853 3.1219 2.6038 0.7573  -0.1318 -0.3884 996  GLY A N   
7517  C CA  . GLY A 996  ? 2.3086 3.1578 2.6627 0.7603  -0.1495 -0.4133 996  GLY A CA  
7518  C C   . GLY A 996  ? 2.2339 3.1333 2.6713 0.7465  -0.1562 -0.4327 996  GLY A C   
7519  O O   . GLY A 996  ? 2.2302 3.1332 2.6913 0.7493  -0.1785 -0.4453 996  GLY A O   
7520  N N   . ILE A 997  ? 2.7439 3.6813 3.2262 0.7302  -0.1374 -0.4363 997  ILE A N   
7521  C CA  . ILE A 997  ? 2.6581 3.6448 3.2192 0.7116  -0.1419 -0.4570 997  ILE A CA  
7522  C C   . ILE A 997  ? 2.7332 3.7115 3.3110 0.7246  -0.1835 -0.4910 997  ILE A C   
7523  O O   . ILE A 997  ? 2.8352 3.7722 3.3652 0.7472  -0.2066 -0.4980 997  ILE A O   
7524  C CB  . ILE A 997  ? 2.5545 3.5717 3.1490 0.6949  -0.1223 -0.4600 997  ILE A CB  
7525  C CG1 . ILE A 997  ? 2.6046 3.6006 3.1806 0.7092  -0.1411 -0.4818 997  ILE A CG1 
7526  C CG2 . ILE A 997  ? 2.5402 3.5589 3.1103 0.6873  -0.0842 -0.4260 997  ILE A CG2 
7527  C CD1 . ILE A 997  ? 2.5591 3.5768 3.1575 0.6951  -0.1209 -0.4824 997  ILE A CD1 
7528  N N   . ASN A 998  ? 2.3251 3.3431 2.9708 0.7091  -0.1934 -0.5129 998  ASN A N   
7529  C CA  . ASN A 998  ? 2.3672 3.3788 3.0313 0.7220  -0.2331 -0.5447 998  ASN A CA  
7530  C C   . ASN A 998  ? 2.2020 3.2660 2.9505 0.6990  -0.2408 -0.5756 998  ASN A C   
7531  O O   . ASN A 998  ? 2.1541 3.2560 2.9464 0.6729  -0.2171 -0.5657 998  ASN A O   
7532  C CB  . ASN A 998  ? 2.5178 3.4945 3.1443 0.7392  -0.2463 -0.5302 998  ASN A CB  
7533  C CG  . ASN A 998  ? 2.5823 3.5737 3.2580 0.7404  -0.2760 -0.5566 998  ASN A CG  
7534  O OD1 . ASN A 998  ? 2.6368 3.6311 3.3352 0.7491  -0.3073 -0.5903 998  ASN A OD1 
7535  N ND2 . ASN A 998  ? 2.5792 3.5797 3.2704 0.7321  -0.2659 -0.5422 998  ASN A ND2 
7536  N N   . ILE A 999  ? 2.2518 3.3190 3.0222 0.7066  -0.2730 -0.6142 999  ILE A N   
7537  C CA  . ILE A 999  ? 2.0561 3.1717 2.9052 0.6843  -0.2844 -0.6512 999  ILE A CA  
7538  C C   . ILE A 999  ? 1.9232 3.0496 2.8090 0.6826  -0.2984 -0.6577 999  ILE A C   
7539  O O   . ILE A 999  ? 1.9487 3.0371 2.7964 0.7081  -0.3166 -0.6479 999  ILE A O   
7540  C CB  . ILE A 999  ? 3.4932 4.6085 4.3503 0.6942  -0.3152 -0.6942 999  ILE A CB  
7541  C CG1 . ILE A 999  ? 3.5285 4.6281 4.3437 0.6986  -0.3017 -0.6879 999  ILE A CG1 
7542  C CG2 . ILE A 999  ? 3.4060 4.5738 4.3433 0.6659  -0.3233 -0.7349 999  ILE A CG2 
7543  C CD1 . ILE A 999  ? 3.4485 4.5805 4.2903 0.6681  -0.2673 -0.6762 999  ILE A CD1 
7544  N N   . LEU A 1000 ? 1.3273 2.5046 2.2871 0.6511  -0.2903 -0.6745 1000 LEU A N   
7545  C CA  . LEU A 1000 ? 1.2046 2.3944 2.2013 0.6464  -0.2967 -0.6760 1000 LEU A CA  
7546  C C   . LEU A 1000 ? 1.1688 2.3764 2.2209 0.6480  -0.3343 -0.7244 1000 LEU A C   
7547  O O   . LEU A 1000 ? 1.1257 2.3605 2.2336 0.6334  -0.3376 -0.7362 1000 LEU A O   
7548  C CB  . LEU A 1000 ? 1.0255 2.2563 2.0614 0.6107  -0.2575 -0.6527 1000 LEU A CB  
7549  C CG  . LEU A 1000 ? 0.9311 2.1308 1.9029 0.6220  -0.2292 -0.6021 1000 LEU A CG  
7550  C CD1 . LEU A 1000 ? 0.8194 2.0579 1.8150 0.5880  -0.1849 -0.5746 1000 LEU A CD1 
7551  C CD2 . LEU A 1000 ? 0.9510 2.1202 1.8996 0.6432  -0.2435 -0.5923 1000 LEU A CD2 
7552  N N   . THR A 1001 ? 1.7007 2.8925 2.7362 0.6666  -0.3626 -0.7532 1001 THR A N   
7553  C CA  . THR A 1001 ? 1.7035 2.9056 2.7813 0.6749  -0.4019 -0.7993 1001 THR A CA  
7554  C C   . THR A 1001 ? 1.8588 3.0146 2.8769 0.7131  -0.4325 -0.8067 1001 THR A C   
7555  O O   . THR A 1001 ? 1.9413 3.0603 2.8904 0.7288  -0.4208 -0.7766 1001 THR A O   
7556  C CB  . THR A 1001 ? 1.5400 2.7943 2.6843 0.6428  -0.4025 -0.8431 1001 THR A CB  
7557  O OG1 . THR A 1001 ? 1.3978 2.6821 2.5585 0.6074  -0.3622 -0.8219 1001 THR A OG1 
7558  C CG2 . THR A 1001 ? 1.5011 2.7896 2.7223 0.6304  -0.4251 -0.8824 1001 THR A CG2 
7559  N N   . HIS A 1002 ? 1.3865 2.5452 2.4319 0.7271  -0.4717 -0.8476 1002 HIS A N   
7560  C CA  . HIS A 1002 ? 1.5328 2.6533 2.5261 0.7606  -0.5018 -0.8588 1002 HIS A CA  
7561  C C   . HIS A 1002 ? 1.2025 2.3427 2.1961 0.7507  -0.4985 -0.8877 1002 HIS A C   
7562  O O   . HIS A 1002 ? 1.2888 2.4068 2.2459 0.7737  -0.5211 -0.9037 1002 HIS A O   
7563  C CB  . HIS A 1002 ? 1.6846 2.7974 2.7032 0.7828  -0.5469 -0.8888 1002 HIS A CB  
7564  C CG  . HIS A 1002 ? 1.8193 2.8981 2.8184 0.7997  -0.5541 -0.8573 1002 HIS A CG  
7565  N ND1 . HIS A 1002 ? 1.7924 2.8961 2.8438 0.7807  -0.5411 -0.8513 1002 HIS A ND1 
7566  C CD2 . HIS A 1002 ? 1.9600 2.9809 2.8908 0.8322  -0.5728 -0.8308 1002 HIS A CD2 
7567  C CE1 . HIS A 1002 ? 1.8658 2.9276 2.8805 0.8021  -0.5506 -0.8224 1002 HIS A CE1 
7568  N NE2 . HIS A 1002 ? 1.9677 2.9776 2.9081 0.8331  -0.5710 -0.8097 1002 HIS A NE2 
7569  N N   . LEU A 1003 ? 1.4692 2.6502 2.5010 0.7153  -0.4694 -0.8933 1003 LEU A N   
7570  C CA  . LEU A 1003 ? 1.3953 2.5944 2.4268 0.7028  -0.4648 -0.9216 1003 LEU A CA  
7571  C C   . LEU A 1003 ? 1.4875 2.6487 2.4425 0.7216  -0.4534 -0.8979 1003 LEU A C   
7572  O O   . LEU A 1003 ? 1.5333 2.6722 2.4480 0.7229  -0.4261 -0.8527 1003 LEU A O   
7573  C CB  . LEU A 1003 ? 1.1804 2.4296 2.2695 0.6578  -0.4380 -0.9330 1003 LEU A CB  
7574  C CG  . LEU A 1003 ? 1.0446 2.3357 2.2120 0.6396  -0.4604 -0.9810 1003 LEU A CG  
7575  C CD1 . LEU A 1003 ? 0.9299 2.2621 2.1352 0.6058  -0.4558 -1.0241 1003 LEU A CD1 
7576  C CD2 . LEU A 1003 ? 1.1038 2.3752 2.2662 0.6744  -0.5039 -1.0086 1003 LEU A CD2 
7577  N N   . PRO A 1004 ? 1.4181 2.5748 2.3557 0.7348  -0.4738 -0.9314 1004 PRO A N   
7578  C CA  . PRO A 1004 ? 1.4555 2.5837 2.3302 0.7521  -0.4710 -0.9266 1004 PRO A CA  
7579  C C   . PRO A 1004 ? 1.4001 2.5296 2.2534 0.7338  -0.4314 -0.9013 1004 PRO A C   
7580  O O   . PRO A 1004 ? 1.3136 2.4796 2.2082 0.7029  -0.4150 -0.9179 1004 PRO A O   
7581  C CB  . PRO A 1004 ? 1.5006 2.6543 2.3998 0.7499  -0.4947 -0.9846 1004 PRO A CB  
7582  C CG  . PRO A 1004 ? 1.3934 2.5939 2.3723 0.7231  -0.5022 -1.0184 1004 PRO A CG  
7583  C CD  . PRO A 1004 ? 1.3768 2.5661 2.3699 0.7296  -0.5045 -0.9871 1004 PRO A CD  
7584  N N   . LYS A 1005 ? 1.2706 2.3599 2.0594 0.7521  -0.4182 -0.8646 1005 LYS A N   
7585  C CA  . LYS A 1005 ? 1.2962 2.3807 2.0618 0.7388  -0.3800 -0.8328 1005 LYS A CA  
7586  C C   . LYS A 1005 ? 1.2736 2.3762 2.0418 0.7232  -0.3668 -0.8573 1005 LYS A C   
7587  O O   . LYS A 1005 ? 1.2225 2.3218 1.9748 0.7117  -0.3360 -0.8337 1005 LYS A O   
7588  C CB  . LYS A 1005 ? 1.4528 2.4888 2.1490 0.7627  -0.3722 -0.7923 1005 LYS A CB  
7589  C CG  . LYS A 1005 ? 1.5645 2.5797 2.2495 0.7722  -0.3743 -0.7589 1005 LYS A CG  
7590  C CD  . LYS A 1005 ? 1.5660 2.5984 2.2716 0.7496  -0.3393 -0.7271 1005 LYS A CD  
7591  C CE  . LYS A 1005 ? 1.6238 2.6473 2.2975 0.7430  -0.3056 -0.7027 1005 LYS A CE  
7592  N NZ  . LYS A 1005 ? 1.5700 2.6103 2.2623 0.7225  -0.2726 -0.6703 1005 LYS A NZ  
7593  N N   . GLY A 1006 ? 1.5074 2.6293 2.2960 0.7221  -0.3902 -0.9060 1006 GLY A N   
7594  C CA  . GLY A 1006 ? 1.5431 2.6751 2.3209 0.7127  -0.3823 -0.9342 1006 GLY A CA  
7595  C C   . GLY A 1006 ? 1.4234 2.5721 2.2138 0.6832  -0.3489 -0.9242 1006 GLY A C   
7596  O O   . GLY A 1006 ? 1.4183 2.5468 2.1685 0.6870  -0.3266 -0.9035 1006 GLY A O   
7597  N N   . SER A 1007 ? 1.7379 2.9237 2.5857 0.6524  -0.3462 -0.9398 1007 SER A N   
7598  C CA  . SER A 1007 ? 1.6364 2.8417 2.5024 0.6197  -0.3187 -0.9350 1007 SER A CA  
7599  C C   . SER A 1007 ? 1.5707 2.7527 2.4065 0.6234  -0.2876 -0.8806 1007 SER A C   
7600  O O   . SER A 1007 ? 1.5769 2.7271 2.3745 0.6502  -0.2857 -0.8474 1007 SER A O   
7601  C CB  . SER A 1007 ? 1.5724 2.8197 2.5068 0.5846  -0.3203 -0.9503 1007 SER A CB  
7602  O OG  . SER A 1007 ? 1.5282 2.7935 2.4795 0.5502  -0.2950 -0.9437 1007 SER A OG  
7603  N N   . ALA A 1008 ? 1.1686 2.3667 2.0212 0.5946  -0.2641 -0.8738 1008 ALA A N   
7604  C CA  . ALA A 1008 ? 1.1514 2.3400 1.9952 0.5896  -0.2343 -0.8241 1008 ALA A CA  
7605  C C   . ALA A 1008 ? 1.0651 2.2769 1.9530 0.5743  -0.2326 -0.8068 1008 ALA A C   
7606  O O   . ALA A 1008 ? 1.0776 2.2740 1.9499 0.5876  -0.2212 -0.7665 1008 ALA A O   
7607  C CB  . ALA A 1008 ? 1.1363 2.3357 1.9869 0.5625  -0.2133 -0.8262 1008 ALA A CB  
7608  N N   . GLU A 1009 ? 1.0745 2.3245 2.0169 0.5444  -0.2434 -0.8405 1009 GLU A N   
7609  C CA  . GLU A 1009 ? 0.9970 2.2762 1.9902 0.5241  -0.2425 -0.8325 1009 GLU A CA  
7610  C C   . GLU A 1009 ? 1.0078 2.2627 1.9774 0.5546  -0.2446 -0.7989 1009 GLU A C   
7611  O O   . GLU A 1009 ? 0.9883 2.2428 1.9574 0.5502  -0.2224 -0.7577 1009 GLU A O   
7612  C CB  . GLU A 1009 ? 0.9478 2.2600 1.9914 0.5058  -0.2690 -0.8862 1009 GLU A CB  
7613  C CG  . GLU A 1009 ? 0.8121 2.1649 1.9209 0.4714  -0.2638 -0.8852 1009 GLU A CG  
7614  C CD  . GLU A 1009 ? 0.7507 2.1398 1.9147 0.4469  -0.2876 -0.9424 1009 GLU A CD  
7615  O OE1 . GLU A 1009 ? 0.7696 2.1542 1.9209 0.4560  -0.3086 -0.9852 1009 GLU A OE1 
7616  O OE2 . GLU A 1009 ? 0.6878 2.1119 1.9086 0.4172  -0.2840 -0.9451 1009 GLU A OE2 
7617  N N   . ALA A 1010 ? 1.5353 2.7689 2.4822 0.5849  -0.2716 -0.8175 1010 ALA A N   
7618  C CA  . ALA A 1010 ? 1.6132 2.8201 2.5349 0.6134  -0.2793 -0.7911 1010 ALA A CA  
7619  C C   . ALA A 1010 ? 1.6126 2.7878 2.4836 0.6278  -0.2531 -0.7396 1010 ALA A C   
7620  O O   . ALA A 1010 ? 1.5628 2.7309 2.4284 0.6325  -0.2439 -0.7079 1010 ALA A O   
7621  C CB  . ALA A 1010 ? 1.7449 2.9279 2.6397 0.6446  -0.3125 -0.8179 1010 ALA A CB  
7622  N N   . GLU A 1011 ? 2.1118 3.2685 2.9453 0.6340  -0.2402 -0.7329 1011 GLU A N   
7623  C CA  . GLU A 1011 ? 2.1782 3.3066 2.9663 0.6460  -0.2147 -0.6882 1011 GLU A CA  
7624  C C   . GLU A 1011 ? 2.0945 3.2479 2.9125 0.6197  -0.1850 -0.6582 1011 GLU A C   
7625  O O   . GLU A 1011 ? 2.1200 3.2559 2.9078 0.6278  -0.1634 -0.6193 1011 GLU A O   
7626  C CB  . GLU A 1011 ? 2.2627 3.3692 3.0113 0.6558  -0.2067 -0.6913 1011 GLU A CB  
7627  C CG  . GLU A 1011 ? 2.3660 3.4275 3.0501 0.6850  -0.2010 -0.6637 1011 GLU A CG  
7628  C CD  . GLU A 1011 ? 2.4658 3.5015 3.1196 0.7114  -0.2313 -0.6777 1011 GLU A CD  
7629  O OE1 . GLU A 1011 ? 2.5068 3.5476 3.1666 0.7161  -0.2541 -0.7149 1011 GLU A OE1 
7630  O OE2 . GLU A 1011 ? 2.5114 3.5207 3.1329 0.7270  -0.2325 -0.6517 1011 GLU A OE2 
7631  N N   . LEU A 1012 ? 0.7981 1.9934 1.6743 0.5866  -0.1837 -0.6774 1012 LEU A N   
7632  C CA  . LEU A 1012 ? 0.6636 1.8892 1.5759 0.5570  -0.1577 -0.6509 1012 LEU A CA  
7633  C C   . LEU A 1012 ? 0.6708 1.9125 1.6102 0.5525  -0.1608 -0.6425 1012 LEU A C   
7634  O O   . LEU A 1012 ? 0.6659 1.9142 1.6058 0.5453  -0.1372 -0.6066 1012 LEU A O   
7635  C CB  . LEU A 1012 ? 0.5131 1.7752 1.4727 0.5187  -0.1528 -0.6734 1012 LEU A CB  
7636  C CG  . LEU A 1012 ? 0.4898 1.7383 1.4242 0.5163  -0.1357 -0.6629 1012 LEU A CG  
7637  C CD1 . LEU A 1012 ? 0.4374 1.7065 1.3991 0.4884  -0.1435 -0.7012 1012 LEU A CD1 
7638  C CD2 . LEU A 1012 ? 0.4518 1.7054 1.3860 0.5058  -0.1039 -0.6161 1012 LEU A CD2 
7639  N N   . MET A 1013 ? 1.5144 2.7612 2.4743 0.5583  -0.1898 -0.6760 1013 MET A N   
7640  C CA  . MET A 1013 ? 1.4912 2.7523 2.4797 0.5547  -0.1944 -0.6710 1013 MET A CA  
7641  C C   . MET A 1013 ? 1.5841 2.8100 2.5209 0.5817  -0.1843 -0.6302 1013 MET A C   
7642  O O   . MET A 1013 ? 1.5932 2.8262 2.5446 0.5801  -0.1833 -0.6195 1013 MET A O   
7643  C CB  . MET A 1013 ? 1.4899 2.7579 2.5069 0.5611  -0.2305 -0.7157 1013 MET A CB  
7644  C CG  . MET A 1013 ? 1.4272 2.7375 2.5121 0.5323  -0.2310 -0.7281 1013 MET A CG  
7645  S SD  . MET A 1013 ? 1.5930 2.9555 2.7343 0.4778  -0.2046 -0.7323 1013 MET A SD  
7646  C CE  . MET A 1013 ? 1.3292 2.6952 2.4756 0.4718  -0.2278 -0.7855 1013 MET A CE  
7647  N N   . SER A 1014 ? 1.2965 2.4850 2.1728 0.6045  -0.1759 -0.6092 1014 SER A N   
7648  C CA  . SER A 1014 ? 1.3514 2.5032 2.1710 0.6282  -0.1657 -0.5730 1014 SER A CA  
7649  C C   . SER A 1014 ? 1.2343 2.4028 2.0567 0.6101  -0.1277 -0.5341 1014 SER A C   
7650  O O   . SER A 1014 ? 1.2123 2.3694 2.0111 0.6171  -0.1162 -0.5075 1014 SER A O   
7651  C CB  . SER A 1014 ? 1.5215 2.6276 2.2762 0.6569  -0.1719 -0.5696 1014 SER A CB  
7652  O OG  . SER A 1014 ? 1.5491 2.6553 2.2900 0.6495  -0.1451 -0.5512 1014 SER A OG  
7653  N N   . VAL A 1015 ? 0.9552 2.1493 1.8036 0.5871  -0.1087 -0.5313 1015 VAL A N   
7654  C CA  . VAL A 1015 ? 0.9291 2.1406 1.7809 0.5697  -0.0727 -0.4947 1015 VAL A CA  
7655  C C   . VAL A 1015 ? 0.8586 2.1163 1.7661 0.5376  -0.0587 -0.4879 1015 VAL A C   
7656  O O   . VAL A 1015 ? 0.8742 2.1448 1.7786 0.5273  -0.0296 -0.4542 1015 VAL A O   
7657  C CB  . VAL A 1015 ? 0.9996 2.2179 1.8562 0.5576  -0.0578 -0.4913 1015 VAL A CB  
7658  C CG1 . VAL A 1015 ? 0.9791 2.2023 1.8575 0.5518  -0.0809 -0.5320 1015 VAL A CG1 
7659  C CG2 . VAL A 1015 ? 0.9404 2.1999 1.8372 0.5237  -0.0280 -0.4670 1015 VAL A CG2 
7660  N N   . VAL A 1016 ? 0.6892 1.9733 1.6484 0.5208  -0.0791 -0.5218 1016 VAL A N   
7661  C CA  . VAL A 1016 ? 0.5179 1.8479 1.5363 0.4880  -0.0689 -0.5218 1016 VAL A CA  
7662  C C   . VAL A 1016 ? 0.4548 1.7770 1.4531 0.4987  -0.0567 -0.4948 1016 VAL A C   
7663  O O   . VAL A 1016 ? 0.3830 1.7166 1.3722 0.4882  -0.0249 -0.4600 1016 VAL A O   
7664  C CB  . VAL A 1016 ? 0.4543 1.8113 1.5308 0.4697  -0.0963 -0.5691 1016 VAL A CB  
7665  C CG1 . VAL A 1016 ? 0.3854 1.7801 1.5157 0.4449  -0.0910 -0.5717 1016 VAL A CG1 
7666  C CG2 . VAL A 1016 ? 0.4138 1.7961 1.5234 0.4402  -0.0950 -0.5891 1016 VAL A CG2 
7667  N N   . PRO A 1017 ? 0.5386 1.8392 1.5261 0.5205  -0.0816 -0.5103 1017 PRO A N   
7668  C CA  . PRO A 1017 ? 0.5620 1.8609 1.5381 0.5235  -0.0677 -0.4862 1017 PRO A CA  
7669  C C   . PRO A 1017 ? 0.6008 1.8879 1.5279 0.5278  -0.0325 -0.4414 1017 PRO A C   
7670  O O   . PRO A 1017 ? 0.5463 1.8582 1.4886 0.5104  -0.0080 -0.4210 1017 PRO A O   
7671  C CB  . PRO A 1017 ? 0.6280 1.8806 1.5648 0.5605  -0.1015 -0.5010 1017 PRO A CB  
7672  C CG  . PRO A 1017 ? 0.6222 1.8813 1.5928 0.5607  -0.1337 -0.5438 1017 PRO A CG  
7673  C CD  . PRO A 1017 ? 0.5943 1.8703 1.5759 0.5438  -0.1218 -0.5473 1017 PRO A CD  
7674  N N   . VAL A 1018 ? 0.6384 1.8914 1.5098 0.5487  -0.0282 -0.4274 1018 VAL A N   
7675  C CA  . VAL A 1018 ? 0.7439 1.9926 1.5761 0.5486  0.0071  -0.3879 1018 VAL A CA  
7676  C C   . VAL A 1018 ? 0.6988 1.9975 1.5784 0.5132  0.0372  -0.3730 1018 VAL A C   
7677  O O   . VAL A 1018 ? 0.6604 1.9857 1.5499 0.4955  0.0655  -0.3491 1018 VAL A O   
7678  C CB  . VAL A 1018 ? 0.8836 2.0865 1.6488 0.5767  0.0065  -0.3772 1018 VAL A CB  
7679  C CG1 . VAL A 1018 ? 0.9284 2.1255 1.6499 0.5781  0.0413  -0.3395 1018 VAL A CG1 
7680  C CG2 . VAL A 1018 ? 0.9862 2.1407 1.7086 0.6085  -0.0276 -0.3956 1018 VAL A CG2 
7681  N N   . PHE A 1019 ? 1.2105 2.5227 2.1186 0.5010  0.0317  -0.3869 1019 PHE A N   
7682  C CA  . PHE A 1019 ? 1.1269 2.4845 2.0787 0.4653  0.0587  -0.3713 1019 PHE A CA  
7683  C C   . PHE A 1019 ? 1.0214 2.4161 2.0111 0.4236  0.0759  -0.3616 1019 PHE A C   
7684  O O   . PHE A 1019 ? 1.0156 2.4142 1.9856 0.4005  0.1046  -0.3286 1019 PHE A O   
7685  C CB  . PHE A 1019 ? 1.1140 2.4851 2.1024 0.4486  0.0451  -0.3952 1019 PHE A CB  
7686  C CG  . PHE A 1019 ? 1.0234 2.4313 2.0528 0.3978  0.0640  -0.3845 1019 PHE A CG  
7687  C CD1 . PHE A 1019 ? 1.0018 2.4081 2.0082 0.3858  0.0916  -0.3482 1019 PHE A CD1 
7688  C CD2 . PHE A 1019 ? 0.9574 2.3864 2.0325 0.3568  0.0510  -0.4111 1019 PHE A CD2 
7689  C CE1 . PHE A 1019 ? 0.9497 2.3732 1.9771 0.3358  0.1043  -0.3368 1019 PHE A CE1 
7690  C CE2 . PHE A 1019 ? 0.9107 2.3547 2.0043 0.3048  0.0652  -0.4016 1019 PHE A CE2 
7691  C CZ  . PHE A 1019 ? 0.9167 2.3573 1.9860 0.2949  0.0910  -0.3634 1019 PHE A CZ  
7692  N N   . TYR A 1020 ? 0.5806 1.9886 1.6102 0.4077  0.0559  -0.3905 1020 TYR A N   
7693  C CA  . TYR A 1020 ? 0.5187 1.9431 1.5673 0.3633  0.0696  -0.3832 1020 TYR A CA  
7694  C C   . TYR A 1020 ? 0.5150 1.9286 1.5206 0.3755  0.0937  -0.3492 1020 TYR A C   
7695  O O   . TYR A 1020 ? 0.5045 1.9238 1.4948 0.3431  0.1217  -0.3199 1020 TYR A O   
7696  C CB  . TYR A 1020 ? 0.5154 1.9523 1.6126 0.3507  0.0429  -0.4237 1020 TYR A CB  
7697  C CG  . TYR A 1020 ? 0.5311 1.9820 1.6678 0.3227  0.0269  -0.4552 1020 TYR A CG  
7698  C CD1 . TYR A 1020 ? 0.5487 2.0023 1.6783 0.3005  0.0416  -0.4402 1020 TYR A CD1 
7699  C CD2 . TYR A 1020 ? 0.5626 2.0231 1.7416 0.3188  -0.0031 -0.5008 1020 TYR A CD2 
7700  C CE1 . TYR A 1020 ? 0.5663 2.0306 1.7276 0.2742  0.0279  -0.4692 1020 TYR A CE1 
7701  C CE2 . TYR A 1020 ? 0.5742 2.0466 1.7843 0.2915  -0.0165 -0.5324 1020 TYR A CE2 
7702  C CZ  . TYR A 1020 ? 0.5918 2.0654 1.7916 0.2688  -0.0004 -0.5162 1020 TYR A CZ  
7703  O OH  . TYR A 1020 ? 0.6152 2.0987 1.8421 0.2408  -0.0132 -0.5482 1020 TYR A OH  
7704  N N   . VAL A 1021 ? 0.2653 1.6603 1.2464 0.4230  0.0825  -0.3531 1021 VAL A N   
7705  C CA  . VAL A 1021 ? 0.2863 1.6681 1.2221 0.4382  0.1038  -0.3252 1021 VAL A CA  
7706  C C   . VAL A 1021 ? 0.2891 1.6624 1.1738 0.4371  0.1368  -0.2870 1021 VAL A C   
7707  O O   . VAL A 1021 ? 0.2828 1.6500 1.1283 0.4353  0.1611  -0.2609 1021 VAL A O   
7708  C CB  . VAL A 1021 ? 0.2296 1.5743 1.1341 0.4855  0.0772  -0.3402 1021 VAL A CB  
7709  C CG1 . VAL A 1021 ? 0.3907 1.7063 1.2272 0.5032  0.0971  -0.3117 1021 VAL A CG1 
7710  C CG2 . VAL A 1021 ? 0.2135 1.5722 1.1719 0.4779  0.0499  -0.3728 1021 VAL A CG2 
7711  N N   . PHE A 1022 ? 0.7198 2.0931 1.6051 0.4366  0.1379  -0.2844 1022 PHE A N   
7712  C CA  . PHE A 1022 ? 0.7965 2.1624 1.6381 0.4361  0.1668  -0.2505 1022 PHE A CA  
7713  C C   . PHE A 1022 ? 0.7829 2.1700 1.6453 0.3826  0.1833  -0.2333 1022 PHE A C   
7714  O O   . PHE A 1022 ? 0.8152 2.2018 1.6455 0.3670  0.2099  -0.2009 1022 PHE A O   
7715  C CB  . PHE A 1022 ? 0.8453 2.1961 1.6743 0.4677  0.1598  -0.2558 1022 PHE A CB  
7716  C CG  . PHE A 1022 ? 0.8595 2.2037 1.6490 0.4677  0.1877  -0.2244 1022 PHE A CG  
7717  C CD1 . PHE A 1022 ? 0.9070 2.2300 1.6386 0.4955  0.2048  -0.2080 1022 PHE A CD1 
7718  C CD2 . PHE A 1022 ? 0.8318 2.1900 1.6410 0.4391  0.1964  -0.2123 1022 PHE A CD2 
7719  C CE1 . PHE A 1022 ? 0.9451 2.2627 1.6403 0.4946  0.2299  -0.1818 1022 PHE A CE1 
7720  C CE2 . PHE A 1022 ? 0.8724 2.2254 1.6488 0.4399  0.2202  -0.1839 1022 PHE A CE2 
7721  C CZ  . PHE A 1022 ? 0.9265 2.2598 1.6461 0.4676  0.2371  -0.1691 1022 PHE A CZ  
7722  N N   . HIS A 1023 ? 0.8309 2.2344 1.7455 0.3542  0.1657  -0.2570 1023 HIS A N   
7723  C CA  . HIS A 1023 ? 0.7857 2.2052 1.7226 0.3009  0.1768  -0.2461 1023 HIS A CA  
7724  C C   . HIS A 1023 ? 0.7276 2.1513 1.6572 0.2704  0.1924  -0.2319 1023 HIS A C   
7725  O O   . HIS A 1023 ? 0.7329 2.1589 1.6469 0.2373  0.2135  -0.2038 1023 HIS A O   
7726  C CB  . HIS A 1023 ? 0.7660 2.1978 1.7562 0.2802  0.1522  -0.2820 1023 HIS A CB  
7727  C CG  . HIS A 1023 ? 0.7490 2.1927 1.7620 0.2235  0.1605  -0.2771 1023 HIS A CG  
7728  N ND1 . HIS A 1023 ? 0.7418 2.1935 1.7833 0.1859  0.1557  -0.2951 1023 HIS A ND1 
7729  C CD2 . HIS A 1023 ? 0.7504 2.1960 1.7603 0.1990  0.1721  -0.2575 1023 HIS A CD2 
7730  C CE1 . HIS A 1023 ? 0.7408 2.1962 1.7922 0.1397  0.1642  -0.2877 1023 HIS A CE1 
7731  N NE2 . HIS A 1023 ? 0.7527 2.2052 1.7859 0.1472  0.1733  -0.2640 1023 HIS A NE2 
7732  N N   . TYR A 1024 ? 0.3421 1.7652 1.2827 0.2838  0.1801  -0.2519 1024 TYR A N   
7733  C CA  . TYR A 1024 ? 0.3297 1.7525 1.2566 0.2677  0.1948  -0.2391 1024 TYR A CA  
7734  C C   . TYR A 1024 ? 0.3813 1.7903 1.2450 0.2859  0.2213  -0.2021 1024 TYR A C   
7735  O O   . TYR A 1024 ? 0.3762 1.7853 1.2163 0.2561  0.2438  -0.1746 1024 TYR A O   
7736  C CB  . TYR A 1024 ? 0.3537 1.7768 1.3056 0.2889  0.1733  -0.2695 1024 TYR A CB  
7737  C CG  . TYR A 1024 ? 0.4067 1.8287 1.3450 0.2740  0.1893  -0.2566 1024 TYR A CG  
7738  C CD1 . TYR A 1024 ? 0.4280 1.8607 1.4110 0.2448  0.1798  -0.2798 1024 TYR A CD1 
7739  C CD2 . TYR A 1024 ? 0.4637 1.8728 1.3424 0.2869  0.2153  -0.2219 1024 TYR A CD2 
7740  C CE1 . TYR A 1024 ? 0.4730 1.9034 1.4440 0.2300  0.1957  -0.2676 1024 TYR A CE1 
7741  C CE2 . TYR A 1024 ? 0.5088 1.9157 1.3717 0.2718  0.2309  -0.2094 1024 TYR A CE2 
7742  C CZ  . TYR A 1024 ? 0.5416 1.9591 1.4517 0.2438  0.2213  -0.2314 1024 TYR A CZ  
7743  O OH  . TYR A 1024 ? 0.6163 2.0299 1.5102 0.2290  0.2379  -0.2187 1024 TYR A OH  
7744  N N   . LEU A 1025 ? 0.7694 2.1633 1.6016 0.3353  0.2177  -0.2033 1025 LEU A N   
7745  C CA  . LEU A 1025 ? 0.8377 2.2164 1.6060 0.3513  0.2429  -0.1729 1025 LEU A CA  
7746  C C   . LEU A 1025 ? 0.8396 2.2209 1.5847 0.3261  0.2649  -0.1412 1025 LEU A C   
7747  O O   . LEU A 1025 ? 0.8319 2.2092 1.5386 0.3104  0.2871  -0.1135 1025 LEU A O   
7748  C CB  . LEU A 1025 ? 0.8945 2.2513 1.6284 0.4076  0.2352  -0.1816 1025 LEU A CB  
7749  C CG  . LEU A 1025 ? 0.9199 2.2657 1.6593 0.4403  0.2152  -0.2060 1025 LEU A CG  
7750  C CD1 . LEU A 1025 ? 0.9808 2.2984 1.6864 0.4962  0.2027  -0.2174 1025 LEU A CD1 
7751  C CD2 . LEU A 1025 ? 0.9285 2.2712 1.6391 0.4298  0.2339  -0.1905 1025 LEU A CD2 
7752  N N   . GLU A 1026 ? 1.0231 2.4103 1.7921 0.3233  0.2569  -0.1460 1026 GLU A N   
7753  C CA  . GLU A 1026 ? 1.1076 2.4952 1.8557 0.3101  0.2744  -0.1176 1026 GLU A CA  
7754  C C   . GLU A 1026 ? 1.1240 2.5247 1.8931 0.2574  0.2814  -0.1027 1026 GLU A C   
7755  O O   . GLU A 1026 ? 1.1811 2.5792 1.9175 0.2387  0.3007  -0.0726 1026 GLU A O   
7756  C CB  . GLU A 1026 ? 1.1480 2.5346 1.9145 0.3317  0.2622  -0.1299 1026 GLU A CB  
7757  C CG  . GLU A 1026 ? 1.1990 2.5901 1.9615 0.3147  0.2753  -0.1055 1026 GLU A CG  
7758  C CD  . GLU A 1026 ? 1.2824 2.6616 1.9877 0.3310  0.2988  -0.0761 1026 GLU A CD  
7759  O OE1 . GLU A 1026 ? 1.3230 2.6889 1.9872 0.3537  0.3060  -0.0750 1026 GLU A OE1 
7760  O OE2 . GLU A 1026 ? 1.2938 2.6764 1.9945 0.3211  0.3094  -0.0552 1026 GLU A OE2 
7761  N N   . THR A 1027 ? 0.9816 2.3940 1.8032 0.2340  0.2637  -0.1258 1027 THR A N   
7762  C CA  . THR A 1027 ? 0.9519 2.3727 1.7940 0.1846  0.2674  -0.1163 1027 THR A CA  
7763  C C   . THR A 1027 ? 0.9632 2.3819 1.7908 0.1554  0.2789  -0.1045 1027 THR A C   
7764  O O   . THR A 1027 ? 0.9893 2.4067 1.8005 0.1258  0.2918  -0.0791 1027 THR A O   
7765  C CB  . THR A 1027 ? 0.8972 2.3278 1.7943 0.1654  0.2454  -0.1493 1027 THR A CB  
7766  O OG1 . THR A 1027 ? 0.9128 2.3461 1.8181 0.1604  0.2450  -0.1408 1027 THR A OG1 
7767  C CG2 . THR A 1027 ? 0.8632 2.2977 1.7823 0.1171  0.2445  -0.1578 1027 THR A CG2 
7768  N N   . GLY A 1028 ? 0.5558 1.9733 1.3890 0.1662  0.2730  -0.1230 1028 GLY A N   
7769  C CA  . GLY A 1028 ? 0.5959 2.0088 1.4100 0.1464  0.2854  -0.1114 1028 GLY A CA  
7770  C C   . GLY A 1028 ? 0.6613 2.0623 1.4158 0.1740  0.3036  -0.0845 1028 GLY A C   
7771  O O   . GLY A 1028 ? 0.6532 2.0485 1.3905 0.1760  0.3099  -0.0831 1028 GLY A O   
7772  N N   . ASN A 1029 ? 0.9547 2.3508 1.6768 0.1941  0.3126  -0.0639 1029 ASN A N   
7773  C CA  . ASN A 1029 ? 1.0768 2.4593 1.7423 0.2292  0.3263  -0.0481 1029 ASN A CA  
7774  C C   . ASN A 1029 ? 1.0608 2.4351 1.7055 0.2369  0.3305  -0.0524 1029 ASN A C   
7775  O O   . ASN A 1029 ? 1.0359 2.4085 1.6684 0.2093  0.3403  -0.0387 1029 ASN A O   
7776  C CB  . ASN A 1029 ? 1.2177 2.5954 1.8409 0.2223  0.3441  -0.0135 1029 ASN A CB  
7777  C CG  . ASN A 1029 ? 1.3505 2.7216 1.9379 0.2026  0.3579  0.0081  1029 ASN A CG  
7778  O OD1 . ASN A 1029 ? 1.4413 2.8012 1.9760 0.2186  0.3716  0.0276  1029 ASN A OD1 
7779  N ND2 . ASN A 1029 ? 1.3498 2.7263 1.9650 0.1677  0.3537  0.0022  1029 ASN A ND2 
7780  N N   . HIS A 1030 ? 1.4233 2.7911 2.0652 0.2769  0.3212  -0.0734 1030 HIS A N   
7781  C CA  . HIS A 1030 ? 1.4228 2.7820 2.0496 0.2929  0.3216  -0.0826 1030 HIS A CA  
7782  C C   . HIS A 1030 ? 1.4484 2.7876 2.0272 0.3440  0.3234  -0.0863 1030 HIS A C   
7783  O O   . HIS A 1030 ? 1.4508 2.7786 2.0157 0.3696  0.3193  -0.0994 1030 HIS A O   
7784  C CB  . HIS A 1030 ? 1.3521 2.7238 2.0427 0.2885  0.2988  -0.1164 1030 HIS A CB  
7785  C CG  . HIS A 1030 ? 1.2854 2.6700 2.0138 0.2379  0.2994  -0.1171 1030 HIS A CG  
7786  N ND1 . HIS A 1030 ? 1.2776 2.6569 1.9813 0.2125  0.3165  -0.0979 1030 HIS A ND1 
7787  C CD2 . HIS A 1030 ? 1.2331 2.6320 2.0186 0.2074  0.2849  -0.1366 1030 HIS A CD2 
7788  C CE1 . HIS A 1030 ? 1.2362 2.6250 1.9804 0.1696  0.3125  -0.1058 1030 HIS A CE1 
7789  N NE2 . HIS A 1030 ? 1.2031 2.6035 1.9963 0.1648  0.2940  -0.1298 1030 HIS A NE2 
7790  N N   . TRP A 1031 ? 1.3874 2.7201 1.9403 0.3590  0.3292  -0.0761 1031 TRP A N   
7791  C CA  . TRP A 1031 ? 1.3974 2.7060 1.8956 0.4032  0.3339  -0.0789 1031 TRP A CA  
7792  C C   . TRP A 1031 ? 1.4485 2.7376 1.8879 0.4119  0.3486  -0.0699 1031 TRP A C   
7793  O O   . TRP A 1031 ? 1.5359 2.8012 1.9371 0.4504  0.3464  -0.0837 1031 TRP A O   
7794  C CB  . TRP A 1031 ? 1.3916 2.6959 1.8615 0.4067  0.3456  -0.0616 1031 TRP A CB  
7795  C CG  . TRP A 1031 ? 1.3252 2.6413 1.8457 0.4111  0.3294  -0.0759 1031 TRP A CG  
7796  C CD1 . TRP A 1031 ? 1.3004 2.6304 1.8429 0.3885  0.3330  -0.0619 1031 TRP A CD1 
7797  C CD2 . TRP A 1031 ? 1.3127 2.6258 1.8685 0.4403  0.3047  -0.1079 1031 TRP A CD2 
7798  N NE1 . TRP A 1031 ? 1.2786 2.6144 1.8658 0.4007  0.3142  -0.0830 1031 TRP A NE1 
7799  C CE2 . TRP A 1031 ? 1.2985 2.6239 1.8940 0.4323  0.2958  -0.1116 1031 TRP A CE2 
7800  C CE3 . TRP A 1031 ? 1.3407 2.6396 1.8969 0.4740  0.2872  -0.1337 1031 TRP A CE3 
7801  C CZ2 . TRP A 1031 ? 1.3199 2.6438 1.9536 0.4553  0.2702  -0.1405 1031 TRP A CZ2 
7802  C CZ3 . TRP A 1031 ? 1.3586 2.6556 1.9545 0.4980  0.2595  -0.1619 1031 TRP A CZ3 
7803  C CH2 . TRP A 1031 ? 1.3472 2.6567 1.9800 0.4877  0.2516  -0.1652 1031 TRP A CH2 
7804  N N   . ASN A 1032 ? 1.7146 3.0100 2.1451 0.3765  0.3621  -0.0486 1032 ASN A N   
7805  C CA  . ASN A 1032 ? 1.7751 3.0503 2.1453 0.3813  0.3772  -0.0370 1032 ASN A CA  
7806  C C   . ASN A 1032 ? 1.7447 3.0136 2.1256 0.3976  0.3687  -0.0580 1032 ASN A C   
7807  O O   . ASN A 1032 ? 1.7697 3.0214 2.1038 0.3988  0.3811  -0.0491 1032 ASN A O   
7808  C CB  . ASN A 1032 ? 1.7937 3.0774 2.1598 0.3386  0.3897  -0.0102 1032 ASN A CB  
7809  C CG  . ASN A 1032 ? 1.7329 3.0374 2.1634 0.3058  0.3804  -0.0184 1032 ASN A CG  
7810  O OD1 . ASN A 1032 ? 1.6642 2.9878 2.1517 0.2897  0.3680  -0.0284 1032 ASN A OD1 
7811  N ND2 . ASN A 1032 ? 1.7498 3.0489 2.1717 0.2954  0.3857  -0.0170 1032 ASN A ND2 
7812  N N   . ILE A 1033 ? 0.8066 2.0889 1.2512 0.4097  0.3456  -0.0860 1033 ILE A N   
7813  C CA  . ILE A 1033 ? 0.8017 2.0751 1.2586 0.4368  0.3319  -0.1101 1033 ILE A CA  
7814  C C   . ILE A 1033 ? 0.9017 2.1366 1.2825 0.4834  0.3372  -0.1152 1033 ILE A C   
7815  O O   . ILE A 1033 ? 0.9360 2.1534 1.2964 0.5021  0.3361  -0.1245 1033 ILE A O   
7816  C CB  . ILE A 1033 ? 0.7361 2.0220 1.2672 0.4569  0.2976  -0.1444 1033 ILE A CB  
7817  C CG1 . ILE A 1033 ? 0.6684 1.9828 1.2633 0.4248  0.2868  -0.1482 1033 ILE A CG1 
7818  C CG2 . ILE A 1033 ? 0.7265 2.0156 1.2954 0.4632  0.2822  -0.1641 1033 ILE A CG2 
7819  C CD1 . ILE A 1033 ? 0.6313 1.9590 1.3013 0.4333  0.2523  -0.1834 1033 ILE A CD1 
7820  N N   . PHE A 1034 ? 1.5651 2.7841 1.9047 0.5024  0.3416  -0.1122 1034 PHE A N   
7821  C CA  . PHE A 1034 ? 1.6681 2.8354 1.9263 0.5425  0.3375  -0.1212 1034 PHE A CA  
7822  C C   . PHE A 1034 ? 1.8116 2.9576 1.9786 0.5404  0.3711  -0.1031 1034 PHE A C   
7823  O O   . PHE A 1034 ? 1.8221 2.9773 1.9682 0.5100  0.3884  -0.0761 1034 PHE A O   
7824  C CB  . PHE A 1034 ? 1.6244 2.7739 1.8719 0.5571  0.3221  -0.1265 1034 PHE A CB  
7825  C CG  . PHE A 1034 ? 1.5150 2.6803 1.8411 0.5575  0.2891  -0.1441 1034 PHE A CG  
7826  C CD1 . PHE A 1034 ? 1.5198 2.6520 1.8581 0.5732  0.2451  -0.1662 1034 PHE A CD1 
7827  C CD2 . PHE A 1034 ? 1.4142 2.6266 1.8000 0.5420  0.3015  -0.1395 1034 PHE A CD2 
7828  C CE1 . PHE A 1034 ? 1.4541 2.6020 1.8617 0.5728  0.2157  -0.1852 1034 PHE A CE1 
7829  C CE2 . PHE A 1034 ? 1.3389 2.5640 1.7920 0.5407  0.2717  -0.1577 1034 PHE A CE2 
7830  C CZ  . PHE A 1034 ? 1.3600 2.5537 1.8232 0.5559  0.2297  -0.1815 1034 PHE A CZ  
7831  N N   . HIS A 1035 ? 1.6916 2.7773 1.7845 0.5609  0.3547  -0.1108 1035 HIS A N   
7832  C CA  . HIS A 1035 ? 1.8947 2.9500 1.8877 0.5625  0.3833  -0.0992 1035 HIS A CA  
7833  C C   . HIS A 1035 ? 2.0184 3.0365 1.9446 0.5775  0.3798  -0.1016 1035 HIS A C   
7834  O O   . HIS A 1035 ? 2.0926 3.1024 1.9473 0.5734  0.4116  -0.0920 1035 HIS A O   
7835  C CB  . HIS A 1035 ? 2.0784 3.0753 2.0141 0.5757  0.3607  -0.1066 1035 HIS A CB  
7836  C CG  . HIS A 1035 ? 2.1149 3.1364 2.1260 0.5681  0.3473  -0.1123 1035 HIS A CG  
7837  N ND1 . HIS A 1035 ? 2.1395 3.1778 2.1464 0.5530  0.3749  -0.1028 1035 HIS A ND1 
7838  C CD2 . HIS A 1035 ? 2.1009 3.1341 2.1944 0.5723  0.3099  -0.1285 1035 HIS A CD2 
7839  C CE1 . HIS A 1035 ? 2.0973 3.1568 2.1842 0.5482  0.3545  -0.1131 1035 HIS A CE1 
7840  N NE2 . HIS A 1035 ? 2.0773 3.1345 2.2176 0.5597  0.3144  -0.1297 1035 HIS A NE2 
7841  N N   . SER A 1036 ? 1.9554 2.9529 1.9069 0.5932  0.3417  -0.1159 1036 SER A N   
7842  C CA  . SER A 1036 ? 2.0286 2.9903 1.9268 0.6072  0.3340  -0.1214 1036 SER A CA  
7843  C C   . SER A 1036 ? 1.9577 2.9695 1.8792 0.5942  0.3715  -0.1089 1036 SER A C   
7844  O O   . SER A 1036 ? 1.8767 2.9387 1.8288 0.5713  0.4041  -0.0910 1036 SER A O   
7845  C CB  . SER A 1036 ? 2.0711 3.0036 1.9992 0.6254  0.2848  -0.1401 1036 SER A CB  
7846  O OG  . SER A 1036 ? 1.9817 2.9677 2.0068 0.6171  0.2831  -0.1413 1036 SER A OG  
7847  N N   . ASP A 1037 ? 2.4982 3.4901 2.4020 0.6055  0.3619  -0.1158 1037 ASP A N   
7848  C CA  . ASP A 1037 ? 2.4030 3.4457 2.3555 0.5956  0.3867  -0.1064 1037 ASP A CA  
7849  C C   . ASP A 1037 ? 2.2207 3.2960 2.2719 0.5928  0.3635  -0.1115 1037 ASP A C   
7850  O O   . ASP A 1037 ? 2.2432 3.2848 2.3045 0.6080  0.3233  -0.1284 1037 ASP A O   
7851  C CB  . ASP A 1037 ? 2.5101 3.5227 2.4149 0.6078  0.3859  -0.1132 1037 ASP A CB  
7852  C CG  . ASP A 1037 ? 2.4349 3.4998 2.3984 0.5993  0.4079  -0.1036 1037 ASP A CG  
7853  O OD1 . ASP A 1037 ? 2.3010 3.4078 2.3450 0.5817  0.4019  -0.0918 1037 ASP A OD1 
7854  O OD2 . ASP A 1037 ? 2.5069 3.5568 2.4297 0.6024  0.4177  -0.1033 1037 ASP A OD2 
7855  N N   . PRO A 1038 ? 1.6162 2.7509 1.7348 0.5680  0.3834  -0.0953 1038 PRO A N   
7856  C CA  . PRO A 1038 ? 1.4895 2.6607 1.7032 0.5582  0.3652  -0.1005 1038 PRO A CA  
7857  C C   . PRO A 1038 ? 1.4577 2.6377 1.7055 0.5665  0.3580  -0.1062 1038 PRO A C   
7858  O O   . PRO A 1038 ? 1.4378 2.6134 1.7319 0.5743  0.3273  -0.1227 1038 PRO A O   
7859  C CB  . PRO A 1038 ? 1.4424 2.6440 1.6821 0.5132  0.3759  -0.0725 1038 PRO A CB  
7860  C CG  . PRO A 1038 ? 1.5279 2.7075 1.6906 0.5060  0.3954  -0.0556 1038 PRO A CG  
7861  C CD  . PRO A 1038 ? 1.6223 2.7669 1.7148 0.5340  0.4023  -0.0644 1038 PRO A CD  
7862  N N   . LEU A 1039 ? 2.0780 3.2550 2.2920 0.5586  0.3754  -0.0897 1039 LEU A N   
7863  C CA  . LEU A 1039 ? 2.0453 3.2338 2.2957 0.5622  0.3713  -0.0914 1039 LEU A CA  
7864  C C   . LEU A 1039 ? 2.0374 3.1904 2.2855 0.5927  0.3423  -0.1184 1039 LEU A C   
7865  O O   . LEU A 1039 ? 1.9811 3.1431 2.2834 0.5934  0.3229  -0.1268 1039 LEU A O   
7866  C CB  . LEU A 1039 ? 2.1091 3.2903 2.3124 0.5564  0.3921  -0.0740 1039 LEU A CB  
7867  C CG  . LEU A 1039 ? 2.1063 3.3088 2.3569 0.5489  0.3917  -0.0661 1039 LEU A CG  
7868  C CD1 . LEU A 1039 ? 2.0069 3.2388 2.3393 0.5329  0.3742  -0.0678 1039 LEU A CD1 
7869  C CD2 . LEU A 1039 ? 2.1453 3.3580 2.3730 0.5255  0.4107  -0.0376 1039 LEU A CD2 
7870  N N   . ILE A 1040 ? 1.5613 2.6589 1.7330 0.6095  0.3295  -0.1283 1040 ILE A N   
7871  C CA  . ILE A 1040 ? 1.6093 2.6537 1.7560 0.6301  0.2919  -0.1489 1040 ILE A CA  
7872  C C   . ILE A 1040 ? 1.5857 2.6299 1.7807 0.6313  0.2577  -0.1626 1040 ILE A C   
7873  O O   . ILE A 1040 ? 1.6012 2.6323 1.8227 0.6407  0.2296  -0.1781 1040 ILE A O   
7874  C CB  . ILE A 1040 ? 1.6946 2.6792 1.7408 0.6435  0.2885  -0.1549 1040 ILE A CB  
7875  C CG1 . ILE A 1040 ? 1.8098 2.7496 1.8211 0.6597  0.2692  -0.1700 1040 ILE A CG1 
7876  C CG2 . ILE A 1040 ? 1.6778 2.6339 1.6960 0.6471  0.2683  -0.1604 1040 ILE A CG2 
7877  C CD1 . ILE A 1040 ? 2.0114 2.9700 2.0905 0.6627  0.2553  -0.1770 1040 ILE A CD1 
7878  N N   . GLU A 1041 ? 1.5639 2.6248 1.7720 0.6210  0.2613  -0.1580 1041 GLU A N   
7879  C CA  . GLU A 1041 ? 1.5583 2.6236 1.8167 0.6205  0.2304  -0.1727 1041 GLU A CA  
7880  C C   . GLU A 1041 ? 1.4942 2.6007 1.8353 0.6096  0.2248  -0.1781 1041 GLU A C   
7881  O O   . GLU A 1041 ? 1.4500 2.5491 1.8266 0.6153  0.1920  -0.1980 1041 GLU A O   
7882  C CB  . GLU A 1041 ? 1.5568 2.6487 1.8319 0.6048  0.2447  -0.1642 1041 GLU A CB  
7883  C CG  . GLU A 1041 ? 1.6325 2.6941 1.9046 0.6153  0.2100  -0.1808 1041 GLU A CG  
7884  C CD  . GLU A 1041 ? 1.8281 2.8263 2.0044 0.6339  0.2009  -0.1810 1041 GLU A CD  
7885  O OE1 . GLU A 1041 ? 1.8850 2.8748 2.0013 0.6312  0.2311  -0.1661 1041 GLU A OE1 
7886  O OE2 . GLU A 1041 ? 1.9296 2.8862 2.0891 0.6501  0.1633  -0.1970 1041 GLU A OE2 
7887  N N   . LYS A 1042 ? 1.5805 2.7297 1.9491 0.5933  0.2571  -0.1607 1042 LYS A N   
7888  C CA  . LYS A 1042 ? 1.5750 2.7635 2.0176 0.5796  0.2556  -0.1625 1042 LYS A CA  
7889  C C   . LYS A 1042 ? 1.6956 2.8484 2.1288 0.5992  0.2289  -0.1796 1042 LYS A C   
7890  O O   . LYS A 1042 ? 1.6919 2.8446 2.1659 0.6000  0.2006  -0.1988 1042 LYS A O   
7891  C CB  . LYS A 1042 ? 1.5512 2.7833 2.0116 0.5621  0.2945  -0.1385 1042 LYS A CB  
7892  C CG  . LYS A 1042 ? 1.5497 2.8116 2.0750 0.5479  0.2900  -0.1386 1042 LYS A CG  
7893  C CD  . LYS A 1042 ? 1.5798 2.8593 2.1011 0.5154  0.3126  -0.1077 1042 LYS A CD  
7894  C CE  . LYS A 1042 ? 1.5059 2.8147 2.0754 0.4715  0.3092  -0.0973 1042 LYS A CE  
7895  N NZ  . LYS A 1042 ? 1.5076 2.8295 2.0702 0.4416  0.3288  -0.0663 1042 LYS A NZ  
7896  N N   . GLN A 1043 ? 1.6576 2.7816 2.0362 0.6137  0.2394  -0.1739 1043 GLN A N   
7897  C CA  . GLN A 1043 ? 1.7474 2.8381 2.1130 0.6309  0.2199  -0.1882 1043 GLN A CA  
7898  C C   . GLN A 1043 ? 1.7041 2.7658 2.0733 0.6428  0.1804  -0.2125 1043 GLN A C   
7899  O O   . GLN A 1043 ? 1.6799 2.7494 2.0930 0.6422  0.1626  -0.2266 1043 GLN A O   
7900  C CB  . GLN A 1043 ? 1.9188 2.9693 2.2075 0.6462  0.2313  -0.1845 1043 GLN A CB  
7901  C CG  . GLN A 1043 ? 1.9840 3.0637 2.2686 0.6362  0.2699  -0.1634 1043 GLN A CG  
7902  C CD  . GLN A 1043 ? 1.9504 3.0789 2.3107 0.6213  0.2800  -0.1546 1043 GLN A CD  
7903  O OE1 . GLN A 1043 ? 1.9511 3.0756 2.3466 0.6251  0.2603  -0.1669 1043 GLN A OE1 
7904  N NE2 . GLN A 1043 ? 1.8983 3.0731 2.2827 0.6027  0.3109  -0.1335 1043 GLN A NE2 
7905  N N   . LYS A 1044 ? 1.5211 2.5495 1.8423 0.6528  0.1670  -0.2174 1044 LYS A N   
7906  C CA  . LYS A 1044 ? 1.5250 2.5191 1.8379 0.6674  0.1275  -0.2400 1044 LYS A CA  
7907  C C   . LYS A 1044 ? 1.4278 2.4570 1.8188 0.6566  0.1095  -0.2547 1044 LYS A C   
7908  O O   . LYS A 1044 ? 1.4579 2.4699 1.8604 0.6670  0.0782  -0.2770 1044 LYS A O   
7909  C CB  . LYS A 1044 ? 1.5656 2.5244 1.8211 0.6759  0.1180  -0.2391 1044 LYS A CB  
7910  C CG  . LYS A 1044 ? 2.1165 3.0214 2.2825 0.6903  0.1195  -0.2363 1044 LYS A CG  
7911  C CD  . LYS A 1044 ? 2.1252 2.9946 2.2325 0.6957  0.1107  -0.2342 1044 LYS A CD  
7912  C CE  . LYS A 1044 ? 2.1400 2.9822 2.2534 0.7085  0.0675  -0.2531 1044 LYS A CE  
7913  N NZ  . LYS A 1044 ? 2.1687 2.9748 2.2259 0.7136  0.0583  -0.2495 1044 LYS A NZ  
7914  N N   . LEU A 1045 ? 1.5967 2.6768 2.0409 0.6336  0.1300  -0.2435 1045 LEU A N   
7915  C CA  . LEU A 1045 ? 1.4648 2.5817 1.9847 0.6179  0.1156  -0.2588 1045 LEU A CA  
7916  C C   . LEU A 1045 ? 1.4279 2.5618 1.9821 0.6115  0.1192  -0.2618 1045 LEU A C   
7917  O O   . LEU A 1045 ? 1.4009 2.5370 1.9893 0.6113  0.0954  -0.2843 1045 LEU A O   
7918  C CB  . LEU A 1045 ? 1.3394 2.5043 1.9026 0.5920  0.1370  -0.2463 1045 LEU A CB  
7919  C CG  . LEU A 1045 ? 1.3239 2.4677 1.8472 0.5996  0.1354  -0.2424 1045 LEU A CG  
7920  C CD1 . LEU A 1045 ? 1.2529 2.4401 1.8402 0.5764  0.1364  -0.2475 1045 LEU A CD1 
7921  C CD2 . LEU A 1045 ? 1.3632 2.4481 1.8349 0.6283  0.0996  -0.2603 1045 LEU A CD2 
7922  N N   . LYS A 1046 ? 1.3466 2.4902 1.8877 0.6074  0.1487  -0.2400 1046 LYS A N   
7923  C CA  . LYS A 1046 ? 1.3846 2.5393 1.9529 0.6034  0.1530  -0.2404 1046 LYS A CA  
7924  C C   . LYS A 1046 ? 1.4969 2.6107 2.0433 0.6247  0.1246  -0.2637 1046 LYS A C   
7925  O O   . LYS A 1046 ? 1.4922 2.6154 2.0786 0.6196  0.1067  -0.2827 1046 LYS A O   
7926  C CB  . LYS A 1046 ? 1.4219 2.5814 1.9656 0.6034  0.1858  -0.2152 1046 LYS A CB  
7927  C CG  . LYS A 1046 ? 1.3712 2.5818 1.9496 0.5777  0.2169  -0.1913 1046 LYS A CG  
7928  C CD  . LYS A 1046 ? 1.4328 2.6544 2.0096 0.5764  0.2420  -0.1724 1046 LYS A CD  
7929  C CE  . LYS A 1046 ? 1.4353 2.6944 2.0140 0.5599  0.2782  -0.1450 1046 LYS A CE  
7930  N NZ  . LYS A 1046 ? 1.4845 2.7464 2.0519 0.5644  0.2999  -0.1290 1046 LYS A NZ  
7931  N N   . LYS A 1047 ? 1.0396 2.1083 1.5200 0.6467  0.1214  -0.2631 1047 LYS A N   
7932  C CA  . LYS A 1047 ? 1.1212 2.1495 1.5745 0.6662  0.0945  -0.2848 1047 LYS A CA  
7933  C C   . LYS A 1047 ? 1.0054 2.0407 1.4952 0.6642  0.0636  -0.3094 1047 LYS A C   
7934  O O   . LYS A 1047 ? 0.9608 2.0057 1.4856 0.6610  0.0512  -0.3268 1047 LYS A O   
7935  C CB  . LYS A 1047 ? 1.3126 2.2917 1.6888 0.6852  0.0895  -0.2829 1047 LYS A CB  
7936  C CG  . LYS A 1047 ? 1.5074 2.4432 1.8467 0.7035  0.0685  -0.3008 1047 LYS A CG  
7937  C CD  . LYS A 1047 ? 1.7146 2.6056 1.9758 0.7154  0.0736  -0.2938 1047 LYS A CD  
7938  C CE  . LYS A 1047 ? 1.8783 2.7353 2.1111 0.7274  0.0622  -0.3080 1047 LYS A CE  
7939  N NZ  . LYS A 1047 ? 1.9211 2.7675 2.1687 0.7353  0.0287  -0.3314 1047 LYS A NZ  
7940  N N   . LYS A 1048 ? 1.1389 2.1698 1.6203 0.6657  0.0516  -0.3121 1048 LYS A N   
7941  C CA  . LYS A 1048 ? 1.0532 2.0832 1.5607 0.6687  0.0184  -0.3385 1048 LYS A CA  
7942  C C   . LYS A 1048 ? 0.9298 1.9977 1.5048 0.6514  0.0137  -0.3548 1048 LYS A C   
7943  O O   . LYS A 1048 ? 0.9125 1.9760 1.5053 0.6561  -0.0141 -0.3826 1048 LYS A O   
7944  C CB  . LYS A 1048 ? 0.9911 2.0292 1.5046 0.6640  0.0140  -0.3357 1048 LYS A CB  
7945  C CG  . LYS A 1048 ? 1.0689 2.0571 1.5160 0.6860  -0.0026 -0.3356 1048 LYS A CG  
7946  C CD  . LYS A 1048 ? 1.0671 2.0517 1.5344 0.6909  -0.0345 -0.3562 1048 LYS A CD  
7947  C CE  . LYS A 1048 ? 1.0977 2.0669 1.5311 0.6936  -0.0297 -0.3413 1048 LYS A CE  
7948  N NZ  . LYS A 1048 ? 1.0980 2.0604 1.5515 0.7007  -0.0633 -0.3617 1048 LYS A NZ  
7949  N N   . LEU A 1049 ? 1.4156 2.5205 2.0255 0.6302  0.0412  -0.3376 1049 LEU A N   
7950  C CA  . LEU A 1049 ? 1.3356 2.4767 2.0065 0.6086  0.0412  -0.3490 1049 LEU A CA  
7951  C C   . LEU A 1049 ? 1.4135 2.5352 2.0724 0.6187  0.0372  -0.3582 1049 LEU A C   
7952  O O   . LEU A 1049 ? 1.4424 2.5581 2.1143 0.6218  0.0139  -0.3862 1049 LEU A O   
7953  C CB  . LEU A 1049 ? 1.1993 2.3860 1.9094 0.5805  0.0720  -0.3246 1049 LEU A CB  
7954  C CG  . LEU A 1049 ? 1.0506 2.2860 1.8328 0.5479  0.0683  -0.3370 1049 LEU A CG  
7955  C CD1 . LEU A 1049 ? 0.9781 2.2170 1.7734 0.5477  0.0489  -0.3546 1049 LEU A CD1 
7956  C CD2 . LEU A 1049 ? 0.9840 2.2645 1.8021 0.5179  0.1003  -0.3101 1049 LEU A CD2 
7957  N N   . LYS A 1050 ? 1.3305 2.4423 1.9642 0.6239  0.0602  -0.3364 1050 LYS A N   
7958  C CA  . LYS A 1050 ? 1.3844 2.4783 2.0099 0.6326  0.0578  -0.3455 1050 LYS A CA  
7959  C C   . LYS A 1050 ? 1.5000 2.5588 2.0961 0.6530  0.0291  -0.3730 1050 LYS A C   
7960  O O   . LYS A 1050 ? 1.4797 2.5423 2.0980 0.6498  0.0146  -0.3962 1050 LYS A O   
7961  C CB  . LYS A 1050 ? 1.4166 2.4945 2.0082 0.6422  0.0830  -0.3217 1050 LYS A CB  
7962  C CG  . LYS A 1050 ? 1.4429 2.5013 2.0277 0.6514  0.0814  -0.3316 1050 LYS A CG  
7963  C CD  . LYS A 1050 ? 1.4613 2.5265 2.0481 0.6485  0.1095  -0.3078 1050 LYS A CD  
7964  C CE  . LYS A 1050 ? 1.5153 2.5734 2.1168 0.6497  0.1091  -0.3176 1050 LYS A CE  
7965  N NZ  . LYS A 1050 ? 1.5472 2.6144 2.1568 0.6466  0.1357  -0.2933 1050 LYS A NZ  
7966  N N   . GLU A 1051 ? 2.0015 3.0263 2.5462 0.6724  0.0206  -0.3712 1051 GLU A N   
7967  C CA  . GLU A 1051 ? 2.1751 3.1657 2.6886 0.6913  -0.0057 -0.3950 1051 GLU A CA  
7968  C C   . GLU A 1051 ? 2.1275 3.1342 2.6790 0.6862  -0.0337 -0.4253 1051 GLU A C   
7969  O O   . GLU A 1051 ? 2.1661 3.1613 2.7144 0.6936  -0.0503 -0.4492 1051 GLU A O   
7970  C CB  . GLU A 1051 ? 2.3695 3.3212 2.8221 0.7093  -0.0132 -0.3878 1051 GLU A CB  
7971  C CG  . GLU A 1051 ? 2.4535 3.4102 2.9122 0.7085  -0.0296 -0.3908 1051 GLU A CG  
7972  C CD  . GLU A 1051 ? 2.6157 3.5331 3.0102 0.7230  -0.0329 -0.3787 1051 GLU A CD  
7973  O OE1 . GLU A 1051 ? 2.6928 3.5883 3.0434 0.7278  -0.0143 -0.3631 1051 GLU A OE1 
7974  O OE2 . GLU A 1051 ? 2.6585 3.5662 3.0463 0.7286  -0.0545 -0.3859 1051 GLU A OE2 
7975  N N   . GLY A 1052 ? 1.4380 2.4729 2.0256 0.6725  -0.0378 -0.4259 1052 GLY A N   
7976  C CA  . GLY A 1052 ? 1.4152 2.4712 2.0463 0.6638  -0.0625 -0.4567 1052 GLY A CA  
7977  C C   . GLY A 1052 ? 1.3553 2.4352 2.0246 0.6466  -0.0569 -0.4701 1052 GLY A C   
7978  O O   . GLY A 1052 ? 1.3582 2.4427 2.0451 0.6451  -0.0776 -0.5020 1052 GLY A O   
7979  N N   . MET A 1053 ? 1.8157 2.9096 2.4949 0.6338  -0.0287 -0.4458 1053 MET A N   
7980  C CA  . MET A 1053 ? 1.7832 2.8993 2.4982 0.6143  -0.0205 -0.4527 1053 MET A CA  
7981  C C   . MET A 1053 ? 1.8364 2.9255 2.5255 0.6291  -0.0285 -0.4707 1053 MET A C   
7982  O O   . MET A 1053 ? 1.8118 2.9138 2.5267 0.6162  -0.0353 -0.4932 1053 MET A O   
7983  C CB  . MET A 1053 ? 1.7976 2.9291 2.5220 0.6015  0.0112  -0.4183 1053 MET A CB  
7984  C CG  . MET A 1053 ? 1.7405 2.8995 2.5087 0.5756  0.0192  -0.4217 1053 MET A CG  
7985  S SD  . MET A 1053 ? 3.0694 4.2550 3.8853 0.5522  -0.0074 -0.4641 1053 MET A SD  
7986  C CE  . MET A 1053 ? 0.8106 2.0496 1.6894 0.5086  0.0088  -0.4490 1053 MET A CE  
7987  N N   . LEU A 1054 ? 1.1924 2.2443 1.8291 0.6540  -0.0260 -0.4612 1054 LEU A N   
7988  C CA  . LEU A 1054 ? 1.2632 2.2906 1.8751 0.6666  -0.0298 -0.4767 1054 LEU A CA  
7989  C C   . LEU A 1054 ? 1.2490 2.2708 1.8581 0.6741  -0.0603 -0.5118 1054 LEU A C   
7990  O O   . LEU A 1054 ? 1.2517 2.2735 1.8656 0.6724  -0.0682 -0.5371 1054 LEU A O   
7991  C CB  . LEU A 1054 ? 1.4068 2.3981 1.9659 0.6869  -0.0164 -0.4573 1054 LEU A CB  
7992  C CG  . LEU A 1054 ? 1.4517 2.4461 2.0066 0.6833  0.0133  -0.4227 1054 LEU A CG  
7993  C CD1 . LEU A 1054 ? 1.5613 2.5179 2.0607 0.7027  0.0221  -0.4115 1054 LEU A CD1 
7994  C CD2 . LEU A 1054 ? 1.4309 2.4478 2.0234 0.6668  0.0326  -0.4137 1054 LEU A CD2 
7995  N N   . SER A 1055 ? 1.5551 2.5741 2.1583 0.6812  -0.0773 -0.5140 1055 SER A N   
7996  C CA  . SER A 1055 ? 1.5661 2.5766 2.1628 0.6924  -0.1087 -0.5455 1055 SER A CA  
7997  C C   . SER A 1055 ? 1.4579 2.4899 2.0878 0.6798  -0.1203 -0.5813 1055 SER A C   
7998  O O   . SER A 1055 ? 1.5193 2.5414 2.1364 0.6911  -0.1428 -0.6105 1055 SER A O   
7999  C CB  . SER A 1055 ? 1.6094 2.6283 2.2198 0.6927  -0.1251 -0.5456 1055 SER A CB  
8000  O OG  . SER A 1055 ? 1.6745 2.6866 2.2832 0.7042  -0.1576 -0.5775 1055 SER A OG  
8001  N N   . ILE A 1056 ? 1.6184 2.6792 2.2880 0.6552  -0.1047 -0.5793 1056 ILE A N   
8002  C CA  . ILE A 1056 ? 1.5728 2.6566 2.2753 0.6368  -0.1140 -0.6135 1056 ILE A CA  
8003  C C   . ILE A 1056 ? 1.5771 2.6480 2.2616 0.6370  -0.1007 -0.6181 1056 ILE A C   
8004  O O   . ILE A 1056 ? 1.5754 2.6496 2.2618 0.6330  -0.1123 -0.6520 1056 ILE A O   
8005  C CB  . ILE A 1056 ? 1.3334 2.4582 2.0929 0.6041  -0.1081 -0.6118 1056 ILE A CB  
8006  C CG1 . ILE A 1056 ? 1.2509 2.3939 2.0359 0.5786  -0.1013 -0.6289 1056 ILE A CG1 
8007  C CG2 . ILE A 1056 ? 1.2765 2.4053 2.0381 0.6006  -0.0844 -0.5681 1056 ILE A CG2 
8008  C CD1 . ILE A 1056 ? 1.1994 2.3599 2.0091 0.5556  -0.0755 -0.5973 1056 ILE A CD1 
8009  N N   . MET A 1057 ? 1.6174 2.6733 2.2836 0.6418  -0.0759 -0.5854 1057 MET A N   
8010  C CA  . MET A 1057 ? 1.7241 2.7684 2.3783 0.6408  -0.0606 -0.5865 1057 MET A CA  
8011  C C   . MET A 1057 ? 1.8141 2.8492 2.4512 0.6473  -0.0761 -0.6247 1057 MET A C   
8012  O O   . MET A 1057 ? 1.7976 2.8415 2.4468 0.6325  -0.0733 -0.6444 1057 MET A O   
8013  C CB  . MET A 1057 ? 1.8597 2.8749 2.4766 0.6597  -0.0405 -0.5555 1057 MET A CB  
8014  C CG  . MET A 1057 ? 1.8905 2.9068 2.5184 0.6497  -0.0158 -0.5382 1057 MET A CG  
8015  S SD  . MET A 1057 ? 2.2123 3.2677 2.8957 0.6183  -0.0067 -0.5208 1057 MET A SD  
8016  C CE  . MET A 1057 ? 2.6062 3.6583 3.2788 0.6281  0.0123  -0.4768 1057 MET A CE  
8017  N N   . SER A 1058 ? 2.1518 3.1691 2.7585 0.6687  -0.0930 -0.6351 1058 SER A N   
8018  C CA  . SER A 1058 ? 2.1674 3.1756 2.7525 0.6779  -0.1081 -0.6701 1058 SER A CA  
8019  C C   . SER A 1058 ? 2.0799 3.1156 2.6968 0.6572  -0.1199 -0.7085 1058 SER A C   
8020  O O   . SER A 1058 ? 2.1016 3.1329 2.7026 0.6573  -0.1206 -0.7354 1058 SER A O   
8021  C CB  . SER A 1058 ? 2.1913 3.1848 2.7515 0.6991  -0.1314 -0.6765 1058 SER A CB  
8022  O OG  . SER A 1058 ? 2.2062 3.1724 2.7328 0.7149  -0.1209 -0.6425 1058 SER A OG  
8023  N N   . TYR A 1059 ? 1.3853 2.4500 2.0459 0.6373  -0.1279 -0.7125 1059 TYR A N   
8024  C CA  . TYR A 1059 ? 1.3368 2.4295 2.0293 0.6136  -0.1410 -0.7526 1059 TYR A CA  
8025  C C   . TYR A 1059 ? 1.3652 2.4698 2.0782 0.5862  -0.1216 -0.7473 1059 TYR A C   
8026  O O   . TYR A 1059 ? 1.3543 2.4801 2.0904 0.5611  -0.1290 -0.7798 1059 TYR A O   
8027  C CB  . TYR A 1059 ? 1.2136 2.3341 1.9472 0.6018  -0.1605 -0.7646 1059 TYR A CB  
8028  C CG  . TYR A 1059 ? 1.2231 2.3319 1.9410 0.6278  -0.1831 -0.7699 1059 TYR A CG  
8029  C CD1 . TYR A 1059 ? 1.2833 2.3652 1.9701 0.6515  -0.1774 -0.7333 1059 TYR A CD1 
8030  C CD2 . TYR A 1059 ? 1.2500 2.3744 1.9841 0.6275  -0.2113 -0.8124 1059 TYR A CD2 
8031  C CE1 . TYR A 1059 ? 1.3751 2.4429 2.0447 0.6740  -0.2003 -0.7374 1059 TYR A CE1 
8032  C CE2 . TYR A 1059 ? 1.3540 2.4665 2.0753 0.6518  -0.2348 -0.8168 1059 TYR A CE2 
8033  C CZ  . TYR A 1059 ? 1.4141 2.4970 2.1022 0.6748  -0.2297 -0.7784 1059 TYR A CZ  
8034  O OH  . TYR A 1059 ? 1.4721 2.5404 2.1452 0.6975  -0.2553 -0.7833 1059 TYR A OH  
8035  N N   . ARG A 1060 ? 1.5918 2.6823 2.2958 0.5897  -0.0977 -0.7072 1060 ARG A N   
8036  C CA  . ARG A 1060 ? 1.6085 2.7062 2.3296 0.5660  -0.0797 -0.6981 1060 ARG A CA  
8037  C C   . ARG A 1060 ? 1.6886 2.7681 2.3813 0.5684  -0.0732 -0.7186 1060 ARG A C   
8038  O O   . ARG A 1060 ? 1.7597 2.8116 2.4160 0.5925  -0.0623 -0.7067 1060 ARG A O   
8039  C CB  . ARG A 1060 ? 1.6413 2.7291 2.3613 0.5717  -0.0564 -0.6494 1060 ARG A CB  
8040  C CG  . ARG A 1060 ? 1.5488 2.6345 2.2766 0.5546  -0.0381 -0.6390 1060 ARG A CG  
8041  C CD  . ARG A 1060 ? 1.5481 2.6422 2.2975 0.5468  -0.0200 -0.5959 1060 ARG A CD  
8042  N NE  . ARG A 1060 ? 1.6520 2.7242 2.3858 0.5543  0.0008  -0.5745 1060 ARG A NE  
8043  C CZ  . ARG A 1060 ? 1.6881 2.7602 2.4312 0.5558  0.0194  -0.5353 1060 ARG A CZ  
8044  N NH1 . ARG A 1060 ? 1.6811 2.7743 2.4457 0.5493  0.0214  -0.5127 1060 ARG A NH1 
8045  N NH2 . ARG A 1060 ? 1.7205 2.7720 2.4516 0.5638  0.0366  -0.5198 1060 ARG A NH2 
8046  N N   . ASN A 1061 ? 1.1208 2.2151 1.8287 0.5416  -0.0778 -0.7491 1061 ASN A N   
8047  C CA  . ASN A 1061 ? 1.2441 2.3200 1.9225 0.5418  -0.0684 -0.7675 1061 ASN A CA  
8048  C C   . ASN A 1061 ? 1.2944 2.3515 1.9667 0.5406  -0.0428 -0.7339 1061 ASN A C   
8049  O O   . ASN A 1061 ? 1.2746 2.3279 1.9570 0.5481  -0.0303 -0.6927 1061 ASN A O   
8050  C CB  . ASN A 1061 ? 1.2771 2.3708 1.9642 0.5140  -0.0818 -0.8163 1061 ASN A CB  
8051  C CG  . ASN A 1061 ? 1.3788 2.4755 2.0457 0.5280  -0.1016 -0.8590 1061 ASN A CG  
8052  O OD1 . ASN A 1061 ? 1.3972 2.5002 2.0704 0.5445  -0.1167 -0.8578 1061 ASN A OD1 
8053  N ND2 . ASN A 1061 ? 1.4438 2.5355 2.0850 0.5218  -0.1015 -0.8969 1061 ASN A ND2 
8054  N N   . ALA A 1062 ? 1.8253 2.8705 2.4796 0.5316  -0.0352 -0.7536 1062 ALA A N   
8055  C CA  . ALA A 1062 ? 1.8792 2.9006 2.5212 0.5362  -0.0116 -0.7272 1062 ALA A CA  
8056  C C   . ALA A 1062 ? 1.8212 2.8525 2.4957 0.5075  -0.0052 -0.7073 1062 ALA A C   
8057  O O   . ALA A 1062 ? 1.8405 2.8655 2.5271 0.5134  0.0095  -0.6664 1062 ALA A O   
8058  C CB  . ALA A 1062 ? 1.9646 2.9666 2.5699 0.5400  -0.0048 -0.7571 1062 ALA A CB  
8059  N N   . ASP A 1063 ? 2.3448 3.3920 3.0320 0.4749  -0.0170 -0.7386 1063 ASP A N   
8060  C CA  . ASP A 1063 ? 2.2767 3.3347 2.9933 0.4399  -0.0148 -0.7270 1063 ASP A CA  
8061  C C   . ASP A 1063 ? 2.1450 3.2316 2.9041 0.4272  -0.0196 -0.7011 1063 ASP A C   
8062  O O   . ASP A 1063 ? 2.0795 3.1838 2.8691 0.3928  -0.0215 -0.6950 1063 ASP A O   
8063  C CB  . ASP A 1063 ? 2.2923 3.3605 3.0065 0.4059  -0.0285 -0.7747 1063 ASP A CB  
8064  C CG  . ASP A 1063 ? 2.2946 3.3895 3.0192 0.4003  -0.0502 -0.8125 1063 ASP A CG  
8065  O OD1 . ASP A 1063 ? 2.2805 3.3878 3.0209 0.4183  -0.0555 -0.7966 1063 ASP A OD1 
8066  O OD2 . ASP A 1063 ? 2.3171 3.4199 3.0334 0.3777  -0.0621 -0.8594 1063 ASP A OD2 
8067  N N   . TYR A 1064 ? 1.5560 2.6470 2.3154 0.4535  -0.0215 -0.6869 1064 TYR A N   
8068  C CA  . TYR A 1064 ? 1.4646 2.5805 2.2590 0.4466  -0.0225 -0.6595 1064 TYR A CA  
8069  C C   . TYR A 1064 ? 1.4173 2.5652 2.2390 0.4236  -0.0433 -0.6913 1064 TYR A C   
8070  O O   . TYR A 1064 ? 1.4150 2.5859 2.2657 0.4181  -0.0457 -0.6750 1064 TYR A O   
8071  C CB  . TYR A 1064 ? 1.4012 2.5227 2.2209 0.4269  -0.0075 -0.6216 1064 TYR A CB  
8072  C CG  . TYR A 1064 ? 1.4530 2.5442 2.2498 0.4546  0.0127  -0.5888 1064 TYR A CG  
8073  C CD1 . TYR A 1064 ? 1.4619 2.5464 2.2503 0.4847  0.0231  -0.5584 1064 TYR A CD1 
8074  C CD2 . TYR A 1064 ? 1.5014 2.5696 2.2835 0.4504  0.0213  -0.5909 1064 TYR A CD2 
8075  C CE1 . TYR A 1064 ? 1.5360 2.5942 2.3054 0.5088  0.0418  -0.5318 1064 TYR A CE1 
8076  C CE2 . TYR A 1064 ? 1.5780 2.6191 2.3433 0.4762  0.0402  -0.5627 1064 TYR A CE2 
8077  C CZ  . TYR A 1064 ? 1.5842 2.6216 2.3447 0.5050  0.0504  -0.5341 1064 TYR A CZ  
8078  O OH  . TYR A 1064 ? 1.6448 2.6575 2.3915 0.5285  0.0692  -0.5092 1064 TYR A OH  
8079  N N   . SER A 1065 ? 1.9601 3.1100 2.7720 0.4104  -0.0576 -0.7386 1065 SER A N   
8080  C CA  . SER A 1065 ? 1.8850 3.0633 2.7199 0.3951  -0.0791 -0.7752 1065 SER A CA  
8081  C C   . SER A 1065 ? 1.8809 3.0533 2.7014 0.4329  -0.0872 -0.7734 1065 SER A C   
8082  O O   . SER A 1065 ? 1.9476 3.0922 2.7279 0.4659  -0.0830 -0.7713 1065 SER A O   
8083  C CB  . SER A 1065 ? 1.9141 3.0930 2.7340 0.3776  -0.0921 -0.8299 1065 SER A CB  
8084  O OG  . SER A 1065 ? 2.0017 3.1607 2.7817 0.4125  -0.0970 -0.8501 1065 SER A OG  
8085  N N   . TYR A 1066 ? 1.0610 2.2595 1.9145 0.4261  -0.0988 -0.7745 1066 TYR A N   
8086  C CA  . TYR A 1066 ? 1.0862 2.2801 1.9285 0.4579  -0.1113 -0.7774 1066 TYR A CA  
8087  C C   . TYR A 1066 ? 1.1177 2.3167 1.9514 0.4592  -0.1346 -0.8331 1066 TYR A C   
8088  O O   . TYR A 1066 ? 1.1279 2.3319 1.9595 0.4365  -0.1373 -0.8666 1066 TYR A O   
8089  C CB  . TYR A 1066 ? 0.9992 2.2174 1.8801 0.4494  -0.1119 -0.7536 1066 TYR A CB  
8090  C CG  . TYR A 1066 ? 0.9997 2.2071 1.8752 0.4581  -0.0875 -0.6989 1066 TYR A CG  
8091  C CD1 . TYR A 1066 ? 1.0018 2.1997 1.8719 0.4465  -0.0691 -0.6795 1066 TYR A CD1 
8092  C CD2 . TYR A 1066 ? 1.0129 2.2174 1.8856 0.4789  -0.0830 -0.6678 1066 TYR A CD2 
8093  C CE1 . TYR A 1066 ? 1.0377 2.2265 1.9037 0.4559  -0.0470 -0.6311 1066 TYR A CE1 
8094  C CE2 . TYR A 1066 ? 1.0444 2.2396 1.9089 0.4870  -0.0594 -0.6201 1066 TYR A CE2 
8095  C CZ  . TYR A 1066 ? 1.0653 2.2540 1.9283 0.4759  -0.0417 -0.6023 1066 TYR A CZ  
8096  O OH  . TYR A 1066 ? 1.1014 2.2828 1.9585 0.4845  -0.0192 -0.5573 1066 TYR A OH  
8097  N N   . SER A 1067 ? 1.1904 2.3867 2.0159 0.4855  -0.1515 -0.8440 1067 SER A N   
8098  C CA  . SER A 1067 ? 1.2117 2.4166 2.0329 0.4872  -0.1754 -0.8981 1067 SER A CA  
8099  C C   . SER A 1067 ? 1.2270 2.4394 2.0603 0.5072  -0.1981 -0.9072 1067 SER A C   
8100  O O   . SER A 1067 ? 1.2473 2.4446 2.0704 0.5318  -0.1950 -0.8710 1067 SER A O   
8101  C CB  . SER A 1067 ? 1.2848 2.4631 2.0545 0.5067  -0.1716 -0.9159 1067 SER A CB  
8102  O OG  . SER A 1067 ? 1.3002 2.4922 2.0679 0.5017  -0.1926 -0.9719 1067 SER A OG  
8103  N N   . VAL A 1068 ? 1.2463 2.4814 2.1003 0.4957  -0.2215 -0.9579 1068 VAL A N   
8104  C CA  . VAL A 1068 ? 1.2582 2.5052 2.1336 0.5097  -0.2466 -0.9736 1068 VAL A CA  
8105  C C   . VAL A 1068 ? 1.3896 2.6056 2.2236 0.5548  -0.2558 -0.9579 1068 VAL A C   
8106  O O   . VAL A 1068 ? 1.4040 2.6113 2.2414 0.5708  -0.2564 -0.9243 1068 VAL A O   
8107  C CB  . VAL A 1068 ? 1.2397 2.5132 2.1372 0.4933  -0.2707 -1.0370 1068 VAL A CB  
8108  C CG1 . VAL A 1068 ? 1.3399 2.5969 2.1891 0.5048  -0.2715 -1.0683 1068 VAL A CG1 
8109  C CG2 . VAL A 1068 ? 1.2280 2.5111 2.1486 0.5118  -0.2979 -1.0514 1068 VAL A CG2 
8110  N N   . TRP A 1069 ? 1.2458 2.4474 2.0414 0.5728  -0.2643 -0.9857 1069 TRP A N   
8111  C CA  . TRP A 1069 ? 1.3432 2.5117 2.0907 0.6126  -0.2691 -0.9686 1069 TRP A CA  
8112  C C   . TRP A 1069 ? 1.4100 2.5520 2.1085 0.6212  -0.2454 -0.9541 1069 TRP A C   
8113  O O   . TRP A 1069 ? 1.3951 2.5448 2.0896 0.6020  -0.2350 -0.9778 1069 TRP A O   
8114  C CB  . TRP A 1069 ? 1.3782 2.5512 2.1187 0.6301  -0.2998 -1.0114 1069 TRP A CB  
8115  C CG  . TRP A 1069 ? 1.2906 2.4958 2.0828 0.6165  -0.3250 -1.0453 1069 TRP A CG  
8116  C CD1 . TRP A 1069 ? 1.2563 2.4651 2.0759 0.6267  -0.3424 -1.0333 1069 TRP A CD1 
8117  C CD2 . TRP A 1069 ? 1.2080 2.4468 2.0312 0.5895  -0.3365 -1.1009 1069 TRP A CD2 
8118  N NE1 . TRP A 1069 ? 1.1924 2.4363 2.0627 0.6079  -0.3638 -1.0777 1069 TRP A NE1 
8119  C CE2 . TRP A 1069 ? 1.1821 2.4459 2.0559 0.5840  -0.3610 -1.1210 1069 TRP A CE2 
8120  C CE3 . TRP A 1069 ? 1.1761 2.4256 1.9878 0.5681  -0.3280 -1.1372 1069 TRP A CE3 
8121  C CZ2 . TRP A 1069 ? 1.1617 2.4629 2.0782 0.5567  -0.3776 -1.1778 1069 TRP A CZ2 
8122  C CZ3 . TRP A 1069 ? 1.1699 2.4543 2.0182 0.5407  -0.3443 -1.1930 1069 TRP A CZ3 
8123  C CH2 . TRP A 1069 ? 1.1682 2.4795 2.0702 0.5346  -0.3691 -1.2140 1069 TRP A CH2 
8124  N N   . LYS A 1070 ? 1.2512 2.3612 1.9114 0.6490  -0.2377 -0.9180 1070 LYS A N   
8125  C CA  . LYS A 1070 ? 1.2745 2.3593 1.8965 0.6549  -0.2101 -0.8932 1070 LYS A CA  
8126  C C   . LYS A 1070 ? 1.3152 2.4046 1.9217 0.6428  -0.2014 -0.9274 1070 LYS A C   
8127  O O   . LYS A 1070 ? 1.3571 2.4538 1.9512 0.6477  -0.2177 -0.9682 1070 LYS A O   
8128  C CB  . LYS A 1070 ? 1.3201 2.3715 1.8972 0.6863  -0.2092 -0.8666 1070 LYS A CB  
8129  C CG  . LYS A 1070 ? 1.2872 2.3226 1.8638 0.6919  -0.1949 -0.8158 1070 LYS A CG  
8130  C CD  . LYS A 1070 ? 1.3718 2.3731 1.9012 0.7101  -0.1764 -0.7870 1070 LYS A CD  
8131  C CE  . LYS A 1070 ? 1.4420 2.4215 1.9373 0.7347  -0.1960 -0.7853 1070 LYS A CE  
8132  N NZ  . LYS A 1070 ? 1.5243 2.4716 1.9799 0.7471  -0.1769 -0.7502 1070 LYS A NZ  
8133  N N   . GLY A 1071 ? 1.5502 2.6358 2.1576 0.6260  -0.1758 -0.9110 1071 GLY A N   
8134  C CA  . GLY A 1071 ? 1.6254 2.7094 2.2127 0.6139  -0.1629 -0.9374 1071 GLY A CA  
8135  C C   . GLY A 1071 ? 1.6154 2.7285 2.2267 0.5852  -0.1756 -0.9863 1071 GLY A C   
8136  O O   . GLY A 1071 ? 1.6803 2.7927 2.2792 0.5670  -0.1620 -1.0044 1071 GLY A O   
8137  N N   . GLY A 1072 ? 3.8820 5.0195 4.5264 0.5801  -0.2016 -1.0091 1072 GLY A N   
8138  C CA  . GLY A 1072 ? 3.8465 5.0150 4.5187 0.5504  -0.2163 -1.0596 1072 GLY A CA  
8139  C C   . GLY A 1072 ? 3.8100 4.9843 4.4957 0.5148  -0.1979 -1.0569 1072 GLY A C   
8140  O O   . GLY A 1072 ? 3.7916 4.9522 4.4807 0.5128  -0.1780 -1.0110 1072 GLY A O   
8141  N N   . SER A 1073 ? 1.9777 3.1712 2.6689 0.4860  -0.2049 -1.1068 1073 SER A N   
8142  C CA  . SER A 1073 ? 1.9329 3.1306 2.6342 0.4481  -0.1904 -1.1083 1073 SER A CA  
8143  C C   . SER A 1073 ? 1.8161 3.0280 2.5666 0.4310  -0.1893 -1.0725 1073 SER A C   
8144  O O   . SER A 1073 ? 1.7523 2.9875 2.5406 0.4286  -0.2076 -1.0807 1073 SER A O   
8145  C CB  . SER A 1073 ? 1.9385 3.1603 2.6454 0.4151  -0.2041 -1.1731 1073 SER A CB  
8146  O OG  . SER A 1073 ? 1.9272 3.1797 2.6726 0.4109  -0.2310 -1.2046 1073 SER A OG  
8147  N N   . ALA A 1074 ? 1.7505 2.9488 2.5010 0.4198  -0.1675 -1.0325 1074 ALA A N   
8148  C CA  . ALA A 1074 ? 1.6559 2.8686 2.4508 0.4029  -0.1630 -0.9947 1074 ALA A CA  
8149  C C   . ALA A 1074 ? 1.5595 2.8122 2.4059 0.3640  -0.1812 -1.0284 1074 ALA A C   
8150  O O   . ALA A 1074 ? 1.5642 2.8305 2.4155 0.3288  -0.1868 -1.0702 1074 ALA A O   
8151  C CB  . ALA A 1074 ? 1.6766 2.8732 2.4652 0.3881  -0.1393 -0.9584 1074 ALA A CB  
8152  N N   . SER A 1075 ? 1.9054 3.1765 2.7894 0.3691  -0.1901 -1.0124 1075 SER A N   
8153  C CA  . SER A 1075 ? 1.8198 3.1307 2.7581 0.3323  -0.2058 -1.0426 1075 SER A CA  
8154  C C   . SER A 1075 ? 1.7501 3.0763 2.7252 0.2976  -0.1904 -1.0073 1075 SER A C   
8155  O O   . SER A 1075 ? 1.7144 3.0317 2.6925 0.3146  -0.1759 -0.9545 1075 SER A O   
8156  C CB  . SER A 1075 ? 1.8211 3.1448 2.7828 0.3560  -0.2240 -1.0461 1075 SER A CB  
8157  O OG  . SER A 1075 ? 1.8119 3.1247 2.7772 0.3777  -0.2114 -0.9888 1075 SER A OG  
8158  N N   . THR A 1076 ? 1.2733 2.6233 2.2754 0.2474  -0.1935 -1.0371 1076 THR A N   
8159  C CA  . THR A 1076 ? 1.1748 2.5411 2.2116 0.2088  -0.1793 -1.0052 1076 THR A CA  
8160  C C   . THR A 1076 ? 1.0963 2.4923 2.1851 0.2046  -0.1800 -0.9815 1076 THR A C   
8161  O O   . THR A 1076 ? 1.0725 2.4685 2.1727 0.2055  -0.1619 -0.9289 1076 THR A O   
8162  C CB  . THR A 1076 ? 1.1239 2.5071 2.1732 0.1520  -0.1845 -1.0475 1076 THR A CB  
8163  O OG1 . THR A 1076 ? 1.1283 2.5070 2.1826 0.1235  -0.1665 -1.0096 1076 THR A OG1 
8164  C CG2 . THR A 1076 ? 1.0384 2.4656 2.1421 0.1147  -0.2026 -1.0915 1076 THR A CG2 
8165  N N   . TRP A 1077 ? 1.1831 2.6037 2.3013 0.2019  -0.2008 -1.0219 1077 TRP A N   
8166  C CA  . TRP A 1077 ? 1.1327 2.5791 2.2968 0.2048  -0.2056 -1.0098 1077 TRP A CA  
8167  C C   . TRP A 1077 ? 1.0884 2.5131 2.2341 0.2488  -0.1920 -0.9505 1077 TRP A C   
8168  O O   . TRP A 1077 ? 0.9976 2.4383 2.1726 0.2363  -0.1773 -0.9122 1077 TRP A O   
8169  C CB  . TRP A 1077 ? 1.1770 2.6352 2.3523 0.2172  -0.2334 -1.0646 1077 TRP A CB  
8170  C CG  . TRP A 1077 ? 1.1818 2.6690 2.4091 0.2155  -0.2441 -1.0686 1077 TRP A CG  
8171  C CD1 . TRP A 1077 ? 1.1560 2.6867 2.4450 0.1697  -0.2529 -1.1031 1077 TRP A CD1 
8172  C CD2 . TRP A 1077 ? 1.2286 2.7024 2.4503 0.2604  -0.2483 -1.0405 1077 TRP A CD2 
8173  N NE1 . TRP A 1077 ? 1.1554 2.7019 2.4808 0.1839  -0.2610 -1.0972 1077 TRP A NE1 
8174  C CE2 . TRP A 1077 ? 1.1974 2.7080 2.4802 0.2399  -0.2589 -1.0586 1077 TRP A CE2 
8175  C CE3 . TRP A 1077 ? 1.2961 2.7299 2.4666 0.3133  -0.2437 -1.0025 1077 TRP A CE3 
8176  C CZ2 . TRP A 1077 ? 1.1917 2.6978 2.4837 0.2725  -0.2655 -1.0388 1077 TRP A CZ2 
8177  C CZ3 . TRP A 1077 ? 1.3106 2.7399 2.4882 0.3437  -0.2512 -0.9836 1077 TRP A CZ3 
8178  C CH2 . TRP A 1077 ? 1.2451 2.7090 2.4816 0.3242  -0.2621 -1.0011 1077 TRP A CH2 
8179  N N   . LEU A 1078 ? 1.2385 2.6277 2.3345 0.2985  -0.1966 -0.9451 1078 LEU A N   
8180  C CA  . LEU A 1078 ? 1.2396 2.6039 2.3101 0.3399  -0.1850 -0.8937 1078 LEU A CA  
8181  C C   . LEU A 1078 ? 1.2726 2.6158 2.3166 0.3417  -0.1585 -0.8468 1078 LEU A C   
8182  O O   . LEU A 1078 ? 1.2942 2.6254 2.3276 0.3627  -0.1432 -0.7997 1078 LEU A O   
8183  C CB  . LEU A 1078 ? 1.2562 2.5902 2.2830 0.3887  -0.2006 -0.9062 1078 LEU A CB  
8184  C CG  . LEU A 1078 ? 1.2124 2.5237 2.2173 0.4283  -0.1951 -0.8617 1078 LEU A CG  
8185  C CD1 . LEU A 1078 ? 1.2211 2.5164 2.2047 0.4648  -0.2195 -0.8836 1078 LEU A CD1 
8186  C CD2 . LEU A 1078 ? 1.2505 2.5290 2.2105 0.4476  -0.1713 -0.8179 1078 LEU A CD2 
8187  N N   . THR A 1079 ? 1.7726 3.1111 2.8054 0.3191  -0.1531 -0.8608 1079 THR A N   
8188  C CA  . THR A 1079 ? 1.7876 3.1073 2.8006 0.3181  -0.1294 -0.8184 1079 THR A CA  
8189  C C   . THR A 1079 ? 1.7080 3.0544 2.7628 0.2913  -0.1148 -0.7816 1079 THR A C   
8190  O O   . THR A 1079 ? 1.7212 3.0553 2.7648 0.3032  -0.0943 -0.7332 1079 THR A O   
8191  C CB  . THR A 1079 ? 1.9361 3.2497 2.9368 0.2904  -0.1282 -0.8429 1079 THR A CB  
8192  O OG1 . THR A 1079 ? 2.0100 3.2938 2.9622 0.3199  -0.1347 -0.8683 1079 THR A OG1 
8193  C CG2 . THR A 1079 ? 1.9168 3.2193 2.9134 0.2795  -0.1053 -0.7973 1079 THR A CG2 
8194  N N   . ALA A 1080 ? 0.5212 1.9066 1.6260 0.2528  -0.1246 -0.8066 1080 ALA A N   
8195  C CA  . ALA A 1080 ? 0.4208 1.8377 1.5699 0.2263  -0.1108 -0.7743 1080 ALA A CA  
8196  C C   . ALA A 1080 ? 0.3896 1.8097 1.5444 0.2564  -0.1102 -0.7538 1080 ALA A C   
8197  O O   . ALA A 1080 ? 0.3687 1.7846 1.5174 0.2692  -0.0906 -0.7059 1080 ALA A O   
8198  C CB  . ALA A 1080 ? 0.3670 1.8266 1.5703 0.1683  -0.1190 -0.8083 1080 ALA A CB  
8199  N N   . PHE A 1081 ? 0.8527 2.2803 2.0190 0.2668  -0.1319 -0.7904 1081 PHE A N   
8200  C CA  . PHE A 1081 ? 0.8169 2.2496 1.9937 0.2888  -0.1319 -0.7711 1081 PHE A CA  
8201  C C   . PHE A 1081 ? 0.8111 2.2120 1.9439 0.3274  -0.1130 -0.7180 1081 PHE A C   
8202  O O   . PHE A 1081 ? 0.7442 2.1558 1.8892 0.3295  -0.0992 -0.6846 1081 PHE A O   
8203  C CB  . PHE A 1081 ? 0.8778 2.3049 2.0523 0.3131  -0.1596 -0.8112 1081 PHE A CB  
8204  C CG  . PHE A 1081 ? 0.9086 2.3388 2.0941 0.3340  -0.1614 -0.7922 1081 PHE A CG  
8205  C CD1 . PHE A 1081 ? 0.8663 2.3336 2.1086 0.3092  -0.1717 -0.8161 1081 PHE A CD1 
8206  C CD2 . PHE A 1081 ? 1.0063 2.4017 2.1450 0.3767  -0.1526 -0.7521 1081 PHE A CD2 
8207  C CE1 . PHE A 1081 ? 0.8768 2.3450 2.1283 0.3283  -0.1732 -0.7990 1081 PHE A CE1 
8208  C CE2 . PHE A 1081 ? 1.0213 2.4166 2.1654 0.3944  -0.1547 -0.7358 1081 PHE A CE2 
8209  C CZ  . PHE A 1081 ? 0.9542 2.3851 2.1543 0.3711  -0.1649 -0.7585 1081 PHE A CZ  
8210  N N   . ALA A 1082 ? 1.7869 3.1495 2.8680 0.3569  -0.1113 -0.7118 1082 ALA A N   
8211  C CA  . ALA A 1082 ? 1.8367 3.1709 2.8784 0.3873  -0.0908 -0.6628 1082 ALA A CA  
8212  C C   . ALA A 1082 ? 1.7859 3.1393 2.8498 0.3577  -0.0653 -0.6265 1082 ALA A C   
8213  O O   . ALA A 1082 ? 1.7738 3.1333 2.8399 0.3627  -0.0473 -0.5875 1082 ALA A O   
8214  C CB  . ALA A 1082 ? 1.9339 3.2259 2.9206 0.4206  -0.0930 -0.6663 1082 ALA A CB  
8215  N N   . LEU A 1083 ? 0.4215 1.7843 1.4999 0.3261  -0.0640 -0.6397 1083 LEU A N   
8216  C CA  . LEU A 1083 ? 0.3526 1.7340 1.4538 0.2952  -0.0428 -0.6067 1083 LEU A CA  
8217  C C   . LEU A 1083 ? 0.3136 1.7293 1.4517 0.2794  -0.0325 -0.5854 1083 LEU A C   
8218  O O   . LEU A 1083 ? 0.3387 1.7534 1.4681 0.2907  -0.0114 -0.5419 1083 LEU A O   
8219  C CB  . LEU A 1083 ? 0.2810 1.6803 1.4089 0.2494  -0.0501 -0.6354 1083 LEU A CB  
8220  C CG  . LEU A 1083 ? 0.3047 1.6694 1.3940 0.2602  -0.0486 -0.6372 1083 LEU A CG  
8221  C CD1 . LEU A 1083 ? 0.3005 1.6744 1.4030 0.2206  -0.0625 -0.6798 1083 LEU A CD1 
8222  C CD2 . LEU A 1083 ? 0.2815 1.6385 1.3645 0.2618  -0.0247 -0.5860 1083 LEU A CD2 
8223  N N   . ARG A 1084 ? 0.6876 2.1336 1.8660 0.2541  -0.0471 -0.6187 1084 ARG A N   
8224  C CA  . ARG A 1084 ? 0.6591 2.1393 1.8756 0.2385  -0.0380 -0.6038 1084 ARG A CA  
8225  C C   . ARG A 1084 ? 0.7200 2.1794 1.9021 0.2812  -0.0248 -0.5653 1084 ARG A C   
8226  O O   . ARG A 1084 ? 0.7166 2.1814 1.8947 0.2747  -0.0001 -0.5228 1084 ARG A O   
8227  C CB  . ARG A 1084 ? 0.6580 2.1564 1.9076 0.2150  -0.0604 -0.6519 1084 ARG A CB  
8228  C CG  . ARG A 1084 ? 0.6114 2.1093 1.8645 0.2174  -0.0580 -0.6427 1084 ARG A CG  
8229  C CD  . ARG A 1084 ? 0.6063 2.1117 1.8817 0.1595  -0.0529 -0.6546 1084 ARG A CD  
8230  N NE  . ARG A 1084 ? 0.6670 2.1711 1.9445 0.1682  -0.0493 -0.6438 1084 ARG A NE  
8231  C CZ  . ARG A 1084 ? 0.7451 2.2557 2.0475 0.1618  -0.0667 -0.6812 1084 ARG A CZ  
8232  N NH1 . ARG A 1084 ? 0.7910 2.3095 2.1168 0.1443  -0.0887 -0.7344 1084 ARG A NH1 
8233  N NH2 . ARG A 1084 ? 0.7488 2.2574 2.0519 0.1721  -0.0615 -0.6663 1084 ARG A NH2 
8234  N N   . VAL A 1085 ? 0.7480 2.1772 1.8962 0.3224  -0.0410 -0.5791 1085 VAL A N   
8235  C CA  . VAL A 1085 ? 0.8132 2.2245 1.9298 0.3561  -0.0294 -0.5452 1085 VAL A CA  
8236  C C   . VAL A 1085 ? 0.8547 2.2355 1.9236 0.3811  -0.0095 -0.5066 1085 VAL A C   
8237  O O   . VAL A 1085 ? 0.8557 2.2251 1.8980 0.4020  0.0060  -0.4741 1085 VAL A O   
8238  C CB  . VAL A 1085 ? 0.7329 2.1203 1.8270 0.3907  -0.0533 -0.5682 1085 VAL A CB  
8239  C CG1 . VAL A 1085 ? 0.7325 2.1137 1.8093 0.4102  -0.0412 -0.5365 1085 VAL A CG1 
8240  C CG2 . VAL A 1085 ? 0.6673 2.0820 1.8094 0.3676  -0.0777 -0.6160 1085 VAL A CG2 
8241  N N   . LEU A 1086 ? 1.5278 2.8955 2.5860 0.3775  -0.0099 -0.5123 1086 LEU A N   
8242  C CA  . LEU A 1086 ? 1.6197 2.9627 2.6423 0.3959  0.0092  -0.4786 1086 LEU A CA  
8243  C C   . LEU A 1086 ? 1.5748 2.9466 2.6224 0.3706  0.0362  -0.4397 1086 LEU A C   
8244  O O   . LEU A 1086 ? 1.6152 2.9749 2.6358 0.3906  0.0560  -0.4042 1086 LEU A O   
8245  C CB  . LEU A 1086 ? 1.6933 3.0167 2.7034 0.3951  0.0011  -0.4977 1086 LEU A CB  
8246  C CG  . LEU A 1086 ? 1.8611 3.1399 2.8191 0.4367  -0.0101 -0.5113 1086 LEU A CG  
8247  C CD1 . LEU A 1086 ? 1.8926 3.1439 2.8102 0.4674  0.0094  -0.4734 1086 LEU A CD1 
8248  C CD2 . LEU A 1086 ? 1.8859 3.1607 2.8384 0.4523  -0.0326 -0.5395 1086 LEU A CD2 
8249  N N   . GLY A 1087 ? 0.9592 2.3696 2.0575 0.3249  0.0367  -0.4482 1087 GLY A N   
8250  C CA  . GLY A 1087 ? 0.8912 2.3325 2.0173 0.2925  0.0605  -0.4137 1087 GLY A CA  
8251  C C   . GLY A 1087 ? 0.8476 2.2918 1.9638 0.2794  0.0730  -0.3914 1087 GLY A C   
8252  O O   . GLY A 1087 ? 0.8703 2.3157 1.9757 0.2610  0.0948  -0.3540 1087 GLY A O   
8253  N N   . GLN A 1088 ? 0.6067 2.0521 1.7265 0.2893  0.0587  -0.4151 1088 GLN A N   
8254  C CA  . GLN A 1088 ? 0.6197 2.0664 1.7297 0.2816  0.0689  -0.3985 1088 GLN A CA  
8255  C C   . GLN A 1088 ? 0.7201 2.1490 1.7875 0.3248  0.0858  -0.3654 1088 GLN A C   
8256  O O   . GLN A 1088 ? 0.7291 2.1574 1.7763 0.3141  0.1090  -0.3297 1088 GLN A O   
8257  C CB  . GLN A 1088 ? 0.5977 2.0498 1.7267 0.2849  0.0460  -0.4362 1088 GLN A CB  
8258  C CG  . GLN A 1088 ? 0.5849 2.0535 1.7544 0.2394  0.0293  -0.4748 1088 GLN A CG  
8259  C CD  . GLN A 1088 ? 0.5852 2.0605 1.7762 0.2356  0.0111  -0.5079 1088 GLN A CD  
8260  O OE1 . GLN A 1088 ? 0.5583 2.0429 1.7783 0.2209  -0.0115 -0.5525 1088 GLN A OE1 
8261  N NE2 . GLN A 1088 ? 0.5903 2.0609 1.7667 0.2482  0.0210  -0.4872 1088 GLN A NE2 
8262  N N   . VAL A 1089 ? 1.2745 2.6864 2.3242 0.3733  0.0743  -0.3789 1089 VAL A N   
8263  C CA  . VAL A 1089 ? 1.3350 2.7190 2.3340 0.4132  0.0877  -0.3531 1089 VAL A CA  
8264  C C   . VAL A 1089 ? 1.3819 2.7611 2.3658 0.4152  0.1098  -0.3225 1089 VAL A C   
8265  O O   . VAL A 1089 ? 1.4087 2.7663 2.3499 0.4407  0.1249  -0.2987 1089 VAL A O   
8266  C CB  . VAL A 1089 ? 1.3101 2.6470 2.2638 0.4518  0.0629  -0.3767 1089 VAL A CB  
8267  C CG1 . VAL A 1089 ? 1.3473 2.6512 2.2429 0.4856  0.0740  -0.3531 1089 VAL A CG1 
8268  C CG2 . VAL A 1089 ? 1.2952 2.6405 2.2728 0.4470  0.0377  -0.4105 1089 VAL A CG2 
8269  N N   . ASN A 1090 ? 0.7543 2.1511 1.7708 0.3865  0.1109  -0.3238 1090 ASN A N   
8270  C CA  . ASN A 1090 ? 0.8326 2.2256 1.8390 0.3865  0.1304  -0.2939 1090 ASN A CA  
8271  C C   . ASN A 1090 ? 0.8565 2.2550 1.8446 0.3680  0.1547  -0.2555 1090 ASN A C   
8272  O O   . ASN A 1090 ? 0.8853 2.2780 1.8547 0.3766  0.1735  -0.2267 1090 ASN A O   
8273  C CB  . ASN A 1090 ? 0.8366 2.2437 1.8787 0.3535  0.1245  -0.3020 1090 ASN A CB  
8274  C CG  . ASN A 1090 ? 0.8892 2.2920 1.9255 0.3567  0.1422  -0.2719 1090 ASN A CG  
8275  O OD1 . ASN A 1090 ? 0.8940 2.2954 1.9099 0.3565  0.1631  -0.2374 1090 ASN A OD1 
8276  N ND2 . ASN A 1090 ? 0.9436 2.3322 1.9849 0.3565  0.1315  -0.2853 1090 ASN A ND2 
8277  N N   . LYS A 1091 ? 0.7906 2.2001 1.7837 0.3420  0.1543  -0.2563 1091 LYS A N   
8278  C CA  . LYS A 1091 ? 0.8177 2.2331 1.7930 0.3178  0.1773  -0.2214 1091 LYS A CA  
8279  C C   . LYS A 1091 ? 0.8135 2.2132 1.7422 0.3537  0.1961  -0.1965 1091 LYS A C   
8280  O O   . LYS A 1091 ? 0.8397 2.2413 1.7496 0.3428  0.2174  -0.1638 1091 LYS A O   
8281  C CB  . LYS A 1091 ? 0.8905 2.3154 1.8748 0.2897  0.1734  -0.2304 1091 LYS A CB  
8282  C CG  . LYS A 1091 ? 0.9461 2.3868 1.9656 0.2335  0.1688  -0.2378 1091 LYS A CG  
8283  C CD  . LYS A 1091 ? 1.0079 2.4524 2.0183 0.2023  0.1808  -0.2242 1091 LYS A CD  
8284  C CE  . LYS A 1091 ? 1.1010 2.5396 2.0701 0.2085  0.2076  -0.1802 1091 LYS A CE  
8285  N NZ  . LYS A 1091 ? 1.1184 2.5593 2.0752 0.1721  0.2216  -0.1615 1091 LYS A NZ  
8286  N N   . TYR A 1092 ? 1.0294 2.4120 1.9373 0.3962  0.1871  -0.2134 1092 TYR A N   
8287  C CA  . TYR A 1092 ? 1.0634 2.4281 1.9216 0.4287  0.2038  -0.1953 1092 TYR A CA  
8288  C C   . TYR A 1092 ? 1.1889 2.5292 2.0271 0.4756  0.1982  -0.2078 1092 TYR A C   
8289  O O   . TYR A 1092 ? 1.2713 2.5912 2.0646 0.5034  0.2110  -0.1965 1092 TYR A O   
8290  C CB  . TYR A 1092 ? 1.0036 2.3657 1.8450 0.4335  0.2010  -0.2015 1092 TYR A CB  
8291  C CG  . TYR A 1092 ? 0.9308 2.3141 1.7989 0.3881  0.2005  -0.2000 1092 TYR A CG  
8292  C CD1 . TYR A 1092 ? 0.9238 2.3169 1.7802 0.3548  0.2228  -0.1685 1092 TYR A CD1 
8293  C CD2 . TYR A 1092 ? 0.9084 2.3001 1.8119 0.3783  0.1773  -0.2314 1092 TYR A CD2 
8294  C CE1 . TYR A 1092 ? 0.9000 2.3076 1.7771 0.3119  0.2231  -0.1676 1092 TYR A CE1 
8295  C CE2 . TYR A 1092 ? 0.8744 2.2829 1.8022 0.3348  0.1778  -0.2326 1092 TYR A CE2 
8296  C CZ  . TYR A 1092 ? 0.8713 2.2862 1.7846 0.3013  0.2014  -0.2003 1092 TYR A CZ  
8297  O OH  . TYR A 1092 ? 0.8364 2.2630 1.7696 0.2572  0.2027  -0.2017 1092 TYR A OH  
8298  N N   . VAL A 1093 ? 1.3986 2.7307 2.2586 0.4791  0.1767  -0.2324 1093 VAL A N   
8299  C CA  . VAL A 1093 ? 1.4713 2.7561 2.2896 0.5108  0.1639  -0.2446 1093 VAL A CA  
8300  C C   . VAL A 1093 ? 1.4291 2.7180 2.2772 0.4990  0.1590  -0.2504 1093 VAL A C   
8301  O O   . VAL A 1093 ? 1.3973 2.6880 2.2703 0.4875  0.1378  -0.2767 1093 VAL A O   
8302  C CB  . VAL A 1093 ? 1.5212 2.7751 2.3144 0.5302  0.1359  -0.2745 1093 VAL A CB  
8303  C CG1 . VAL A 1093 ? 1.6272 2.8386 2.3876 0.5558  0.1208  -0.2915 1093 VAL A CG1 
8304  C CG2 . VAL A 1093 ? 1.5309 2.7723 2.2843 0.5451  0.1416  -0.2651 1093 VAL A CG2 
8305  N N   . GLU A 1094 ? 0.9764 2.2673 1.8218 0.5007  0.1791  -0.2259 1094 GLU A N   
8306  C CA  . GLU A 1094 ? 0.9526 2.2488 1.8277 0.4871  0.1772  -0.2258 1094 GLU A CA  
8307  C C   . GLU A 1094 ? 0.9707 2.2343 1.8337 0.5002  0.1524  -0.2581 1094 GLU A C   
8308  O O   . GLU A 1094 ? 1.0769 2.3041 1.8972 0.5302  0.1467  -0.2677 1094 GLU A O   
8309  C CB  . GLU A 1094 ? 1.0346 2.3225 1.8965 0.4996  0.1977  -0.1997 1094 GLU A CB  
8310  C CG  . GLU A 1094 ? 1.0990 2.3831 1.9867 0.4899  0.1920  -0.2022 1094 GLU A CG  
8311  C CD  . GLU A 1094 ? 1.2078 2.4892 2.0936 0.4988  0.2117  -0.1752 1094 GLU A CD  
8312  O OE1 . GLU A 1094 ? 1.2744 2.5465 2.1285 0.5204  0.2282  -0.1608 1094 GLU A OE1 
8313  O OE2 . GLU A 1094 ? 1.2234 2.5108 2.1390 0.4835  0.2097  -0.1699 1094 GLU A OE2 
8314  N N   . GLN A 1095 ? 0.5809 1.8583 1.4798 0.4759  0.1381  -0.2763 1095 GLN A N   
8315  C CA  . GLN A 1095 ? 0.6273 1.8761 1.5136 0.4867  0.1165  -0.3087 1095 GLN A CA  
8316  C C   . GLN A 1095 ? 0.7288 1.9637 1.6187 0.4859  0.1206  -0.3044 1095 GLN A C   
8317  O O   . GLN A 1095 ? 0.7244 1.9779 1.6380 0.4696  0.1356  -0.2791 1095 GLN A O   
8318  C CB  . GLN A 1095 ? 0.5566 1.8253 1.4732 0.4624  0.0955  -0.3395 1095 GLN A CB  
8319  C CG  . GLN A 1095 ? 0.5941 1.8707 1.5056 0.4681  0.0885  -0.3472 1095 GLN A CG  
8320  C CD  . GLN A 1095 ? 1.0340 2.2689 1.8924 0.5079  0.0789  -0.3573 1095 GLN A CD  
8321  O OE1 . GLN A 1095 ? 1.0798 2.2865 1.9171 0.5236  0.0644  -0.3801 1095 GLN A OE1 
8322  N NE2 . GLN A 1095 ? 1.0428 2.2738 1.8774 0.5222  0.0876  -0.3406 1095 GLN A NE2 
8323  N N   . ASN A 1096 ? 1.7339 2.9353 2.5987 0.5044  0.1075  -0.3288 1096 ASN A N   
8324  C CA  . ASN A 1096 ? 1.8355 3.0151 2.6946 0.5109  0.1122  -0.3268 1096 ASN A CA  
8325  C C   . ASN A 1096 ? 1.8039 3.0033 2.7018 0.4762  0.1074  -0.3306 1096 ASN A C   
8326  O O   . ASN A 1096 ? 1.7723 2.9777 2.6816 0.4582  0.0896  -0.3607 1096 ASN A O   
8327  C CB  . ASN A 1096 ? 1.9565 3.0985 2.7791 0.5360  0.1000  -0.3554 1096 ASN A CB  
8328  C CG  . ASN A 1096 ? 2.0675 3.1847 2.8824 0.5441  0.1068  -0.3545 1096 ASN A CG  
8329  O OD1 . ASN A 1096 ? 2.1826 3.2697 2.9649 0.5715  0.1131  -0.3550 1096 ASN A OD1 
8330  N ND2 . ASN A 1096 ? 2.0342 3.1630 2.8788 0.5186  0.1056  -0.3538 1096 ASN A ND2 
8331  N N   . GLN A 1097 ? 1.4652 2.6744 2.3824 0.4655  0.1224  -0.3015 1097 GLN A N   
8332  C CA  . GLN A 1097 ? 1.4480 2.6769 2.4016 0.4281  0.1170  -0.3024 1097 GLN A CA  
8333  C C   . GLN A 1097 ? 1.5065 2.7118 2.4504 0.4237  0.0997  -0.3372 1097 GLN A C   
8334  O O   . GLN A 1097 ? 1.4601 2.6758 2.4114 0.4057  0.0830  -0.3681 1097 GLN A O   
8335  C CB  . GLN A 1097 ? 1.4321 2.6702 2.4058 0.4190  0.1334  -0.2657 1097 GLN A CB  
8336  C CG  . GLN A 1097 ? 1.3620 2.6265 2.3759 0.3722  0.1262  -0.2648 1097 GLN A CG  
8337  C CD  . GLN A 1097 ? 1.3640 2.6497 2.4053 0.3558  0.1416  -0.2247 1097 GLN A CD  
8338  O OE1 . GLN A 1097 ? 1.3958 2.6748 2.4266 0.3816  0.1581  -0.1980 1097 GLN A OE1 
8339  N NE2 . GLN A 1097 ? 1.3175 2.6296 2.3941 0.3109  0.1356  -0.2218 1097 GLN A NE2 
8340  N N   . ASN A 1098 ? 1.2384 2.4126 2.1651 0.4400  0.1041  -0.3345 1098 ASN A N   
8341  C CA  . ASN A 1098 ? 1.3000 2.4544 2.2188 0.4298  0.0905  -0.3653 1098 ASN A CA  
8342  C C   . ASN A 1098 ? 1.1124 2.2612 2.0118 0.4345  0.0734  -0.4072 1098 ASN A C   
8343  O O   . ASN A 1098 ? 1.0885 2.2307 1.9849 0.4179  0.0603  -0.4383 1098 ASN A O   
8344  C CB  . ASN A 1098 ? 1.4235 2.5417 2.3224 0.4520  0.0996  -0.3578 1098 ASN A CB  
8345  C CG  . ASN A 1098 ? 1.5106 2.6074 2.3975 0.4402  0.0878  -0.3895 1098 ASN A CG  
8346  O OD1 . ASN A 1098 ? 1.5811 2.6554 2.4372 0.4595  0.0833  -0.4173 1098 ASN A OD1 
8347  N ND2 . ASN A 1098 ? 1.5170 2.6208 2.4261 0.4068  0.0831  -0.3860 1098 ASN A ND2 
8348  N N   . SER A 1099 ? 1.5064 2.6576 2.3912 0.4565  0.0729  -0.4087 1099 SER A N   
8349  C CA  . SER A 1099 ? 1.4592 2.6099 2.3310 0.4596  0.0546  -0.4465 1099 SER A CA  
8350  C C   . SER A 1099 ? 1.3365 2.5218 2.2453 0.4191  0.0417  -0.4636 1099 SER A C   
8351  O O   . SER A 1099 ? 1.3486 2.5335 2.2607 0.3982  0.0284  -0.4959 1099 SER A O   
8352  C CB  . SER A 1099 ? 1.4471 2.5957 2.2999 0.4872  0.0554  -0.4402 1099 SER A CB  
8353  O OG  . SER A 1099 ? 1.4033 2.5588 2.2533 0.4857  0.0354  -0.4739 1099 SER A OG  
8354  N N   . ILE A 1100 ? 1.4272 2.6433 2.3630 0.4063  0.0471  -0.4427 1100 ILE A N   
8355  C CA  . ILE A 1100 ? 1.2825 2.5366 2.2586 0.3658  0.0373  -0.4569 1100 ILE A CA  
8356  C C   . ILE A 1100 ? 1.2895 2.5489 2.2848 0.3286  0.0331  -0.4665 1100 ILE A C   
8357  O O   . ILE A 1100 ? 1.2558 2.5293 2.2668 0.2989  0.0171  -0.5017 1100 ILE A O   
8358  C CB  . ILE A 1100 ? 1.1320 2.4191 2.1365 0.3537  0.0518  -0.4224 1100 ILE A CB  
8359  C CG1 . ILE A 1100 ? 1.0655 2.3557 2.0584 0.3770  0.0494  -0.4251 1100 ILE A CG1 
8360  C CG2 . ILE A 1100 ? 1.0450 2.3722 2.0973 0.3024  0.0476  -0.4289 1100 ILE A CG2 
8361  C CD1 . ILE A 1100 ? 1.0031 2.3162 2.0201 0.3562  0.0299  -0.4616 1100 ILE A CD1 
8362  N N   . CYS A 1101 ? 1.2164 2.4629 2.2091 0.3300  0.0468  -0.4363 1101 CYS A N   
8363  C CA  . CYS A 1101 ? 1.2170 2.4633 2.2240 0.2953  0.0430  -0.4402 1101 CYS A CA  
8364  C C   . CYS A 1101 ? 1.2260 2.4553 2.2147 0.2863  0.0249  -0.4885 1101 CYS A C   
8365  O O   . CYS A 1101 ? 1.1744 2.4263 2.1844 0.2485  0.0113  -0.5172 1101 CYS A O   
8366  C CB  . CYS A 1101 ? 1.2841 2.5059 2.2801 0.3112  0.0578  -0.4060 1101 CYS A CB  
8367  S SG  . CYS A 1101 ? 1.5600 2.8126 2.5974 0.2800  0.0718  -0.3578 1101 CYS A SG  
8368  N N   . ASN A 1102 ? 1.2240 2.4151 2.1730 0.3195  0.0258  -0.4993 1102 ASN A N   
8369  C CA  . ASN A 1102 ? 1.2426 2.4168 2.1685 0.3133  0.0113  -0.5457 1102 ASN A CA  
8370  C C   . ASN A 1102 ? 1.1893 2.3887 2.1269 0.2999  -0.0058 -0.5836 1102 ASN A C   
8371  O O   . ASN A 1102 ? 1.1710 2.3778 2.1124 0.2690  -0.0201 -0.6225 1102 ASN A O   
8372  C CB  . ASN A 1102 ? 1.3165 2.4514 2.1979 0.3569  0.0175  -0.5510 1102 ASN A CB  
8373  C CG  . ASN A 1102 ? 1.3641 2.4729 2.2366 0.3702  0.0342  -0.5174 1102 ASN A CG  
8374  O OD1 . ASN A 1102 ? 1.3759 2.4805 2.2585 0.3436  0.0344  -0.5117 1102 ASN A OD1 
8375  N ND2 . ASN A 1102 ? 1.3900 2.4804 2.2437 0.4105  0.0477  -0.4959 1102 ASN A ND2 
8376  N N   . SER A 1103 ? 1.4365 2.6489 2.3800 0.3222  -0.0043 -0.5722 1103 SER A N   
8377  C CA  . SER A 1103 ? 1.3893 2.6250 2.3466 0.3161  -0.0205 -0.6040 1103 SER A CA  
8378  C C   . SER A 1103 ? 1.3368 2.6097 2.3371 0.2625  -0.0314 -0.6261 1103 SER A C   
8379  O O   . SER A 1103 ? 1.3173 2.6010 2.3224 0.2478  -0.0492 -0.6720 1103 SER A O   
8380  C CB  . SER A 1103 ? 1.3671 2.6105 2.3269 0.3445  -0.0144 -0.5784 1103 SER A CB  
8381  O OG  . SER A 1103 ? 1.4338 2.6428 2.3503 0.3909  -0.0099 -0.5718 1103 SER A OG  
8382  N N   . LEU A 1104 ? 1.1126 2.4062 2.1447 0.2321  -0.0204 -0.5944 1104 LEU A N   
8383  C CA  . LEU A 1104 ? 1.0659 2.3929 2.1379 0.1748  -0.0285 -0.6124 1104 LEU A CA  
8384  C C   . LEU A 1104 ? 1.1578 2.4644 2.2100 0.1516  -0.0382 -0.6436 1104 LEU A C   
8385  O O   . LEU A 1104 ? 1.1495 2.4651 2.2042 0.1270  -0.0552 -0.6930 1104 LEU A O   
8386  C CB  . LEU A 1104 ? 0.9903 2.3428 2.0976 0.1485  -0.0123 -0.5659 1104 LEU A CB  
8387  C CG  . LEU A 1104 ? 0.9166 2.2962 2.0473 0.1604  0.0005  -0.5341 1104 LEU A CG  
8388  C CD1 . LEU A 1104 ? 0.8844 2.2795 2.0356 0.1449  0.0205  -0.4834 1104 LEU A CD1 
8389  C CD2 . LEU A 1104 ? 0.8260 2.2450 1.9952 0.1312  -0.0101 -0.5629 1104 LEU A CD2 
8390  N N   . LEU A 1105 ? 1.1014 2.3792 2.1321 0.1613  -0.0270 -0.6153 1105 LEU A N   
8391  C CA  . LEU A 1105 ? 1.1679 2.4211 2.1764 0.1400  -0.0326 -0.6352 1105 LEU A CA  
8392  C C   . LEU A 1105 ? 1.2163 2.4486 2.1876 0.1526  -0.0455 -0.6877 1105 LEU A C   
8393  O O   . LEU A 1105 ? 1.2676 2.4797 2.2156 0.1335  -0.0506 -0.7119 1105 LEU A O   
8394  C CB  . LEU A 1105 ? 1.2227 2.4441 2.2126 0.1607  -0.0170 -0.5923 1105 LEU A CB  
8395  C CG  . LEU A 1105 ? 1.2118 2.4504 2.2355 0.1368  -0.0061 -0.5439 1105 LEU A CG  
8396  C CD1 . LEU A 1105 ? 1.2646 2.4896 2.2819 0.1817  0.0130  -0.4949 1105 LEU A CD1 
8397  C CD2 . LEU A 1105 ? 1.2394 2.4635 2.2604 0.0974  -0.0115 -0.5459 1105 LEU A CD2 
8398  N N   . TRP A 1106 ? 1.3589 2.5959 2.3228 0.1842  -0.0507 -0.7056 1106 TRP A N   
8399  C CA  . TRP A 1106 ? 1.4035 2.6295 2.3380 0.1907  -0.0648 -0.7596 1106 TRP A CA  
8400  C C   . TRP A 1106 ? 1.3443 2.6045 2.3081 0.1429  -0.0830 -0.8061 1106 TRP A C   
8401  O O   . TRP A 1106 ? 1.3727 2.6261 2.3196 0.1145  -0.0924 -0.8469 1106 TRP A O   
8402  C CB  . TRP A 1106 ? 1.4361 2.6523 2.3491 0.2422  -0.0657 -0.7632 1106 TRP A CB  
8403  C CG  . TRP A 1106 ? 1.4564 2.6640 2.3393 0.2499  -0.0800 -0.8183 1106 TRP A CG  
8404  C CD1 . TRP A 1106 ? 1.5004 2.6787 2.3402 0.2553  -0.0777 -0.8415 1106 TRP A CD1 
8405  C CD2 . TRP A 1106 ? 1.4432 2.6727 2.3368 0.2530  -0.0980 -0.8573 1106 TRP A CD2 
8406  N NE1 . TRP A 1106 ? 1.5143 2.6968 2.3359 0.2609  -0.0923 -0.8928 1106 TRP A NE1 
8407  C CE2 . TRP A 1106 ? 1.4880 2.7017 2.3434 0.2602  -0.1062 -0.9036 1106 TRP A CE2 
8408  C CE3 . TRP A 1106 ? 1.4166 2.6775 2.3489 0.2505  -0.1078 -0.8578 1106 TRP A CE3 
8409  C CZ2 . TRP A 1106 ? 1.5210 2.7505 2.3766 0.2658  -0.1251 -0.9505 1106 TRP A CZ2 
8410  C CZ3 . TRP A 1106 ? 1.4249 2.6995 2.3592 0.2562  -0.1273 -0.9039 1106 TRP A CZ3 
8411  C CH2 . TRP A 1106 ? 1.4771 2.7365 2.3738 0.2643  -0.1365 -0.9498 1106 TRP A CH2 
8412  N N   . LEU A 1107 ? 1.3176 2.6144 2.3246 0.1327  -0.0875 -0.8018 1107 LEU A N   
8413  C CA  . LEU A 1107 ? 1.2822 2.6142 2.3218 0.0901  -0.1051 -0.8499 1107 LEU A CA  
8414  C C   . LEU A 1107 ? 1.3499 2.6874 2.3988 0.0327  -0.1071 -0.8620 1107 LEU A C   
8415  O O   . LEU A 1107 ? 1.3859 2.7185 2.4167 0.0078  -0.1197 -0.9121 1107 LEU A O   
8416  C CB  . LEU A 1107 ? 1.1565 2.5284 2.2481 0.0810  -0.1051 -0.8343 1107 LEU A CB  
8417  C CG  . LEU A 1107 ? 1.1135 2.4776 2.1957 0.1362  -0.1012 -0.8117 1107 LEU A CG  
8418  C CD1 . LEU A 1107 ? 1.0981 2.4596 2.1874 0.1492  -0.0796 -0.7478 1107 LEU A CD1 
8419  C CD2 . LEU A 1107 ? 1.0422 2.4398 2.1610 0.1305  -0.1157 -0.8403 1107 LEU A CD2 
8420  N N   . VAL A 1108 ? 1.3534 2.7004 2.4278 0.0115  -0.0945 -0.8155 1108 VAL A N   
8421  C CA  . VAL A 1108 ? 1.3639 2.7160 2.4498 -0.0458 -0.0958 -0.8172 1108 VAL A CA  
8422  C C   . VAL A 1108 ? 1.4731 2.7866 2.5088 -0.0512 -0.1014 -0.8462 1108 VAL A C   
8423  O O   . VAL A 1108 ? 1.4946 2.8150 2.5255 -0.0910 -0.1160 -0.8988 1108 VAL A O   
8424  C CB  . VAL A 1108 ? 1.3374 2.6904 2.4410 -0.0489 -0.0784 -0.7528 1108 VAL A CB  
8425  C CG1 . VAL A 1108 ? 1.3832 2.7017 2.4537 0.0146  -0.0638 -0.7127 1108 VAL A CG1 
8426  C CG2 . VAL A 1108 ? 1.3613 2.7041 2.4611 -0.0981 -0.0805 -0.7498 1108 VAL A CG2 
8427  N N   . GLU A 1109 ? 1.4655 2.7384 2.4628 -0.0119 -0.0892 -0.8144 1109 GLU A N   
8428  C CA  . GLU A 1109 ? 1.5663 2.8008 2.5177 -0.0202 -0.0907 -0.8329 1109 GLU A CA  
8429  C C   . GLU A 1109 ? 1.6135 2.8390 2.5293 -0.0194 -0.1033 -0.8978 1109 GLU A C   
8430  O O   . GLU A 1109 ? 1.6716 2.8734 2.5525 -0.0429 -0.1073 -0.9258 1109 GLU A O   
8431  C CB  . GLU A 1109 ? 1.6329 2.8277 2.5541 0.0273  -0.0738 -0.7875 1109 GLU A CB  
8432  C CG  . GLU A 1109 ? 1.6047 2.8108 2.5603 0.0334  -0.0606 -0.7248 1109 GLU A CG  
8433  C CD  . GLU A 1109 ? 1.6585 2.8246 2.5882 0.0643  -0.0461 -0.6839 1109 GLU A CD  
8434  O OE1 . GLU A 1109 ? 1.6399 2.8087 2.5858 0.0934  -0.0323 -0.6352 1109 GLU A OE1 
8435  O OE2 . GLU A 1109 ? 1.7196 2.8514 2.6122 0.0588  -0.0481 -0.7022 1109 GLU A OE2 
8436  N N   . ASN A 1110 ? 1.8048 3.0496 2.7288 0.0059  -0.1100 -0.9227 1110 ASN A N   
8437  C CA  . ASN A 1110 ? 1.8389 3.0760 2.7276 0.0147  -0.1210 -0.9824 1110 ASN A CA  
8438  C C   . ASN A 1110 ? 1.7745 3.0522 2.6945 -0.0145 -0.1401 -1.0358 1110 ASN A C   
8439  O O   . ASN A 1110 ? 1.8056 3.0838 2.7040 -0.0384 -0.1519 -1.0939 1110 ASN A O   
8440  C CB  . ASN A 1110 ? 1.8958 3.1086 2.7509 0.0811  -0.1124 -0.9699 1110 ASN A CB  
8441  C CG  . ASN A 1110 ? 1.9634 3.1373 2.7908 0.1110  -0.0928 -0.9202 1110 ASN A CG  
8442  O OD1 . ASN A 1110 ? 1.9679 3.1377 2.8049 0.1491  -0.0814 -0.8743 1110 ASN A OD1 
8443  N ND2 . ASN A 1110 ? 2.0257 3.1703 2.8183 0.0928  -0.0888 -0.9306 1110 ASN A ND2 
8444  N N   . TYR A 1111 ? 1.8759 3.1880 2.8468 -0.0137 -0.1425 -1.0182 1111 TYR A N   
8445  C CA  . TYR A 1111 ? 1.8289 3.1786 2.8320 -0.0324 -0.1605 -1.0687 1111 TYR A CA  
8446  C C   . TYR A 1111 ? 1.7715 3.1647 2.8352 -0.0919 -0.1664 -1.0746 1111 TYR A C   
8447  O O   . TYR A 1111 ? 1.7050 3.1333 2.8127 -0.0940 -0.1744 -1.0876 1111 TYR A O   
8448  C CB  . TYR A 1111 ? 1.8087 3.1628 2.8167 0.0232  -0.1626 -1.0598 1111 TYR A CB  
8449  C CG  . TYR A 1111 ? 1.8817 3.2009 2.8317 0.0708  -0.1618 -1.0748 1111 TYR A CG  
8450  C CD1 . TYR A 1111 ? 1.9131 3.2391 2.8468 0.0746  -0.1782 -1.1360 1111 TYR A CD1 
8451  C CD2 . TYR A 1111 ? 1.9232 3.2044 2.8355 0.1097  -0.1440 -1.0297 1111 TYR A CD2 
8452  C CE1 . TYR A 1111 ? 1.9893 3.2858 2.8689 0.1163  -0.1759 -1.1500 1111 TYR A CE1 
8453  C CE2 . TYR A 1111 ? 1.9994 3.2506 2.8596 0.1502  -0.1412 -1.0439 1111 TYR A CE2 
8454  C CZ  . TYR A 1111 ? 2.0353 3.2945 2.8782 0.1530  -0.1567 -1.1033 1111 TYR A CZ  
8455  O OH  . TYR A 1111 ? 2.1161 3.3482 2.9070 0.1915  -0.1525 -1.1172 1111 TYR A OH  
8456  N N   . GLN A 1112 ? 1.5853 2.9758 2.6516 -0.1418 -0.1623 -1.0658 1112 GLN A N   
8457  C CA  . GLN A 1112 ? 1.5907 2.9810 2.6742 -0.1811 -0.1391 -1.0576 1112 GLN A CA  
8458  C C   . GLN A 1112 ? 1.7079 3.0765 2.7586 -0.2213 -0.1245 -1.0913 1112 GLN A C   
8459  O O   . GLN A 1112 ? 1.7549 3.1024 2.7849 -0.2474 -0.1193 -1.0702 1112 GLN A O   
8460  C CB  . GLN A 1112 ? 1.5223 2.9175 2.6308 -0.1921 -0.1288 -0.9916 1112 GLN A CB  
8461  C CG  . GLN A 1112 ? 1.4882 2.8737 2.5986 -0.2372 -0.1057 -0.9810 1112 GLN A CG  
8462  C CD  . GLN A 1112 ? 1.4334 2.8178 2.5578 -0.2485 -0.0962 -0.9161 1112 GLN A CD  
8463  O OE1 . GLN A 1112 ? 1.4391 2.8186 2.5597 -0.2428 -0.1032 -0.8887 1112 GLN A OE1 
8464  N NE2 . GLN A 1112 ? 1.3821 2.7718 2.5231 -0.2637 -0.0791 -0.8908 1112 GLN A NE2 
8465  N N   . LEU A 1113 ? 1.9530 3.3331 3.0058 -0.2254 -0.1167 -1.1408 1113 LEU A N   
8466  C CA  . LEU A 1113 ? 2.0378 3.4121 3.0672 -0.2571 -0.1010 -1.1765 1113 LEU A CA  
8467  C C   . LEU A 1113 ? 2.0869 3.4448 3.1045 -0.3051 -0.0831 -1.1484 1113 LEU A C   
8468  O O   . LEU A 1113 ? 2.0450 3.3994 3.0785 -0.3172 -0.0789 -1.1032 1113 LEU A O   
8469  C CB  . LEU A 1113 ? 2.0127 3.4175 3.0680 -0.2572 -0.0910 -1.2245 1113 LEU A CB  
8470  C CG  . LEU A 1113 ? 1.9684 3.3898 3.0328 -0.2113 -0.1097 -1.2584 1113 LEU A CG  
8471  C CD1 . LEU A 1113 ? 1.9432 3.3989 3.0476 -0.2105 -0.1018 -1.2983 1113 LEU A CD1 
8472  C CD2 . LEU A 1113 ? 2.0235 3.4338 3.0473 -0.1983 -0.1172 -1.2851 1113 LEU A CD2 
8473  N N   . ASP A 1114 ? 2.4908 3.8401 3.4791 -0.3322 -0.0724 -1.1742 1114 ASP A N   
8474  C CA  . ASP A 1114 ? 2.5612 3.8937 3.5307 -0.3802 -0.0567 -1.1532 1114 ASP A CA  
8475  C C   . ASP A 1114 ? 2.5212 3.8733 3.5153 -0.4102 -0.0357 -1.1532 1114 ASP A C   
8476  O O   . ASP A 1114 ? 2.5769 3.9294 3.5552 -0.4506 -0.0179 -1.1655 1114 ASP A O   
8477  C CB  . ASP A 1114 ? 2.6982 4.0195 3.6284 -0.4007 -0.0505 -1.1845 1114 ASP A CB  
8478  C CG  . ASP A 1114 ? 2.7929 4.0752 3.6838 -0.3979 -0.0645 -1.1606 1114 ASP A CG  
8479  O OD1 . ASP A 1114 ? 2.7760 4.0404 3.6718 -0.3982 -0.0737 -1.1127 1114 ASP A OD1 
8480  O OD2 . ASP A 1114 ? 2.8761 4.1470 3.7326 -0.3956 -0.0655 -1.1892 1114 ASP A OD2 
8481  N N   . ASN A 1115 ? 1.3714 2.7391 2.4012 -0.3911 -0.0373 -1.1399 1115 ASN A N   
8482  C CA  . ASN A 1115 ? 1.3169 2.7002 2.3681 -0.4164 -0.0175 -1.1388 1115 ASN A CA  
8483  C C   . ASN A 1115 ? 1.1669 2.5540 2.2474 -0.3925 -0.0239 -1.1037 1115 ASN A C   
8484  O O   . ASN A 1115 ? 1.1143 2.5173 2.2193 -0.3972 -0.0122 -1.1098 1115 ASN A O   
8485  C CB  . ASN A 1115 ? 1.3578 2.7724 2.4268 -0.4204 -0.0050 -1.1980 1115 ASN A CB  
8486  C CG  . ASN A 1115 ? 1.3223 2.7593 2.4267 -0.3755 -0.0183 -1.2241 1115 ASN A CG  
8487  O OD1 . ASN A 1115 ? 1.3279 2.7938 2.4582 -0.3746 -0.0100 -1.2680 1115 ASN A OD1 
8488  N ND2 . ASN A 1115 ? 1.2851 2.7107 2.3920 -0.3386 -0.0398 -1.1976 1115 ASN A ND2 
8489  N N   . GLY A 1116 ? 0.9946 2.3687 2.0725 -0.3663 -0.0420 -1.0676 1116 GLY A N   
8490  C CA  . GLY A 1116 ? 0.8881 2.2688 1.9929 -0.3421 -0.0479 -1.0274 1116 GLY A CA  
8491  C C   . GLY A 1116 ? 0.7900 2.1917 1.9226 -0.3020 -0.0592 -1.0522 1116 GLY A C   
8492  O O   . GLY A 1116 ? 0.7420 2.1511 1.8963 -0.2794 -0.0641 -1.0185 1116 GLY A O   
8493  N N   . SER A 1117 ? 1.5566 2.9702 2.6901 -0.2925 -0.0628 -1.1090 1117 SER A N   
8494  C CA  . SER A 1117 ? 1.5131 2.9458 2.6724 -0.2528 -0.0774 -1.1350 1117 SER A CA  
8495  C C   . SER A 1117 ? 1.5250 2.9551 2.6728 -0.2109 -0.1039 -1.1318 1117 SER A C   
8496  O O   . SER A 1117 ? 1.5766 2.9904 2.6961 -0.2142 -0.1093 -1.1199 1117 SER A O   
8497  C CB  . SER A 1117 ? 1.5298 2.9832 2.7040 -0.2580 -0.0696 -1.1960 1117 SER A CB  
8498  O OG  . SER A 1117 ? 1.5705 3.0277 2.7266 -0.2468 -0.0783 -1.2357 1117 SER A OG  
8499  N N   . PHE A 1118 ? 1.2421 2.6877 2.4105 -0.1720 -0.1209 -1.1417 1118 PHE A N   
8500  C CA  . PHE A 1118 ? 1.2110 2.6587 2.3706 -0.1291 -0.1466 -1.1304 1118 PHE A CA  
8501  C C   . PHE A 1118 ? 1.2214 2.6767 2.3719 -0.0979 -0.1657 -1.1849 1118 PHE A C   
8502  O O   . PHE A 1118 ? 1.2101 2.6818 2.3868 -0.0802 -0.1723 -1.2055 1118 PHE A O   
8503  C CB  . PHE A 1118 ? 1.1576 2.6206 2.3480 -0.1033 -0.1508 -1.0783 1118 PHE A CB  
8504  C CG  . PHE A 1118 ? 1.1491 2.6080 2.3422 -0.1146 -0.1378 -1.0151 1118 PHE A CG  
8505  C CD1 . PHE A 1118 ? 1.1599 2.5999 2.3387 -0.1605 -0.1189 -1.0043 1118 PHE A CD1 
8506  C CD2 . PHE A 1118 ? 1.1331 2.6107 2.3458 -0.0748 -0.1410 -0.9642 1118 PHE A CD2 
8507  C CE1 . PHE A 1118 ? 1.1426 2.5790 2.3247 -0.1697 -0.1084 -0.9462 1118 PHE A CE1 
8508  C CE2 . PHE A 1118 ? 1.1115 2.5885 2.3305 -0.0803 -0.1245 -0.9056 1118 PHE A CE2 
8509  C CZ  . PHE A 1118 ? 1.1130 2.5686 2.3167 -0.1295 -0.1110 -0.8976 1118 PHE A CZ  
8510  N N   . LYS A 1119 ? 1.6160 3.0570 2.7269 -0.0909 -0.1741 -1.2079 1119 LYS A N   
8511  C CA  . LYS A 1119 ? 1.6447 3.0902 2.7395 -0.0607 -0.1895 -1.2577 1119 LYS A CA  
8512  C C   . LYS A 1119 ? 1.6144 3.0611 2.7016 -0.0141 -0.2180 -1.2431 1119 LYS A C   
8513  O O   . LYS A 1119 ? 1.6176 3.0408 2.6782 0.0087  -0.2117 -1.1962 1119 LYS A O   
8514  C CB  . LYS A 1119 ? 1.8296 3.2586 2.8796 -0.0702 -0.1827 -1.2881 1119 LYS A CB  
8515  C CG  . LYS A 1119 ? 1.9558 3.3505 2.9573 -0.0695 -0.1874 -1.2591 1119 LYS A CG  
8516  C CD  . LYS A 1119 ? 2.3921 3.7655 3.3372 -0.0523 -0.1892 -1.2947 1119 LYS A CD  
8517  C CE  . LYS A 1119 ? 2.4250 3.7979 3.3589 -0.0898 -0.1672 -1.3134 1119 LYS A CE  
8518  N NZ  . LYS A 1119 ? 2.4359 3.7724 3.3337 -0.1117 -0.1616 -1.2814 1119 LYS A NZ  
8519  N N   . GLU A 1120 ? 1.8886 3.3510 2.9925 0.0135  -0.2326 -1.2715 1120 GLU A N   
8520  C CA  . GLU A 1120 ? 1.9385 3.3884 3.0232 0.0714  -0.2442 -1.2500 1120 GLU A CA  
8521  C C   . GLU A 1120 ? 2.0603 3.4772 3.0784 0.1017  -0.2447 -1.2737 1120 GLU A C   
8522  O O   . GLU A 1120 ? 2.0977 3.5239 3.1030 0.0830  -0.2582 -1.3364 1120 GLU A O   
8523  C CB  . GLU A 1120 ? 1.9258 3.4033 3.0519 0.0887  -0.2634 -1.2723 1120 GLU A CB  
8524  C CG  . GLU A 1120 ? 1.9948 3.4462 3.0848 0.1550  -0.2683 -1.2585 1120 GLU A CG  
8525  C CD  . GLU A 1120 ? 1.9874 3.4096 3.0570 0.1926  -0.2481 -1.1842 1120 GLU A CD  
8526  O OE1 . GLU A 1120 ? 1.9526 3.3793 3.0438 0.2193  -0.2513 -1.1569 1120 GLU A OE1 
8527  O OE2 . GLU A 1120 ? 2.0137 3.4081 3.0456 0.1948  -0.2294 -1.1544 1120 GLU A OE2 
8528  N N   . ASN A 1121 ? 1.6992 3.0792 2.6752 0.1473  -0.2291 -1.2256 1121 ASN A N   
8529  C CA  . ASN A 1121 ? 1.7918 3.1391 2.7030 0.1745  -0.2243 -1.2416 1121 ASN A CA  
8530  C C   . ASN A 1121 ? 1.8773 3.2278 2.7707 0.2087  -0.2417 -1.2833 1121 ASN A C   
8531  O O   . ASN A 1121 ? 1.9063 3.2642 2.7797 0.1938  -0.2522 -1.3431 1121 ASN A O   
8532  C CB  . ASN A 1121 ? 1.7942 3.1031 2.6703 0.2119  -0.2017 -1.1784 1121 ASN A CB  
8533  C CG  . ASN A 1121 ? 1.8279 3.1038 2.6397 0.2321  -0.1924 -1.1932 1121 ASN A CG  
8534  O OD1 . ASN A 1121 ? 1.8443 3.1162 2.6338 0.2005  -0.1907 -1.2280 1121 ASN A OD1 
8535  N ND2 . ASN A 1121 ? 1.8329 3.0851 2.6134 0.2827  -0.1856 -1.1681 1121 ASN A ND2 
8536  N N   . SER A 1122 ? 1.9609 3.3049 2.8590 0.2540  -0.2447 -1.2508 1122 SER A N   
8537  C CA  . SER A 1122 ? 2.0350 3.3788 2.9164 0.2918  -0.2619 -1.2798 1122 SER A CA  
8538  C C   . SER A 1122 ? 2.0479 3.4301 2.9678 0.2678  -0.2881 -1.3439 1122 SER A C   
8539  O O   . SER A 1122 ? 2.0091 3.4184 2.9681 0.2192  -0.2919 -1.3680 1122 SER A O   
8540  C CB  . SER A 1122 ? 2.0016 3.3337 2.8905 0.3360  -0.2624 -1.2294 1122 SER A CB  
8541  O OG  . SER A 1122 ? 1.9135 3.2737 2.8630 0.3189  -0.2713 -1.2190 1122 SER A OG  
8542  N N   . GLN A 1123 ? 2.4517 3.8369 3.3620 0.3009  -0.3067 -1.3721 1123 GLN A N   
8543  C CA  . GLN A 1123 ? 2.4663 3.8886 3.4170 0.2836  -0.3336 -1.4332 1123 GLN A CA  
8544  C C   . GLN A 1123 ? 2.3321 3.7737 3.3427 0.2911  -0.3469 -1.4113 1123 GLN A C   
8545  O O   . GLN A 1123 ? 2.3153 3.7883 3.3692 0.2811  -0.3703 -1.4559 1123 GLN A O   
8546  C CB  . GLN A 1123 ? 2.6565 4.0751 3.5689 0.3142  -0.3487 -1.4782 1123 GLN A CB  
8547  C CG  . GLN A 1123 ? 2.8298 4.2251 3.6753 0.3133  -0.3310 -1.4924 1123 GLN A CG  
8548  C CD  . GLN A 1123 ? 3.0014 4.4218 3.8413 0.3285  -0.3420 -1.5370 1123 GLN A CD  
8549  O OE1 . GLN A 1123 ? 3.0259 4.4924 3.9245 0.3226  -0.3590 -1.5701 1123 GLN A OE1 
8550  N NE2 . GLN A 1123 ? 3.1213 4.5170 3.8986 0.3493  -0.3285 -1.5328 1123 GLN A NE2 
8551  N N   . TYR A 1124 ? 1.5100 2.9333 2.5237 0.3077  -0.3310 -1.3438 1124 TYR A N   
8552  C CA  . TYR A 1124 ? 1.3770 2.8127 2.4370 0.3213  -0.3412 -1.3186 1124 TYR A CA  
8553  C C   . TYR A 1124 ? 1.2777 2.7585 2.4095 0.2755  -0.3533 -1.3533 1124 TYR A C   
8554  O O   . TYR A 1124 ? 1.2042 2.7016 2.3588 0.2278  -0.3406 -1.3547 1124 TYR A O   
8555  C CB  . TYR A 1124 ? 1.2928 2.7045 2.3432 0.3376  -0.3181 -1.2428 1124 TYR A CB  
8556  C CG  . TYR A 1124 ? 1.2119 2.6227 2.2860 0.3673  -0.3271 -1.2111 1124 TYR A CG  
8557  C CD1 . TYR A 1124 ? 1.2413 2.6368 2.2943 0.4118  -0.3471 -1.2194 1124 TYR A CD1 
8558  C CD2 . TYR A 1124 ? 1.1204 2.5442 2.2349 0.3504  -0.3150 -1.1716 1124 TYR A CD2 
8559  C CE1 . TYR A 1124 ? 1.2018 2.5921 2.2724 0.4385  -0.3563 -1.1894 1124 TYR A CE1 
8560  C CE2 . TYR A 1124 ? 1.0754 2.4962 2.2073 0.3768  -0.3215 -1.1423 1124 TYR A CE2 
8561  C CZ  . TYR A 1124 ? 1.0913 2.4936 2.2002 0.4209  -0.3427 -1.1511 1124 TYR A CZ  
8562  O OH  . TYR A 1124 ? 1.0186 2.4143 2.1412 0.4457  -0.3499 -1.1215 1124 TYR A OH  
8563  N N   . GLN A 1125 ? 1.4570 2.9576 2.6241 0.2891  -0.3790 -1.3842 1125 GLN A N   
8564  C CA  . GLN A 1125 ? 1.3774 2.9199 2.6203 0.2540  -0.3904 -1.4078 1125 GLN A CA  
8565  C C   . GLN A 1125 ? 1.2718 2.8054 2.5347 0.2841  -0.3884 -1.3527 1125 GLN A C   
8566  O O   . GLN A 1125 ? 1.2615 2.7773 2.5078 0.3304  -0.4046 -1.3471 1125 GLN A O   
8567  C CB  . GLN A 1125 ? 1.5068 3.0728 2.7766 0.2553  -0.4167 -1.4790 1125 GLN A CB  
8568  C CG  . GLN A 1125 ? 1.6613 3.2239 2.8954 0.2585  -0.4105 -1.5277 1125 GLN A CG  
8569  C CD  . GLN A 1125 ? 1.7210 3.2966 2.9675 0.2164  -0.3727 -1.5379 1125 GLN A CD  
8570  O OE1 . GLN A 1125 ? 1.6987 3.2614 2.9332 0.1900  -0.3525 -1.5006 1125 GLN A OE1 
8571  N NE2 . GLN A 1125 ? 1.7781 3.3836 3.0500 0.2102  -0.3644 -1.5871 1125 GLN A NE2 
8572  N N   . PRO A 1126 ? 1.1543 2.6988 2.4490 0.2576  -0.3680 -1.3108 1126 PRO A N   
8573  C CA  . PRO A 1126 ? 1.1389 2.6769 2.4519 0.2838  -0.3652 -1.2622 1126 PRO A CA  
8574  C C   . PRO A 1126 ? 1.1430 2.7196 2.5277 0.2676  -0.3861 -1.2990 1126 PRO A C   
8575  O O   . PRO A 1126 ? 1.1955 2.7635 2.5865 0.3046  -0.4040 -1.2956 1126 PRO A O   
8576  C CB  . PRO A 1126 ? 1.0514 2.5917 2.3719 0.2561  -0.3332 -1.2082 1126 PRO A CB  
8577  C CG  . PRO A 1126 ? 1.0633 2.6032 2.3611 0.2220  -0.3211 -1.2248 1126 PRO A CG  
8578  C CD  . PRO A 1126 ? 1.1063 2.6653 2.4143 0.2058  -0.3454 -1.3004 1126 PRO A CD  
8579  N N   . ILE A 1127 ? 1.4141 3.0047 2.8288 0.2162  -0.3724 -1.3341 1127 ILE A N   
8580  C CA  . ILE A 1127 ? 1.4308 3.0249 2.8903 0.2004  -0.3689 -1.3637 1127 ILE A CA  
8581  C C   . ILE A 1127 ? 1.4832 3.0839 2.9567 0.1842  -0.3670 -1.4357 1127 ILE A C   
8582  O O   . ILE A 1127 ? 1.4821 3.0822 2.9343 0.1624  -0.3486 -1.4550 1127 ILE A O   
8583  C CB  . ILE A 1127 ? 1.4555 3.0431 2.9311 0.1593  -0.3316 -1.3309 1127 ILE A CB  
8584  C CG1 . ILE A 1127 ? 1.4329 3.0109 2.8728 0.1325  -0.3057 -1.3024 1127 ILE A CG1 
8585  C CG2 . ILE A 1127 ? 1.4284 3.0158 2.9194 0.1792  -0.3330 -1.2764 1127 ILE A CG2 
8586  C CD1 . ILE A 1127 ? 1.4774 3.0543 2.8958 0.1139  -0.2996 -1.3496 1127 ILE A CD1 
8587  N N   . LYS A 1128 ? 1.3439 2.9554 2.8586 0.1968  -0.3835 -1.4732 1128 LYS A N   
8588  C CA  . LYS A 1128 ? 1.4090 3.0382 2.9524 0.1849  -0.3768 -1.5393 1128 LYS A CA  
8589  C C   . LYS A 1128 ? 1.4427 3.0794 3.0235 0.1396  -0.3378 -1.5455 1128 LYS A C   
8590  O O   . LYS A 1128 ? 1.4385 3.0747 3.0560 0.1337  -0.3353 -1.5382 1128 LYS A O   
8591  C CB  . LYS A 1128 ? 1.4292 3.0702 3.0050 0.2205  -0.4133 -1.5800 1128 LYS A CB  
8592  C CG  . LYS A 1128 ? 1.4501 3.1202 3.0721 0.2111  -0.4056 -1.6482 1128 LYS A CG  
8593  C CD  . LYS A 1128 ? 1.4763 3.1628 3.0732 0.2125  -0.4004 -1.6820 1128 LYS A CD  
8594  C CE  . LYS A 1128 ? 1.4420 3.1453 3.0483 0.1659  -0.3548 -1.6910 1128 LYS A CE  
8595  N NZ  . LYS A 1128 ? 1.4769 3.2175 3.0979 0.1620  -0.3470 -1.7446 1128 LYS A NZ  
8596  N N   . LEU A 1129 ? 1.9531 3.5971 3.5232 0.1072  -0.3067 -1.5579 1129 LEU A N   
8597  C CA  . LEU A 1129 ? 1.9863 3.6404 3.5885 0.0632  -0.2688 -1.5672 1129 LEU A CA  
8598  C C   . LEU A 1129 ? 2.0927 3.7825 3.7465 0.0588  -0.2643 -1.6339 1129 LEU A C   
8599  O O   . LEU A 1129 ? 2.1668 3.8773 3.8197 0.0761  -0.2771 -1.6726 1129 LEU A O   
8600  C CB  . LEU A 1129 ? 1.9276 3.5725 3.4926 0.0265  -0.2360 -1.5407 1129 LEU A CB  
8601  C CG  . LEU A 1129 ? 1.8588 3.4732 3.3850 0.0190  -0.2300 -1.4723 1129 LEU A CG  
8602  C CD1 . LEU A 1129 ? 1.8353 3.4429 3.3434 -0.0280 -0.1915 -1.4520 1129 LEU A CD1 
8603  C CD2 . LEU A 1129 ? 1.8237 3.4288 3.3722 0.0278  -0.2376 -1.4415 1129 LEU A CD2 
8604  N N   . GLN A 1130 ? 1.3840 3.0836 3.0833 0.0352  -0.2449 -1.6468 1130 GLN A N   
8605  C CA  . GLN A 1130 ? 1.4179 3.1563 3.1723 0.0270  -0.2364 -1.7098 1130 GLN A CA  
8606  C C   . GLN A 1130 ? 1.3553 3.1170 3.1018 -0.0095 -0.2018 -1.7300 1130 GLN A C   
8607  O O   . GLN A 1130 ? 1.3011 3.0441 3.0013 -0.0335 -0.1814 -1.6927 1130 GLN A O   
8608  C CB  . GLN A 1130 ? 1.4933 3.2345 3.2980 0.0115  -0.2247 -1.7168 1130 GLN A CB  
8609  C CG  . GLN A 1130 ? 1.5374 3.2561 3.3521 0.0420  -0.2559 -1.6932 1130 GLN A CG  
8610  C CD  . GLN A 1130 ? 1.5902 3.3222 3.4688 0.0351  -0.2519 -1.7218 1130 GLN A CD  
8611  O OE1 . GLN A 1130 ? 1.6429 3.4084 3.5716 0.0397  -0.2555 -1.7811 1130 GLN A OE1 
8612  N NE2 . GLN A 1130 ? 1.5645 3.2729 3.4439 0.0239  -0.2438 -1.6801 1130 GLN A NE2 
8613  N N   . GLY A 1131 ? 1.7685 3.5727 3.5614 -0.0141 -0.1960 -1.7895 1131 GLY A N   
8614  C CA  . GLY A 1131 ? 1.7968 3.6288 3.5879 -0.0522 -0.1616 -1.8120 1131 GLY A CA  
8615  C C   . GLY A 1131 ? 1.8767 3.7378 3.6569 -0.0400 -0.1704 -1.8453 1131 GLY A C   
8616  O O   . GLY A 1131 ? 1.9232 3.7782 3.6858 -0.0006 -0.2036 -1.8455 1131 GLY A O   
8617  N N   . THR A 1132 ? 1.9570 3.8503 3.7449 -0.0762 -0.1393 -1.8729 1132 THR A N   
8618  C CA  . THR A 1132 ? 1.9841 3.9116 3.7648 -0.0736 -0.1408 -1.9076 1132 THR A CA  
8619  C C   . THR A 1132 ? 1.9554 3.8512 3.6687 -0.0602 -0.1528 -1.8671 1132 THR A C   
8620  O O   . THR A 1132 ? 1.8985 3.7495 3.5704 -0.0644 -0.1510 -1.8125 1132 THR A O   
8621  C CB  . THR A 1132 ? 2.0321 3.9927 3.8214 -0.1239 -0.1000 -1.9331 1132 THR A CB  
8622  O OG1 . THR A 1132 ? 2.0188 3.9842 3.8457 -0.1506 -0.0773 -1.9402 1132 THR A OG1 
8623  C CG2 . THR A 1132 ? 2.1010 4.1184 3.9227 -0.1187 -0.1031 -1.9954 1132 THR A CG2 
8624  N N   . LEU A 1133 ? 1.7507 3.6710 3.4534 -0.0445 -0.1648 -1.8945 1133 LEU A N   
8625  C CA  . LEU A 1133 ? 1.7897 3.6832 3.4277 -0.0353 -0.1728 -1.8611 1133 LEU A CA  
8626  C C   . LEU A 1133 ? 1.8232 3.6917 3.4172 -0.0788 -0.1406 -1.8217 1133 LEU A C   
8627  O O   . LEU A 1133 ? 1.8400 3.6680 3.3813 -0.0721 -0.1472 -1.7754 1133 LEU A O   
8628  C CB  . LEU A 1133 ? 1.8248 3.7542 3.4596 -0.0196 -0.1841 -1.9016 1133 LEU A CB  
8629  C CG  . LEU A 1133 ? 1.8080 3.7521 3.4660 0.0310  -0.2236 -1.9310 1133 LEU A CG  
8630  C CD1 . LEU A 1133 ? 1.8113 3.7909 3.5445 0.0353  -0.2278 -1.9770 1133 LEU A CD1 
8631  C CD2 . LEU A 1133 ? 1.8477 3.8180 3.4830 0.0451  -0.2334 -1.9581 1133 LEU A CD2 
8632  N N   . PRO A 1134 ? 1.7789 3.6715 3.3927 -0.1237 -0.1065 -1.8409 1134 PRO A N   
8633  C CA  . PRO A 1134 ? 1.7825 3.6496 3.3567 -0.1681 -0.0761 -1.8035 1134 PRO A CA  
8634  C C   . PRO A 1134 ? 1.7617 3.5885 3.3305 -0.1724 -0.0734 -1.7568 1134 PRO A C   
8635  O O   . PRO A 1134 ? 1.7268 3.5116 3.2481 -0.1759 -0.0740 -1.7052 1134 PRO A O   
8636  C CB  . PRO A 1134 ? 1.8087 3.7185 3.4154 -0.2103 -0.0440 -1.8459 1134 PRO A CB  
8637  C CG  . PRO A 1134 ? 1.8509 3.8117 3.5042 -0.1885 -0.0572 -1.9060 1134 PRO A CG  
8638  C CD  . PRO A 1134 ? 1.8229 3.7715 3.4940 -0.1353 -0.0955 -1.9028 1134 PRO A CD  
8639  N N   . VAL A 1135 ? 1.3454 3.1867 2.9642 -0.1733 -0.0698 -1.7761 1135 VAL A N   
8640  C CA  . VAL A 1135 ? 1.2798 3.0864 2.8976 -0.1770 -0.0673 -1.7346 1135 VAL A CA  
8641  C C   . VAL A 1135 ? 1.2329 2.9977 2.8133 -0.1428 -0.0952 -1.6870 1135 VAL A C   
8642  O O   . VAL A 1135 ? 1.1995 2.9295 2.7352 -0.1580 -0.0869 -1.6373 1135 VAL A O   
8643  C CB  . VAL A 1135 ? 1.2688 3.0944 2.9483 -0.1646 -0.0733 -1.7650 1135 VAL A CB  
8644  C CG1 . VAL A 1135 ? 1.2139 2.9992 2.8866 -0.1554 -0.0811 -1.7175 1135 VAL A CG1 
8645  C CG2 . VAL A 1135 ? 1.2931 3.1535 3.0076 -0.2053 -0.0398 -1.8024 1135 VAL A CG2 
8646  N N   . GLU A 1136 ? 1.9454 3.7152 3.5433 -0.0971 -0.1291 -1.7033 1136 GLU A N   
8647  C CA  . GLU A 1136 ? 1.9046 3.6379 3.4694 -0.0615 -0.1584 -1.6620 1136 GLU A CA  
8648  C C   . GLU A 1136 ? 1.9044 3.6070 3.4073 -0.0721 -0.1523 -1.6169 1136 GLU A C   
8649  O O   . GLU A 1136 ? 1.8806 3.5484 3.3563 -0.0668 -0.1585 -1.5669 1136 GLU A O   
8650  C CB  . GLU A 1136 ? 1.9065 3.6546 3.4832 -0.0132 -0.1955 -1.6939 1136 GLU A CB  
8651  C CG  . GLU A 1136 ? 1.8820 3.5946 3.4181 0.0249  -0.2272 -1.6548 1136 GLU A CG  
8652  C CD  . GLU A 1136 ? 1.8980 3.6228 3.4454 0.0726  -0.2654 -1.6864 1136 GLU A CD  
8653  O OE1 . GLU A 1136 ? 1.9084 3.6710 3.4899 0.0772  -0.2678 -1.7389 1136 GLU A OE1 
8654  O OE2 . GLU A 1136 ? 1.8957 3.5932 3.4162 0.1049  -0.2936 -1.6579 1136 GLU A OE2 
8655  N N   . ALA A 1137 ? 1.8580 3.5753 3.3406 -0.0879 -0.1403 -1.6351 1137 ALA A N   
8656  C CA  . ALA A 1137 ? 1.8674 3.5563 3.2930 -0.0988 -0.1350 -1.5975 1137 ALA A CA  
8657  C C   . ALA A 1137 ? 1.8360 3.4972 3.2452 -0.1346 -0.1120 -1.5513 1137 ALA A C   
8658  O O   . ALA A 1137 ? 1.8035 3.4305 3.1815 -0.1273 -0.1201 -1.5025 1137 ALA A O   
8659  C CB  . ALA A 1137 ? 1.9292 3.6416 3.3410 -0.1173 -0.1216 -1.6286 1137 ALA A CB  
8660  N N   . ARG A 1138 ? 2.0472 3.7256 3.4776 -0.1740 -0.0831 -1.5673 1138 ARG A N   
8661  C CA  . ARG A 1138 ? 2.0270 3.6819 3.4429 -0.2104 -0.0599 -1.5266 1138 ARG A CA  
8662  C C   . ARG A 1138 ? 1.9284 3.5614 3.3559 -0.1922 -0.0718 -1.4910 1138 ARG A C   
8663  O O   . ARG A 1138 ? 1.8873 3.4903 3.2875 -0.2048 -0.0660 -1.4391 1138 ARG A O   
8664  C CB  . ARG A 1138 ? 2.1183 3.8007 3.5595 -0.2519 -0.0289 -1.5583 1138 ARG A CB  
8665  C CG  . ARG A 1138 ? 2.1603 3.8211 3.5752 -0.2974 -0.0013 -1.5206 1138 ARG A CG  
8666  C CD  . ARG A 1138 ? 2.2516 3.9438 3.6822 -0.3396 0.0289  -1.5590 1138 ARG A CD  
8667  N NE  . ARG A 1138 ? 2.3034 3.9792 3.7176 -0.3815 0.0547  -1.5287 1138 ARG A NE  
8668  C CZ  . ARG A 1138 ? 2.3842 4.0808 3.8001 -0.4244 0.0832  -1.5523 1138 ARG A CZ  
8669  N NH1 . ARG A 1138 ? 2.4382 4.1745 3.8743 -0.4317 0.0905  -1.6067 1138 ARG A NH1 
8670  N NH2 . ARG A 1138 ? 2.3946 4.0743 3.7907 -0.4609 0.1044  -1.5218 1138 ARG A NH2 
8671  N N   . GLU A 1139 ? 1.8827 3.5322 3.3513 -0.1628 -0.0891 -1.5185 1139 GLU A N   
8672  C CA  . GLU A 1139 ? 1.7847 3.4159 3.2660 -0.1424 -0.1035 -1.4883 1139 GLU A CA  
8673  C C   . GLU A 1139 ? 1.7650 3.3697 3.2097 -0.1119 -0.1287 -1.4465 1139 GLU A C   
8674  O O   . GLU A 1139 ? 1.7251 3.3061 3.1534 -0.1157 -0.1269 -1.3947 1139 GLU A O   
8675  C CB  . GLU A 1139 ? 1.7566 3.4114 3.2887 -0.1139 -0.1220 -1.5317 1139 GLU A CB  
8676  C CG  . GLU A 1139 ? 1.7277 3.4039 3.3060 -0.1399 -0.0995 -1.5616 1139 GLU A CG  
8677  C CD  . GLU A 1139 ? 1.6790 3.3325 3.2609 -0.1547 -0.0880 -1.5203 1139 GLU A CD  
8678  O OE1 . GLU A 1139 ? 1.6840 3.3426 3.3049 -0.1388 -0.0988 -1.5328 1139 GLU A OE1 
8679  O OE2 . GLU A 1139 ? 1.6563 3.2873 3.2019 -0.1826 -0.0686 -1.4750 1139 GLU A OE2 
8680  N N   . ASN A 1140 ? 2.2277 3.8398 3.6598 -0.0814 -0.1514 -1.4697 1140 ASN A N   
8681  C CA  . ASN A 1140 ? 2.2151 3.8059 3.6110 -0.0493 -0.1770 -1.4370 1140 ASN A CA  
8682  C C   . ASN A 1140 ? 2.1362 3.7018 3.4898 -0.0715 -0.1632 -1.3879 1140 ASN A C   
8683  O O   . ASN A 1140 ? 2.0923 3.6401 3.4264 -0.0542 -0.1766 -1.3431 1140 ASN A O   
8684  C CB  . ASN A 1140 ? 2.3325 3.9363 3.7170 -0.0173 -0.1997 -1.4758 1140 ASN A CB  
8685  C CG  . ASN A 1140 ? 2.4121 3.9985 3.7682 0.0253  -0.2327 -1.4518 1140 ASN A CG  
8686  O OD1 . ASN A 1140 ? 2.4957 4.0820 3.8230 0.0488  -0.2490 -1.4693 1140 ASN A OD1 
8687  N ND2 . ASN A 1140 ? 2.3959 3.9696 3.7583 0.0351  -0.2413 -1.4101 1140 ASN A ND2 
8688  N N   . SER A 1141 ? 2.1349 3.7024 3.4770 -0.1097 -0.1371 -1.3955 1141 SER A N   
8689  C CA  . SER A 1141 ? 2.1000 3.6429 3.4041 -0.1348 -0.1237 -1.3508 1141 SER A CA  
8690  C C   . SER A 1141 ? 1.9996 3.5277 3.3098 -0.1536 -0.1106 -1.3014 1141 SER A C   
8691  O O   . SER A 1141 ? 1.9552 3.4644 3.2435 -0.1510 -0.1143 -1.2512 1141 SER A O   
8692  C CB  . SER A 1141 ? 2.1577 3.7069 3.4484 -0.1739 -0.0990 -1.3721 1141 SER A CB  
8693  O OG  . SER A 1141 ? 2.1657 3.6906 3.4279 -0.2058 -0.0831 -1.3266 1141 SER A OG  
8694  N N   . LEU A 1142 ? 1.5388 3.0784 2.8802 -0.1732 -0.0938 -1.3159 1142 LEU A N   
8695  C CA  . LEU A 1142 ? 1.4478 2.9747 2.7941 -0.1922 -0.0790 -1.2718 1142 LEU A CA  
8696  C C   . LEU A 1142 ? 1.4023 2.9215 2.7523 -0.1560 -0.1009 -1.2336 1142 LEU A C   
8697  O O   . LEU A 1142 ? 1.3711 2.8756 2.7038 -0.1600 -0.0967 -1.1784 1142 LEU A O   
8698  C CB  . LEU A 1142 ? 1.4068 2.9496 2.7884 -0.2127 -0.0606 -1.3016 1142 LEU A CB  
8699  C CG  . LEU A 1142 ? 1.3373 2.8675 2.7126 -0.2501 -0.0338 -1.2638 1142 LEU A CG  
8700  C CD1 . LEU A 1142 ? 1.3381 2.8872 2.7475 -0.2706 -0.0151 -1.3019 1142 LEU A CD1 
8701  C CD2 . LEU A 1142 ? 1.2597 2.7733 2.6310 -0.2335 -0.0419 -1.2073 1142 LEU A CD2 
8702  N N   . TYR A 1143 ? 1.2394 2.7715 2.6127 -0.1196 -0.1245 -1.2616 1143 TYR A N   
8703  C CA  . TYR A 1143 ? 1.1875 2.7171 2.5672 -0.0845 -0.1450 -1.2264 1143 TYR A CA  
8704  C C   . TYR A 1143 ? 1.1500 2.6701 2.4984 -0.0689 -0.1536 -1.1789 1143 TYR A C   
8705  O O   . TYR A 1143 ? 1.1000 2.6150 2.4465 -0.0677 -0.1457 -1.1236 1143 TYR A O   
8706  C CB  . TYR A 1143 ? 1.1810 2.7254 2.5837 -0.0444 -0.1748 -1.2660 1143 TYR A CB  
8707  C CG  . TYR A 1143 ? 1.1460 2.6910 2.5552 -0.0070 -0.1956 -1.2269 1143 TYR A CG  
8708  C CD1 . TYR A 1143 ? 1.1131 2.6627 2.5549 -0.0010 -0.1970 -1.2240 1143 TYR A CD1 
8709  C CD2 . TYR A 1143 ? 1.1476 2.6917 2.5319 0.0237  -0.2113 -1.1905 1143 TYR A CD2 
8710  C CE1 . TYR A 1143 ? 1.1052 2.6578 2.5521 0.0351  -0.2132 -1.1846 1143 TYR A CE1 
8711  C CE2 . TYR A 1143 ? 1.1216 2.6724 2.5139 0.0628  -0.2250 -1.1501 1143 TYR A CE2 
8712  C CZ  . TYR A 1143 ? 1.1030 2.6573 2.5249 0.0685  -0.2257 -1.1469 1143 TYR A CZ  
8713  O OH  . TYR A 1143 ? 1.0863 2.6460 2.5131 0.1098  -0.2357 -1.1053 1143 TYR A OH  
8714  N N   . LEU A 1144 ? 2.3181 3.8381 3.6434 -0.0561 -0.1676 -1.2004 1144 LEU A N   
8715  C CA  . LEU A 1144 ? 2.3192 3.8332 3.6179 -0.0394 -0.1760 -1.1594 1144 LEU A CA  
8716  C C   . LEU A 1144 ? 2.3151 3.8167 3.6047 -0.0734 -0.1498 -1.1101 1144 LEU A C   
8717  O O   . LEU A 1144 ? 2.2877 3.7911 3.5820 -0.0603 -0.1455 -1.0550 1144 LEU A O   
8718  C CB  . LEU A 1144 ? 2.3333 3.8437 3.6018 -0.0325 -0.1886 -1.1944 1144 LEU A CB  
8719  C CG  . LEU A 1144 ? 2.2961 3.8089 3.5438 0.0055  -0.2103 -1.1695 1144 LEU A CG  
8720  C CD1 . LEU A 1144 ? 2.2835 3.8135 3.5463 0.0545  -0.2370 -1.1754 1144 LEU A CD1 
8721  C CD2 . LEU A 1144 ? 2.3309 3.8301 3.5381 -0.0007 -0.2155 -1.2018 1144 LEU A CD2 
8722  N N   . THR A 1145 ? 1.2463 2.7376 2.5240 -0.1155 -0.1299 -1.1284 1145 THR A N   
8723  C CA  . THR A 1145 ? 1.2285 2.7057 2.4924 -0.1494 -0.1076 -1.0835 1145 THR A CA  
8724  C C   . THR A 1145 ? 1.1952 2.6728 2.4767 -0.1560 -0.0930 -1.0411 1145 THR A C   
8725  O O   . THR A 1145 ? 1.1808 2.6493 2.4519 -0.1726 -0.0782 -0.9916 1145 THR A O   
8726  C CB  . THR A 1145 ? 1.3185 2.7872 2.5677 -0.1947 -0.0872 -1.1108 1145 THR A CB  
8727  O OG1 . THR A 1145 ? 1.3410 2.8147 2.5792 -0.1875 -0.0973 -1.1627 1145 THR A OG1 
8728  C CG2 . THR A 1145 ? 1.3294 2.7807 2.5541 -0.2216 -0.0746 -1.0646 1145 THR A CG2 
8729  N N   . ALA A 1146 ? 0.7488 2.2363 2.0559 -0.1429 -0.0970 -1.0602 1146 ALA A N   
8730  C CA  . ALA A 1146 ? 0.7703 2.2570 2.0910 -0.1466 -0.0834 -1.0202 1146 ALA A CA  
8731  C C   . ALA A 1146 ? 0.7599 2.2531 2.0814 -0.1063 -0.0933 -0.9685 1146 ALA A C   
8732  O O   . ALA A 1146 ? 0.7218 2.2105 2.0375 -0.1115 -0.0763 -0.9138 1146 ALA A O   
8733  C CB  . ALA A 1146 ? 0.7784 2.2733 2.1280 -0.1462 -0.0841 -1.0585 1146 ALA A CB  
8734  N N   . PHE A 1147 ? 1.3211 2.8264 2.6479 -0.0639 -0.1191 -0.9869 1147 PHE A N   
8735  C CA  . PHE A 1147 ? 1.2934 2.8097 2.6232 -0.0141 -0.1290 -0.9465 1147 PHE A CA  
8736  C C   . PHE A 1147 ? 1.2703 2.7858 2.5816 -0.0005 -0.1211 -0.8995 1147 PHE A C   
8737  O O   . PHE A 1147 ? 1.2588 2.7764 2.5677 0.0261  -0.1093 -0.8467 1147 PHE A O   
8738  C CB  . PHE A 1147 ? 1.3046 2.8337 2.6425 0.0268  -0.1594 -0.9866 1147 PHE A CB  
8739  C CG  . PHE A 1147 ? 1.2781 2.8165 2.6260 0.0764  -0.1677 -0.9583 1147 PHE A CG  
8740  C CD1 . PHE A 1147 ? 1.2555 2.8020 2.6215 0.0999  -0.1907 -0.9946 1147 PHE A CD1 
8741  C CD2 . PHE A 1147 ? 1.2721 2.8079 2.6081 0.1013  -0.1504 -0.8954 1147 PHE A CD2 
8742  C CE1 . PHE A 1147 ? 1.2433 2.7939 2.6142 0.1472  -0.1978 -0.9673 1147 PHE A CE1 
8743  C CE2 . PHE A 1147 ? 1.2697 2.8070 2.6059 0.1492  -0.1535 -0.8692 1147 PHE A CE2 
8744  C CZ  . PHE A 1147 ? 1.2547 2.7986 2.6077 0.1722  -0.1778 -0.9044 1147 PHE A CZ  
8745  N N   . THR A 1148 ? 0.9728 2.4842 2.2697 -0.0160 -0.1264 -0.9209 1148 THR A N   
8746  C CA  . THR A 1148 ? 0.9933 2.5037 2.2765 -0.0070 -0.1185 -0.8811 1148 THR A CA  
8747  C C   . THR A 1148 ? 0.8987 2.3988 2.1779 -0.0351 -0.0918 -0.8289 1148 THR A C   
8748  O O   . THR A 1148 ? 0.8847 2.3873 2.1605 -0.0104 -0.0796 -0.7773 1148 THR A O   
8749  C CB  . THR A 1148 ? 0.9268 2.4312 2.1928 -0.0267 -0.1297 -0.9184 1148 THR A CB  
8750  O OG1 . THR A 1148 ? 0.9549 2.4470 2.2090 -0.0579 -0.1131 -0.8862 1148 THR A OG1 
8751  C CG2 . THR A 1148 ? 0.9281 2.4231 2.1887 -0.0595 -0.1370 -0.9836 1148 THR A CG2 
8752  N N   . VAL A 1149 ? 0.9563 2.4438 2.2337 -0.0841 -0.0803 -0.8434 1149 VAL A N   
8753  C CA  . VAL A 1149 ? 0.9416 2.4186 2.2123 -0.1140 -0.0556 -0.7977 1149 VAL A CA  
8754  C C   . VAL A 1149 ? 0.8917 2.3766 2.1694 -0.0819 -0.0461 -0.7517 1149 VAL A C   
8755  O O   . VAL A 1149 ? 0.8796 2.3645 2.1495 -0.0685 -0.0327 -0.6999 1149 VAL A O   
8756  C CB  . VAL A 1149 ? 0.7483 2.2136 2.0178 -0.1608 -0.0435 -0.8245 1149 VAL A CB  
8757  C CG1 . VAL A 1149 ? 0.7458 2.2026 2.0075 -0.1853 -0.0187 -0.7746 1149 VAL A CG1 
8758  C CG2 . VAL A 1149 ? 0.7496 2.2038 2.0047 -0.1959 -0.0450 -0.8664 1149 VAL A CG2 
8759  N N   . ILE A 1150 ? 0.5893 2.0800 1.8804 -0.0680 -0.0525 -0.7720 1150 ILE A N   
8760  C CA  . ILE A 1150 ? 0.5176 2.0121 1.8110 -0.0422 -0.0418 -0.7320 1150 ILE A CA  
8761  C C   . ILE A 1150 ? 0.5048 2.0043 1.7874 0.0045  -0.0386 -0.6888 1150 ILE A C   
8762  O O   . ILE A 1150 ? 0.5103 2.0055 1.7800 0.0092  -0.0178 -0.6367 1150 ILE A O   
8763  C CB  . ILE A 1150 ? 0.4662 1.9691 1.7776 -0.0174 -0.0584 -0.7647 1150 ILE A CB  
8764  C CG1 . ILE A 1150 ? 0.4963 1.9961 1.8218 -0.0539 -0.0664 -0.8241 1150 ILE A CG1 
8765  C CG2 . ILE A 1150 ? 0.3917 1.8943 1.7022 -0.0026 -0.0439 -0.7256 1150 ILE A CG2 
8766  C CD1 . ILE A 1150 ? 0.5118 2.0198 1.8602 -0.0336 -0.0813 -0.8552 1150 ILE A CD1 
8767  N N   . GLY A 1151 ? 2.2553 3.7622 3.5402 0.0407  -0.0583 -0.7133 1151 GLY A N   
8768  C CA  . GLY A 1151 ? 2.2830 3.7901 3.5544 0.0885  -0.0542 -0.6815 1151 GLY A CA  
8769  C C   . GLY A 1151 ? 2.3025 3.8034 3.5640 0.0686  -0.0344 -0.6410 1151 GLY A C   
8770  O O   . GLY A 1151 ? 2.3081 3.8039 3.5580 0.0802  -0.0138 -0.5920 1151 GLY A O   
8771  N N   . ILE A 1152 ? 0.5216 2.0219 1.7859 0.0370  -0.0410 -0.6619 1152 ILE A N   
8772  C CA  . ILE A 1152 ? 0.5545 2.0497 1.8119 0.0254  -0.0264 -0.6247 1152 ILE A CA  
8773  C C   . ILE A 1152 ? 0.5994 2.0882 1.8506 0.0029  -0.0039 -0.5791 1152 ILE A C   
8774  O O   . ILE A 1152 ? 0.6161 2.1024 1.8596 0.0162  0.0127  -0.5327 1152 ILE A O   
8775  C CB  . ILE A 1152 ? 0.5171 2.0074 1.7753 -0.0226 -0.0356 -0.6536 1152 ILE A CB  
8776  C CG1 . ILE A 1152 ? 0.4653 1.9616 1.7258 -0.0115 -0.0602 -0.7103 1152 ILE A CG1 
8777  C CG2 . ILE A 1152 ? 0.1399 1.6261 1.3944 -0.0271 -0.0224 -0.6105 1152 ILE A CG2 
8778  C CD1 . ILE A 1152 ? 0.4351 1.9214 1.6906 -0.0643 -0.0717 -0.7638 1152 ILE A CD1 
8779  N N   . ARG A 1153 ? 1.5191 3.0043 2.7726 -0.0311 -0.0025 -0.5947 1153 ARG A N   
8780  C CA  . ARG A 1153 ? 1.5400 3.0193 2.7843 -0.0495 0.0192  -0.5541 1153 ARG A CA  
8781  C C   . ARG A 1153 ? 1.5049 2.9884 2.7405 0.0015  0.0299  -0.5162 1153 ARG A C   
8782  O O   . ARG A 1153 ? 1.5312 3.0128 2.7557 0.0187  0.0444  -0.4738 1153 ARG A O   
8783  C CB  . ARG A 1153 ? 1.6074 3.0811 2.8550 -0.0877 0.0199  -0.5818 1153 ARG A CB  
8784  C CG  . ARG A 1153 ? 1.6998 3.1621 2.9449 -0.1414 0.0174  -0.6134 1153 ARG A CG  
8785  C CD  . ARG A 1153 ? 1.7674 3.2183 2.9957 -0.1764 0.0365  -0.5711 1153 ARG A CD  
8786  N NE  . ARG A 1153 ? 1.8042 3.2413 3.0235 -0.2267 0.0366  -0.5991 1153 ARG A NE  
8787  C CZ  . ARG A 1153 ? 1.8289 3.2547 3.0319 -0.2605 0.0480  -0.5711 1153 ARG A CZ  
8788  N NH1 . ARG A 1153 ? 1.8102 3.2380 3.0075 -0.2504 0.0595  -0.5146 1153 ARG A NH1 
8789  N NH2 . ARG A 1153 ? 1.8836 3.2967 3.0746 -0.3031 0.0484  -0.5998 1153 ARG A NH2 
8790  N N   . LYS A 1154 ? 0.7801 2.2674 2.0186 0.0274  0.0229  -0.5323 1154 LYS A N   
8791  C CA  . LYS A 1154 ? 0.7800 2.2656 2.0020 0.0685  0.0362  -0.4953 1154 LYS A CA  
8792  C C   . LYS A 1154 ? 0.8396 2.3205 2.0437 0.1036  0.0494  -0.4553 1154 LYS A C   
8793  O O   . LYS A 1154 ? 0.8347 2.3109 2.0195 0.1125  0.0704  -0.4119 1154 LYS A O   
8794  C CB  . LYS A 1154 ? 0.7604 2.2490 1.9868 0.1088  0.0188  -0.5240 1154 LYS A CB  
8795  C CG  . LYS A 1154 ? 0.7311 2.2233 1.9722 0.0863  0.0120  -0.5499 1154 LYS A CG  
8796  C CD  . LYS A 1154 ? 0.7379 2.2256 1.9628 0.0890  0.0328  -0.5107 1154 LYS A CD  
8797  C CE  . LYS A 1154 ? 0.7359 2.2270 1.9754 0.0891  0.0228  -0.5368 1154 LYS A CE  
8798  N NZ  . LYS A 1154 ? 0.7439 2.2303 1.9643 0.0917  0.0444  -0.4976 1154 LYS A NZ  
8799  N N   . ALA A 1155 ? 1.3238 2.8051 2.5330 0.1241  0.0376  -0.4728 1155 ALA A N   
8800  C CA  . ALA A 1155 ? 1.3900 2.8631 2.5827 0.1662  0.0485  -0.4437 1155 ALA A CA  
8801  C C   . ALA A 1155 ? 1.4744 2.9484 2.6722 0.1380  0.0600  -0.4175 1155 ALA A C   
8802  O O   . ALA A 1155 ? 1.5223 2.9894 2.7072 0.1651  0.0748  -0.3837 1155 ALA A O   
8803  C CB  . ALA A 1155 ? 1.3807 2.8436 2.5665 0.2055  0.0311  -0.4759 1155 ALA A CB  
8804  N N   . PHE A 1156 ? 1.2765 2.7562 2.4911 0.0835  0.0527  -0.4346 1156 PHE A N   
8805  C CA  . PHE A 1156 ? 1.3248 2.8038 2.5461 0.0541  0.0575  -0.4173 1156 PHE A CA  
8806  C C   . PHE A 1156 ? 1.3259 2.8012 2.5355 0.0732  0.0798  -0.3628 1156 PHE A C   
8807  O O   . PHE A 1156 ? 1.3425 2.8171 2.5585 0.0804  0.0822  -0.3486 1156 PHE A O   
8808  C CB  . PHE A 1156 ? 1.3412 2.8180 2.5682 -0.0125 0.0545  -0.4294 1156 PHE A CB  
8809  C CG  . PHE A 1156 ? 1.3744 2.8472 2.6042 -0.0442 0.0589  -0.4079 1156 PHE A CG  
8810  C CD1 . PHE A 1156 ? 1.3990 2.8706 2.6388 -0.0629 0.0427  -0.4373 1156 PHE A CD1 
8811  C CD2 . PHE A 1156 ? 1.3879 2.8580 2.6088 -0.0536 0.0783  -0.3580 1156 PHE A CD2 
8812  C CE1 . PHE A 1156 ? 1.4197 2.8861 2.6618 -0.0913 0.0452  -0.4160 1156 PHE A CE1 
8813  C CE2 . PHE A 1156 ? 1.4113 2.8780 2.6364 -0.0804 0.0803  -0.3367 1156 PHE A CE2 
8814  C CZ  . PHE A 1156 ? 1.4337 2.8981 2.6702 -0.0995 0.0635  -0.3650 1156 PHE A CZ  
8815  N N   . ASP A 1157 ? 1.4531 2.9261 2.6452 0.0821  0.0961  -0.3334 1157 ASP A N   
8816  C CA  . ASP A 1157 ? 1.4825 2.9532 2.6626 0.0877  0.1175  -0.2835 1157 ASP A CA  
8817  C C   . ASP A 1157 ? 1.5050 2.9700 2.6777 0.1396  0.1255  -0.2651 1157 ASP A C   
8818  O O   . ASP A 1157 ? 1.5138 2.9787 2.6851 0.1392  0.1395  -0.2293 1157 ASP A O   
8819  C CB  . ASP A 1157 ? 1.5245 2.9938 2.6835 0.0796  0.1336  -0.2582 1157 ASP A CB  
8820  C CG  . ASP A 1157 ? 1.5913 3.0613 2.7554 0.0228  0.1306  -0.2681 1157 ASP A CG  
8821  O OD1 . ASP A 1157 ? 1.6203 3.0904 2.8021 -0.0108 0.1166  -0.2936 1157 ASP A OD1 
8822  O OD2 . ASP A 1157 ? 1.6000 3.0678 2.7473 0.0118  0.1426  -0.2523 1157 ASP A OD2 
8823  N N   . ILE A 1158 ? 1.0892 2.5469 2.2556 0.1845  0.1168  -0.2899 1158 ILE A N   
8824  C CA  . ILE A 1158 ? 1.0725 2.5109 2.2201 0.2341  0.1245  -0.2757 1158 ILE A CA  
8825  C C   . ILE A 1158 ? 1.1549 2.5644 2.2942 0.2291  0.1114  -0.2887 1158 ILE A C   
8826  O O   . ILE A 1158 ? 1.2421 2.6199 2.3553 0.2587  0.1171  -0.2731 1158 ILE A O   
8827  C CB  . ILE A 1158 ? 1.0250 2.4315 2.1294 0.2836  0.1208  -0.2893 1158 ILE A CB  
8828  C CG1 . ILE A 1158 ? 0.9053 2.3277 2.0211 0.2750  0.1073  -0.3205 1158 ILE A CG1 
8829  C CG2 . ILE A 1158 ? 1.0321 2.4349 2.1137 0.3146  0.1442  -0.2519 1158 ILE A CG2 
8830  C CD1 . ILE A 1158 ? 0.9175 2.3023 1.9939 0.3141  0.0903  -0.3510 1158 ILE A CD1 
8831  N N   . CYS A 1159 ? 1.6419 3.0619 2.8032 0.1903  0.0943  -0.3186 1159 CYS A N   
8832  C CA  . CYS A 1159 ? 1.6991 3.0954 2.8544 0.1770  0.0844  -0.3264 1159 CYS A CA  
8833  C C   . CYS A 1159 ? 1.7023 3.1308 2.8984 0.1154  0.0788  -0.3294 1159 CYS A C   
8834  O O   . CYS A 1159 ? 1.7384 3.1601 2.9361 0.0886  0.0605  -0.3654 1159 CYS A O   
8835  C CB  . CYS A 1159 ? 1.6966 3.0551 2.8182 0.1985  0.0660  -0.3687 1159 CYS A CB  
8836  S SG  . CYS A 1159 ? 2.5444 3.8565 3.6374 0.2110  0.0635  -0.3651 1159 CYS A SG  
8837  N N   . PRO A 1160 ? 1.2331 2.6979 2.4610 0.0908  0.0952  -0.2920 1160 PRO A N   
8838  C CA  . PRO A 1160 ? 1.1960 2.6726 2.4442 0.0286  0.0903  -0.2878 1160 PRO A CA  
8839  C C   . PRO A 1160 ? 1.2285 2.6874 2.4779 0.0214  0.0787  -0.2933 1160 PRO A C   
8840  O O   . PRO A 1160 ? 1.2562 2.6863 2.4846 0.0526  0.0857  -0.2661 1160 PRO A O   
8841  C CB  . PRO A 1160 ? 1.2432 2.7198 2.4817 0.0205  0.1110  -0.2367 1160 PRO A CB  
8842  C CG  . PRO A 1160 ? 1.2685 2.7429 2.4947 0.0820  0.1270  -0.2140 1160 PRO A CG  
8843  C CD  . PRO A 1160 ? 1.2443 2.7142 2.4617 0.1164  0.1177  -0.2516 1160 PRO A CD  
8844  N N   . LEU A 1161 ? 1.0491 2.5087 2.3067 -0.0208 0.0598  -0.3301 1161 LEU A N   
8845  C CA  . LEU A 1161 ? 1.1151 2.5336 2.3468 -0.0246 0.0460  -0.3429 1161 LEU A CA  
8846  C C   . LEU A 1161 ? 1.1285 2.5609 2.3801 -0.0907 0.0298  -0.3691 1161 LEU A C   
8847  O O   . LEU A 1161 ? 1.1026 2.5587 2.3706 -0.1207 0.0199  -0.4080 1161 LEU A O   
8848  C CB  . LEU A 1161 ? 1.1090 2.4851 2.2963 0.0221  0.0370  -0.3770 1161 LEU A CB  
8849  C CG  . LEU A 1161 ? 1.1392 2.4647 2.2888 0.0349  0.0274  -0.3897 1161 LEU A CG  
8850  C CD1 . LEU A 1161 ? 1.0710 2.3873 2.2295 0.0108  0.0293  -0.3557 1161 LEU A CD1 
8851  C CD2 . LEU A 1161 ? 1.1477 2.4365 2.2583 0.1012  0.0349  -0.3876 1161 LEU A CD2 
8852  N N   . VAL A 1162 ? 1.3038 2.7205 2.5539 -0.1139 0.0267  -0.3480 1162 VAL A N   
8853  C CA  . VAL A 1162 ? 1.3297 2.7507 2.5904 -0.1782 0.0100  -0.3712 1162 VAL A CA  
8854  C C   . VAL A 1162 ? 1.3325 2.7398 2.5718 -0.1829 -0.0071 -0.4331 1162 VAL A C   
8855  O O   . VAL A 1162 ? 1.2740 2.6993 2.5223 -0.2194 -0.0128 -0.4655 1162 VAL A O   
8856  C CB  . VAL A 1162 ? 1.4589 2.8397 2.6982 -0.1832 0.0039  -0.3495 1162 VAL A CB  
8857  C CG1 . VAL A 1162 ? 1.4520 2.8564 2.7228 -0.2006 0.0161  -0.2923 1162 VAL A CG1 
8858  C CG2 . VAL A 1162 ? 1.5577 2.8852 2.7509 -0.1172 0.0060  -0.3496 1162 VAL A CG2 
8859  N N   . LYS A 1163 ? 0.9774 2.3359 2.1701 -0.1404 -0.0125 -0.4499 1163 LYS A N   
8860  C CA  . LYS A 1163 ? 1.0118 2.3521 2.1773 -0.1482 -0.0294 -0.5092 1163 LYS A CA  
8861  C C   . LYS A 1163 ? 0.9554 2.3284 2.1383 -0.1451 -0.0324 -0.5450 1163 LYS A C   
8862  O O   . LYS A 1163 ? 0.9547 2.3266 2.1274 -0.1655 -0.0480 -0.5986 1163 LYS A O   
8863  C CB  . LYS A 1163 ? 1.0799 2.3637 2.1915 -0.0986 -0.0304 -0.5175 1163 LYS A CB  
8864  C CG  . LYS A 1163 ? 1.1102 2.3666 2.1885 -0.1281 -0.0481 -0.5684 1163 LYS A CG  
8865  C CD  . LYS A 1163 ? 1.1724 2.3786 2.1965 -0.0792 -0.0475 -0.5869 1163 LYS A CD  
8866  C CE  . LYS A 1163 ? 1.2010 2.3891 2.1930 -0.1146 -0.0643 -0.6451 1163 LYS A CE  
8867  N NZ  . LYS A 1163 ? 1.2505 2.4040 2.1926 -0.0729 -0.0643 -0.6801 1163 LYS A NZ  
8868  N N   . ILE A 1164 ? 1.6316 3.0334 2.8400 -0.1207 -0.0182 -0.5172 1164 ILE A N   
8869  C CA  . ILE A 1164 ? 1.6079 3.0387 2.8341 -0.1167 -0.0220 -0.5492 1164 ILE A CA  
8870  C C   . ILE A 1164 ? 1.5931 3.0403 2.8355 -0.1622 -0.0146 -0.5424 1164 ILE A C   
8871  O O   . ILE A 1164 ? 1.5863 3.0312 2.8207 -0.1712 -0.0180 -0.5759 1164 ILE A O   
8872  C CB  . ILE A 1164 ? 1.3151 2.7354 2.5239 -0.0495 -0.0112 -0.5330 1164 ILE A CB  
8873  C CG1 . ILE A 1164 ? 1.2533 2.7121 2.4985 -0.0487 0.0070  -0.4916 1164 ILE A CG1 
8874  C CG2 . ILE A 1164 ? 1.3796 2.7495 2.5412 0.0020  -0.0055 -0.5137 1164 ILE A CG2 
8875  C CD1 . ILE A 1164 ? 1.2537 2.7134 2.4894 0.0004  0.0119  -0.4938 1164 ILE A CD1 
8876  N N   . ASP A 1165 ? 1.3264 2.7664 2.5674 -0.1860 -0.0018 -0.4982 1165 ASP A N   
8877  C CA  . ASP A 1165 ? 1.3469 2.7727 2.5706 -0.2303 0.0076  -0.4937 1165 ASP A CA  
8878  C C   . ASP A 1165 ? 1.3702 2.7750 2.5721 -0.2778 -0.0044 -0.5432 1165 ASP A C   
8879  O O   . ASP A 1165 ? 1.3566 2.7548 2.5458 -0.2976 -0.0019 -0.5751 1165 ASP A O   
8880  C CB  . ASP A 1165 ? 1.3899 2.8111 2.6123 -0.2487 0.0215  -0.4379 1165 ASP A CB  
8881  C CG  . ASP A 1165 ? 1.4084 2.8153 2.6090 -0.2935 0.0319  -0.4333 1165 ASP A CG  
8882  O OD1 . ASP A 1165 ? 1.3808 2.7844 2.5719 -0.3027 0.0316  -0.4708 1165 ASP A OD1 
8883  O OD2 . ASP A 1165 ? 1.4482 2.8486 2.6419 -0.3173 0.0405  -0.3932 1165 ASP A OD2 
8884  N N   . THR A 1166 ? 1.2840 2.6775 2.4803 -0.2945 -0.0157 -0.5487 1166 THR A N   
8885  C CA  . THR A 1166 ? 1.3222 2.6926 2.4907 -0.3335 -0.0271 -0.5986 1166 THR A CA  
8886  C C   . THR A 1166 ? 1.2936 2.6687 2.4575 -0.3223 -0.0321 -0.6538 1166 THR A C   
8887  O O   . THR A 1166 ? 1.3098 2.6797 2.4626 -0.3450 -0.0222 -0.6729 1166 THR A O   
8888  C CB  . THR A 1166 ? 1.3618 2.7245 2.5281 -0.3297 -0.0443 -0.6088 1166 THR A CB  
8889  O OG1 . THR A 1166 ? 1.4000 2.7553 2.5711 -0.3465 -0.0413 -0.5604 1166 THR A OG1 
8890  C CG2 . THR A 1166 ? 1.4061 2.7428 2.5353 -0.3625 -0.0553 -0.6693 1166 THR A CG2 
8891  N N   . ALA A 1167 ? 2.1918 3.5792 3.3660 -0.2852 -0.0470 -0.6788 1167 ALA A N   
8892  C CA  . ALA A 1167 ? 2.1365 3.5277 3.3051 -0.2742 -0.0555 -0.7354 1167 ALA A CA  
8893  C C   . ALA A 1167 ? 2.0404 3.4394 3.2177 -0.2751 -0.0423 -0.7353 1167 ALA A C   
8894  O O   . ALA A 1167 ? 2.0306 3.4260 3.1996 -0.2876 -0.0429 -0.7830 1167 ALA A O   
8895  C CB  . ALA A 1167 ? 2.1126 3.5244 3.2974 -0.2225 -0.0711 -0.7461 1167 ALA A CB  
8896  N N   . LEU A 1168 ? 0.9909 2.4003 2.1840 -0.2617 -0.0288 -0.6828 1168 LEU A N   
8897  C CA  . LEU A 1168 ? 0.9448 2.3598 2.1437 -0.2608 -0.0169 -0.6809 1168 LEU A CA  
8898  C C   . LEU A 1168 ? 1.0367 2.4356 2.2170 -0.3099 -0.0059 -0.7063 1168 LEU A C   
8899  O O   . LEU A 1168 ? 1.0489 2.4521 2.2341 -0.3110 -0.0016 -0.7341 1168 LEU A O   
8900  C CB  . LEU A 1168 ? 0.8582 2.2825 2.0677 -0.2418 -0.0015 -0.6180 1168 LEU A CB  
8901  C CG  . LEU A 1168 ? 0.8040 2.2450 2.0284 -0.1989 -0.0008 -0.6170 1168 LEU A CG  
8902  C CD1 . LEU A 1168 ? 0.7866 2.2362 2.0157 -0.1705 0.0153  -0.5552 1168 LEU A CD1 
8903  C CD2 . LEU A 1168 ? 0.7728 2.2096 1.9950 -0.2187 0.0025  -0.6498 1168 LEU A CD2 
8904  N N   . ILE A 1169 ? 0.9794 2.3616 2.1395 -0.3483 -0.0010 -0.6958 1169 ILE A N   
8905  C CA  . ILE A 1169 ? 0.9833 2.3522 2.1216 -0.3953 0.0120  -0.7148 1169 ILE A CA  
8906  C C   . ILE A 1169 ? 1.0189 2.3830 2.1449 -0.4081 0.0056  -0.7790 1169 ILE A C   
8907  O O   . ILE A 1169 ? 1.0159 2.3846 2.1414 -0.4220 0.0152  -0.8159 1169 ILE A O   
8908  C CB  . ILE A 1169 ? 0.9986 2.3527 2.1178 -0.4292 0.0183  -0.6743 1169 ILE A CB  
8909  C CG1 . ILE A 1169 ? 0.9459 2.3059 2.0727 -0.4242 0.0310  -0.6142 1169 ILE A CG1 
8910  C CG2 . ILE A 1169 ? 1.0493 2.3909 2.1408 -0.4766 0.0279  -0.7031 1169 ILE A CG2 
8911  C CD1 . ILE A 1169 ? 0.9386 2.2979 2.0715 -0.4151 0.0270  -0.5620 1169 ILE A CD1 
8912  N N   . LYS A 1170 ? 1.7098 3.0664 2.8266 -0.4023 -0.0092 -0.7929 1170 LYS A N   
8913  C CA  . LYS A 1170 ? 1.7759 3.1297 2.8789 -0.4082 -0.0150 -0.8545 1170 LYS A CA  
8914  C C   . LYS A 1170 ? 1.6981 3.0706 2.8226 -0.3845 -0.0149 -0.8927 1170 LYS A C   
8915  O O   . LYS A 1170 ? 1.6976 3.0752 2.8181 -0.3971 -0.0092 -0.9431 1170 LYS A O   
8916  C CB  . LYS A 1170 ? 1.8705 3.2182 2.9663 -0.3863 -0.0352 -0.8648 1170 LYS A CB  
8917  C CG  . LYS A 1170 ? 2.0004 3.3272 3.0757 -0.4094 -0.0385 -0.8340 1170 LYS A CG  
8918  C CD  . LYS A 1170 ? 2.1469 3.4564 3.1892 -0.4590 -0.0263 -0.8538 1170 LYS A CD  
8919  C CE  . LYS A 1170 ? 2.2472 3.5569 3.2713 -0.4614 -0.0273 -0.9188 1170 LYS A CE  
8920  N NZ  . LYS A 1170 ? 2.3256 3.6263 3.3203 -0.5095 -0.0113 -0.9375 1170 LYS A NZ  
8921  N N   . ALA A 1171 ? 1.2597 2.6450 2.4090 -0.3494 -0.0205 -0.8668 1171 ALA A N   
8922  C CA  . ALA A 1171 ? 1.2475 2.6494 2.4191 -0.3221 -0.0250 -0.8982 1171 ALA A CA  
8923  C C   . ALA A 1171 ? 1.2473 2.6527 2.4269 -0.3439 -0.0059 -0.9022 1171 ALA A C   
8924  O O   . ALA A 1171 ? 1.2610 2.6743 2.4479 -0.3507 -0.0019 -0.9515 1171 ALA A O   
8925  C CB  . ALA A 1171 ? 1.2196 2.6346 2.4116 -0.2758 -0.0378 -0.8668 1171 ALA A CB  
8926  N N   . ASP A 1172 ? 1.5444 2.9459 2.7236 -0.3538 0.0068  -0.8506 1172 ASP A N   
8927  C CA  . ASP A 1172 ? 1.5510 2.9541 2.7332 -0.3765 0.0258  -0.8512 1172 ASP A CA  
8928  C C   . ASP A 1172 ? 1.5994 2.9998 2.7667 -0.4174 0.0388  -0.8928 1172 ASP A C   
8929  O O   . ASP A 1172 ? 1.5850 2.9952 2.7641 -0.4271 0.0496  -0.9265 1172 ASP A O   
8930  C CB  . ASP A 1172 ? 1.5699 2.9667 2.7440 -0.3864 0.0388  -0.7866 1172 ASP A CB  
8931  C CG  . ASP A 1172 ? 1.5542 2.9611 2.7475 -0.3459 0.0344  -0.7519 1172 ASP A CG  
8932  O OD1 . ASP A 1172 ? 1.5316 2.9491 2.7420 -0.3082 0.0175  -0.7700 1172 ASP A OD1 
8933  O OD2 . ASP A 1172 ? 1.5701 2.9752 2.7586 -0.3510 0.0484  -0.7062 1172 ASP A OD2 
8934  N N   . ASN A 1173 ? 1.8148 3.2039 2.9575 -0.4404 0.0380  -0.8916 1173 ASN A N   
8935  C CA  . ASN A 1173 ? 1.8877 3.2767 3.0124 -0.4799 0.0516  -0.9280 1173 ASN A CA  
8936  C C   . ASN A 1173 ? 1.8632 3.2700 3.0051 -0.4704 0.0510  -0.9942 1173 ASN A C   
8937  O O   . ASN A 1173 ? 1.8763 3.2960 3.0266 -0.4900 0.0675  -1.0234 1173 ASN A O   
8938  C CB  . ASN A 1173 ? 2.0017 3.3746 3.0963 -0.5013 0.0468  -0.9172 1173 ASN A CB  
8939  C CG  . ASN A 1173 ? 2.1019 3.4604 3.1746 -0.5328 0.0559  -0.8638 1173 ASN A CG  
8940  O OD1 . ASN A 1173 ? 2.1941 3.5442 3.2391 -0.5716 0.0638  -0.8667 1173 ASN A OD1 
8941  N ND2 . ASN A 1173 ? 2.0760 3.4335 3.1601 -0.5163 0.0551  -0.8138 1173 ASN A ND2 
8942  N N   . PHE A 1174 ? 1.6627 3.0721 2.8101 -0.4403 0.0322  -1.0183 1174 PHE A N   
8943  C CA  . PHE A 1174 ? 1.6479 3.0775 2.8153 -0.4244 0.0287  -1.0800 1174 PHE A CA  
8944  C C   . PHE A 1174 ? 1.5847 3.0289 2.7833 -0.4171 0.0367  -1.0902 1174 PHE A C   
8945  O O   . PHE A 1174 ? 1.6146 3.0776 2.8295 -0.4293 0.0487  -1.1358 1174 PHE A O   
8946  C CB  . PHE A 1174 ? 1.6233 3.0540 2.7963 -0.3806 0.0028  -1.0915 1174 PHE A CB  
8947  C CG  . PHE A 1174 ? 1.5996 3.0532 2.7967 -0.3563 -0.0050 -1.1516 1174 PHE A CG  
8948  C CD1 . PHE A 1174 ? 1.6406 3.1035 2.8274 -0.3621 -0.0049 -1.1966 1174 PHE A CD1 
8949  C CD2 . PHE A 1174 ? 1.5524 3.0191 2.7826 -0.3262 -0.0138 -1.1609 1174 PHE A CD2 
8950  C CE1 . PHE A 1174 ? 1.6453 3.1333 2.8571 -0.3379 -0.0126 -1.2500 1174 PHE A CE1 
8951  C CE2 . PHE A 1174 ? 1.5525 3.0410 2.8071 -0.3022 -0.0238 -1.2148 1174 PHE A CE2 
8952  C CZ  . PHE A 1174 ? 1.5992 3.0997 2.8457 -0.3075 -0.0231 -1.2592 1174 PHE A CZ  
8953  N N   . LEU A 1175 ? 1.5960 3.0331 2.8034 -0.3990 0.0318  -1.0463 1175 LEU A N   
8954  C CA  . LEU A 1175 ? 1.5605 3.0090 2.7976 -0.3863 0.0356  -1.0550 1175 LEU A CA  
8955  C C   . LEU A 1175 ? 1.5755 3.0300 2.8141 -0.4248 0.0616  -1.0681 1175 LEU A C   
8956  O O   . LEU A 1175 ? 1.5672 3.0404 2.8317 -0.4249 0.0672  -1.1164 1175 LEU A O   
8957  C CB  . LEU A 1175 ? 1.5223 2.9634 2.7652 -0.3602 0.0270  -1.0024 1175 LEU A CB  
8958  C CG  . LEU A 1175 ? 1.4938 2.9422 2.7533 -0.3117 0.0004  -1.0107 1175 LEU A CG  
8959  C CD1 . LEU A 1175 ? 1.4474 2.8949 2.7156 -0.2874 -0.0032 -0.9604 1175 LEU A CD1 
8960  C CD2 . LEU A 1175 ? 1.4958 2.9616 2.7827 -0.2947 -0.0088 -1.0726 1175 LEU A CD2 
8961  N N   . LEU A 1176 ? 1.3355 2.7765 2.5475 -0.4571 0.0770  -1.0265 1176 LEU A N   
8962  C CA  . LEU A 1176 ? 1.3708 2.8185 2.5775 -0.4968 0.1018  -1.0399 1176 LEU A CA  
8963  C C   . LEU A 1176 ? 1.4798 2.9452 2.6895 -0.5159 0.1097  -1.0996 1176 LEU A C   
8964  O O   . LEU A 1176 ? 1.5070 2.9940 2.7448 -0.5181 0.1193  -1.1456 1176 LEU A O   
8965  C CB  . LEU A 1176 ? 1.3397 2.7700 2.5088 -0.5298 0.1126  -0.9882 1176 LEU A CB  
8966  C CG  . LEU A 1176 ? 1.2503 2.6661 2.4167 -0.5045 0.1009  -0.9284 1176 LEU A CG  
8967  C CD1 . LEU A 1176 ? 1.2656 2.6653 2.3976 -0.5300 0.1044  -0.8793 1176 LEU A CD1 
8968  C CD2 . LEU A 1176 ? 1.2130 2.6329 2.3964 -0.4956 0.1095  -0.9139 1176 LEU A CD2 
8969  N N   . GLU A 1177 ? 1.8426 3.3002 3.0249 -0.5285 0.1054  -1.0981 1177 GLU A N   
8970  C CA  . GLU A 1177 ? 1.9316 3.4050 3.1072 -0.5525 0.1150  -1.1465 1177 GLU A CA  
8971  C C   . GLU A 1177 ? 1.9250 3.4247 3.1372 -0.5255 0.1080  -1.2073 1177 GLU A C   
8972  O O   . GLU A 1177 ? 1.9937 3.5104 3.2029 -0.5408 0.1149  -1.2488 1177 GLU A O   
8973  C CB  . GLU A 1177 ? 2.0267 3.4820 3.1641 -0.5662 0.1076  -1.1277 1177 GLU A CB  
8974  C CG  . GLU A 1177 ? 2.1335 3.5733 3.2311 -0.6130 0.1217  -1.0917 1177 GLU A CG  
8975  C CD  . GLU A 1177 ? 2.2555 3.6824 3.3177 -0.6339 0.1171  -1.0907 1177 GLU A CD  
8976  O OE1 . GLU A 1177 ? 2.3381 3.7640 3.3709 -0.6787 0.1322  -1.0908 1177 GLU A OE1 
8977  O OE2 . GLU A 1177 ? 2.2680 3.6853 3.3296 -0.6064 0.0980  -1.0903 1177 GLU A OE2 
8978  N N   . ASN A 1178 ? 1.5453 3.0501 2.7914 -0.4863 0.0941  -1.2126 1178 ASN A N   
8979  C CA  . ASN A 1178 ? 1.5045 3.0351 2.7869 -0.4576 0.0834  -1.2689 1178 ASN A CA  
8980  C C   . ASN A 1178 ? 1.4350 2.9771 2.7615 -0.4288 0.0764  -1.2837 1178 ASN A C   
8981  O O   . ASN A 1178 ? 1.4319 2.9946 2.7906 -0.4003 0.0629  -1.3274 1178 ASN A O   
8982  C CB  . ASN A 1178 ? 1.4777 3.0018 2.7491 -0.4262 0.0589  -1.2712 1178 ASN A CB  
8983  C CG  . ASN A 1178 ? 1.5064 3.0452 2.7639 -0.4435 0.0648  -1.3105 1178 ASN A CG  
8984  O OD1 . ASN A 1178 ? 1.5128 3.0821 2.7983 -0.4343 0.0652  -1.3645 1178 ASN A OD1 
8985  N ND2 . ASN A 1178 ? 1.5325 3.0504 2.7474 -0.4676 0.0682  -1.2822 1178 ASN A ND2 
8986  N N   . THR A 1179 ? 1.4498 2.9795 2.7780 -0.4353 0.0843  -1.2483 1179 THR A N   
8987  C CA  . THR A 1179 ? 1.3883 2.9262 2.7570 -0.4076 0.0760  -1.2604 1179 THR A CA  
8988  C C   . THR A 1179 ? 1.3785 2.9402 2.7805 -0.4269 0.0957  -1.3035 1179 THR A C   
8989  O O   . THR A 1179 ? 1.3490 2.9296 2.7948 -0.4027 0.0860  -1.3432 1179 THR A O   
8990  C CB  . THR A 1179 ? 1.1760 2.6913 2.5350 -0.4010 0.0745  -1.2016 1179 THR A CB  
8991  O OG1 . THR A 1179 ? 1.1721 2.6667 2.4998 -0.3888 0.0609  -1.1538 1179 THR A OG1 
8992  C CG2 . THR A 1179 ? 1.0390 2.5609 2.4376 -0.3658 0.0594  -1.2128 1179 THR A CG2 
8993  N N   . LEU A 1180 ? 2.3797 3.9406 3.7611 -0.4706 0.1226  -1.2946 1180 LEU A N   
8994  C CA  . LEU A 1180 ? 2.3922 3.9656 3.7990 -0.4882 0.1421  -1.3118 1180 LEU A CA  
8995  C C   . LEU A 1180 ? 2.4841 4.0940 3.9395 -0.4880 0.1489  -1.3818 1180 LEU A C   
8996  O O   . LEU A 1180 ? 2.4862 4.1052 3.9798 -0.4790 0.1511  -1.3990 1180 LEU A O   
8997  C CB  . LEU A 1180 ? 2.3680 3.9291 3.7364 -0.5332 0.1675  -1.2773 1180 LEU A CB  
8998  C CG  . LEU A 1180 ? 2.2771 3.8115 3.6327 -0.5207 0.1620  -1.2174 1180 LEU A CG  
8999  C CD1 . LEU A 1180 ? 2.2800 3.8035 3.6008 -0.5610 0.1853  -1.1813 1180 LEU A CD1 
9000  C CD2 . LEU A 1180 ? 2.2293 3.7712 3.6319 -0.4903 0.1532  -1.2356 1180 LEU A CD2 
9001  N N   . PRO A 1181 ? 1.6500 3.2827 3.1062 -0.4983 0.1526  -1.4228 1181 PRO A N   
9002  C CA  . PRO A 1181 ? 1.6474 3.3184 3.1596 -0.4865 0.1526  -1.4899 1181 PRO A CA  
9003  C C   . PRO A 1181 ? 1.5995 3.2677 3.1463 -0.4339 0.1207  -1.4953 1181 PRO A C   
9004  O O   . PRO A 1181 ? 1.5873 3.2679 3.1444 -0.4072 0.1008  -1.5206 1181 PRO A O   
9005  C CB  . PRO A 1181 ? 1.6623 3.3559 3.1636 -0.4994 0.1565  -1.5242 1181 PRO A CB  
9006  C CG  . PRO A 1181 ? 1.6876 3.3588 3.1286 -0.5390 0.1728  -1.4826 1181 PRO A CG  
9007  C CD  . PRO A 1181 ? 1.6627 3.2924 3.0746 -0.5272 0.1617  -1.4153 1181 PRO A CD  
9008  N N   . ALA A 1182 ? 1.5925 3.2446 3.1544 -0.4203 0.1156  -1.4708 1182 ALA A N   
9009  C CA  . ALA A 1182 ? 1.5290 3.1700 3.1114 -0.3729 0.0837  -1.4602 1182 ALA A CA  
9010  C C   . ALA A 1182 ? 1.5666 3.2383 3.1989 -0.3408 0.0631  -1.5206 1182 ALA A C   
9011  O O   . ALA A 1182 ? 1.6075 3.3093 3.2847 -0.3496 0.0742  -1.5705 1182 ALA A O   
9012  C CB  . ALA A 1182 ? 1.4494 3.0743 3.0449 -0.3706 0.0869  -1.4313 1182 ALA A CB  
9013  N N   . GLN A 1183 ? 1.3770 3.0423 3.0008 -0.3036 0.0328  -1.5156 1183 GLN A N   
9014  C CA  . GLN A 1183 ? 1.3478 3.0392 3.0126 -0.2669 0.0069  -1.5668 1183 GLN A CA  
9015  C C   . GLN A 1183 ? 1.2628 2.9464 2.9610 -0.2286 -0.0209 -1.5638 1183 GLN A C   
9016  O O   . GLN A 1183 ? 1.2773 2.9866 3.0277 -0.2097 -0.0335 -1.6131 1183 GLN A O   
9017  C CB  . GLN A 1183 ? 1.3851 3.0743 3.0179 -0.2473 -0.0118 -1.5643 1183 GLN A CB  
9018  C CG  . GLN A 1183 ? 1.4480 3.1703 3.1176 -0.2164 -0.0338 -1.6221 1183 GLN A CG  
9019  C CD  . GLN A 1183 ? 1.5122 3.2767 3.2151 -0.2436 -0.0101 -1.6789 1183 GLN A CD  
9020  O OE1 . GLN A 1183 ? 1.5294 3.2959 3.2208 -0.2867 0.0226  -1.6733 1183 GLN A OE1 
9021  N NE2 . GLN A 1183 ? 1.5403 3.3407 3.2833 -0.2192 -0.0268 -1.7338 1183 GLN A NE2 
9022  N N   . SER A 1184 ? 1.1617 2.8116 2.8306 -0.2179 -0.0307 -1.5054 1184 SER A N   
9023  C CA  . SER A 1184 ? 1.1171 2.7568 2.8111 -0.1873 -0.0540 -1.4922 1184 SER A CA  
9024  C C   . SER A 1184 ? 1.0657 2.6744 2.7304 -0.1955 -0.0463 -1.4241 1184 SER A C   
9025  O O   . SER A 1184 ? 1.0434 2.6335 2.6607 -0.2106 -0.0354 -1.3786 1184 SER A O   
9026  C CB  . SER A 1184 ? 1.1351 2.7773 2.8334 -0.1386 -0.0955 -1.5048 1184 SER A CB  
9027  O OG  . SER A 1184 ? 1.1144 2.7437 2.8279 -0.1111 -0.1183 -1.4819 1184 SER A OG  
9028  N N   . THR A 1185 ? 0.6972 2.3027 2.3927 -0.1847 -0.0525 -1.4181 1185 THR A N   
9029  C CA  . THR A 1185 ? 0.6513 2.2334 2.3259 -0.1915 -0.0435 -1.3566 1185 THR A CA  
9030  C C   . THR A 1185 ? 0.6242 2.1895 2.2585 -0.1668 -0.0631 -1.3054 1185 THR A C   
9031  O O   . THR A 1185 ? 0.5750 2.1228 2.1712 -0.1820 -0.0475 -1.2491 1185 THR A O   
9032  C CB  . THR A 1185 ? 0.6336 2.2182 2.3524 -0.1736 -0.0555 -1.3628 1185 THR A CB  
9033  O OG1 . THR A 1185 ? 0.6436 2.2440 2.4034 -0.1976 -0.0347 -1.4069 1185 THR A OG1 
9034  C CG2 . THR A 1185 ? 0.5962 2.1596 2.2907 -0.1755 -0.0478 -1.2957 1185 THR A CG2 
9035  N N   . PHE A 1186 ? 1.4145 2.9875 3.0589 -0.1268 -0.0983 -1.3262 1186 PHE A N   
9036  C CA  . PHE A 1186 ? 1.3912 2.9542 3.0006 -0.0983 -0.1200 -1.2863 1186 PHE A CA  
9037  C C   . PHE A 1186 ? 1.4190 2.9734 2.9849 -0.1227 -0.1016 -1.2675 1186 PHE A C   
9038  O O   . PHE A 1186 ? 1.4186 2.9583 2.9516 -0.1293 -0.0919 -1.2107 1186 PHE A O   
9039  C CB  . PHE A 1186 ? 1.3633 2.9388 2.9890 -0.0542 -0.1601 -1.3242 1186 PHE A CB  
9040  C CG  . PHE A 1186 ? 1.3239 2.8930 2.9139 -0.0214 -0.1839 -1.2888 1186 PHE A CG  
9041  C CD1 . PHE A 1186 ? 1.2970 2.8609 2.8809 0.0053  -0.1964 -1.2390 1186 PHE A CD1 
9042  C CD2 . PHE A 1186 ? 1.3303 2.9014 2.8935 -0.0154 -0.1921 -1.3059 1186 PHE A CD2 
9043  C CE1 . PHE A 1186 ? 1.2790 2.8420 2.8325 0.0384  -0.2153 -1.2063 1186 PHE A CE1 
9044  C CE2 . PHE A 1186 ? 1.3202 2.8871 2.8516 0.0156  -0.2130 -1.2749 1186 PHE A CE2 
9045  C CZ  . PHE A 1186 ? 1.2947 2.8588 2.8226 0.0434  -0.2243 -1.2248 1186 PHE A CZ  
9046  N N   . THR A 1187 ? 0.7304 2.2963 2.2984 -0.1376 -0.0947 -1.3139 1187 THR A N   
9047  C CA  . THR A 1187 ? 0.7101 2.2686 2.2376 -0.1605 -0.0794 -1.2993 1187 THR A CA  
9048  C C   . THR A 1187 ? 0.6816 2.2222 2.1822 -0.1948 -0.0508 -1.2457 1187 THR A C   
9049  O O   . THR A 1187 ? 0.6621 2.1875 2.1269 -0.1950 -0.0502 -1.1966 1187 THR A O   
9050  C CB  . THR A 1187 ? 0.7266 2.3033 2.2645 -0.1863 -0.0621 -1.3526 1187 THR A CB  
9051  O OG1 . THR A 1187 ? 0.7296 2.3303 2.3061 -0.1606 -0.0818 -1.4117 1187 THR A OG1 
9052  C CG2 . THR A 1187 ? 0.7361 2.3059 2.2311 -0.2003 -0.0556 -1.3406 1187 THR A CG2 
9053  N N   . LEU A 1188 ? 0.9963 2.5408 2.5159 -0.2237 -0.0268 -1.2579 1188 LEU A N   
9054  C CA  . LEU A 1188 ? 0.9874 2.5176 2.4827 -0.2606 0.0030  -1.2162 1188 LEU A CA  
9055  C C   . LEU A 1188 ? 0.9496 2.4621 2.4214 -0.2465 -0.0023 -1.1498 1188 LEU A C   
9056  O O   . LEU A 1188 ? 0.9451 2.4440 2.3801 -0.2624 0.0090  -1.1055 1188 LEU A O   
9057  C CB  . LEU A 1188 ? 0.9956 2.5343 2.5240 -0.2783 0.0206  -1.2391 1188 LEU A CB  
9058  C CG  . LEU A 1188 ? 0.9603 2.4949 2.4681 -0.3261 0.0558  -1.2285 1188 LEU A CG  
9059  C CD1 . LEU A 1188 ? 0.9634 2.5010 2.4429 -0.3466 0.0633  -1.2405 1188 LEU A CD1 
9060  C CD2 . LEU A 1188 ? 0.9523 2.5045 2.5014 -0.3410 0.0710  -1.2739 1188 LEU A CD2 
9061  N N   . ALA A 1189 ? 0.7847 2.3006 2.2806 -0.2141 -0.0210 -1.1449 1189 ALA A N   
9062  C CA  . ALA A 1189 ? 0.7936 2.2994 2.2777 -0.2019 -0.0199 -1.0853 1189 ALA A CA  
9063  C C   . ALA A 1189 ? 0.7602 2.2586 2.2094 -0.1857 -0.0276 -1.0356 1189 ALA A C   
9064  O O   . ALA A 1189 ? 0.7226 2.2117 2.1495 -0.1912 -0.0130 -0.9789 1189 ALA A O   
9065  C CB  . ALA A 1189 ? 0.7867 2.3014 2.3062 -0.1677 -0.0412 -1.0970 1189 ALA A CB  
9066  N N   . ILE A 1190 ? 1.1743 2.6783 2.6191 -0.1640 -0.0496 -1.0570 1190 ILE A N   
9067  C CA  . ILE A 1190 ? 1.1804 2.6796 2.5950 -0.1485 -0.0559 -1.0140 1190 ILE A CA  
9068  C C   . ILE A 1190 ? 1.1909 2.6781 2.5763 -0.1884 -0.0330 -0.9982 1190 ILE A C   
9069  O O   . ILE A 1190 ? 1.1706 2.6492 2.5319 -0.1933 -0.0220 -0.9438 1190 ILE A O   
9070  C CB  . ILE A 1190 ? 1.1708 2.6801 2.5875 -0.1097 -0.0879 -1.0404 1190 ILE A CB  
9071  C CG1 . ILE A 1190 ? 1.1623 2.6832 2.6045 -0.0674 -0.1125 -1.0483 1190 ILE A CG1 
9072  C CG2 . ILE A 1190 ? 1.1581 2.6640 2.5455 -0.0952 -0.0907 -0.9963 1190 ILE A CG2 
9073  C CD1 . ILE A 1190 ? 1.1754 2.7064 2.6154 -0.0248 -0.1454 -1.0690 1190 ILE A CD1 
9074  N N   . SER A 1191 ? 0.8526 2.3411 2.2409 -0.2164 -0.0247 -1.0450 1191 SER A N   
9075  C CA  . SER A 1191 ? 0.8439 2.3218 2.2034 -0.2553 -0.0038 -1.0324 1191 SER A CA  
9076  C C   . SER A 1191 ? 0.8168 2.2838 2.1625 -0.2817 0.0210  -0.9849 1191 SER A C   
9077  O O   . SER A 1191 ? 0.8003 2.2560 2.1166 -0.3046 0.0342  -0.9481 1191 SER A O   
9078  C CB  . SER A 1191 ? 0.8719 2.3582 2.2395 -0.2809 0.0057  -1.0908 1191 SER A CB  
9079  O OG  . SER A 1191 ? 0.8967 2.3738 2.2322 -0.3127 0.0199  -1.0778 1191 SER A OG  
9080  N N   . ALA A 1192 ? 0.5326 2.0034 1.9000 -0.2775 0.0260  -0.9869 1192 ALA A N   
9081  C CA  . ALA A 1192 ? 0.5066 1.9684 1.8619 -0.2973 0.0483  -0.9431 1192 ALA A CA  
9082  C C   . ALA A 1192 ? 0.5337 1.9897 1.8701 -0.2758 0.0451  -0.8796 1192 ALA A C   
9083  O O   . ALA A 1192 ? 0.5625 2.0086 1.8692 -0.2933 0.0584  -0.8357 1192 ALA A O   
9084  C CB  . ALA A 1192 ? 0.4644 1.9331 1.8516 -0.2914 0.0507  -0.9648 1192 ALA A CB  
9085  N N   . TYR A 1193 ? 0.7710 2.2356 2.1260 -0.2360 0.0275  -0.8753 1193 TYR A N   
9086  C CA  . TYR A 1193 ? 0.7445 2.2087 2.0851 -0.2109 0.0278  -0.8170 1193 TYR A CA  
9087  C C   . TYR A 1193 ? 0.7486 2.2087 2.0636 -0.2098 0.0272  -0.7857 1193 TYR A C   
9088  O O   . TYR A 1193 ? 0.7671 2.2236 2.0623 -0.2053 0.0393  -0.7305 1193 TYR A O   
9089  C CB  . TYR A 1193 ? 0.7263 2.2033 2.0897 -0.1640 0.0060  -0.8232 1193 TYR A CB  
9090  C CG  . TYR A 1193 ? 0.7035 2.1826 2.0487 -0.1331 0.0090  -0.7634 1193 TYR A CG  
9091  C CD1 . TYR A 1193 ? 0.7195 2.1929 2.0497 -0.1402 0.0312  -0.7172 1193 TYR A CD1 
9092  C CD2 . TYR A 1193 ? 0.6742 2.1611 2.0137 -0.0962 -0.0076 -0.7528 1193 TYR A CD2 
9093  C CE1 . TYR A 1193 ? 0.7111 2.1869 2.0210 -0.1103 0.0376  -0.6631 1193 TYR A CE1 
9094  C CE2 . TYR A 1193 ? 0.6679 2.1570 1.9889 -0.0649 -0.0004 -0.6986 1193 TYR A CE2 
9095  C CZ  . TYR A 1193 ? 0.6737 2.1573 1.9797 -0.0721 0.0227  -0.6547 1193 TYR A CZ  
9096  O OH  . TYR A 1193 ? 0.6394 2.1245 1.9235 -0.0395 0.0322  -0.6037 1193 TYR A OH  
9097  N N   . ALA A 1194 ? 1.2923 2.7530 2.6073 -0.2153 0.0151  -0.8210 1194 ALA A N   
9098  C CA  . ALA A 1194 ? 1.2792 2.7366 2.5741 -0.2123 0.0116  -0.7965 1194 ALA A CA  
9099  C C   . ALA A 1194 ? 1.2638 2.7074 2.5326 -0.2539 0.0322  -0.7685 1194 ALA A C   
9100  O O   . ALA A 1194 ? 1.2527 2.6933 2.5056 -0.2492 0.0365  -0.7218 1194 ALA A O   
9101  C CB  . ALA A 1194 ? 1.3017 2.7646 2.6038 -0.2008 -0.0103 -0.8453 1194 ALA A CB  
9102  N N   . LEU A 1195 ? 0.8411 2.2782 2.1063 -0.2927 0.0449  -0.7977 1195 LEU A N   
9103  C CA  . LEU A 1195 ? 0.8454 2.2705 2.0841 -0.3317 0.0650  -0.7681 1195 LEU A CA  
9104  C C   . LEU A 1195 ? 0.8502 2.2733 2.0804 -0.3258 0.0785  -0.7128 1195 LEU A C   
9105  O O   . LEU A 1195 ? 0.8743 2.2909 2.0827 -0.3355 0.0877  -0.6649 1195 LEU A O   
9106  C CB  . LEU A 1195 ? 0.8383 2.2619 2.0767 -0.3689 0.0782  -0.8103 1195 LEU A CB  
9107  C CG  . LEU A 1195 ? 0.8672 2.2981 2.1202 -0.3606 0.0625  -0.8688 1195 LEU A CG  
9108  C CD1 . LEU A 1195 ? 0.8916 2.3295 2.1555 -0.3864 0.0737  -0.9236 1195 LEU A CD1 
9109  C CD2 . LEU A 1195 ? 0.8830 2.3071 2.1152 -0.3668 0.0550  -0.8600 1195 LEU A CD2 
9110  N N   . SER A 1196 ? 0.1212 1.5504 1.3690 -0.3080 0.0788  -0.7198 1196 SER A N   
9111  C CA  . SER A 1196 ? 0.1359 1.5643 1.3752 -0.2977 0.0917  -0.6709 1196 SER A CA  
9112  C C   . SER A 1196 ? 0.1669 1.5969 1.3910 -0.2732 0.0920  -0.6140 1196 SER A C   
9113  O O   . SER A 1196 ? 0.1396 1.5657 1.3436 -0.2769 0.1083  -0.5652 1196 SER A O   
9114  C CB  . SER A 1196 ? 0.1169 1.5539 1.3819 -0.2716 0.0851  -0.6906 1196 SER A CB  
9115  O OG  . SER A 1196 ? 0.1225 1.5570 1.3757 -0.2685 0.1010  -0.6484 1196 SER A OG  
9116  N N   . LEU A 1197 ? 1.2651 2.7019 2.4979 -0.2471 0.0747  -0.6213 1197 LEU A N   
9117  C CA  . LEU A 1197 ? 1.3738 2.8147 2.5960 -0.2196 0.0763  -0.5713 1197 LEU A CA  
9118  C C   . LEU A 1197 ? 1.4601 2.8933 2.6665 -0.2440 0.0802  -0.5519 1197 LEU A C   
9119  O O   . LEU A 1197 ? 1.4584 2.8962 2.6641 -0.2217 0.0754  -0.5277 1197 LEU A O   
9120  C CB  . LEU A 1197 ? 1.3984 2.8528 2.6376 -0.1703 0.0572  -0.5834 1197 LEU A CB  
9121  C CG  . LEU A 1197 ? 1.4254 2.8878 2.6795 -0.1427 0.0514  -0.5978 1197 LEU A CG  
9122  C CD1 . LEU A 1197 ? 1.4477 2.9227 2.7176 -0.0964 0.0278  -0.6213 1197 LEU A CD1 
9123  C CD2 . LEU A 1197 ? 1.4259 2.8876 2.6641 -0.1301 0.0708  -0.5477 1197 LEU A CD2 
9124  N N   . GLY A 1198 ? 1.6723 3.0941 2.8658 -0.2890 0.0899  -0.5617 1198 GLY A N   
9125  C CA  . GLY A 1198 ? 1.7646 3.1778 2.9415 -0.3164 0.0928  -0.5446 1198 GLY A CA  
9126  C C   . GLY A 1198 ? 1.8238 3.2267 2.9776 -0.3591 0.1103  -0.5288 1198 GLY A C   
9127  O O   . GLY A 1198 ? 1.8541 3.2569 2.9971 -0.3588 0.1244  -0.4962 1198 GLY A O   
9128  N N   . ASP A 1199 ? 2.0353 3.4299 3.1780 -0.3952 0.1095  -0.5510 1199 ASP A N   
9129  C CA  . ASP A 1199 ? 2.0196 3.4067 3.1387 -0.4376 0.1248  -0.5444 1199 ASP A CA  
9130  C C   . ASP A 1199 ? 1.9098 3.2993 3.0354 -0.4487 0.1333  -0.5841 1199 ASP A C   
9131  O O   . ASP A 1199 ? 1.9131 3.3035 3.0461 -0.4642 0.1311  -0.6365 1199 ASP A O   
9132  C CB  . ASP A 1199 ? 2.1203 3.4995 3.2235 -0.4726 0.1219  -0.5577 1199 ASP A CB  
9133  C CG  . ASP A 1199 ? 2.2183 3.5933 3.2955 -0.5153 0.1374  -0.5518 1199 ASP A CG  
9134  O OD1 . ASP A 1199 ? 2.2093 3.5870 3.2811 -0.5156 0.1498  -0.5335 1199 ASP A OD1 
9135  O OD2 . ASP A 1199 ? 2.2999 3.6697 3.3602 -0.5483 0.1372  -0.5652 1199 ASP A OD2 
9136  N N   . LYS A 1200 ? 1.4351 2.8264 2.5578 -0.4404 0.1443  -0.5582 1200 LYS A N   
9137  C CA  . LYS A 1200 ? 1.3754 2.7698 2.5093 -0.4444 0.1520  -0.5905 1200 LYS A CA  
9138  C C   . LYS A 1200 ? 1.4540 2.8451 2.5679 -0.4887 0.1674  -0.6025 1200 LYS A C   
9139  O O   . LYS A 1200 ? 1.5153 2.9090 2.6340 -0.4976 0.1784  -0.6212 1200 LYS A O   
9140  C CB  . LYS A 1200 ? 1.2975 2.6940 2.4312 -0.4195 0.1584  -0.5531 1200 LYS A CB  
9141  C CG  . LYS A 1200 ? 1.3135 2.7099 2.4322 -0.4008 0.1581  -0.4937 1200 LYS A CG  
9142  C CD  . LYS A 1200 ? 1.3297 2.7326 2.4577 -0.3605 0.1579  -0.4714 1200 LYS A CD  
9143  C CE  . LYS A 1200 ? 1.3607 2.7616 2.4810 -0.3687 0.1722  -0.4678 1200 LYS A CE  
9144  N NZ  . LYS A 1200 ? 1.3479 2.7546 2.4727 -0.3303 0.1731  -0.4439 1200 LYS A NZ  
9145  N N   . THR A 1201 ? 1.9526 3.3393 3.0441 -0.5167 0.1682  -0.5917 1201 THR A N   
9146  C CA  . THR A 1201 ? 1.9526 3.3386 3.0191 -0.5601 0.1832  -0.5959 1201 THR A CA  
9147  C C   . THR A 1201 ? 2.0048 3.3921 3.0653 -0.5918 0.1833  -0.6392 1201 THR A C   
9148  O O   . THR A 1201 ? 2.0443 3.4339 3.0829 -0.6293 0.1963  -0.6455 1201 THR A O   
9149  C CB  . THR A 1201 ? 1.9411 3.3231 2.9762 -0.5746 0.1883  -0.5361 1201 THR A CB  
9150  O OG1 . THR A 1201 ? 1.9284 3.3062 2.9622 -0.5632 0.1750  -0.5085 1201 THR A OG1 
9151  C CG2 . THR A 1201 ? 1.8944 3.2777 2.9261 -0.5551 0.1962  -0.4976 1201 THR A CG2 
9152  N N   . HIS A 1202 ? 1.3902 2.7774 2.4674 -0.5776 0.1695  -0.6689 1202 HIS A N   
9153  C CA  . HIS A 1202 ? 1.4713 2.8615 2.5429 -0.6059 0.1710  -0.7152 1202 HIS A CA  
9154  C C   . HIS A 1202 ? 1.5251 2.9270 2.6064 -0.6239 0.1871  -0.7620 1202 HIS A C   
9155  O O   . HIS A 1202 ? 1.4974 2.9067 2.6105 -0.6005 0.1856  -0.7947 1202 HIS A O   
9156  C CB  . HIS A 1202 ? 1.4422 2.8331 2.5337 -0.5829 0.1541  -0.7483 1202 HIS A CB  
9157  C CG  . HIS A 1202 ? 1.5098 2.9014 2.5861 -0.6131 0.1550  -0.7820 1202 HIS A CG  
9158  N ND1 . HIS A 1202 ? 1.5470 2.9287 2.6096 -0.6147 0.1419  -0.7681 1202 HIS A ND1 
9159  C CD2 . HIS A 1202 ? 1.5455 2.9475 2.6167 -0.6445 0.1689  -0.8277 1202 HIS A CD2 
9160  C CE1 . HIS A 1202 ? 1.5814 2.9657 2.6287 -0.6460 0.1471  -0.8037 1202 HIS A CE1 
9161  N NE2 . HIS A 1202 ? 1.5955 2.9937 2.6478 -0.6644 0.1641  -0.8403 1202 HIS A NE2 
9162  N N   . PRO A 1203 ? 1.2450 2.6503 2.3002 -0.6660 0.2021  -0.7659 1203 PRO A N   
9163  C CA  . PRO A 1203 ? 1.2658 2.6856 2.3310 -0.6865 0.2197  -0.8133 1203 PRO A CA  
9164  C C   . PRO A 1203 ? 1.2156 2.6451 2.3222 -0.6598 0.2132  -0.8679 1203 PRO A C   
9165  O O   . PRO A 1203 ? 1.2033 2.6396 2.3387 -0.6427 0.2171  -0.8876 1203 PRO A O   
9166  C CB  . PRO A 1203 ? 1.3587 2.7834 2.3945 -0.7313 0.2285  -0.8294 1203 PRO A CB  
9167  C CG  . PRO A 1203 ? 1.3712 2.7813 2.3722 -0.7416 0.2202  -0.7683 1203 PRO A CG  
9168  C CD  . PRO A 1203 ? 1.2962 2.6946 2.3145 -0.6976 0.2014  -0.7364 1203 PRO A CD  
9169  N N   . GLN A 1204 ? 1.1567 2.5868 2.2664 -0.6547 0.2016  -0.8907 1204 GLN A N   
9170  C CA  . GLN A 1204 ? 1.0737 2.5164 2.2209 -0.6309 0.1942  -0.9458 1204 GLN A CA  
9171  C C   . GLN A 1204 ? 0.9467 2.3889 2.1286 -0.5879 0.1834  -0.9427 1204 GLN A C   
9172  O O   . GLN A 1204 ? 0.9017 2.3578 2.1165 -0.5800 0.1882  -0.9844 1204 GLN A O   
9173  C CB  . GLN A 1204 ? 1.0761 2.5155 2.2168 -0.6244 0.1792  -0.9572 1204 GLN A CB  
9174  C CG  . GLN A 1204 ? 1.0427 2.4982 2.2185 -0.6019 0.1713  -1.0165 1204 GLN A CG  
9175  C CD  . GLN A 1204 ? 1.0392 2.5180 2.2335 -0.6244 0.1906  -1.0715 1204 GLN A CD  
9176  O OE1 . GLN A 1204 ? 1.0449 2.5272 2.2202 -0.6610 0.2106  -1.0668 1204 GLN A OE1 
9177  N NE2 . GLN A 1204 ? 1.0321 2.5295 2.2646 -0.6024 0.1844  -1.1250 1204 GLN A NE2 
9178  N N   . PHE A 1205 ? 1.0415 2.4698 2.2175 -0.5611 0.1691  -0.8935 1205 PHE A N   
9179  C CA  . PHE A 1205 ? 0.9815 2.4094 2.1841 -0.5226 0.1596  -0.8822 1205 PHE A CA  
9180  C C   . PHE A 1205 ? 0.9834 2.4183 2.2008 -0.5326 0.1760  -0.8977 1205 PHE A C   
9181  O O   . PHE A 1205 ? 0.9695 2.4124 2.2227 -0.5083 0.1699  -0.9266 1205 PHE A O   
9182  C CB  . PHE A 1205 ? 0.8254 2.2398 2.0088 -0.5053 0.1524  -0.8142 1205 PHE A CB  
9183  C CG  . PHE A 1205 ? 0.7486 2.1631 1.9489 -0.4735 0.1492  -0.7897 1205 PHE A CG  
9184  C CD1 . PHE A 1205 ? 0.7271 2.1468 1.9550 -0.4329 0.1304  -0.8016 1205 PHE A CD1 
9185  C CD2 . PHE A 1205 ? 0.7090 2.1188 1.8933 -0.4842 0.1645  -0.7513 1205 PHE A CD2 
9186  C CE1 . PHE A 1205 ? 0.6906 2.1113 1.9303 -0.4056 0.1282  -0.7766 1205 PHE A CE1 
9187  C CE2 . PHE A 1205 ? 0.6670 2.0768 1.8627 -0.4564 0.1631  -0.7271 1205 PHE A CE2 
9188  C CZ  . PHE A 1205 ? 0.6592 2.0746 1.8824 -0.4180 0.1456  -0.7392 1205 PHE A CZ  
9189  N N   . ARG A 1206 ? 0.8127 2.2456 2.0028 -0.5691 0.1958  -0.8807 1206 ARG A N   
9190  C CA  . ARG A 1206 ? 0.8318 2.2711 2.0315 -0.5829 0.2136  -0.8935 1206 ARG A CA  
9191  C C   . ARG A 1206 ? 0.8295 2.2875 2.0683 -0.5843 0.2176  -0.9640 1206 ARG A C   
9192  O O   . ARG A 1206 ? 0.7976 2.2622 2.0679 -0.5729 0.2215  -0.9854 1206 ARG A O   
9193  C CB  . ARG A 1206 ? 0.9198 2.3574 2.0799 -0.6263 0.2333  -0.8711 1206 ARG A CB  
9194  C CG  . ARG A 1206 ? 0.9829 2.4057 2.1041 -0.6296 0.2294  -0.8043 1206 ARG A CG  
9195  C CD  . ARG A 1206 ? 1.0529 2.4697 2.1677 -0.6190 0.2355  -0.7627 1206 ARG A CD  
9196  N NE  . ARG A 1206 ? 1.1153 2.5213 2.1982 -0.6154 0.2307  -0.6974 1206 ARG A NE  
9197  C CZ  . ARG A 1206 ? 1.1882 2.5910 2.2396 -0.6397 0.2299  -0.6728 1206 ARG A CZ  
9198  N NH1 . ARG A 1206 ? 1.2327 2.6412 2.2753 -0.6716 0.2344  -0.7073 1206 ARG A NH1 
9199  N NH2 . ARG A 1206 ? 1.1818 2.5772 2.2110 -0.6321 0.2250  -0.6131 1206 ARG A NH2 
9200  N N   . SER A 1207 ? 1.0329 2.5005 2.2701 -0.5989 0.2172  -1.0001 1207 SER A N   
9201  C CA  . SER A 1207 ? 1.0222 2.5127 2.2963 -0.6023 0.2227  -1.0692 1207 SER A CA  
9202  C C   . SER A 1207 ? 0.9541 2.4489 2.2717 -0.5566 0.2006  -1.0930 1207 SER A C   
9203  O O   . SER A 1207 ? 0.9601 2.4699 2.3201 -0.5458 0.2022  -1.1348 1207 SER A O   
9204  C CB  . SER A 1207 ? 1.0617 2.5631 2.3184 -0.6301 0.2285  -1.0984 1207 SER A CB  
9205  O OG  . SER A 1207 ? 1.0773 2.6061 2.3636 -0.6464 0.2435  -1.1627 1207 SER A OG  
9206  N N   . ILE A 1208 ? 1.0305 2.5129 2.3383 -0.5294 0.1790  -1.0656 1208 ILE A N   
9207  C CA  . ILE A 1208 ? 0.9117 2.3988 2.2553 -0.4856 0.1550  -1.0857 1208 ILE A CA  
9208  C C   . ILE A 1208 ? 0.8118 2.2945 2.1776 -0.4637 0.1519  -1.0676 1208 ILE A C   
9209  O O   . ILE A 1208 ? 0.7670 2.2629 2.1761 -0.4456 0.1454  -1.1080 1208 ILE A O   
9210  C CB  . ILE A 1208 ? 0.8676 2.3431 2.1914 -0.4632 0.1336  -1.0576 1208 ILE A CB  
9211  C CG1 . ILE A 1208 ? 0.8623 2.3303 2.1444 -0.4964 0.1433  -1.0400 1208 ILE A CG1 
9212  C CG2 . ILE A 1208 ? 0.8738 2.3626 2.2292 -0.4299 0.1109  -1.1036 1208 ILE A CG2 
9213  C CD1 . ILE A 1208 ? 0.8356 2.2948 2.1015 -0.4790 0.1238  -1.0242 1208 ILE A CD1 
9214  N N   . VAL A 1209 ? 0.3070 1.7727 1.6432 -0.4664 0.1570  -1.0066 1209 VAL A N   
9215  C CA  . VAL A 1209 ? 0.3341 1.7943 1.6813 -0.4512 0.1586  -0.9800 1209 VAL A CA  
9216  C C   . VAL A 1209 ? 0.4394 1.9107 1.8149 -0.4677 0.1750  -1.0194 1209 VAL A C   
9217  O O   . VAL A 1209 ? 0.4298 1.9034 1.8358 -0.4481 0.1704  -1.0258 1209 VAL A O   
9218  C CB  . VAL A 1209 ? 0.3306 1.7746 1.6338 -0.4646 0.1704  -0.9117 1209 VAL A CB  
9219  C CG1 . VAL A 1209 ? 0.3122 1.7515 1.6216 -0.4524 0.1761  -0.8830 1209 VAL A CG1 
9220  C CG2 . VAL A 1209 ? 0.3219 1.7571 1.6021 -0.4472 0.1552  -0.8715 1209 VAL A CG2 
9221  N N   . SER A 1210 ? 0.9082 2.3878 2.2735 -0.5048 0.1945  -1.0456 1210 SER A N   
9222  C CA  . SER A 1210 ? 0.9999 2.4945 2.3940 -0.5233 0.2121  -1.0896 1210 SER A CA  
9223  C C   . SER A 1210 ? 1.0397 2.5528 2.4900 -0.4971 0.1969  -1.1491 1210 SER A C   
9224  O O   . SER A 1210 ? 1.0486 2.5668 2.5380 -0.4808 0.1936  -1.1666 1210 SER A O   
9225  C CB  . SER A 1210 ? 1.0711 2.5757 2.4418 -0.5677 0.2346  -1.1098 1210 SER A CB  
9226  O OG  . SER A 1210 ? 1.1206 2.6485 2.5223 -0.5701 0.2337  -1.1732 1210 SER A OG  
9227  N N   . ALA A 1211 ? 1.3156 2.8393 2.7695 -0.4928 0.1867  -1.1798 1211 ALA A N   
9228  C CA  . ALA A 1211 ? 1.3106 2.8562 2.8157 -0.4698 0.1721  -1.2406 1211 ALA A CA  
9229  C C   . ALA A 1211 ? 1.2526 2.7933 2.7910 -0.4274 0.1476  -1.2346 1211 ALA A C   
9230  O O   . ALA A 1211 ? 1.2366 2.7890 2.8206 -0.4189 0.1473  -1.2670 1211 ALA A O   
9231  C CB  . ALA A 1211 ? 1.3165 2.8683 2.8090 -0.4641 0.1597  -1.2571 1211 ALA A CB  
9232  N N   . LEU A 1212 ? 1.0940 2.6186 2.6101 -0.4011 0.1268  -1.1928 1212 LEU A N   
9233  C CA  . LEU A 1212 ? 1.0728 2.5923 2.6112 -0.3625 0.1038  -1.1773 1212 LEU A CA  
9234  C C   . LEU A 1212 ? 1.0645 2.5801 2.6182 -0.3718 0.1192  -1.1651 1212 LEU A C   
9235  O O   . LEU A 1212 ? 1.0721 2.5987 2.6737 -0.3553 0.1101  -1.1992 1212 LEU A O   
9236  C CB  . LEU A 1212 ? 1.0217 2.5235 2.5212 -0.3440 0.0902  -1.1177 1212 LEU A CB  
9237  C CG  . LEU A 1212 ? 0.9681 2.4655 2.4807 -0.3058 0.0694  -1.0889 1212 LEU A CG  
9238  C CD1 . LEU A 1212 ? 0.9688 2.4825 2.5304 -0.2748 0.0433  -1.1418 1212 LEU A CD1 
9239  C CD2 . LEU A 1212 ? 0.9390 2.4260 2.4160 -0.2861 0.0569  -1.0365 1212 LEU A CD2 
9240  N N   . LYS A 1213 ? 0.5113 2.0121 2.0247 -0.3990 0.1423  -1.1182 1213 LYS A N   
9241  C CA  . LYS A 1213 ? 0.4818 1.9765 2.0005 -0.4078 0.1580  -1.0985 1213 LYS A CA  
9242  C C   . LYS A 1213 ? 0.5563 2.0685 2.1214 -0.4214 0.1696  -1.1575 1213 LYS A C   
9243  O O   . LYS A 1213 ? 0.5493 2.0616 2.1427 -0.4153 0.1725  -1.1606 1213 LYS A O   
9244  C CB  . LYS A 1213 ? 0.4128 1.8927 1.8779 -0.4401 0.1826  -1.0486 1213 LYS A CB  
9245  C CG  . LYS A 1213 ? 0.3857 1.8526 1.8379 -0.4318 0.1875  -0.9992 1213 LYS A CG  
9246  C CD  . LYS A 1213 ? 0.3846 1.8368 1.7867 -0.4276 0.1855  -0.9350 1213 LYS A CD  
9247  C CE  . LYS A 1213 ? 0.3978 1.8382 1.7727 -0.4346 0.2019  -0.8837 1213 LYS A CE  
9248  N NZ  . LYS A 1213 ? 0.3830 1.8123 1.7154 -0.4229 0.1986  -0.8190 1213 LYS A NZ  
9249  N N   . ARG A 1214 ? 1.5886 3.1170 3.1612 -0.4405 0.1774  -1.2037 1214 ARG A N   
9250  C CA  . ARG A 1214 ? 1.7310 3.2832 3.3527 -0.4520 0.1880  -1.2680 1214 ARG A CA  
9251  C C   . ARG A 1214 ? 1.7331 3.2964 3.4147 -0.4124 0.1604  -1.3035 1214 ARG A C   
9252  O O   . ARG A 1214 ? 1.7701 3.3410 3.4952 -0.4097 0.1639  -1.3274 1214 ARG A O   
9253  C CB  . ARG A 1214 ? 1.8933 3.4647 3.5087 -0.4756 0.1986  -1.3085 1214 ARG A CB  
9254  C CG  . ARG A 1214 ? 2.0656 3.6698 3.7431 -0.4712 0.1975  -1.3850 1214 ARG A CG  
9255  C CD  . ARG A 1214 ? 2.2219 3.8488 3.8886 -0.5053 0.2185  -1.4221 1214 ARG A CD  
9256  N NE  . ARG A 1214 ? 2.2979 3.9151 3.9157 -0.5086 0.2118  -1.3967 1214 ARG A NE  
9257  C CZ  . ARG A 1214 ? 2.3845 4.0078 3.9651 -0.5459 0.2325  -1.3976 1214 ARG A CZ  
9258  N NH1 . ARG A 1214 ? 2.4507 4.0909 4.0353 -0.5831 0.2615  -1.4226 1214 ARG A NH1 
9259  N NH2 . ARG A 1214 ? 2.3890 4.0018 3.9280 -0.5469 0.2240  -1.3734 1214 ARG A NH2 
9260  N N   . GLU A 1215 ? 0.8350 2.3985 2.5176 -0.3808 0.1313  -1.3050 1215 GLU A N   
9261  C CA  . GLU A 1215 ? 0.8043 2.3841 2.5437 -0.3445 0.1022  -1.3509 1215 GLU A CA  
9262  C C   . GLU A 1215 ? 0.7390 2.3111 2.5085 -0.3151 0.0831  -1.3354 1215 GLU A C   
9263  O O   . GLU A 1215 ? 0.7579 2.3457 2.5827 -0.2901 0.0614  -1.3801 1215 GLU A O   
9264  C CB  . GLU A 1215 ? 0.7784 2.3618 2.5058 -0.3193 0.0759  -1.3591 1215 GLU A CB  
9265  C CG  . GLU A 1215 ? 0.8143 2.4185 2.5409 -0.3396 0.0879  -1.4038 1215 GLU A CG  
9266  C CD  . GLU A 1215 ? 0.8661 2.5023 2.6569 -0.3269 0.0787  -1.4772 1215 GLU A CD  
9267  O OE1 . GLU A 1215 ? 0.8768 2.5170 2.7146 -0.3064 0.0649  -1.4936 1215 GLU A OE1 
9268  O OE2 . GLU A 1215 ? 0.8994 2.5583 2.6944 -0.3373 0.0849  -1.5179 1215 GLU A OE2 
9269  N N   . ALA A 1216 ? 0.7795 2.3294 2.5134 -0.3178 0.0906  -1.2728 1216 ALA A N   
9270  C CA  . ALA A 1216 ? 0.6987 2.2417 2.4538 -0.2903 0.0738  -1.2498 1216 ALA A CA  
9271  C C   . ALA A 1216 ? 0.6949 2.2526 2.5158 -0.2875 0.0724  -1.2994 1216 ALA A C   
9272  O O   . ALA A 1216 ? 0.7446 2.3188 2.5934 -0.3092 0.0885  -1.3498 1216 ALA A O   
9273  C CB  . ALA A 1216 ? 0.6515 2.1736 2.3600 -0.3044 0.0942  -1.1810 1216 ALA A CB  
9274  N N   . LEU A 1217 ? 0.7816 2.3357 2.6286 -0.2599 0.0528  -1.2850 1217 LEU A N   
9275  C CA  . LEU A 1217 ? 0.7704 2.3349 2.6801 -0.2561 0.0508  -1.3219 1217 LEU A CA  
9276  C C   . LEU A 1217 ? 0.7477 2.2978 2.6491 -0.2408 0.0459  -1.2697 1217 LEU A C   
9277  O O   . LEU A 1217 ? 0.6683 2.2037 2.5158 -0.2365 0.0484  -1.2102 1217 LEU A O   
9278  C CB  . LEU A 1217 ? 0.7617 2.3463 2.7312 -0.2231 0.0139  -1.3811 1217 LEU A CB  
9279  C CG  . LEU A 1217 ? 0.7549 2.3486 2.7057 -0.2161 0.0012  -1.4042 1217 LEU A CG  
9280  C CD1 . LEU A 1217 ? 0.7270 2.3235 2.6904 -0.1686 -0.0457 -1.4076 1217 LEU A CD1 
9281  C CD2 . LEU A 1217 ? 0.8050 2.4234 2.7931 -0.2360 0.0156  -1.4728 1217 LEU A CD2 
9282  N N   . VAL A 1218 ? 0.2160 1.7720 2.1711 -0.2312 0.0390  -1.2908 1218 VAL A N   
9283  C CA  . VAL A 1218 ? 0.2339 1.7763 2.1747 -0.2271 0.0467  -1.2375 1218 VAL A CA  
9284  C C   . VAL A 1218 ? 0.2337 1.7823 2.2361 -0.2147 0.0374  -1.2583 1218 VAL A C   
9285  O O   . VAL A 1218 ? 0.2096 1.7732 2.2740 -0.2171 0.0320  -1.3198 1218 VAL A O   
9286  C CB  . VAL A 1218 ? 0.3135 1.8417 2.2075 -0.2680 0.0906  -1.2036 1218 VAL A CB  
9287  C CG1 . VAL A 1218 ? 0.2892 1.8024 2.1091 -0.2696 0.0978  -1.1401 1218 VAL A CG1 
9288  C CG2 . VAL A 1218 ? 0.4112 1.9501 2.3199 -0.3012 0.1125  -1.2561 1218 VAL A CG2 
9289  N N   . LYS A 1219 ? 0.6767 2.2144 2.6596 -0.2038 0.0397  -1.2042 1219 LYS A N   
9290  C CA  . LYS A 1219 ? 0.8268 2.3698 2.8614 -0.1800 0.0212  -1.2097 1219 LYS A CA  
9291  C C   . LYS A 1219 ? 0.9223 2.4532 2.9443 -0.2030 0.0561  -1.1744 1219 LYS A C   
9292  O O   . LYS A 1219 ? 0.9216 2.4390 2.8837 -0.2064 0.0739  -1.1116 1219 LYS A O   
9293  C CB  . LYS A 1219 ? 0.8650 2.4113 2.8904 -0.1320 -0.0180 -1.1776 1219 LYS A CB  
9294  C CG  . LYS A 1219 ? 1.6759 3.2387 3.7474 -0.0937 -0.0692 -1.2285 1219 LYS A CG  
9295  C CD  . LYS A 1219 ? 1.4906 3.0557 3.5340 -0.0454 -0.1062 -1.1910 1219 LYS A CD  
9296  C CE  . LYS A 1219 ? 1.2971 2.8763 3.3792 -0.0073 -0.1580 -1.2416 1219 LYS A CE  
9297  N NZ  . LYS A 1219 ? 1.2724 2.8524 3.3144 0.0362  -0.1888 -1.2063 1219 LYS A NZ  
9298  N N   . GLY A 1220 ? 1.8440 3.3808 3.9236 -0.2167 0.0653  -1.2162 1220 GLY A N   
9299  C CA  . GLY A 1220 ? 1.8676 3.3934 3.9402 -0.2397 0.0990  -1.1906 1220 GLY A CA  
9300  C C   . GLY A 1220 ? 1.8902 3.4024 3.9018 -0.2834 0.1437  -1.1693 1220 GLY A C   
9301  O O   . GLY A 1220 ? 1.8780 3.3826 3.8281 -0.2893 0.1491  -1.1376 1220 GLY A O   
9302  N N   . ASN A 1221 ? 1.3811 2.8912 3.4108 -0.3133 0.1742  -1.1878 1221 ASN A N   
9303  C CA  . ASN A 1221 ? 1.3981 2.8967 3.3710 -0.3549 0.2154  -1.1701 1221 ASN A CA  
9304  C C   . ASN A 1221 ? 1.3519 2.8327 3.2845 -0.3650 0.2404  -1.1155 1221 ASN A C   
9305  O O   . ASN A 1221 ? 1.3661 2.8475 3.3377 -0.3517 0.2360  -1.1152 1221 ASN A O   
9306  C CB  . ASN A 1221 ? 1.4753 2.9881 3.4922 -0.3835 0.2340  -1.2359 1221 ASN A CB  
9307  C CG  . ASN A 1221 ? 1.5013 3.0058 3.4582 -0.4264 0.2740  -1.2212 1221 ASN A CG  
9308  O OD1 . ASN A 1221 ? 1.5277 3.0288 3.4870 -0.4507 0.3021  -1.2248 1221 ASN A OD1 
9309  N ND2 . ASN A 1221 ? 1.4863 2.9883 3.3897 -0.4357 0.2752  -1.2057 1221 ASN A ND2 
9310  N N   . PRO A 1222 ? 1.3368 2.8022 3.1896 -0.3863 0.2641  -1.0672 1222 PRO A N   
9311  C CA  . PRO A 1222 ? 1.2847 2.7493 3.0905 -0.3952 0.2627  -1.0591 1222 PRO A CA  
9312  C C   . PRO A 1222 ? 1.2454 2.7152 3.0556 -0.3570 0.2264  -1.0475 1222 PRO A C   
9313  O O   . PRO A 1222 ? 1.2617 2.7355 3.1043 -0.3257 0.2048  -1.0408 1222 PRO A O   
9314  C CB  . PRO A 1222 ? 1.2783 2.7240 3.0004 -0.4149 0.2886  -0.9959 1222 PRO A CB  
9315  C CG  . PRO A 1222 ? 1.3056 2.7443 3.0352 -0.4293 0.3122  -0.9904 1222 PRO A CG  
9316  C CD  . PRO A 1222 ? 1.3158 2.7638 3.1177 -0.4004 0.2912  -1.0155 1222 PRO A CD  
9317  N N   . PRO A 1223 ? 1.5653 3.0366 3.3447 -0.3588 0.2189  -1.0463 1223 PRO A N   
9318  C CA  . PRO A 1223 ? 1.4539 2.9291 3.2290 -0.3224 0.1861  -1.0294 1223 PRO A CA  
9319  C C   . PRO A 1223 ? 1.3650 2.8337 3.1171 -0.2934 0.1777  -0.9713 1223 PRO A C   
9320  O O   . PRO A 1223 ? 1.3218 2.7764 3.0146 -0.3052 0.2007  -0.9170 1223 PRO A O   
9321  C CB  . PRO A 1223 ? 1.4283 2.8977 3.1458 -0.3388 0.1941  -1.0106 1223 PRO A CB  
9322  C CG  . PRO A 1223 ? 1.4924 2.9665 3.2202 -0.3759 0.2162  -1.0553 1223 PRO A CG  
9323  C CD  . PRO A 1223 ? 1.5771 3.0505 3.3342 -0.3917 0.2366  -1.0700 1223 PRO A CD  
9324  N N   . ILE A 1224 ? 0.9388 2.4195 2.7368 -0.2550 0.1449  -0.9844 1224 ILE A N   
9325  C CA  . ILE A 1224 ? 0.8836 2.3644 2.6580 -0.2192 0.1304  -0.9331 1224 ILE A CA  
9326  C C   . ILE A 1224 ? 0.8551 2.3455 2.6227 -0.1862 0.0972  -0.9322 1224 ILE A C   
9327  O O   . ILE A 1224 ? 0.8357 2.3237 2.5566 -0.1655 0.0955  -0.8808 1224 ILE A O   
9328  C CB  . ILE A 1224 ? 0.8696 2.3576 2.6917 -0.1946 0.1178  -0.9365 1224 ILE A CB  
9329  C CG1 . ILE A 1224 ? 0.9304 2.4119 2.7774 -0.2250 0.1451  -0.9541 1224 ILE A CG1 
9330  C CG2 . ILE A 1224 ? 0.8109 2.2949 2.5868 -0.1695 0.1217  -0.8714 1224 ILE A CG2 
9331  C CD1 . ILE A 1224 ? 0.9658 2.4483 2.8304 -0.2046 0.1437  -0.9306 1224 ILE A CD1 
9332  N N   . TYR A 1225 ? 0.6039 2.1058 2.4163 -0.1805 0.0722  -0.9898 1225 TYR A N   
9333  C CA  . TYR A 1225 ? 0.5670 2.0765 2.3690 -0.1542 0.0429  -0.9942 1225 TYR A CA  
9334  C C   . TYR A 1225 ? 0.5486 2.0589 2.3512 -0.1786 0.0462  -1.0359 1225 TYR A C   
9335  O O   . TYR A 1225 ? 0.5689 2.0863 2.4183 -0.1927 0.0452  -1.0931 1225 TYR A O   
9336  C CB  . TYR A 1225 ? 0.5985 2.1237 2.4519 -0.1088 -0.0022 -1.0233 1225 TYR A CB  
9337  C CG  . TYR A 1225 ? 0.6223 2.1503 2.4844 -0.0784 -0.0109 -0.9903 1225 TYR A CG  
9338  C CD1 . TYR A 1225 ? 0.6200 2.1474 2.4356 -0.0466 -0.0155 -0.9339 1225 TYR A CD1 
9339  C CD2 . TYR A 1225 ? 0.6631 2.1955 2.5813 -0.0789 -0.0144 -1.0172 1225 TYR A CD2 
9340  C CE1 . TYR A 1225 ? 0.6400 2.1704 2.4603 -0.0154 -0.0219 -0.9045 1225 TYR A CE1 
9341  C CE2 . TYR A 1225 ? 0.6843 2.2195 2.6108 -0.0495 -0.0228 -0.9874 1225 TYR A CE2 
9342  C CZ  . TYR A 1225 ? 0.6627 2.1968 2.5381 -0.0175 -0.0259 -0.9308 1225 TYR A CZ  
9343  O OH  . TYR A 1225 ? 0.6686 2.2053 2.5487 0.0139  -0.0320 -0.9021 1225 TYR A OH  
9344  N N   . ARG A 1226 ? 0.6979 2.2026 2.4489 -0.1813 0.0502  -1.0071 1226 ARG A N   
9345  C CA  . ARG A 1226 ? 0.7608 2.2666 2.5043 -0.2016 0.0528  -1.0400 1226 ARG A CA  
9346  C C   . ARG A 1226 ? 0.7653 2.2794 2.5063 -0.1678 0.0188  -1.0468 1226 ARG A C   
9347  O O   . ARG A 1226 ? 0.7520 2.2646 2.4633 -0.1413 0.0087  -1.0011 1226 ARG A O   
9348  C CB  . ARG A 1226 ? 0.8081 2.2990 2.4884 -0.2343 0.0855  -0.9974 1226 ARG A CB  
9349  C CG  . ARG A 1226 ? 0.8438 2.3364 2.5189 -0.2625 0.0946  -1.0350 1226 ARG A CG  
9350  C CD  . ARG A 1226 ? 0.8316 2.3098 2.4461 -0.2984 0.1267  -0.9954 1226 ARG A CD  
9351  N NE  . ARG A 1226 ? 0.8056 2.2713 2.3916 -0.3167 0.1539  -0.9521 1226 ARG A NE  
9352  C CZ  . ARG A 1226 ? 0.7573 2.2209 2.3525 -0.3467 0.1785  -0.9695 1226 ARG A CZ  
9353  N NH1 . ARG A 1226 ? 0.7344 2.2096 2.3715 -0.3625 0.1814  -1.0317 1226 ARG A NH1 
9354  N NH2 . ARG A 1226 ? 0.7314 2.1826 2.2930 -0.3600 0.2008  -0.9252 1226 ARG A NH2 
9355  N N   . PHE A 1227 ? 0.8290 2.3528 2.5976 -0.1680 0.0029  -1.1034 1227 PHE A N   
9356  C CA  . PHE A 1227 ? 0.7875 2.3178 2.5462 -0.1387 -0.0275 -1.1108 1227 PHE A CA  
9357  C C   . PHE A 1227 ? 0.7866 2.3261 2.5674 -0.1506 -0.0331 -1.1737 1227 PHE A C   
9358  O O   . PHE A 1227 ? 0.8053 2.3511 2.6219 -0.1728 -0.0197 -1.2181 1227 PHE A O   
9359  C CB  . PHE A 1227 ? 0.8075 2.3473 2.5902 -0.0888 -0.0669 -1.1085 1227 PHE A CB  
9360  C CG  . PHE A 1227 ? 0.8657 2.4169 2.7140 -0.0760 -0.0883 -1.1617 1227 PHE A CG  
9361  C CD1 . PHE A 1227 ? 0.8841 2.4471 2.7686 -0.0705 -0.1098 -1.2270 1227 PHE A CD1 
9362  C CD2 . PHE A 1227 ? 0.8698 2.4209 2.7440 -0.0674 -0.0878 -1.1464 1227 PHE A CD2 
9363  C CE1 . PHE A 1227 ? 0.8916 2.4664 2.8396 -0.0566 -0.1314 -1.2775 1227 PHE A CE1 
9364  C CE2 . PHE A 1227 ? 0.8685 2.4305 2.8076 -0.0539 -0.1104 -1.1958 1227 PHE A CE2 
9365  C CZ  . PHE A 1227 ? 0.8881 2.4621 2.8654 -0.0483 -0.1330 -1.2621 1227 PHE A CZ  
9366  N N   . TRP A 1228 ? 0.3232 1.8652 2.0816 -0.1362 -0.0504 -1.1778 1228 TRP A N   
9367  C CA  . TRP A 1228 ? 0.3667 1.9187 2.1400 -0.1483 -0.0519 -1.2355 1228 TRP A CA  
9368  C C   . TRP A 1228 ? 0.6121 2.1782 2.4191 -0.1068 -0.0952 -1.2770 1228 TRP A C   
9369  O O   . TRP A 1228 ? 0.5924 2.1577 2.3985 -0.0707 -0.1223 -1.2512 1228 TRP A O   
9370  C CB  . TRP A 1228 ? 0.3359 1.8803 2.0572 -0.1673 -0.0367 -1.2143 1228 TRP A CB  
9371  C CG  . TRP A 1228 ? 0.3432 1.8712 2.0190 -0.2056 0.0023  -1.1630 1228 TRP A CG  
9372  C CD1 . TRP A 1228 ? 0.3696 1.8939 2.0178 -0.2427 0.0286  -1.1667 1228 TRP A CD1 
9373  C CD2 . TRP A 1228 ? 0.3224 1.8372 1.9724 -0.2083 0.0168  -1.1012 1228 TRP A CD2 
9374  N NE1 . TRP A 1228 ? 0.3528 1.8612 1.9601 -0.2671 0.0553  -1.1120 1228 TRP A NE1 
9375  C CE2 . TRP A 1228 ? 0.3276 1.8303 1.9353 -0.2465 0.0495  -1.0719 1228 TRP A CE2 
9376  C CE3 . TRP A 1228 ? 0.2817 1.7952 1.9384 -0.1813 0.0059  -1.0674 1228 TRP A CE3 
9377  C CZ2 . TRP A 1228 ? 0.2951 1.7844 1.8681 -0.2574 0.0700  -1.0126 1228 TRP A CZ2 
9378  C CZ3 . TRP A 1228 ? 0.2525 1.7535 1.8738 -0.1937 0.0302  -1.0078 1228 TRP A CZ3 
9379  C CH2 . TRP A 1228 ? 0.2555 1.7443 1.8356 -0.2308 0.0611  -0.9818 1228 TRP A CH2 
9380  N N   . LYS A 1229 ? 0.7883 2.3693 2.6235 -0.1104 -0.1010 -1.3402 1229 LYS A N   
9381  C CA  . LYS A 1229 ? 0.8390 2.4349 2.7067 -0.0714 -0.1429 -1.3872 1229 LYS A CA  
9382  C C   . LYS A 1229 ? 0.9433 2.5428 2.7779 -0.0642 -0.1523 -1.4002 1229 LYS A C   
9383  O O   . LYS A 1229 ? 0.9475 2.5409 2.7450 -0.0941 -0.1241 -1.3836 1229 LYS A O   
9384  C CB  . LYS A 1229 ? 0.8572 2.4726 2.7900 -0.0767 -0.1436 -1.4555 1229 LYS A CB  
9385  C CG  . LYS A 1229 ? 0.9033 2.5270 2.8857 -0.0369 -0.1849 -1.4812 1229 LYS A CG  
9386  C CD  . LYS A 1229 ? 1.3599 2.9989 3.4090 -0.0512 -0.1744 -1.5318 1229 LYS A CD  
9387  C CE  . LYS A 1229 ? 1.3295 2.9926 3.4041 -0.0699 -0.1585 -1.5957 1229 LYS A CE  
9388  N NZ  . LYS A 1229 ? 1.2908 2.9737 3.3968 -0.0333 -0.1983 -1.6495 1229 LYS A NZ  
9389  N N   . ASP A 1230 ? 1.4261 3.0353 3.2723 -0.0250 -0.1921 -1.4295 1230 ASP A N   
9390  C CA  . ASP A 1230 ? 1.5224 3.1358 3.3369 -0.0164 -0.2015 -1.4442 1230 ASP A CA  
9391  C C   . ASP A 1230 ? 1.6272 3.2555 3.4515 -0.0510 -0.1718 -1.4890 1230 ASP A C   
9392  O O   . ASP A 1230 ? 1.6023 3.2263 3.3861 -0.0708 -0.1529 -1.4751 1230 ASP A O   
9393  C CB  . ASP A 1230 ? 1.5903 3.2137 3.4191 0.0318  -0.2495 -1.4764 1230 ASP A CB  
9394  C CG  . ASP A 1230 ? 1.6586 3.2853 3.4492 0.0434  -0.2600 -1.4883 1230 ASP A CG  
9395  O OD1 . ASP A 1230 ? 1.6626 3.2858 3.4220 0.0131  -0.2302 -1.4771 1230 ASP A OD1 
9396  O OD2 . ASP A 1230 ? 1.7017 3.3340 3.4918 0.0833  -0.2988 -1.5083 1230 ASP A OD2 
9397  N N   . ASN A 1231 ? 2.5008 4.1488 4.3808 -0.0580 -0.1671 -1.5416 1231 ASN A N   
9398  C CA  . ASN A 1231 ? 2.6317 4.3033 4.5297 -0.0871 -0.1397 -1.5901 1231 ASN A CA  
9399  C C   . ASN A 1231 ? 2.6999 4.3623 4.5616 -0.1350 -0.0946 -1.5598 1231 ASN A C   
9400  O O   . ASN A 1231 ? 2.6686 4.3060 4.4790 -0.1433 -0.0868 -1.5017 1231 ASN A O   
9401  C CB  . ASN A 1231 ? 2.7173 4.4132 4.6868 -0.0883 -0.1390 -1.6458 1231 ASN A CB  
9402  C CG  . ASN A 1231 ? 2.7579 4.4431 4.7426 -0.1171 -0.1109 -1.6232 1231 ASN A CG  
9403  O OD1 . ASN A 1231 ? 2.7662 4.4300 4.7454 -0.1054 -0.1219 -1.5813 1231 ASN A OD1 
9404  N ND2 . ASN A 1231 ? 2.7848 4.4870 4.7869 -0.1553 -0.0736 -1.6504 1231 ASN A ND2 
9405  N N   . LEU A 1232 ? 1.4681 3.1533 3.3576 -0.1659 -0.0657 -1.6010 1232 LEU A N   
9406  C CA  . LEU A 1232 ? 1.5057 3.1853 3.3643 -0.2133 -0.0232 -1.5795 1232 LEU A CA  
9407  C C   . LEU A 1232 ? 1.6457 3.3570 3.5530 -0.2393 0.0019  -1.6356 1232 LEU A C   
9408  O O   . LEU A 1232 ? 1.7313 3.4717 3.6491 -0.2491 0.0104  -1.6799 1232 LEU A O   
9409  C CB  . LEU A 1232 ? 1.3889 3.0655 3.1951 -0.2248 -0.0158 -1.5653 1232 LEU A CB  
9410  C CG  . LEU A 1232 ? 1.2764 2.9597 3.0596 -0.2745 0.0254  -1.5659 1232 LEU A CG  
9411  C CD1 . LEU A 1232 ? 1.2065 2.8557 2.9299 -0.2971 0.0419  -1.4966 1232 LEU A CD1 
9412  C CD2 . LEU A 1232 ? 1.2589 2.9667 3.0346 -0.2802 0.0281  -1.6027 1232 LEU A CD2 
9413  N N   . GLN A 1233 ? 2.5137 4.2219 4.4522 -0.2499 0.0139  -1.6349 1233 GLN A N   
9414  C CA  . GLN A 1233 ? 2.6294 4.3666 4.6139 -0.2782 0.0416  -1.6844 1233 GLN A CA  
9415  C C   . GLN A 1233 ? 2.8131 4.5933 4.8639 -0.2609 0.0279  -1.7613 1233 GLN A C   
9416  O O   . GLN A 1233 ? 2.8181 4.6290 4.9069 -0.2862 0.0530  -1.8069 1233 GLN A O   
9417  C CB  . GLN A 1233 ? 2.7542 4.4939 4.6964 -0.3274 0.0834  -1.6733 1233 GLN A CB  
9418  C CG  . GLN A 1233 ? 2.8818 4.6477 4.8116 -0.3366 0.0886  -1.7060 1233 GLN A CG  
9419  C CD  . GLN A 1233 ? 2.9872 4.7531 4.8707 -0.3863 0.1274  -1.6910 1233 GLN A CD  
9420  O OE1 . GLN A 1233 ? 3.0558 4.8395 4.9581 -0.4189 0.1569  -1.7154 1233 GLN A OE1 
9421  N NE2 . GLN A 1233 ? 2.9923 4.7385 4.8145 -0.3927 0.1268  -1.6510 1233 GLN A NE2 
9422  N N   . HIS A 1234 ? 1.8911 3.6758 3.9548 -0.2184 -0.0116 -1.7764 1234 HIS A N   
9423  C CA  . HIS A 1234 ? 1.9452 3.7698 4.0761 -0.1958 -0.0309 -1.8473 1234 HIS A CA  
9424  C C   . HIS A 1234 ? 2.0035 3.8240 4.1923 -0.1742 -0.0509 -1.8595 1234 HIS A C   
9425  O O   . HIS A 1234 ? 2.0281 3.8807 4.2847 -0.1587 -0.0647 -1.9190 1234 HIS A O   
9426  C CB  . HIS A 1234 ? 1.8945 3.7262 4.0112 -0.1592 -0.0657 -1.8589 1234 HIS A CB  
9427  C CG  . HIS A 1234 ? 1.8536 3.6886 3.9145 -0.1798 -0.0471 -1.8460 1234 HIS A CG  
9428  N ND1 . HIS A 1234 ? 1.8770 3.7431 3.9417 -0.2180 -0.0114 -1.8774 1234 HIS A ND1 
9429  C CD2 . HIS A 1234 ? 1.8153 3.6267 3.8158 -0.1677 -0.0599 -1.8055 1234 HIS A CD2 
9430  C CE1 . HIS A 1234 ? 1.8613 3.7214 3.8697 -0.2292 -0.0038 -1.8554 1234 HIS A CE1 
9431  N NE2 . HIS A 1234 ? 1.8238 3.6507 3.7941 -0.1987 -0.0326 -1.8124 1234 HIS A NE2 
9432  N N   . LYS A 1235 ? 2.0631 3.8447 4.2239 -0.1733 -0.0532 -1.8011 1235 LYS A N   
9433  C CA  . LYS A 1235 ? 2.1542 3.9266 4.3597 -0.1664 -0.0600 -1.7991 1235 LYS A CA  
9434  C C   . LYS A 1235 ? 2.3120 4.1073 4.5933 -0.1297 -0.0971 -1.8555 1235 LYS A C   
9435  O O   . LYS A 1235 ? 2.3613 4.1740 4.7043 -0.1385 -0.0877 -1.8922 1235 LYS A O   
9436  C CB  . LYS A 1235 ? 2.1370 3.9147 4.3534 -0.2124 -0.0130 -1.8021 1235 LYS A CB  
9437  C CG  . LYS A 1235 ? 2.0707 3.8197 4.2119 -0.2481 0.0209  -1.7387 1235 LYS A CG  
9438  C CD  . LYS A 1235 ? 1.9947 3.7058 4.1111 -0.2413 0.0149  -1.6749 1235 LYS A CD  
9439  C CE  . LYS A 1235 ? 1.9407 3.6278 3.9906 -0.2801 0.0521  -1.6173 1235 LYS A CE  
9440  N NZ  . LYS A 1235 ? 1.9049 3.5785 3.8874 -0.2830 0.0515  -1.5810 1235 LYS A NZ  
9441  N N   . ASP A 1236 ? 2.6025 4.3980 4.8792 -0.0883 -0.1401 -1.8632 1236 ASP A N   
9442  C CA  . ASP A 1236 ? 2.7425 4.5518 5.0834 -0.0491 -0.1828 -1.9063 1236 ASP A CA  
9443  C C   . ASP A 1236 ? 2.7933 4.5732 5.1457 -0.0415 -0.1943 -1.8674 1236 ASP A C   
9444  O O   . ASP A 1236 ? 2.8201 4.6075 5.2342 -0.0192 -0.2213 -1.8976 1236 ASP A O   
9445  C CB  . ASP A 1236 ? 2.7902 4.5993 5.1094 -0.0058 -0.2281 -1.9123 1236 ASP A CB  
9446  C CG  . ASP A 1236 ? 2.8795 4.7006 5.2517 0.0312  -0.2694 -1.9581 1236 ASP A CG  
9447  O OD1 . ASP A 1236 ? 2.9087 4.6980 5.2923 0.0295  -0.2711 -1.9355 1236 ASP A OD1 
9448  O OD2 . ASP A 1236 ? 2.9218 4.7251 5.2440 0.0563  -0.2937 -1.9475 1236 ASP A OD2 
9449  N N   . SER A 1237 ? 2.4612 4.2092 4.7531 -0.0609 -0.1732 -1.7991 1237 SER A N   
9450  C CA  . SER A 1237 ? 2.4781 4.1996 4.7691 -0.0625 -0.1726 -1.7514 1237 SER A CA  
9451  C C   . SER A 1237 ? 2.4915 4.2001 4.7927 -0.0155 -0.2255 -1.7357 1237 SER A C   
9452  O O   . SER A 1237 ? 2.5313 4.2231 4.8398 -0.0119 -0.2297 -1.6997 1237 SER A O   
9453  C CB  . SER A 1237 ? 2.4999 4.2338 4.8492 -0.0896 -0.1441 -1.7799 1237 SER A CB  
9454  O OG  . SER A 1237 ? 2.4688 4.1760 4.7995 -0.1030 -0.1287 -1.7238 1237 SER A OG  
9455  N N   . SER A 1238 ? 4.2980 5.5458 5.9360 -0.0212 -0.2159 -1.2006 1238 SER A N   
9456  C CA  . SER A 1238 ? 4.2402 5.5105 5.9171 0.0155  -0.2570 -1.2196 1238 SER A CA  
9457  C C   . SER A 1238 ? 4.1129 5.4584 5.8723 0.0321  -0.2711 -1.2655 1238 SER A C   
9458  O O   . SER A 1238 ? 4.0271 5.4192 5.8168 0.0521  -0.2899 -1.3109 1238 SER A O   
9459  C CB  . SER A 1238 ? 4.3622 5.5717 5.9422 0.0319  -0.2742 -1.1741 1238 SER A CB  
9460  O OG  . SER A 1238 ? 4.4005 5.6041 5.9360 0.0266  -0.2645 -1.1656 1238 SER A OG  
9461  N N   . VAL A 1239 ? 1.8847 3.5486 4.1191 0.0613  -0.3051 -1.6231 1239 VAL A N   
9462  C CA  . VAL A 1239 ? 1.7893 3.4327 3.9702 0.0721  -0.3076 -1.5471 1239 VAL A CA  
9463  C C   . VAL A 1239 ? 1.7575 3.4001 3.9693 0.1142  -0.3519 -1.5378 1239 VAL A C   
9464  O O   . VAL A 1239 ? 1.7171 3.3496 3.9219 0.1142  -0.3428 -1.4873 1239 VAL A O   
9465  C CB  . VAL A 1239 ? 1.7734 3.4039 3.9325 0.0294  -0.2559 -1.4996 1239 VAL A CB  
9466  C CG1 . VAL A 1239 ? 1.7921 3.4247 3.9282 -0.0134 -0.2125 -1.5141 1239 VAL A CG1 
9467  C CG2 . VAL A 1239 ? 1.8265 3.4597 4.0443 0.0196  -0.2477 -1.5126 1239 VAL A CG2 
9468  N N   . PRO A 1240 ? 2.4819 4.1356 4.7244 0.1521  -0.4004 -1.5848 1240 PRO A N   
9469  C CA  . PRO A 1240 ? 2.5088 4.1660 4.8024 0.1884  -0.4440 -1.5984 1240 PRO A CA  
9470  C C   . PRO A 1240 ? 2.4160 4.0600 4.6817 0.2145  -0.4562 -1.5273 1240 PRO A C   
9471  O O   . PRO A 1240 ? 2.4767 4.1189 4.7285 0.2638  -0.5021 -1.5141 1240 PRO A O   
9472  C CB  . PRO A 1240 ? 2.5996 4.2664 4.8978 0.2288  -0.4947 -1.6446 1240 PRO A CB  
9473  C CG  . PRO A 1240 ? 2.5749 4.2372 4.8037 0.2241  -0.4820 -1.6255 1240 PRO A CG  
9474  C CD  . PRO A 1240 ? 2.5182 4.1785 4.7328 0.1694  -0.4210 -1.6144 1240 PRO A CD  
9475  N N   . ASN A 1241 ? 3.1198 4.7553 5.3751 0.1839  -0.4138 -1.4817 1241 ASN A N   
9476  C CA  . ASN A 1241 ? 2.9607 4.5866 5.1916 0.2077  -0.4176 -1.4143 1241 ASN A CA  
9477  C C   . ASN A 1241 ? 2.6928 4.3116 4.8550 0.2452  -0.4354 -1.3661 1241 ASN A C   
9478  O O   . ASN A 1241 ? 2.6516 4.2640 4.7975 0.2883  -0.4574 -1.3238 1241 ASN A O   
9479  C CB  . ASN A 1241 ? 3.1393 4.7697 5.4291 0.2431  -0.4581 -1.4316 1241 ASN A CB  
9480  C CG  . ASN A 1241 ? 3.2592 4.8982 5.6243 0.2106  -0.4435 -1.4839 1241 ASN A CG  
9481  O OD1 . ASN A 1241 ? 3.2538 4.8904 5.6193 0.1615  -0.3922 -1.4804 1241 ASN A OD1 
9482  N ND2 . ASN A 1241 ? 3.3438 4.9657 5.7267 0.2329  -0.4800 -1.4967 1241 ASN A ND2 
9483  N N   . THR A 1242 ? 1.4620 3.0805 3.5825 0.2314  -0.4242 -1.3718 1242 THR A N   
9484  C CA  . THR A 1242 ? 1.2370 2.8504 3.2997 0.2711  -0.4465 -1.3384 1242 THR A CA  
9485  C C   . THR A 1242 ? 0.9347 2.5443 2.9421 0.2443  -0.4150 -1.3194 1242 THR A C   
9486  O O   . THR A 1242 ? 0.8504 2.4649 2.8649 0.2112  -0.4007 -1.3629 1242 THR A O   
9487  C CB  . THR A 1242 ? 1.3342 2.9548 3.4133 0.3084  -0.4983 -1.3894 1242 THR A CB  
9488  O OG1 . THR A 1242 ? 1.3658 2.9968 3.4750 0.2728  -0.4883 -1.4558 1242 THR A OG1 
9489  C CG2 . THR A 1242 ? 1.3907 3.0123 3.5160 0.3496  -0.5415 -1.4022 1242 THR A CG2 
9490  N N   . GLY A 1243 ? 1.2341 2.8343 3.1853 0.2642  -0.4058 -1.2548 1243 GLY A N   
9491  C CA  . GLY A 1243 ? 1.0880 2.6837 2.9844 0.2456  -0.3788 -1.2279 1243 GLY A CA  
9492  C C   . GLY A 1243 ? 1.0090 2.6088 2.8849 0.2655  -0.4062 -1.2586 1243 GLY A C   
9493  O O   . GLY A 1243 ? 1.0600 2.6658 2.9586 0.2984  -0.4488 -1.2990 1243 GLY A O   
9494  N N   . THR A 1244 ? 0.8471 2.4432 2.6777 0.2452  -0.3808 -1.2376 1244 THR A N   
9495  C CA  . THR A 1244 ? 0.8429 2.4427 2.6496 0.2541  -0.3973 -1.2655 1244 THR A CA  
9496  C C   . THR A 1244 ? 0.9185 2.5104 2.6667 0.2569  -0.3757 -1.2096 1244 THR A C   
9497  O O   . THR A 1244 ? 0.9205 2.5053 2.6508 0.2334  -0.3394 -1.1629 1244 THR A O   
9498  C CB  . THR A 1244 ? 0.7904 2.3956 2.6167 0.2063  -0.3786 -1.3224 1244 THR A CB  
9499  O OG1 . THR A 1244 ? 0.8110 2.4253 2.6959 0.2053  -0.3966 -1.3819 1244 THR A OG1 
9500  C CG2 . THR A 1244 ? 0.7807 2.3883 2.5721 0.2116  -0.3879 -1.3438 1244 THR A CG2 
9501  N N   . ALA A 1245 ? 0.9781 2.5711 2.6961 0.2866  -0.3977 -1.2151 1245 ALA A N   
9502  C CA  . ALA A 1245 ? 0.9817 2.5679 2.6476 0.2897  -0.3773 -1.1685 1245 ALA A CA  
9503  C C   . ALA A 1245 ? 0.9624 2.5479 2.6226 0.2299  -0.3393 -1.1747 1245 ALA A C   
9504  O O   . ALA A 1245 ? 0.9073 2.4853 2.5385 0.2132  -0.3072 -1.1247 1245 ALA A O   
9505  C CB  . ALA A 1245 ? 1.0235 2.6118 2.6628 0.3282  -0.4070 -1.1837 1245 ALA A CB  
9506  N N   . ARG A 1246 ? 1.0848 2.6763 2.7700 0.2005  -0.3421 -1.2366 1246 ARG A N   
9507  C CA  . ARG A 1246 ? 1.0807 2.6683 2.7561 0.1487  -0.3069 -1.2479 1246 ARG A CA  
9508  C C   . ARG A 1246 ? 1.0274 2.6094 2.7234 0.1082  -0.2719 -1.2340 1246 ARG A C   
9509  O O   . ARG A 1246 ? 0.9937 2.5671 2.6655 0.0725  -0.2366 -1.2055 1246 ARG A O   
9510  C CB  . ARG A 1246 ? 1.1146 2.7099 2.8057 0.1367  -0.3166 -1.3192 1246 ARG A CB  
9511  C CG  . ARG A 1246 ? 1.1155 2.7064 2.7854 0.0922  -0.2813 -1.3258 1246 ARG A CG  
9512  C CD  . ARG A 1246 ? 1.1961 2.7986 2.8800 0.0855  -0.2870 -1.3950 1246 ARG A CD  
9513  N NE  . ARG A 1246 ? 1.3058 2.9131 2.9687 0.1238  -0.3219 -1.4136 1246 ARG A NE  
9514  C CZ  . ARG A 1246 ? 1.3942 3.0020 3.0233 0.1190  -0.3177 -1.4260 1246 ARG A CZ  
9515  N NH1 . ARG A 1246 ? 1.4028 3.0072 3.0174 0.0781  -0.2813 -1.4213 1246 ARG A NH1 
9516  N NH2 . ARG A 1246 ? 1.4484 3.0599 3.0561 0.1552  -0.3499 -1.4422 1246 ARG A NH2 
9517  N N   . MET A 1247 ? 1.5114 3.0978 3.2513 0.1143  -0.2822 -1.2540 1247 MET A N   
9518  C CA  . MET A 1247 ? 1.4596 3.0408 3.2195 0.0793  -0.2495 -1.2386 1247 MET A CA  
9519  C C   . MET A 1247 ? 1.4148 2.9852 3.1330 0.0735  -0.2228 -1.1638 1247 MET A C   
9520  O O   . MET A 1247 ? 1.3873 2.9493 3.0783 0.0367  -0.1892 -1.1431 1247 MET A O   
9521  C CB  . MET A 1247 ? 1.4462 3.0337 3.2565 0.0986  -0.2704 -1.2588 1247 MET A CB  
9522  C CG  . MET A 1247 ? 1.4286 3.0147 3.2757 0.0585  -0.2401 -1.2749 1247 MET A CG  
9523  S SD  . MET A 1247 ? 1.6510 3.2503 3.5730 0.0784  -0.2728 -1.3379 1247 MET A SD  
9524  C CE  . MET A 1247 ? 1.4137 3.0255 3.3423 0.0946  -0.3024 -1.4056 1247 MET A CE  
9525  N N   . VAL A 1248 ? 0.7368 2.3075 2.4477 0.1126  -0.2374 -1.1230 1248 VAL A N   
9526  C CA  . VAL A 1248 ? 0.6830 2.2452 2.3531 0.1135  -0.2109 -1.0527 1248 VAL A CA  
9527  C C   . VAL A 1248 ? 0.6135 2.1709 2.2385 0.1026  -0.1958 -1.0292 1248 VAL A C   
9528  O O   . VAL A 1248 ? 0.5602 2.1093 2.1546 0.0822  -0.1637 -0.9814 1248 VAL A O   
9529  C CB  . VAL A 1248 ? 0.3894 1.9517 2.0502 0.1678  -0.2296 -1.0141 1248 VAL A CB  
9530  C CG1 . VAL A 1248 ? 0.3213 1.8744 1.9334 0.1722  -0.1991 -0.9436 1248 VAL A CG1 
9531  C CG2 . VAL A 1248 ? 0.4133 1.9784 2.1173 0.1723  -0.2382 -1.0285 1248 VAL A CG2 
9532  N N   . GLU A 1249 ? 1.1504 2.7126 2.7700 0.1155  -0.2184 -1.0623 1249 GLU A N   
9533  C CA  . GLU A 1249 ? 1.1720 2.7293 2.7517 0.1027  -0.2029 -1.0406 1249 GLU A CA  
9534  C C   . GLU A 1249 ? 1.1797 2.7290 2.7575 0.0439  -0.1678 -1.0468 1249 GLU A C   
9535  O O   . GLU A 1249 ? 1.1760 2.7163 2.7233 0.0232  -0.1391 -1.0004 1249 GLU A O   
9536  C CB  . GLU A 1249 ? 1.2426 2.8062 2.8134 0.1261  -0.2318 -1.0756 1249 GLU A CB  
9537  C CG  . GLU A 1249 ? 1.2915 2.8501 2.8206 0.1171  -0.2164 -1.0483 1249 GLU A CG  
9538  C CD  . GLU A 1249 ? 1.3852 2.9494 2.8952 0.1579  -0.2445 -1.0595 1249 GLU A CD  
9539  O OE1 . GLU A 1249 ? 1.4645 3.0343 2.9835 0.2032  -0.2749 -1.0714 1249 GLU A OE1 
9540  O OE2 . GLU A 1249 ? 1.3826 2.9445 2.8671 0.1455  -0.2355 -1.0547 1249 GLU A OE2 
9541  N N   . THR A 1250 ? 1.1033 2.6552 2.7130 0.0190  -0.1686 -1.1035 1250 THR A N   
9542  C CA  . THR A 1250 ? 1.0573 2.6010 2.6625 -0.0332 -0.1337 -1.1118 1250 THR A CA  
9543  C C   . THR A 1250 ? 0.9580 2.4914 2.5515 -0.0569 -0.1013 -1.0611 1250 THR A C   
9544  O O   . THR A 1250 ? 0.8938 2.4169 2.4510 -0.0802 -0.0762 -1.0214 1250 THR A O   
9545  C CB  . THR A 1250 ? 1.1263 2.6777 2.7721 -0.0499 -0.1362 -1.1815 1250 THR A CB  
9546  O OG1 . THR A 1250 ? 1.1716 2.7276 2.8581 -0.0416 -0.1423 -1.1925 1250 THR A OG1 
9547  C CG2 . THR A 1250 ? 1.1328 2.6953 2.7861 -0.0230 -0.1685 -1.2298 1250 THR A CG2 
9548  N N   . THR A 1251 ? 0.5731 2.1091 2.1960 -0.0501 -0.1027 -1.0619 1251 THR A N   
9549  C CA  . THR A 1251 ? 0.5723 2.0987 2.1834 -0.0726 -0.0712 -1.0172 1251 THR A CA  
9550  C C   . THR A 1251 ? 0.5605 2.0802 2.1248 -0.0621 -0.0580 -0.9468 1251 THR A C   
9551  O O   . THR A 1251 ? 0.5755 2.0846 2.1146 -0.0892 -0.0265 -0.9072 1251 THR A O   
9552  C CB  . THR A 1251 ? 0.5824 2.1138 2.2324 -0.0589 -0.0787 -1.0253 1251 THR A CB  
9553  O OG1 . THR A 1251 ? 0.6063 2.1395 2.2405 -0.0204 -0.0887 -0.9766 1251 THR A OG1 
9554  C CG2 . THR A 1251 ? 0.5766 2.1202 2.2789 -0.0446 -0.1088 -1.0948 1251 THR A CG2 
9555  N N   . ALA A 1252 ? 0.9406 2.4668 2.4920 -0.0202 -0.0814 -0.9317 1252 ALA A N   
9556  C CA  . ALA A 1252 ? 0.9572 2.4784 2.4646 -0.0091 -0.0669 -0.8708 1252 ALA A CA  
9557  C C   . ALA A 1252 ? 0.9698 2.4818 2.4531 -0.0501 -0.0458 -0.8676 1252 ALA A C   
9558  O O   . ALA A 1252 ? 0.9428 2.4448 2.3972 -0.0738 -0.0172 -0.8247 1252 ALA A O   
9559  C CB  . ALA A 1252 ? 0.9765 2.5056 2.4734 0.0440  -0.0947 -0.8627 1252 ALA A CB  
9560  N N   . TYR A 1253 ? 0.8268 2.3415 2.3204 -0.0585 -0.0601 -0.9145 1253 TYR A N   
9561  C CA  . TYR A 1253 ? 0.8615 2.3679 2.3291 -0.0907 -0.0441 -0.9109 1253 TYR A CA  
9562  C C   . TYR A 1253 ? 0.8680 2.3622 2.3256 -0.1399 -0.0109 -0.9021 1253 TYR A C   
9563  O O   . TYR A 1253 ? 0.8980 2.3828 2.3243 -0.1641 0.0070  -0.8754 1253 TYR A O   
9564  C CB  . TYR A 1253 ? 0.9091 2.4211 2.3888 -0.0900 -0.0644 -0.9676 1253 TYR A CB  
9565  C CG  . TYR A 1253 ? 0.9432 2.4631 2.4126 -0.0474 -0.0915 -0.9628 1253 TYR A CG  
9566  C CD1 . TYR A 1253 ? 0.9355 2.4518 2.3714 -0.0380 -0.0838 -0.9138 1253 TYR A CD1 
9567  C CD2 . TYR A 1253 ? 0.9622 2.4937 2.4549 -0.0149 -0.1246 -1.0079 1253 TYR A CD2 
9568  C CE1 . TYR A 1253 ? 0.9273 2.4512 2.3532 0.0034  -0.1060 -0.9096 1253 TYR A CE1 
9569  C CE2 . TYR A 1253 ? 0.9639 2.5021 2.4426 0.0255  -0.1488 -1.0032 1253 TYR A CE2 
9570  C CZ  . TYR A 1253 ? 0.9493 2.4836 2.3947 0.0348  -0.1381 -0.9539 1253 TYR A CZ  
9571  O OH  . TYR A 1253 ? 0.9900 2.5303 2.4209 0.0772  -0.1585 -0.9484 1253 TYR A OH  
9572  N N   . ALA A 1254 ? 1.2844 2.7790 2.7684 -0.1532 -0.0034 -0.9243 1254 ALA A N   
9573  C CA  . ALA A 1254 ? 1.2142 2.6981 2.6877 -0.1972 0.0289  -0.9161 1254 ALA A CA  
9574  C C   . ALA A 1254 ? 1.1869 2.6633 2.6370 -0.1962 0.0472  -0.8557 1254 ALA A C   
9575  O O   . ALA A 1254 ? 1.1572 2.6223 2.5748 -0.2258 0.0727  -0.8227 1254 ALA A O   
9576  C CB  . ALA A 1254 ? 1.1864 2.6757 2.7005 -0.2119 0.0308  -0.9710 1254 ALA A CB  
9577  N N   . LEU A 1255 ? 0.4487 1.9323 1.9135 -0.1611 0.0341  -0.8420 1255 LEU A N   
9578  C CA  . LEU A 1255 ? 0.4961 1.9743 1.9356 -0.1552 0.0522  -0.7843 1255 LEU A CA  
9579  C C   . LEU A 1255 ? 0.4722 1.9451 1.8661 -0.1513 0.0626  -0.7310 1255 LEU A C   
9580  O O   . LEU A 1255 ? 0.4337 1.8973 1.7946 -0.1667 0.0871  -0.6849 1255 LEU A O   
9581  C CB  . LEU A 1255 ? 0.5422 2.0307 2.0031 -0.1128 0.0344  -0.7798 1255 LEU A CB  
9582  C CG  . LEU A 1255 ? 0.5417 2.0265 1.9682 -0.0967 0.0519  -0.7165 1255 LEU A CG  
9583  C CD1 . LEU A 1255 ? 0.5446 2.0158 1.9463 -0.1374 0.0855  -0.6902 1255 LEU A CD1 
9584  C CD2 . LEU A 1255 ? 0.5293 2.0230 1.9768 -0.0586 0.0376  -0.7154 1255 LEU A CD2 
9585  N N   . LEU A 1256 ? 0.9459 2.4251 2.3384 -0.1298 0.0434  -0.7386 1256 LEU A N   
9586  C CA  . LEU A 1256 ? 1.0054 2.4804 2.3610 -0.1273 0.0525  -0.6946 1256 LEU A CA  
9587  C C   . LEU A 1256 ? 1.0553 2.5178 2.3907 -0.1751 0.0724  -0.6914 1256 LEU A C   
9588  O O   . LEU A 1256 ? 1.0754 2.5299 2.3771 -0.1870 0.0924  -0.6428 1256 LEU A O   
9589  C CB  . LEU A 1256 ? 1.0275 2.5121 2.3879 -0.0925 0.0270  -0.7072 1256 LEU A CB  
9590  C CG  . LEU A 1256 ? 1.0263 2.5216 2.3910 -0.0371 0.0092  -0.6946 1256 LEU A CG  
9591  C CD1 . LEU A 1256 ? 1.0610 2.5630 2.4263 -0.0094 -0.0138 -0.7114 1256 LEU A CD1 
9592  C CD2 . LEU A 1256 ? 0.9796 2.4710 2.3108 -0.0206 0.0307  -0.6325 1256 LEU A CD2 
9593  N N   . THR A 1257 ? 0.4594 1.9206 1.8127 -0.2009 0.0674  -0.7425 1257 THR A N   
9594  C CA  . THR A 1257 ? 0.4415 1.8914 1.7715 -0.2437 0.0862  -0.7383 1257 THR A CA  
9595  C C   . THR A 1257 ? 0.3920 1.8326 1.7012 -0.2664 0.1124  -0.7026 1257 THR A C   
9596  O O   . THR A 1257 ? 0.3553 1.7887 1.6296 -0.2746 0.1264  -0.6532 1257 THR A O   
9597  C CB  . THR A 1257 ? 0.3199 1.7706 1.6683 -0.2701 0.0831  -0.7994 1257 THR A CB  
9598  O OG1 . THR A 1257 ? 0.3298 1.7927 1.7150 -0.2434 0.0584  -0.8481 1257 THR A OG1 
9599  C CG2 . THR A 1257 ? 0.3105 1.7561 1.6349 -0.2884 0.0844  -0.7957 1257 THR A CG2 
9600  N N   . SER A 1258 ? 0.6894 2.1310 2.0201 -0.2735 0.1180  -0.7261 1258 SER A N   
9601  C CA  . SER A 1258 ? 0.7409 2.1739 2.0519 -0.2935 0.1423  -0.6956 1258 SER A CA  
9602  C C   . SER A 1258 ? 0.7359 2.1645 2.0102 -0.2788 0.1525  -0.6291 1258 SER A C   
9603  O O   . SER A 1258 ? 0.7283 2.1475 1.9683 -0.3034 0.1718  -0.5958 1258 SER A O   
9604  C CB  . SER A 1258 ? 0.7523 2.1898 2.0970 -0.2866 0.1415  -0.7227 1258 SER A CB  
9605  O OG  . SER A 1258 ? 0.7766 2.2187 2.1552 -0.3039 0.1374  -0.7844 1258 SER A OG  
9606  N N   . LEU A 1259 ? 0.5019 1.9389 1.7828 -0.2372 0.1394  -0.6119 1259 LEU A N   
9607  C CA  . LEU A 1259 ? 0.4642 1.9004 1.7120 -0.2149 0.1494  -0.5520 1259 LEU A CA  
9608  C C   . LEU A 1259 ? 0.4661 1.8987 1.6812 -0.2178 0.1548  -0.5140 1259 LEU A C   
9609  O O   . LEU A 1259 ? 0.4553 1.8850 1.6375 -0.2087 0.1688  -0.4632 1259 LEU A O   
9610  C CB  . LEU A 1259 ? 0.3914 1.8394 1.6556 -0.1669 0.1336  -0.5504 1259 LEU A CB  
9611  C CG  . LEU A 1259 ? 0.3448 1.7947 1.6267 -0.1594 0.1360  -0.5597 1259 LEU A CG  
9612  C CD1 . LEU A 1259 ? 0.3497 1.8126 1.6492 -0.1093 0.1157  -0.5632 1259 LEU A CD1 
9613  C CD2 . LEU A 1259 ? 0.3166 1.7566 1.5609 -0.1718 0.1629  -0.5129 1259 LEU A CD2 
9614  N N   . ASN A 1260 ? 0.6603 2.0936 1.8857 -0.2295 0.1434  -0.5407 1260 ASN A N   
9615  C CA  . ASN A 1260 ? 0.6941 2.1213 1.8936 -0.2487 0.1502  -0.5154 1260 ASN A CA  
9616  C C   . ASN A 1260 ? 0.7551 2.1708 1.9305 -0.2924 0.1700  -0.5039 1260 ASN A C   
9617  O O   . ASN A 1260 ? 0.8014 2.2123 1.9444 -0.2998 0.1830  -0.4574 1260 ASN A O   
9618  C CB  . ASN A 1260 ? 0.6712 2.1013 1.8894 -0.2537 0.1328  -0.5552 1260 ASN A CB  
9619  C CG  . ASN A 1260 ? 0.6791 2.1159 1.8947 -0.2225 0.1211  -0.5356 1260 ASN A CG  
9620  O OD1 . ASN A 1260 ? 0.7050 2.1396 1.8958 -0.2180 0.1313  -0.4885 1260 ASN A OD1 
9621  N ND2 . ASN A 1260 ? 0.6611 2.1069 1.9023 -0.1996 0.0994  -0.5729 1260 ASN A ND2 
9622  N N   . LEU A 1261 ? 0.7759 2.1888 1.9668 -0.3201 0.1723  -0.5473 1261 LEU A N   
9623  C CA  . LEU A 1261 ? 0.7375 2.1419 1.9052 -0.3613 0.1901  -0.5422 1261 LEU A CA  
9624  C C   . LEU A 1261 ? 0.7360 2.1362 1.8860 -0.3652 0.2073  -0.5143 1261 LEU A C   
9625  O O   . LEU A 1261 ? 0.7471 2.1419 1.8768 -0.3972 0.2222  -0.5097 1261 LEU A O   
9626  C CB  . LEU A 1261 ? 0.7043 2.1097 1.8938 -0.3883 0.1883  -0.6018 1261 LEU A CB  
9627  C CG  . LEU A 1261 ? 0.6708 2.0801 1.8743 -0.3839 0.1712  -0.6307 1261 LEU A CG  
9628  C CD1 . LEU A 1261 ? 0.7028 2.1150 1.9250 -0.4104 0.1718  -0.6920 1261 LEU A CD1 
9629  C CD2 . LEU A 1261 ? 0.6272 2.0317 1.8001 -0.3903 0.1718  -0.5889 1261 LEU A CD2 
9630  N N   . LYS A 1262 ? 0.4075 1.8113 1.5633 -0.3319 0.2049  -0.4961 1262 LYS A N   
9631  C CA  . LYS A 1262 ? 0.3979 1.7975 1.5312 -0.3302 0.2209  -0.4625 1262 LYS A CA  
9632  C C   . LYS A 1262 ? 0.3681 1.7640 1.5127 -0.3554 0.2315  -0.4926 1262 LYS A C   
9633  O O   . LYS A 1262 ? 0.3693 1.7597 1.4889 -0.3673 0.2472  -0.4681 1262 LYS A O   
9634  C CB  . LYS A 1262 ? 0.4632 1.8582 1.5518 -0.3383 0.2327  -0.4081 1262 LYS A CB  
9635  C CG  . LYS A 1262 ? 0.5612 1.9611 1.6444 -0.3137 0.2228  -0.3825 1262 LYS A CG  
9636  C CD  . LYS A 1262 ? 0.6651 2.0664 1.7177 -0.2865 0.2317  -0.3267 1262 LYS A CD  
9637  C CE  . LYS A 1262 ? 0.7105 2.1193 1.7680 -0.2543 0.2216  -0.3119 1262 LYS A CE  
9638  N NZ  . LYS A 1262 ? 0.7142 2.1307 1.8093 -0.2300 0.2043  -0.3522 1262 LYS A NZ  
9639  N N   . ASP A 1263 ? 0.5348 1.9352 1.7193 -0.3602 0.2219  -0.5479 1263 ASP A N   
9640  C CA  . ASP A 1263 ? 0.5651 1.9651 1.7728 -0.3805 0.2300  -0.5886 1263 ASP A CA  
9641  C C   . ASP A 1263 ? 0.5262 1.9263 1.7464 -0.3630 0.2343  -0.5823 1263 ASP A C   
9642  O O   . ASP A 1263 ? 0.5815 1.9855 1.8400 -0.3641 0.2323  -0.6237 1263 ASP A O   
9643  C CB  . ASP A 1263 ? 0.5883 1.9964 1.8400 -0.3795 0.2145  -0.6487 1263 ASP A CB  
9644  C CG  . ASP A 1263 ? 0.9549 2.3639 2.2213 -0.4137 0.2263  -0.6941 1263 ASP A CG  
9645  O OD1 . ASP A 1263 ? 0.9531 2.3605 2.2268 -0.4222 0.2392  -0.6993 1263 ASP A OD1 
9646  O OD2 . ASP A 1263 ? 0.9426 2.3549 2.2122 -0.4321 0.2239  -0.7242 1263 ASP A OD2 
9647  N N   . ILE A 1264 ? 0.2107 1.6072 1.3982 -0.3464 0.2408  -0.5299 1264 ILE A N   
9648  C CA  . ILE A 1264 ? 0.2325 1.6294 1.4246 -0.3247 0.2445  -0.5155 1264 ILE A CA  
9649  C C   . ILE A 1264 ? 0.2785 1.6765 1.5088 -0.3317 0.2474  -0.5553 1264 ILE A C   
9650  O O   . ILE A 1264 ? 0.2822 1.6837 1.5278 -0.3065 0.2435  -0.5504 1264 ILE A O   
9651  C CB  . ILE A 1264 ? 0.2077 1.5971 1.3468 -0.3252 0.2615  -0.4569 1264 ILE A CB  
9652  C CG1 . ILE A 1264 ? 0.4192 1.8103 1.5293 -0.3105 0.2566  -0.4188 1264 ILE A CG1 
9653  C CG2 . ILE A 1264 ? 0.2349 1.6232 1.3713 -0.3039 0.2684  -0.4390 1264 ILE A CG2 
9654  C CD1 . ILE A 1264 ? 0.4171 1.8027 1.4757 -0.3112 0.2713  -0.3636 1264 ILE A CD1 
9655  N N   . ASN A 1265 ? 0.4518 1.8483 1.6992 -0.3636 0.2546  -0.5951 1265 ASN A N   
9656  C CA  . ASN A 1265 ? 0.5383 1.9364 1.8222 -0.3659 0.2592  -0.6265 1265 ASN A CA  
9657  C C   . ASN A 1265 ? 0.5420 1.9507 1.8843 -0.3610 0.2423  -0.6877 1265 ASN A C   
9658  O O   . ASN A 1265 ? 0.5544 1.9684 1.9406 -0.3522 0.2378  -0.7185 1265 ASN A O   
9659  C CB  . ASN A 1265 ? 0.6159 2.0062 1.8809 -0.4018 0.2834  -0.6277 1265 ASN A CB  
9660  C CG  . ASN A 1265 ? 0.6874 2.0699 1.9237 -0.3947 0.2975  -0.5852 1265 ASN A CG  
9661  O OD1 . ASN A 1265 ? 0.7177 2.1023 1.9681 -0.3652 0.2908  -0.5738 1265 ASN A OD1 
9662  N ND2 . ASN A 1265 ? 0.7117 2.0867 1.9067 -0.4216 0.3164  -0.5632 1265 ASN A ND2 
9663  N N   . TYR A 1266 ? 0.4382 1.8507 1.7811 -0.3665 0.2321  -0.7058 1266 TYR A N   
9664  C CA  . TYR A 1266 ? 0.4261 1.8500 1.8206 -0.3595 0.2135  -0.7652 1266 TYR A CA  
9665  C C   . TYR A 1266 ? 0.4399 1.8723 1.8616 -0.3166 0.1886  -0.7636 1266 TYR A C   
9666  O O   . TYR A 1266 ? 0.4858 1.9294 1.9586 -0.3027 0.1697  -0.8126 1266 TYR A O   
9667  C CB  . TYR A 1266 ? 0.3607 1.7867 1.7434 -0.3684 0.2056  -0.7778 1266 TYR A CB  
9668  C CG  . TYR A 1266 ? 0.3125 1.7505 1.7433 -0.3689 0.1917  -0.8447 1266 TYR A CG  
9669  C CD1 . TYR A 1266 ? 0.3237 1.7687 1.7987 -0.3767 0.1959  -0.8913 1266 TYR A CD1 
9670  C CD2 . TYR A 1266 ? 0.2784 1.7215 1.7102 -0.3623 0.1756  -0.8623 1266 TYR A CD2 
9671  C CE1 . TYR A 1266 ? 0.3594 1.8177 1.8789 -0.3771 0.1848  -0.9547 1266 TYR A CE1 
9672  C CE2 . TYR A 1266 ? 0.2883 1.7438 1.7615 -0.3633 0.1643  -0.9260 1266 TYR A CE2 
9673  C CZ  . TYR A 1266 ? 0.3338 1.7977 1.8513 -0.3701 0.1690  -0.9723 1266 TYR A CZ  
9674  O OH  . TYR A 1266 ? 0.3454 1.8246 1.9068 -0.3700 0.1592  -1.0377 1266 TYR A OH  
9675  N N   . VAL A 1267 ? 0.3425 1.7718 1.7286 -0.2945 0.1877  -0.7085 1267 VAL A N   
9676  C CA  . VAL A 1267 ? 0.2457 1.6854 1.6449 -0.2511 0.1631  -0.7003 1267 VAL A CA  
9677  C C   . VAL A 1267 ? 0.2421 1.6878 1.6637 -0.2219 0.1567  -0.6935 1267 VAL A C   
9678  O O   . VAL A 1267 ? 0.2269 1.6852 1.6855 -0.1905 0.1307  -0.7184 1267 VAL A O   
9679  C CB  . VAL A 1267 ? 0.2074 1.6441 1.5588 -0.2397 0.1645  -0.6502 1267 VAL A CB  
9680  C CG1 . VAL A 1267 ? 0.1877 1.6307 1.5295 -0.1978 0.1573  -0.6140 1267 VAL A CG1 
9681  C CG2 . VAL A 1267 ? 0.1798 1.6207 1.5372 -0.2407 0.1487  -0.6743 1267 VAL A CG2 
9682  N N   . ASN A 1268 ? 0.4982 1.9351 1.8985 -0.2337 0.1794  -0.6641 1268 ASN A N   
9683  C CA  . ASN A 1268 ? 0.6011 2.0416 2.0147 -0.2099 0.1788  -0.6511 1268 ASN A CA  
9684  C C   . ASN A 1268 ? 0.6230 2.0760 2.1017 -0.1900 0.1567  -0.6973 1268 ASN A C   
9685  O O   . ASN A 1268 ? 0.6730 2.1303 2.1592 -0.1645 0.1536  -0.6807 1268 ASN A O   
9686  C CB  . ASN A 1268 ? 0.6947 2.1212 2.0759 -0.2370 0.2095  -0.6228 1268 ASN A CB  
9687  C CG  . ASN A 1268 ? 0.7754 2.1910 2.0913 -0.2497 0.2275  -0.5721 1268 ASN A CG  
9688  O OD1 . ASN A 1268 ? 0.7825 2.2019 2.0750 -0.2268 0.2194  -0.5444 1268 ASN A OD1 
9689  N ND2 . ASN A 1268 ? 0.8197 2.2229 2.1069 -0.2843 0.2506  -0.5608 1268 ASN A ND2 
9690  N N   . PRO A 1269 ? 0.3945 1.8532 1.9194 -0.2028 0.1430  -0.7557 1269 PRO A N   
9691  C CA  . PRO A 1269 ? 0.3680 1.8401 1.9602 -0.1843 0.1165  -0.8089 1269 PRO A CA  
9692  C C   . PRO A 1269 ? 0.3110 1.7934 1.9253 -0.1705 0.0877  -0.8475 1269 PRO A C   
9693  O O   . PRO A 1269 ? 0.2893 1.7816 1.9579 -0.1651 0.0669  -0.9035 1269 PRO A O   
9694  C CB  . PRO A 1269 ? 0.4366 1.9036 2.0568 -0.2228 0.1354  -0.8479 1269 PRO A CB  
9695  C CG  . PRO A 1269 ? 0.4651 1.9155 2.0246 -0.2612 0.1708  -0.8119 1269 PRO A CG  
9696  C CD  . PRO A 1269 ? 0.4321 1.8806 1.9449 -0.2479 0.1650  -0.7729 1269 PRO A CD  
9697  N N   . VAL A 1270 ? 0.3751 1.8543 1.9458 -0.1675 0.0884  -0.8190 1270 VAL A N   
9698  C CA  . VAL A 1270 ? 0.3219 1.8115 1.9022 -0.1397 0.0577  -0.8383 1270 VAL A CA  
9699  C C   . VAL A 1270 ? 0.2593 1.7558 1.8260 -0.0928 0.0422  -0.7998 1270 VAL A C   
9700  O O   . VAL A 1270 ? 0.2805 1.7893 1.8787 -0.0549 0.0092  -0.8233 1270 VAL A O   
9701  C CB  . VAL A 1270 ? 0.2999 1.7829 1.8415 -0.1591 0.0664  -0.8280 1270 VAL A CB  
9702  C CG1 . VAL A 1270 ? 0.2535 1.7458 1.7900 -0.1220 0.0384  -0.8255 1270 VAL A CG1 
9703  C CG2 . VAL A 1270 ? 0.3291 1.8105 1.8912 -0.1939 0.0718  -0.8803 1270 VAL A CG2 
9704  N N   . ILE A 1271 ? 0.2079 1.6963 1.7249 -0.0925 0.0660  -0.7406 1271 ILE A N   
9705  C CA  . ILE A 1271 ? 0.1796 1.6742 1.6776 -0.0450 0.0561  -0.7026 1271 ILE A CA  
9706  C C   . ILE A 1271 ? 0.1793 1.6784 1.7020 -0.0228 0.0512  -0.7016 1271 ILE A C   
9707  O O   . ILE A 1271 ? 0.2103 1.7136 1.7174 0.0205  0.0418  -0.6746 1271 ILE A O   
9708  C CB  . ILE A 1271 ? 0.1997 1.6863 1.6309 -0.0400 0.0798  -0.6385 1271 ILE A CB  
9709  C CG1 . ILE A 1271 ? 0.2000 1.6754 1.5968 -0.0590 0.1138  -0.5960 1271 ILE A CG1 
9710  C CG2 . ILE A 1271 ? 0.1968 1.6793 1.6056 -0.0594 0.0831  -0.6365 1271 ILE A CG2 
9711  C CD1 . ILE A 1271 ? 0.2138 1.6929 1.6139 -0.0264 0.1130  -0.5795 1271 ILE A CD1 
9712  N N   . LYS A 1272 ? 0.5372 2.0340 2.0946 -0.0501 0.0594  -0.7285 1272 LYS A N   
9713  C CA  . LYS A 1272 ? 0.6322 2.1346 2.2176 -0.0250 0.0508  -0.7290 1272 LYS A CA  
9714  C C   . LYS A 1272 ? 0.6824 2.1991 2.3160 0.0151  0.0053  -0.7712 1272 LYS A C   
9715  O O   . LYS A 1272 ? 0.7198 2.2423 2.3685 0.0555  -0.0140 -0.7664 1272 LYS A O   
9716  C CB  . LYS A 1272 ? 0.6837 2.1800 2.2985 -0.0626 0.0707  -0.7492 1272 LYS A CB  
9717  C CG  . LYS A 1272 ? 0.6836 2.1905 2.3605 -0.0398 0.0472  -0.7822 1272 LYS A CG  
9718  C CD  . LYS A 1272 ? 0.6877 2.1926 2.3492 -0.0197 0.0600  -0.7415 1272 LYS A CD  
9719  C CE  . LYS A 1272 ? 0.7425 2.2539 2.4697 -0.0155 0.0468  -0.7772 1272 LYS A CE  
9720  N NZ  . LYS A 1272 ? 0.7792 2.2864 2.4871 -0.0026 0.0653  -0.7369 1272 LYS A NZ  
9721  N N   . TRP A 1273 ? 0.5862 2.1067 2.2385 0.0055  -0.0123 -0.8116 1273 TRP A N   
9722  C CA  . TRP A 1273 ? 0.5510 2.0837 2.2527 0.0352  -0.0562 -0.8630 1273 TRP A CA  
9723  C C   . TRP A 1273 ? 0.4986 2.0356 2.1764 0.0748  -0.0834 -0.8573 1273 TRP A C   
9724  O O   . TRP A 1273 ? 0.5367 2.0815 2.2404 0.1165  -0.1231 -0.8831 1273 TRP A O   
9725  C CB  . TRP A 1273 ? 0.5519 2.0853 2.2946 -0.0041 -0.0556 -0.9218 1273 TRP A CB  
9726  C CG  . TRP A 1273 ? 0.5641 2.1081 2.3458 0.0137  -0.0948 -0.9803 1273 TRP A CG  
9727  C CD1 . TRP A 1273 ? 0.6113 2.1648 2.4553 0.0262  -0.1236 -1.0342 1273 TRP A CD1 
9728  C CD2 . TRP A 1273 ? 0.5570 2.1026 2.3185 0.0169  -0.1075 -0.9953 1273 TRP A CD2 
9729  N NE1 . TRP A 1273 ? 0.6186 2.1795 2.4786 0.0384  -0.1537 -1.0812 1273 TRP A NE1 
9730  C CE2 . TRP A 1273 ? 0.5818 2.1380 2.3914 0.0326  -0.1438 -1.0585 1273 TRP A CE2 
9731  C CE3 . TRP A 1273 ? 0.5522 2.0915 2.2605 0.0091  -0.0922 -0.9617 1273 TRP A CE3 
9732  C CZ2 . TRP A 1273 ? 0.6034 2.1636 2.4047 0.0400  -0.1636 -1.0888 1273 TRP A CZ2 
9733  C CZ3 . TRP A 1273 ? 0.5691 2.1126 2.2735 0.0161  -0.1123 -0.9914 1273 TRP A CZ3 
9734  C CH2 . TRP A 1273 ? 0.5926 2.1463 2.3411 0.0311  -0.1468 -1.0543 1273 TRP A CH2 
9735  N N   . LEU A 1274 ? 0.2612 1.7920 1.8889 0.0635  -0.0633 -0.8240 1274 LEU A N   
9736  C CA  . LEU A 1274 ? 0.3203 1.8526 1.9161 0.1083  -0.0825 -0.8033 1274 LEU A CA  
9737  C C   . LEU A 1274 ? 0.3981 1.9282 1.9801 0.1550  -0.0881 -0.7689 1274 LEU A C   
9738  O O   . LEU A 1274 ? 0.4444 1.9774 2.0488 0.1987  -0.1241 -0.7894 1274 LEU A O   
9739  C CB  . LEU A 1274 ? 0.3604 1.8858 1.9044 0.0908  -0.0570 -0.7669 1274 LEU A CB  
9740  C CG  . LEU A 1274 ? 0.4055 1.9325 1.9608 0.0619  -0.0639 -0.8063 1274 LEU A CG  
9741  C CD1 . LEU A 1274 ? 0.4074 1.9327 1.9230 0.0771  -0.0645 -0.7824 1274 LEU A CD1 
9742  C CD2 . LEU A 1274 ? 0.4290 1.9658 2.0340 0.0763  -0.1013 -0.8679 1274 LEU A CD2 
9743  N N   . SER A 1275 ? 0.1085 1.6309 1.6531 0.1451  -0.0529 -0.7194 1275 SER A N   
9744  C CA  . SER A 1275 ? 0.1870 1.7041 1.7115 0.1873  -0.0527 -0.6859 1275 SER A CA  
9745  C C   . SER A 1275 ? 0.2074 1.7280 1.7793 0.2126  -0.0796 -0.7127 1275 SER A C   
9746  O O   . SER A 1275 ? 0.2060 1.7198 1.7606 0.2364  -0.0709 -0.6833 1275 SER A O   
9747  C CB  . SER A 1275 ? 0.2847 1.7934 1.7622 0.1628  -0.0062 -0.6336 1275 SER A CB  
9748  O OG  . SER A 1275 ? 0.3617 1.8635 1.8143 0.2030  -0.0031 -0.6027 1275 SER A OG  
9749  N N   . GLU A 1276 ? 0.6856 2.2156 2.3148 0.2095  -0.1124 -0.7684 1276 GLU A N   
9750  C CA  . GLU A 1276 ? 0.7786 2.3108 2.4514 0.2455  -0.1476 -0.7946 1276 GLU A CA  
9751  C C   . GLU A 1276 ? 0.8024 2.3402 2.5075 0.2710  -0.1956 -0.8443 1276 GLU A C   
9752  O O   . GLU A 1276 ? 0.8597 2.3972 2.5987 0.3081  -0.2343 -0.8701 1276 GLU A O   
9753  C CB  . GLU A 1276 ? 0.8325 2.3707 2.5541 0.2071  -0.1330 -0.8147 1276 GLU A CB  
9754  C CG  . GLU A 1276 ? 0.8534 2.3842 2.5391 0.1882  -0.0882 -0.7643 1276 GLU A CG  
9755  C CD  . GLU A 1276 ? 0.8392 2.3733 2.5713 0.1488  -0.0715 -0.7848 1276 GLU A CD  
9756  O OE1 . GLU A 1276 ? 0.8233 2.3648 2.6127 0.1274  -0.0885 -0.8391 1276 GLU A OE1 
9757  O OE2 . GLU A 1276 ? 0.8431 2.3710 2.5527 0.1400  -0.0407 -0.7485 1276 GLU A OE2 
9758  N N   . GLU A 1277 ? 1.3828 2.9243 3.0745 0.2502  -0.1924 -0.8574 1277 GLU A N   
9759  C CA  . GLU A 1277 ? 1.4135 2.9582 3.1148 0.2775  -0.2325 -0.8946 1277 GLU A CA  
9760  C C   . GLU A 1277 ? 1.4321 2.9617 3.0810 0.3383  -0.2487 -0.8591 1277 GLU A C   
9761  O O   . GLU A 1277 ? 1.4668 2.9883 3.1232 0.3886  -0.2886 -0.8730 1277 GLU A O   
9762  C CB  . GLU A 1277 ? 1.3915 2.9421 3.0868 0.2343  -0.2178 -0.9146 1277 GLU A CB  
9763  C CG  . GLU A 1277 ? 1.4064 2.9665 3.1412 0.2356  -0.2538 -0.9790 1277 GLU A CG  
9764  C CD  . GLU A 1277 ? 1.4347 3.0024 3.2344 0.2259  -0.2707 -1.0261 1277 GLU A CD  
9765  O OE1 . GLU A 1277 ? 1.4702 3.0461 3.3062 0.2289  -0.3016 -1.0839 1277 GLU A OE1 
9766  O OE2 . GLU A 1277 ? 1.4354 3.0009 3.2500 0.2152  -0.2523 -1.0068 1277 GLU A OE2 
9767  N N   . GLN A 1278 ? 0.6323 2.1542 2.2255 0.3336  -0.2169 -0.8130 1278 GLN A N   
9768  C CA  . GLN A 1278 ? 0.7134 2.2159 2.2480 0.3872  -0.2241 -0.7776 1278 GLN A CA  
9769  C C   . GLN A 1278 ? 0.8096 2.2923 2.3375 0.4489  -0.2568 -0.7732 1278 GLN A C   
9770  O O   . GLN A 1278 ? 0.8134 2.2939 2.3576 0.4500  -0.2523 -0.7648 1278 GLN A O   
9771  C CB  . GLN A 1278 ? 0.7869 2.2814 2.2653 0.3737  -0.1777 -0.7205 1278 GLN A CB  
9772  C CG  . GLN A 1278 ? 1.1520 2.6578 2.6239 0.3231  -0.1505 -0.7188 1278 GLN A CG  
9773  C CD  . GLN A 1278 ? 0.5714 2.0854 2.0625 0.3204  -0.1773 -0.7619 1278 GLN A CD  
9774  O OE1 . GLN A 1278 ? 0.5460 2.0573 2.0060 0.3193  -0.1679 -0.7484 1278 GLN A OE1 
9775  N NE2 . GLN A 1278 ? 0.5670 2.0915 2.1096 0.3169  -0.2089 -0.8151 1278 GLN A NE2 
9776  N N   . ARG A 1279 ? 0.8921 2.3353 2.3705 0.4929  -0.2893 -0.7799 1279 ARG A N   
9777  C CA  . ARG A 1279 ? 0.9639 2.3512 2.3982 0.5412  -0.3240 -0.7787 1279 ARG A CA  
9778  C C   . ARG A 1279 ? 0.9617 2.2897 2.2940 0.5735  -0.3111 -0.7264 1279 ARG A C   
9779  O O   . ARG A 1279 ? 0.9542 2.2646 2.2298 0.5791  -0.2971 -0.7045 1279 ARG A O   
9780  C CB  . ARG A 1279 ? 1.0759 2.4486 2.5173 0.5657  -0.3729 -0.8249 1279 ARG A CB  
9781  C CG  . ARG A 1279 ? 1.0773 2.5043 2.6239 0.5380  -0.3914 -0.8815 1279 ARG A CG  
9782  C CD  . ARG A 1279 ? 1.2105 2.6192 2.7677 0.5692  -0.4445 -0.9278 1279 ARG A CD  
9783  N NE  . ARG A 1279 ? 1.3537 2.6929 2.8279 0.6219  -0.4695 -0.9031 1279 ARG A NE  
9784  C CZ  . ARG A 1279 ? 1.4598 2.7725 2.9305 0.6562  -0.5169 -0.9331 1279 ARG A CZ  
9785  N NH1 . ARG A 1279 ? 1.4315 2.7832 2.9787 0.6444  -0.5433 -0.9906 1279 ARG A NH1 
9786  N NH2 . ARG A 1279 ? 1.5815 2.8297 2.9727 0.7003  -0.5377 -0.9065 1279 ARG A NH2 
9787  N N   . TYR A 1280 ? 1.3932 2.6911 2.7040 0.5925  -0.3150 -0.7080 1280 TYR A N   
9788  C CA  . TYR A 1280 ? 1.4643 2.7066 2.6787 0.6184  -0.3007 -0.6597 1280 TYR A CA  
9789  C C   . TYR A 1280 ? 1.2641 2.4757 2.4087 0.6354  -0.3018 -0.6465 1280 TYR A C   
9790  O O   . TYR A 1280 ? 1.2858 2.4810 2.4241 0.6551  -0.3367 -0.6736 1280 TYR A O   
9791  C CB  . TYR A 1280 ? 1.5536 2.7416 2.7341 0.6565  -0.3363 -0.6601 1280 TYR A CB  
9792  C CG  . TYR A 1280 ? 1.6221 2.7417 2.6914 0.6875  -0.3330 -0.6182 1280 TYR A CG  
9793  C CD1 . TYR A 1280 ? 1.7873 2.8444 2.8041 0.7279  -0.3756 -0.6208 1280 TYR A CD1 
9794  C CD2 . TYR A 1280 ? 1.5559 2.6735 2.5723 0.6750  -0.2885 -0.5776 1280 TYR A CD2 
9795  C CE1 . TYR A 1280 ? 1.8838 2.8772 2.7971 0.7523  -0.3739 -0.5849 1280 TYR A CE1 
9796  C CE2 . TYR A 1280 ? 1.6812 2.7368 2.5957 0.7007  -0.2858 -0.5435 1280 TYR A CE2 
9797  C CZ  . TYR A 1280 ? 1.8406 2.8335 2.7030 0.7381  -0.3288 -0.5477 1280 TYR A CZ  
9798  O OH  . TYR A 1280 ? 1.9576 2.8872 2.7164 0.7602  -0.3276 -0.5159 1280 TYR A OH  
9799  N N   . GLY A 1281 ? 0.4216 1.6287 1.5168 0.6264  -0.2624 -0.6066 1281 GLY A N   
9800  C CA  . GLY A 1281 ? 0.4443 1.6308 1.4845 0.6365  -0.2583 -0.5954 1281 GLY A CA  
9801  C C   . GLY A 1281 ? 0.3816 1.6203 1.4676 0.6022  -0.2344 -0.6037 1281 GLY A C   
9802  O O   . GLY A 1281 ? 0.3778 1.6257 1.4392 0.5876  -0.1973 -0.5722 1281 GLY A O   
9803  N N   . GLY A 1282 ? 0.7998 2.0720 1.9504 0.5887  -0.2557 -0.6465 1282 GLY A N   
9804  C CA  . GLY A 1282 ? 0.8180 2.1315 2.0024 0.5577  -0.2377 -0.6564 1282 GLY A CA  
9805  C C   . GLY A 1282 ? 0.9311 2.2965 2.2084 0.5283  -0.2532 -0.7044 1282 GLY A C   
9806  O O   . GLY A 1282 ? 0.9402 2.3105 2.2570 0.5331  -0.2759 -0.7282 1282 GLY A O   
9807  N N   . GLY A 1283 ? 0.3868 1.7897 1.6989 0.4971  -0.2423 -0.7209 1283 GLY A N   
9808  C CA  . GLY A 1283 ? 0.4467 1.9063 1.8506 0.4579  -0.2492 -0.7651 1283 GLY A CA  
9809  C C   . GLY A 1283 ? 0.4892 1.9526 1.9315 0.4679  -0.2936 -0.8221 1283 GLY A C   
9810  O O   . GLY A 1283 ? 0.4071 1.9077 1.8988 0.4383  -0.2996 -0.8609 1283 GLY A O   
9811  N N   . PHE A 1284 ? 1.2780 2.7043 2.6991 0.5071  -0.3245 -0.8286 1284 PHE A N   
9812  C CA  . PHE A 1284 ? 1.4687 2.8849 2.9032 0.5292  -0.3704 -0.8777 1284 PHE A CA  
9813  C C   . PHE A 1284 ? 1.3354 2.7772 2.7920 0.5109  -0.3807 -0.9199 1284 PHE A C   
9814  O O   . PHE A 1284 ? 1.4243 2.8361 2.8222 0.5319  -0.3863 -0.9150 1284 PHE A O   
9815  C CB  . PHE A 1284 ? 1.7502 3.1855 3.2518 0.5274  -0.3944 -0.9102 1284 PHE A CB  
9816  C CG  . PHE A 1284 ? 2.1933 3.5967 3.6819 0.5682  -0.4440 -0.9435 1284 PHE A CG  
9817  C CD1 . PHE A 1284 ? 2.4694 3.8094 3.8734 0.6159  -0.4608 -0.9158 1284 PHE A CD1 
9818  C CD2 . PHE A 1284 ? 2.3608 3.7983 3.9217 0.5575  -0.4740 -1.0032 1284 PHE A CD2 
9819  C CE1 . PHE A 1284 ? 2.7282 4.0395 4.1195 0.6523  -0.5068 -0.9445 1284 PHE A CE1 
9820  C CE2 . PHE A 1284 ? 2.5953 4.0052 4.1449 0.5957  -0.5200 -1.0337 1284 PHE A CE2 
9821  C CZ  . PHE A 1284 ? 2.8113 4.1580 4.2757 0.6435  -0.5366 -1.0030 1284 PHE A CZ  
9822  N N   . TYR A 1285 ? 1.1509 2.6474 2.6909 0.4706  -0.3832 -0.9634 1285 TYR A N   
9823  C CA  . TYR A 1285 ? 1.0151 2.5344 2.5774 0.4540  -0.3995 -1.0136 1285 TYR A CA  
9824  C C   . TYR A 1285 ? 0.9620 2.4661 2.4666 0.4518  -0.3801 -0.9928 1285 TYR A C   
9825  O O   . TYR A 1285 ? 0.9562 2.4747 2.4581 0.4242  -0.3439 -0.9589 1285 TYR A O   
9826  C CB  . TYR A 1285 ? 0.9047 2.4625 2.5350 0.3936  -0.3895 -1.0561 1285 TYR A CB  
9827  C CG  . TYR A 1285 ? 0.8862 2.4483 2.5659 0.3869  -0.3996 -1.0749 1285 TYR A CG  
9828  C CD1 . TYR A 1285 ? 0.9255 2.4777 2.6124 0.4386  -0.4336 -1.0730 1285 TYR A CD1 
9829  C CD2 . TYR A 1285 ? 0.8323 2.4044 2.5492 0.3302  -0.3745 -1.0944 1285 TYR A CD2 
9830  C CE1 . TYR A 1285 ? 0.9181 2.4743 2.6532 0.4336  -0.4437 -1.0901 1285 TYR A CE1 
9831  C CE2 . TYR A 1285 ? 0.8146 2.3901 2.5788 0.3242  -0.3815 -1.1122 1285 TYR A CE2 
9832  C CZ  . TYR A 1285 ? 0.8619 2.4316 2.6379 0.3756  -0.4170 -1.1104 1285 TYR A CZ  
9833  O OH  . TYR A 1285 ? 0.8822 2.4557 2.7088 0.3702  -0.4250 -1.1286 1285 TYR A OH  
9834  N N   . SER A 1286 ? 0.9205 2.3955 2.3792 0.4811  -0.4037 -1.0123 1286 SER A N   
9835  C CA  . SER A 1286 ? 0.8432 2.3087 2.2568 0.4759  -0.3891 -1.0055 1286 SER A CA  
9836  C C   . SER A 1286 ? 0.7626 2.2192 2.1399 0.4644  -0.3476 -0.9480 1286 SER A C   
9837  O O   . SER A 1286 ? 0.7519 2.1958 2.1144 0.4726  -0.3293 -0.9033 1286 SER A O   
9838  C CB  . SER A 1286 ? 0.7912 2.2990 2.2531 0.4376  -0.3971 -1.0628 1286 SER A CB  
9839  O OG  . SER A 1286 ? 0.7704 2.2685 2.1893 0.4306  -0.3829 -1.0583 1286 SER A OG  
9840  N N   . THR A 1287 ? 1.2208 2.6842 2.5831 0.4451  -0.3333 -0.9513 1287 THR A N   
9841  C CA  . THR A 1287 ? 1.2573 2.7067 2.5781 0.4408  -0.2988 -0.9007 1287 THR A CA  
9842  C C   . THR A 1287 ? 1.2695 2.7653 2.6414 0.3867  -0.2703 -0.8950 1287 THR A C   
9843  O O   . THR A 1287 ? 1.2573 2.7657 2.6432 0.3731  -0.2452 -0.8577 1287 THR A O   
9844  C CB  . THR A 1287 ? 1.2654 2.6842 2.5271 0.4596  -0.3011 -0.9029 1287 THR A CB  
9845  O OG1 . THR A 1287 ? 1.2341 2.6772 2.5248 0.4381  -0.3182 -0.9583 1287 THR A OG1 
9846  C CG2 . THR A 1287 ? 1.3629 2.7310 2.5619 0.5126  -0.3208 -0.8925 1287 THR A CG2 
9847  N N   . GLN A 1288 ? 1.4417 2.9627 2.8390 0.3544  -0.2743 -0.9330 1288 GLN A N   
9848  C CA  . GLN A 1288 ? 1.4088 2.9543 2.8297 0.2989  -0.2473 -0.9276 1288 GLN A CA  
9849  C C   . GLN A 1288 ? 1.4209 2.9667 2.8622 0.2615  -0.2267 -0.9134 1288 GLN A C   
9850  O O   . GLN A 1288 ? 1.4400 2.9816 2.8686 0.2288  -0.1950 -0.8799 1288 GLN A O   
9851  C CB  . GLN A 1288 ? 1.3908 2.9491 2.8291 0.2638  -0.2604 -0.9849 1288 GLN A CB  
9852  C CG  . GLN A 1288 ? 1.4189 2.9727 2.8250 0.2824  -0.2653 -0.9883 1288 GLN A CG  
9853  C CD  . GLN A 1288 ? 1.3979 2.9406 2.7732 0.2731  -0.2330 -0.9374 1288 GLN A CD  
9854  O OE1 . GLN A 1288 ? 1.3886 2.9373 2.7754 0.2258  -0.2105 -0.9256 1288 GLN A OE1 
9855  N NE2 . GLN A 1288 ? 1.4250 2.9226 2.7328 0.3144  -0.2282 -0.9076 1288 GLN A NE2 
9856  N N   . ASP A 1289 ? 0.9368 2.4870 2.4096 0.2668  -0.2447 -0.9390 1289 ASP A N   
9857  C CA  . ASP A 1289 ? 0.9193 2.4683 2.4106 0.2375  -0.2242 -0.9235 1289 ASP A CA  
9858  C C   . ASP A 1289 ? 0.9096 2.4465 2.3692 0.2638  -0.2031 -0.8594 1289 ASP A C   
9859  O O   . ASP A 1289 ? 0.9269 2.4601 2.3727 0.2322  -0.1694 -0.8240 1289 ASP A O   
9860  C CB  . ASP A 1289 ? 0.9394 2.4957 2.4758 0.2385  -0.2491 -0.9691 1289 ASP A CB  
9861  C CG  . ASP A 1289 ? 0.9860 2.5395 2.5213 0.3000  -0.2830 -0.9707 1289 ASP A CG  
9862  O OD1 . ASP A 1289 ? 1.0002 2.5568 2.5311 0.3263  -0.3111 -1.0004 1289 ASP A OD1 
9863  O OD2 . ASP A 1289 ? 1.0175 2.5633 2.5519 0.3226  -0.2806 -0.9411 1289 ASP A OD2 
9864  N N   . THR A 1290 ? 0.4851 2.0123 1.9273 0.3223  -0.2222 -0.8455 1290 THR A N   
9865  C CA  . THR A 1290 ? 0.4070 1.9182 1.8167 0.3517  -0.2045 -0.7917 1290 THR A CA  
9866  C C   . THR A 1290 ? 0.2988 1.7987 1.6605 0.3523  -0.1711 -0.7402 1290 THR A C   
9867  O O   . THR A 1290 ? 0.2778 1.7626 1.6060 0.3761  -0.1537 -0.6966 1290 THR A O   
9868  C CB  . THR A 1290 ? 0.4596 1.9484 1.8510 0.4137  -0.2352 -0.7934 1290 THR A CB  
9869  O OG1 . THR A 1290 ? 0.4685 1.9752 1.9148 0.4116  -0.2648 -0.8383 1290 THR A OG1 
9870  C CG2 . THR A 1290 ? 0.4390 1.8995 1.7858 0.4369  -0.2160 -0.7425 1290 THR A CG2 
9871  N N   . ILE A 1291 ? 0.8525 2.3586 2.2100 0.3260  -0.1618 -0.7460 1291 ILE A N   
9872  C CA  . ILE A 1291 ? 0.8215 2.3193 2.1417 0.3184  -0.1293 -0.6993 1291 ILE A CA  
9873  C C   . ILE A 1291 ? 0.7665 2.2736 2.1002 0.2561  -0.1019 -0.6897 1291 ILE A C   
9874  O O   . ILE A 1291 ? 0.7833 2.2844 2.0936 0.2452  -0.0723 -0.6456 1291 ILE A O   
9875  C CB  . ILE A 1291 ? 0.6959 2.1907 1.9983 0.3322  -0.1346 -0.7057 1291 ILE A CB  
9876  C CG1 . ILE A 1291 ? 0.6157 2.1096 1.8991 0.3010  -0.1022 -0.6705 1291 ILE A CG1 
9877  C CG2 . ILE A 1291 ? 0.6891 2.1990 2.0253 0.3154  -0.1623 -0.7639 1291 ILE A CG2 
9878  C CD1 . ILE A 1291 ? 0.5935 2.0799 1.8533 0.3238  -0.1029 -0.6664 1291 ILE A CD1 
9879  N N   . ASN A 1292 ? 0.4000 1.9186 1.7675 0.2152  -0.1118 -0.7332 1292 ASN A N   
9880  C CA  . ASN A 1292 ? 0.3576 1.8782 1.7387 0.1565  -0.0892 -0.7332 1292 ASN A CA  
9881  C C   . ASN A 1292 ? 0.3744 1.8937 1.7652 0.1549  -0.0800 -0.7199 1292 ASN A C   
9882  O O   . ASN A 1292 ? 0.4025 1.9161 1.7747 0.1331  -0.0499 -0.6809 1292 ASN A O   
9883  C CB  . ASN A 1292 ? 0.3351 1.8625 1.7482 0.1202  -0.1042 -0.7914 1292 ASN A CB  
9884  C CG  . ASN A 1292 ? 0.3460 1.8756 1.7490 0.1249  -0.1165 -0.8096 1292 ASN A CG  
9885  O OD1 . ASN A 1292 ? 0.3421 1.8668 1.7171 0.1262  -0.1010 -0.7750 1292 ASN A OD1 
9886  N ND2 . ASN A 1292 ? 0.3482 1.8853 1.7741 0.1278  -0.1442 -0.8654 1292 ASN A ND2 
9887  N N   . ALA A 1293 ? 0.1493 1.6733 1.5674 0.1801  -0.1066 -0.7510 1293 ALA A N   
9888  C CA  . ALA A 1293 ? 0.1037 1.6268 1.5348 0.1801  -0.0998 -0.7411 1293 ALA A CA  
9889  C C   . ALA A 1293 ? 0.1370 1.6500 1.5247 0.2003  -0.0735 -0.6799 1293 ALA A C   
9890  O O   . ALA A 1293 ? 0.1285 1.6392 1.5118 0.1750  -0.0480 -0.6562 1293 ALA A O   
9891  C CB  . ALA A 1293 ? 0.1469 1.6746 1.6090 0.2182  -0.1372 -0.7777 1293 ALA A CB  
9892  N N   . ILE A 1294 ? 0.9299 2.4345 2.2817 0.2446  -0.0773 -0.6553 1294 ILE A N   
9893  C CA  . ILE A 1294 ? 0.9555 2.4476 2.2605 0.2664  -0.0514 -0.6007 1294 ILE A CA  
9894  C C   . ILE A 1294 ? 0.9523 2.4437 2.2330 0.2267  -0.0162 -0.5661 1294 ILE A C   
9895  O O   . ILE A 1294 ? 0.9769 2.4624 2.2286 0.2207  0.0118  -0.5257 1294 ILE A O   
9896  C CB  . ILE A 1294 ? 0.9744 2.4500 2.2417 0.3302  -0.0646 -0.5861 1294 ILE A CB  
9897  C CG1 . ILE A 1294 ? 0.9804 2.4500 2.2637 0.3744  -0.1014 -0.6156 1294 ILE A CG1 
9898  C CG2 . ILE A 1294 ? 0.9792 2.4397 2.1946 0.3480  -0.0342 -0.5330 1294 ILE A CG2 
9899  C CD1 . ILE A 1294 ? 0.9705 2.4344 2.2543 0.3879  -0.0995 -0.6032 1294 ILE A CD1 
9900  N N   . GLU A 1295 ? 1.0024 2.4988 2.2926 0.2003  -0.0185 -0.5820 1295 GLU A N   
9901  C CA  . GLU A 1295 ? 0.9782 2.4719 2.2471 0.1626  0.0109  -0.5507 1295 GLU A CA  
9902  C C   . GLU A 1295 ? 0.8961 2.3894 2.1719 0.1144  0.0326  -0.5427 1295 GLU A C   
9903  O O   . GLU A 1295 ? 0.8873 2.3739 2.1313 0.1004  0.0613  -0.4998 1295 GLU A O   
9904  C CB  . GLU A 1295 ? 1.0496 2.5472 2.3310 0.1402  0.0017  -0.5748 1295 GLU A CB  
9905  C CG  . GLU A 1295 ? 1.1027 2.5963 2.3714 0.0905  0.0281  -0.5513 1295 GLU A CG  
9906  C CD  . GLU A 1295 ? 1.1570 2.6504 2.4187 0.0866  0.0253  -0.5515 1295 GLU A CD  
9907  O OE1 . GLU A 1295 ? 1.1471 2.6444 2.4176 0.1167  0.0022  -0.5773 1295 GLU A OE1 
9908  O OE2 . GLU A 1295 ? 1.1940 2.6822 2.4400 0.0543  0.0460  -0.5249 1295 GLU A OE2 
9909  N N   . GLY A 1296 ? 0.5094 2.0081 1.8249 0.0897  0.0189  -0.5863 1296 GLY A N   
9910  C CA  . GLY A 1296 ? 0.5177 2.0131 1.8418 0.0525  0.0370  -0.5843 1296 GLY A CA  
9911  C C   . GLY A 1296 ? 0.5127 2.0042 1.8105 0.0762  0.0535  -0.5433 1296 GLY A C   
9912  O O   . GLY A 1296 ? 0.5141 1.9982 1.7710 0.0709  0.0799  -0.4973 1296 GLY A O   
9913  N N   . LEU A 1297 ? 0.2601 1.7558 1.5792 0.1049  0.0365  -0.5609 1297 LEU A N   
9914  C CA  . LEU A 1297 ? 0.2775 1.7685 1.5749 0.1229  0.0521  -0.5286 1297 LEU A CA  
9915  C C   . LEU A 1297 ? 0.3438 1.8254 1.5828 0.1363  0.0802  -0.4725 1297 LEU A C   
9916  O O   . LEU A 1297 ? 0.3432 1.8193 1.5577 0.1369  0.1008  -0.4439 1297 LEU A O   
9917  C CB  . LEU A 1297 ? 0.2545 1.7486 1.5724 0.1721  0.0227  -0.5500 1297 LEU A CB  
9918  C CG  . LEU A 1297 ? 0.2577 1.7585 1.6257 0.1469  0.0137  -0.5868 1297 LEU A CG  
9919  C CD1 . LEU A 1297 ? 0.2413 1.7515 1.6600 0.1426  -0.0204 -0.6459 1297 LEU A CD1 
9920  C CD2 . LEU A 1297 ? 0.2948 1.7929 1.6615 0.1801  0.0110  -0.5747 1297 LEU A CD2 
9921  N N   . THR A 1298 ? 1.1803 2.6597 2.3964 0.1479  0.0808  -0.4586 1298 THR A N   
9922  C CA  . THR A 1298 ? 1.2016 2.6721 2.3642 0.1558  0.1080  -0.4087 1298 THR A CA  
9923  C C   . THR A 1298 ? 1.1810 2.6494 2.3352 0.1015  0.1307  -0.3917 1298 THR A C   
9924  O O   . THR A 1298 ? 1.1595 2.6212 2.2855 0.0816  0.1559  -0.3607 1298 THR A O   
9925  C CB  . THR A 1298 ? 1.1832 2.6496 2.3238 0.1969  0.0991  -0.4006 1298 THR A CB  
9926  O OG1 . THR A 1298 ? 1.2030 2.6682 2.3590 0.2437  0.0686  -0.4293 1298 THR A OG1 
9927  C CG2 . THR A 1298 ? 1.1965 2.6516 2.2799 0.2164  0.1261  -0.3522 1298 THR A CG2 
9928  N N   . GLU A 1299 ? 0.7777 2.2497 1.9541 0.0782  0.1200  -0.4139 1299 GLU A N   
9929  C CA  . GLU A 1299 ? 0.7996 2.2662 1.9648 0.0310  0.1377  -0.3988 1299 GLU A CA  
9930  C C   . GLU A 1299 ? 0.7983 2.2581 1.9574 -0.0051 0.1565  -0.3898 1299 GLU A C   
9931  O O   . GLU A 1299 ? 0.8474 2.2986 1.9713 -0.0250 0.1794  -0.3528 1299 GLU A O   
9932  C CB  . GLU A 1299 ? 0.8111 2.2814 2.0101 0.0057  0.1201  -0.4388 1299 GLU A CB  
9933  C CG  . GLU A 1299 ? 0.8868 2.3519 2.0662 -0.0186 0.1316  -0.4170 1299 GLU A CG  
9934  C CD  . GLU A 1299 ? 0.9581 2.4241 2.1098 0.0198  0.1356  -0.3832 1299 GLU A CD  
9935  O OE1 . GLU A 1299 ? 0.9923 2.4638 2.1574 0.0491  0.1165  -0.4025 1299 GLU A OE1 
9936  O OE2 . GLU A 1299 ? 0.9753 2.4354 2.0901 0.0219  0.1579  -0.3389 1299 GLU A OE2 
9937  N N   . TYR A 1300 ? 0.3674 1.8307 1.5618 -0.0108 0.1449  -0.4255 1300 TYR A N   
9938  C CA  . TYR A 1300 ? 0.3320 1.7886 1.5273 -0.0421 0.1606  -0.4248 1300 TYR A CA  
9939  C C   . TYR A 1300 ? 0.2968 1.7484 1.4554 -0.0254 0.1804  -0.3846 1300 TYR A C   
9940  O O   . TYR A 1300 ? 0.2393 1.6810 1.3758 -0.0556 0.2014  -0.3647 1300 TYR A O   
9941  C CB  . TYR A 1300 ? 0.3675 1.8300 1.6155 -0.0499 0.1421  -0.4776 1300 TYR A CB  
9942  C CG  . TYR A 1300 ? 0.3691 1.8251 1.6212 -0.0726 0.1579  -0.4776 1300 TYR A CG  
9943  C CD1 . TYR A 1300 ? 0.3899 1.8376 1.6540 -0.1196 0.1678  -0.4991 1300 TYR A CD1 
9944  C CD2 . TYR A 1300 ? 0.3486 1.8057 1.5895 -0.0459 0.1641  -0.4566 1300 TYR A CD2 
9945  C CE1 . TYR A 1300 ? 0.4033 1.8442 1.6708 -0.1391 0.1831  -0.5001 1300 TYR A CE1 
9946  C CE2 . TYR A 1300 ? 0.3658 1.8165 1.6100 -0.0668 0.1793  -0.4561 1300 TYR A CE2 
9947  C CZ  . TYR A 1300 ? 0.4121 1.8548 1.6708 -0.1131 0.1885  -0.4780 1300 TYR A CZ  
9948  O OH  . TYR A 1300 ? 0.4644 1.9004 1.7267 -0.1308 0.2036  -0.4784 1300 TYR A OH  
9949  N N   . SER A 1301 ? 0.3495 1.8060 1.4987 0.0224  0.1737  -0.3745 1301 SER A N   
9950  C CA  . SER A 1301 ? 0.4072 1.8565 1.5127 0.0370  0.1954  -0.3351 1301 SER A CA  
9951  C C   . SER A 1301 ? 0.3688 1.8101 1.4212 0.0329  0.2164  -0.2899 1301 SER A C   
9952  O O   . SER A 1301 ? 0.3373 1.7702 1.3443 0.0371  0.2375  -0.2537 1301 SER A O   
9953  C CB  . SER A 1301 ? 0.4875 1.9404 1.5921 0.0896  0.1840  -0.3382 1301 SER A CB  
9954  O OG  . SER A 1301 ? 0.5302 1.9794 1.6305 0.0872  0.1952  -0.3323 1301 SER A OG  
9955  N N   . LEU A 1302 ? 0.9727 2.4164 2.0323 0.0235  0.2094  -0.2941 1302 LEU A N   
9956  C CA  . LEU A 1302 ? 1.0407 2.4787 2.0604 0.0183  0.2250  -0.2562 1302 LEU A CA  
9957  C C   . LEU A 1302 ? 1.0760 2.5060 2.0846 -0.0311 0.2391  -0.2429 1302 LEU A C   
9958  O O   . LEU A 1302 ? 1.1682 2.5909 2.1339 -0.0370 0.2574  -0.2037 1302 LEU A O   
9959  C CB  . LEU A 1302 ? 1.0847 2.5291 2.1218 0.0313  0.2093  -0.2692 1302 LEU A CB  
9960  C CG  . LEU A 1302 ? 1.1372 2.5806 2.1414 0.0774  0.2134  -0.2439 1302 LEU A CG  
9961  C CD1 . LEU A 1302 ? 1.1274 2.5765 2.1535 0.0906  0.1961  -0.2615 1302 LEU A CD1 
9962  C CD2 . LEU A 1302 ? 1.1729 2.6077 2.1255 0.0707  0.2396  -0.1959 1302 LEU A CD2 
9963  N N   . LEU A 1303 ? 0.9210 2.3516 1.9676 -0.0642 0.2289  -0.2789 1303 LEU A N   
9964  C CA  . LEU A 1303 ? 0.8560 2.2781 1.8996 -0.1127 0.2372  -0.2798 1303 LEU A CA  
9965  C C   . LEU A 1303 ? 0.8013 2.2141 1.8308 -0.1371 0.2526  -0.2733 1303 LEU A C   
9966  O O   . LEU A 1303 ? 0.8086 2.2131 1.8035 -0.1586 0.2674  -0.2441 1303 LEU A O   
9967  C CB  . LEU A 1303 ? 0.8422 2.2680 1.9304 -0.1332 0.2192  -0.3273 1303 LEU A CB  
9968  C CG  . LEU A 1303 ? 0.8172 2.2349 1.9106 -0.1813 0.2231  -0.3442 1303 LEU A CG  
9969  C CD1 . LEU A 1303 ? 0.7855 2.1986 1.8939 -0.2008 0.2286  -0.3678 1303 LEU A CD1 
9970  C CD2 . LEU A 1303 ? 0.8577 2.2682 1.9080 -0.1978 0.2387  -0.3001 1303 LEU A CD2 
9971  N N   . VAL A 1304 ? 0.5146 1.9297 1.5727 -0.1330 0.2476  -0.3019 1304 VAL A N   
9972  C CA  . VAL A 1304 ? 0.5752 1.9828 1.6200 -0.1430 0.2622  -0.2933 1304 VAL A CA  
9973  C C   . VAL A 1304 ? 0.5911 1.9949 1.5845 -0.1175 0.2774  -0.2454 1304 VAL A C   
9974  O O   . VAL A 1304 ? 0.6446 2.0508 1.6133 -0.0973 0.2780  -0.2201 1304 VAL A O   
9975  C CB  . VAL A 1304 ? 0.6097 2.0241 1.6990 -0.1292 0.2504  -0.3304 1304 VAL A CB  
9976  C CG1 . VAL A 1304 ? 0.6638 2.0706 1.7435 -0.1392 0.2656  -0.3234 1304 VAL A CG1 
9977  C CG2 . VAL A 1304 ? 0.5803 1.9991 1.7199 -0.1505 0.2341  -0.3809 1304 VAL A CG2 
9978  N N   . LYS A 1305 ? 0.8193 2.3399 1.8137 0.1822  0.0917  -0.0433 1305 LYS A N   
9979  C CA  . LYS A 1305 ? 0.8882 2.3829 1.8264 0.1847  0.0856  -0.0193 1305 LYS A CA  
9980  C C   . LYS A 1305 ? 1.0000 2.4391 1.8742 0.2017  0.0547  -0.0569 1305 LYS A C   
9981  O O   . LYS A 1305 ? 1.0334 2.4596 1.8851 0.2015  0.0367  -0.0895 1305 LYS A O   
9982  C CB  . LYS A 1305 ? 0.8996 2.4277 1.8095 0.1567  0.0971  0.0345  1305 LYS A CB  
9983  C CG  . LYS A 1305 ? 1.0152 2.5350 1.8996 0.1585  0.1049  0.0741  1305 LYS A CG  
9984  C CD  . LYS A 1305 ? 1.1276 2.7014 2.0250 0.1321  0.1305  0.1356  1305 LYS A CD  
9985  C CE  . LYS A 1305 ? 1.2121 2.8340 2.1935 0.1280  0.1598  0.1513  1305 LYS A CE  
9986  N NZ  . LYS A 1305 ? 1.1683 2.8441 2.1697 0.1067  0.1875  0.2121  1305 LYS A NZ  
9987  N N   . GLN A 1306 ? 1.2104 2.6176 2.0570 0.2173  0.0496  -0.0513 1306 GLN A N   
9988  C CA  . GLN A 1306 ? 1.2714 2.6250 2.0627 0.2381  0.0219  -0.0866 1306 GLN A CA  
9989  C C   . GLN A 1306 ? 1.3308 2.6693 2.0492 0.2242  0.0042  -0.0815 1306 GLN A C   
9990  O O   . GLN A 1306 ? 1.3441 2.7088 2.0433 0.1991  0.0138  -0.0408 1306 GLN A O   
9991  C CB  . GLN A 1306 ? 1.7910 3.1176 2.5717 0.2578  0.0226  -0.0775 1306 GLN A CB  
9992  C CG  . GLN A 1306 ? 2.4398 3.7440 3.2602 0.2874  0.0192  -0.1191 1306 GLN A CG  
9993  C CD  . GLN A 1306 ? 1.5901 2.8644 2.3924 0.3079  0.0174  -0.1125 1306 GLN A CD  
9994  O OE1 . GLN A 1306 ? 1.6382 2.8761 2.3798 0.3189  -0.0027 -0.1202 1306 GLN A OE1 
9995  N NE2 . GLN A 1306 ? 1.5747 2.8641 2.4309 0.3135  0.0389  -0.0990 1306 GLN A NE2 
9996  N N   . LEU A 1307 ? 1.3140 2.6106 1.9920 0.2407  -0.0211 -0.1232 1307 LEU A N   
9997  C CA  . LEU A 1307 ? 1.3534 2.6332 1.9674 0.2288  -0.0383 -0.1273 1307 LEU A CA  
9998  C C   . LEU A 1307 ? 1.4060 2.6381 1.9543 0.2437  -0.0570 -0.1319 1307 LEU A C   
9999  O O   . LEU A 1307 ? 1.4452 2.6396 1.9667 0.2638  -0.0779 -0.1728 1307 LEU A O   
10000 C CB  . LEU A 1307 ? 1.3567 2.6295 1.9783 0.2343  -0.0516 -0.1734 1307 LEU A CB  
10001 C CG  . LEU A 1307 ? 1.2868 2.5968 1.9883 0.2340  -0.0349 -0.1824 1307 LEU A CG  
10002 C CD1 . LEU A 1307 ? 1.3298 2.6157 2.0626 0.2653  -0.0416 -0.2219 1307 LEU A CD1 
10003 C CD2 . LEU A 1307 ? 1.2645 2.5980 1.9774 0.2178  -0.0361 -0.1967 1307 LEU A CD2 
10004 N N   . ARG A 1308 ? 1.1571 2.3927 1.6794 0.2337  -0.0491 -0.0888 1308 ARG A N   
10005 C CA  . ARG A 1308 ? 1.1773 2.3703 1.6371 0.2464  -0.0650 -0.0866 1308 ARG A CA  
10006 C C   . ARG A 1308 ? 1.1715 2.3195 1.5922 0.2666  -0.0910 -0.1344 1308 ARG A C   
10007 O O   . ARG A 1308 ? 1.1504 2.2930 1.5425 0.2553  -0.1008 -0.1482 1308 ARG A O   
10008 C CB  . ARG A 1308 ? 1.1894 2.3910 1.5991 0.2200  -0.0621 -0.0431 1308 ARG A CB  
10009 C CG  . ARG A 1308 ? 1.2735 2.4268 1.6086 0.2296  -0.0836 -0.0513 1308 ARG A CG  
10010 C CD  . ARG A 1308 ? 1.3223 2.4831 1.6175 0.2100  -0.0770 -0.0017 1308 ARG A CD  
10011 N NE  . ARG A 1308 ? 1.4274 2.5416 1.6522 0.2192  -0.0967 -0.0078 1308 ARG A NE  
10012 C CZ  . ARG A 1308 ? 1.5059 2.5924 1.6854 0.2169  -0.1138 -0.0331 1308 ARG A CZ  
10013 N NH1 . ARG A 1308 ? 1.4582 2.5587 1.6546 0.2061  -0.1145 -0.0560 1308 ARG A NH1 
10014 N NH2 . ARG A 1308 ? 1.6082 2.6525 1.7256 0.2261  -0.1297 -0.0351 1308 ARG A NH2 
10015 N N   . LEU A 1309 ? 0.7972 1.9133 1.2162 0.2969  -0.1016 -0.1596 1309 LEU A N   
10016 C CA  . LEU A 1309 ? 0.8503 1.9250 1.2345 0.3194  -0.1257 -0.2051 1309 LEU A CA  
10017 C C   . LEU A 1309 ? 0.9339 1.9735 1.2400 0.3176  -0.1412 -0.1958 1309 LEU A C   
10018 O O   . LEU A 1309 ? 0.9391 1.9751 1.2174 0.3112  -0.1368 -0.1595 1309 LEU A O   
10019 C CB  . LEU A 1309 ? 0.8396 1.8944 1.2468 0.3527  -0.1317 -0.2338 1309 LEU A CB  
10020 C CG  . LEU A 1309 ? 0.7716 1.8390 1.2414 0.3675  -0.1296 -0.2730 1309 LEU A CG  
10021 C CD1 . LEU A 1309 ? 0.7916 1.8439 1.2832 0.3963  -0.1311 -0.2893 1309 LEU A CD1 
10022 C CD2 . LEU A 1309 ? 0.9005 1.9509 1.3526 0.3755  -0.1481 -0.3166 1309 LEU A CD2 
10023 N N   . SER A 1310 ? 1.0170 2.0297 1.2884 0.3244  -0.1591 -0.2292 1310 SER A N   
10024 C CA  . SER A 1310 ? 1.1144 2.0875 1.3123 0.3278  -0.1750 -0.2268 1310 SER A CA  
10025 C C   . SER A 1310 ? 1.2081 2.1482 1.3744 0.3428  -0.1949 -0.2708 1310 SER A C   
10026 O O   . SER A 1310 ? 1.2021 2.1174 1.3105 0.3349  -0.2044 -0.2670 1310 SER A O   
10027 C CB  . SER A 1310 ? 1.1547 2.1417 1.3186 0.2942  -0.1665 -0.1833 1310 SER A CB  
10028 O OG  . SER A 1310 ? 1.2477 2.1948 1.3409 0.2966  -0.1816 -0.1826 1310 SER A OG  
10029 N N   . MET A 1311 ? 0.9658 1.9058 1.1698 0.3645  -0.2005 -0.3120 1311 MET A N   
10030 C CA  . MET A 1311 ? 1.0430 1.9541 1.2224 0.3821  -0.2189 -0.3558 1311 MET A CA  
10031 C C   . MET A 1311 ? 1.1798 2.0436 1.2918 0.4003  -0.2363 -0.3620 1311 MET A C   
10032 O O   . MET A 1311 ? 1.1955 2.0477 1.2675 0.3902  -0.2347 -0.3288 1311 MET A O   
10033 C CB  . MET A 1311 ? 1.2577 2.1754 1.4881 0.4074  -0.2227 -0.3966 1311 MET A CB  
10034 C CG  . MET A 1311 ? 1.2114 2.1492 1.4749 0.3999  -0.2215 -0.4229 1311 MET A CG  
10035 S SD  . MET A 1311 ? 0.9927 1.9754 1.3477 0.3996  -0.2046 -0.4291 1311 MET A SD  
10036 C CE  . MET A 1311 ? 0.9840 1.9989 1.3542 0.3690  -0.1813 -0.3694 1311 MET A CE  
10037 N N   . ASP A 1312 ? 1.1396 1.9771 1.2391 0.4274  -0.2527 -0.4041 1312 ASP A N   
10038 C CA  . ASP A 1312 ? 1.1984 1.9911 1.2363 0.4478  -0.2692 -0.4123 1312 ASP A CA  
10039 C C   . ASP A 1312 ? 1.2395 2.0141 1.2796 0.4785  -0.2847 -0.4620 1312 ASP A C   
10040 O O   . ASP A 1312 ? 1.2840 2.0325 1.2829 0.4832  -0.2958 -0.4798 1312 ASP A O   
10041 C CB  . ASP A 1312 ? 1.3082 2.0822 1.2877 0.4255  -0.2708 -0.3924 1312 ASP A CB  
10042 C CG  . ASP A 1312 ? 1.3200 2.0517 1.2370 0.4410  -0.2829 -0.3856 1312 ASP A CG  
10043 O OD1 . ASP A 1312 ? 1.3108 2.0229 1.2249 0.4742  -0.2943 -0.4087 1312 ASP A OD1 
10044 O OD2 . ASP A 1312 ? 1.3284 2.0477 1.2000 0.4200  -0.2807 -0.3572 1312 ASP A OD2 
10045 N N   . ILE A 1313 ? 1.2409 2.0298 1.3293 0.4994  -0.2849 -0.4841 1313 ILE A N   
10046 C CA  . ILE A 1313 ? 1.2316 2.0155 1.3372 0.5255  -0.2971 -0.5326 1313 ILE A CA  
10047 C C   . ILE A 1313 ? 1.3621 2.1053 1.4136 0.5538  -0.3161 -0.5558 1313 ILE A C   
10048 O O   . ILE A 1313 ? 1.4915 2.2081 1.4964 0.5609  -0.3214 -0.5376 1313 ILE A O   
10049 C CB  . ILE A 1313 ? 1.2216 2.0260 1.3856 0.5447  -0.2946 -0.5525 1313 ILE A CB  
10050 C CG1 . ILE A 1313 ? 1.1586 1.9969 1.3707 0.5231  -0.2743 -0.5194 1313 ILE A CG1 
10051 C CG2 . ILE A 1313 ? 1.1938 2.0085 1.3905 0.5582  -0.3015 -0.5979 1313 ILE A CG2 
10052 C CD1 . ILE A 1313 ? 1.1061 1.9812 1.3689 0.4985  -0.2602 -0.5174 1313 ILE A CD1 
10053 N N   . ASP A 1314 ? 1.6532 2.3930 1.7127 0.5712  -0.3262 -0.5965 1314 ASP A N   
10054 C CA  . ASP A 1314 ? 1.7111 2.4175 1.7292 0.6034  -0.3440 -0.6234 1314 ASP A CA  
10055 C C   . ASP A 1314 ? 1.6677 2.3871 1.7226 0.6250  -0.3516 -0.6693 1314 ASP A C   
10056 O O   . ASP A 1314 ? 1.6543 2.3818 1.7190 0.6161  -0.3513 -0.6858 1314 ASP A O   
10057 C CB  . ASP A 1314 ? 1.7894 2.4630 1.7433 0.5957  -0.3497 -0.6157 1314 ASP A CB  
10058 C CG  . ASP A 1314 ? 1.9007 2.5403 1.8129 0.6301  -0.3671 -0.6451 1314 ASP A CG  
10059 O OD1 . ASP A 1314 ? 1.8811 2.5258 1.8112 0.6480  -0.3747 -0.6828 1314 ASP A OD1 
10060 O OD2 . ASP A 1314 ? 2.0144 2.6233 1.8761 0.6396  -0.3730 -0.6297 1314 ASP A OD2 
10061 N N   . VAL A 1315 ? 1.3249 2.0490 1.4027 0.6522  -0.3576 -0.6892 1315 VAL A N   
10062 C CA  . VAL A 1315 ? 1.3173 2.0499 1.4213 0.6784  -0.3680 -0.7355 1315 VAL A CA  
10063 C C   . VAL A 1315 ? 1.4042 2.1016 1.4499 0.7058  -0.3852 -0.7547 1315 VAL A C   
10064 O O   . VAL A 1315 ? 1.4737 2.1431 1.4703 0.7124  -0.3895 -0.7347 1315 VAL A O   
10065 C CB  . VAL A 1315 ? 1.2887 2.0408 1.4388 0.6956  -0.3670 -0.7484 1315 VAL A CB  
10066 C CG1 . VAL A 1315 ? 1.3404 2.0678 1.4514 0.7189  -0.3758 -0.7405 1315 VAL A CG1 
10067 C CG2 . VAL A 1315 ? 1.3143 2.0849 1.5042 0.7150  -0.3743 -0.7949 1315 VAL A CG2 
10068 N N   . SER A 1316 ? 1.8844 2.5837 1.9353 0.7212  -0.3942 -0.7917 1316 SER A N   
10069 C CA  . SER A 1316 ? 2.0376 2.7049 2.0342 0.7466  -0.4090 -0.8100 1316 SER A CA  
10070 C C   . SER A 1316 ? 2.1029 2.7814 2.1190 0.7690  -0.4188 -0.8553 1316 SER A C   
10071 O O   . SER A 1316 ? 2.0649 2.7696 2.1244 0.7556  -0.4132 -0.8688 1316 SER A O   
10072 C CB  . SER A 1316 ? 2.0777 2.7174 2.0223 0.7260  -0.4059 -0.7865 1316 SER A CB  
10073 O OG  . SER A 1316 ? 2.1745 2.7772 2.0588 0.7412  -0.4136 -0.7737 1316 SER A OG  
10074 N N   . TYR A 1317 ? 2.5212 3.1809 2.5049 0.8035  -0.4333 -0.8776 1317 TYR A N   
10075 C CA  . TYR A 1317 ? 2.5903 3.2580 2.5834 0.8278  -0.4438 -0.9195 1317 TYR A CA  
10076 C C   . TYR A 1317 ? 2.6390 3.2873 2.5977 0.8203  -0.4445 -0.9221 1317 TYR A C   
10077 O O   . TYR A 1317 ? 2.6956 3.3101 2.5998 0.8146  -0.4441 -0.8998 1317 TYR A O   
10078 C CB  . TYR A 1317 ? 2.7114 3.3672 2.6791 0.8681  -0.4585 -0.9402 1317 TYR A CB  
10079 C CG  . TYR A 1317 ? 2.7441 3.4199 2.7464 0.8780  -0.4587 -0.9425 1317 TYR A CG  
10080 C CD1 . TYR A 1317 ? 2.7978 3.4573 2.7761 0.8771  -0.4566 -0.9128 1317 TYR A CD1 
10081 C CD2 . TYR A 1317 ? 2.7334 3.4448 2.7937 0.8867  -0.4600 -0.9738 1317 TYR A CD2 
10082 C CE1 . TYR A 1317 ? 2.8077 3.4852 2.8180 0.8860  -0.4558 -0.9147 1317 TYR A CE1 
10083 C CE2 . TYR A 1317 ? 2.7462 3.4753 2.8392 0.8947  -0.4591 -0.9769 1317 TYR A CE2 
10084 C CZ  . TYR A 1317 ? 2.7891 3.5008 2.8568 0.8947  -0.4569 -0.9473 1317 TYR A CZ  
10085 O OH  . TYR A 1317 ? 2.7872 3.5159 2.8871 0.9032  -0.4554 -0.9507 1317 TYR A OH  
10086 N N   . LYS A 1318 ? 2.3635 3.0326 2.3534 0.8212  -0.4455 -0.9501 1318 LYS A N   
10087 C CA  . LYS A 1318 ? 2.4158 3.0699 2.3790 0.8125  -0.4448 -0.9542 1318 LYS A CA  
10088 C C   . LYS A 1318 ? 2.5706 3.1838 2.4662 0.8358  -0.4543 -0.9571 1318 LYS A C   
10089 O O   . LYS A 1318 ? 2.5937 3.1793 2.4475 0.8213  -0.4503 -0.9410 1318 LYS A O   
10090 C CB  . LYS A 1318 ? 2.3740 3.0583 2.3818 0.8177  -0.4469 -0.9889 1318 LYS A CB  
10091 C CG  . LYS A 1318 ? 2.4539 3.1207 2.4298 0.8192  -0.4493 -1.0007 1318 LYS A CG  
10092 C CD  . LYS A 1318 ? 2.4187 3.1092 2.4316 0.7902  -0.4393 -1.0012 1318 LYS A CD  
10093 C CE  . LYS A 1318 ? 2.3842 3.1149 2.4580 0.8009  -0.4424 -1.0350 1318 LYS A CE  
10094 N NZ  . LYS A 1318 ? 2.3528 3.1011 2.4517 0.7789  -0.4350 -1.0394 1318 LYS A NZ  
10095 N N   . HIS A 1319 ? 2.4015 3.0114 2.2869 0.8720  -0.4663 -0.9773 1319 HIS A N   
10096 C CA  . HIS A 1319 ? 2.5602 3.1342 2.3851 0.8982  -0.4751 -0.9821 1319 HIS A CA  
10097 C C   . HIS A 1319 ? 2.7364 3.2893 2.5278 0.9132  -0.4793 -0.9632 1319 HIS A C   
10098 O O   . HIS A 1319 ? 2.8026 3.3176 2.5382 0.9139  -0.4791 -0.9431 1319 HIS A O   
10099 C CB  . HIS A 1319 ? 2.5233 3.1112 2.3586 0.9318  -0.4863 -1.0233 1319 HIS A CB  
10100 C CG  . HIS A 1319 ? 2.4630 3.0720 2.3306 0.9195  -0.4829 -1.0429 1319 HIS A CG  
10101 N ND1 . HIS A 1319 ? 2.3873 3.0390 2.3200 0.9122  -0.4811 -1.0607 1319 HIS A ND1 
10102 C CD2 . HIS A 1319 ? 2.5010 3.0939 2.3443 0.9139  -0.4807 -1.0474 1319 HIS A CD2 
10103 C CE1 . HIS A 1319 ? 2.3739 3.0360 2.3216 0.9029  -0.4784 -1.0750 1319 HIS A CE1 
10104 N NE2 . HIS A 1319 ? 2.4453 3.0724 2.3392 0.9038  -0.4782 -1.0674 1319 HIS A NE2 
10105 N N   . LYS A 1320 ? 2.7402 3.3173 2.5659 0.9249  -0.4827 -0.9698 1320 LYS A N   
10106 C CA  . LYS A 1320 ? 2.9231 3.4844 2.7226 0.9378  -0.4861 -0.9510 1320 LYS A CA  
10107 C C   . LYS A 1320 ? 3.0082 3.5475 2.7827 0.9059  -0.4753 -0.9072 1320 LYS A C   
10108 O O   . LYS A 1320 ? 2.9761 3.5279 2.7760 0.8716  -0.4639 -0.8918 1320 LYS A O   
10109 C CB  . LYS A 1320 ? 2.9293 3.5245 2.7784 0.9484  -0.4886 -0.9637 1320 LYS A CB  
10110 C CG  . LYS A 1320 ? 3.0035 3.5873 2.8356 0.9523  -0.4884 -0.9377 1320 LYS A CG  
10111 C CD  . LYS A 1320 ? 3.1323 3.6841 2.9045 0.9832  -0.4987 -0.9357 1320 LYS A CD  
10112 C CE  . LYS A 1320 ? 3.1498 3.6911 2.9056 0.9864  -0.4983 -0.9084 1320 LYS A CE  
10113 N NZ  . LYS A 1320 ? 3.2101 3.7181 2.9055 1.0139  -0.5070 -0.9015 1320 LYS A NZ  
10114 N N   . GLY A 1321 ? 2.8721 3.3804 2.5971 0.9175  -0.4786 -0.8868 1321 GLY A N   
10115 C CA  . GLY A 1321 ? 2.8542 3.3436 2.5553 0.8898  -0.4694 -0.8446 1321 GLY A CA  
10116 C C   . GLY A 1321 ? 2.7790 3.2993 2.5308 0.8637  -0.4595 -0.8282 1321 GLY A C   
10117 O O   . GLY A 1321 ? 2.7814 3.3360 2.5871 0.8681  -0.4597 -0.8500 1321 GLY A O   
10118 N N   . ALA A 1322 ? 2.9962 3.5048 2.7309 0.8363  -0.4500 -0.7891 1322 ALA A N   
10119 C CA  . ALA A 1322 ? 2.8675 3.4050 2.6484 0.8077  -0.4381 -0.7692 1322 ALA A CA  
10120 C C   . ALA A 1322 ? 2.7716 3.3265 2.5807 0.8223  -0.4394 -0.7671 1322 ALA A C   
10121 O O   . ALA A 1322 ? 2.7449 3.2810 2.5216 0.8424  -0.4460 -0.7579 1322 ALA A O   
10122 C CB  . ALA A 1322 ? 2.8147 3.3379 2.5693 0.7715  -0.4266 -0.7273 1322 ALA A CB  
10123 N N   . LEU A 1323 ? 2.8674 3.4585 2.7381 0.8117  -0.4324 -0.7760 1323 LEU A N   
10124 C CA  . LEU A 1323 ? 2.7622 3.3735 2.6686 0.8145  -0.4283 -0.7679 1323 LEU A CA  
10125 C C   . LEU A 1323 ? 2.7868 3.3983 2.6915 0.7804  -0.4136 -0.7214 1323 LEU A C   
10126 O O   . LEU A 1323 ? 2.8839 3.4790 2.7560 0.7578  -0.4089 -0.6985 1323 LEU A O   
10127 C CB  . LEU A 1323 ? 2.4184 3.0674 2.3921 0.8161  -0.4257 -0.7987 1323 LEU A CB  
10128 C CG  . LEU A 1323 ? 2.1375 2.8142 2.1645 0.8100  -0.4163 -0.7924 1323 LEU A CG  
10129 C CD1 . LEU A 1323 ? 2.0505 2.7150 2.0565 0.8337  -0.4226 -0.7855 1323 LEU A CD1 
10130 C CD2 . LEU A 1323 ? 1.9466 2.6553 2.0326 0.8181  -0.4171 -0.8317 1323 LEU A CD2 
10131 N N   . HIS A 1324 ? 2.0729 2.7034 2.0121 0.7765  -0.4060 -0.7073 1324 HIS A N   
10132 C CA  . HIS A 1324 ? 2.0287 2.6609 1.9653 0.7472  -0.3921 -0.6613 1324 HIS A CA  
10133 C C   . HIS A 1324 ? 1.9517 2.5961 1.9004 0.7085  -0.3789 -0.6413 1324 HIS A C   
10134 O O   . HIS A 1324 ? 1.9059 2.5622 1.8759 0.7027  -0.3789 -0.6647 1324 HIS A O   
10135 C CB  . HIS A 1324 ? 2.0072 2.6616 1.9871 0.7499  -0.3843 -0.6525 1324 HIS A CB  
10136 C CG  . HIS A 1324 ? 2.0113 2.7025 2.0616 0.7391  -0.3741 -0.6692 1324 HIS A CG  
10137 N ND1 . HIS A 1324 ? 1.9805 2.6948 2.0684 0.7094  -0.3559 -0.6403 1324 HIS A ND1 
10138 C CD2 . HIS A 1324 ? 2.0242 2.7339 2.1151 0.7544  -0.3791 -0.7112 1324 HIS A CD2 
10139 C CE1 . HIS A 1324 ? 1.9450 2.6889 2.0938 0.7071  -0.3497 -0.6637 1324 HIS A CE1 
10140 N NE2 . HIS A 1324 ? 1.9759 2.7175 2.1278 0.7336  -0.3638 -0.7072 1324 HIS A NE2 
10141 N N   . ASN A 1325 ? 2.1474 2.7896 2.0809 0.6826  -0.3679 -0.5977 1325 ASN A N   
10142 C CA  . ASN A 1325 ? 2.1348 2.7924 2.0794 0.6440  -0.3539 -0.5730 1325 ASN A CA  
10143 C C   . ASN A 1325 ? 2.0511 2.7161 1.9939 0.6218  -0.3410 -0.5262 1325 ASN A C   
10144 O O   . ASN A 1325 ? 2.0864 2.7271 1.9827 0.6259  -0.3448 -0.5033 1325 ASN A O   
10145 C CB  . ASN A 1325 ? 2.2753 2.9080 2.1702 0.6336  -0.3589 -0.5730 1325 ASN A CB  
10146 C CG  . ASN A 1325 ? 2.4021 2.9962 2.2299 0.6422  -0.3667 -0.5543 1325 ASN A CG  
10147 O OD1 . ASN A 1325 ? 2.4522 3.0187 2.2447 0.6687  -0.3804 -0.5772 1325 ASN A OD1 
10148 N ND2 . ASN A 1325 ? 2.3987 2.9914 2.2089 0.6201  -0.3577 -0.5120 1325 ASN A ND2 
10149 N N   . TYR A 1326 ? 2.2299 2.9294 2.2232 0.5984  -0.3251 -0.5106 1326 TYR A N   
10150 C CA  . TYR A 1326 ? 2.2190 2.9290 2.2173 0.5828  -0.3124 -0.4682 1326 TYR A CA  
10151 C C   . TYR A 1326 ? 2.0380 2.7777 2.0617 0.5445  -0.2941 -0.4358 1326 TYR A C   
10152 O O   . TYR A 1326 ? 1.9643 2.7339 2.0399 0.5336  -0.2850 -0.4471 1326 TYR A O   
10153 C CB  . TYR A 1326 ? 2.3024 3.0257 2.3419 0.6036  -0.3101 -0.4768 1326 TYR A CB  
10154 C CG  . TYR A 1326 ? 2.3363 3.0900 2.4432 0.6061  -0.3043 -0.5062 1326 TYR A CG  
10155 C CD1 . TYR A 1326 ? 2.3115 3.0976 2.4732 0.5894  -0.2858 -0.4873 1326 TYR A CD1 
10156 C CD2 . TYR A 1326 ? 2.3963 3.1466 2.5126 0.6259  -0.3166 -0.5523 1326 TYR A CD2 
10157 C CE1 . TYR A 1326 ? 2.2883 3.1013 2.5129 0.5917  -0.2797 -0.5141 1326 TYR A CE1 
10158 C CE2 . TYR A 1326 ? 2.3738 3.1523 2.5522 0.6280  -0.3114 -0.5794 1326 TYR A CE2 
10159 C CZ  . TYR A 1326 ? 2.3216 3.1307 2.5542 0.6106  -0.2929 -0.5605 1326 TYR A CZ  
10160 O OH  . TYR A 1326 ? 2.2776 3.1139 2.5732 0.6124  -0.2870 -0.5876 1326 TYR A OH  
10161 N N   . LYS A 1327 ? 1.9992 2.7321 1.9867 0.5243  -0.2882 -0.3941 1327 LYS A N   
10162 C CA  . LYS A 1327 ? 1.8550 2.6184 1.8631 0.4879  -0.2701 -0.3578 1327 LYS A CA  
10163 C C   . LYS A 1327 ? 1.6695 2.4673 1.7405 0.4861  -0.2547 -0.3463 1327 LYS A C   
10164 O O   . LYS A 1327 ? 1.6606 2.4561 1.7312 0.4951  -0.2512 -0.3262 1327 LYS A O   
10165 C CB  . LYS A 1327 ? 1.9370 2.6857 1.8908 0.4694  -0.2680 -0.3155 1327 LYS A CB  
10166 C CG  . LYS A 1327 ? 1.9441 2.7241 1.9096 0.4294  -0.2508 -0.2782 1327 LYS A CG  
10167 C CD  . LYS A 1327 ? 2.0360 2.7959 1.9388 0.4085  -0.2541 -0.2553 1327 LYS A CD  
10168 C CE  . LYS A 1327 ? 1.9645 2.7588 1.8803 0.3679  -0.2386 -0.2274 1327 LYS A CE  
10169 N NZ  . LYS A 1327 ? 1.8975 2.7103 1.8460 0.3592  -0.2366 -0.2552 1327 LYS A NZ  
10170 N N   . MET A 1328 ? 1.6502 2.4791 1.7760 0.4755  -0.2451 -0.3599 1328 MET A N   
10171 C CA  . MET A 1328 ? 1.4627 2.3268 1.6511 0.4687  -0.2271 -0.3457 1328 MET A CA  
10172 C C   . MET A 1328 ? 1.4403 2.3283 1.6277 0.4354  -0.2090 -0.2928 1328 MET A C   
10173 O O   . MET A 1328 ? 1.4457 2.3311 1.5964 0.4135  -0.2097 -0.2755 1328 MET A O   
10174 C CB  . MET A 1328 ? 1.3058 2.1948 1.5510 0.4677  -0.2230 -0.3778 1328 MET A CB  
10175 C CG  . MET A 1328 ? 1.1776 2.1072 1.4902 0.4533  -0.2012 -0.3603 1328 MET A CG  
10176 S SD  . MET A 1328 ? 1.1019 2.0523 1.4854 0.4666  -0.2000 -0.4081 1328 MET A SD  
10177 C CE  . MET A 1328 ? 1.7826 2.7036 2.1587 0.5077  -0.2161 -0.4440 1328 MET A CE  
10178 N N   . THR A 1329 ? 1.3235 2.2348 1.5496 0.4319  -0.1926 -0.2671 1329 THR A N   
10179 C CA  . THR A 1329 ? 1.2878 2.2299 1.5244 0.4008  -0.1728 -0.2174 1329 THR A CA  
10180 C C   . THR A 1329 ? 1.2156 2.1860 1.5171 0.4047  -0.1546 -0.2085 1329 THR A C   
10181 O O   . THR A 1329 ? 1.2037 2.1745 1.5454 0.4241  -0.1568 -0.2440 1329 THR A O   
10182 C CB  . THR A 1329 ? 1.3562 2.2813 1.5364 0.3943  -0.1747 -0.1787 1329 THR A CB  
10183 O OG1 . THR A 1329 ? 1.3963 2.2922 1.5591 0.4248  -0.1852 -0.1893 1329 THR A OG1 
10184 C CG2 . THR A 1329 ? 1.4239 2.3265 1.5427 0.3823  -0.1877 -0.1794 1329 THR A CG2 
10185 N N   . ASP A 1330 ? 1.5280 2.5221 1.8405 0.3867  -0.1361 -0.1615 1330 ASP A N   
10186 C CA  . ASP A 1330 ? 1.5144 2.5319 1.8862 0.3921  -0.1174 -0.1504 1330 ASP A CA  
10187 C C   . ASP A 1330 ? 1.5856 2.5778 1.9396 0.4169  -0.1220 -0.1458 1330 ASP A C   
10188 O O   . ASP A 1330 ? 1.5859 2.5913 1.9823 0.4244  -0.1073 -0.1360 1330 ASP A O   
10189 C CB  . ASP A 1330 ? 1.4855 2.5451 1.8838 0.3616  -0.0927 -0.1008 1330 ASP A CB  
10190 C CG  . ASP A 1330 ? 1.4474 2.5360 1.8632 0.3358  -0.0869 -0.1015 1330 ASP A CG  
10191 O OD1 . ASP A 1330 ? 1.3699 2.4660 1.8256 0.3419  -0.0883 -0.1375 1330 ASP A OD1 
10192 O OD2 . ASP A 1330 ? 1.4823 2.5879 1.8722 0.3090  -0.0807 -0.0653 1330 ASP A OD2 
10193 N N   . LYS A 1331 ? 1.9447 2.9007 2.2350 0.4289  -0.1418 -0.1515 1331 LYS A N   
10194 C CA  . LYS A 1331 ? 2.0076 2.9343 2.2728 0.4565  -0.1514 -0.1549 1331 LYS A CA  
10195 C C   . LYS A 1331 ? 2.0108 2.9234 2.3038 0.4878  -0.1619 -0.2065 1331 LYS A C   
10196 O O   . LYS A 1331 ? 1.9898 2.9095 2.3228 0.5018  -0.1526 -0.2104 1331 LYS A O   
10197 C CB  . LYS A 1331 ? 2.0847 2.9770 2.2737 0.4602  -0.1704 -0.1496 1331 LYS A CB  
10198 C CG  . LYS A 1331 ? 2.0672 2.9702 2.2212 0.4293  -0.1626 -0.1013 1331 LYS A CG  
10199 C CD  . LYS A 1331 ? 2.0225 2.9575 2.2100 0.4152  -0.1392 -0.0564 1331 LYS A CD  
10200 C CE  . LYS A 1331 ? 2.0590 3.0048 2.2077 0.3871  -0.1323 -0.0061 1331 LYS A CE  
10201 N NZ  . LYS A 1331 ? 2.0580 3.0258 2.2273 0.3824  -0.1129 0.0383  1331 LYS A NZ  
10202 N N   . ASN A 1332 ? 1.3549 2.2474 1.6250 0.4989  -0.1812 -0.2461 1332 ASN A N   
10203 C CA  . ASN A 1332 ? 1.3842 2.2706 1.6852 0.5243  -0.1908 -0.2977 1332 ASN A CA  
10204 C C   . ASN A 1332 ? 1.3649 2.2751 1.7081 0.5101  -0.1857 -0.3194 1332 ASN A C   
10205 O O   . ASN A 1332 ? 1.3874 2.2972 1.7058 0.4938  -0.1908 -0.3183 1332 ASN A O   
10206 C CB  . ASN A 1332 ? 1.4860 2.3352 1.7342 0.5494  -0.2164 -0.3299 1332 ASN A CB  
10207 C CG  . ASN A 1332 ? 1.5064 2.3517 1.7435 0.5442  -0.2277 -0.3593 1332 ASN A CG  
10208 O OD1 . ASN A 1332 ? 1.5016 2.3387 1.6970 0.5266  -0.2312 -0.3422 1332 ASN A OD1 
10209 N ND2 . ASN A 1332 ? 1.4900 2.3417 1.7650 0.5591  -0.2329 -0.4037 1332 ASN A ND2 
10210 N N   . PHE A 1333 ? 1.5624 2.4930 1.9691 0.5162  -0.1757 -0.3403 1333 PHE A N   
10211 C CA  . PHE A 1333 ? 1.4905 2.4372 1.9310 0.5098  -0.1766 -0.3712 1333 PHE A CA  
10212 C C   . PHE A 1333 ? 1.5494 2.4981 2.0355 0.5331  -0.1805 -0.4171 1333 PHE A C   
10213 O O   . PHE A 1333 ? 1.5675 2.5189 2.0669 0.5374  -0.1895 -0.4535 1333 PHE A O   
10214 C CB  . PHE A 1333 ? 1.3161 2.2991 1.7907 0.4763  -0.1566 -0.3422 1333 PHE A CB  
10215 C CG  . PHE A 1333 ? 1.1747 2.1880 1.7083 0.4667  -0.1312 -0.3160 1333 PHE A CG  
10216 C CD1 . PHE A 1333 ? 1.0850 2.1183 1.6863 0.4722  -0.1211 -0.3417 1333 PHE A CD1 
10217 C CD2 . PHE A 1333 ? 1.1687 2.1924 1.6909 0.4502  -0.1159 -0.2637 1333 PHE A CD2 
10218 C CE1 . PHE A 1333 ? 1.0478 2.1084 1.7047 0.4629  -0.0957 -0.3161 1333 PHE A CE1 
10219 C CE2 . PHE A 1333 ? 1.0410 2.0933 1.6175 0.4415  -0.0908 -0.2372 1333 PHE A CE2 
10220 C CZ  . PHE A 1333 ? 0.9951 2.0648 1.6393 0.4481  -0.0803 -0.2635 1333 PHE A CZ  
10221 N N   . LEU A 1334 ? 1.3675 2.3139 1.8751 0.5489  -0.1745 -0.4165 1334 LEU A N   
10222 C CA  . LEU A 1334 ? 1.3023 2.2495 1.8513 0.5722  -0.1788 -0.4622 1334 LEU A CA  
10223 C C   . LEU A 1334 ? 1.4509 2.3658 1.9533 0.6032  -0.2039 -0.4951 1334 LEU A C   
10224 O O   . LEU A 1334 ? 1.4864 2.3963 2.0083 0.6270  -0.2085 -0.5242 1334 LEU A O   
10225 C CB  . LEU A 1334 ? 1.1523 2.1134 1.7506 0.5745  -0.1589 -0.4488 1334 LEU A CB  
10226 C CG  . LEU A 1334 ? 1.0172 2.0073 1.6531 0.5466  -0.1312 -0.4030 1334 LEU A CG  
10227 C CD1 . LEU A 1334 ? 0.9174 1.9363 1.6028 0.5289  -0.1213 -0.4143 1334 LEU A CD1 
10228 C CD2 . LEU A 1334 ? 1.0120 1.9981 1.5973 0.5284  -0.1284 -0.3522 1334 LEU A CD2 
10229 N N   . GLY A 1335 ? 1.6529 2.5470 2.0941 0.6020  -0.2193 -0.4896 1335 GLY A N   
10230 C CA  . GLY A 1335 ? 1.8039 2.6670 2.1940 0.6296  -0.2428 -0.5155 1335 GLY A CA  
10231 C C   . GLY A 1335 ? 1.8760 2.7373 2.2904 0.6589  -0.2547 -0.5674 1335 GLY A C   
10232 O O   . GLY A 1335 ? 1.8441 2.7276 2.3158 0.6576  -0.2477 -0.5932 1335 GLY A O   
10233 N N   . ARG A 1336 ? 2.2269 3.0620 2.5958 0.6857  -0.2728 -0.5821 1336 ARG A N   
10234 C CA  . ARG A 1336 ? 2.3375 3.1692 2.7175 0.7164  -0.2874 -0.6311 1336 ARG A CA  
10235 C C   . ARG A 1336 ? 2.2170 3.0625 2.6238 0.7145  -0.2927 -0.6685 1336 ARG A C   
10236 O O   . ARG A 1336 ? 2.2041 3.0495 2.5946 0.6964  -0.2931 -0.6591 1336 ARG A O   
10237 C CB  . ARG A 1336 ? 2.5871 3.3878 2.9005 0.7410  -0.3083 -0.6374 1336 ARG A CB  
10238 C CG  . ARG A 1336 ? 2.7556 3.5388 3.0152 0.7254  -0.3131 -0.6121 1336 ARG A CG  
10239 C CD  . ARG A 1336 ? 2.9519 3.7103 3.1604 0.7491  -0.3353 -0.6384 1336 ARG A CD  
10240 N NE  . ARG A 1336 ? 3.0752 3.8169 3.2363 0.7314  -0.3378 -0.6153 1336 ARG A NE  
10241 C CZ  . ARG A 1336 ? 3.2199 3.9320 3.3200 0.7461  -0.3531 -0.6169 1336 ARG A CZ  
10242 N NH1 . ARG A 1336 ? 3.3015 3.9991 3.3806 0.7799  -0.3678 -0.6396 1336 ARG A NH1 
10243 N NH2 . ARG A 1336 ? 3.2559 3.9534 3.3165 0.7270  -0.3532 -0.5956 1336 ARG A NH2 
10244 N N   . PRO A 1337 ? 1.3858 2.2448 1.8354 0.7322  -0.2961 -0.7109 1337 PRO A N   
10245 C CA  . PRO A 1337 ? 1.2862 2.1541 1.7514 0.7412  -0.3076 -0.7558 1337 PRO A CA  
10246 C C   . PRO A 1337 ? 1.3067 2.1499 1.7122 0.7670  -0.3315 -0.7775 1337 PRO A C   
10247 O O   . PRO A 1337 ? 1.3282 2.1481 1.6847 0.7788  -0.3387 -0.7593 1337 PRO A O   
10248 C CB  . PRO A 1337 ? 1.2797 2.1681 1.8052 0.7538  -0.3032 -0.7899 1337 PRO A CB  
10249 C CG  . PRO A 1337 ? 1.2910 2.1879 1.8483 0.7387  -0.2812 -0.7550 1337 PRO A CG  
10250 C CD  . PRO A 1337 ? 1.3502 2.2231 1.8485 0.7367  -0.2829 -0.7129 1337 PRO A CD  
10251 N N   . VAL A 1338 ? 1.2794 2.1275 1.6878 0.7757  -0.3432 -0.8138 1338 VAL A N   
10252 C CA  . VAL A 1338 ? 1.4047 2.2310 1.7594 0.8028  -0.3650 -0.8360 1338 VAL A CA  
10253 C C   . VAL A 1338 ? 1.4864 2.3275 1.8639 0.8178  -0.3760 -0.8850 1338 VAL A C   
10254 O O   . VAL A 1338 ? 1.4698 2.3276 1.8783 0.8009  -0.3703 -0.8935 1338 VAL A O   
10255 C CB  . VAL A 1338 ? 1.9423 2.7406 2.2310 0.7937  -0.3702 -0.8061 1338 VAL A CB  
10256 C CG1 . VAL A 1338 ? 1.9761 2.7623 2.2311 0.8113  -0.3878 -0.8367 1338 VAL A CG1 
10257 C CG2 . VAL A 1338 ? 1.9929 2.7666 2.2345 0.8031  -0.3729 -0.7764 1338 VAL A CG2 
10258 N N   . GLU A 1339 ? 2.0882 2.9250 2.4512 0.8503  -0.3918 -0.9172 1339 GLU A N   
10259 C CA  . GLU A 1339 ? 2.1559 3.0085 2.5384 0.8676  -0.4034 -0.9648 1339 GLU A CA  
10260 C C   . GLU A 1339 ? 2.1881 3.0197 2.5135 0.8790  -0.4184 -0.9700 1339 GLU A C   
10261 O O   . GLU A 1339 ? 2.2207 3.0251 2.4886 0.8922  -0.4270 -0.9540 1339 GLU A O   
10262 C CB  . GLU A 1339 ? 2.2603 3.1254 2.6638 0.8960  -0.4113 -0.9992 1339 GLU A CB  
10263 C CG  . GLU A 1339 ? 2.2809 3.1713 2.7540 0.8833  -0.3948 -1.0033 1339 GLU A CG  
10264 C CD  . GLU A 1339 ? 2.3702 3.2656 2.8543 0.9076  -0.3992 -1.0234 1339 GLU A CD  
10265 O OE1 . GLU A 1339 ? 2.4355 3.3340 2.9040 0.9366  -0.4164 -1.0590 1339 GLU A OE1 
10266 O OE2 . GLU A 1339 ? 2.3611 3.2588 2.8706 0.8977  -0.3847 -1.0036 1339 GLU A OE2 
10267 N N   . VAL A 1340 ? 1.8629 2.7066 2.2049 0.8722  -0.4200 -0.9901 1340 VAL A N   
10268 C CA  . VAL A 1340 ? 1.9420 2.7673 2.2347 0.8836  -0.4331 -0.9987 1340 VAL A CA  
10269 C C   . VAL A 1340 ? 2.0189 2.8460 2.2966 0.9214  -0.4511 -1.0376 1340 VAL A C   
10270 O O   . VAL A 1340 ? 2.0344 2.8881 2.3527 0.9319  -0.4553 -1.0756 1340 VAL A O   
10271 C CB  . VAL A 1340 ? 1.9287 2.7671 2.2438 0.8651  -0.4288 -1.0079 1340 VAL A CB  
10272 C CG1 . VAL A 1340 ? 1.9958 2.8184 2.2654 0.8834  -0.4438 -1.0269 1340 VAL A CG1 
10273 C CG2 . VAL A 1340 ? 1.8840 2.7169 2.1991 0.8289  -0.4128 -0.9656 1340 VAL A CG2 
10274 N N   . LEU A 1341 ? 2.4646 3.2642 2.6833 0.9415  -0.4615 -1.0270 1341 LEU A N   
10275 C CA  . LEU A 1341 ? 2.5389 3.3378 2.7338 0.9796  -0.4789 -1.0586 1341 LEU A CA  
10276 C C   . LEU A 1341 ? 2.6212 3.4214 2.8012 0.9919  -0.4892 -1.0858 1341 LEU A C   
10277 O O   . LEU A 1341 ? 2.6026 3.4313 2.8234 0.9980  -0.4923 -1.1213 1341 LEU A O   
10278 C CB  . LEU A 1341 ? 2.5863 3.3537 2.7202 0.9957  -0.4854 -1.0340 1341 LEU A CB  
10279 C CG  . LEU A 1341 ? 2.8149 3.5810 2.9551 0.9966  -0.4801 -1.0141 1341 LEU A CG  
10280 C CD1 . LEU A 1341 ? 2.7896 3.5868 2.9774 1.0146  -0.4836 -1.0504 1341 LEU A CD1 
10281 C CD2 . LEU A 1341 ? 2.7638 3.5263 2.9219 0.9594  -0.4617 -0.9739 1341 LEU A CD2 
10282 N N   . LEU A 1342 ? 2.0838 2.8524 2.2054 0.9942  -0.4934 -1.0674 1342 LEU A N   
10283 C CA  . LEU A 1342 ? 2.1406 2.9012 2.2309 1.0130  -0.5046 -1.0891 1342 LEU A CA  
10284 C C   . LEU A 1342 ? 2.0895 2.8739 2.2183 1.0033  -0.5029 -1.1152 1342 LEU A C   
10285 O O   . LEU A 1342 ? 2.0067 2.8192 2.1935 0.9853  -0.4944 -1.1234 1342 LEU A O   
10286 C CB  . LEU A 1342 ? 2.1669 2.8864 2.1929 1.0068  -0.5039 -1.0568 1342 LEU A CB  
10287 C CG  . LEU A 1342 ? 2.1287 2.8258 2.1286 0.9968  -0.4980 -1.0167 1342 LEU A CG  
10288 C CD1 . LEU A 1342 ? 2.1702 2.8272 2.1074 0.9894  -0.4971 -0.9859 1342 LEU A CD1 
10289 C CD2 . LEU A 1342 ? 2.1526 2.8534 2.1456 1.0272  -0.5072 -1.0265 1342 LEU A CD2 
10290 N N   . ASN A 1343 ? 2.5150 3.2881 2.6113 1.0164  -0.5108 -1.1283 1343 ASN A N   
10291 C CA  . ASN A 1343 ? 2.5508 3.3448 2.6786 1.0087  -0.5098 -1.1521 1343 ASN A CA  
10292 C C   . ASN A 1343 ? 2.5467 3.3171 2.6454 0.9875  -0.5036 -1.1317 1343 ASN A C   
10293 O O   . ASN A 1343 ? 2.5974 3.3473 2.6515 1.0034  -0.5107 -1.1373 1343 ASN A O   
10294 C CB  . ASN A 1343 ? 2.6870 3.4987 2.8150 1.0439  -0.5244 -1.1940 1343 ASN A CB  
10295 C CG  . ASN A 1343 ? 2.7745 3.6212 2.9497 1.0580  -0.5286 -1.2218 1343 ASN A CG  
10296 O OD1 . ASN A 1343 ? 2.8145 3.6900 3.0163 1.0748  -0.5364 -1.2590 1343 ASN A OD1 
10297 N ND2 . ASN A 1343 ? 2.7889 3.6342 2.9757 1.0504  -0.5230 -1.2040 1343 ASN A ND2 
10298 N N   . ASP A 1344 ? 2.8227 3.5975 2.9482 0.9514  -0.4895 -1.1082 1344 ASP A N   
10299 C CA  . ASP A 1344 ? 2.7778 3.5308 2.8760 0.9267  -0.4818 -1.0841 1344 ASP A CA  
10300 C C   . ASP A 1344 ? 2.6876 3.4661 2.8405 0.8921  -0.4678 -1.0755 1344 ASP A C   
10301 O O   . ASP A 1344 ? 2.6517 3.4591 2.8584 0.8869  -0.4630 -1.0829 1344 ASP A O   
10302 C CB  . ASP A 1344 ? 2.7447 3.4609 2.7900 0.9185  -0.4784 -1.0450 1344 ASP A CB  
10303 C CG  . ASP A 1344 ? 2.7106 3.3913 2.6964 0.9185  -0.4804 -1.0345 1344 ASP A CG  
10304 O OD1 . ASP A 1344 ? 2.6907 3.3756 2.6789 0.9190  -0.4818 -1.0532 1344 ASP A OD1 
10305 O OD2 . ASP A 1344 ? 2.7086 3.3569 2.6453 0.9180  -0.4800 -1.0074 1344 ASP A OD2 
10306 N N   . ASP A 1345 ? 2.6642 3.4327 2.8041 0.8684  -0.4606 -1.0601 1345 ASP A N   
10307 C CA  . ASP A 1345 ? 2.5612 3.3528 2.7486 0.8337  -0.4459 -1.0454 1345 ASP A CA  
10308 C C   . ASP A 1345 ? 2.1715 2.9484 2.3437 0.8085  -0.4346 -1.0012 1345 ASP A C   
10309 O O   . ASP A 1345 ? 2.2305 2.9735 2.3454 0.8090  -0.4367 -0.9793 1345 ASP A O   
10310 C CB  . ASP A 1345 ? 2.5622 3.3559 2.7485 0.8204  -0.4434 -1.0522 1345 ASP A CB  
10311 C CG  . ASP A 1345 ? 2.6432 3.4488 2.8371 0.8479  -0.4554 -1.0944 1345 ASP A CG  
10312 O OD1 . ASP A 1345 ? 2.6337 3.4594 2.8577 0.8376  -0.4522 -1.1082 1345 ASP A OD1 
10313 O OD2 . ASP A 1345 ? 2.7071 3.5036 2.8769 0.8803  -0.4680 -1.1132 1345 ASP A OD2 
10314 N N   . LEU A 1346 ? 2.0084 2.8109 2.2318 0.7870  -0.4222 -0.9876 1346 LEU A N   
10315 C CA  . LEU A 1346 ? 1.9564 2.7487 2.1684 0.7665  -0.4117 -0.9465 1346 LEU A CA  
10316 C C   . LEU A 1346 ? 1.9492 2.7411 2.1566 0.7304  -0.3986 -0.9156 1346 LEU A C   
10317 O O   . LEU A 1346 ? 1.9612 2.7696 2.1923 0.7183  -0.3951 -0.9269 1346 LEU A O   
10318 C CB  . LEU A 1346 ? 1.8385 2.6570 2.1051 0.7639  -0.4039 -0.9446 1346 LEU A CB  
10319 C CG  . LEU A 1346 ? 1.8072 2.6114 2.0536 0.7501  -0.3955 -0.9031 1346 LEU A CG  
10320 C CD1 . LEU A 1346 ? 1.8835 2.6486 2.0583 0.7682  -0.4069 -0.8935 1346 LEU A CD1 
10321 C CD2 . LEU A 1346 ? 1.7620 2.5869 2.0554 0.7542  -0.3893 -0.9040 1346 LEU A CD2 
10322 N N   . ILE A 1347 ? 1.8357 2.6103 2.0129 0.7132  -0.3916 -0.8765 1347 ILE A N   
10323 C CA  . ILE A 1347 ? 1.7212 2.4982 1.8934 0.6769  -0.3783 -0.8439 1347 ILE A CA  
10324 C C   . ILE A 1347 ? 1.6197 2.3966 1.7888 0.6550  -0.3662 -0.8002 1347 ILE A C   
10325 O O   . ILE A 1347 ? 1.6560 2.4035 1.7725 0.6562  -0.3693 -0.7783 1347 ILE A O   
10326 C CB  . ILE A 1347 ? 1.7722 2.5180 1.8840 0.6737  -0.3839 -0.8414 1347 ILE A CB  
10327 C CG1 . ILE A 1347 ? 1.8522 2.5733 1.9274 0.7101  -0.4010 -0.8736 1347 ILE A CG1 
10328 C CG2 . ILE A 1347 ? 1.7257 2.4905 1.8600 0.6504  -0.3763 -0.8448 1347 ILE A CG2 
10329 C CD1 . ILE A 1347 ? 1.9503 2.6356 1.9622 0.7088  -0.4054 -0.8693 1347 ILE A CD1 
10330 N N   . VAL A 1348 ? 1.7633 2.5740 1.9896 0.6351  -0.3518 -0.7873 1348 VAL A N   
10331 C CA  . VAL A 1348 ? 1.7238 2.5418 1.9536 0.6077  -0.3368 -0.7428 1348 VAL A CA  
10332 C C   . VAL A 1348 ? 1.8448 2.6618 2.0516 0.5773  -0.3295 -0.7204 1348 VAL A C   
10333 O O   . VAL A 1348 ? 1.8610 2.6909 2.0850 0.5709  -0.3293 -0.7387 1348 VAL A O   
10334 C CB  . VAL A 1348 ? 1.5799 2.4372 1.8832 0.5969  -0.3222 -0.7386 1348 VAL A CB  
10335 C CG1 . VAL A 1348 ? 1.5628 2.4282 1.8699 0.5731  -0.3065 -0.6918 1348 VAL A CG1 
10336 C CG2 . VAL A 1348 ? 1.5752 2.4378 1.9091 0.6268  -0.3298 -0.7712 1348 VAL A CG2 
10337 N N   . SER A 1349 ? 1.9267 2.7303 2.0960 0.5579  -0.3234 -0.6813 1349 SER A N   
10338 C CA  . SER A 1349 ? 1.9516 2.7461 2.0838 0.5321  -0.3197 -0.6629 1349 SER A CA  
10339 C C   . SER A 1349 ? 2.0123 2.8001 2.1120 0.5065  -0.3104 -0.6161 1349 SER A C   
10340 O O   . SER A 1349 ? 2.0649 2.8200 2.1038 0.5044  -0.3164 -0.6056 1349 SER A O   
10341 C CB  . SER A 1349 ? 1.9983 2.7557 2.0758 0.5510  -0.3353 -0.6878 1349 SER A CB  
10342 O OG  . SER A 1349 ? 2.0497 2.7758 2.0885 0.5773  -0.3465 -0.6903 1349 SER A OG  
10343 N N   . THR A 1350 ? 1.7367 2.5562 1.8773 0.4866  -0.2950 -0.5880 1350 THR A N   
10344 C CA  . THR A 1350 ? 1.7554 2.5750 1.8709 0.4614  -0.2849 -0.5421 1350 THR A CA  
10345 C C   . THR A 1350 ? 1.7658 2.5714 1.8326 0.4379  -0.2848 -0.5291 1350 THR A C   
10346 O O   . THR A 1350 ? 1.7445 2.5488 1.8095 0.4365  -0.2889 -0.5530 1350 THR A O   
10347 C CB  . THR A 1350 ? 1.7972 2.6613 1.9719 0.4394  -0.2655 -0.5150 1350 THR A CB  
10348 O OG1 . THR A 1350 ? 1.8320 2.6955 1.9858 0.4243  -0.2570 -0.4715 1350 THR A OG1 
10349 C CG2 . THR A 1350 ? 1.7307 2.6266 1.9344 0.4124  -0.2549 -0.5124 1350 THR A CG2 
10350 N N   . GLY A 1351 ? 1.7290 2.5230 1.7553 0.4202  -0.2805 -0.4923 1351 GLY A N   
10351 C CA  . GLY A 1351 ? 1.7367 2.5232 1.7211 0.3920  -0.2772 -0.4739 1351 GLY A CA  
10352 C C   . GLY A 1351 ? 1.6212 2.4539 1.6457 0.3576  -0.2594 -0.4476 1351 GLY A C   
10353 O O   . GLY A 1351 ? 1.5415 2.4059 1.6220 0.3575  -0.2535 -0.4622 1351 GLY A O   
10354 N N   . PHE A 1352 ? 1.7392 2.5784 1.7375 0.3284  -0.2503 -0.4085 1352 PHE A N   
10355 C CA  . PHE A 1352 ? 1.6474 2.5344 1.6845 0.2959  -0.2330 -0.3834 1352 PHE A CA  
10356 C C   . PHE A 1352 ? 1.5677 2.4905 1.6629 0.2968  -0.2202 -0.3640 1352 PHE A C   
10357 O O   . PHE A 1352 ? 1.5424 2.4793 1.6883 0.3145  -0.2199 -0.3876 1352 PHE A O   
10358 C CB  . PHE A 1352 ? 1.6437 2.5339 1.6388 0.2613  -0.2258 -0.3478 1352 PHE A CB  
10359 C CG  . PHE A 1352 ? 1.5413 2.4850 1.5775 0.2286  -0.2079 -0.3228 1352 PHE A CG  
10360 C CD1 . PHE A 1352 ? 1.4646 2.4344 1.5426 0.2249  -0.2044 -0.3450 1352 PHE A CD1 
10361 C CD2 . PHE A 1352 ? 1.5186 2.4890 1.5541 0.2027  -0.1943 -0.2767 1352 PHE A CD2 
10362 C CE1 . PHE A 1352 ? 1.3663 2.3874 1.4844 0.1965  -0.1876 -0.3223 1352 PHE A CE1 
10363 C CE2 . PHE A 1352 ? 1.4212 2.4446 1.4970 0.1738  -0.1771 -0.2533 1352 PHE A CE2 
10364 C CZ  . PHE A 1352 ? 1.3524 2.4007 1.4694 0.1711  -0.1738 -0.2764 1352 PHE A CZ  
10365 N N   . GLY A 1353 ? 1.3719 2.3106 1.4599 0.2762  -0.2087 -0.3203 1353 GLY A N   
10366 C CA  . GLY A 1353 ? 1.3169 2.2805 1.4477 0.2796  -0.1970 -0.2968 1353 GLY A CA  
10367 C C   . GLY A 1353 ? 1.2301 2.2486 1.4213 0.2572  -0.1762 -0.2723 1353 GLY A C   
10368 O O   . GLY A 1353 ? 1.1897 2.2345 1.3792 0.2277  -0.1669 -0.2531 1353 GLY A O   
10369 N N   . SER A 1354 ? 1.4880 2.5237 1.7320 0.2718  -0.1682 -0.2720 1354 SER A N   
10370 C CA  . SER A 1354 ? 1.3901 2.4770 1.6991 0.2556  -0.1472 -0.2506 1354 SER A CA  
10371 C C   . SER A 1354 ? 1.3270 2.4211 1.6927 0.2794  -0.1421 -0.2642 1354 SER A C   
10372 O O   . SER A 1354 ? 1.3687 2.4301 1.7193 0.3065  -0.1537 -0.2819 1354 SER A O   
10373 C CB  . SER A 1354 ? 1.3993 2.5128 1.6981 0.2272  -0.1313 -0.1966 1354 SER A CB  
10374 O OG  . SER A 1354 ? 1.4247 2.5191 1.7006 0.2380  -0.1323 -0.1752 1354 SER A OG  
10375 N N   . GLY A 1355 ? 1.1555 2.2929 1.5866 0.2691  -0.1241 -0.2555 1355 GLY A N   
10376 C CA  . GLY A 1355 ? 1.1109 2.2574 1.6007 0.2890  -0.1170 -0.2691 1355 GLY A CA  
10377 C C   . GLY A 1355 ? 1.1242 2.2588 1.6394 0.3115  -0.1292 -0.3220 1355 GLY A C   
10378 O O   . GLY A 1355 ? 1.1606 2.2959 1.6677 0.3059  -0.1369 -0.3440 1355 GLY A O   
10379 N N   . LEU A 1356 ? 1.2881 2.4109 1.8307 0.3374  -0.1316 -0.3430 1356 LEU A N   
10380 C CA  . LEU A 1356 ? 1.2886 2.4144 1.8768 0.3560  -0.1365 -0.3878 1356 LEU A CA  
10381 C C   . LEU A 1356 ? 1.4338 2.5270 2.0154 0.3897  -0.1508 -0.4205 1356 LEU A C   
10382 O O   . LEU A 1356 ? 1.4840 2.5764 2.0824 0.3985  -0.1430 -0.4071 1356 LEU A O   
10383 C CB  . LEU A 1356 ? 1.1886 2.3581 1.8535 0.3449  -0.1130 -0.3739 1356 LEU A CB  
10384 C CG  . LEU A 1356 ? 1.0909 2.2950 1.7897 0.3251  -0.1045 -0.3758 1356 LEU A CG  
10385 C CD1 . LEU A 1356 ? 0.9807 2.2294 1.7491 0.3108  -0.0779 -0.3487 1356 LEU A CD1 
10386 C CD2 . LEU A 1356 ? 1.0875 2.2790 1.7997 0.3448  -0.1199 -0.4285 1356 LEU A CD2 
10387 N N   . ALA A 1357 ? 1.8920 2.9602 2.4509 0.4092  -0.1711 -0.4633 1357 ALA A N   
10388 C CA  . ALA A 1357 ? 1.8547 2.8945 2.4055 0.4421  -0.1857 -0.4957 1357 ALA A CA  
10389 C C   . ALA A 1357 ? 1.7995 2.8466 2.3947 0.4601  -0.1921 -0.5441 1357 ALA A C   
10390 O O   . ALA A 1357 ? 1.7860 2.8306 2.3708 0.4606  -0.2024 -0.5690 1357 ALA A O   
10391 C CB  . ALA A 1357 ? 1.8918 2.8896 2.3659 0.4550  -0.2062 -0.5020 1357 ALA A CB  
10392 N N   . THR A 1358 ? 1.2272 2.2832 1.8708 0.4746  -0.1857 -0.5574 1358 THR A N   
10393 C CA  . THR A 1358 ? 1.2003 2.2650 1.8892 0.4916  -0.1911 -0.6037 1358 THR A CA  
10394 C C   . THR A 1358 ? 1.2867 2.3199 1.9428 0.5241  -0.2138 -0.6433 1358 THR A C   
10395 O O   . THR A 1358 ? 1.3031 2.3276 1.9685 0.5424  -0.2151 -0.6521 1358 THR A O   
10396 C CB  . THR A 1358 ? 1.4013 2.4944 2.1655 0.4895  -0.1715 -0.6020 1358 THR A CB  
10397 O OG1 . THR A 1358 ? 1.4028 2.4907 2.1622 0.4882  -0.1605 -0.5687 1358 THR A OG1 
10398 C CG2 . THR A 1358 ? 1.3218 2.4523 2.1336 0.4631  -0.1528 -0.5841 1358 THR A CG2 
10399 N N   . VAL A 1359 ? 1.0700 2.0872 1.6872 0.5310  -0.2311 -0.6663 1359 VAL A N   
10400 C CA  . VAL A 1359 ? 1.1888 2.1800 1.7755 0.5618  -0.2529 -0.7060 1359 VAL A CA  
10401 C C   . VAL A 1359 ? 1.2335 2.2443 1.8795 0.5770  -0.2541 -0.7485 1359 VAL A C   
10402 O O   . VAL A 1359 ? 1.1781 2.2081 1.8534 0.5696  -0.2529 -0.7662 1359 VAL A O   
10403 C CB  . VAL A 1359 ? 1.1761 2.1471 1.7070 0.5618  -0.2680 -0.7152 1359 VAL A CB  
10404 C CG1 . VAL A 1359 ? 1.2329 2.1864 1.7460 0.5926  -0.2885 -0.7611 1359 VAL A CG1 
10405 C CG2 . VAL A 1359 ? 1.2140 2.1590 1.6801 0.5528  -0.2702 -0.6798 1359 VAL A CG2 
10406 N N   . HIS A 1360 ? 1.1048 2.1129 1.7710 0.5967  -0.2555 -0.7642 1360 HIS A N   
10407 C CA  . HIS A 1360 ? 1.1370 2.1584 1.8479 0.6154  -0.2613 -0.8108 1360 HIS A CA  
10408 C C   . HIS A 1360 ? 1.2155 2.2121 1.8838 0.6472  -0.2844 -0.8446 1360 HIS A C   
10409 O O   . HIS A 1360 ? 1.2992 2.2688 1.9150 0.6584  -0.2929 -0.8313 1360 HIS A O   
10410 C CB  . HIS A 1360 ? 1.1475 2.1868 1.9185 0.6167  -0.2463 -0.8122 1360 HIS A CB  
10411 C CG  . HIS A 1360 ? 1.0862 2.1562 1.9155 0.5893  -0.2221 -0.7876 1360 HIS A CG  
10412 N ND1 . HIS A 1360 ? 1.0465 2.1206 1.8776 0.5697  -0.2039 -0.7402 1360 HIS A ND1 
10413 C CD2 . HIS A 1360 ? 1.0409 2.1404 1.9308 0.5795  -0.2124 -0.8037 1360 HIS A CD2 
10414 C CE1 . HIS A 1360 ? 0.9875 2.0929 1.8778 0.5492  -0.1836 -0.7274 1360 HIS A CE1 
10415 N NE2 . HIS A 1360 ? 0.9883 2.1090 1.9154 0.5545  -0.1883 -0.7654 1360 HIS A NE2 
10416 N N   . VAL A 1361 ? 1.1871 2.1952 1.8814 0.6624  -0.2940 -0.8886 1361 VAL A N   
10417 C CA  . VAL A 1361 ? 1.2561 2.2461 1.9149 0.6939  -0.3159 -0.9243 1361 VAL A CA  
10418 C C   . VAL A 1361 ? 1.2644 2.2780 1.9775 0.7092  -0.3196 -0.9709 1361 VAL A C   
10419 O O   . VAL A 1361 ? 1.2445 2.2761 1.9839 0.7053  -0.3213 -0.9933 1361 VAL A O   
10420 C CB  . VAL A 1361 ? 1.2710 2.2382 1.8658 0.6984  -0.3311 -0.9250 1361 VAL A CB  
10421 C CG1 . VAL A 1361 ? 1.2186 2.1915 1.8163 0.7185  -0.3466 -0.9710 1361 VAL A CG1 
10422 C CG2 . VAL A 1361 ? 1.2478 2.1807 1.7758 0.7119  -0.3410 -0.9073 1361 VAL A CG2 
10423 N N   . THR A 1362 ? 0.9202 1.9345 1.6510 0.7253  -0.3198 -0.9840 1362 THR A N   
10424 C CA  . THR A 1362 ? 0.9063 1.9431 1.6908 0.7391  -0.3216 -1.0268 1362 THR A CA  
10425 C C   . THR A 1362 ? 0.9376 1.9638 1.6877 0.7729  -0.3448 -1.0657 1362 THR A C   
10426 O O   . THR A 1362 ? 1.0927 2.1030 1.8146 0.7909  -0.3516 -1.0653 1362 THR A O   
10427 C CB  . THR A 1362 ? 0.9008 1.9505 1.7388 0.7306  -0.3026 -1.0165 1362 THR A CB  
10428 O OG1 . THR A 1362 ? 0.9101 1.9838 1.8059 0.7396  -0.3022 -1.0584 1362 THR A OG1 
10429 C CG2 . THR A 1362 ? 0.9458 1.9724 1.7463 0.7431  -0.3050 -0.9984 1362 THR A CG2 
10430 N N   . THR A 1363 ? 1.0668 2.1030 1.8180 0.7810  -0.3565 -1.0969 1363 THR A N   
10431 C CA  . THR A 1363 ? 1.2046 2.2346 1.9221 0.8124  -0.3788 -1.1340 1363 THR A CA  
10432 C C   . THR A 1363 ? 1.2897 2.3475 2.0594 0.8272  -0.3825 -1.1801 1363 THR A C   
10433 O O   . THR A 1363 ? 1.2677 2.3520 2.0930 0.8147  -0.3746 -1.1962 1363 THR A O   
10434 C CB  . THR A 1363 ? 1.9443 2.9683 2.6277 0.8137  -0.3896 -1.1408 1363 THR A CB  
10435 O OG1 . THR A 1363 ? 1.9163 2.9699 2.6495 0.8104  -0.3890 -1.1718 1363 THR A OG1 
10436 C CG2 . THR A 1363 ? 1.9162 2.9236 2.5712 0.7880  -0.3799 -1.0970 1363 THR A CG2 
10437 N N   . VAL A 1364 ? 0.9089 1.9615 1.6601 0.8541  -0.3947 -1.2013 1364 VAL A N   
10438 C CA  . VAL A 1364 ? 0.8977 1.9759 1.6945 0.8693  -0.3986 -1.2449 1364 VAL A CA  
10439 C C   . VAL A 1364 ? 0.9962 2.0800 1.7659 0.9011  -0.4212 -1.2859 1364 VAL A C   
10440 O O   . VAL A 1364 ? 1.0707 2.1332 1.7801 0.9219  -0.4353 -1.2820 1364 VAL A O   
10441 C CB  . VAL A 1364 ? 0.9251 1.9993 1.7341 0.8739  -0.3917 -1.2388 1364 VAL A CB  
10442 C CG1 . VAL A 1364 ? 0.9149 2.0118 1.7546 0.8952  -0.4006 -1.2872 1364 VAL A CG1 
10443 C CG2 . VAL A 1364 ? 0.8487 1.9285 1.7061 0.8437  -0.3668 -1.2087 1364 VAL A CG2 
10444 N N   . VAL A 1365 ? 1.6457 2.7600 2.4617 0.9051  -0.4242 -1.3254 1365 VAL A N   
10445 C CA  . VAL A 1365 ? 1.7173 2.8408 2.5094 0.9334  -0.4447 -1.3627 1365 VAL A CA  
10446 C C   . VAL A 1365 ? 1.8103 2.9693 2.6589 0.9427  -0.4470 -1.4092 1365 VAL A C   
10447 O O   . VAL A 1365 ? 1.8009 2.9792 2.7123 0.9224  -0.4320 -1.4139 1365 VAL A O   
10448 C CB  . VAL A 1365 ? 1.6477 2.7678 2.4166 0.9292  -0.4503 -1.3596 1365 VAL A CB  
10449 C CG1 . VAL A 1365 ? 1.5914 2.7443 2.4218 0.9155  -0.4444 -1.3838 1365 VAL A CG1 
10450 C CG2 . VAL A 1365 ? 1.7002 2.8104 2.4105 0.9606  -0.4713 -1.3770 1365 VAL A CG2 
10451 N N   . HIS A 1366 ? 1.6619 2.8298 2.4883 0.9734  -0.4651 -1.4426 1366 HIS A N   
10452 C CA  . HIS A 1366 ? 1.6676 2.8710 2.5429 0.9841  -0.4693 -1.4897 1366 HIS A CA  
10453 C C   . HIS A 1366 ? 1.6327 2.8612 2.5164 0.9937  -0.4812 -1.5231 1366 HIS A C   
10454 O O   . HIS A 1366 ? 1.6721 2.8938 2.5049 1.0153  -0.4972 -1.5289 1366 HIS A O   
10455 C CB  . HIS A 1366 ? 1.7571 2.9604 2.6086 1.0115  -0.4807 -1.5074 1366 HIS A CB  
10456 C CG  . HIS A 1366 ? 1.7807 2.9585 2.6183 1.0050  -0.4705 -1.4743 1366 HIS A CG  
10457 N ND1 . HIS A 1366 ? 1.7807 2.9227 2.5668 0.9992  -0.4678 -1.4288 1366 HIS A ND1 
10458 C CD2 . HIS A 1366 ? 1.8152 2.9973 2.6824 1.0034  -0.4618 -1.4788 1366 HIS A CD2 
10459 C CE1 . HIS A 1366 ? 1.7945 2.9216 2.5797 0.9945  -0.4583 -1.4066 1366 HIS A CE1 
10460 N NE2 . HIS A 1366 ? 1.8168 2.9671 2.6509 0.9973  -0.4542 -1.4360 1366 HIS A NE2 
10461 N N   . LYS A 1367 ? 1.6362 2.8939 2.5856 0.9776  -0.4723 -1.5442 1367 LYS A N   
10462 C CA  . LYS A 1367 ? 1.6777 2.9634 2.6425 0.9857  -0.4827 -1.5780 1367 LYS A CA  
10463 C C   . LYS A 1367 ? 1.6883 3.0125 2.7008 0.9969  -0.4880 -1.6272 1367 LYS A C   
10464 O O   . LYS A 1367 ? 1.6903 3.0215 2.7379 0.9920  -0.4796 -1.6358 1367 LYS A O   
10465 C CB  . LYS A 1367 ? 1.6735 2.9628 2.6668 0.9593  -0.4711 -1.5623 1367 LYS A CB  
10466 C CG  . LYS A 1367 ? 1.6406 2.9339 2.6940 0.9273  -0.4481 -1.5440 1367 LYS A CG  
10467 C CD  . LYS A 1367 ? 1.6087 2.9010 2.6748 0.9038  -0.4384 -1.5215 1367 LYS A CD  
10468 C CE  . LYS A 1367 ? 1.6227 2.8804 2.6196 0.9045  -0.4427 -1.4845 1367 LYS A CE  
10469 N NZ  . LYS A 1367 ? 1.5854 2.8414 2.5980 0.8775  -0.4299 -1.4576 1367 LYS A NZ  
10470 N N   . THR A 1368 ? 1.2752 3.4171 2.9950 0.8082  -0.6548 -1.3149 1368 THR A N   
10471 C CA  . THR A 1368 ? 1.2753 3.4470 3.0307 0.8007  -0.6796 -1.3389 1368 THR A CA  
10472 C C   . THR A 1368 ? 1.2652 3.4730 3.0736 0.7668  -0.6580 -1.3623 1368 THR A C   
10473 O O   . THR A 1368 ? 1.3286 3.5526 3.1582 0.7534  -0.6730 -1.3805 1368 THR A O   
10474 C CB  . THR A 1368 ? 1.3103 3.5249 3.1113 0.8269  -0.7125 -1.3523 1368 THR A CB  
10475 O OG1 . THR A 1368 ? 1.3084 3.5726 3.1740 0.8226  -0.6965 -1.3675 1368 THR A OG1 
10476 C CG2 . THR A 1368 ? 1.2920 3.4756 3.0473 0.8603  -0.7295 -1.3289 1368 THR A CG2 
10477 N N   . SER A 1369 ? 0.6216 2.8422 2.4518 0.7530  -0.6232 -1.3620 1369 SER A N   
10478 C CA  . SER A 1369 ? 0.6252 2.8836 2.5098 0.7216  -0.6006 -1.3840 1369 SER A CA  
10479 C C   . SER A 1369 ? 0.5993 2.8328 2.4617 0.6960  -0.5561 -1.3725 1369 SER A C   
10480 O O   . SER A 1369 ? 0.5302 2.7380 2.3607 0.7049  -0.5371 -1.3520 1369 SER A O   
10481 C CB  . SER A 1369 ? 0.6510 2.9752 2.6149 0.7283  -0.6054 -1.4064 1369 SER A CB  
10482 O OG  . SER A 1369 ? 0.7142 3.0692 2.7099 0.7454  -0.6449 -1.4222 1369 SER A OG  
10483 N N   . THR A 1370 ? 0.9910 3.2326 2.8712 0.6640  -0.5404 -1.3861 1370 THR A N   
10484 C CA  . THR A 1370 ? 1.0263 3.2542 2.8984 0.6360  -0.4984 -1.3805 1370 THR A CA  
10485 C C   . THR A 1370 ? 1.1575 3.4452 3.1064 0.6199  -0.4813 -1.4041 1370 THR A C   
10486 O O   . THR A 1370 ? 1.1594 3.4470 3.1150 0.5961  -0.4458 -1.4034 1370 THR A O   
10487 C CB  . THR A 1370 ? 0.9773 3.1730 2.8176 0.6090  -0.4906 -1.3799 1370 THR A CB  
10488 O OG1 . THR A 1370 ? 0.9307 3.0692 2.6977 0.6232  -0.5039 -1.3573 1370 THR A OG1 
10489 C CG2 . THR A 1370 ? 0.9474 3.1315 2.7831 0.5791  -0.4473 -1.3753 1370 THR A CG2 
10490 N N   . SER A 1371 ? 1.4869 3.8260 3.4941 0.6329  -0.5066 -1.4249 1371 SER A N   
10491 C CA  . SER A 1371 ? 1.6018 4.0018 3.6862 0.6199  -0.4934 -1.4487 1371 SER A CA  
10492 C C   . SER A 1371 ? 1.6302 4.0300 3.7164 0.6152  -0.4559 -1.4389 1371 SER A C   
10493 O O   . SER A 1371 ? 1.6515 4.0799 3.7781 0.5906  -0.4286 -1.4518 1371 SER A O   
10494 C CB  . SER A 1371 ? 1.6776 4.1273 3.8157 0.6441  -0.5265 -1.4661 1371 SER A CB  
10495 O OG  . SER A 1371 ? 1.6916 4.1284 3.8073 0.6765  -0.5365 -1.4501 1371 SER A OG  
10496 N N   . GLU A 1372 ? 1.8651 4.2322 3.9069 0.6386  -0.4546 -1.4160 1372 GLU A N   
10497 C CA  . GLU A 1372 ? 1.8717 4.2308 3.9053 0.6354  -0.4199 -1.4037 1372 GLU A CA  
10498 C C   . GLU A 1372 ? 1.7405 4.0684 3.7440 0.6030  -0.3839 -1.3950 1372 GLU A C   
10499 O O   . GLU A 1372 ? 1.7370 4.0939 3.7810 0.5787  -0.3571 -1.4083 1372 GLU A O   
10500 C CB  . GLU A 1372 ? 1.9994 4.3190 3.9791 0.6655  -0.4277 -1.3775 1372 GLU A CB  
10501 C CG  . GLU A 1372 ? 2.1318 4.3961 4.0419 0.6749  -0.4476 -1.3582 1372 GLU A CG  
10502 C CD  . GLU A 1372 ? 2.2081 4.4232 4.0545 0.6958  -0.4433 -1.3278 1372 GLU A CD  
10503 O OE1 . GLU A 1372 ? 2.2410 4.4687 4.1006 0.7106  -0.4351 -1.3233 1372 GLU A OE1 
10504 O OE2 . GLU A 1372 ? 2.2232 4.3867 4.0062 0.6974  -0.4484 -1.3085 1372 GLU A OE2 
10505 N N   . GLU A 1373 ? 1.4018 3.6706 3.3342 0.6033  -0.3848 -1.3727 1373 GLU A N   
10506 C CA  . GLU A 1373 ? 1.2653 3.4905 3.1515 0.5791  -0.3520 -1.3567 1373 GLU A CA  
10507 C C   . GLU A 1373 ? 1.2127 3.4597 3.1344 0.5419  -0.3246 -1.3730 1373 GLU A C   
10508 O O   . GLU A 1373 ? 1.2352 3.5323 3.2194 0.5312  -0.3319 -1.3990 1373 GLU A O   
10509 C CB  . GLU A 1373 ? 1.1882 3.3560 3.0047 0.5831  -0.3669 -1.3383 1373 GLU A CB  
10510 C CG  . GLU A 1373 ? 1.1084 3.2450 2.8782 0.6183  -0.3904 -1.3174 1373 GLU A CG  
10511 C CD  . GLU A 1373 ? 1.0344 3.1161 2.7368 0.6222  -0.4055 -1.3003 1373 GLU A CD  
10512 O OE1 . GLU A 1373 ? 1.0082 3.0760 2.7003 0.5983  -0.3995 -1.3055 1373 GLU A OE1 
10513 O OE2 . GLU A 1373 ? 0.9897 3.0420 2.6493 0.6494  -0.4231 -1.2815 1373 GLU A OE2 
10514 N N   . VAL A 1374 ? 1.0912 3.2986 2.9706 0.5225  -0.2930 -1.3565 1374 VAL A N   
10515 C CA  . VAL A 1374 ? 1.0409 3.2595 2.9430 0.4866  -0.2619 -1.3668 1374 VAL A CA  
10516 C C   . VAL A 1374 ? 1.0404 3.2370 2.9230 0.4658  -0.2681 -1.3708 1374 VAL A C   
10517 O O   . VAL A 1374 ? 1.0439 3.1851 2.8614 0.4657  -0.2667 -1.3502 1374 VAL A O   
10518 C CB  . VAL A 1374 ? 0.9936 3.1711 2.8492 0.4753  -0.2252 -1.3439 1374 VAL A CB  
10519 C CG1 . VAL A 1374 ? 0.9997 3.2030 2.8940 0.4422  -0.1903 -1.3569 1374 VAL A CG1 
10520 C CG2 . VAL A 1374 ? 0.9644 3.1315 2.7997 0.5028  -0.2235 -1.3265 1374 VAL A CG2 
10521 N N   . CYS A 1375 ? 1.6117 3.8496 3.5490 0.4467  -0.2731 -1.3965 1375 CYS A N   
10522 C CA  . CYS A 1375 ? 1.5932 3.8068 3.5095 0.4234  -0.2745 -1.3995 1375 CYS A CA  
10523 C C   . CYS A 1375 ? 1.5941 3.7898 3.4992 0.3894  -0.2342 -1.3947 1375 CYS A C   
10524 O O   . CYS A 1375 ? 1.5784 3.8109 3.5310 0.3717  -0.2099 -1.4071 1375 CYS A O   
10525 C CB  . CYS A 1375 ? 1.6009 3.8558 3.5682 0.4187  -0.3033 -1.4266 1375 CYS A CB  
10526 S SG  . CYS A 1375 ? 2.6150 4.8457 4.5452 0.4488  -0.3520 -1.4215 1375 CYS A SG  
10527 N N   . SER A 1376 ? 0.8810 3.0181 2.7204 0.3820  -0.2276 -1.3755 1376 SER A N   
10528 C CA  . SER A 1376 ? 0.8944 3.0049 2.7125 0.3504  -0.1928 -1.3685 1376 SER A CA  
10529 C C   . SER A 1376 ? 0.9649 3.0624 2.7768 0.3297  -0.2033 -1.3787 1376 SER A C   
10530 O O   . SER A 1376 ? 0.9900 3.0726 2.7949 0.2996  -0.1783 -1.3788 1376 SER A O   
10531 C CB  . SER A 1376 ? 0.8456 2.8955 2.5896 0.3590  -0.1766 -1.3367 1376 SER A CB  
10532 O OG  . SER A 1376 ? 0.7973 2.8454 2.5277 0.3926  -0.1907 -1.3245 1376 SER A OG  
10533 N N   . PHE A 1377 ? 1.1613 3.2640 2.9750 0.3461  -0.2410 -1.3871 1377 PHE A N   
10534 C CA  . PHE A 1377 ? 1.1879 3.2813 2.9983 0.3294  -0.2564 -1.3989 1377 PHE A CA  
10535 C C   . PHE A 1377 ? 1.2635 3.4090 3.1336 0.3341  -0.2888 -1.4265 1377 PHE A C   
10536 O O   . PHE A 1377 ? 1.2694 3.4327 3.1502 0.3631  -0.3173 -1.4288 1377 PHE A O   
10537 C CB  . PHE A 1377 ? 1.1722 3.2024 2.9058 0.3416  -0.2704 -1.3780 1377 PHE A CB  
10538 C CG  . PHE A 1377 ? 1.1652 3.1419 2.8426 0.3252  -0.2388 -1.3561 1377 PHE A CG  
10539 C CD1 . PHE A 1377 ? 1.2058 3.1667 2.8779 0.2931  -0.2234 -1.3619 1377 PHE A CD1 
10540 C CD2 . PHE A 1377 ? 1.1379 3.0801 2.7682 0.3416  -0.2245 -1.3297 1377 PHE A CD2 
10541 C CE1 . PHE A 1377 ? 1.1944 3.1057 2.8149 0.2780  -0.1944 -1.3417 1377 PHE A CE1 
10542 C CE2 . PHE A 1377 ? 1.1269 3.0198 2.7056 0.3266  -0.1957 -1.3093 1377 PHE A CE2 
10543 C CZ  . PHE A 1377 ? 1.1567 3.0341 2.7305 0.2948  -0.1805 -1.3152 1377 PHE A CZ  
10544 N N   . TYR A 1378 ? 1.2357 3.4051 3.1446 0.3049  -0.2843 -1.4470 1378 TYR A N   
10545 C CA  . TYR A 1378 ? 1.2479 3.4625 3.2102 0.3049  -0.3147 -1.4733 1378 TYR A CA  
10546 C C   . TYR A 1378 ? 1.2746 3.4507 3.1907 0.3128  -0.3450 -1.4696 1378 TYR A C   
10547 O O   . TYR A 1378 ? 1.2605 3.3861 3.1239 0.2988  -0.3341 -1.4570 1378 TYR A O   
10548 C CB  . TYR A 1378 ? 1.2553 3.5077 3.2745 0.2689  -0.2970 -1.4958 1378 TYR A CB  
10549 C CG  . TYR A 1378 ? 1.1805 3.4839 3.2598 0.2613  -0.2723 -1.5058 1378 TYR A CG  
10550 C CD1 . TYR A 1378 ? 1.1369 3.4860 3.2601 0.2858  -0.2871 -1.5143 1378 TYR A CD1 
10551 C CD2 . TYR A 1378 ? 1.1591 3.4658 3.2523 0.2293  -0.2345 -1.5074 1378 TYR A CD2 
10552 C CE1 . TYR A 1378 ? 1.1072 3.5032 3.2854 0.2795  -0.2646 -1.5240 1378 TYR A CE1 
10553 C CE2 . TYR A 1378 ? 1.1237 3.4773 3.2715 0.2223  -0.2115 -1.5169 1378 TYR A CE2 
10554 C CZ  . TYR A 1378 ? 1.1011 3.4996 3.2915 0.2478  -0.2266 -1.5253 1378 TYR A CZ  
10555 O OH  . TYR A 1378 ? 1.0842 3.5300 3.3293 0.2423  -0.2042 -1.5352 1378 TYR A OH  
10556 N N   . LEU A 1379 ? 1.0282 3.2282 2.9640 0.3354  -0.3830 -1.4806 1379 LEU A N   
10557 C CA  . LEU A 1379 ? 1.1411 3.3077 3.0348 0.3462  -0.4150 -1.4779 1379 LEU A CA  
10558 C C   . LEU A 1379 ? 1.2919 3.5032 3.2375 0.3474  -0.4499 -1.5048 1379 LEU A C   
10559 O O   . LEU A 1379 ? 1.3234 3.5945 3.3388 0.3467  -0.4539 -1.5244 1379 LEU A O   
10560 C CB  . LEU A 1379 ? 1.0868 3.2199 2.9276 0.3826  -0.4319 -1.4556 1379 LEU A CB  
10561 C CG  . LEU A 1379 ? 1.0204 3.1029 2.8000 0.3877  -0.4045 -1.4261 1379 LEU A CG  
10562 C CD1 . LEU A 1379 ? 0.9880 3.0423 2.7209 0.4245  -0.4279 -1.4072 1379 LEU A CD1 
10563 C CD2 . LEU A 1379 ? 1.0477 3.0811 2.7804 0.3622  -0.3858 -1.4172 1379 LEU A CD2 
10564 N N   . LYS A 1380 ? 1.5729 3.7535 3.4821 0.3496  -0.4751 -1.5049 1380 LYS A N   
10565 C CA  . LYS A 1380 ? 1.6430 3.8524 3.5811 0.3612  -0.5161 -1.5239 1380 LYS A CA  
10566 C C   . LYS A 1380 ? 1.6601 3.8138 3.5275 0.3751  -0.5400 -1.5106 1380 LYS A C   
10567 O O   . LYS A 1380 ? 1.6613 3.7679 3.4811 0.3578  -0.5270 -1.5015 1380 LYS A O   
10568 C CB  . LYS A 1380 ? 1.5026 3.7565 3.5041 0.3315  -0.5182 -1.5527 1380 LYS A CB  
10569 C CG  . LYS A 1380 ? 1.5943 3.8238 3.5826 0.2944  -0.4879 -1.5527 1380 LYS A CG  
10570 C CD  . LYS A 1380 ? 1.6168 3.8985 3.6773 0.2654  -0.4874 -1.5817 1380 LYS A CD  
10571 C CE  . LYS A 1380 ? 1.4202 3.6741 3.4641 0.2283  -0.4615 -1.5823 1380 LYS A CE  
10572 N NZ  . LYS A 1380 ? 1.4622 3.7667 3.5764 0.1997  -0.4622 -1.6105 1380 LYS A NZ  
10573 N N   . ILE A 1381 ? 0.7958 2.9537 2.6548 0.4072  -0.5738 -1.5085 1381 ILE A N   
10574 C CA  . ILE A 1381 ? 0.8000 2.9111 2.5971 0.4228  -0.6006 -1.4981 1381 ILE A CA  
10575 C C   . ILE A 1381 ? 0.9392 3.0843 2.7685 0.4388  -0.6445 -1.5171 1381 ILE A C   
10576 O O   . ILE A 1381 ? 0.9808 3.1725 2.8580 0.4566  -0.6585 -1.5260 1381 ILE A O   
10577 C CB  . ILE A 1381 ? 0.7612 2.8274 2.4945 0.4514  -0.5987 -1.4687 1381 ILE A CB  
10578 C CG1 . ILE A 1381 ? 0.7878 2.7891 2.4445 0.4512  -0.6035 -1.4530 1381 ILE A CG1 
10579 C CG2 . ILE A 1381 ? 0.7511 2.8402 2.4968 0.4862  -0.6324 -1.4698 1381 ILE A CG2 
10580 C CD1 . ILE A 1381 ? 1.1706 3.1280 2.7646 0.4787  -0.6028 -1.4244 1381 ILE A CD1 
10581 N N   . ASP A 1382 ? 1.7795 3.9001 3.5814 0.4325  -0.6660 -1.5231 1382 ASP A N   
10582 C CA  . ASP A 1382 ? 1.8648 4.0114 3.6903 0.4455  -0.7088 -1.5409 1382 ASP A CA  
10583 C C   . ASP A 1382 ? 1.9375 4.0344 3.7034 0.4445  -0.7284 -1.5370 1382 ASP A C   
10584 O O   . ASP A 1382 ? 1.9192 3.9739 3.6450 0.4235  -0.7082 -1.5295 1382 ASP A O   
10585 C CB  . ASP A 1382 ? 1.9472 4.1582 3.8568 0.4245  -0.7137 -1.5715 1382 ASP A CB  
10586 C CG  . ASP A 1382 ? 2.0271 4.2282 3.9407 0.3868  -0.6985 -1.5832 1382 ASP A CG  
10587 O OD1 . ASP A 1382 ? 1.9893 4.1824 3.9043 0.3642  -0.6609 -1.5778 1382 ASP A OD1 
10588 O OD2 . ASP A 1382 ? 2.1290 4.3296 4.0437 0.3799  -0.7248 -1.5979 1382 ASP A OD2 
10589 N N   . THR A 1383 ? 1.5329 3.6343 3.2923 0.4676  -0.7680 -1.5419 1383 THR A N   
10590 C CA  . THR A 1383 ? 1.6155 3.6692 3.3151 0.4713  -0.7893 -1.5371 1383 THR A CA  
10591 C C   . THR A 1383 ? 1.7036 3.7839 3.4403 0.4533  -0.8143 -1.5651 1383 THR A C   
10592 O O   . THR A 1383 ? 1.7183 3.8481 3.5080 0.4627  -0.8420 -1.5836 1383 THR A O   
10593 C CB  . THR A 1383 ? 1.6186 3.6495 3.2733 0.5102  -0.8154 -1.5199 1383 THR A CB  
10594 O OG1 . THR A 1383 ? 1.6004 3.6836 3.3085 0.5309  -0.8308 -1.5275 1383 THR A OG1 
10595 C CG2 . THR A 1383 ? 1.5406 3.5182 3.1294 0.5209  -0.7896 -1.4886 1383 THR A CG2 
10596 N N   . GLN A 1384 ? 1.5860 3.6336 3.2959 0.4269  -0.8039 -1.5682 1384 GLN A N   
10597 C CA  . GLN A 1384 ? 1.7222 3.7902 3.4640 0.4056  -0.8239 -1.5942 1384 GLN A CA  
10598 C C   . GLN A 1384 ? 1.8320 3.8663 3.5246 0.4204  -0.8606 -1.5942 1384 GLN A C   
10599 O O   . GLN A 1384 ? 1.8112 3.8065 3.4451 0.4472  -0.8693 -1.5735 1384 GLN A O   
10600 C CB  . GLN A 1384 ? 1.7559 3.8106 3.5015 0.3664  -0.7924 -1.5998 1384 GLN A CB  
10601 C CG  . GLN A 1384 ? 1.7308 3.8289 3.5374 0.3475  -0.7597 -1.6061 1384 GLN A CG  
10602 C CD  . GLN A 1384 ? 1.7843 3.8724 3.5986 0.3079  -0.7315 -1.6137 1384 GLN A CD  
10603 O OE1 . GLN A 1384 ? 1.8203 3.8521 3.5746 0.2978  -0.7182 -1.6008 1384 GLN A OE1 
10604 N NE2 . GLN A 1384 ? 1.7875 3.9305 3.6761 0.2853  -0.7221 -1.6347 1384 GLN A NE2 
10605 N N   . ASP A 1385 ? 2.4731 4.5222 4.1890 0.4033  -0.8822 -1.6172 1385 ASP A N   
10606 C CA  . ASP A 1385 ? 2.5800 4.5969 4.2493 0.4157  -0.9171 -1.6185 1385 ASP A CA  
10607 C C   . ASP A 1385 ? 2.6482 4.6286 4.2875 0.3877  -0.9144 -1.6264 1385 ASP A C   
10608 O O   . ASP A 1385 ? 2.6981 4.6307 4.2750 0.3973  -0.9314 -1.6188 1385 ASP A O   
10609 C CB  . ASP A 1385 ? 2.6425 4.7083 4.3581 0.4331  -0.9591 -1.6373 1385 ASP A CB  
10610 C CG  . ASP A 1385 ? 2.5992 4.6803 4.3162 0.4694  -0.9698 -1.6239 1385 ASP A CG  
10611 O OD1 . ASP A 1385 ? 2.6008 4.6362 4.2518 0.4940  -0.9768 -1.6023 1385 ASP A OD1 
10612 O OD2 . ASP A 1385 ? 2.5683 4.7068 4.3524 0.4733  -0.9708 -1.6347 1385 ASP A OD2 
10613 N N   . ILE A 1386 ? 2.2706 4.2727 3.9534 0.3534  -0.8925 -1.6411 1386 ILE A N   
10614 C CA  . ILE A 1386 ? 2.3223 4.2927 3.9829 0.3233  -0.8866 -1.6497 1386 ILE A CA  
10615 C C   . ILE A 1386 ? 2.2719 4.1674 3.8472 0.3232  -0.8643 -1.6247 1386 ILE A C   
10616 O O   . ILE A 1386 ? 2.2793 4.1299 3.7910 0.3434  -0.8827 -1.6127 1386 ILE A O   
10617 C CB  . ILE A 1386 ? 3.1089 5.1178 4.8343 0.2862  -0.8613 -1.6673 1386 ILE A CB  
10618 C CG1 . ILE A 1386 ? 3.0958 5.1822 4.9090 0.2886  -0.8744 -1.6873 1386 ILE A CG1 
10619 C CG2 . ILE A 1386 ? 3.1984 5.1873 4.9156 0.2556  -0.8656 -1.6828 1386 ILE A CG2 
10620 C CD1 . ILE A 1386 ? 3.0806 5.2083 4.9598 0.2544  -0.8476 -1.7030 1386 ILE A CD1 
10621 N N   . TYR A 1399 ? 2.8550 4.6304 4.2292 0.4312  -0.9428 -1.5729 1399 TYR A N   
10622 C CA  . TYR A 1399 ? 2.8471 4.6318 4.2113 0.4685  -0.9680 -1.5631 1399 TYR A CA  
10623 C C   . TYR A 1399 ? 2.5833 4.4129 3.9986 0.4771  -0.9519 -1.5586 1399 TYR A C   
10624 O O   . TYR A 1399 ? 2.5783 4.4629 4.0527 0.4860  -0.9725 -1.5737 1399 TYR A O   
10625 C CB  . TYR A 1399 ? 3.0225 4.7414 4.2980 0.4907  -0.9659 -1.5353 1399 TYR A CB  
10626 C CG  . TYR A 1399 ? 3.1750 4.8962 4.4317 0.5299  -0.9881 -1.5208 1399 TYR A CG  
10627 C CD1 . TYR A 1399 ? 3.3000 5.0580 4.5877 0.5469  -1.0281 -1.5361 1399 TYR A CD1 
10628 C CD2 . TYR A 1399 ? 3.1688 4.8534 4.3747 0.5498  -0.9696 -1.4913 1399 TYR A CD2 
10629 C CE1 . TYR A 1399 ? 3.3321 5.0906 4.6011 0.5827  -1.0484 -1.5223 1399 TYR A CE1 
10630 C CE2 . TYR A 1399 ? 3.1964 4.8815 4.3838 0.5851  -0.9896 -1.4774 1399 TYR A CE2 
10631 C CZ  . TYR A 1399 ? 3.2757 4.9972 4.4942 0.6015  -1.0288 -1.4929 1399 TYR A CZ  
10632 O OH  . TYR A 1399 ? 3.2773 4.9983 4.4767 0.6365  -1.0485 -1.4786 1399 TYR A OH  
10633 N N   . LYS A 1400 ? 2.2424 4.0476 3.6341 0.4743  -0.9149 -1.5377 1400 LYS A N   
10634 C CA  . LYS A 1400 ? 1.9597 3.8027 3.3964 0.4787  -0.8937 -1.5325 1400 LYS A CA  
10635 C C   . LYS A 1400 ? 1.7138 3.5209 3.1171 0.4684  -0.8495 -1.5103 1400 LYS A C   
10636 O O   . LYS A 1400 ? 1.6882 3.4392 3.0204 0.4802  -0.8417 -1.4871 1400 LYS A O   
10637 C CB  . LYS A 1400 ? 1.8954 3.7594 3.3381 0.5158  -0.9174 -1.5247 1400 LYS A CB  
10638 C CG  . LYS A 1400 ? 1.8951 3.7067 3.2602 0.5452  -0.9320 -1.5015 1400 LYS A CG  
10639 C CD  . LYS A 1400 ? 1.8335 3.6699 3.2113 0.5797  -0.9511 -1.4934 1400 LYS A CD  
10640 C CE  . LYS A 1400 ? 1.8583 3.7585 3.3083 0.5827  -0.9816 -1.5198 1400 LYS A CE  
10641 N NZ  . LYS A 1400 ? 1.8013 3.7281 3.2681 0.6156  -0.9993 -1.5127 1400 LYS A NZ  
10642 N N   . ARG A 1401 ? 1.6575 3.4983 3.1133 0.4464  -0.8211 -1.5177 1401 ARG A N   
10643 C CA  . ARG A 1401 ? 1.4580 3.2699 2.8908 0.4303  -0.7776 -1.5006 1401 ARG A CA  
10644 C C   . ARG A 1401 ? 1.3572 3.2161 2.8499 0.4242  -0.7524 -1.5027 1401 ARG A C   
10645 O O   . ARG A 1401 ? 1.3738 3.2916 2.9381 0.4172  -0.7618 -1.5248 1401 ARG A O   
10646 C CB  . ARG A 1401 ? 1.3889 3.1704 2.8031 0.3970  -0.7630 -1.5079 1401 ARG A CB  
10647 C CG  . ARG A 1401 ? 1.2418 3.0306 2.6830 0.3645  -0.7219 -1.5096 1401 ARG A CG  
10648 C CD  . ARG A 1401 ? 1.2100 3.0597 2.7344 0.3382  -0.7237 -1.5396 1401 ARG A CD  
10649 N NE  . ARG A 1401 ? 1.1837 3.0181 2.7102 0.3013  -0.6947 -1.5446 1401 ARG A NE  
10650 C CZ  . ARG A 1401 ? 1.1564 3.0346 2.7478 0.2729  -0.6803 -1.5640 1401 ARG A CZ  
10651 N NH1 . ARG A 1401 ? 1.1380 3.0812 2.8019 0.2759  -0.6912 -1.5813 1401 ARG A NH1 
10652 N NH2 . ARG A 1401 ? 1.1577 3.0143 2.7417 0.2408  -0.6543 -1.5658 1401 ARG A NH2 
10653 N N   . ILE A 1402 ? 1.8422 3.6739 3.3034 0.4280  -0.7208 -1.4790 1402 ILE A N   
10654 C CA  . ILE A 1402 ? 1.7069 3.5739 3.2117 0.4264  -0.6951 -1.4759 1402 ILE A CA  
10655 C C   . ILE A 1402 ? 1.6911 3.5640 3.2214 0.3899  -0.6580 -1.4820 1402 ILE A C   
10656 O O   . ILE A 1402 ? 1.6852 3.5096 3.1673 0.3747  -0.6358 -1.4693 1402 ILE A O   
10657 C CB  . ILE A 1402 ? 1.5861 3.4179 3.0395 0.4513  -0.6806 -1.4451 1402 ILE A CB  
10658 C CG1 . ILE A 1402 ? 1.5754 3.4084 3.0114 0.4892  -0.7148 -1.4379 1402 ILE A CG1 
10659 C CG2 . ILE A 1402 ? 1.4914 3.3511 2.9818 0.4459  -0.6490 -1.4402 1402 ILE A CG2 
10660 C CD1 . ILE A 1402 ? 1.4996 3.2996 2.8869 0.5140  -0.7010 -1.4073 1402 ILE A CD1 
10661 N N   . VAL A 1403 ? 0.9243 2.8563 2.5299 0.3762  -0.6508 -1.5011 1403 VAL A N   
10662 C CA  . VAL A 1403 ? 0.9166 2.8587 2.5500 0.3437  -0.6129 -1.5052 1403 VAL A CA  
10663 C C   . VAL A 1403 ? 0.8778 2.8566 2.5512 0.3506  -0.5918 -1.5005 1403 VAL A C   
10664 O O   . VAL A 1403 ? 0.8635 2.9018 2.6046 0.3529  -0.6029 -1.5193 1403 VAL A O   
10665 C CB  . VAL A 1403 ? 0.9338 2.9155 2.6266 0.3137  -0.6184 -1.5347 1403 VAL A CB  
10666 C CG1 . VAL A 1403 ? 0.9255 2.9164 2.6451 0.2806  -0.5779 -1.5373 1403 VAL A CG1 
10667 C CG2 . VAL A 1403 ? 0.9735 2.9208 2.6299 0.3052  -0.6394 -1.5412 1403 VAL A CG2 
10668 N N   . ALA A 1404 ? 1.3632 3.3055 2.9938 0.3537  -0.5616 -1.4756 1404 ALA A N   
10669 C CA  . ALA A 1404 ? 1.2758 3.2408 2.9300 0.3607  -0.5370 -1.4661 1404 ALA A CA  
10670 C C   . ALA A 1404 ? 1.2508 3.2128 2.9160 0.3290  -0.4948 -1.4643 1404 ALA A C   
10671 O O   . ALA A 1404 ? 1.2389 3.1531 2.8570 0.3120  -0.4771 -1.4534 1404 ALA A O   
10672 C CB  . ALA A 1404 ? 1.1963 3.1212 2.7908 0.3910  -0.5364 -1.4374 1404 ALA A CB  
10673 N N   . CYS A 1405 ? 2.4227 4.4347 4.1486 0.3220  -0.4783 -1.4743 1405 CYS A N   
10674 C CA  . CYS A 1405 ? 2.4164 4.4359 4.1649 0.2896  -0.4401 -1.4773 1405 CYS A CA  
10675 C C   . CYS A 1405 ? 2.3303 4.3560 4.0824 0.2964  -0.4107 -1.4622 1405 CYS A C   
10676 O O   . CYS A 1405 ? 2.3226 4.3491 4.0628 0.3263  -0.4201 -1.4500 1405 CYS A O   
10677 C CB  . CYS A 1405 ? 2.4576 4.5383 4.2861 0.2670  -0.4438 -1.5079 1405 CYS A CB  
10678 S SG  . CYS A 1405 ? 2.7746 4.8727 4.6243 0.2654  -0.4874 -1.5324 1405 CYS A SG  
10679 N N   . ALA A 1406 ? 1.3627 3.3947 3.1338 0.2678  -0.3752 -1.4639 1406 ALA A N   
10680 C CA  . ALA A 1406 ? 1.2585 3.2947 3.0323 0.2699  -0.3437 -1.4501 1406 ALA A CA  
10681 C C   . ALA A 1406 ? 1.2835 3.3351 3.0894 0.2337  -0.3080 -1.4583 1406 ALA A C   
10682 O O   . ALA A 1406 ? 1.3074 3.3422 3.1061 0.2070  -0.3015 -1.4650 1406 ALA A O   
10683 C CB  . ALA A 1406 ? 1.1835 3.1569 2.8785 0.2857  -0.3332 -1.4187 1406 ALA A CB  
10684 N N   . SER A 1407 ? 1.4404 3.5244 3.2821 0.2331  -0.2851 -1.4582 1407 SER A N   
10685 C CA  . SER A 1407 ? 1.4343 3.5215 3.2906 0.2026  -0.2449 -1.4578 1407 SER A CA  
10686 C C   . SER A 1407 ? 1.3759 3.4618 3.2235 0.2152  -0.2205 -1.4405 1407 SER A C   
10687 O O   . SER A 1407 ? 1.3595 3.4729 3.2277 0.2414  -0.2336 -1.4411 1407 SER A O   
10688 C CB  . SER A 1407 ? 1.4464 3.5951 3.3826 0.1784  -0.2406 -1.4864 1407 SER A CB  
10689 O OG  . SER A 1407 ? 1.3976 3.5537 3.3494 0.1550  -0.2000 -1.4834 1407 SER A OG  
10690 N N   . TYR A 1408 ? 1.6938 3.7477 3.5109 0.1961  -0.1848 -1.4254 1408 TYR A N   
10691 C CA  . TYR A 1408 ? 1.6075 3.6540 3.4096 0.2065  -0.1599 -1.4071 1408 TYR A CA  
10692 C C   . TYR A 1408 ? 1.5680 3.6769 3.4414 0.2009  -0.1456 -1.4236 1408 TYR A C   
10693 O O   . TYR A 1408 ? 1.6142 3.7603 3.5400 0.1748  -0.1366 -1.4445 1408 TYR A O   
10694 C CB  . TYR A 1408 ? 1.6063 3.6007 3.3556 0.1867  -0.1260 -1.3865 1408 TYR A CB  
10695 C CG  . TYR A 1408 ? 1.5778 3.5675 3.3156 0.1943  -0.0988 -1.3692 1408 TYR A CG  
10696 C CD1 . TYR A 1408 ? 1.5591 3.5528 3.2877 0.2278  -0.1124 -1.3589 1408 TYR A CD1 
10697 C CD2 . TYR A 1408 ? 1.5843 3.5657 3.3205 0.1679  -0.0598 -1.3633 1408 TYR A CD2 
10698 C CE1 . TYR A 1408 ? 1.5521 3.5418 3.2704 0.2353  -0.0884 -1.3435 1408 TYR A CE1 
10699 C CE2 . TYR A 1408 ? 1.5727 3.5497 3.2977 0.1751  -0.0352 -1.3475 1408 TYR A CE2 
10700 C CZ  . TYR A 1408 ? 1.5718 3.5529 3.2878 0.2090  -0.0497 -1.3377 1408 TYR A CZ  
10701 O OH  . TYR A 1408 ? 1.5703 3.5464 3.2744 0.2165  -0.0260 -1.3221 1408 TYR A OH  
10702 N N   . LYS A 1409 ? 1.4298 3.5502 3.3053 0.2258  -0.1439 -1.4143 1409 LYS A N   
10703 C CA  . LYS A 1409 ? 1.3961 3.5716 3.3334 0.2235  -0.1281 -1.4270 1409 LYS A CA  
10704 C C   . LYS A 1409 ? 1.4275 3.5819 3.3423 0.2100  -0.0867 -1.4102 1409 LYS A C   
10705 O O   . LYS A 1409 ? 1.4023 3.5319 3.2798 0.2304  -0.0804 -1.3897 1409 LYS A O   
10706 C CB  . LYS A 1409 ? 1.3259 3.5283 3.2812 0.2597  -0.1515 -1.4278 1409 LYS A CB  
10707 C CG  . LYS A 1409 ? 1.2810 3.5169 3.2723 0.2743  -0.1925 -1.4476 1409 LYS A CG  
10708 C CD  . LYS A 1409 ? 1.2288 3.4941 3.2420 0.3095  -0.2142 -1.4490 1409 LYS A CD  
10709 C CE  . LYS A 1409 ? 1.2432 3.5807 3.3410 0.3050  -0.2110 -1.4741 1409 LYS A CE  
10710 N NZ  . LYS A 1409 ? 1.2465 3.6234 3.3811 0.3359  -0.2441 -1.4853 1409 LYS A NZ  
10711 N N   . PRO A 1410 ? 2.0268 4.1912 3.9643 0.1755  -0.0584 -1.4188 1410 PRO A N   
10712 C CA  . PRO A 1410 ? 2.0602 4.2041 3.9761 0.1602  -0.0178 -1.4032 1410 PRO A CA  
10713 C C   . PRO A 1410 ? 2.1424 4.3201 4.0881 0.1752  -0.0049 -1.4027 1410 PRO A C   
10714 O O   . PRO A 1410 ? 2.1453 4.3820 4.1588 0.1725  -0.0068 -1.4249 1410 PRO A O   
10715 C CB  . PRO A 1410 ? 2.0496 4.2127 4.0015 0.1207  0.0040  -1.4194 1410 PRO A CB  
10716 C CG  . PRO A 1410 ? 2.0589 4.2278 4.0240 0.1148  -0.0254 -1.4356 1410 PRO A CG  
10717 C CD  . PRO A 1410 ? 2.0658 4.2598 4.0489 0.1484  -0.0629 -1.4430 1410 PRO A CD  
10718 N N   . SER A 1411 ? 2.2346 4.3753 4.1302 0.1910  0.0075  -1.3779 1411 SER A N   
10719 C CA  . SER A 1411 ? 2.3699 4.5349 4.2856 0.2029  0.0243  -1.3747 1411 SER A CA  
10720 C C   . SER A 1411 ? 2.5411 4.7292 4.4903 0.1713  0.0625  -1.3829 1411 SER A C   
10721 O O   . SER A 1411 ? 2.5630 4.7306 4.4987 0.1423  0.0802  -1.3819 1411 SER A O   
10722 C CB  . SER A 1411 ? 2.3484 4.4618 4.1965 0.2232  0.0312  -1.3443 1411 SER A CB  
10723 O OG  . SER A 1411 ? 2.3387 4.4273 4.1513 0.2527  -0.0024 -1.3344 1411 SER A OG  
10724 N N   . ARG A 1412 ? 2.0640 4.2938 4.0557 0.1771  0.0756  -1.3907 1412 ARG A N   
10725 C CA  . ARG A 1412 ? 2.2384 4.4921 4.2627 0.1483  0.1125  -1.3984 1412 ARG A CA  
10726 C C   . ARG A 1412 ? 2.2266 4.4241 4.1903 0.1296  0.1430  -1.3751 1412 ARG A C   
10727 O O   . ARG A 1412 ? 2.2211 4.3675 4.1213 0.1456  0.1399  -1.3507 1412 ARG A O   
10728 C CB  . ARG A 1412 ? 2.3899 4.6854 4.4538 0.1622  0.1236  -1.4043 1412 ARG A CB  
10729 C CG  . ARG A 1412 ? 2.5050 4.7657 4.5184 0.1893  0.1253  -1.3800 1412 ARG A CG  
10730 C CD  . ARG A 1412 ? 2.6332 4.9278 4.6790 0.1950  0.1469  -1.3836 1412 ARG A CD  
10731 N NE  . ARG A 1412 ? 2.7068 4.9568 4.6944 0.2077  0.1621  -1.3566 1412 ARG A NE  
10732 C CZ  . ARG A 1412 ? 2.7758 5.0405 4.7739 0.2142  0.1827  -1.3535 1412 ARG A CZ  
10733 N NH1 . ARG A 1412 ? 2.8193 5.1430 4.8845 0.2097  0.1911  -1.3758 1412 ARG A NH1 
10734 N NH2 . ARG A 1412 ? 2.7785 4.9989 4.7197 0.2252  0.1948  -1.3280 1412 ARG A NH2 
10735 N N   . GLU A 1413 ? 2.1296 4.3372 4.1139 0.0955  0.1721  -1.3826 1413 GLU A N   
10736 C CA  . GLU A 1413 ? 2.0958 4.2545 4.0289 0.0743  0.2038  -1.3623 1413 GLU A CA  
10737 C C   . GLU A 1413 ? 1.9192 4.0267 3.8020 0.0650  0.1933  -1.3519 1413 GLU A C   
10738 O O   . GLU A 1413 ? 1.9005 3.9690 3.7455 0.0431  0.2180  -1.3381 1413 GLU A O   
10739 C CB  . GLU A 1413 ? 2.2018 4.3286 4.0880 0.0934  0.2175  -1.3375 1413 GLU A CB  
10740 C CG  . GLU A 1413 ? 2.3144 4.4868 4.2439 0.1051  0.2281  -1.3458 1413 GLU A CG  
10741 C CD  . GLU A 1413 ? 2.4232 4.6276 4.3940 0.0747  0.2638  -1.3578 1413 GLU A CD  
10742 O OE1 . GLU A 1413 ? 2.4663 4.6391 4.4077 0.0484  0.2903  -1.3472 1413 GLU A OE1 
10743 O OE2 . GLU A 1413 ? 2.4583 4.7196 4.4909 0.0773  0.2658  -1.3775 1413 GLU A OE2 
10744 N N   . GLU A 1414 ? 1.6920 3.7988 3.5735 0.0818  0.1567  -1.3583 1414 GLU A N   
10745 C CA  . GLU A 1414 ? 1.5080 3.5636 3.3375 0.0772  0.1439  -1.3474 1414 GLU A CA  
10746 C C   . GLU A 1414 ? 1.4526 3.5177 3.3074 0.0458  0.1447  -1.3649 1414 GLU A C   
10747 O O   . GLU A 1414 ? 1.4612 3.5802 3.3813 0.0352  0.1392  -1.3903 1414 GLU A O   
10748 C CB  . GLU A 1414 ? 1.3897 3.4305 3.1942 0.1108  0.1048  -1.3423 1414 GLU A CB  
10749 C CG  . GLU A 1414 ? 1.2561 3.2494 2.9962 0.1354  0.1063  -1.3133 1414 GLU A CG  
10750 C CD  . GLU A 1414 ? 1.1651 3.1576 2.8940 0.1718  0.0688  -1.3107 1414 GLU A CD  
10751 O OE1 . GLU A 1414 ? 1.1500 3.1769 2.9191 0.1774  0.0411  -1.3314 1414 GLU A OE1 
10752 O OE2 . GLU A 1414 ? 1.1205 3.0785 2.8010 0.1947  0.0666  -1.2880 1414 GLU A OE2 
10753 N N   . SER A 1415 ? 1.8504 3.8617 3.6518 0.0317  0.1510  -1.3507 1415 SER A N   
10754 C CA  . SER A 1415 ? 1.8491 3.8596 3.6647 0.0002  0.1546  -1.3639 1415 SER A CA  
10755 C C   . SER A 1415 ? 1.8552 3.8895 3.7009 0.0062  0.1172  -1.3847 1415 SER A C   
10756 O O   . SER A 1415 ? 1.8531 3.8827 3.6844 0.0358  0.0863  -1.3821 1415 SER A O   
10757 C CB  . SER A 1415 ? 1.8323 3.7747 3.5776 -0.0124 0.1688  -1.3414 1415 SER A CB  
10758 O OG  . SER A 1415 ? 1.8433 3.7822 3.6004 -0.0450 0.1762  -1.3530 1415 SER A OG  
10759 N N   . SER A 1416 ? 1.1925 3.2521 3.0797 -0.0228 0.1205  -1.4051 1416 SER A N   
10760 C CA  . SER A 1416 ? 1.2471 3.3282 3.1634 -0.0221 0.0870  -1.4257 1416 SER A CA  
10761 C C   . SER A 1416 ? 1.2716 3.2966 3.1253 -0.0111 0.0634  -1.4131 1416 SER A C   
10762 O O   . SER A 1416 ? 1.2902 3.3265 3.1549 0.0026  0.0289  -1.4249 1416 SER A O   
10763 C CB  . SER A 1416 ? 1.3141 3.4270 3.2816 -0.0592 0.0991  -1.4477 1416 SER A CB  
10764 O OG  . SER A 1416 ? 1.3567 3.4226 3.2835 -0.0866 0.1210  -1.4367 1416 SER A OG  
10765 N N   . SER A 1417 ? 1.7276 3.6924 3.5156 -0.0166 0.0819  -1.3891 1417 SER A N   
10766 C CA  . SER A 1417 ? 1.7560 3.6660 3.4845 -0.0101 0.0630  -1.3775 1417 SER A CA  
10767 C C   . SER A 1417 ? 1.7141 3.6209 3.4255 0.0275  0.0259  -1.3743 1417 SER A C   
10768 O O   . SER A 1417 ? 1.8085 3.6882 3.4909 0.0338  0.0011  -1.3743 1417 SER A O   
10769 C CB  . SER A 1417 ? 1.7552 3.6005 3.4135 -0.0176 0.0892  -1.3497 1417 SER A CB  
10770 O OG  . SER A 1417 ? 1.7082 3.5248 3.3199 0.0127  0.0861  -1.3263 1417 SER A OG  
10771 N N   . GLY A 1418 ? 1.6433 3.5777 3.3727 0.0525  0.0216  -1.3719 1418 GLY A N   
10772 C CA  . GLY A 1418 ? 1.5475 3.4808 3.2627 0.0883  -0.0135 -1.3688 1418 GLY A CA  
10773 C C   . GLY A 1418 ? 1.4888 3.3622 3.1274 0.1098  -0.0123 -1.3383 1418 GLY A C   
10774 O O   . GLY A 1418 ? 1.4250 3.2720 3.0337 0.1033  0.0176  -1.3197 1418 GLY A O   
10775 N N   . SER A 1419 ? 1.4294 3.2809 3.0358 0.1348  -0.0445 -1.3330 1419 SER A N   
10776 C CA  . SER A 1419 ? 1.3611 3.1674 2.9044 0.1625  -0.0482 -1.3054 1419 SER A CA  
10777 C C   . SER A 1419 ? 1.2864 3.0249 2.7572 0.1535  -0.0279 -1.2796 1419 SER A C   
10778 O O   . SER A 1419 ? 1.3263 3.0445 2.7872 0.1259  -0.0144 -1.2825 1419 SER A O   
10779 C CB  . SER A 1419 ? 1.3751 3.1821 2.9088 0.1935  -0.0896 -1.3079 1419 SER A CB  
10780 O OG  . SER A 1419 ? 1.3162 3.0936 2.8032 0.2233  -0.0938 -1.2837 1419 SER A OG  
10781 N N   . SER A 1420 ? 1.2552 2.9602 2.6770 0.1771  -0.0255 -1.2543 1420 SER A N   
10782 C CA  . SER A 1420 ? 1.2132 2.8524 2.5615 0.1765  -0.0127 -1.2276 1420 SER A CA  
10783 C C   . SER A 1420 ? 1.2502 2.8591 2.5564 0.2020  -0.0460 -1.2200 1420 SER A C   
10784 O O   . SER A 1420 ? 1.3000 2.9397 2.6352 0.2183  -0.0768 -1.2354 1420 SER A O   
10785 C CB  . SER A 1420 ? 1.1093 2.7308 2.4296 0.1873  0.0107  -1.2035 1420 SER A CB  
10786 O OG  . SER A 1420 ? 1.0532 2.6671 2.3499 0.2230  -0.0110 -1.1905 1420 SER A OG  
10787 N N   . HIS A 1421 ? 1.3977 2.9465 2.6353 0.2061  -0.0400 -1.1959 1421 HIS A N   
10788 C CA  . HIS A 1421 ? 1.3909 2.9055 2.5820 0.2300  -0.0693 -1.1862 1421 HIS A CA  
10789 C C   . HIS A 1421 ? 1.2987 2.8456 2.5117 0.2624  -0.1010 -1.1923 1421 HIS A C   
10790 O O   . HIS A 1421 ? 1.1995 2.7591 2.4173 0.2801  -0.0961 -1.1822 1421 HIS A O   
10791 C CB  . HIS A 1421 ? 1.4213 2.8730 2.5380 0.2377  -0.0543 -1.1541 1421 HIS A CB  
10792 C CG  . HIS A 1421 ? 1.4308 2.8507 2.4993 0.2686  -0.0819 -1.1397 1421 HIS A CG  
10793 N ND1 . HIS A 1421 ? 1.3851 2.7752 2.4083 0.2918  -0.0782 -1.1128 1421 HIS A ND1 
10794 C CD2 . HIS A 1421 ? 1.4753 2.8890 2.5340 0.2797  -0.1136 -1.1485 1421 HIS A CD2 
10795 C CE1 . HIS A 1421 ? 1.4157 2.7824 2.4031 0.3160  -0.1061 -1.1053 1421 HIS A CE1 
10796 N NE2 . HIS A 1421 ? 1.4672 2.8477 2.4749 0.3095  -0.1280 -1.1268 1421 HIS A NE2 
10797 N N   . ALA A 1422 ? 1.2125 2.7713 2.4378 0.2700  -0.1335 -1.2085 1422 ALA A N   
10798 C CA  . ALA A 1422 ? 1.2448 2.8407 2.4999 0.2975  -0.1652 -1.2188 1422 ALA A CA  
10799 C C   . ALA A 1422 ? 1.3337 2.9105 2.5609 0.3160  -0.2016 -1.2205 1422 ALA A C   
10800 O O   . ALA A 1422 ? 1.3699 2.9207 2.5753 0.3019  -0.2064 -1.2248 1422 ALA A O   
10801 C CB  . ALA A 1422 ? 1.2231 2.8854 2.5586 0.2849  -0.1674 -1.2478 1422 ALA A CB  
10802 N N   . VAL A 1423 ? 1.2436 2.8336 2.4715 0.3477  -0.2269 -1.2172 1423 VAL A N   
10803 C CA  . VAL A 1423 ? 1.3210 2.8963 2.5236 0.3691  -0.2629 -1.2181 1423 VAL A CA  
10804 C C   . VAL A 1423 ? 1.3642 2.9961 2.6287 0.3759  -0.2933 -1.2461 1423 VAL A C   
10805 O O   . VAL A 1423 ? 1.3630 3.0449 2.6862 0.3715  -0.2870 -1.2603 1423 VAL A O   
10806 C CB  . VAL A 1423 ? 1.1332 2.6748 2.2824 0.4021  -0.2711 -1.1906 1423 VAL A CB  
10807 C CG1 . VAL A 1423 ? 1.0985 2.5989 2.2033 0.3951  -0.2371 -1.1645 1423 VAL A CG1 
10808 C CG2 . VAL A 1423 ? 1.0982 2.6813 2.2837 0.4267  -0.2861 -1.1944 1423 VAL A CG2 
10809 N N   . MET A 1424 ? 1.1837 2.8084 2.4362 0.3858  -0.3256 -1.2544 1424 MET A N   
10810 C CA  . MET A 1424 ? 1.1427 2.8160 2.4447 0.3998  -0.3588 -1.2764 1424 MET A CA  
10811 C C   . MET A 1424 ? 1.1789 2.8295 2.4391 0.4348  -0.3898 -1.2631 1424 MET A C   
10812 O O   . MET A 1424 ? 1.2281 2.8282 2.4279 0.4398  -0.3954 -1.2485 1424 MET A O   
10813 C CB  . MET A 1424 ? 1.1077 2.8023 2.4447 0.3767  -0.3711 -1.3034 1424 MET A CB  
10814 C CG  . MET A 1424 ? 1.0744 2.7828 2.4438 0.3398  -0.3392 -1.3143 1424 MET A CG  
10815 S SD  . MET A 1424 ? 1.1976 2.9537 2.6337 0.3138  -0.3545 -1.3512 1424 MET A SD  
10816 C CE  . MET A 1424 ? 1.0912 2.9207 2.6021 0.3331  -0.3758 -1.3702 1424 MET A CE  
10817 N N   . ASP A 1425 ? 0.8862 2.5725 2.1766 0.4594  -0.4090 -1.2670 1425 ASP A N   
10818 C CA  . ASP A 1425 ? 0.9187 2.5843 2.1698 0.4942  -0.4368 -1.2523 1425 ASP A CA  
10819 C C   . ASP A 1425 ? 0.9971 2.7046 2.2895 0.5101  -0.4757 -1.2736 1425 ASP A C   
10820 O O   . ASP A 1425 ? 0.9895 2.7468 2.3371 0.5177  -0.4812 -1.2860 1425 ASP A O   
10821 C CB  . ASP A 1425 ? 0.8750 2.5314 2.1072 0.5145  -0.4231 -1.2290 1425 ASP A CB  
10822 C CG  . ASP A 1425 ? 0.9259 2.5623 2.1193 0.5504  -0.4508 -1.2132 1425 ASP A CG  
10823 O OD1 . ASP A 1425 ? 0.9361 2.5192 2.0637 0.5585  -0.4468 -1.1896 1425 ASP A OD1 
10824 O OD2 . ASP A 1425 ? 0.9518 2.6262 2.1812 0.5703  -0.4752 -1.2236 1425 ASP A OD2 
10825 N N   . ILE A 1426 ? 0.7536 2.4400 2.0182 0.5150  -0.5022 -1.2778 1426 ILE A N   
10826 C CA  . ILE A 1426 ? 0.7830 2.5024 2.0784 0.5303  -0.5416 -1.2967 1426 ILE A CA  
10827 C C   . ILE A 1426 ? 0.7724 2.4642 2.0198 0.5644  -0.5692 -1.2802 1426 ILE A C   
10828 O O   . ILE A 1426 ? 0.7849 2.4248 1.9685 0.5693  -0.5714 -1.2637 1426 ILE A O   
10829 C CB  . ILE A 1426 ? 0.8397 2.5631 2.1477 0.5094  -0.5553 -1.3185 1426 ILE A CB  
10830 C CG1 . ILE A 1426 ? 0.8050 2.5439 2.1482 0.4726  -0.5249 -1.3315 1426 ILE A CG1 
10831 C CG2 . ILE A 1426 ? 0.7972 2.5678 2.1537 0.5220  -0.5919 -1.3412 1426 ILE A CG2 
10832 C CD1 . ILE A 1426 ? 0.8733 2.6453 2.2632 0.4525  -0.5410 -1.3612 1426 ILE A CD1 
10833 N N   . SER A 1427 ? 1.6328 3.3608 2.9125 0.5881  -0.5897 -1.2847 1427 SER A N   
10834 C CA  . SER A 1427 ? 1.6367 3.3485 2.8820 0.6216  -0.6197 -1.2725 1427 SER A CA  
10835 C C   . SER A 1427 ? 1.7045 3.4325 2.9658 0.6230  -0.6555 -1.2939 1427 SER A C   
10836 O O   . SER A 1427 ? 1.7256 3.4992 3.0472 0.6073  -0.6616 -1.3201 1427 SER A O   
10837 C CB  . SER A 1427 ? 1.4744 3.2209 2.7529 0.6445  -0.6246 -1.2694 1427 SER A CB  
10838 O OG  . SER A 1427 ? 1.4973 3.2270 2.7413 0.6777  -0.6519 -1.2553 1427 SER A OG  
10839 N N   . LEU A 1428 ? 1.2839 2.9740 2.4905 0.6409  -0.6786 -1.2829 1428 LEU A N   
10840 C CA  . LEU A 1428 ? 1.3562 3.0561 2.5700 0.6438  -0.7140 -1.3014 1428 LEU A CA  
10841 C C   . LEU A 1428 ? 1.3876 3.1012 2.6013 0.6782  -0.7500 -1.2993 1428 LEU A C   
10842 O O   . LEU A 1428 ? 1.3651 3.0430 2.5259 0.7020  -0.7547 -1.2754 1428 LEU A O   
10843 C CB  . LEU A 1428 ? 1.3606 3.0055 2.5115 0.6348  -0.7139 -1.2933 1428 LEU A CB  
10844 C CG  . LEU A 1428 ? 1.3257 2.9560 2.4766 0.5999  -0.6804 -1.2967 1428 LEU A CG  
10845 C CD1 . LEU A 1428 ? 1.3658 2.9369 2.4486 0.5939  -0.6787 -1.2854 1428 LEU A CD1 
10846 C CD2 . LEU A 1428 ? 1.3138 2.9950 2.5360 0.5743  -0.6823 -1.3282 1428 LEU A CD2 
10847 N N   . PRO A 1429 ? 1.1500 2.9148 2.4222 0.6806  -0.7763 -1.3243 1429 PRO A N   
10848 C CA  . PRO A 1429 ? 1.1556 2.9455 2.4436 0.7112  -0.8113 -1.3272 1429 PRO A CA  
10849 C C   . PRO A 1429 ? 1.1968 2.9378 2.4137 0.7351  -0.8316 -1.3074 1429 PRO A C   
10850 O O   . PRO A 1429 ? 1.2163 2.9212 2.3916 0.7252  -0.8344 -1.3063 1429 PRO A O   
10851 C CB  . PRO A 1429 ? 1.2035 3.0354 2.5435 0.7006  -0.8375 -1.3582 1429 PRO A CB  
10852 C CG  . PRO A 1429 ? 1.1898 3.0370 2.5643 0.6652  -0.8109 -1.3733 1429 PRO A CG  
10853 C CD  . PRO A 1429 ? 1.1559 2.9509 2.4755 0.6515  -0.7765 -1.3522 1429 PRO A CD  
10854 N N   . THR A 1430 ? 1.7798 3.5198 2.9828 0.7661  -0.8463 -1.2926 1430 THR A N   
10855 C CA  . THR A 1430 ? 1.8256 3.5138 2.9547 0.7884  -0.8592 -1.2691 1430 THR A CA  
10856 C C   . THR A 1430 ? 1.9689 3.6323 3.0645 0.7847  -0.8832 -1.2774 1430 THR A C   
10857 O O   . THR A 1430 ? 2.0651 3.7577 3.1906 0.7892  -0.9148 -1.2976 1430 THR A O   
10858 C CB  . THR A 1430 ? 1.7935 3.4917 2.9210 0.8234  -0.8791 -1.2564 1430 THR A CB  
10859 O OG1 . THR A 1430 ? 1.7160 3.4427 2.8830 0.8235  -0.8574 -1.2536 1430 THR A OG1 
10860 C CG2 . THR A 1430 ? 1.7761 3.4173 2.8252 0.8438  -0.8805 -1.2265 1430 THR A CG2 
10861 N N   . GLY A 1431 ? 1.7883 3.3975 2.8218 0.7759  -0.8670 -1.2617 1431 GLY A N   
10862 C CA  . GLY A 1431 ? 1.8777 3.4585 2.8764 0.7677  -0.8825 -1.2690 1431 GLY A CA  
10863 C C   . GLY A 1431 ? 1.9330 3.5412 2.9775 0.7370  -0.8816 -1.2980 1431 GLY A C   
10864 O O   . GLY A 1431 ? 1.9398 3.5821 3.0212 0.7390  -0.9114 -1.3200 1431 GLY A O   
10865 N N   . ILE A 1432 ? 1.2586 2.8519 2.3007 0.7086  -0.8482 -1.2977 1432 ILE A N   
10866 C CA  . ILE A 1432 ? 1.3292 2.9452 2.4127 0.6764  -0.8434 -1.3239 1432 ILE A CA  
10867 C C   . ILE A 1432 ? 1.3339 2.9079 2.3820 0.6493  -0.8104 -1.3165 1432 ILE A C   
10868 O O   . ILE A 1432 ? 1.3422 2.9370 2.4302 0.6210  -0.7892 -1.3303 1432 ILE A O   
10869 C CB  . ILE A 1432 ? 1.1951 2.8760 2.3639 0.6639  -0.8356 -1.3441 1432 ILE A CB  
10870 C CG1 . ILE A 1432 ? 1.2563 2.9800 2.4632 0.6909  -0.8648 -1.3503 1432 ILE A CG1 
10871 C CG2 . ILE A 1432 ? 1.2311 2.9395 2.4458 0.6327  -0.8367 -1.3729 1432 ILE A CG2 
10872 C CD1 . ILE A 1432 ? 1.2595 3.0128 2.4967 0.6932  -0.9029 -1.3748 1432 ILE A CD1 
10873 N N   . SER A 1433 ? 2.5910 4.1063 3.5648 0.6579  -0.8065 -1.2950 1433 SER A N   
10874 C CA  . SER A 1433 ? 2.5764 4.0477 3.5113 0.6341  -0.7780 -1.2874 1433 SER A CA  
10875 C C   . SER A 1433 ? 2.5704 4.0674 3.5539 0.5985  -0.7650 -1.3120 1433 SER A C   
10876 O O   . SER A 1433 ? 2.6084 4.1423 3.6369 0.5909  -0.7878 -1.3377 1433 SER A O   
10877 C CB  . SER A 1433 ? 2.6762 4.0948 3.5421 0.6421  -0.7939 -1.2792 1433 SER A CB  
10878 O OG  . SER A 1433 ? 2.6894 4.0700 3.4967 0.6696  -0.7946 -1.2507 1433 SER A OG  
10879 N N   . ALA A 1434 ? 1.4341 2.9101 2.4069 0.5764  -0.7284 -1.3034 1434 ALA A N   
10880 C CA  . ALA A 1434 ? 1.4743 2.9729 2.4919 0.5416  -0.7118 -1.3242 1434 ALA A CA  
10881 C C   . ALA A 1434 ? 1.5407 2.9895 2.5106 0.5216  -0.7005 -1.3219 1434 ALA A C   
10882 O O   . ALA A 1434 ? 1.5732 2.9685 2.4748 0.5338  -0.6971 -1.3003 1434 ALA A O   
10883 C CB  . ALA A 1434 ? 1.4125 2.9316 2.4631 0.5296  -0.6772 -1.3183 1434 ALA A CB  
10884 N N   . ASN A 1435 ? 1.3438 2.8101 2.3503 0.4905  -0.6937 -1.3439 1435 ASN A N   
10885 C CA  . ASN A 1435 ? 1.4176 2.8413 2.3851 0.4707  -0.6892 -1.3470 1435 ASN A CA  
10886 C C   . ASN A 1435 ? 1.3618 2.7345 2.2794 0.4592  -0.6520 -1.3243 1435 ASN A C   
10887 O O   . ASN A 1435 ? 1.3288 2.7043 2.2672 0.4299  -0.6254 -1.3305 1435 ASN A O   
10888 C CB  . ASN A 1435 ? 1.4722 2.9317 2.4966 0.4403  -0.6940 -1.3780 1435 ASN A CB  
10889 C CG  . ASN A 1435 ? 1.5829 3.0163 2.5787 0.4335  -0.7182 -1.3912 1435 ASN A CG  
10890 O OD1 . ASN A 1435 ? 1.6078 2.9842 2.5365 0.4369  -0.7148 -1.3766 1435 ASN A OD1 
10891 N ND2 . ASN A 1435 ? 1.6600 3.1356 2.7076 0.4237  -0.7428 -1.4193 1435 ASN A ND2 
10892 N N   . GLU A 1436 ? 1.6711 2.9968 2.5226 0.4821  -0.6512 -1.2982 1436 GLU A N   
10893 C CA  . GLU A 1436 ? 1.6700 2.9442 2.4689 0.4744  -0.6183 -1.2747 1436 GLU A CA  
10894 C C   . GLU A 1436 ? 1.6904 2.9494 2.4930 0.4387  -0.5978 -1.2861 1436 GLU A C   
10895 O O   . GLU A 1436 ? 1.6515 2.8990 2.4531 0.4212  -0.5635 -1.2763 1436 GLU A O   
10896 C CB  . GLU A 1436 ? 1.7530 2.9712 2.4742 0.4978  -0.6295 -1.2537 1436 GLU A CB  
10897 C CG  . GLU A 1436 ? 1.7656 2.9297 2.4303 0.4928  -0.5957 -1.2270 1436 GLU A CG  
10898 C CD  . GLU A 1436 ? 1.7085 2.8735 2.3650 0.5119  -0.5791 -1.2020 1436 GLU A CD  
10899 O OE1 . GLU A 1436 ? 1.7025 2.9079 2.3943 0.5299  -0.5955 -1.2057 1436 GLU A OE1 
10900 O OE2 . GLU A 1436 ? 1.6532 2.7788 2.2683 0.5092  -0.5506 -1.1788 1436 GLU A OE2 
10901 N N   . GLU A 1437 ? 1.4814 2.7386 2.2863 0.4282  -0.6194 -1.3064 1437 GLU A N   
10902 C CA  . GLU A 1437 ? 1.4976 2.7365 2.3018 0.3949  -0.6034 -1.3179 1437 GLU A CA  
10903 C C   . GLU A 1437 ? 1.4895 2.7812 2.3694 0.3678  -0.5893 -1.3382 1437 GLU A C   
10904 O O   . GLU A 1437 ? 1.4902 2.7720 2.3772 0.3383  -0.5647 -1.3428 1437 GLU A O   
10905 C CB  . GLU A 1437 ? 1.6265 2.8478 2.4101 0.3926  -0.6330 -1.3343 1437 GLU A CB  
10906 C CG  . GLU A 1437 ? 2.2324 3.4423 2.9804 0.4271  -0.6680 -1.3283 1437 GLU A CG  
10907 C CD  . GLU A 1437 ? 2.1897 3.3327 2.8529 0.4434  -0.6633 -1.3029 1437 GLU A CD  
10908 O OE1 . GLU A 1437 ? 2.1731 3.2752 2.8026 0.4262  -0.6362 -1.2929 1437 GLU A OE1 
10909 O OE2 . GLU A 1437 ? 2.1577 3.2894 2.7883 0.4735  -0.6869 -1.2931 1437 GLU A OE2 
10910 N N   . ASP A 1438 ? 1.9946 3.3428 2.9316 0.3779  -0.6050 -1.3504 1438 ASP A N   
10911 C CA  . ASP A 1438 ? 1.9765 3.3787 2.9885 0.3536  -0.5938 -1.3710 1438 ASP A CA  
10912 C C   . ASP A 1438 ? 1.8736 3.2709 2.8906 0.3382  -0.5518 -1.3568 1438 ASP A C   
10913 O O   . ASP A 1438 ? 1.8722 3.2834 2.9228 0.3070  -0.5316 -1.3693 1438 ASP A O   
10914 C CB  . ASP A 1438 ? 1.9837 3.4464 3.0537 0.3707  -0.6175 -1.3842 1438 ASP A CB  
10915 C CG  . ASP A 1438 ? 2.0637 3.5612 3.1765 0.3615  -0.6482 -1.4141 1438 ASP A CG  
10916 O OD1 . ASP A 1438 ? 2.1203 3.6060 3.2347 0.3343  -0.6438 -1.4276 1438 ASP A OD1 
10917 O OD2 . ASP A 1438 ? 2.0653 3.6011 3.2096 0.3812  -0.6769 -1.4239 1438 ASP A OD2 
10918 N N   . LEU A 1439 ? 1.3899 2.7671 2.3729 0.3599  -0.5389 -1.3305 1439 LEU A N   
10919 C CA  . LEU A 1439 ? 1.2521 2.6283 2.2407 0.3501  -0.5005 -1.3150 1439 LEU A CA  
10920 C C   . LEU A 1439 ? 1.2413 2.5649 2.1842 0.3282  -0.4710 -1.3026 1439 LEU A C   
10921 O O   . LEU A 1439 ? 1.2133 2.5476 2.1845 0.2998  -0.4439 -1.3086 1439 LEU A O   
10922 C CB  . LEU A 1439 ? 1.1439 2.5138 2.1084 0.3818  -0.4989 -1.2906 1439 LEU A CB  
10923 C CG  . LEU A 1439 ? 1.1093 2.5240 2.1092 0.4082  -0.5302 -1.2994 1439 LEU A CG  
10924 C CD1 . LEU A 1439 ? 1.0623 2.4578 2.0226 0.4420  -0.5334 -1.2730 1439 LEU A CD1 
10925 C CD2 . LEU A 1439 ? 1.0575 2.5392 2.1405 0.3953  -0.5267 -1.3209 1439 LEU A CD2 
10926 N N   . LYS A 1440 ? 1.3565 2.6238 2.2290 0.3417  -0.4768 -1.2855 1440 LYS A N   
10927 C CA  . LYS A 1440 ? 1.4069 2.6195 2.2299 0.3235  -0.4537 -1.2742 1440 LYS A CA  
10928 C C   . LYS A 1440 ? 1.4158 2.6423 2.2763 0.2861  -0.4439 -1.2974 1440 LYS A C   
10929 O O   . LYS A 1440 ? 1.3893 2.5866 2.2318 0.2635  -0.4149 -1.2904 1440 LYS A O   
10930 C CB  . LYS A 1440 ? 1.5438 2.7049 2.2991 0.3412  -0.4741 -1.2646 1440 LYS A CB  
10931 C CG  . LYS A 1440 ? 1.5961 2.7323 2.3023 0.3773  -0.4814 -1.2381 1440 LYS A CG  
10932 C CD  . LYS A 1440 ? 1.6169 2.7114 2.2783 0.3773  -0.4465 -1.2085 1440 LYS A CD  
10933 C CE  . LYS A 1440 ? 1.7274 2.7626 2.3092 0.4010  -0.4514 -1.1833 1440 LYS A CE  
10934 N NZ  . LYS A 1440 ? 1.7608 2.8010 2.3252 0.4375  -0.4768 -1.1724 1440 LYS A NZ  
10935 N N   . ALA A 1441 ? 1.3708 2.6424 2.2838 0.2800  -0.4689 -1.3250 1441 ALA A N   
10936 C CA  . ALA A 1441 ? 1.4387 2.7283 2.3917 0.2456  -0.4650 -1.3496 1441 ALA A CA  
10937 C C   . ALA A 1441 ? 1.4310 2.7516 2.4316 0.2230  -0.4322 -1.3515 1441 ALA A C   
10938 O O   . ALA A 1441 ? 1.4630 2.7644 2.4594 0.1949  -0.4053 -1.3510 1441 ALA A O   
10939 C CB  . ALA A 1441 ? 1.4902 2.8261 2.4918 0.2482  -0.5023 -1.3781 1441 ALA A CB  
10940 N N   . LEU A 1442 ? 1.7210 3.0893 2.7657 0.2369  -0.4351 -1.3530 1442 LEU A N   
10941 C CA  . LEU A 1442 ? 1.6730 3.0767 2.7655 0.2212  -0.4064 -1.3542 1442 LEU A CA  
10942 C C   . LEU A 1442 ? 1.7225 3.0819 2.7720 0.2114  -0.3675 -1.3293 1442 LEU A C   
10943 O O   . LEU A 1442 ? 1.7684 3.1309 2.8382 0.1813  -0.3405 -1.3342 1442 LEU A O   
10944 C CB  . LEU A 1442 ? 1.5678 3.0189 2.6983 0.2464  -0.4189 -1.3545 1442 LEU A CB  
10945 C CG  . LEU A 1442 ? 1.5909 3.0902 2.7691 0.2566  -0.4571 -1.3793 1442 LEU A CG  
10946 C CD1 . LEU A 1442 ? 1.5611 3.0772 2.7376 0.2938  -0.4787 -1.3703 1442 LEU A CD1 
10947 C CD2 . LEU A 1442 ? 1.5860 3.1456 2.8450 0.2312  -0.4516 -1.4054 1442 LEU A CD2 
10948 N N   . VAL A 1443 ? 1.6369 2.9543 2.6262 0.2361  -0.3649 -1.3025 1443 VAL A N   
10949 C CA  . VAL A 1443 ? 1.6291 2.9064 2.5778 0.2301  -0.3290 -1.2770 1443 VAL A CA  
10950 C C   . VAL A 1443 ? 1.6886 2.9089 2.5867 0.2113  -0.3154 -1.2703 1443 VAL A C   
10951 O O   . VAL A 1443 ? 1.6751 2.8798 2.5695 0.1882  -0.2833 -1.2635 1443 VAL A O   
10952 C CB  . VAL A 1443 ? 1.5851 2.8398 2.4896 0.2640  -0.3294 -1.2490 1443 VAL A CB  
10953 C CG1 . VAL A 1443 ? 1.5827 2.8783 2.5162 0.2919  -0.3603 -1.2565 1443 VAL A CG1 
10954 C CG2 . VAL A 1443 ? 1.6316 2.8199 2.4569 0.2760  -0.3325 -1.2288 1443 VAL A CG2 
10955 N N   . GLU A 1444 ? 2.1395 3.3286 2.9983 0.2214  -0.3402 -1.2724 1444 GLU A N   
10956 C CA  . GLU A 1444 ? 2.2266 3.3529 3.0233 0.2125  -0.3290 -1.2601 1444 GLU A CA  
10957 C C   . GLU A 1444 ? 2.2358 3.3566 3.0503 0.1741  -0.3115 -1.2751 1444 GLU A C   
10958 O O   . GLU A 1444 ? 2.2625 3.3352 3.0317 0.1649  -0.3091 -1.2715 1444 GLU A O   
10959 C CB  . GLU A 1444 ? 2.3924 3.4894 3.1446 0.2340  -0.3618 -1.2603 1444 GLU A CB  
10960 C CG  . GLU A 1444 ? 2.5200 3.5468 3.1946 0.2381  -0.3519 -1.2391 1444 GLU A CG  
10961 C CD  . GLU A 1444 ? 2.6134 3.6149 3.2396 0.2717  -0.3802 -1.2288 1444 GLU A CD  
10962 O OE1 . GLU A 1444 ? 2.5764 3.6019 3.2120 0.2978  -0.3923 -1.2213 1444 GLU A OE1 
10963 O OE2 . GLU A 1444 ? 2.7117 3.6693 3.2906 0.2721  -0.3899 -1.2280 1444 GLU A OE2 
10964 N N   . GLY A 1445 ? 2.0431 3.2116 2.9219 0.1513  -0.2987 -1.2915 1445 GLY A N   
10965 C CA  . GLY A 1445 ? 2.1244 3.2908 3.0236 0.1144  -0.2843 -1.3073 1445 GLY A CA  
10966 C C   . GLY A 1445 ? 2.1023 3.2881 3.0371 0.0880  -0.2480 -1.3062 1445 GLY A C   
10967 O O   . GLY A 1445 ? 2.0425 3.2575 3.0021 0.0966  -0.2354 -1.2984 1445 GLY A O   
10968 N N   . VAL A 1446 ? 1.4165 2.5842 2.3519 0.0556  -0.2313 -1.3141 1446 VAL A N   
10969 C CA  . VAL A 1446 ? 1.3888 2.5756 2.3617 0.0249  -0.1980 -1.3174 1446 VAL A CA  
10970 C C   . VAL A 1446 ? 1.3489 2.6083 2.4048 0.0139  -0.2053 -1.3429 1446 VAL A C   
10971 O O   . VAL A 1446 ? 1.2981 2.5846 2.3946 -0.0086 -0.1797 -1.3472 1446 VAL A O   
10972 C CB  . VAL A 1446 ? 1.4853 2.6323 2.4366 -0.0070 -0.1822 -1.3210 1446 VAL A CB  
10973 C CG1 . VAL A 1446 ? 1.4721 2.6451 2.4702 -0.0416 -0.1514 -1.3291 1446 VAL A CG1 
10974 C CG2 . VAL A 1446 ? 1.4995 2.5749 2.3702 0.0025  -0.1694 -1.2939 1446 VAL A CG2 
10975 N N   . ASP A 1447 ? 2.4086 3.6994 3.4897 0.0296  -0.2406 -1.3599 1447 ASP A N   
10976 C CA  . ASP A 1447 ? 2.4014 3.7626 3.5579 0.0282  -0.2504 -1.3803 1447 ASP A CA  
10977 C C   . ASP A 1447 ? 2.3105 3.6888 3.4645 0.0629  -0.2578 -1.3663 1447 ASP A C   
10978 O O   . ASP A 1447 ? 2.3009 3.7262 3.4973 0.0776  -0.2822 -1.3806 1447 ASP A O   
10979 C CB  . ASP A 1447 ? 2.5101 3.8993 3.7005 0.0241  -0.2854 -1.4084 1447 ASP A CB  
10980 C CG  . ASP A 1447 ? 2.5662 3.9383 3.7198 0.0572  -0.3217 -1.4052 1447 ASP A CG  
10981 O OD1 . ASP A 1447 ? 2.5274 3.8660 3.6294 0.0833  -0.3195 -1.3810 1447 ASP A OD1 
10982 O OD2 . ASP A 1447 ? 2.6391 4.0315 3.8154 0.0570  -0.3526 -1.4268 1447 ASP A OD2 
10983 N N   . GLN A 1448 ? 1.5604 2.8998 2.6641 0.0760  -0.2373 -1.3380 1448 GLN A N   
10984 C CA  . GLN A 1448 ? 1.4812 2.8287 2.5731 0.1106  -0.2454 -1.3222 1448 GLN A CA  
10985 C C   . GLN A 1448 ? 1.4064 2.8175 2.5647 0.1129  -0.2411 -1.3319 1448 GLN A C   
10986 O O   . GLN A 1448 ? 1.3718 2.7946 2.5487 0.0991  -0.2101 -1.3256 1448 GLN A O   
10987 C CB  . GLN A 1448 ? 1.4466 2.7389 2.4704 0.1242  -0.2247 -1.2892 1448 GLN A CB  
10988 C CG  . GLN A 1448 ? 1.4206 2.7023 2.4426 0.1044  -0.1827 -1.2750 1448 GLN A CG  
10989 C CD  . GLN A 1448 ? 1.4001 2.6293 2.3542 0.1229  -0.1671 -1.2418 1448 GLN A CD  
10990 O OE1 . GLN A 1448 ? 1.3497 2.5865 2.2957 0.1503  -0.1725 -1.2281 1448 GLN A OE1 
10991 N NE2 . GLN A 1448 ? 1.4305 2.6061 2.3360 0.1081  -0.1485 -1.2289 1448 GLN A NE2 
10992 N N   . LEU A 1449 ? 1.7536 3.2052 2.9467 0.1307  -0.2733 -1.3477 1449 LEU A N   
10993 C CA  . LEU A 1449 ? 1.7200 3.2354 2.9788 0.1367  -0.2763 -1.3599 1449 LEU A CA  
10994 C C   . LEU A 1449 ? 1.5907 3.1013 2.8274 0.1664  -0.2714 -1.3374 1449 LEU A C   
10995 O O   . LEU A 1449 ? 1.5104 3.0578 2.7859 0.1672  -0.2563 -1.3374 1449 LEU A O   
10996 C CB  . LEU A 1449 ? 1.8332 3.3893 3.1328 0.1458  -0.3152 -1.3847 1449 LEU A CB  
10997 C CG  . LEU A 1449 ? 1.8553 3.4704 3.2089 0.1659  -0.3302 -1.3939 1449 LEU A CG  
10998 C CD1 . LEU A 1449 ? 1.8238 3.4800 3.2304 0.1488  -0.3000 -1.3981 1449 LEU A CD1 
10999 C CD2 . LEU A 1449 ? 1.9340 3.5877 3.3293 0.1696  -0.3681 -1.4205 1449 LEU A CD2 
11000 N N   . PHE A 1450 ? 1.5550 3.0201 2.7289 0.1911  -0.2849 -1.3185 1450 PHE A N   
11001 C CA  . PHE A 1450 ? 1.4615 2.9111 2.6029 0.2187  -0.2788 -1.2934 1450 PHE A CA  
11002 C C   . PHE A 1450 ? 1.4661 2.8484 2.5340 0.2175  -0.2606 -1.2680 1450 PHE A C   
11003 O O   . PHE A 1450 ? 1.5200 2.8730 2.5688 0.1947  -0.2519 -1.2716 1450 PHE A O   
11004 C CB  . PHE A 1450 ? 1.4422 2.9033 2.5784 0.2532  -0.3152 -1.2938 1450 PHE A CB  
11005 C CG  . PHE A 1450 ? 1.4265 2.9538 2.6344 0.2568  -0.3340 -1.3177 1450 PHE A CG  
11006 C CD1 . PHE A 1450 ? 1.5071 3.0614 2.7523 0.2439  -0.3560 -1.3445 1450 PHE A CD1 
11007 C CD2 . PHE A 1450 ? 1.3513 2.9145 2.5910 0.2719  -0.3288 -1.3139 1450 PHE A CD2 
11008 C CE1 . PHE A 1450 ? 1.4939 3.1108 2.8075 0.2469  -0.3734 -1.3668 1450 PHE A CE1 
11009 C CE2 . PHE A 1450 ? 1.3503 2.9756 2.6580 0.2751  -0.3456 -1.3364 1450 PHE A CE2 
11010 C CZ  . PHE A 1450 ? 1.4183 3.0709 2.7634 0.2626  -0.3679 -1.3628 1450 PHE A CZ  
11011 N N   . THR A 1451 ? 1.1603 2.5171 2.1864 0.2421  -0.2552 -1.2422 1451 THR A N   
11012 C CA  . THR A 1451 ? 1.1146 2.4100 2.0742 0.2399  -0.2330 -1.2162 1451 THR A CA  
11013 C C   . THR A 1451 ? 1.0870 2.3498 1.9920 0.2745  -0.2464 -1.1925 1451 THR A C   
11014 O O   . THR A 1451 ? 1.0879 2.2962 1.9312 0.2783  -0.2354 -1.1705 1451 THR A O   
11015 C CB  . THR A 1451 ? 1.0200 2.3187 1.9895 0.2253  -0.1956 -1.2046 1451 THR A CB  
11016 O OG1 . THR A 1451 ? 0.9357 2.2607 1.9204 0.2490  -0.1975 -1.1956 1451 THR A OG1 
11017 C CG2 . THR A 1451 ? 1.0240 2.3629 2.0551 0.1920  -0.1807 -1.2281 1451 THR A CG2 
11018 N N   . ASP A 1452 ? 1.3061 2.6027 2.2345 0.3000  -0.2694 -1.1962 1452 ASP A N   
11019 C CA  . ASP A 1452 ? 1.3039 2.5713 2.1823 0.3331  -0.2890 -1.1775 1452 ASP A CA  
11020 C C   . ASP A 1452 ? 1.3304 2.6382 2.2408 0.3572  -0.3241 -1.1908 1452 ASP A C   
11021 O O   . ASP A 1452 ? 1.2838 2.6420 2.2490 0.3598  -0.3255 -1.2019 1452 ASP A O   
11022 C CB  . ASP A 1452 ? 1.1860 2.4261 2.0267 0.3459  -0.2659 -1.1474 1452 ASP A CB  
11023 C CG  . ASP A 1452 ? 1.1413 2.3282 1.9104 0.3700  -0.2765 -1.1236 1452 ASP A CG  
11024 O OD1 . ASP A 1452 ? 1.1419 2.3365 1.9037 0.3991  -0.3027 -1.1199 1452 ASP A OD1 
11025 O OD2 . ASP A 1452 ? 1.1130 2.2506 1.8333 0.3597  -0.2587 -1.1087 1452 ASP A OD2 
11026 N N   . TYR A 1453 ? 1.8492 3.1330 2.7235 0.3749  -0.3524 -1.1896 1453 TYR A N   
11027 C CA  . TYR A 1453 ? 1.8635 3.1767 2.7567 0.4005  -0.3887 -1.1996 1453 TYR A CA  
11028 C C   . TYR A 1453 ? 1.8440 3.1184 2.6762 0.4330  -0.4002 -1.1736 1453 TYR A C   
11029 O O   . TYR A 1453 ? 1.8508 3.0726 2.6239 0.4333  -0.3855 -1.1524 1453 TYR A O   
11030 C CB  . TYR A 1453 ? 1.9444 3.2658 2.8513 0.3914  -0.4155 -1.2241 1453 TYR A CB  
11031 C CG  . TYR A 1453 ? 2.0096 3.2798 2.8511 0.4053  -0.4334 -1.2136 1453 TYR A CG  
11032 C CD1 . TYR A 1453 ? 2.0633 3.2773 2.8484 0.3943  -0.4129 -1.1973 1453 TYR A CD1 
11033 C CD2 . TYR A 1453 ? 2.0586 3.3366 2.8945 0.4297  -0.4707 -1.2199 1453 TYR A CD2 
11034 C CE1 . TYR A 1453 ? 2.1350 3.3023 2.8603 0.4076  -0.4287 -1.1878 1453 TYR A CE1 
11035 C CE2 . TYR A 1453 ? 2.1347 3.3664 2.9106 0.4427  -0.4868 -1.2105 1453 TYR A CE2 
11036 C CZ  . TYR A 1453 ? 2.1519 3.3283 2.8725 0.4317  -0.4656 -1.1946 1453 TYR A CZ  
11037 O OH  . TYR A 1453 ? 2.1702 3.3001 2.8302 0.4454  -0.4814 -1.1852 1453 TYR A OH  
11038 N N   . GLN A 1454 ? 1.7015 3.0018 2.5479 0.4603  -0.4269 -1.1753 1454 GLN A N   
11039 C CA  . GLN A 1454 ? 1.6902 2.9561 2.4808 0.4918  -0.4406 -1.1519 1454 GLN A CA  
11040 C C   . GLN A 1454 ? 1.6873 2.9899 2.5049 0.5190  -0.4717 -1.1585 1454 GLN A C   
11041 O O   . GLN A 1454 ? 1.6283 2.9709 2.4895 0.5245  -0.4680 -1.1616 1454 GLN A O   
11042 C CB  . GLN A 1454 ? 1.6360 2.8743 2.3934 0.4973  -0.4112 -1.1229 1454 GLN A CB  
11043 C CG  . GLN A 1454 ? 1.5837 2.8642 2.3936 0.4896  -0.3911 -1.1264 1454 GLN A CG  
11044 C CD  . GLN A 1454 ? 1.5446 2.8040 2.3238 0.5041  -0.3709 -1.0975 1454 GLN A CD  
11045 O OE1 . GLN A 1454 ? 1.5309 2.7881 2.2928 0.5332  -0.3870 -1.0842 1454 GLN A OE1 
11046 N NE2 . GLN A 1454 ? 1.5216 2.7660 2.2947 0.4835  -0.3356 -1.0876 1454 GLN A NE2 
11047 N N   . ILE A 1455 ? 2.2293 3.5171 3.0192 0.5369  -0.5027 -1.1602 1455 ILE A N   
11048 C CA  . ILE A 1455 ? 2.2183 3.5361 3.0274 0.5648  -0.5339 -1.1645 1455 ILE A CA  
11049 C C   . ILE A 1455 ? 2.1697 3.4588 2.9312 0.5942  -0.5338 -1.1347 1455 ILE A C   
11050 O O   . ILE A 1455 ? 2.1972 3.4406 2.8980 0.6078  -0.5416 -1.1182 1455 ILE A O   
11051 C CB  . ILE A 1455 ? 2.3941 3.7127 3.1984 0.5713  -0.5697 -1.1812 1455 ILE A CB  
11052 C CG1 . ILE A 1455 ? 2.4323 3.7869 3.2920 0.5432  -0.5733 -1.2128 1455 ILE A CG1 
11053 C CG2 . ILE A 1455 ? 2.3964 3.7387 3.2106 0.6033  -0.6019 -1.1809 1455 ILE A CG2 
11054 C CD1 . ILE A 1455 ? 2.4720 3.7916 3.3064 0.5151  -0.5557 -1.2159 1455 ILE A CD1 
11055 N N   . LYS A 1456 ? 1.6534 2.9692 2.4423 0.6040  -0.5247 -1.1278 1456 LYS A N   
11056 C CA  . LYS A 1456 ? 1.6200 2.9141 2.3696 0.6334  -0.5284 -1.1014 1456 LYS A CA  
11057 C C   . LYS A 1456 ? 1.5623 2.8978 2.3476 0.6578  -0.5577 -1.1100 1456 LYS A C   
11058 O O   . LYS A 1456 ? 1.5217 2.9084 2.3709 0.6502  -0.5641 -1.1329 1456 LYS A O   
11059 C CB  . LYS A 1456 ? 1.6014 2.8824 2.3406 0.6282  -0.4930 -1.0804 1456 LYS A CB  
11060 C CG  . LYS A 1456 ? 1.6566 2.8982 2.3376 0.6543  -0.4920 -1.0484 1456 LYS A CG  
11061 C CD  . LYS A 1456 ? 1.6392 2.8746 2.3174 0.6497  -0.4588 -1.0295 1456 LYS A CD  
11062 C CE  . LYS A 1456 ? 1.6526 2.8424 2.2672 0.6721  -0.4546 -0.9960 1456 LYS A CE  
11063 N NZ  . LYS A 1456 ? 1.7079 2.8437 2.2606 0.6685  -0.4513 -0.9834 1456 LYS A NZ  
11064 N N   . ASP A 1457 ? 1.8492 3.1607 2.5915 0.6873  -0.5754 -1.0910 1457 ASP A N   
11065 C CA  . ASP A 1457 ? 1.8538 3.1962 2.6189 0.7147  -0.6029 -1.0932 1457 ASP A CA  
11066 C C   . ASP A 1457 ? 1.8203 3.2242 2.6620 0.7060  -0.6152 -1.1235 1457 ASP A C   
11067 O O   . ASP A 1457 ? 1.7632 3.2021 2.6474 0.7083  -0.6067 -1.1262 1457 ASP A O   
11068 C CB  . ASP A 1457 ? 1.8309 3.1655 2.5811 0.7325  -0.5887 -1.0681 1457 ASP A CB  
11069 C CG  . ASP A 1457 ? 1.8820 3.1564 2.5576 0.7403  -0.5744 -1.0369 1457 ASP A CG  
11070 O OD1 . ASP A 1457 ? 1.9718 3.2148 2.6008 0.7553  -0.5940 -1.0284 1457 ASP A OD1 
11071 O OD2 . ASP A 1457 ? 1.8350 3.0938 2.4988 0.7315  -0.5432 -1.0206 1457 ASP A OD2 
11072 N N   . GLY A 1458 ? 1.6494 3.0660 2.5085 0.6956  -0.6348 -1.1464 1458 GLY A N   
11073 C CA  . GLY A 1458 ? 1.6212 3.0963 2.5510 0.6909  -0.6529 -1.1755 1458 GLY A CA  
11074 C C   . GLY A 1458 ? 1.5567 3.0668 2.5433 0.6610  -0.6278 -1.1932 1458 GLY A C   
11075 O O   . GLY A 1458 ? 1.5438 3.1069 2.5943 0.6585  -0.6376 -1.2145 1458 GLY A O   
11076 N N   . HIS A 1459 ? 1.8520 3.3333 2.8165 0.6380  -0.5952 -1.1847 1459 HIS A N   
11077 C CA  . HIS A 1459 ? 1.8159 3.3297 2.8330 0.6099  -0.5701 -1.2001 1459 HIS A CA  
11078 C C   . HIS A 1459 ? 1.8111 3.2986 2.8115 0.5794  -0.5506 -1.2048 1459 HIS A C   
11079 O O   . HIS A 1459 ? 1.7973 3.2319 2.7369 0.5779  -0.5378 -1.1851 1459 HIS A O   
11080 C CB  . HIS A 1459 ? 1.7593 3.2756 2.7805 0.6123  -0.5412 -1.1831 1459 HIS A CB  
11081 C CG  . HIS A 1459 ? 1.7804 3.3250 2.8230 0.6406  -0.5569 -1.1789 1459 HIS A CG  
11082 N ND1 . HIS A 1459 ? 1.7844 3.3872 2.8967 0.6396  -0.5614 -1.1987 1459 HIS A ND1 
11083 C CD2 . HIS A 1459 ? 1.7850 3.3074 2.7884 0.6704  -0.5679 -1.1566 1459 HIS A CD2 
11084 C CE1 . HIS A 1459 ? 1.7578 3.3721 2.8725 0.6679  -0.5750 -1.1891 1459 HIS A CE1 
11085 N NE2 . HIS A 1459 ? 1.7571 3.3232 2.8063 0.6867  -0.5793 -1.1635 1459 HIS A NE2 
11086 N N   . VAL A 1460 ? 1.3851 2.9110 2.4416 0.5550  -0.5485 -1.2312 1460 VAL A N   
11087 C CA  . VAL A 1460 ? 1.4308 2.9403 2.4842 0.5219  -0.5270 -1.2389 1460 VAL A CA  
11088 C C   . VAL A 1460 ? 1.4204 2.9384 2.4943 0.5028  -0.4880 -1.2331 1460 VAL A C   
11089 O O   . VAL A 1460 ? 1.4151 2.9830 2.5497 0.4971  -0.4829 -1.2474 1460 VAL A O   
11090 C CB  . VAL A 1460 ? 1.4908 3.0400 2.5982 0.5032  -0.5440 -1.2714 1460 VAL A CB  
11091 C CG1 . VAL A 1460 ? 1.4836 3.0414 2.6195 0.4662  -0.5130 -1.2825 1460 VAL A CG1 
11092 C CG2 . VAL A 1460 ? 1.5791 3.1020 2.6515 0.5087  -0.5736 -1.2772 1460 VAL A CG2 
11093 N N   . ILE A 1461 ? 1.5247 2.9943 2.5484 0.4924  -0.4605 -1.2127 1461 ILE A N   
11094 C CA  . ILE A 1461 ? 1.4451 2.9168 2.4802 0.4757  -0.4224 -1.2037 1461 ILE A CA  
11095 C C   . ILE A 1461 ? 1.4653 2.9151 2.4922 0.4415  -0.3946 -1.2067 1461 ILE A C   
11096 O O   . ILE A 1461 ? 1.4732 2.8702 2.4420 0.4375  -0.3838 -1.1899 1461 ILE A O   
11097 C CB  . ILE A 1461 ? 1.3350 2.7742 2.3231 0.4966  -0.4097 -1.1728 1461 ILE A CB  
11098 C CG1 . ILE A 1461 ? 1.2945 2.7698 2.3112 0.5243  -0.4278 -1.1728 1461 ILE A CG1 
11099 C CG2 . ILE A 1461 ? 1.2473 2.6758 2.2336 0.4758  -0.3693 -1.1619 1461 ILE A CG2 
11100 C CD1 . ILE A 1461 ? 1.2661 2.7062 2.2293 0.5523  -0.4291 -1.1433 1461 ILE A CD1 
11101 N N   . LEU A 1462 ? 1.3016 2.7933 2.3884 0.4167  -0.3825 -1.2281 1462 LEU A N   
11102 C CA  . LEU A 1462 ? 1.3398 2.8179 2.4281 0.3823  -0.3588 -1.2351 1462 LEU A CA  
11103 C C   . LEU A 1462 ? 1.3176 2.7985 2.4174 0.3650  -0.3195 -1.2257 1462 LEU A C   
11104 O O   . LEU A 1462 ? 1.2738 2.7989 2.4224 0.3666  -0.3128 -1.2327 1462 LEU A O   
11105 C CB  . LEU A 1462 ? 1.3538 2.8767 2.5022 0.3634  -0.3734 -1.2676 1462 LEU A CB  
11106 C CG  . LEU A 1462 ? 1.2445 2.7539 2.3732 0.3723  -0.4081 -1.2774 1462 LEU A CG  
11107 C CD1 . LEU A 1462 ? 1.2881 2.8517 2.4841 0.3603  -0.4273 -1.3093 1462 LEU A CD1 
11108 C CD2 . LEU A 1462 ? 1.2846 2.7384 2.3593 0.3555  -0.3963 -1.2688 1462 LEU A CD2 
11109 N N   . GLN A 1463 ? 1.3349 2.7691 2.3903 0.3482  -0.2937 -1.2105 1463 GLN A N   
11110 C CA  . GLN A 1463 ? 1.2603 2.6943 2.3254 0.3268  -0.2548 -1.2030 1463 GLN A CA  
11111 C C   . GLN A 1463 ? 1.2577 2.6988 2.3495 0.2896  -0.2386 -1.2211 1463 GLN A C   
11112 O O   . GLN A 1463 ? 1.2858 2.7116 2.3669 0.2792  -0.2523 -1.2320 1463 GLN A O   
11113 C CB  . GLN A 1463 ? 1.2534 2.6304 2.2504 0.3343  -0.2335 -1.1704 1463 GLN A CB  
11114 C CG  . GLN A 1463 ? 1.2129 2.5922 2.1988 0.3602  -0.2294 -1.1502 1463 GLN A CG  
11115 C CD  . GLN A 1463 ? 1.2317 2.5511 2.1457 0.3695  -0.2142 -1.1182 1463 GLN A CD  
11116 O OE1 . GLN A 1463 ? 1.2041 2.5121 2.0919 0.3959  -0.2198 -1.0991 1463 GLN A OE1 
11117 N NE2 . GLN A 1463 ? 1.2801 2.5606 2.1617 0.3478  -0.1951 -1.1122 1463 GLN A NE2 
11118 N N   . LEU A 1464 ? 1.5669 3.0310 2.6931 0.2696  -0.2089 -1.2237 1464 LEU A N   
11119 C CA  . LEU A 1464 ? 1.5895 3.0583 2.7391 0.2331  -0.1878 -1.2373 1464 LEU A CA  
11120 C C   . LEU A 1464 ? 1.5576 3.0463 2.7339 0.2191  -0.1537 -1.2326 1464 LEU A C   
11121 O O   . LEU A 1464 ? 1.4727 2.9765 2.6552 0.2381  -0.1500 -1.2224 1464 LEU A O   
11122 C CB  . LEU A 1464 ? 1.6377 3.1535 2.8469 0.2205  -0.2085 -1.2693 1464 LEU A CB  
11123 C CG  . LEU A 1464 ? 1.5862 3.1591 2.8489 0.2409  -0.2323 -1.2842 1464 LEU A CG  
11124 C CD1 . LEU A 1464 ? 1.4953 3.0940 2.7801 0.2511  -0.2141 -1.2750 1464 LEU A CD1 
11125 C CD2 . LEU A 1464 ? 1.6327 3.2552 2.9613 0.2206  -0.2440 -1.3164 1464 LEU A CD2 
11126 N N   . ASN A 1465 ? 1.5263 3.0158 2.7197 0.1856  -0.1293 -1.2409 1465 ASN A N   
11127 C CA  . ASN A 1465 ? 1.5296 3.0270 2.7375 0.1682  -0.0923 -1.2337 1465 ASN A CA  
11128 C C   . ASN A 1465 ? 1.5146 3.0778 2.7963 0.1626  -0.0872 -1.2528 1465 ASN A C   
11129 O O   . ASN A 1465 ? 1.4529 3.0267 2.7427 0.1645  -0.0649 -1.2426 1465 ASN A O   
11130 C CB  . ASN A 1465 ? 1.5889 3.0579 2.7826 0.1339  -0.0676 -1.2341 1465 ASN A CB  
11131 C CG  . ASN A 1465 ? 1.6356 3.0457 2.7657 0.1366  -0.0771 -1.2221 1465 ASN A CG  
11132 O OD1 . ASN A 1465 ? 1.5998 2.9612 2.6784 0.1318  -0.0555 -1.2000 1465 ASN A OD1 
11133 N ND2 . ASN A 1465 ? 1.6879 3.1016 2.8204 0.1450  -0.1100 -1.2364 1465 ASN A ND2 
11134 N N   . SER A 1466 ? 1.6415 3.2490 2.9774 0.1553  -0.1073 -1.2804 1466 SER A N   
11135 C CA  . SER A 1466 ? 1.6562 3.3278 3.0657 0.1470  -0.1011 -1.3003 1466 SER A CA  
11136 C C   . SER A 1466 ? 1.6677 3.3866 3.1257 0.1600  -0.1369 -1.3242 1466 SER A C   
11137 O O   . SER A 1466 ? 1.6872 3.3901 3.1255 0.1691  -0.1653 -1.3287 1466 SER A O   
11138 C CB  . SER A 1466 ? 1.7109 3.3951 3.1517 0.1077  -0.0723 -1.3122 1466 SER A CB  
11139 O OG  . SER A 1466 ? 1.7309 3.4791 3.2453 0.0989  -0.0670 -1.3329 1466 SER A OG  
11140 N N   . ILE A 1467 ? 1.3725 3.1494 2.8933 0.1616  -0.1355 -1.3392 1467 ILE A N   
11141 C CA  . ILE A 1467 ? 1.4274 3.2558 3.0037 0.1702  -0.1666 -1.3642 1467 ILE A CA  
11142 C C   . ILE A 1467 ? 1.4688 3.3531 3.1178 0.1449  -0.1486 -1.3859 1467 ILE A C   
11143 O O   . ILE A 1467 ? 1.4780 3.4124 3.1774 0.1563  -0.1531 -1.3965 1467 ILE A O   
11144 C CB  . ILE A 1467 ? 1.3383 3.1851 2.9185 0.2077  -0.1886 -1.3588 1467 ILE A CB  
11145 C CG1 . ILE A 1467 ? 1.2680 3.0576 2.7729 0.2335  -0.2009 -1.3332 1467 ILE A CG1 
11146 C CG2 . ILE A 1467 ? 1.3954 3.2925 3.0297 0.2174  -0.2234 -1.3844 1467 ILE A CG2 
11147 C CD1 . ILE A 1467 ? 1.2186 3.0247 2.7262 0.2706  -0.2281 -1.3295 1467 ILE A CD1 
11148 N N   . PRO A 1468 ? 0.9856 2.8610 2.6400 0.1103  -0.1275 -1.3924 1468 PRO A N   
11149 C CA  . PRO A 1468 ? 0.9791 2.9019 2.6976 0.0816  -0.1052 -1.4111 1468 PRO A CA  
11150 C C   . PRO A 1468 ? 0.9929 2.9876 2.7896 0.0877  -0.1238 -1.4371 1468 PRO A C   
11151 O O   . PRO A 1468 ? 0.9790 2.9903 2.7873 0.1087  -0.1590 -1.4467 1468 PRO A O   
11152 C CB  . PRO A 1468 ? 1.0378 2.9370 2.7465 0.0491  -0.0983 -1.4184 1468 PRO A CB  
11153 C CG  . PRO A 1468 ? 1.0342 2.8612 2.6600 0.0564  -0.0940 -1.3922 1468 PRO A CG  
11154 C CD  . PRO A 1468 ? 1.0101 2.8256 2.6056 0.0962  -0.1222 -1.3807 1468 PRO A CD  
11155 N N   . SER A 1469 ? 0.8013 2.8386 2.6511 0.0695  -0.0990 -1.4478 1469 SER A N   
11156 C CA  . SER A 1469 ? 0.8188 2.9230 2.7390 0.0794  -0.1109 -1.4678 1469 SER A CA  
11157 C C   . SER A 1469 ? 0.8925 3.0418 2.8768 0.0499  -0.1100 -1.4951 1469 SER A C   
11158 O O   . SER A 1469 ? 0.9239 3.1334 2.9748 0.0506  -0.1131 -1.5137 1469 SER A O   
11159 C CB  . SER A 1469 ? 0.7593 2.8826 2.6948 0.0852  -0.0832 -1.4590 1469 SER A CB  
11160 O OG  . SER A 1469 ? 0.7141 2.7917 2.5871 0.1091  -0.0792 -1.4316 1469 SER A OG  
11161 N N   . SER A 1470 ? 1.6752 3.7958 3.6401 0.0234  -0.1049 -1.4974 1470 SER A N   
11162 C CA  . SER A 1470 ? 1.7272 3.8877 3.7506 -0.0054 -0.1073 -1.5237 1470 SER A CA  
11163 C C   . SER A 1470 ? 1.7350 3.9291 3.7926 0.0101  -0.1502 -1.5438 1470 SER A C   
11164 O O   . SER A 1470 ? 1.7724 4.0252 3.9004 0.0002  -0.1578 -1.5680 1470 SER A O   
11165 C CB  . SER A 1470 ? 1.7892 3.9042 3.7763 -0.0357 -0.0932 -1.5194 1470 SER A CB  
11166 O OG  . SER A 1470 ? 1.8179 3.8673 3.7266 -0.0200 -0.1023 -1.4976 1470 SER A OG  
11167 N N   . ASP A 1471 ? 1.1216 3.2776 3.1280 0.0347  -0.1779 -1.5331 1471 ASP A N   
11168 C CA  . ASP A 1471 ? 1.1492 3.3290 3.1760 0.0550  -0.2205 -1.5479 1471 ASP A CA  
11169 C C   . ASP A 1471 ? 1.0386 3.1747 3.0013 0.0905  -0.2387 -1.5260 1471 ASP A C   
11170 O O   . ASP A 1471 ? 0.9523 3.0563 2.8728 0.1003  -0.2173 -1.5030 1471 ASP A O   
11171 C CB  . ASP A 1471 ? 1.3085 3.4827 3.3413 0.0334  -0.2384 -1.5645 1471 ASP A CB  
11172 C CG  . ASP A 1471 ? 1.3995 3.5012 3.3563 0.0239  -0.2321 -1.5472 1471 ASP A CG  
11173 O OD1 . ASP A 1471 ? 1.4912 3.5837 3.4517 -0.0029 -0.2329 -1.5586 1471 ASP A OD1 
11174 O OD2 . ASP A 1471 ? 1.3648 3.4185 3.2587 0.0431  -0.2264 -1.5224 1471 ASP A OD2 
11175 N N   . PHE A 1472 ? 1.3088 3.4432 3.2633 0.1097  -0.2776 -1.5326 1472 PHE A N   
11176 C CA  . PHE A 1472 ? 1.2229 3.3139 3.1144 0.1428  -0.2956 -1.5117 1472 PHE A CA  
11177 C C   . PHE A 1472 ? 1.2212 3.2413 3.0368 0.1351  -0.2895 -1.4938 1472 PHE A C   
11178 O O   . PHE A 1472 ? 1.2409 3.2426 3.0498 0.1045  -0.2687 -1.4957 1472 PHE A O   
11179 C CB  . PHE A 1472 ? 1.2497 3.3642 3.1581 0.1682  -0.3400 -1.5243 1472 PHE A CB  
11180 C CG  . PHE A 1472 ? 1.2082 3.3807 3.1734 0.1883  -0.3498 -1.5340 1472 PHE A CG  
11181 C CD1 . PHE A 1472 ? 1.2238 3.4574 3.2657 0.1703  -0.3386 -1.5554 1472 PHE A CD1 
11182 C CD2 . PHE A 1472 ? 1.1826 3.3493 3.1256 0.2254  -0.3709 -1.5223 1472 PHE A CD2 
11183 C CE1 . PHE A 1472 ? 1.2021 3.4897 3.2974 0.1893  -0.3477 -1.5650 1472 PHE A CE1 
11184 C CE2 . PHE A 1472 ? 1.1605 3.3803 3.1562 0.2443  -0.3805 -1.5317 1472 PHE A CE2 
11185 C CZ  . PHE A 1472 ? 1.1704 3.4508 3.2425 0.2265  -0.3689 -1.5532 1472 PHE A CZ  
11186 N N   . LEU A 1473 ? 1.8285 3.8093 3.5872 0.1641  -0.3081 -1.4761 1473 LEU A N   
11187 C CA  . LEU A 1473 ? 1.8668 3.7823 3.5535 0.1626  -0.3112 -1.4610 1473 LEU A CA  
11188 C C   . LEU A 1473 ? 1.9217 3.8263 3.5818 0.1955  -0.3509 -1.4585 1473 LEU A C   
11189 O O   . LEU A 1473 ? 1.8782 3.7850 3.5267 0.2252  -0.3584 -1.4458 1473 LEU A O   
11190 C CB  . LEU A 1473 ? 1.7683 3.6341 3.3975 0.1634  -0.2788 -1.4321 1473 LEU A CB  
11191 C CG  . LEU A 1473 ? 1.7915 3.5858 3.3392 0.1683  -0.2812 -1.4117 1473 LEU A CG  
11192 C CD1 . LEU A 1473 ? 1.7810 3.5361 3.2955 0.1441  -0.2421 -1.3961 1473 LEU A CD1 
11193 C CD2 . LEU A 1473 ? 1.7563 3.5245 3.2564 0.2064  -0.2982 -1.3910 1473 LEU A CD2 
11194 N N   . CYS A 1474 ? 1.5461 3.4397 3.1974 0.1904  -0.3767 -1.4707 1474 CYS A N   
11195 C CA  . CYS A 1474 ? 1.5484 3.4375 3.1809 0.2206  -0.4166 -1.4713 1474 CYS A CA  
11196 C C   . CYS A 1474 ? 1.6071 3.4329 3.1645 0.2288  -0.4303 -1.4574 1474 CYS A C   
11197 O O   . CYS A 1474 ? 1.6758 3.4739 3.2137 0.2057  -0.4260 -1.4621 1474 CYS A O   
11198 C CB  . CYS A 1474 ? 1.5602 3.5071 3.2591 0.2190  -0.4466 -1.5008 1474 CYS A CB  
11199 S SG  . CYS A 1474 ? 1.6485 3.6630 3.4138 0.2407  -0.4523 -1.5085 1474 CYS A SG  
11200 N N   . VAL A 1475 ? 1.2841 3.0882 2.8005 0.2626  -0.4472 -1.4404 1475 VAL A N   
11201 C CA  . VAL A 1475 ? 1.3498 3.0984 2.7962 0.2775  -0.4654 -1.4269 1475 VAL A CA  
11202 C C   . VAL A 1475 ? 1.4568 3.2273 2.9217 0.2896  -0.5088 -1.4464 1475 VAL A C   
11203 O O   . VAL A 1475 ? 1.4499 3.2769 2.9758 0.2957  -0.5256 -1.4644 1475 VAL A O   
11204 C CB  . VAL A 1475 ? 1.2574 2.9768 2.6551 0.3090  -0.4630 -1.3992 1475 VAL A CB  
11205 C CG1 . VAL A 1475 ? 1.2132 2.9840 2.6576 0.3330  -0.4780 -1.4045 1475 VAL A CG1 
11206 C CG2 . VAL A 1475 ? 1.2901 2.9557 2.6173 0.3278  -0.4846 -1.3853 1475 VAL A CG2 
11207 N N   . ARG A 1476 ? 1.3190 3.0455 2.7322 0.2927  -0.5270 -1.4433 1476 ARG A N   
11208 C CA  . ARG A 1476 ? 1.3605 3.0994 2.7784 0.3096  -0.5697 -1.4572 1476 ARG A CA  
11209 C C   . ARG A 1476 ? 1.3393 3.0178 2.6783 0.3285  -0.5852 -1.4397 1476 ARG A C   
11210 O O   . ARG A 1476 ? 1.3191 2.9464 2.6073 0.3153  -0.5681 -1.4282 1476 ARG A O   
11211 C CB  . ARG A 1476 ? 1.4723 3.2402 2.9360 0.2834  -0.5832 -1.4865 1476 ARG A CB  
11212 C CG  . ARG A 1476 ? 1.5627 3.3032 3.0139 0.2483  -0.5562 -1.4883 1476 ARG A CG  
11213 C CD  . ARG A 1476 ? 1.6030 3.3945 3.1257 0.2219  -0.5331 -1.5039 1476 ARG A CD  
11214 N NE  . ARG A 1476 ? 1.6664 3.4276 3.1700 0.1936  -0.4950 -1.4951 1476 ARG A NE  
11215 C CZ  . ARG A 1476 ? 1.7030 3.4977 3.2577 0.1671  -0.4684 -1.5049 1476 ARG A CZ  
11216 N NH1 . ARG A 1476 ? 1.7087 3.5695 3.3382 0.1652  -0.4752 -1.5243 1476 ARG A NH1 
11217 N NH2 . ARG A 1476 ? 1.6993 3.4610 3.2299 0.1427  -0.4346 -1.4950 1476 ARG A NH2 
11218 N N   . PHE A 1477 ? 2.0712 3.7566 3.4011 0.3598  -0.6175 -1.4379 1477 PHE A N   
11219 C CA  . PHE A 1477 ? 2.0928 3.7263 3.3513 0.3816  -0.6371 -1.4226 1477 PHE A CA  
11220 C C   . PHE A 1477 ? 2.1400 3.7995 3.4134 0.4069  -0.6807 -1.4342 1477 PHE A C   
11221 O O   . PHE A 1477 ? 2.1264 3.8405 3.4584 0.4149  -0.6927 -1.4471 1477 PHE A O   
11222 C CB  . PHE A 1477 ? 2.0026 3.5928 3.2031 0.4003  -0.6164 -1.3900 1477 PHE A CB  
11223 C CG  . PHE A 1477 ? 1.9417 3.5618 3.1633 0.4270  -0.6199 -1.3807 1477 PHE A CG  
11224 C CD1 . PHE A 1477 ? 1.9464 3.5453 3.1257 0.4610  -0.6403 -1.3639 1477 PHE A CD1 
11225 C CD2 . PHE A 1477 ? 1.8796 3.5483 3.1626 0.4180  -0.6024 -1.3887 1477 PHE A CD2 
11226 C CE1 . PHE A 1477 ? 1.8896 3.5146 3.0877 0.4853  -0.6438 -1.3552 1477 PHE A CE1 
11227 C CE2 . PHE A 1477 ? 1.8309 3.5256 3.1323 0.4427  -0.6058 -1.3805 1477 PHE A CE2 
11228 C CZ  . PHE A 1477 ? 1.8301 3.5026 3.0890 0.4762  -0.6267 -1.3637 1477 PHE A CZ  
11229 N N   . ARG A 1478 ? 1.1840 2.8043 2.4041 0.4197  -0.7043 -1.4298 1478 ARG A N   
11230 C CA  . ARG A 1478 ? 1.2313 2.8739 2.4642 0.4394  -0.7466 -1.4433 1478 ARG A CA  
11231 C C   . ARG A 1478 ? 1.2127 2.8281 2.3943 0.4769  -0.7612 -1.4201 1478 ARG A C   
11232 O O   . ARG A 1478 ? 1.1136 2.6839 2.2405 0.4847  -0.7399 -1.3944 1478 ARG A O   
11233 C CB  . ARG A 1478 ? 1.3273 2.9505 2.5447 0.4225  -0.7642 -1.4597 1478 ARG A CB  
11234 C CG  . ARG A 1478 ? 1.3490 2.9764 2.5938 0.3824  -0.7369 -1.4727 1478 ARG A CG  
11235 C CD  . ARG A 1478 ? 1.4822 3.0854 2.7090 0.3616  -0.7496 -1.4882 1478 ARG A CD  
11236 N NE  . ARG A 1478 ? 1.5116 3.0443 2.6575 0.3630  -0.7407 -1.4695 1478 ARG A NE  
11237 C CZ  . ARG A 1478 ? 1.5833 3.0841 2.7037 0.3426  -0.7427 -1.4784 1478 ARG A CZ  
11238 N NH1 . ARG A 1478 ? 1.6510 3.1835 2.8204 0.3178  -0.7533 -1.5058 1478 ARG A NH1 
11239 N NH2 . ARG A 1478 ? 1.5946 3.0310 2.6400 0.3470  -0.7340 -1.4597 1478 ARG A NH2 
11240 N N   . ILE A 1479 ? 1.7242 3.3677 2.9243 0.5003  -0.7969 -1.4287 1479 ILE A N   
11241 C CA  . ILE A 1479 ? 1.7841 3.4089 2.9435 0.5366  -0.8110 -1.4074 1479 ILE A CA  
11242 C C   . ILE A 1479 ? 1.9269 3.5541 3.0737 0.5593  -0.8556 -1.4154 1479 ILE A C   
11243 O O   . ILE A 1479 ? 1.9990 3.6668 3.1943 0.5531  -0.8802 -1.4406 1479 ILE A O   
11244 C CB  . ILE A 1479 ? 1.7187 3.3812 2.9178 0.5504  -0.7993 -1.4000 1479 ILE A CB  
11245 C CG1 . ILE A 1479 ? 1.7404 3.4727 3.0261 0.5405  -0.8100 -1.4276 1479 ILE A CG1 
11246 C CG2 . ILE A 1479 ? 1.6671 3.3101 2.8539 0.5362  -0.7558 -1.3830 1479 ILE A CG2 
11247 C CD1 . ILE A 1479 ? 1.6566 3.4275 2.9839 0.5534  -0.7992 -1.4225 1479 ILE A CD1 
11248 N N   . PHE A 1480 ? 2.3082 3.8921 3.3898 0.5855  -0.8655 -1.3933 1480 PHE A N   
11249 C CA  . PHE A 1480 ? 2.5004 4.0772 3.5580 0.6077  -0.9059 -1.3974 1480 PHE A CA  
11250 C C   . PHE A 1480 ? 2.4062 3.9775 3.4384 0.6447  -0.9200 -1.3772 1480 PHE A C   
11251 O O   . PHE A 1480 ? 2.3751 3.8986 3.3445 0.6590  -0.9087 -1.3512 1480 PHE A O   
11252 C CB  . PHE A 1480 ? 2.8098 4.3295 3.8015 0.6008  -0.9094 -1.3931 1480 PHE A CB  
11253 C CG  . PHE A 1480 ? 2.8854 4.3562 3.8302 0.5870  -0.8711 -1.3731 1480 PHE A CG  
11254 C CD1 . PHE A 1480 ? 2.8202 4.2647 3.7274 0.6049  -0.8516 -1.3444 1480 PHE A CD1 
11255 C CD2 . PHE A 1480 ? 2.9568 4.4073 3.8947 0.5562  -0.8553 -1.3830 1480 PHE A CD2 
11256 C CE1 . PHE A 1480 ? 2.7713 4.1711 3.6357 0.5924  -0.8170 -1.3258 1480 PHE A CE1 
11257 C CE2 . PHE A 1480 ? 2.9012 4.3064 3.7960 0.5438  -0.8206 -1.3646 1480 PHE A CE2 
11258 C CZ  . PHE A 1480 ? 2.8133 4.1934 3.6715 0.5620  -0.8015 -1.3360 1480 PHE A CZ  
11259 N N   . GLU A 1481 ? 2.0685 3.6892 3.1503 0.6602  -0.9455 -1.3896 1481 GLU A N   
11260 C CA  . GLU A 1481 ? 2.0325 3.6538 3.0977 0.6953  -0.9612 -1.3726 1481 GLU A CA  
11261 C C   . GLU A 1481 ? 2.0634 3.6249 3.0453 0.7145  -0.9712 -1.3513 1481 GLU A C   
11262 O O   . GLU A 1481 ? 2.1623 3.7133 3.1239 0.7205  -1.0008 -1.3604 1481 GLU A O   
11263 C CB  . GLU A 1481 ? 2.0818 3.7556 3.2001 0.7097  -0.9987 -1.3927 1481 GLU A CB  
11264 C CG  . GLU A 1481 ? 2.4592 4.1974 3.6640 0.6947  -0.9919 -1.4140 1481 GLU A CG  
11265 C CD  . GLU A 1481 ? 2.4919 4.2808 3.7460 0.7150  -1.0277 -1.4287 1481 GLU A CD  
11266 O OE1 . GLU A 1481 ? 2.5302 4.3057 3.7522 0.7451  -1.0526 -1.4169 1481 GLU A OE1 
11267 O OE2 . GLU A 1481 ? 2.4782 4.3211 3.8043 0.7008  -1.0304 -1.4520 1481 GLU A OE2 
11268 N N   . LEU A 1482 ? 1.4102 2.9327 2.3440 0.7238  -0.9466 -1.3232 1482 LEU A N   
11269 C CA  . LEU A 1482 ? 1.4155 2.8823 2.2703 0.7445  -0.9547 -1.3005 1482 LEU A CA  
11270 C C   . LEU A 1482 ? 1.4125 2.8900 2.2599 0.7790  -0.9898 -1.2953 1482 LEU A C   
11271 O O   . LEU A 1482 ? 1.4707 2.9086 2.2582 0.7969  -1.0054 -1.2819 1482 LEU A O   
11272 C CB  . LEU A 1482 ? 1.3551 2.7789 2.1629 0.7445  -0.9179 -1.2714 1482 LEU A CB  
11273 C CG  . LEU A 1482 ? 1.3864 2.7552 2.1160 0.7690  -0.9156 -1.2398 1482 LEU A CG  
11274 C CD1 . LEU A 1482 ? 1.3279 2.6525 2.0158 0.7555  -0.8753 -1.2185 1482 LEU A CD1 
11275 C CD2 . LEU A 1482 ? 1.3629 2.7468 2.0953 0.8010  -0.9287 -1.2246 1482 LEU A CD2 
11276 N N   . PHE A 1483 ? 1.8423 3.3727 2.7497 0.7885  -1.0020 -1.3055 1483 PHE A N   
11277 C CA  . PHE A 1483 ? 1.8721 3.4206 2.7836 0.8179  -1.0408 -1.3076 1483 PHE A CA  
11278 C C   . PHE A 1483 ? 1.8898 3.5039 2.8793 0.8233  -1.0557 -1.3256 1483 PHE A C   
11279 O O   . PHE A 1483 ? 1.8518 3.5031 2.8993 0.8026  -1.0379 -1.3401 1483 PHE A O   
11280 C CB  . PHE A 1483 ? 1.8074 3.3162 2.6560 0.8488  -1.0446 -1.2772 1483 PHE A CB  
11281 C CG  . PHE A 1483 ? 1.6673 3.1698 2.5123 0.8536  -1.0136 -1.2552 1483 PHE A CG  
11282 C CD1 . PHE A 1483 ? 1.5827 3.1300 2.4920 0.8424  -0.9963 -1.2647 1483 PHE A CD1 
11283 C CD2 . PHE A 1483 ? 1.6292 3.0813 2.4068 0.8692  -1.0013 -1.2250 1483 PHE A CD2 
11284 C CE1 . PHE A 1483 ? 1.4508 2.9920 2.3564 0.8464  -0.9674 -1.2447 1483 PHE A CE1 
11285 C CE2 . PHE A 1483 ? 1.5108 2.9568 2.2848 0.8731  -0.9728 -1.2045 1483 PHE A CE2 
11286 C CZ  . PHE A 1483 ? 1.4217 2.9119 2.2594 0.8617  -0.9559 -1.2145 1483 PHE A CZ  
11287 N N   . GLU A 1484 ? 2.6328 4.2600 3.6222 0.8516  -1.0892 -1.3244 1484 GLU A N   
11288 C CA  . GLU A 1484 ? 2.6935 4.3815 3.7535 0.8583  -1.1125 -1.3449 1484 GLU A CA  
11289 C C   . GLU A 1484 ? 2.6031 4.3145 3.6902 0.8743  -1.1002 -1.3324 1484 GLU A C   
11290 O O   . GLU A 1484 ? 2.6095 4.3009 3.6607 0.9017  -1.1079 -1.3110 1484 GLU A O   
11291 C CB  . GLU A 1484 ? 2.8846 4.5757 3.9320 0.8795  -1.1575 -1.3522 1484 GLU A CB  
11292 C CG  . GLU A 1484 ? 3.0677 4.7400 4.0930 0.8637  -1.1739 -1.3680 1484 GLU A CG  
11293 C CD  . GLU A 1484 ? 3.1638 4.7681 4.1010 0.8691  -1.1691 -1.3471 1484 GLU A CD  
11294 O OE1 . GLU A 1484 ? 3.1296 4.7004 4.0231 0.8823  -1.1497 -1.3199 1484 GLU A OE1 
11295 O OE2 . GLU A 1484 ? 3.2591 4.8438 4.1713 0.8600  -1.1847 -1.3581 1484 GLU A OE2 
11296 N N   . VAL A 1485 ? 1.9655 3.7191 3.1162 0.8564  -1.0808 -1.3462 1485 VAL A N   
11297 C CA  . VAL A 1485 ? 1.8365 3.6108 3.0141 0.8666  -1.0627 -1.3353 1485 VAL A CA  
11298 C C   . VAL A 1485 ? 1.8161 3.6545 3.0695 0.8744  -1.0838 -1.3563 1485 VAL A C   
11299 O O   . VAL A 1485 ? 1.8246 3.7015 3.1320 0.8547  -1.0891 -1.3824 1485 VAL A O   
11300 C CB  . VAL A 1485 ? 1.9859 3.7554 3.1740 0.8398  -1.0184 -1.3319 1485 VAL A CB  
11301 C CG1 . VAL A 1485 ? 1.9512 3.6560 3.0617 0.8389  -0.9952 -1.3047 1485 VAL A CG1 
11302 C CG2 . VAL A 1485 ? 2.0188 3.8145 3.2516 0.8069  -1.0129 -1.3593 1485 VAL A CG2 
11303 N N   . GLY A 1486 ? 1.9169 3.7666 3.1745 0.9030  -1.0958 -1.3446 1486 GLY A N   
11304 C CA  . GLY A 1486 ? 1.9210 3.8282 3.2446 0.9157  -1.1203 -1.3625 1486 GLY A CA  
11305 C C   . GLY A 1486 ? 1.8407 3.7999 3.2406 0.8953  -1.1003 -1.3818 1486 GLY A C   
11306 O O   . GLY A 1486 ? 1.8623 3.8246 3.2778 0.8652  -1.0792 -1.3936 1486 GLY A O   
11307 N N   . PHE A 1487 ? 2.1797 4.1805 3.6282 0.9115  -1.1071 -1.3857 1487 PHE A N   
11308 C CA  . PHE A 1487 ? 2.1215 4.1673 3.6366 0.8944  -1.0828 -1.3995 1487 PHE A CA  
11309 C C   . PHE A 1487 ? 1.9978 4.0072 3.4774 0.8807  -1.0400 -1.3797 1487 PHE A C   
11310 O O   . PHE A 1487 ? 1.9390 3.9192 3.3785 0.8994  -1.0311 -1.3550 1487 PHE A O   
11311 C CB  . PHE A 1487 ? 2.1510 4.2380 3.7120 0.9183  -1.0942 -1.4009 1487 PHE A CB  
11312 C CG  . PHE A 1487 ? 2.2479 4.3246 3.7815 0.9526  -1.1311 -1.3910 1487 PHE A CG  
11313 C CD1 . PHE A 1487 ? 2.3112 4.4360 3.8978 0.9687  -1.1632 -1.4081 1487 PHE A CD1 
11314 C CD2 . PHE A 1487 ? 2.2676 4.2872 3.7232 0.9689  -1.1335 -1.3643 1487 PHE A CD2 
11315 C CE1 . PHE A 1487 ? 2.3763 4.4915 3.9377 1.0002  -1.1973 -1.3987 1487 PHE A CE1 
11316 C CE2 . PHE A 1487 ? 2.3330 4.3432 3.7634 1.0000  -1.1670 -1.3549 1487 PHE A CE2 
11317 C CZ  . PHE A 1487 ? 2.3860 4.4436 3.8689 1.0156  -1.1992 -1.3720 1487 PHE A CZ  
11318 N N   . LEU A 1488 ? 2.0684 4.0781 3.5608 0.8482  -1.0136 -1.3896 1488 LEU A N   
11319 C CA  . LEU A 1488 ? 1.9754 3.9496 3.4333 0.8342  -0.9724 -1.3707 1488 LEU A CA  
11320 C C   . LEU A 1488 ? 1.9090 3.9186 3.4194 0.8238  -0.9422 -1.3748 1488 LEU A C   
11321 O O   . LEU A 1488 ? 1.9281 3.9897 3.5073 0.8103  -0.9434 -1.3993 1488 LEU A O   
11322 C CB  . LEU A 1488 ? 1.9814 3.9210 3.4056 0.8060  -0.9571 -1.3725 1488 LEU A CB  
11323 C CG  . LEU A 1488 ? 1.9817 3.9486 3.4528 0.7704  -0.9413 -1.3965 1488 LEU A CG  
11324 C CD1 . LEU A 1488 ? 1.9112 3.9132 3.4354 0.7552  -0.9090 -1.4020 1488 LEU A CD1 
11325 C CD2 . LEU A 1488 ? 1.9898 3.9049 3.4047 0.7500  -0.9250 -1.3883 1488 LEU A CD2 
11326 N N   . SER A 1489 ? 1.2180 3.1997 2.6959 0.8301  -0.9154 -1.3509 1489 SER A N   
11327 C CA  . SER A 1489 ? 1.0982 3.1060 2.6170 0.8186  -0.8827 -1.3523 1489 SER A CA  
11328 C C   . SER A 1489 ? 1.0367 3.0240 2.5433 0.7850  -0.8469 -1.3520 1489 SER A C   
11329 O O   . SER A 1489 ? 1.0486 2.9821 2.4906 0.7819  -0.8333 -1.3316 1489 SER A O   
11330 C CB  . SER A 1489 ? 0.9839 2.9728 2.4750 0.8424  -0.8727 -1.3271 1489 SER A CB  
11331 O OG  . SER A 1489 ? 0.9317 2.8649 2.3579 0.8361  -0.8466 -1.3023 1489 SER A OG  
11332 N N   . PRO A 1490 ? 1.2849 3.3151 2.8538 0.7601  -0.8312 -1.3740 1490 PRO A N   
11333 C CA  . PRO A 1490 ? 1.2443 3.2625 2.8112 0.7251  -0.8034 -1.3801 1490 PRO A CA  
11334 C C   . PRO A 1490 ? 1.2152 3.1788 2.7200 0.7194  -0.7707 -1.3531 1490 PRO A C   
11335 O O   . PRO A 1490 ? 1.1438 3.0868 2.6177 0.7409  -0.7660 -1.3312 1490 PRO A O   
11336 C CB  . PRO A 1490 ? 1.2050 3.2802 2.8494 0.7075  -0.7853 -1.4006 1490 PRO A CB  
11337 C CG  . PRO A 1490 ? 1.2372 3.3601 2.9313 0.7306  -0.8130 -1.4129 1490 PRO A CG  
11338 C CD  . PRO A 1490 ? 1.2366 3.3276 2.8798 0.7650  -0.8332 -1.3907 1490 PRO A CD  
11339 N N   . ALA A 1491 ? 1.8521 3.7915 3.3381 0.6909  -0.7493 -1.3543 1491 ALA A N   
11340 C CA  . ALA A 1491 ? 1.8092 3.7023 3.2452 0.6813  -0.7142 -1.3309 1491 ALA A CA  
11341 C C   . ALA A 1491 ? 1.7969 3.7204 3.2803 0.6596  -0.6795 -1.3382 1491 ALA A C   
11342 O O   . ALA A 1491 ? 1.7614 3.7379 3.3083 0.6622  -0.6836 -1.3546 1491 ALA A O   
11343 C CB  . ALA A 1491 ? 1.8202 3.6660 3.2046 0.6637  -0.7094 -1.3262 1491 ALA A CB  
11344 N N   . THR A 1492 ? 1.1074 2.9979 2.5605 0.6382  -0.6454 -1.3263 1492 THR A N   
11345 C CA  . THR A 1492 ? 1.0379 2.9497 2.5250 0.6218  -0.6104 -1.3272 1492 THR A CA  
11346 C C   . THR A 1492 ? 1.0712 2.9597 2.5439 0.5878  -0.5793 -1.3272 1492 THR A C   
11347 O O   . THR A 1492 ? 1.0713 2.9061 2.4815 0.5850  -0.5647 -1.3060 1492 THR A O   
11348 C CB  . THR A 1492 ? 0.9148 2.8067 2.3719 0.6434  -0.5970 -1.3016 1492 THR A CB  
11349 O OG1 . THR A 1492 ? 0.8616 2.6906 2.2401 0.6516  -0.5935 -1.2750 1492 THR A OG1 
11350 C CG2 . THR A 1492 ? 0.8626 2.7853 2.3450 0.6752  -0.6262 -1.3046 1492 THR A CG2 
11351 N N   . PHE A 1493 ? 1.2511 3.1798 2.7816 0.5618  -0.5696 -1.3510 1493 PHE A N   
11352 C CA  . PHE A 1493 ? 1.2164 3.1250 2.7363 0.5287  -0.5383 -1.3509 1493 PHE A CA  
11353 C C   . PHE A 1493 ? 1.1900 3.1068 2.7243 0.5202  -0.5018 -1.3420 1493 PHE A C   
11354 O O   . PHE A 1493 ? 1.1745 3.1433 2.7716 0.5170  -0.4969 -1.3577 1493 PHE A O   
11355 C CB  . PHE A 1493 ? 1.1877 3.1330 2.7608 0.5022  -0.5436 -1.3802 1493 PHE A CB  
11356 C CG  . PHE A 1493 ? 1.1103 3.0453 2.6863 0.4663  -0.5080 -1.3825 1493 PHE A CG  
11357 C CD1 . PHE A 1493 ? 1.0649 2.9407 2.5756 0.4572  -0.4862 -1.3608 1493 PHE A CD1 
11358 C CD2 . PHE A 1493 ? 1.1036 3.0884 2.7479 0.4416  -0.4965 -1.4064 1493 PHE A CD2 
11359 C CE1 . PHE A 1493 ? 1.0606 2.9264 2.5739 0.4240  -0.4537 -1.3628 1493 PHE A CE1 
11360 C CE2 . PHE A 1493 ? 1.0841 3.0597 2.7315 0.4081  -0.4640 -1.4086 1493 PHE A CE2 
11361 C CZ  . PHE A 1493 ? 1.0707 2.9863 2.6521 0.3993  -0.4426 -1.3867 1493 PHE A CZ  
11362 N N   . THR A 1494 ? 0.8408 2.7068 2.3171 0.5167  -0.4764 -1.3170 1494 THR A N   
11363 C CA  . THR A 1494 ? 0.7698 2.6357 2.2507 0.5067  -0.4387 -1.3058 1494 THR A CA  
11364 C C   . THR A 1494 ? 0.9035 2.7416 2.3653 0.4725  -0.4045 -1.3021 1494 THR A C   
11365 O O   . THR A 1494 ? 0.8502 2.6499 2.2713 0.4622  -0.4077 -1.2982 1494 THR A O   
11366 C CB  . THR A 1494 ? 0.7462 2.5871 2.1867 0.5364  -0.4369 -1.2788 1494 THR A CB  
11367 O OG1 . THR A 1494 ? 0.7083 2.5467 2.1503 0.5259  -0.4004 -1.2676 1494 THR A OG1 
11368 C CG2 . THR A 1494 ? 0.7785 2.5590 2.1416 0.5518  -0.4483 -1.2553 1494 THR A CG2 
11369 N N   . VAL A 1495 ? 0.9951 2.8551 2.4897 0.4543  -0.3727 -1.3052 1495 VAL A N   
11370 C CA  . VAL A 1495 ? 1.0658 2.9033 2.5470 0.4216  -0.3385 -1.3019 1495 VAL A CA  
11371 C C   . VAL A 1495 ? 1.0465 2.8834 2.5293 0.4143  -0.3009 -1.2886 1495 VAL A C   
11372 O O   . VAL A 1495 ? 1.0795 2.9645 2.6196 0.4088  -0.2900 -1.3023 1495 VAL A O   
11373 C CB  . VAL A 1495 ? 0.9153 2.7881 2.4497 0.3916  -0.3377 -1.3303 1495 VAL A CB  
11374 C CG1 . VAL A 1495 ? 1.0134 2.9507 2.6245 0.3853  -0.3297 -1.3502 1495 VAL A CG1 
11375 C CG2 . VAL A 1495 ? 0.9350 2.7722 2.4412 0.3598  -0.3083 -1.3244 1495 VAL A CG2 
11376 N N   . TYR A 1496 ? 1.3372 3.1195 2.7566 0.4138  -0.2812 -1.2621 1496 TYR A N   
11377 C CA  . TYR A 1496 ? 1.2672 3.0404 2.6778 0.4072  -0.2458 -1.2464 1496 TYR A CA  
11378 C C   . TYR A 1496 ? 1.2738 2.9993 2.6388 0.3827  -0.2156 -1.2313 1496 TYR A C   
11379 O O   . TYR A 1496 ? 1.2958 2.9799 2.6154 0.3795  -0.2232 -1.2238 1496 TYR A O   
11380 C CB  . TYR A 1496 ? 1.1984 2.9575 2.5797 0.4394  -0.2517 -1.2249 1496 TYR A CB  
11381 C CG  . TYR A 1496 ? 1.2231 2.9246 2.5302 0.4593  -0.2646 -1.1996 1496 TYR A CG  
11382 C CD1 . TYR A 1496 ? 1.2427 2.8972 2.5013 0.4453  -0.2587 -1.1903 1496 TYR A CD1 
11383 C CD2 . TYR A 1496 ? 1.1988 2.8929 2.4845 0.4924  -0.2817 -1.1845 1496 TYR A CD2 
11384 C CE1 . TYR A 1496 ? 1.2357 2.8387 2.4274 0.4641  -0.2695 -1.1669 1496 TYR A CE1 
11385 C CE2 . TYR A 1496 ? 1.1982 2.8411 2.4173 0.5108  -0.2927 -1.1609 1496 TYR A CE2 
11386 C CZ  . TYR A 1496 ? 1.2207 2.8188 2.3934 0.4966  -0.2864 -1.1523 1496 TYR A CZ  
11387 O OH  . TYR A 1496 ? 1.2257 2.7737 2.3327 0.5151  -0.2968 -1.1289 1496 TYR A OH  
11388 N N   . GLU A 1497 ? 1.6021 3.3334 2.9790 0.3662  -0.1811 -1.2265 1497 GLU A N   
11389 C CA  . GLU A 1497 ? 1.5808 3.2728 2.9224 0.3404  -0.1487 -1.2135 1497 GLU A CA  
11390 C C   . GLU A 1497 ? 1.5397 3.1742 2.8093 0.3542  -0.1375 -1.1805 1497 GLU A C   
11391 O O   . GLU A 1497 ? 1.4847 3.1208 2.7481 0.3706  -0.1294 -1.1666 1497 GLU A O   
11392 C CB  . GLU A 1497 ? 1.5415 3.2672 2.9293 0.3165  -0.1166 -1.2234 1497 GLU A CB  
11393 C CG  . GLU A 1497 ? 1.5369 3.2370 2.9086 0.2829  -0.0864 -1.2203 1497 GLU A CG  
11394 C CD  . GLU A 1497 ? 1.5206 3.2627 2.9477 0.2586  -0.0589 -1.2351 1497 GLU A CD  
11395 O OE1 . GLU A 1497 ? 1.4711 3.2611 2.9474 0.2691  -0.0631 -1.2470 1497 GLU A OE1 
11396 O OE2 . GLU A 1497 ? 1.5546 3.2817 2.9760 0.2291  -0.0328 -1.2347 1497 GLU A OE2 
11397 N N   . TYR A 1498 ? 1.6039 3.1880 2.8201 0.3469  -0.1360 -1.1680 1498 TYR A N   
11398 C CA  . TYR A 1498 ? 1.6097 3.1387 2.7556 0.3644  -0.1329 -1.1372 1498 TYR A CA  
11399 C C   . TYR A 1498 ? 1.5607 3.0860 2.6993 0.3664  -0.1052 -1.1198 1498 TYR A C   
11400 O O   . TYR A 1498 ? 1.5227 3.0378 2.6382 0.3925  -0.1124 -1.1028 1498 TYR A O   
11401 C CB  . TYR A 1498 ? 1.6649 3.1402 2.7574 0.3486  -0.1236 -1.1257 1498 TYR A CB  
11402 C CG  . TYR A 1498 ? 1.6889 3.1094 2.7096 0.3714  -0.1297 -1.0963 1498 TYR A CG  
11403 C CD1 . TYR A 1498 ? 1.7309 3.1484 2.7356 0.4017  -0.1627 -1.0929 1498 TYR A CD1 
11404 C CD2 . TYR A 1498 ? 1.6847 3.0574 2.6545 0.3628  -0.1028 -1.0720 1498 TYR A CD2 
11405 C CE1 . TYR A 1498 ? 1.7408 3.1100 2.6816 0.4225  -0.1683 -1.0664 1498 TYR A CE1 
11406 C CE2 . TYR A 1498 ? 1.6989 3.0234 2.6050 0.3837  -0.1086 -1.0454 1498 TYR A CE2 
11407 C CZ  . TYR A 1498 ? 1.7309 3.0544 2.6233 0.4135  -0.1413 -1.0428 1498 TYR A CZ  
11408 O OH  . TYR A 1498 ? 1.7567 3.0339 2.5872 0.4347  -0.1475 -1.0165 1498 TYR A OH  
11409 N N   . HIS A 1499 ? 1.2205 2.7548 2.3794 0.3385  -0.0736 -1.1242 1499 HIS A N   
11410 C CA  . HIS A 1499 ? 1.1769 2.7010 2.3214 0.3390  -0.0458 -1.1056 1499 HIS A CA  
11411 C C   . HIS A 1499 ? 1.2032 2.7746 2.3944 0.3528  -0.0473 -1.1138 1499 HIS A C   
11412 O O   . HIS A 1499 ? 1.2209 2.7802 2.3918 0.3647  -0.0345 -1.0953 1499 HIS A O   
11413 C CB  . HIS A 1499 ? 1.1200 2.6243 2.2542 0.3063  -0.0096 -1.1008 1499 HIS A CB  
11414 C CG  . HIS A 1499 ? 1.0864 2.5293 2.1545 0.3017  -0.0043 -1.0804 1499 HIS A CG  
11415 N ND1 . HIS A 1499 ? 1.1155 2.5396 2.1759 0.2727  0.0104  -1.0855 1499 HIS A ND1 
11416 C CD2 . HIS A 1499 ? 1.0851 2.4813 2.0920 0.3230  -0.0129 -1.0552 1499 HIS A CD2 
11417 C CE1 . HIS A 1499 ? 1.1425 2.5106 2.1396 0.2767  0.0112  -1.0643 1499 HIS A CE1 
11418 N NE2 . HIS A 1499 ? 1.1198 2.4705 2.0837 0.3070  -0.0027 -1.0456 1499 HIS A NE2 
11419 N N   . ARG A 1500 ? 1.2521 2.8766 2.5047 0.3529  -0.0641 -1.1409 1500 ARG A N   
11420 C CA  . ARG A 1500 ? 1.2159 2.8861 2.5136 0.3682  -0.0674 -1.1492 1500 ARG A CA  
11421 C C   . ARG A 1500 ? 1.1975 2.9005 2.5254 0.3929  -0.1059 -1.1645 1500 ARG A C   
11422 O O   . ARG A 1500 ? 1.2346 2.9850 2.6207 0.3849  -0.1166 -1.1912 1500 ARG A O   
11423 C CB  . ARG A 1500 ? 1.2423 2.9540 2.5953 0.3425  -0.0405 -1.1666 1500 ARG A CB  
11424 C CG  . ARG A 1500 ? 1.2846 2.9822 2.6348 0.3075  -0.0187 -1.1719 1500 ARG A CG  
11425 C CD  . ARG A 1500 ? 1.3387 3.0913 2.7595 0.2875  -0.0181 -1.2026 1500 ARG A CD  
11426 N NE  . ARG A 1500 ? 1.3520 3.1300 2.8051 0.2697  0.0145  -1.2067 1500 ARG A NE  
11427 C CZ  . ARG A 1500 ? 1.3772 3.2059 2.8946 0.2508  0.0221  -1.2318 1500 ARG A CZ  
11428 N NH1 . ARG A 1500 ? 1.3861 3.2460 2.9432 0.2471  -0.0013 -1.2552 1500 ARG A NH1 
11429 N NH2 . ARG A 1500 ? 1.3916 3.2399 2.9332 0.2356  0.0532  -1.2333 1500 ARG A NH2 
11430 N N   . PRO A 1501 ? 1.0615 2.7387 2.3490 0.4231  -0.1265 -1.1467 1501 PRO A N   
11431 C CA  . PRO A 1501 ? 1.0726 2.7684 2.3720 0.4526  -0.1642 -1.1533 1501 PRO A CA  
11432 C C   . PRO A 1501 ? 1.1086 2.8657 2.4761 0.4602  -0.1706 -1.1738 1501 PRO A C   
11433 O O   . PRO A 1501 ? 1.1044 2.8850 2.4916 0.4843  -0.2002 -1.1816 1501 PRO A O   
11434 C CB  . PRO A 1501 ? 1.0452 2.6982 2.2850 0.4790  -0.1685 -1.1234 1501 PRO A CB  
11435 C CG  . PRO A 1501 ? 1.0418 2.6428 2.2270 0.4619  -0.1408 -1.1018 1501 PRO A CG  
11436 C CD  . PRO A 1501 ? 1.0384 2.6594 2.2582 0.4287  -0.1105 -1.1151 1501 PRO A CD  
11437 N N   . ASP A 1502 ? 1.1438 2.9264 2.5471 0.4389  -0.1416 -1.1825 1502 ASP A N   
11438 C CA  . ASP A 1502 ? 1.1861 3.0248 2.6524 0.4438  -0.1412 -1.2004 1502 ASP A CA  
11439 C C   . ASP A 1502 ? 1.2677 3.1543 2.7945 0.4331  -0.1582 -1.2314 1502 ASP A C   
11440 O O   . ASP A 1502 ? 1.2960 3.2341 2.8803 0.4408  -0.1672 -1.2499 1502 ASP A O   
11441 C CB  . ASP A 1502 ? 1.1775 3.0221 2.6554 0.4231  -0.1013 -1.1970 1502 ASP A CB  
11442 C CG  . ASP A 1502 ? 1.1304 2.9176 2.5405 0.4229  -0.0794 -1.1659 1502 ASP A CG  
11443 O OD1 . ASP A 1502 ? 1.0751 2.8313 2.4409 0.4489  -0.0944 -1.1458 1502 ASP A OD1 
11444 O OD2 . ASP A 1502 ? 1.1404 2.9138 2.5419 0.3967  -0.0475 -1.1615 1502 ASP A OD2 
11445 N N   . LYS A 1503 ? 1.2516 3.1208 2.7652 0.4152  -0.1627 -1.2369 1503 LYS A N   
11446 C CA  . LYS A 1503 ? 1.3448 3.2568 2.9150 0.3979  -0.1734 -1.2663 1503 LYS A CA  
11447 C C   . LYS A 1503 ? 1.1870 3.1114 2.7667 0.4169  -0.2159 -1.2784 1503 LYS A C   
11448 O O   . LYS A 1503 ? 1.1572 3.0987 2.7630 0.4017  -0.2282 -1.2979 1503 LYS A O   
11449 C CB  . LYS A 1503 ? 1.4069 3.2977 2.9650 0.3629  -0.1507 -1.2684 1503 LYS A CB  
11450 C CG  . LYS A 1503 ? 1.4449 3.3427 3.0178 0.3380  -0.1095 -1.2666 1503 LYS A CG  
11451 C CD  . LYS A 1503 ? 1.4480 3.3591 3.0279 0.3553  -0.0974 -1.2568 1503 LYS A CD  
11452 C CE  . LYS A 1503 ? 1.5008 3.4662 3.1476 0.3384  -0.0763 -1.2766 1503 LYS A CE  
11453 N NZ  . LYS A 1503 ? 1.5135 3.4948 3.1705 0.3565  -0.0663 -1.2693 1503 LYS A NZ  
11454 N N   . GLN A 1504 ? 1.2763 3.1927 2.8354 0.4500  -0.2383 -1.2668 1504 GLN A N   
11455 C CA  . GLN A 1504 ? 1.1955 3.1144 2.7510 0.4714  -0.2787 -1.2729 1504 GLN A CA  
11456 C C   . GLN A 1504 ? 1.2268 3.2071 2.8535 0.4751  -0.3015 -1.3019 1504 GLN A C   
11457 O O   . GLN A 1504 ? 0.9744 2.9847 2.6289 0.4977  -0.3140 -1.3052 1504 GLN A O   
11458 C CB  . GLN A 1504 ? 1.1686 3.0598 2.6799 0.5060  -0.2945 -1.2503 1504 GLN A CB  
11459 C CG  . GLN A 1504 ? 1.7151 3.5456 3.1528 0.5130  -0.3041 -1.2290 1504 GLN A CG  
11460 C CD  . GLN A 1504 ? 1.4183 3.2146 2.8055 0.5428  -0.3101 -1.2018 1504 GLN A CD  
11461 O OE1 . GLN A 1504 ? 1.3467 3.0906 2.6699 0.5490  -0.3121 -1.1804 1504 GLN A OE1 
11462 N NE2 . GLN A 1504 ? 1.4347 3.2605 2.8505 0.5614  -0.3128 -1.2024 1504 GLN A NE2 
11463 N N   . CYS A 1505 ? 0.8678 2.8658 2.5229 0.4533  -0.3076 -1.3225 1505 CYS A N   
11464 C CA  . CYS A 1505 ? 0.9233 2.9715 2.6355 0.4594  -0.3383 -1.3488 1505 CYS A CA  
11465 C C   . CYS A 1505 ? 0.9735 2.9994 2.6530 0.4795  -0.3765 -1.3462 1505 CYS A C   
11466 O O   . CYS A 1505 ? 0.9468 2.9463 2.6000 0.4660  -0.3831 -1.3477 1505 CYS A O   
11467 C CB  . CYS A 1505 ? 0.9616 3.0458 2.7273 0.4267  -0.3285 -1.3744 1505 CYS A CB  
11468 S SG  . CYS A 1505 ? 1.6499 3.8093 3.5013 0.4351  -0.3597 -1.4074 1505 CYS A SG  
11469 N N   . THR A 1506 ? 0.9013 2.9393 2.5840 0.5117  -0.4014 -1.3428 1506 THR A N   
11470 C CA  . THR A 1506 ? 0.9656 2.9822 2.6144 0.5359  -0.4378 -1.3370 1506 THR A CA  
11471 C C   . THR A 1506 ? 1.0226 3.0944 2.7337 0.5442  -0.4692 -1.3638 1506 THR A C   
11472 O O   . THR A 1506 ? 1.0003 3.1231 2.7722 0.5445  -0.4645 -1.3788 1506 THR A O   
11473 C CB  . THR A 1506 ? 0.9817 2.9702 2.5868 0.5678  -0.4427 -1.3116 1506 THR A CB  
11474 O OG1 . THR A 1506 ? 0.9866 2.9351 2.5477 0.5588  -0.4086 -1.2887 1506 THR A OG1 
11475 C CG2 . THR A 1506 ? 1.0073 2.9619 2.5635 0.5909  -0.4755 -1.3006 1506 THR A CG2 
11476 N N   . MET A 1507 ? 1.3930 3.4541 3.0883 0.5509  -0.5010 -1.3695 1507 MET A N   
11477 C CA  . MET A 1507 ? 1.4011 3.5108 3.1511 0.5577  -0.5341 -1.3949 1507 MET A CA  
11478 C C   . MET A 1507 ? 1.4079 3.4972 3.1253 0.5776  -0.5737 -1.3933 1507 MET A C   
11479 O O   . MET A 1507 ? 1.3838 3.4293 3.0510 0.5697  -0.5767 -1.3853 1507 MET A O   
11480 C CB  . MET A 1507 ? 1.4076 3.5513 3.2090 0.5248  -0.5249 -1.4202 1507 MET A CB  
11481 C CG  . MET A 1507 ? 1.4660 3.6556 3.3193 0.5297  -0.5598 -1.4459 1507 MET A CG  
11482 S SD  . MET A 1507 ? 1.3713 3.5778 3.2585 0.4891  -0.5521 -1.4698 1507 MET A SD  
11483 C CE  . MET A 1507 ? 1.3007 3.4366 3.1122 0.4688  -0.5179 -1.4454 1507 MET A CE  
11484 N N   . PHE A 1508 ? 1.5329 3.6555 3.2809 0.6033  -0.6039 -1.4018 1508 PHE A N   
11485 C CA  . PHE A 1508 ? 1.6206 3.7331 3.3476 0.6239  -0.6444 -1.4033 1508 PHE A CA  
11486 C C   . PHE A 1508 ? 1.8108 3.9395 3.5624 0.6033  -0.6607 -1.4266 1508 PHE A C   
11487 O O   . PHE A 1508 ? 1.8874 4.0504 3.6897 0.5768  -0.6449 -1.4457 1508 PHE A O   
11488 C CB  . PHE A 1508 ? 1.5510 3.7038 3.3166 0.6536  -0.6711 -1.4100 1508 PHE A CB  
11489 C CG  . PHE A 1508 ? 1.4139 3.5403 3.1396 0.6823  -0.6699 -1.3849 1508 PHE A CG  
11490 C CD1 . PHE A 1508 ? 1.4261 3.4940 3.0759 0.6961  -0.6766 -1.3604 1508 PHE A CD1 
11491 C CD2 . PHE A 1508 ? 1.3408 3.5010 3.1051 0.6960  -0.6631 -1.3858 1508 PHE A CD2 
11492 C CE1 . PHE A 1508 ? 1.3842 3.4277 2.9973 0.7222  -0.6759 -1.3368 1508 PHE A CE1 
11493 C CE2 . PHE A 1508 ? 1.3072 3.4422 3.0344 0.7222  -0.6627 -1.3626 1508 PHE A CE2 
11494 C CZ  . PHE A 1508 ? 1.3231 3.3999 2.9749 0.7351  -0.6692 -1.3379 1508 PHE A CZ  
11495 N N   . TYR A 1509 ? 1.1898 3.2946 2.9063 0.6154  -0.6922 -1.4252 1509 TYR A N   
11496 C CA  . TYR A 1509 ? 1.2308 3.3560 2.9744 0.6019  -0.7163 -1.4491 1509 TYR A CA  
11497 C C   . TYR A 1509 ? 1.3284 3.4245 3.0260 0.6252  -0.7537 -1.4424 1509 TYR A C   
11498 O O   . TYR A 1509 ? 1.3329 3.3836 2.9689 0.6451  -0.7545 -1.4177 1509 TYR A O   
11499 C CB  . TYR A 1509 ? 1.1465 3.2521 2.8800 0.5659  -0.6928 -1.4543 1509 TYR A CB  
11500 C CG  . TYR A 1509 ? 1.1067 3.1445 2.7585 0.5667  -0.6912 -1.4336 1509 TYR A CG  
11501 C CD1 . TYR A 1509 ? 1.1430 3.1589 2.7765 0.5439  -0.6927 -1.4416 1509 TYR A CD1 
11502 C CD2 . TYR A 1509 ? 1.0770 3.0724 2.6693 0.5914  -0.6892 -1.4057 1509 TYR A CD2 
11503 C CE1 . TYR A 1509 ? 1.1679 3.1201 2.7246 0.5457  -0.6914 -1.4225 1509 TYR A CE1 
11504 C CE2 . TYR A 1509 ? 1.0935 3.0264 2.6097 0.5935  -0.6880 -1.3860 1509 TYR A CE2 
11505 C CZ  . TYR A 1509 ? 1.1435 3.0543 2.6414 0.5707  -0.6889 -1.3944 1509 TYR A CZ  
11506 O OH  . TYR A 1509 ? 1.1576 3.0059 2.5799 0.5727  -0.6873 -1.3754 1509 TYR A OH  
11507 N N   . SER A 1510 ? 1.8682 3.9903 3.5953 0.6229  -0.7846 -1.4642 1510 SER A N   
11508 C CA  . SER A 1510 ? 1.9172 4.0129 3.6018 0.6440  -0.8212 -1.4595 1510 SER A CA  
11509 C C   . SER A 1510 ? 2.0165 4.1004 3.6916 0.6242  -0.8358 -1.4743 1510 SER A C   
11510 O O   . SER A 1510 ? 2.0187 4.1400 3.7474 0.6004  -0.8352 -1.4983 1510 SER A O   
11511 C CB  . SER A 1510 ? 1.9349 4.0700 3.6549 0.6736  -0.8556 -1.4674 1510 SER A CB  
11512 O OG  . SER A 1510 ? 1.9614 4.0622 3.6281 0.6982  -0.8866 -1.4558 1510 SER A OG  
11513 N N   . THR A 1511 ? 1.2320 3.2634 2.8377 0.6351  -0.8496 -1.4593 1511 THR A N   
11514 C CA  . THR A 1511 ? 1.3111 3.3138 2.8877 0.6161  -0.8566 -1.4665 1511 THR A CA  
11515 C C   . THR A 1511 ? 1.5073 3.5368 3.1088 0.6244  -0.8994 -1.4871 1511 THR A C   
11516 O O   . THR A 1511 ? 1.5965 3.5975 3.1630 0.6192  -0.9162 -1.4905 1511 THR A O   
11517 C CB  . THR A 1511 ? 1.2469 3.1783 2.7339 0.6256  -0.8505 -1.4393 1511 THR A CB  
11518 O OG1 . THR A 1511 ? 1.2766 3.1752 2.7356 0.5980  -0.8373 -1.4426 1511 THR A OG1 
11519 C CG2 . THR A 1511 ? 1.2754 3.1894 2.7249 0.6578  -0.8888 -1.4318 1511 THR A CG2 
11520 N N   . SER A 1512 ? 1.9019 3.9866 3.5644 0.6374  -0.9173 -1.5012 1512 SER A N   
11521 C CA  . SER A 1512 ? 2.0991 4.2114 3.7869 0.6477  -0.9595 -1.5201 1512 SER A CA  
11522 C C   . SER A 1512 ? 2.2197 4.4024 3.9919 0.6509  -0.9694 -1.5406 1512 SER A C   
11523 O O   . SER A 1512 ? 2.1629 4.3667 3.9593 0.6624  -0.9548 -1.5335 1512 SER A O   
11524 C CB  . SER A 1512 ? 2.1219 4.2019 3.7545 0.6821  -0.9885 -1.5031 1512 SER A CB  
11525 O OG  . SER A 1512 ? 2.0703 4.1683 3.7167 0.7085  -0.9893 -1.4919 1512 SER A OG  
11526 N N   . ASN A 1513 ? 2.3230 4.5418 4.1397 0.6411  -0.9948 -1.5662 1513 ASN A N   
11527 C CA  . ASN A 1513 ? 2.4583 4.7468 4.3590 0.6424  -1.0064 -1.5882 1513 ASN A CA  
11528 C C   . ASN A 1513 ? 2.5798 4.8860 4.4867 0.6775  -1.0458 -1.5882 1513 ASN A C   
11529 O O   . ASN A 1513 ? 2.6124 4.9753 4.5857 0.6854  -1.0591 -1.6040 1513 ASN A O   
11530 C CB  . ASN A 1513 ? 2.5607 4.8805 4.5089 0.6122  -1.0131 -1.6160 1513 ASN A CB  
11531 C CG  . ASN A 1513 ? 2.5848 4.8681 4.5028 0.5794  -0.9824 -1.6131 1513 ASN A CG  
11532 O OD1 . ASN A 1513 ? 2.5131 4.7751 4.4121 0.5706  -0.9454 -1.5978 1513 ASN A OD1 
11533 N ND2 . ASN A 1513 ? 2.6815 4.9565 4.5939 0.5611  -0.9980 -1.6275 1513 ASN A ND2 
11534 N N   . ILE A 1514 ? 2.5143 4.7712 4.3510 0.6989  -1.0637 -1.5700 1514 ILE A N   
11535 C CA  . ILE A 1514 ? 2.5885 4.8547 4.4213 0.7323  -1.1034 -1.5685 1514 ILE A CA  
11536 C C   . ILE A 1514 ? 2.5445 4.8428 4.4114 0.7563  -1.1009 -1.5621 1514 ILE A C   
11537 O O   . ILE A 1514 ? 2.4764 4.7498 4.3136 0.7649  -1.0755 -1.5406 1514 ILE A O   
11538 C CB  . ILE A 1514 ? 2.7916 4.9938 4.5362 0.7508  -1.1189 -1.5469 1514 ILE A CB  
11539 C CG1 . ILE A 1514 ? 2.8130 4.9761 4.5166 0.7262  -1.1149 -1.5502 1514 ILE A CG1 
11540 C CG2 . ILE A 1514 ? 2.8767 5.0918 4.6215 0.7810  -1.1643 -1.5502 1514 ILE A CG2 
11541 C CD1 . ILE A 1514 ? 2.8319 4.9329 4.4497 0.7434  -1.1300 -1.5304 1514 ILE A CD1 
11542 N N   . SER B 1    ? 4.6743 5.1972 5.3402 0.7477  -0.4940 -0.2454 129  SER X N   
11543 C CA  . SER B 1    ? 4.6654 5.1965 5.3291 0.7105  -0.4882 -0.2237 129  SER X CA  
11544 C C   . SER B 1    ? 4.6894 5.2352 5.3210 0.6916  -0.4661 -0.2132 129  SER X C   
11545 O O   . SER B 1    ? 4.6656 5.2485 5.2995 0.6774  -0.4584 -0.1984 129  SER X O   
11546 C CB  . SER B 1    ? 2.2178 2.7863 2.9141 0.7108  -0.4977 -0.2138 129  SER X CB  
11547 O OG  . SER B 1    ? 2.2180 2.8335 2.9184 0.7286  -0.4899 -0.2140 129  SER X OG  
11548 N N   . SER B 2    ? 3.5934 4.1097 4.1950 0.6916  -0.4564 -0.2207 130  SER X N   
11549 C CA  . SER B 2    ? 3.6288 4.1513 4.1961 0.6735  -0.4357 -0.2117 130  SER X CA  
11550 C C   . SER B 2    ? 3.6448 4.1628 4.2024 0.6319  -0.4293 -0.1906 130  SER X C   
11551 O O   . SER B 2    ? 3.6308 4.1211 4.1968 0.6157  -0.4388 -0.1865 130  SER X O   
11552 C CB  . SER B 2    ? 3.6425 4.1276 4.1808 0.6819  -0.4288 -0.2245 130  SER X CB  
11553 O OG  . SER B 2    ? 3.6420 4.1330 4.1462 0.6681  -0.4089 -0.2172 130  SER X OG  
11554 N N   . GLU B 3    ? 3.4214 3.9669 3.9609 0.6144  -0.4134 -0.1771 131  GLU X N   
11555 C CA  . GLU B 3    ? 3.4052 3.9487 3.9322 0.5740  -0.4062 -0.1565 131  GLU X CA  
11556 C C   . GLU B 3    ? 3.4291 3.9618 3.9135 0.5550  -0.3858 -0.1501 131  GLU X C   
11557 O O   . GLU B 3    ? 3.4475 4.0138 3.9212 0.5439  -0.3738 -0.1388 131  GLU X O   
11558 C CB  . GLU B 3    ? 3.3718 3.9647 3.9218 0.5650  -0.4083 -0.1418 131  GLU X CB  
11559 C CG  . GLU B 3    ? 3.3249 3.9252 3.9153 0.5725  -0.4283 -0.1420 131  GLU X CG  
11560 C CD  . GLU B 3    ? 3.2912 3.9386 3.9016 0.5583  -0.4294 -0.1246 131  GLU X CD  
11561 O OE1 . GLU B 3    ? 3.2926 3.9731 3.8890 0.5485  -0.4154 -0.1145 131  GLU X OE1 
11562 O OE2 . GLU B 3    ? 3.2632 3.9147 3.9035 0.5567  -0.4447 -0.1206 131  GLU X OE2 
11563 N N   . THR B 4    ? 3.4467 3.9330 3.9068 0.5511  -0.3819 -0.1568 132  THR X N   
11564 C CA  . THR B 4    ? 3.4623 3.9331 3.8801 0.5342  -0.3630 -0.1514 132  THR X CA  
11565 C C   . THR B 4    ? 3.4236 3.8823 3.8237 0.4918  -0.3556 -0.1316 132  THR X C   
11566 O O   . THR B 4    ? 3.3945 3.8321 3.8066 0.4763  -0.3651 -0.1268 132  THR X O   
11567 C CB  . THR B 4    ? 3.4985 3.9253 3.8955 0.5492  -0.3608 -0.1669 132  THR X CB  
11568 O OG1 . THR B 4    ? 3.5145 3.9532 3.9262 0.5878  -0.3675 -0.1853 132  THR X OG1 
11569 C CG2 . THR B 4    ? 3.5233 3.9351 3.8761 0.5334  -0.3411 -0.1613 132  THR X CG2 
11570 N N   . ASN B 5    ? 3.6354 4.1075 4.0065 0.4729  -0.3388 -0.1199 133  ASN X N   
11571 C CA  . ASN B 5    ? 3.5812 4.0400 3.9297 0.4320  -0.3301 -0.1012 133  ASN X CA  
11572 C C   . ASN B 5    ? 3.5657 3.9778 3.8713 0.4189  -0.3169 -0.1022 133  ASN X C   
11573 O O   . ASN B 5    ? 3.6318 4.0481 3.9056 0.4097  -0.3011 -0.0968 133  ASN X O   
11574 C CB  . ASN B 5    ? 3.5671 4.0720 3.9119 0.4148  -0.3210 -0.0851 133  ASN X CB  
11575 C CG  . ASN B 5    ? 3.5520 4.0777 3.8756 0.4291  -0.3072 -0.0893 133  ASN X CG  
11576 O OD1 . ASN B 5    ? 3.5333 4.0623 3.8642 0.4627  -0.3097 -0.1059 133  ASN X OD1 
11577 N ND2 . ASN B 5    ? 3.5644 4.1041 3.8611 0.4030  -0.2927 -0.0740 133  ASN X ND2 
11578 N N   . THR B 6    ? 3.6533 4.0214 3.9582 0.4184  -0.3233 -0.1088 134  THR X N   
11579 C CA  . THR B 6    ? 3.6106 3.9319 3.8771 0.4086  -0.3120 -0.1108 134  THR X CA  
11580 C C   . THR B 6    ? 3.5665 3.8716 3.8018 0.3679  -0.2998 -0.0923 134  THR X C   
11581 O O   . THR B 6    ? 3.5113 3.8333 3.7585 0.3448  -0.3036 -0.0784 134  THR X O   
11582 C CB  . THR B 6    ? 3.8885 4.1690 4.1652 0.4194  -0.3229 -0.1226 134  THR X CB  
11583 O OG1 . THR B 6    ? 3.9303 4.1656 4.1701 0.4016  -0.3116 -0.1197 134  THR X OG1 
11584 C CG2 . THR B 6    ? 3.8357 4.1190 4.1451 0.4088  -0.3385 -0.1172 134  THR X CG2 
11585 N N   . HIS B 7    ? 5.1857 5.4567 5.3805 0.3594  -0.2856 -0.0924 135  HIS X N   
11586 C CA  . HIS B 7    ? 5.2037 5.4532 5.3638 0.3215  -0.2732 -0.0761 135  HIS X CA  
11587 C C   . HIS B 7    ? 5.1972 5.3904 5.3352 0.3128  -0.2705 -0.0792 135  HIS X C   
11588 O O   . HIS B 7    ? 5.2234 5.3908 5.3443 0.3308  -0.2654 -0.0909 135  HIS X O   
11589 C CB  . HIS B 7    ? 3.2534 3.5153 3.3785 0.3140  -0.2558 -0.0697 135  HIS X CB  
11590 C CG  . HIS B 7    ? 3.2338 3.5525 3.3779 0.3225  -0.2567 -0.0661 135  HIS X CG  
11591 N ND1 . HIS B 7    ? 3.2145 3.5659 3.3678 0.2979  -0.2573 -0.0496 135  HIS X ND1 
11592 C CD2 . HIS B 7    ? 3.2319 3.5815 3.3873 0.3528  -0.2568 -0.0768 135  HIS X CD2 
11593 C CE1 . HIS B 7    ? 3.2008 3.6016 3.3710 0.3132  -0.2576 -0.0500 135  HIS X CE1 
11594 N NE2 . HIS B 7    ? 3.2113 3.6116 3.3829 0.3468  -0.2572 -0.0667 135  HIS X NE2 
11595 N N   . LEU B 8    ? 2.5096 2.6844 2.6481 0.2854  -0.2737 -0.0686 136  LEU X N   
11596 C CA  . LEU B 8    ? 2.4815 2.6035 2.5972 0.2736  -0.2699 -0.0696 136  LEU X CA  
11597 C C   . LEU B 8    ? 2.5088 2.6078 2.5843 0.2351  -0.2557 -0.0531 136  LEU X C   
11598 O O   . LEU B 8    ? 2.4874 2.6097 2.5635 0.2106  -0.2546 -0.0384 136  LEU X O   
11599 C CB  . LEU B 8    ? 2.3692 2.4778 2.5177 0.2779  -0.2864 -0.0747 136  LEU X CB  
11600 C CG  . LEU B 8    ? 2.2457 2.3831 2.4336 0.2705  -0.3018 -0.0683 136  LEU X CG  
11601 C CD1 . LEU B 8    ? 2.1811 2.2920 2.3911 0.2749  -0.3154 -0.0748 136  LEU X CD1 
11602 C CD2 . LEU B 8    ? 2.2190 2.4049 2.4392 0.2962  -0.3104 -0.0744 136  LEU X CD2 
11603 N N   . PHE B 9    ? 3.5363 3.5892 3.5766 0.2305  -0.2450 -0.0557 137  PHE X N   
11604 C CA  . PHE B 9    ? 3.5773 3.6010 3.5744 0.1960  -0.2305 -0.0417 137  PHE X CA  
11605 C C   . PHE B 9    ? 3.5202 3.5081 3.5161 0.1757  -0.2345 -0.0370 137  PHE X C   
11606 O O   . PHE B 9    ? 3.4773 3.4396 3.4837 0.1910  -0.2406 -0.0478 137  PHE X O   
11607 C CB  . PHE B 9    ? 3.6917 3.6856 3.6453 0.2022  -0.2143 -0.0460 137  PHE X CB  
11608 C CG  . PHE B 9    ? 3.7781 3.8020 3.7333 0.2280  -0.2110 -0.0540 137  PHE X CG  
11609 C CD1 . PHE B 9    ? 3.7373 3.8131 3.7165 0.2319  -0.2159 -0.0504 137  PHE X CD1 
11610 C CD2 . PHE B 9    ? 3.8345 3.8347 3.7662 0.2482  -0.2026 -0.0647 137  PHE X CD2 
11611 C CE1 . PHE B 9    ? 3.7601 3.8632 3.7398 0.2557  -0.2124 -0.0578 137  PHE X CE1 
11612 C CE2 . PHE B 9    ? 3.8625 3.8893 3.7942 0.2715  -0.1994 -0.0720 137  PHE X CE2 
11613 C CZ  . PHE B 9    ? 3.8181 3.8962 3.7735 0.2752  -0.2041 -0.0687 137  PHE X CZ  
11614 N N   . VAL B 10   ? 3.0426 3.0296 3.0254 0.1405  -0.2311 -0.0207 138  VAL X N   
11615 C CA  . VAL B 10   ? 2.9647 2.9170 2.9409 0.1174  -0.2329 -0.0147 138  VAL X CA  
11616 C C   . VAL B 10   ? 3.0458 2.9548 2.9676 0.0931  -0.2149 -0.0068 138  VAL X C   
11617 O O   . VAL B 10   ? 3.1009 3.0172 2.9936 0.0773  -0.2034 0.0025  138  VAL X O   
11618 C CB  . VAL B 10   ? 2.8574 2.8368 2.8584 0.0939  -0.2433 -0.0017 138  VAL X CB  
11619 C CG1 . VAL B 10   ? 2.8236 2.7664 2.7996 0.0586  -0.2386 0.0102  138  VAL X CG1 
11620 C CG2 . VAL B 10   ? 2.7570 2.7611 2.8110 0.1166  -0.2630 -0.0106 138  VAL X CG2 
11621 N N   . ASN B 11   ? 2.9572 2.8208 2.8650 0.0904  -0.2127 -0.0107 139  ASN X N   
11622 C CA  . ASN B 11   ? 2.9998 2.8171 2.8561 0.0673  -0.1962 -0.0036 139  ASN X CA  
11623 C C   . ASN B 11   ? 2.9462 2.7270 2.7985 0.0485  -0.1985 0.0001  139  ASN X C   
11624 O O   . ASN B 11   ? 2.9191 2.6795 2.7850 0.0662  -0.2037 -0.0106 139  ASN X O   
11625 C CB  . ASN B 11   ? 3.0632 2.8546 2.8932 0.0902  -0.1852 -0.0148 139  ASN X CB  
11626 C CG  . ASN B 11   ? 3.1194 2.9474 2.9630 0.1171  -0.1865 -0.0226 139  ASN X CG  
11627 O OD1 . ASN B 11   ? 3.1528 3.0038 2.9824 0.1068  -0.1799 -0.0146 139  ASN X OD1 
11628 N ND2 . ASN B 11   ? 3.1307 2.9645 3.0015 0.1515  -0.1951 -0.0383 139  ASN X ND2 
11629 N N   . LYS B 12   ? 3.3732 3.1465 3.2069 0.0123  -0.1947 0.0154  140  LYS X N   
11630 C CA  . LYS B 12   ? 3.3297 3.0670 3.1554 -0.0074 -0.1954 0.0196  140  LYS X CA  
11631 C C   . LYS B 12   ? 3.3861 3.0689 3.1594 -0.0157 -0.1778 0.0195  140  LYS X C   
11632 O O   . LYS B 12   ? 3.4434 3.1160 3.1769 -0.0294 -0.1640 0.0263  140  LYS X O   
11633 C CB  . LYS B 12   ? 3.2927 3.0451 3.1225 -0.0427 -0.2002 0.0358  140  LYS X CB  
11634 C CG  . LYS B 12   ? 3.2282 3.0369 3.1067 -0.0361 -0.2164 0.0378  140  LYS X CG  
11635 C CD  . LYS B 12   ? 3.1513 2.9713 3.0401 -0.0688 -0.2240 0.0526  140  LYS X CD  
11636 C CE  . LYS B 12   ? 3.0663 2.8770 2.9871 -0.0649 -0.2379 0.0484  140  LYS X CE  
11637 N NZ  . LYS B 12   ? 2.9998 2.8354 2.9435 -0.0890 -0.2494 0.0612  140  LYS X NZ  
11638 N N   . VAL B 13   ? 3.3849 3.0329 3.1577 -0.0068 -0.1781 0.0119  141  VAL X N   
11639 C CA  . VAL B 13   ? 3.4788 3.0740 3.2026 -0.0137 -0.1614 0.0118  141  VAL X CA  
11640 C C   . VAL B 13   ? 3.4913 3.0512 3.1919 -0.0465 -0.1570 0.0222  141  VAL X C   
11641 O O   . VAL B 13   ? 3.4153 2.9535 3.1265 -0.0423 -0.1609 0.0174  141  VAL X O   
11642 C CB  . VAL B 13   ? 3.5128 3.0881 3.2427 0.0203  -0.1608 -0.0040 141  VAL X CB  
11643 C CG1 . VAL B 13   ? 3.6047 3.1305 3.2812 0.0162  -0.1420 -0.0038 141  VAL X CG1 
11644 C CG2 . VAL B 13   ? 3.5191 3.1308 3.2768 0.0534  -0.1676 -0.0151 141  VAL X CG2 
11645 N N   . TYR B 14   ? 5.8884 5.4434 5.5572 -0.0794 -0.1488 0.0364  142  TYR X N   
11646 C CA  . TYR B 14   ? 5.8881 5.4062 5.5274 -0.1123 -0.1427 0.0467  142  TYR X CA  
11647 C C   . TYR B 14   ? 5.9700 5.4335 5.5570 -0.1134 -0.1245 0.0446  142  TYR X C   
11648 O O   . TYR B 14   ? 6.0201 5.4541 5.5618 -0.1425 -0.1124 0.0552  142  TYR X O   
11649 C CB  . TYR B 14   ? 3.7302 3.2644 3.3552 -0.1484 -0.1418 0.0633  142  TYR X CB  
11650 C CG  . TYR B 14   ? 3.6701 3.2559 3.3451 -0.1514 -0.1597 0.0675  142  TYR X CG  
11651 C CD1 . TYR B 14   ? 3.6013 3.1869 3.2978 -0.1672 -0.1702 0.0723  142  TYR X CD1 
11652 C CD2 . TYR B 14   ? 3.6832 3.3180 3.3838 -0.1380 -0.1660 0.0668  142  TYR X CD2 
11653 C CE1 . TYR B 14   ? 3.5466 3.1790 3.2889 -0.1693 -0.1869 0.0765  142  TYR X CE1 
11654 C CE2 . TYR B 14   ? 3.6301 3.3122 3.3766 -0.1392 -0.1822 0.0707  142  TYR X CE2 
11655 C CZ  . TYR B 14   ? 3.5618 3.2422 3.3290 -0.1548 -0.1928 0.0757  142  TYR X CZ  
11656 O OH  . TYR B 14   ? 3.5104 3.2371 3.3228 -0.1556 -0.2092 0.0799  142  TYR X OH  
11657 N N   . GLY B 15   ? 3.0094 2.4593 2.6024 -0.0815 -0.1229 0.0308  143  GLY X N   
11658 C CA  . GLY B 15   ? 3.0900 2.4918 2.6359 -0.0767 -0.1058 0.0275  143  GLY X CA  
11659 C C   . GLY B 15   ? 3.2317 2.6371 2.7462 -0.0763 -0.0949 0.0302  143  GLY X C   
11660 O O   . GLY B 15   ? 3.2792 2.7271 2.8195 -0.0619 -0.1020 0.0275  143  GLY X O   
11661 N N   . GLY B 16   ? 2.2825 1.6428 1.7408 -0.0918 -0.0777 0.0356  144  GLY X N   
11662 C CA  . GLY B 16   ? 2.4130 1.7709 1.8338 -0.0988 -0.0662 0.0409  144  GLY X CA  
11663 C C   . GLY B 16   ? 2.3965 1.7958 1.8274 -0.1210 -0.0719 0.0523  144  GLY X C   
11664 O O   . GLY B 16   ? 2.4613 1.8496 1.8519 -0.1459 -0.0617 0.0632  144  GLY X O   
11665 N N   . ASN B 17   ? 5.4050 4.8518 4.8902 -0.1123 -0.0888 0.0500  145  ASN X N   
11666 C CA  . ASN B 17   ? 5.3457 4.8419 4.8525 -0.1252 -0.0969 0.0586  145  ASN X CA  
11667 C C   . ASN B 17   ? 5.2359 4.7804 4.7987 -0.0918 -0.1115 0.0475  145  ASN X C   
11668 O O   . ASN B 17   ? 5.1756 4.7184 4.7693 -0.0696 -0.1202 0.0367  145  ASN X O   
11669 C CB  . ASN B 17   ? 3.0498 2.5519 2.5663 -0.1576 -0.1044 0.0705  145  ASN X CB  
11670 C CG  . ASN B 17   ? 3.0687 2.5173 2.5345 -0.1884 -0.0918 0.0792  145  ASN X CG  
11671 O OD1 . ASN B 17   ? 3.1388 2.5571 2.5545 -0.1999 -0.0768 0.0836  145  ASN X OD1 
11672 N ND2 . ASN B 17   ? 3.0085 2.4436 2.4855 -0.2020 -0.0979 0.0817  145  ASN X ND2 
11673 N N   . LEU B 18   ? 2.6068 2.1940 2.1816 -0.0883 -0.1141 0.0502  146  LEU X N   
11674 C CA  . LEU B 18   ? 2.5086 2.1467 2.1380 -0.0615 -0.1292 0.0419  146  LEU X CA  
11675 C C   . LEU B 18   ? 2.4748 2.1627 2.1188 -0.0749 -0.1340 0.0521  146  LEU X C   
11676 O O   . LEU B 18   ? 2.5211 2.2164 2.1381 -0.0814 -0.1242 0.0574  146  LEU X O   
11677 C CB  . LEU B 18   ? 2.5556 2.1949 2.1896 -0.0235 -0.1269 0.0270  146  LEU X CB  
11678 C CG  . LEU B 18   ? 2.5100 2.2055 2.1916 0.0026  -0.1397 0.0198  146  LEU X CG  
11679 C CD1 . LEU B 18   ? 2.5784 2.3046 2.2460 -0.0022 -0.1332 0.0263  146  LEU X CD1 
11680 C CD2 . LEU B 18   ? 2.3977 2.1258 2.1287 -0.0003 -0.1573 0.0214  146  LEU X CD2 
11681 N N   . ASP B 19   ? 2.6817 2.4043 2.3689 -0.0789 -0.1492 0.0552  147  ASP X N   
11682 C CA  . ASP B 19   ? 2.6522 2.4297 2.3644 -0.0851 -0.1565 0.0630  147  ASP X CA  
11683 C C   . ASP B 19   ? 2.6781 2.4963 2.4398 -0.0460 -0.1690 0.0494  147  ASP X C   
11684 O O   . ASP B 19   ? 2.6135 2.4379 2.4135 -0.0314 -0.1824 0.0419  147  ASP X O   
11685 C CB  . ASP B 19   ? 2.4960 2.2859 2.2223 -0.1162 -0.1652 0.0765  147  ASP X CB  
11686 C CG  . ASP B 19   ? 2.4493 2.1991 2.1246 -0.1566 -0.1530 0.0904  147  ASP X CG  
11687 O OD1 . ASP B 19   ? 2.5069 2.2316 2.1358 -0.1654 -0.1377 0.0935  147  ASP X OD1 
11688 O OD2 . ASP B 19   ? 2.3630 2.1057 2.0441 -0.1800 -0.1590 0.0986  147  ASP X OD2 
11689 N N   . ALA B 20   ? 2.4552 2.2991 2.2140 -0.0296 -0.1643 0.0460  148  ALA X N   
11690 C CA  . ALA B 20   ? 2.4694 2.3492 2.2684 0.0091  -0.1739 0.0321  148  ALA X CA  
11691 C C   . ALA B 20   ? 2.4869 2.4272 2.3145 0.0106  -0.1807 0.0377  148  ALA X C   
11692 O O   . ALA B 20   ? 2.5694 2.5255 2.3735 -0.0039 -0.1713 0.0472  148  ALA X O   
11693 C CB  . ALA B 20   ? 2.5533 2.4123 2.3286 0.0345  -0.1634 0.0202  148  ALA X CB  
11694 N N   . SER B 21   ? 3.0281 3.0020 2.9064 0.0287  -0.1971 0.0318  149  SER X N   
11695 C CA  . SER B 21   ? 2.9900 3.0225 2.9007 0.0334  -0.2051 0.0362  149  SER X CA  
11696 C C   . SER B 21   ? 2.9169 2.9726 2.8550 0.0757  -0.2106 0.0194  149  SER X C   
11697 O O   . SER B 21   ? 2.8624 2.8977 2.8158 0.0990  -0.2171 0.0056  149  SER X O   
11698 C CB  . SER B 21   ? 2.9343 2.9874 2.8836 0.0226  -0.2208 0.0423  149  SER X CB  
11699 O OG  . SER B 21   ? 2.9362 2.9595 2.8619 -0.0141 -0.2174 0.0552  149  SER X OG  
11700 N N   . ILE B 22   ? 3.5145 3.6123 3.4582 0.0853  -0.2080 0.0206  150  ILE X N   
11701 C CA  . ILE B 22   ? 3.4078 3.5354 3.3827 0.1253  -0.2151 0.0054  150  ILE X CA  
11702 C C   . ILE B 22   ? 3.3115 3.4919 3.3346 0.1317  -0.2299 0.0081  150  ILE X C   
11703 O O   . ILE B 22   ? 3.3014 3.5096 3.3260 0.1069  -0.2296 0.0234  150  ILE X O   
11704 C CB  . ILE B 22   ? 3.2627 3.4024 3.2123 0.1371  -0.2021 0.0027  150  ILE X CB  
11705 C CG1 . ILE B 22   ? 3.1768 3.3781 3.1511 0.1426  -0.2056 0.0076  150  ILE X CG1 
11706 C CG2 . ILE B 22   ? 3.4001 3.5045 3.2944 0.1085  -0.1846 0.0132  150  ILE X CG2 
11707 C CD1 . ILE B 22   ? 2.9862 3.2183 3.0009 0.1835  -0.2167 -0.0084 150  ILE X CD1 
11708 N N   . ASP B 23   ? 3.1008 3.2949 3.1628 0.1648  -0.2432 -0.0065 151  ASP X N   
11709 C CA  . ASP B 23   ? 3.0268 3.2637 3.1360 0.1712  -0.2589 -0.0046 151  ASP X CA  
11710 C C   . ASP B 23   ? 3.0968 3.3518 3.2427 0.2136  -0.2707 -0.0228 151  ASP X C   
11711 O O   . ASP B 23   ? 3.1095 3.3491 3.2434 0.2375  -0.2657 -0.0363 151  ASP X O   
11712 C CB  . ASP B 23   ? 2.8833 3.1008 3.0037 0.1482  -0.2681 0.0033  151  ASP X CB  
11713 C CG  . ASP B 23   ? 2.7513 3.0135 2.9113 0.1429  -0.2815 0.0118  151  ASP X CG  
11714 O OD1 . ASP B 23   ? 2.7624 3.0715 2.9346 0.1493  -0.2808 0.0157  151  ASP X OD1 
11715 O OD2 . ASP B 23   ? 2.6453 2.8955 2.8236 0.1322  -0.2926 0.0149  151  ASP X OD2 
11716 N N   . SER B 24   ? 2.6285 2.9150 2.8183 0.2226  -0.2866 -0.0232 152  SER X N   
11717 C CA  . SER B 24   ? 2.7322 3.0421 2.9584 0.2622  -0.2984 -0.0393 152  SER X CA  
11718 C C   . SER B 24   ? 2.8093 3.1133 3.0744 0.2726  -0.3174 -0.0456 152  SER X C   
11719 O O   . SER B 24   ? 2.7463 3.0436 3.0190 0.2482  -0.3233 -0.0346 152  SER X O   
11720 C CB  . SER B 24   ? 2.7236 3.0915 2.9680 0.2720  -0.2986 -0.0353 152  SER X CB  
11721 O OG  . SER B 24   ? 2.7048 3.1031 2.9755 0.2549  -0.3079 -0.0222 152  SER X OG  
11722 N N   . PHE B 25   ? 3.2562 3.5625 3.5447 0.3087  -0.3269 -0.0632 153  PHE X N   
11723 C CA  . PHE B 25   ? 3.3319 3.6383 3.6605 0.3235  -0.3462 -0.0706 153  PHE X CA  
11724 C C   . PHE B 25   ? 3.3962 3.7479 3.7585 0.3543  -0.3554 -0.0787 153  PHE X C   
11725 O O   . PHE B 25   ? 3.4117 3.7914 3.7649 0.3648  -0.3462 -0.0796 153  PHE X O   
11726 C CB  . PHE B 25   ? 3.4159 3.6770 3.7408 0.3387  -0.3504 -0.0854 153  PHE X CB  
11727 C CG  . PHE B 25   ? 3.4477 3.7067 3.8126 0.3551  -0.3706 -0.0941 153  PHE X CG  
11728 C CD1 . PHE B 25   ? 3.4102 3.6467 3.7835 0.3341  -0.3787 -0.0871 153  PHE X CD1 
11729 C CD2 . PHE B 25   ? 3.5048 3.7823 3.8972 0.3913  -0.3814 -0.1095 153  PHE X CD2 
11730 C CE1 . PHE B 25   ? 3.3882 3.6219 3.7973 0.3485  -0.3974 -0.0948 153  PHE X CE1 
11731 C CE2 . PHE B 25   ? 3.4805 3.7540 3.9080 0.4057  -0.4002 -0.1173 153  PHE X CE2 
11732 C CZ  . PHE B 25   ? 3.4189 3.6705 3.8547 0.3841  -0.4083 -0.1098 153  PHE X CZ  
11733 N N   . SER B 26   ? 5.3386 5.6972 5.7392 0.3689  -0.3734 -0.0846 154  SER X N   
11734 C CA  . SER B 26   ? 5.3475 5.7460 5.7807 0.3999  -0.3831 -0.0933 154  SER X CA  
11735 C C   . SER B 26   ? 5.3598 5.7411 5.8202 0.4288  -0.3997 -0.1105 154  SER X C   
11736 O O   . SER B 26   ? 5.3092 5.6828 5.7944 0.4238  -0.4142 -0.1086 154  SER X O   
11737 C CB  . SER B 26   ? 2.8122 3.2537 3.2693 0.3862  -0.3887 -0.0783 154  SER X CB  
11738 O OG  . SER B 26   ? 2.7941 3.2529 3.2249 0.3599  -0.3731 -0.0627 154  SER X OG  
11739 N N   . ILE B 27   ? 2.6929 3.0669 3.1468 0.4582  -0.3975 -0.1272 155  ILE X N   
11740 C CA  . ILE B 27   ? 2.7253 3.0840 3.2023 0.4881  -0.4126 -0.1451 155  ILE X CA  
11741 C C   . ILE B 27   ? 2.7528 3.1522 3.2640 0.5155  -0.4240 -0.1515 155  ILE X C   
11742 O O   . ILE B 27   ? 2.7622 3.1912 3.2693 0.5327  -0.4167 -0.1555 155  ILE X O   
11743 C CB  . ILE B 27   ? 2.7239 3.0563 3.1775 0.5077  -0.4053 -0.1603 155  ILE X CB  
11744 C CG1 . ILE B 27   ? 2.7299 3.0256 3.1450 0.4813  -0.3908 -0.1530 155  ILE X CG1 
11745 C CG2 . ILE B 27   ? 2.7305 3.0424 3.2065 0.5345  -0.4218 -0.1777 155  ILE X CG2 
11746 C CD1 . ILE B 27   ? 2.7603 3.0324 3.1486 0.4983  -0.3814 -0.1657 155  ILE X CD1 
11747 N N   . ASN B 28   ? 5.8388 6.2388 6.3833 0.5200  -0.4419 -0.1526 156  ASN X N   
11748 C CA  . ASN B 28   ? 5.8848 6.3220 6.4590 0.5291  -0.4393 -0.1405 156  ASN X CA  
11749 C C   . ASN B 28   ? 5.9101 6.3344 6.4923 0.5342  -0.4166 -0.1234 156  ASN X C   
11750 O O   . ASN B 28   ? 5.8918 6.3351 6.5014 0.5426  -0.4195 -0.1154 156  ASN X O   
11751 C CB  . ASN B 28   ? 3.0567 3.5051 3.6614 0.5231  -0.4657 -0.1425 156  ASN X CB  
11752 C CG  . ASN B 28   ? 3.0610 3.5065 3.6454 0.4819  -0.4548 -0.1223 156  ASN X CG  
11753 O OD1 . ASN B 28   ? 3.0785 3.5277 3.6323 0.4689  -0.4374 -0.1163 156  ASN X OD1 
11754 N ND2 . ASN B 28   ? 3.0121 3.4496 3.6121 0.4608  -0.4651 -0.1117 156  ASN X ND2 
11755 N N   . LYS B 29   ? 3.1130 3.5131 3.6891 0.5921  -0.4617 -0.1898 157  LYS X N   
11756 C CA  . LYS B 29   ? 3.1776 3.5647 3.7678 0.6265  -0.4741 -0.2102 157  LYS X CA  
11757 C C   . LYS B 29   ? 3.2463 3.6212 3.8085 0.6435  -0.4623 -0.2228 157  LYS X C   
11758 O O   . LYS B 29   ? 3.2622 3.6355 3.7937 0.6273  -0.4448 -0.2154 157  LYS X O   
11759 C CB  . LYS B 29   ? 3.1824 3.5313 3.7868 0.6217  -0.4898 -0.2141 157  LYS X CB  
11760 C CG  . LYS B 29   ? 3.1618 3.5213 3.7973 0.6096  -0.5044 -0.2039 157  LYS X CG  
11761 C CD  . LYS B 29   ? 3.1567 3.4762 3.8016 0.5992  -0.5178 -0.2054 157  LYS X CD  
11762 C CE  . LYS B 29   ? 3.1476 3.4512 3.8123 0.6305  -0.5351 -0.2244 157  LYS X CE  
11763 N NZ  . LYS B 29   ? 3.1425 3.4088 3.8167 0.6192  -0.5482 -0.2251 157  LYS X NZ  
11764 N N   . GLU B 30   ? 4.0223 4.3891 4.5948 0.6761  -0.4722 -0.2417 158  GLU X N   
11765 C CA  . GLU B 30   ? 4.0839 4.4377 4.6323 0.6950  -0.4636 -0.2553 158  GLU X CA  
11766 C C   . GLU B 30   ? 4.0848 4.3906 4.6176 0.6880  -0.4648 -0.2608 158  GLU X C   
11767 O O   . GLU B 30   ? 4.1163 4.4065 4.6208 0.6909  -0.4531 -0.2657 158  GLU X O   
11768 C CB  . GLU B 30   ? 4.1531 4.5232 4.7186 0.7342  -0.4733 -0.2733 158  GLU X CB  
11769 C CG  . GLU B 30   ? 4.2060 4.5672 4.8055 0.7485  -0.4957 -0.2815 158  GLU X CG  
11770 C CD  . GLU B 30   ? 4.2569 4.6237 4.8673 0.7877  -0.5052 -0.3016 158  GLU X CD  
11771 O OE1 . GLU B 30   ? 4.2684 4.6500 4.8614 0.8040  -0.4940 -0.3087 158  GLU X OE1 
11772 O OE2 . GLU B 30   ? 4.2834 4.6389 4.9187 0.8018  -0.5238 -0.3104 158  GLU X OE2 
11773 N N   . GLU B 31   ? 4.9922 5.2757 5.5440 0.6788  -0.4792 -0.2595 159  GLU X N   
11774 C CA  . GLU B 31   ? 4.9642 5.2039 5.5044 0.6685  -0.4811 -0.2622 159  GLU X CA  
11775 C C   . GLU B 31   ? 4.8813 5.1085 5.4355 0.6408  -0.4887 -0.2490 159  GLU X C   
11776 O O   . GLU B 31   ? 4.8522 5.0931 5.4364 0.6437  -0.5032 -0.2474 159  GLU X O   
11777 C CB  . GLU B 31   ? 4.9996 5.2196 5.5508 0.6980  -0.4951 -0.2820 159  GLU X CB  
11778 C CG  . GLU B 31   ? 4.9964 5.2183 5.5845 0.7101  -0.5173 -0.2876 159  GLU X CG  
11779 C CD  . GLU B 31   ? 5.0230 5.2791 5.6295 0.7380  -0.5236 -0.2959 159  GLU X CD  
11780 O OE1 . GLU B 31   ? 5.0493 5.3249 5.6404 0.7526  -0.5120 -0.3008 159  GLU X OE1 
11781 O OE2 . GLU B 31   ? 5.0224 5.2855 5.6588 0.7457  -0.5402 -0.2976 159  GLU X OE2 
11782 N N   . VAL B 32   ? 5.2674 5.4685 5.7996 0.6139  -0.4790 -0.2394 160  VAL X N   
11783 C CA  . VAL B 32   ? 5.1764 5.3657 5.7189 0.5856  -0.4848 -0.2261 160  VAL X CA  
11784 C C   . VAL B 32   ? 5.1659 5.3123 5.7004 0.5758  -0.4877 -0.2286 160  VAL X C   
11785 O O   . VAL B 32   ? 5.2018 5.3265 5.7107 0.5784  -0.4774 -0.2339 160  VAL X O   
11786 C CB  . VAL B 32   ? 2.3516 2.5556 2.8767 0.5542  -0.4697 -0.2067 160  VAL X CB  
11787 C CG1 . VAL B 32   ? 2.2916 2.4823 2.8272 0.5250  -0.4764 -0.1933 160  VAL X CG1 
11788 C CG2 . VAL B 32   ? 2.3388 2.5884 2.8739 0.5622  -0.4671 -0.2025 160  VAL X CG2 
11789 N N   . SER B 33   ? 3.8926 4.0276 4.4497 0.5647  -0.5021 -0.2246 161  SER X N   
11790 C CA  . SER B 33   ? 3.8659 3.9627 4.4176 0.5518  -0.5052 -0.2247 161  SER X CA  
11791 C C   . SER B 33   ? 3.8434 3.9252 4.3635 0.5210  -0.4870 -0.2107 161  SER X C   
11792 O O   . SER B 33   ? 3.8132 3.9113 4.3285 0.4989  -0.4799 -0.1959 161  SER X O   
11793 C CB  . SER B 33   ? 3.8004 3.8915 4.3834 0.5445  -0.5243 -0.2216 161  SER X CB  
11794 O OG  . SER B 33   ? 3.7459 3.8015 4.3235 0.5302  -0.5266 -0.2206 161  SER X OG  
11795 N N   . LEU B 34   ? 3.2185 3.2687 3.7167 0.5198  -0.4797 -0.2153 162  LEU X N   
11796 C CA  . LEU B 34   ? 3.2005 3.2305 3.6668 0.4921  -0.4627 -0.2034 162  LEU X CA  
11797 C C   . LEU B 34   ? 3.1175 3.1397 3.5929 0.4618  -0.4673 -0.1890 162  LEU X C   
11798 O O   . LEU B 34   ? 3.0792 3.0914 3.5306 0.4344  -0.4538 -0.1758 162  LEU X O   
11799 C CB  . LEU B 34   ? 3.2463 3.2425 3.6935 0.4997  -0.4576 -0.2125 162  LEU X CB  
11800 C CG  . LEU B 34   ? 3.2560 3.2269 3.6652 0.4783  -0.4383 -0.2038 162  LEU X CG  
11801 C CD1 . LEU B 34   ? 3.2798 3.2683 3.6627 0.4706  -0.4209 -0.1961 162  LEU X CD1 
11802 C CD2 . LEU B 34   ? 3.3089 3.2525 3.7047 0.4945  -0.4359 -0.2157 162  LEU X CD2 
11803 N N   . LYS B 35   ? 4.2869 4.3128 4.7962 0.4668  -0.4866 -0.1915 163  LYS X N   
11804 C CA  . LYS B 35   ? 4.2125 4.2360 4.7349 0.4401  -0.4933 -0.1780 163  LYS X CA  
11805 C C   . LYS B 35   ? 4.2022 4.2578 4.7246 0.4256  -0.4877 -0.1647 163  LYS X C   
11806 O O   . LYS B 35   ? 4.1948 4.2459 4.6988 0.3961  -0.4769 -0.1500 163  LYS X O   
11807 C CB  . LYS B 35   ? 4.1709 4.1936 4.7307 0.4518  -0.5163 -0.1846 163  LYS X CB  
11808 C CG  . LYS B 35   ? 4.0757 4.0998 4.6522 0.4259  -0.5251 -0.1705 163  LYS X CG  
11809 C CD  . LYS B 35   ? 4.0412 4.0721 4.6565 0.4409  -0.5484 -0.1768 163  LYS X CD  
11810 C CE  . LYS B 35   ? 3.9575 3.9904 4.5894 0.4152  -0.5574 -0.1623 163  LYS X CE  
11811 N NZ  . LYS B 35   ? 3.9186 3.9180 4.5390 0.3913  -0.5551 -0.1563 163  LYS X NZ  
11812 N N   . GLU B 36   ? 3.8276 3.9159 4.3704 0.4466  -0.4950 -0.1699 164  GLU X N   
11813 C CA  . GLU B 36   ? 3.8204 3.9443 4.3655 0.4365  -0.4900 -0.1581 164  GLU X CA  
11814 C C   . GLU B 36   ? 3.7647 3.8904 4.2720 0.4234  -0.4677 -0.1512 164  GLU X C   
11815 O O   . GLU B 36   ? 3.7069 3.8484 4.2045 0.3995  -0.4593 -0.1360 164  GLU X O   
11816 C CB  . GLU B 36   ? 3.9458 4.1035 4.5170 0.4667  -0.5003 -0.1675 164  GLU X CB  
11817 C CG  . GLU B 36   ? 4.0099 4.1670 4.6185 0.4801  -0.5231 -0.1738 164  GLU X CG  
11818 C CD  . GLU B 36   ? 4.1238 4.3129 4.7560 0.5111  -0.5324 -0.1835 164  GLU X CD  
11819 O OE1 . GLU B 36   ? 4.1939 4.4019 4.8127 0.5262  -0.5215 -0.1886 164  GLU X OE1 
11820 O OE2 . GLU B 36   ? 4.1389 4.3338 4.8024 0.5205  -0.5507 -0.1861 164  GLU X OE2 
11821 N N   . LEU B 37   ? 2.9615 3.0705 3.4472 0.4389  -0.4585 -0.1623 165  LEU X N   
11822 C CA  . LEU B 37   ? 2.9428 3.0475 3.3899 0.4285  -0.4374 -0.1574 165  LEU X CA  
11823 C C   . LEU B 37   ? 2.9095 2.9882 3.3332 0.3929  -0.4277 -0.1430 165  LEU X C   
11824 O O   . LEU B 37   ? 2.9087 2.9936 3.3077 0.3712  -0.4133 -0.1306 165  LEU X O   
11825 C CB  . LEU B 37   ? 2.9441 3.0290 3.3745 0.4520  -0.4320 -0.1726 165  LEU X CB  
11826 C CG  . LEU B 37   ? 2.9344 3.0234 3.3293 0.4514  -0.4121 -0.1710 165  LEU X CG  
11827 C CD1 . LEU B 37   ? 2.9405 3.0731 3.3454 0.4636  -0.4113 -0.1705 165  LEU X CD1 
11828 C CD2 . LEU B 37   ? 2.9579 3.0232 3.3356 0.4728  -0.4073 -0.1853 165  LEU X CD2 
11829 N N   . ASP B 38   ? 3.7075 3.7566 4.1390 0.3870  -0.4361 -0.1450 166  ASP X N   
11830 C CA  . ASP B 38   ? 3.6885 3.7086 4.0982 0.3556  -0.4278 -0.1333 166  ASP X CA  
11831 C C   . ASP B 38   ? 3.6427 3.6755 4.0657 0.3283  -0.4335 -0.1176 166  ASP X C   
11832 O O   . ASP B 38   ? 3.6178 3.6397 4.0165 0.2985  -0.4220 -0.1040 166  ASP X O   
11833 C CB  . ASP B 38   ? 3.6992 3.6834 4.1115 0.3610  -0.4339 -0.1418 166  ASP X CB  
11834 C CG  . ASP B 38   ? 3.7346 3.6848 4.1082 0.3458  -0.4166 -0.1383 166  ASP X CG  
11835 O OD1 . ASP B 38   ? 3.7689 3.7218 4.1129 0.3299  -0.4004 -0.1291 166  ASP X OD1 
11836 O OD2 . ASP B 38   ? 3.7414 3.6623 4.1138 0.3497  -0.4193 -0.1446 166  ASP X OD2 
11837 N N   . PHE B 39   ? 4.3320 4.3870 4.7929 0.3382  -0.4515 -0.1192 167  PHE X N   
11838 C CA  . PHE B 39   ? 4.3154 4.3848 4.7919 0.3138  -0.4586 -0.1043 167  PHE X CA  
11839 C C   . PHE B 39   ? 4.2774 4.3785 4.7423 0.3003  -0.4480 -0.0921 167  PHE X C   
11840 O O   . PHE B 39   ? 4.2586 4.3659 4.7210 0.2715  -0.4468 -0.0764 167  PHE X O   
11841 C CB  . PHE B 39   ? 4.3545 4.4399 4.8746 0.3296  -0.4810 -0.1094 167  PHE X CB  
11842 C CG  . PHE B 39   ? 4.3507 4.4495 4.8880 0.3048  -0.4895 -0.0939 167  PHE X CG  
11843 C CD1 . PHE B 39   ? 4.3612 4.4995 4.9102 0.3017  -0.4905 -0.0848 167  PHE X CD1 
11844 C CD2 . PHE B 39   ? 4.3274 4.4002 4.8691 0.2847  -0.4965 -0.0881 167  PHE X CD2 
11845 C CE1 . PHE B 39   ? 4.3237 4.4750 4.8886 0.2789  -0.4986 -0.0702 167  PHE X CE1 
11846 C CE2 . PHE B 39   ? 4.2914 4.3761 4.8481 0.2617  -0.5045 -0.0737 167  PHE X CE2 
11847 C CZ  . PHE B 39   ? 4.2862 4.4100 4.8546 0.2589  -0.5058 -0.0647 167  PHE X CZ  
11848 N N   . LYS B 40   ? 2.9581 3.0800 3.4159 0.3208  -0.4406 -0.0990 168  LYS X N   
11849 C CA  . LYS B 40   ? 2.8838 3.0382 3.3303 0.3097  -0.4301 -0.0880 168  LYS X CA  
11850 C C   . LYS B 40   ? 2.8549 2.9895 3.2563 0.2842  -0.4093 -0.0785 168  LYS X C   
11851 O O   . LYS B 40   ? 2.8199 2.9678 3.2090 0.2571  -0.4021 -0.0627 168  LYS X O   
11852 C CB  . LYS B 40   ? 2.9078 3.0960 3.3671 0.3419  -0.4313 -0.0986 168  LYS X CB  
11853 C CG  . LYS B 40   ? 2.8584 3.0725 3.3619 0.3634  -0.4513 -0.1045 168  LYS X CG  
11854 C CD  . LYS B 40   ? 2.8816 3.1407 3.3967 0.3839  -0.4502 -0.1070 168  LYS X CD  
11855 C CE  . LYS B 40   ? 2.8398 3.1286 3.3970 0.3958  -0.4686 -0.1065 168  LYS X CE  
11856 N NZ  . LYS B 40   ? 2.8799 3.2153 3.4485 0.4139  -0.4666 -0.1072 168  LYS X NZ  
11857 N N   . ILE B 41   ? 2.8321 2.9340 3.2086 0.2925  -0.4001 -0.0879 169  ILE X N   
11858 C CA  . ILE B 41   ? 2.8061 2.8839 3.1376 0.2714  -0.3803 -0.0807 169  ILE X CA  
11859 C C   . ILE B 41   ? 2.7693 2.8270 3.0867 0.2333  -0.3770 -0.0649 169  ILE X C   
11860 O O   . ILE B 41   ? 2.7949 2.8604 3.0900 0.2077  -0.3660 -0.0509 169  ILE X O   
11861 C CB  . ILE B 41   ? 2.7621 2.8049 3.0729 0.2889  -0.3732 -0.0944 169  ILE X CB  
11862 C CG1 . ILE B 41   ? 2.7654 2.8278 3.0860 0.3253  -0.3752 -0.1096 169  ILE X CG1 
11863 C CG2 . ILE B 41   ? 2.7757 2.7904 3.0391 0.2670  -0.3530 -0.0866 169  ILE X CG2 
11864 C CD1 . ILE B 41   ? 2.7710 2.8631 3.0753 0.3262  -0.3631 -0.1051 169  ILE X CD1 
11865 N N   . ARG B 42   ? 3.6695 3.7016 3.9996 0.2291  -0.3867 -0.0670 170  ARG X N   
11866 C CA  . ARG B 42   ? 3.6429 3.6555 3.9621 0.1944  -0.3852 -0.0529 170  ARG X CA  
11867 C C   . ARG B 42   ? 3.5649 3.6106 3.9046 0.1758  -0.3934 -0.0389 170  ARG X C   
11868 O O   . ARG B 42   ? 3.5384 3.5778 3.8587 0.1433  -0.3864 -0.0240 170  ARG X O   
11869 C CB  . ARG B 42   ? 3.6688 3.6488 3.9996 0.1959  -0.3946 -0.0589 170  ARG X CB  
11870 C CG  . ARG B 42   ? 3.7487 3.7449 4.1256 0.2177  -0.4162 -0.0677 170  ARG X CG  
11871 C CD  . ARG B 42   ? 3.7807 3.7443 4.1668 0.2138  -0.4250 -0.0711 170  ARG X CD  
11872 N NE  . ARG B 42   ? 3.8452 3.8182 4.2709 0.2397  -0.4445 -0.0829 170  ARG X NE  
11873 C CZ  . ARG B 42   ? 3.8496 3.7992 4.2897 0.2416  -0.4552 -0.0878 170  ARG X CZ  
11874 N NH1 . ARG B 42   ? 3.8247 3.7412 4.2436 0.2197  -0.4477 -0.0820 170  ARG X NH1 
11875 N NH2 . ARG B 42   ? 3.8682 3.8270 4.3431 0.2652  -0.4733 -0.0985 170  ARG X NH2 
11876 N N   . GLN B 43   ? 2.8684 2.9489 3.2466 0.1964  -0.4083 -0.0436 171  GLN X N   
11877 C CA  . GLN B 43   ? 2.8175 2.9319 3.2192 0.1818  -0.4178 -0.0307 171  GLN X CA  
11878 C C   . GLN B 43   ? 2.8272 2.9593 3.2023 0.1570  -0.4033 -0.0157 171  GLN X C   
11879 O O   . GLN B 43   ? 2.7777 2.9160 3.1510 0.1270  -0.4042 0.0001  171  GLN X O   
11880 C CB  . GLN B 43   ? 2.8046 2.9564 3.2470 0.2131  -0.4328 -0.0395 171  GLN X CB  
11881 C CG  . GLN B 43   ? 2.7364 2.9220 3.2102 0.2029  -0.4462 -0.0279 171  GLN X CG  
11882 C CD  . GLN B 43   ? 2.7244 2.9507 3.2318 0.2343  -0.4569 -0.0358 171  GLN X CD  
11883 O OE1 . GLN B 43   ? 2.7631 3.0114 3.2622 0.2496  -0.4480 -0.0401 171  GLN X OE1 
11884 N NE2 . GLN B 43   ? 2.6714 2.9074 3.2162 0.2440  -0.4760 -0.0376 171  GLN X NE2 
11885 N N   . HIS B 44   ? 5.1460 5.2858 5.4998 0.1693  -0.3901 -0.0206 172  HIS X N   
11886 C CA  . HIS B 44   ? 5.1595 5.3166 5.4858 0.1488  -0.3754 -0.0080 172  HIS X CA  
11887 C C   . HIS B 44   ? 5.1991 5.3174 5.4807 0.1171  -0.3600 0.0013  172  HIS X C   
11888 O O   . HIS B 44   ? 5.1919 5.3158 5.4600 0.0852  -0.3556 0.0175  172  HIS X O   
11889 C CB  . HIS B 44   ? 3.0242 3.2016 3.3430 0.1745  -0.3669 -0.0173 172  HIS X CB  
11890 C CG  . HIS B 44   ? 3.0201 3.2417 3.3790 0.2030  -0.3797 -0.0240 172  HIS X CG  
11891 N ND1 . HIS B 44   ? 3.0487 3.2720 3.4234 0.2400  -0.3853 -0.0420 172  HIS X ND1 
11892 C CD2 . HIS B 44   ? 2.9913 3.2565 3.3768 0.1993  -0.3879 -0.0147 172  HIS X CD2 
11893 C CE1 . HIS B 44   ? 3.0393 3.3046 3.4482 0.2590  -0.3962 -0.0441 172  HIS X CE1 
11894 N NE2 . HIS B 44   ? 3.0039 3.2954 3.4204 0.2354  -0.3979 -0.0277 172  HIS X NE2 
11895 N N   . LEU B 45   ? 2.8289 2.9081 3.0870 0.1262  -0.3517 -0.0090 173  LEU X N   
11896 C CA  . LEU B 45   ? 2.8516 2.8886 3.0686 0.0984  -0.3383 -0.0018 173  LEU X CA  
11897 C C   . LEU B 45   ? 2.8048 2.8339 3.0290 0.0678  -0.3457 0.0114  173  LEU X C   
11898 O O   . LEU B 45   ? 2.8243 2.8391 3.0180 0.0350  -0.3355 0.0250  173  LEU X O   
11899 C CB  . LEU B 45   ? 2.8744 2.8705 3.0789 0.1162  -0.3346 -0.0160 173  LEU X CB  
11900 C CG  . LEU B 45   ? 2.9441 2.9471 3.1450 0.1491  -0.3296 -0.0304 173  LEU X CG  
11901 C CD1 . LEU B 45   ? 2.9647 2.9336 3.1655 0.1706  -0.3313 -0.0454 173  LEU X CD1 
11902 C CD2 . LEU B 45   ? 3.0133 3.0136 3.1720 0.1367  -0.3104 -0.0238 173  LEU X CD2 
11903 N N   . VAL B 46   ? 3.0938 3.1319 3.3582 0.0788  -0.3637 0.0072  174  VAL X N   
11904 C CA  . VAL B 46   ? 3.0160 3.0477 3.2925 0.0534  -0.3732 0.0182  174  VAL X CA  
11905 C C   . VAL B 46   ? 2.9998 3.0687 3.2841 0.0317  -0.3759 0.0345  174  VAL X C   
11906 O O   . VAL B 46   ? 2.9645 3.0255 3.2400 -0.0003 -0.3761 0.0484  174  VAL X O   
11907 C CB  . VAL B 46   ? 3.0515 3.0839 3.3702 0.0731  -0.3928 0.0088  174  VAL X CB  
11908 C CG1 . VAL B 46   ? 2.9988 3.0424 3.3391 0.0500  -0.4056 0.0218  174  VAL X CG1 
11909 C CG2 . VAL B 46   ? 3.0578 3.0459 3.3649 0.0820  -0.3905 -0.0025 174  VAL X CG2 
11910 N N   . LYS B 47   ? 4.8603 4.9710 5.1603 0.0485  -0.3774 0.0331  175  LYS X N   
11911 C CA  . LYS B 47   ? 4.8204 4.9704 5.1305 0.0291  -0.3804 0.0489  175  LYS X CA  
11912 C C   . LYS B 47   ? 4.8317 4.9902 5.1049 0.0110  -0.3628 0.0585  175  LYS X C   
11913 O O   . LYS B 47   ? 4.8235 5.0147 5.1003 -0.0082 -0.3634 0.0730  175  LYS X O   
11914 C CB  . LYS B 47   ? 4.7992 4.9963 5.1542 0.0573  -0.3947 0.0436  175  LYS X CB  
11915 C CG  . LYS B 47   ? 4.7294 4.9277 5.1263 0.0695  -0.4153 0.0389  175  LYS X CG  
11916 C CD  . LYS B 47   ? 1.8992 2.1451 2.3360 0.0921  -0.4281 0.0369  175  LYS X CD  
11917 C CE  . LYS B 47   ? 1.8845 2.1374 2.3598 0.0930  -0.4481 0.0392  175  LYS X CE  
11918 N NZ  . LYS B 47   ? 1.8871 2.1263 2.3580 0.0571  -0.4519 0.0546  175  LYS X NZ  
11919 N N   . ASN B 48   ? 3.3673 3.4985 3.6061 0.0181  -0.3478 0.0506  176  ASN X N   
11920 C CA  . ASN B 48   ? 3.3857 3.5256 3.5895 0.0054  -0.3311 0.0579  176  ASN X CA  
11921 C C   . ASN B 48   ? 3.3692 3.4612 3.5201 -0.0131 -0.3129 0.0595  176  ASN X C   
11922 O O   . ASN B 48   ? 3.3961 3.4877 3.5150 -0.0413 -0.3014 0.0727  176  ASN X O   
11923 C CB  . ASN B 48   ? 3.4318 3.6047 3.6483 0.0385  -0.3296 0.0474  176  ASN X CB  
11924 C CG  . ASN B 48   ? 3.3953 3.6186 3.6599 0.0558  -0.3455 0.0473  176  ASN X CG  
11925 O OD1 . ASN B 48   ? 3.4075 3.6723 3.6777 0.0498  -0.3439 0.0568  176  ASN X OD1 
11926 N ND2 . ASN B 48   ? 3.3502 3.5700 3.6497 0.0773  -0.3610 0.0367  176  ASN X ND2 
11927 N N   . TYR B 49   ? 2.5483 2.6008 2.6892 0.0029  -0.3101 0.0462  177  TYR X N   
11928 C CA  . TYR B 49   ? 2.5844 2.5921 2.6752 -0.0102 -0.2923 0.0465  177  TYR X CA  
11929 C C   . TYR B 49   ? 2.6074 2.5694 2.6831 -0.0300 -0.2917 0.0491  177  TYR X C   
11930 O O   . TYR B 49   ? 2.6647 2.5841 2.7079 -0.0300 -0.2803 0.0438  177  TYR X O   
11931 C CB  . TYR B 49   ? 2.5591 2.5556 2.6401 0.0224  -0.2850 0.0303  177  TYR X CB  
11932 C CG  . TYR B 49   ? 2.5462 2.5807 2.6258 0.0340  -0.2795 0.0305  177  TYR X CG  
11933 C CD1 . TYR B 49   ? 2.5045 2.5810 2.6245 0.0640  -0.2910 0.0219  177  TYR X CD1 
11934 C CD2 . TYR B 49   ? 2.5782 2.6073 2.6158 0.0139  -0.2631 0.0400  177  TYR X CD2 
11935 C CE1 . TYR B 49   ? 2.5250 2.6383 2.6439 0.0745  -0.2857 0.0225  177  TYR X CE1 
11936 C CE2 . TYR B 49   ? 2.6059 2.6717 2.6423 0.0233  -0.2580 0.0410  177  TYR X CE2 
11937 C CZ  . TYR B 49   ? 2.5701 2.6786 2.6476 0.0538  -0.2691 0.0322  177  TYR X CZ  
11938 O OH  . TYR B 49   ? 2.5937 2.7395 2.6699 0.0634  -0.2636 0.0332  177  TYR X OH  
11939 N N   . GLY B 50   ? 3.2389 3.2105 3.3383 -0.0466 -0.3042 0.0575  178  GLY X N   
11940 C CA  . GLY B 50   ? 3.2567 3.1885 3.3445 -0.0668 -0.3047 0.0610  178  GLY X CA  
11941 C C   . GLY B 50   ? 3.3178 3.2163 3.4084 -0.0422 -0.3054 0.0450  178  GLY X C   
11942 O O   . GLY B 50   ? 3.3350 3.1956 3.3888 -0.0433 -0.2912 0.0410  178  GLY X O   
11943 N N   . LEU B 51   ? 3.0307 2.9442 3.1651 -0.0193 -0.3221 0.0359  179  LEU X N   
11944 C CA  . LEU B 51   ? 3.1022 2.9853 3.2442 0.0002  -0.3257 0.0224  179  LEU X CA  
11945 C C   . LEU B 51   ? 3.1135 2.9932 3.2849 -0.0088 -0.3414 0.0253  179  LEU X C   
11946 O O   . LEU B 51   ? 3.0707 2.9833 3.2736 -0.0132 -0.3548 0.0317  179  LEU X O   
11947 C CB  . LEU B 51   ? 3.1140 3.0131 3.2791 0.0411  -0.3311 0.0055  179  LEU X CB  
11948 C CG  . LEU B 51   ? 3.0816 2.9559 3.2637 0.0613  -0.3392 -0.0078 179  LEU X CG  
11949 C CD1 . LEU B 51   ? 3.1159 2.9413 3.2587 0.0511  -0.3246 -0.0089 179  LEU X CD1 
11950 C CD2 . LEU B 51   ? 3.0887 2.9811 3.2952 0.1009  -0.3462 -0.0241 179  LEU X CD2 
11951 N N   . TYR B 52   ? 3.4457 3.2860 3.6068 -0.0111 -0.3394 0.0208  180  TYR X N   
11952 C CA  . TYR B 52   ? 3.4728 3.3049 3.6571 -0.0220 -0.3527 0.0240  180  TYR X CA  
11953 C C   . TYR B 52   ? 3.5178 3.3518 3.6911 -0.0608 -0.3522 0.0421  180  TYR X C   
11954 O O   . TYR B 52   ? 3.4891 3.3264 3.6862 -0.0717 -0.3654 0.0472  180  TYR X O   
11955 C CB  . TYR B 52   ? 3.4502 3.3132 3.6863 0.0035  -0.3734 0.0160  180  TYR X CB  
11956 C CG  . TYR B 52   ? 3.4956 3.3479 3.7449 0.0381  -0.3769 -0.0019 180  TYR X CG  
11957 C CD1 . TYR B 52   ? 3.5313 3.3431 3.7598 0.0392  -0.3689 -0.0080 180  TYR X CD1 
11958 C CD2 . TYR B 52   ? 3.4985 3.3814 3.7808 0.0695  -0.3882 -0.0126 180  TYR X CD2 
11959 C CE1 . TYR B 52   ? 3.5570 3.3600 3.7977 0.0700  -0.3725 -0.0238 180  TYR X CE1 
11960 C CE2 . TYR B 52   ? 3.5250 3.3976 3.8185 0.1003  -0.3920 -0.0289 180  TYR X CE2 
11961 C CZ  . TYR B 52   ? 3.5495 3.3826 3.8224 0.1000  -0.3843 -0.0342 180  TYR X CZ  
11962 O OH  . TYR B 52   ? 3.5704 3.3945 3.8549 0.1301  -0.3884 -0.0499 180  TYR X OH  
11963 N N   . LYS B 53   ? 3.3980 3.2300 3.5348 -0.0817 -0.3375 0.0520  181  LYS X N   
11964 C CA  . LYS B 53   ? 3.4243 3.2538 3.5434 -0.1209 -0.3350 0.0695  181  LYS X CA  
11965 C C   . LYS B 53   ? 3.4627 3.2486 3.5267 -0.1439 -0.3150 0.0743  181  LYS X C   
11966 O O   . LYS B 53   ? 3.5006 3.2883 3.5332 -0.1549 -0.3021 0.0802  181  LYS X O   
11967 C CB  . LYS B 53   ? 3.4840 3.3590 3.6139 -0.1296 -0.3384 0.0801  181  LYS X CB  
11968 C CG  . LYS B 53   ? 3.4675 3.3885 3.6497 -0.1039 -0.3566 0.0750  181  LYS X CG  
11969 C CD  . LYS B 53   ? 3.4878 3.4100 3.7070 -0.1036 -0.3750 0.0748  181  LYS X CD  
11970 C CE  . LYS B 53   ? 3.4796 3.4052 3.6966 -0.1408 -0.3796 0.0926  181  LYS X CE  
11971 N NZ  . LYS B 53   ? 3.4728 3.3958 3.7238 -0.1402 -0.3971 0.0921  181  LYS X NZ  
11972 N N   . GLY B 54   ? 3.5953 3.3417 3.6471 -0.1509 -0.3126 0.0720  182  GLY X N   
11973 C CA  . GLY B 54   ? 3.6230 3.3244 3.6230 -0.1708 -0.2940 0.0756  182  GLY X CA  
11974 C C   . GLY B 54   ? 3.6228 3.2939 3.6081 -0.1451 -0.2844 0.0609  182  GLY X C   
11975 O O   . GLY B 54   ? 3.5664 3.2382 3.5817 -0.1200 -0.2941 0.0493  182  GLY X O   
11976 N N   . THR B 55   ? 3.6209 3.2651 3.5594 -0.1517 -0.2657 0.0618  183  THR X N   
11977 C CA  . THR B 55   ? 3.6508 3.2647 3.5702 -0.1288 -0.2548 0.0491  183  THR X CA  
11978 C C   . THR B 55   ? 3.7234 3.3650 3.6697 -0.0909 -0.2603 0.0358  183  THR X C   
11979 O O   . THR B 55   ? 3.7693 3.3922 3.7034 -0.0686 -0.2526 0.0248  183  THR X O   
11980 C CB  . THR B 55   ? 3.6101 3.1885 3.4710 -0.1465 -0.2335 0.0545  183  THR X CB  
11981 O OG1 . THR B 55   ? 3.6460 3.2481 3.4939 -0.1632 -0.2300 0.0649  183  THR X OG1 
11982 C CG2 . THR B 55   ? 3.5728 3.1110 3.4054 -0.1751 -0.2267 0.0622  183  THR X CG2 
11983 N N   . THR B 56   ? 5.3142 5.0010 5.2974 -0.0832 -0.2740 0.0370  184  THR X N   
11984 C CA  . THR B 56   ? 5.3503 5.0646 5.3598 -0.0474 -0.2799 0.0243  184  THR X CA  
11985 C C   . THR B 56   ? 5.3252 5.0483 5.3796 -0.0211 -0.2967 0.0123  184  THR X C   
11986 O O   . THR B 56   ? 5.2660 5.0051 5.3531 -0.0277 -0.3119 0.0161  184  THR X O   
11987 C CB  . THR B 56   ? 5.3442 5.1046 5.3694 -0.0481 -0.2849 0.0302  184  THR X CB  
11988 O OG1 . THR B 56   ? 2.0515 1.8165 2.0631 -0.0850 -0.2834 0.0472  184  THR X OG1 
11989 C CG2 . THR B 56   ? 2.0523 1.8191 2.0538 -0.0314 -0.2718 0.0248  184  THR X CG2 
11990 N N   . LYS B 57   ? 3.4020 3.1147 3.4570 0.0088  -0.2939 -0.0020 185  LYS X N   
11991 C CA  . LYS B 57   ? 3.3786 3.0987 3.4737 0.0363  -0.3092 -0.0147 185  LYS X CA  
11992 C C   . LYS B 57   ? 3.3799 3.0828 3.4662 0.0663  -0.3028 -0.0296 185  LYS X C   
11993 O O   . LYS B 57   ? 3.3688 3.0869 3.4875 0.0950  -0.3149 -0.0418 185  LYS X O   
11994 C CB  . LYS B 57   ? 3.3722 3.0746 3.4813 0.0212  -0.3181 -0.0110 185  LYS X CB  
11995 C CG  . LYS B 57   ? 3.4136 3.0702 3.4833 0.0028  -0.3032 -0.0073 185  LYS X CG  
11996 C CD  . LYS B 57   ? 3.3596 3.0007 3.4434 -0.0127 -0.3118 -0.0032 185  LYS X CD  
11997 C CE  . LYS B 57   ? 3.3461 2.9934 3.4241 -0.0483 -0.3135 0.0131  185  LYS X CE  
11998 N NZ  . LYS B 57   ? 3.2879 2.9100 3.3650 -0.0683 -0.3162 0.0183  185  LYS X NZ  
11999 N N   . TYR B 58   ? 3.5403 3.2108 3.5822 0.0597  -0.2843 -0.0285 186  TYR X N   
12000 C CA  . TYR B 58   ? 3.5501 3.2013 3.5805 0.0864  -0.2772 -0.0415 186  TYR X CA  
12001 C C   . TYR B 58   ? 3.5679 3.2310 3.5799 0.1018  -0.2675 -0.0456 186  TYR X C   
12002 O O   . TYR B 58   ? 3.5929 3.2450 3.5665 0.0843  -0.2524 -0.0373 186  TYR X O   
12003 C CB  . TYR B 58   ? 3.5453 3.1498 3.5400 0.0737  -0.2634 -0.0394 186  TYR X CB  
12004 C CG  . TYR B 58   ? 3.4889 3.0731 3.4710 0.1006  -0.2558 -0.0518 186  TYR X CG  
12005 C CD1 . TYR B 58   ? 3.4305 3.0109 3.4402 0.1223  -0.2661 -0.0628 186  TYR X CD1 
12006 C CD2 . TYR B 58   ? 3.5095 3.0787 3.4522 0.1042  -0.2388 -0.0523 186  TYR X CD2 
12007 C CE1 . TYR B 58   ? 3.3882 2.9516 3.3873 0.1469  -0.2596 -0.0738 186  TYR X CE1 
12008 C CE2 . TYR B 58   ? 3.4683 3.0194 3.3996 0.1292  -0.2322 -0.0633 186  TYR X CE2 
12009 C CZ  . TYR B 58   ? 3.4080 2.9569 3.3679 0.1506  -0.2427 -0.0740 186  TYR X CZ  
12010 O OH  . TYR B 58   ? 3.3650 2.8973 3.3143 0.1753  -0.2365 -0.0845 186  TYR X OH  
12011 N N   . GLY B 59   ? 3.4115 3.0955 3.4496 0.1344  -0.2760 -0.0586 187  GLY X N   
12012 C CA  . GLY B 59   ? 3.4345 3.1330 3.4590 0.1515  -0.2683 -0.0635 187  GLY X CA  
12013 C C   . GLY B 59   ? 3.4119 3.1266 3.4646 0.1893  -0.2783 -0.0797 187  GLY X C   
12014 O O   . GLY B 59   ? 3.3653 3.0761 3.4458 0.2028  -0.2904 -0.0877 187  GLY X O   
12015 N N   . LYS B 60   ? 3.3294 3.0625 3.3745 0.2058  -0.2732 -0.0843 188  LYS X N   
12016 C CA  . LYS B 60   ? 3.3637 3.1118 3.4311 0.2420  -0.2813 -0.0999 188  LYS X CA  
12017 C C   . LYS B 60   ? 3.3782 3.1644 3.4529 0.2541  -0.2822 -0.1015 188  LYS X C   
12018 O O   . LYS B 60   ? 3.4530 3.2385 3.4957 0.2487  -0.2678 -0.0971 188  LYS X O   
12019 C CB  . LYS B 60   ? 3.4346 3.1503 3.4745 0.2572  -0.2699 -0.1081 188  LYS X CB  
12020 C CG  . LYS B 60   ? 3.4185 3.1003 3.4579 0.2537  -0.2710 -0.1100 188  LYS X CG  
12021 C CD  . LYS B 60   ? 3.3850 3.0794 3.4692 0.2749  -0.2905 -0.1210 188  LYS X CD  
12022 C CE  . LYS B 60   ? 3.3661 3.0278 3.4486 0.2749  -0.2906 -0.1240 188  LYS X CE  
12023 N NZ  . LYS B 60   ? 3.2945 2.9380 3.3684 0.2432  -0.2878 -0.1115 188  LYS X NZ  
12024 N N   . ILE B 61   ? 4.9256 4.7446 5.0423 0.2706  -0.2991 -0.1077 189  ILE X N   
12025 C CA  . ILE B 61   ? 4.9285 4.7867 5.0573 0.2853  -0.3017 -0.1104 189  ILE X CA  
12026 C C   . ILE B 61   ? 4.9919 4.8506 5.1187 0.3190  -0.3004 -0.1258 189  ILE X C   
12027 O O   . ILE B 61   ? 4.9879 4.8385 5.1352 0.3401  -0.3108 -0.1378 189  ILE X O   
12028 C CB  . ILE B 61   ? 4.8447 4.7371 5.0198 0.2903  -0.3209 -0.1110 189  ILE X CB  
12029 C CG1 . ILE B 61   ? 4.7630 4.6472 4.9458 0.2603  -0.3260 -0.0985 189  ILE X CG1 
12030 C CG2 . ILE B 61   ? 4.8617 4.7963 5.0450 0.2963  -0.3209 -0.1087 189  ILE X CG2 
12031 C CD1 . ILE B 61   ? 4.6966 4.6097 4.9252 0.2654  -0.3459 -0.0990 189  ILE X CD1 
12032 N N   . THR B 62   ? 6.1222 5.9909 6.2244 0.3236  -0.2881 -0.1252 190  THR X N   
12033 C CA  . THR B 62   ? 6.2109 6.0780 6.3062 0.3539  -0.2851 -0.1389 190  THR X CA  
12034 C C   . THR B 62   ? 6.2583 6.1673 6.3731 0.3755  -0.2908 -0.1454 190  THR X C   
12035 O O   . THR B 62   ? 6.2973 6.2234 6.3929 0.3696  -0.2802 -0.1394 190  THR X O   
12036 C CB  . THR B 62   ? 3.7368 3.5758 3.7832 0.3463  -0.2649 -0.1352 190  THR X CB  
12037 O OG1 . THR B 62   ? 3.7789 3.6376 3.8051 0.3320  -0.2543 -0.1251 190  THR X OG1 
12038 C CG2 . THR B 62   ? 3.7122 3.5105 3.7360 0.3224  -0.2575 -0.1271 190  THR X CG2 
12039 N N   . ILE B 63   ? 4.8586 4.7834 5.0107 0.4006  -0.3075 -0.1577 191  ILE X N   
12040 C CA  . ILE B 63   ? 4.9253 4.8893 5.0983 0.4236  -0.3142 -0.1653 191  ILE X CA  
12041 C C   . ILE B 63   ? 5.0510 5.0130 5.2027 0.4469  -0.3051 -0.1755 191  ILE X C   
12042 O O   . ILE B 63   ? 5.1017 5.0390 5.2480 0.4630  -0.3059 -0.1858 191  ILE X O   
12043 C CB  . ILE B 63   ? 4.2066 4.1852 4.4250 0.4449  -0.3355 -0.1764 191  ILE X CB  
12044 C CG1 . ILE B 63   ? 4.0672 4.0411 4.3076 0.4239  -0.3461 -0.1679 191  ILE X CG1 
12045 C CG2 . ILE B 63   ? 4.2335 4.2549 4.4734 0.4649  -0.3419 -0.1819 191  ILE X CG2 
12046 C CD1 . ILE B 63   ? 3.9783 3.9670 4.2631 0.4430  -0.3675 -0.1777 191  ILE X CD1 
12047 N N   . ASN B 64   ? 4.5750 4.5639 4.7148 0.4483  -0.2966 -0.1722 192  ASN X N   
12048 C CA  . ASN B 64   ? 4.6648 4.6588 4.7891 0.4730  -0.2899 -0.1825 192  ASN X CA  
12049 C C   . ASN B 64   ? 4.6875 4.7124 4.8468 0.5045  -0.3046 -0.1965 192  ASN X C   
12050 O O   . ASN B 64   ? 4.6322 4.6885 4.8197 0.5038  -0.3140 -0.1939 192  ASN X O   
12051 C CB  . ASN B 64   ? 4.7012 4.7081 4.7930 0.4594  -0.2728 -0.1723 192  ASN X CB  
12052 C CG  . ASN B 64   ? 4.7487 4.7207 4.8002 0.4306  -0.2572 -0.1598 192  ASN X CG  
12053 O OD1 . ASN B 64   ? 4.7714 4.7081 4.8170 0.4235  -0.2578 -0.1600 192  ASN X OD1 
12054 N ND2 . ASN B 64   ? 4.7622 4.7438 4.7852 0.4137  -0.2431 -0.1488 192  ASN X ND2 
12055 N N   . LEU B 65   ? 6.6367 6.6788 6.8741 0.2757  -0.0803 0.0036  193  LEU X N   
12056 C CA  . LEU B 65   ? 6.6359 6.6937 6.9033 0.2786  -0.0700 0.0172  193  LEU X CA  
12057 C C   . LEU B 65   ? 6.6868 6.7402 6.9607 0.2509  -0.0379 0.0341  193  LEU X C   
12058 O O   . LEU B 65   ? 6.6820 6.7477 6.9605 0.2488  -0.0389 0.0341  193  LEU X O   
12059 C CB  . LEU B 65   ? 6.6027 6.6520 6.8779 0.3036  -0.0835 0.0056  193  LEU X CB  
12060 C CG  . LEU B 65   ? 6.5545 6.6044 6.8266 0.3244  -0.1174 -0.0131 193  LEU X CG  
12061 C CD1 . LEU B 65   ? 6.5395 6.5721 6.8165 0.3384  -0.1236 -0.0210 193  LEU X CD1 
12062 C CD2 . LEU B 65   ? 6.5134 6.5921 6.8044 0.3382  -0.1382 -0.0167 193  LEU X CD2 
12063 N N   . LYS B 66   ? 4.0679 4.0845 4.2037 0.5869  -0.3015 -0.2371 194  LYS X N   
12064 C CA  . LYS B 66   ? 4.1652 4.1839 4.2797 0.6086  -0.2936 -0.2461 194  LYS X CA  
12065 C C   . LYS B 66   ? 4.2243 4.2108 4.2949 0.5949  -0.2759 -0.2391 194  LYS X C   
12066 O O   . LYS B 66   ? 4.1951 4.1563 4.2529 0.5702  -0.2705 -0.2285 194  LYS X O   
12067 C CB  . LYS B 66   ? 4.2221 4.2366 4.3568 0.6407  -0.3076 -0.2645 194  LYS X CB  
12068 C CG  . LYS B 66   ? 4.3178 4.3437 4.4376 0.6661  -0.3024 -0.2751 194  LYS X CG  
12069 C CD  . LYS B 66   ? 4.4004 4.4674 4.5234 0.6683  -0.2983 -0.2719 194  LYS X CD  
12070 C CE  . LYS B 66   ? 4.4941 4.5691 4.5920 0.6863  -0.2881 -0.2784 194  LYS X CE  
12071 N NZ  . LYS B 66   ? 4.5748 4.6203 4.6308 0.6713  -0.2712 -0.2703 194  LYS X NZ  
12072 N N   . ASP B 67   ? 2.9581 2.9447 3.0048 0.6110  -0.2669 -0.2451 195  ASP X N   
12073 C CA  . ASP B 67   ? 3.0216 2.9803 3.0239 0.5987  -0.2491 -0.2378 195  ASP X CA  
12074 C C   . ASP B 67   ? 3.1226 3.0373 3.1123 0.5955  -0.2479 -0.2390 195  ASP X C   
12075 O O   . ASP B 67   ? 3.1923 3.0820 3.1466 0.5937  -0.2348 -0.2368 195  ASP X O   
12076 C CB  . ASP B 67   ? 2.9897 2.9603 2.9705 0.6181  -0.2406 -0.2442 195  ASP X CB  
12077 C CG  . ASP B 67   ? 2.8814 2.8841 2.8513 0.6067  -0.2309 -0.2347 195  ASP X CG  
12078 O OD1 . ASP B 67   ? 2.8475 2.8392 2.7888 0.5800  -0.2172 -0.2203 195  ASP X OD1 
12079 O OD2 . ASP B 67   ? 2.8446 2.8835 2.8341 0.6244  -0.2368 -0.2417 195  ASP X OD2 
12080 N N   . GLY B 68   ? 4.9169 4.8224 4.9351 0.5946  -0.2614 -0.2420 196  GLY X N   
12081 C CA  . GLY B 68   ? 5.0051 4.8718 5.0144 0.5919  -0.2609 -0.2431 196  GLY X CA  
12082 C C   . GLY B 68   ? 4.8848 4.7428 4.9242 0.5830  -0.2742 -0.2424 196  GLY X C   
12083 O O   . GLY B 68   ? 4.9010 4.7306 4.9395 0.5853  -0.2766 -0.2455 196  GLY X O   
12084 N N   . GLU B 69   ? 6.5349 6.4610 6.6942 0.3806  -0.1210 -0.0934 197  GLU X N   
12085 C CA  . GLU B 69   ? 6.4940 6.4119 6.6583 0.4015  -0.1495 -0.1078 197  GLU X CA  
12086 C C   . GLU B 69   ? 6.4866 6.3980 6.6323 0.3983  -0.1686 -0.1147 197  GLU X C   
12087 O O   . GLU B 69   ? 6.4924 6.4254 6.6387 0.3871  -0.1680 -0.1073 197  GLU X O   
12088 C CB  . GLU B 69   ? 3.8437 3.7489 3.9815 0.5848  -0.3157 -0.2480 197  GLU X CB  
12089 C CG  . GLU B 69   ? 3.8117 3.7050 3.9801 0.5864  -0.3321 -0.2526 197  GLU X CG  
12090 C CD  . GLU B 69   ? 3.7829 3.6968 3.9853 0.6141  -0.3501 -0.2674 197  GLU X CD  
12091 O OE1 . GLU B 69   ? 3.7942 3.7218 3.9906 0.6367  -0.3486 -0.2770 197  GLU X OE1 
12092 O OE2 . GLU B 69   ? 3.7515 3.6673 3.9855 0.6131  -0.3658 -0.2694 197  GLU X OE2 
12093 N N   . LYS B 70   ? 3.5934 3.4349 3.6796 0.5151  -0.2905 -0.2159 198  LYS X N   
12094 C CA  . LYS B 70   ? 3.4602 3.2921 3.5374 0.4817  -0.2845 -0.2004 198  LYS X CA  
12095 C C   . LYS B 70   ? 3.3704 3.1850 3.4701 0.4729  -0.2958 -0.1998 198  LYS X C   
12096 O O   . LYS B 70   ? 3.3952 3.1803 3.4865 0.4766  -0.2942 -0.2034 198  LYS X O   
12097 C CB  . LYS B 70   ? 3.4325 3.2367 3.4619 0.4643  -0.2637 -0.1908 198  LYS X CB  
12098 C CG  . LYS B 70   ? 3.3988 3.2172 3.4018 0.4697  -0.2513 -0.1897 198  LYS X CG  
12099 C CD  . LYS B 70   ? 3.3570 3.1499 3.3137 0.4448  -0.2315 -0.1767 198  LYS X CD  
12100 C CE  . LYS B 70   ? 3.3524 3.1046 3.2807 0.4509  -0.2223 -0.1800 198  LYS X CE  
12101 N NZ  . LYS B 70   ? 3.3180 3.0741 3.2375 0.4797  -0.2200 -0.1914 198  LYS X NZ  
12102 N N   . GLN B 71   ? 6.1567 5.9907 6.2847 0.4610  -0.3069 -0.1947 199  GLN X N   
12103 C CA  . GLN B 71   ? 6.0569 5.8794 6.2104 0.4524  -0.3195 -0.1938 199  GLN X CA  
12104 C C   . GLN B 71   ? 5.9543 5.7805 6.1091 0.4201  -0.3183 -0.1783 199  GLN X C   
12105 O O   . GLN B 71   ? 5.9438 5.7877 6.0860 0.4069  -0.3103 -0.1694 199  GLN X O   
12106 C CB  . GLN B 71   ? 3.3989 3.2419 3.5949 0.4770  -0.3403 -0.2067 199  GLN X CB  
12107 C CG  . GLN B 71   ? 3.4459 3.3260 3.6550 0.4952  -0.3446 -0.2125 199  GLN X CG  
12108 C CD  . GLN B 71   ? 3.4188 3.3184 3.6706 0.5159  -0.3659 -0.2236 199  GLN X CD  
12109 O OE1 . GLN B 71   ? 3.3648 3.2704 3.6425 0.5048  -0.3777 -0.2191 199  GLN X OE1 
12110 N NE2 . GLN B 71   ? 3.4254 3.3343 3.6837 0.5458  -0.3711 -0.2379 199  GLN X NE2 
12111 N N   . GLU B 72   ? 4.6038 4.4146 4.7744 0.4074  -0.3266 -0.1752 200  GLU X N   
12112 C CA  . GLU B 72   ? 4.4952 4.3037 4.6640 0.3749  -0.3249 -0.1602 200  GLU X CA  
12113 C C   . GLU B 72   ? 4.3903 4.2013 4.5960 0.3699  -0.3427 -0.1601 200  GLU X C   
12114 O O   . GLU B 72   ? 4.3554 4.1652 4.5864 0.3903  -0.3561 -0.1715 200  GLU X O   
12115 C CB  . GLU B 72   ? 4.5147 4.2868 4.6432 0.3526  -0.3074 -0.1509 200  GLU X CB  
12116 C CG  . GLU B 72   ? 4.5934 4.3552 4.6824 0.3580  -0.2896 -0.1515 200  GLU X CG  
12117 C CD  . GLU B 72   ? 4.6286 4.3481 4.6817 0.3464  -0.2751 -0.1476 200  GLU X CD  
12118 O OE1 . GLU B 72   ? 4.5817 4.2815 4.6357 0.3271  -0.2761 -0.1410 200  GLU X OE1 
12119 O OE2 . GLU B 72   ? 4.7086 4.4144 4.7320 0.3568  -0.2625 -0.1509 200  GLU X OE2 
12120 N N   . ILE B 73   ? 4.0821 3.8956 4.2894 0.3415  -0.3429 -0.1466 201  ILE X N   
12121 C CA  . ILE B 73   ? 3.9968 3.8099 4.2349 0.3317  -0.3583 -0.1439 201  ILE X CA  
12122 C C   . ILE B 73   ? 4.0060 3.7963 4.2227 0.2972  -0.3491 -0.1293 201  ILE X C   
12123 O O   . ILE B 73   ? 3.9956 3.7973 4.2016 0.2750  -0.3433 -0.1170 201  ILE X O   
12124 C CB  . ILE B 73   ? 3.8881 3.7388 4.1603 0.3340  -0.3728 -0.1422 201  ILE X CB  
12125 C CG1 . ILE B 73   ? 3.8936 3.7700 4.1814 0.3668  -0.3790 -0.1555 201  ILE X CG1 
12126 C CG2 . ILE B 73   ? 3.8036 3.6521 4.1090 0.3275  -0.3903 -0.1411 201  ILE X CG2 
12127 C CD1 . ILE B 73   ? 3.8452 3.7612 4.1492 0.3676  -0.3835 -0.1513 201  ILE X CD1 
12128 N N   . ASP B 74   ? 3.3886 3.1471 3.5986 0.2924  -0.3477 -0.1304 202  ASP X N   
12129 C CA  . ASP B 74   ? 3.4192 3.1524 3.6048 0.2607  -0.3374 -0.1173 202  ASP X CA  
12130 C C   . ASP B 74   ? 3.4033 3.1557 3.6074 0.2380  -0.3462 -0.1059 202  ASP X C   
12131 O O   . ASP B 74   ? 3.3464 3.1177 3.5889 0.2455  -0.3642 -0.1091 202  ASP X O   
12132 C CB  . ASP B 74   ? 3.4272 3.1287 3.6126 0.2603  -0.3385 -0.1207 202  ASP X CB  
12133 C CG  . ASP B 74   ? 3.4196 3.0919 3.5749 0.2286  -0.3257 -0.1078 202  ASP X CG  
12134 O OD1 . ASP B 74   ? 3.3727 3.0229 3.5320 0.2234  -0.3282 -0.1080 202  ASP X OD1 
12135 O OD2 . ASP B 74   ? 3.4525 3.1239 3.5797 0.2087  -0.3132 -0.0974 202  ASP X OD2 
12136 N N   . LEU B 75   ? 4.1376 3.8851 4.3135 0.2103  -0.3336 -0.0924 203  LEU X N   
12137 C CA  . LEU B 75   ? 4.1486 3.9125 4.3377 0.1854  -0.3404 -0.0798 203  LEU X CA  
12138 C C   . LEU B 75   ? 4.2113 3.9470 4.3962 0.1623  -0.3410 -0.0727 203  LEU X C   
12139 O O   . LEU B 75   ? 4.1644 3.9083 4.3607 0.1399  -0.3477 -0.0621 203  LEU X O   
12140 C CB  . LEU B 75   ? 4.1278 3.9030 4.2891 0.1663  -0.3273 -0.0683 203  LEU X CB  
12141 C CG  . LEU B 75   ? 4.1368 3.9419 4.3023 0.1892  -0.3263 -0.0751 203  LEU X CG  
12142 C CD1 . LEU B 75   ? 4.1486 3.9666 4.2872 0.1687  -0.3137 -0.0628 203  LEU X CD1 
12143 C CD2 . LEU B 75   ? 4.0907 3.9314 4.3039 0.2098  -0.3462 -0.0821 203  LEU X CD2 
12144 N N   . GLY B 76   ? 3.6099 3.3128 3.7781 0.1681  -0.3339 -0.0785 204  GLY X N   
12145 C CA  . GLY B 76   ? 3.6506 3.3264 3.8169 0.1504  -0.3348 -0.0737 204  GLY X CA  
12146 C C   . GLY B 76   ? 3.6912 3.3790 3.9026 0.1601  -0.3560 -0.0790 204  GLY X C   
12147 O O   . GLY B 76   ? 3.6413 3.3151 3.8591 0.1424  -0.3606 -0.0731 204  GLY X O   
12148 N N   . ASP B 77   ? 3.6490 3.3622 3.8909 0.1879  -0.3690 -0.0900 205  ASP X N   
12149 C CA  . ASP B 77   ? 3.6850 3.4079 3.9691 0.1999  -0.3897 -0.0963 205  ASP X CA  
12150 C C   . ASP B 77   ? 3.7067 3.4621 4.0225 0.2280  -0.4037 -0.1067 205  ASP X C   
12151 O O   . ASP B 77   ? 3.7621 3.5230 4.0696 0.2506  -0.3984 -0.1162 205  ASP X O   
12152 C CB  . ASP B 77   ? 3.7371 3.4321 4.0204 0.2097  -0.3897 -0.1043 205  ASP X CB  
12153 C CG  . ASP B 77   ? 3.7445 3.4409 4.0638 0.2089  -0.4087 -0.1057 205  ASP X CG  
12154 O OD1 . ASP B 77   ? 3.7321 3.4450 4.0713 0.1946  -0.4196 -0.0979 205  ASP X OD1 
12155 O OD2 . ASP B 77   ? 3.7607 3.4419 4.0882 0.2221  -0.4130 -0.1141 205  ASP X OD2 
12156 N N   . LYS B 78   ? 3.4330 3.2087 3.7843 0.2264  -0.4218 -0.1048 206  LYS X N   
12157 C CA  . LYS B 78   ? 3.4190 3.2244 3.8033 0.2528  -0.4372 -0.1146 206  LYS X CA  
12158 C C   . LYS B 78   ? 3.3929 3.1896 3.8015 0.2769  -0.4511 -0.1286 206  LYS X C   
12159 O O   . LYS B 78   ? 3.3883 3.2034 3.8311 0.2923  -0.4692 -0.1348 206  LYS X O   
12160 C CB  . LYS B 78   ? 3.3781 3.2100 3.7889 0.2406  -0.4503 -0.1056 206  LYS X CB  
12161 C CG  . LYS B 78   ? 3.3409 3.1604 3.7670 0.2190  -0.4607 -0.0974 206  LYS X CG  
12162 C CD  . LYS B 78   ? 3.2978 3.1442 3.7467 0.2057  -0.4721 -0.0871 206  LYS X CD  
12163 C CE  . LYS B 78   ? 3.2628 3.0958 3.7240 0.1821  -0.4816 -0.0779 206  LYS X CE  
12164 N NZ  . LYS B 78   ? 3.2190 3.0411 3.7075 0.1980  -0.4978 -0.0881 206  LYS X NZ  
12165 N N   . LEU B 79   ? 4.6225 4.3910 5.0128 0.2799  -0.4427 -0.1333 207  LEU X N   
12166 C CA  . LEU B 79   ? 4.5713 4.3284 4.9819 0.2985  -0.4548 -0.1449 207  LEU X CA  
12167 C C   . LEU B 79   ? 4.5692 4.3401 4.9920 0.3333  -0.4613 -0.1606 207  LEU X C   
12168 O O   . LEU B 79   ? 4.5900 4.3511 5.0260 0.3505  -0.4701 -0.1712 207  LEU X O   
12169 C CB  . LEU B 79   ? 4.5490 4.2726 4.9352 0.2895  -0.4427 -0.1437 207  LEU X CB  
12170 C CG  . LEU B 79   ? 4.5291 4.2367 4.9325 0.3008  -0.4531 -0.1521 207  LEU X CG  
12171 C CD1 . LEU B 79   ? 4.4697 4.1818 4.9066 0.2905  -0.4723 -0.1486 207  LEU X CD1 
12172 C CD2 . LEU B 79   ? 4.5183 4.1951 4.8915 0.2906  -0.4368 -0.1491 207  LEU X CD2 
12173 N N   . GLN B 80   ? 3.6794 3.4732 4.0973 0.3432  -0.4570 -0.1620 208  GLN X N   
12174 C CA  . GLN B 80   ? 3.6745 3.4824 4.1014 0.3759  -0.4620 -0.1768 208  GLN X CA  
12175 C C   . GLN B 80   ? 3.6282 3.4569 4.0961 0.3925  -0.4848 -0.1842 208  GLN X C   
12176 O O   . GLN B 80   ? 3.6188 3.4746 4.0976 0.3994  -0.4887 -0.1840 208  GLN X O   
12177 C CB  . GLN B 80   ? 3.6800 3.5041 4.0835 0.3804  -0.4472 -0.1754 208  GLN X CB  
12178 C CG  . GLN B 80   ? 3.7391 3.5417 4.0998 0.3686  -0.4247 -0.1702 208  GLN X CG  
12179 C CD  . GLN B 80   ? 3.7666 3.5636 4.1068 0.3345  -0.4131 -0.1532 208  GLN X CD  
12180 O OE1 . GLN B 80   ? 3.7795 3.5919 4.1373 0.3194  -0.4214 -0.1447 208  GLN X OE1 
12181 N NE2 . GLN B 80   ? 3.7833 3.5574 4.0852 0.3224  -0.3940 -0.1481 208  GLN X NE2 
12182 N N   . PHE B 81   ? 3.6880 3.5041 4.1779 0.3993  -0.4997 -0.1906 209  PHE X N   
12183 C CA  . PHE B 81   ? 3.6671 3.4985 4.1951 0.4124  -0.5223 -0.1967 209  PHE X CA  
12184 C C   . PHE B 81   ? 3.7691 3.6066 4.3118 0.4465  -0.5335 -0.2142 209  PHE X C   
12185 O O   . PHE B 81   ? 3.7794 3.6337 4.3498 0.4603  -0.5500 -0.2198 209  PHE X O   
12186 C CB  . PHE B 81   ? 3.5658 3.3832 4.1136 0.3949  -0.5354 -0.1908 209  PHE X CB  
12187 C CG  . PHE B 81   ? 3.5191 3.3085 4.0604 0.3943  -0.5343 -0.1948 209  PHE X CG  
12188 C CD1 . PHE B 81   ? 3.5396 3.3241 4.0960 0.4186  -0.5463 -0.2090 209  PHE X CD1 
12189 C CD2 . PHE B 81   ? 3.4519 3.2205 3.9724 0.3689  -0.5216 -0.1840 209  PHE X CD2 
12190 C CE1 . PHE B 81   ? 3.5192 3.2805 4.0709 0.4178  -0.5454 -0.2120 209  PHE X CE1 
12191 C CE2 . PHE B 81   ? 3.4176 3.1624 3.9329 0.3689  -0.5202 -0.1873 209  PHE X CE2 
12192 C CZ  . PHE B 81   ? 3.4568 3.1990 3.9884 0.3933  -0.5322 -0.2011 209  PHE X CZ  
12193 N N   . GLU B 82   ? 3.4813 3.3048 4.0055 0.4601  -0.5247 -0.2228 210  GLU X N   
12194 C CA  . GLU B 82   ? 3.5840 3.4112 4.1194 0.4919  -0.5346 -0.2395 210  GLU X CA  
12195 C C   . GLU B 82   ? 3.6186 3.4662 4.1415 0.5108  -0.5261 -0.2456 210  GLU X C   
12196 O O   . GLU B 82   ? 3.6751 3.5364 4.2143 0.5359  -0.5376 -0.2577 210  GLU X O   
12197 C CB  . GLU B 82   ? 3.6821 3.4847 4.2066 0.4983  -0.5317 -0.2462 210  GLU X CB  
12198 C CG  . GLU B 82   ? 3.8074 3.6071 4.3027 0.5130  -0.5153 -0.2523 210  GLU X CG  
12199 C CD  . GLU B 82   ? 3.8481 3.6416 4.3093 0.4925  -0.4924 -0.2400 210  GLU X CD  
12200 O OE1 . GLU B 82   ? 3.8083 3.5931 4.2662 0.4658  -0.4884 -0.2272 210  GLU X OE1 
12201 O OE2 . GLU B 82   ? 3.9188 3.7154 4.3558 0.5028  -0.4785 -0.2431 210  GLU X OE2 
12202 N N   . ARG B 83   ? 3.9374 3.7858 4.4302 0.4985  -0.5058 -0.2373 211  ARG X N   
12203 C CA  . ARG B 83   ? 3.9159 3.7833 4.3934 0.5132  -0.4955 -0.2412 211  ARG X CA  
12204 C C   . ARG B 83   ? 3.8826 3.7804 4.3759 0.5113  -0.5005 -0.2363 211  ARG X C   
12205 O O   . ARG B 83   ? 3.8969 3.8160 4.3856 0.5272  -0.4962 -0.2411 211  ARG X O   
12206 C CB  . ARG B 83   ? 3.8677 3.7232 4.3056 0.4996  -0.4720 -0.2336 211  ARG X CB  
12207 C CG  . ARG B 83   ? 3.8391 3.6862 4.2643 0.4655  -0.4624 -0.2164 211  ARG X CG  
12208 C CD  . ARG B 83   ? 3.8157 3.6489 4.1998 0.4536  -0.4394 -0.2097 211  ARG X CD  
12209 N NE  . ARG B 83   ? 3.7241 3.5325 4.0924 0.4650  -0.4338 -0.2175 211  ARG X NE  
12210 C CZ  . ARG B 83   ? 3.6938 3.4755 4.0565 0.4522  -0.4319 -0.2139 211  ARG X CZ  
12211 N NH1 . ARG B 83   ? 3.7319 3.5074 4.1026 0.4272  -0.4351 -0.2029 211  ARG X NH1 
12212 N NH2 . ARG B 83   ? 3.6430 3.4051 3.9921 0.4646  -0.4267 -0.2211 211  ARG X NH2 
12213 N N   . MET B 84   ? 3.8911 3.7916 4.4030 0.4920  -0.5095 -0.2264 212  MET X N   
12214 C CA  . MET B 84   ? 3.8531 3.7830 4.3828 0.4891  -0.5156 -0.2206 212  MET X CA  
12215 C C   . MET B 84   ? 3.8586 3.8079 4.4143 0.5200  -0.5314 -0.2344 212  MET X C   
12216 O O   . MET B 84   ? 3.8693 3.8450 4.4417 0.5230  -0.5374 -0.2316 212  MET X O   
12217 C CB  . MET B 84   ? 3.7780 3.7047 4.3241 0.4631  -0.5241 -0.2077 212  MET X CB  
12218 C CG  . MET B 84   ? 3.7387 3.6612 4.2607 0.4303  -0.5078 -0.1905 212  MET X CG  
12219 S SD  . MET B 84   ? 3.3848 3.3060 3.9281 0.4011  -0.5195 -0.1758 212  MET X SD  
12220 C CE  . MET B 84   ? 2.1210 2.0343 2.6280 0.3650  -0.4974 -0.1577 212  MET X CE  
12221 N N   . GLY B 85   ? 3.3783 3.3143 3.9371 0.5427  -0.5382 -0.2492 213  GLY X N   
12222 C CA  . GLY B 85   ? 3.3960 3.3472 3.9736 0.5738  -0.5512 -0.2640 213  GLY X CA  
12223 C C   . GLY B 85   ? 3.4469 3.4134 4.0039 0.5919  -0.5378 -0.2706 213  GLY X C   
12224 O O   . GLY B 85   ? 3.4703 3.4591 4.0393 0.6140  -0.5440 -0.2790 213  GLY X O   
12225 N N   . ASP B 86   ? 4.2284 4.1823 4.7534 0.5824  -0.5192 -0.2666 214  ASP X N   
12226 C CA  . ASP B 86   ? 4.2587 4.2242 4.7594 0.5959  -0.5042 -0.2710 214  ASP X CA  
12227 C C   . ASP B 86   ? 4.2770 4.2779 4.7845 0.5992  -0.5023 -0.2670 214  ASP X C   
12228 O O   . ASP B 86   ? 4.2554 4.2684 4.7731 0.5797  -0.5036 -0.2545 214  ASP X O   
12229 C CB  . ASP B 86   ? 4.1892 4.1370 4.6541 0.5759  -0.4833 -0.2614 214  ASP X CB  
12230 C CG  . ASP B 86   ? 4.1767 4.1174 4.6162 0.5943  -0.4721 -0.2711 214  ASP X CG  
12231 O OD1 . ASP B 86   ? 4.1822 4.1443 4.6205 0.6148  -0.4707 -0.2788 214  ASP X OD1 
12232 O OD2 . ASP B 86   ? 4.1640 4.0781 4.5843 0.5884  -0.4643 -0.2707 214  ASP X OD2 
12233 N N   . VAL B 87   ? 4.6822 4.7005 5.1845 0.6239  -0.4992 -0.2773 215  VAL X N   
12234 C CA  . VAL B 87   ? 4.6217 4.6759 5.1299 0.6294  -0.4964 -0.2742 215  VAL X CA  
12235 C C   . VAL B 87   ? 4.6029 4.6676 5.0798 0.6339  -0.4769 -0.2741 215  VAL X C   
12236 O O   . VAL B 87   ? 4.6190 4.6674 5.0770 0.6465  -0.4710 -0.2831 215  VAL X O   
12237 C CB  . VAL B 87   ? 5.0957 5.1671 5.6338 0.6580  -0.5146 -0.2875 215  VAL X CB  
12238 C CG1 . VAL B 87   ? 5.0707 5.1366 5.6402 0.6502  -0.5333 -0.2845 215  VAL X CG1 
12239 C CG2 . VAL B 87   ? 5.1417 5.1990 5.6754 0.6860  -0.5194 -0.3056 215  VAL X CG2 
12240 N N   . LEU B 88   ? 4.3307 4.4229 4.8019 0.6232  -0.4670 -0.2633 216  LEU X N   
12241 C CA  . LEU B 88   ? 4.3014 4.4038 4.7412 0.6228  -0.4475 -0.2606 216  LEU X CA  
12242 C C   . LEU B 88   ? 4.2566 4.3988 4.7034 0.6405  -0.4459 -0.2637 216  LEU X C   
12243 O O   . LEU B 88   ? 4.2153 4.3818 4.6895 0.6441  -0.4567 -0.2620 216  LEU X O   
12244 C CB  . LEU B 88   ? 4.2555 4.3501 4.6709 0.5882  -0.4317 -0.2425 216  LEU X CB  
12245 C CG  . LEU B 88   ? 4.2192 4.2738 4.6175 0.5691  -0.4272 -0.2380 216  LEU X CG  
12246 C CD1 . LEU B 88   ? 4.2518 4.2827 4.6350 0.5890  -0.4250 -0.2516 216  LEU X CD1 
12247 C CD2 . LEU B 88   ? 4.1459 4.1883 4.5711 0.5574  -0.4429 -0.2348 216  LEU X CD2 
12248 N N   . ASN B 89   ? 4.4948 4.6434 4.9162 0.6515  -0.4322 -0.2680 217  ASN X N   
12249 C CA  . ASN B 89   ? 4.4833 4.6692 4.9076 0.6699  -0.4288 -0.2720 217  ASN X CA  
12250 C C   . ASN B 89   ? 4.4633 4.6748 4.8740 0.6473  -0.4141 -0.2551 217  ASN X C   
12251 O O   . ASN B 89   ? 4.4572 4.6543 4.8379 0.6257  -0.3987 -0.2451 217  ASN X O   
12252 C CB  . ASN B 89   ? 4.5352 4.7158 4.9392 0.6945  -0.4222 -0.2858 217  ASN X CB  
12253 C CG  . ASN B 89   ? 4.5807 4.7293 4.9900 0.7110  -0.4338 -0.3004 217  ASN X CG  
12254 O OD1 . ASN B 89   ? 4.5778 4.7120 5.0101 0.7081  -0.4488 -0.3019 217  ASN X OD1 
12255 N ND2 . ASN B 89   ? 4.6242 4.7621 5.0121 0.7280  -0.4272 -0.3107 217  ASN X ND2 
12256 N N   . SER B 90   ? 3.2472 3.4965 3.6795 0.6525  -0.4187 -0.2519 218  SER X N   
12257 C CA  . SER B 90   ? 3.2664 3.5432 3.6912 0.6291  -0.4073 -0.2345 218  SER X CA  
12258 C C   . SER B 90   ? 3.3536 3.6397 3.7434 0.6247  -0.3871 -0.2303 218  SER X C   
12259 O O   . SER B 90   ? 3.3429 3.6214 3.7087 0.5960  -0.3740 -0.2159 218  SER X O   
12260 C CB  . SER B 90   ? 3.2078 3.5262 3.6648 0.6392  -0.4170 -0.2329 218  SER X CB  
12261 O OG  . SER B 90   ? 3.1557 3.4672 3.6400 0.6285  -0.4320 -0.2280 218  SER X OG  
12262 N N   . LYS B 91   ? 2.2500 2.5519 2.6359 0.6528  -0.3846 -0.2428 219  LYS X N   
12263 C CA  . LYS B 91   ? 2.3716 2.6880 2.7266 0.6509  -0.3662 -0.2390 219  LYS X CA  
12264 C C   . LYS B 91   ? 2.3302 2.6089 2.6496 0.6485  -0.3552 -0.2429 219  LYS X C   
12265 O O   . LYS B 91   ? 2.3900 2.6743 2.6801 0.6474  -0.3397 -0.2407 219  LYS X O   
12266 C CB  . LYS B 91   ? 2.5858 2.9400 2.9524 0.6812  -0.3676 -0.2494 219  LYS X CB  
12267 C CG  . LYS B 91   ? 2.8273 3.2192 3.2302 0.6861  -0.3787 -0.2459 219  LYS X CG  
12268 C CD  . LYS B 91   ? 2.8361 3.2122 3.2712 0.7004  -0.3996 -0.2563 219  LYS X CD  
12269 C CE  . LYS B 91   ? 2.9038 3.3116 3.3734 0.6997  -0.4107 -0.2500 219  LYS X CE  
12270 N NZ  . LYS B 91   ? 2.9392 3.3311 3.4385 0.7180  -0.4313 -0.2623 219  LYS X NZ  
12271 N N   . ASP B 92   ? 3.3121 3.5529 3.6348 0.6474  -0.3635 -0.2483 220  ASP X N   
12272 C CA  . ASP B 92   ? 3.2749 3.4772 3.5673 0.6449  -0.3550 -0.2518 220  ASP X CA  
12273 C C   . ASP B 92   ? 3.2277 3.4121 3.4906 0.6101  -0.3400 -0.2348 220  ASP X C   
12274 O O   . ASP B 92   ? 3.2796 3.4574 3.5083 0.6043  -0.3240 -0.2311 220  ASP X O   
12275 C CB  . ASP B 92   ? 3.2571 3.4274 3.5661 0.6545  -0.3700 -0.2624 220  ASP X CB  
12276 C CG  . ASP B 92   ? 3.2840 3.4568 3.6058 0.6908  -0.3806 -0.2821 220  ASP X CG  
12277 O OD1 . ASP B 92   ? 3.3088 3.5105 3.6306 0.7098  -0.3777 -0.2881 220  ASP X OD1 
12278 O OD2 . ASP B 92   ? 3.2872 3.4330 3.6185 0.7000  -0.3917 -0.2917 220  ASP X OD2 
12279 N N   . ILE B 93   ? 5.0444 5.2200 5.3204 0.5869  -0.3458 -0.2244 221  ILE X N   
12280 C CA  . ILE B 93   ? 4.9740 5.1286 5.2240 0.5527  -0.3336 -0.2085 221  ILE X CA  
12281 C C   . ILE B 93   ? 4.9301 5.1012 5.1489 0.5407  -0.3153 -0.1986 221  ILE X C   
12282 O O   . ILE B 93   ? 4.9373 5.1476 5.1653 0.5488  -0.3143 -0.1977 221  ILE X O   
12283 C CB  . ILE B 93   ? 4.4068 4.5672 4.6793 0.5293  -0.3423 -0.1966 221  ILE X CB  
12284 C CG1 . ILE B 93   ? 4.3443 4.4946 4.6519 0.5438  -0.3623 -0.2068 221  ILE X CG1 
12285 C CG2 . ILE B 93   ? 4.4422 4.5745 4.6870 0.4942  -0.3309 -0.1815 221  ILE X CG2 
12286 C CD1 . ILE B 93   ? 4.2652 4.4157 4.5938 0.5205  -0.3714 -0.1954 221  ILE X CD1 
12287 N N   . ASN B 94   ? 4.6079 4.7492 4.7895 0.5216  -0.3008 -0.1913 222  ASN X N   
12288 C CA  . ASN B 94   ? 4.5987 4.7514 4.7475 0.5081  -0.2832 -0.1813 222  ASN X CA  
12289 C C   . ASN B 94   ? 4.5642 4.7149 4.6983 0.4695  -0.2750 -0.1615 222  ASN X C   
12290 O O   . ASN B 94   ? 4.5167 4.7001 4.6487 0.4581  -0.2693 -0.1514 222  ASN X O   
12291 C CB  . ASN B 94   ? 2.4362 2.5598 2.5486 0.5169  -0.2709 -0.1875 222  ASN X CB  
12292 C CG  . ASN B 94   ? 2.4717 2.6067 2.5492 0.5047  -0.2531 -0.1779 222  ASN X CG  
12293 O OD1 . ASN B 94   ? 2.4757 2.5970 2.5276 0.4745  -0.2421 -0.1632 222  ASN X OD1 
12294 N ND2 . ASN B 94   ? 2.4996 2.6593 2.5749 0.5278  -0.2501 -0.1861 222  ASN X ND2 
12295 N N   . LYS B 95   ? 4.8231 4.9365 4.9476 0.4494  -0.2747 -0.1560 223  LYS X N   
12296 C CA  . LYS B 95   ? 4.7780 4.8832 4.8843 0.4116  -0.2665 -0.1377 223  LYS X CA  
12297 C C   . LYS B 95   ? 4.6635 4.7332 4.7747 0.3956  -0.2726 -0.1348 223  LYS X C   
12298 O O   . LYS B 95   ? 4.6932 4.7248 4.7878 0.3999  -0.2694 -0.1408 223  LYS X O   
12299 C CB  . LYS B 95   ? 2.7282 2.8164 2.7860 0.3966  -0.2464 -0.1301 223  LYS X CB  
12300 C CG  . LYS B 95   ? 2.7313 2.8558 2.7792 0.4040  -0.2379 -0.1285 223  LYS X CG  
12301 C CD  . LYS B 95   ? 2.7764 2.8773 2.7757 0.3963  -0.2195 -0.1249 223  LYS X CD  
12302 C CE  . LYS B 95   ? 2.7960 2.9349 2.7862 0.4024  -0.2113 -0.1226 223  LYS X CE  
12303 N NZ  . LYS B 95   ? 2.7762 2.9508 2.8005 0.4369  -0.2221 -0.1367 223  LYS X NZ  
12304 N N   . ILE B 96   ? 3.7915 3.8740 3.9254 0.3772  -0.2813 -0.1254 224  ILE X N   
12305 C CA  . ILE B 96   ? 3.7816 3.8313 3.9180 0.3589  -0.2862 -0.1211 224  ILE X CA  
12306 C C   . ILE B 96   ? 3.8696 3.8912 3.9635 0.3253  -0.2698 -0.1066 224  ILE X C   
12307 O O   . ILE B 96   ? 3.9092 3.9459 3.9806 0.3113  -0.2582 -0.0969 224  ILE X O   
12308 C CB  . ILE B 96   ? 3.4864 3.5589 3.6622 0.3512  -0.3021 -0.1160 224  ILE X CB  
12309 C CG1 . ILE B 96   ? 3.4579 3.5611 3.6739 0.3842  -0.3177 -0.1295 224  ILE X CG1 
12310 C CG2 . ILE B 96   ? 3.4270 3.4650 3.6074 0.3356  -0.3084 -0.1134 224  ILE X CG2 
12311 C CD1 . ILE B 96   ? 3.3594 3.4852 3.6144 0.3785  -0.3338 -0.1247 224  ILE X CD1 
12312 N N   . GLU B 97   ? 6.2710 6.2520 6.3535 0.3124  -0.2689 -0.1051 225  GLU X N   
12313 C CA  . GLU B 97   ? 6.3492 6.2976 6.3890 0.2820  -0.2532 -0.0927 225  GLU X CA  
12314 C C   . GLU B 97   ? 6.3477 6.2603 6.3872 0.2647  -0.2567 -0.0892 225  GLU X C   
12315 O O   . GLU B 97   ? 6.3594 6.2484 6.4067 0.2810  -0.2617 -0.0999 225  GLU X O   
12316 C CB  . GLU B 97   ? 4.2890 4.2138 4.2900 0.2923  -0.2380 -0.0980 225  GLU X CB  
12317 C CG  . GLU B 97   ? 4.3475 4.3029 4.3364 0.2995  -0.2299 -0.0969 225  GLU X CG  
12318 C CD  . GLU B 97   ? 4.3806 4.3224 4.3490 0.3248  -0.2221 -0.1086 225  GLU X CD  
12319 O OE1 . GLU B 97   ? 4.3975 4.3053 4.3601 0.3363  -0.2226 -0.1172 225  GLU X OE1 
12320 O OE2 . GLU B 97   ? 4.3903 4.3564 4.3488 0.3333  -0.2156 -0.1090 225  GLU X OE2 
12321 N N   . VAL B 98   ? 4.4320 4.3411 4.4617 0.2312  -0.2536 -0.0739 226  VAL X N   
12322 C CA  . VAL B 98   ? 4.3952 4.2728 4.4243 0.2119  -0.2567 -0.0691 226  VAL X CA  
12323 C C   . VAL B 98   ? 4.4647 4.3029 4.4445 0.1839  -0.2391 -0.0586 226  VAL X C   
12324 O O   . VAL B 98   ? 4.4952 4.3364 4.4437 0.1718  -0.2261 -0.0511 226  VAL X O   
12325 C CB  . VAL B 98   ? 4.7585 4.6611 4.8200 0.1950  -0.2701 -0.0601 226  VAL X CB  
12326 C CG1 . VAL B 98   ? 4.6951 4.5663 4.7606 0.1792  -0.2752 -0.0572 226  VAL X CG1 
12327 C CG2 . VAL B 98   ? 4.7287 4.6716 4.8369 0.2221  -0.2868 -0.0694 226  VAL X CG2 
12328 N N   . THR B 99   ? 3.8504 3.6517 3.8230 0.1738  -0.2390 -0.0581 227  THR X N   
12329 C CA  . THR B 99   ? 3.9197 3.6798 3.8463 0.1472  -0.2232 -0.0486 227  THR X CA  
12330 C C   . THR B 99   ? 3.9126 3.6520 3.8469 0.1259  -0.2289 -0.0424 227  THR X C   
12331 O O   . THR B 99   ? 3.8907 3.6227 3.8513 0.1403  -0.2396 -0.0510 227  THR X O   
12332 C CB  . THR B 99   ? 3.9475 3.6719 3.8436 0.1640  -0.2112 -0.0576 227  THR X CB  
12333 O OG1 . THR B 99   ? 3.9988 3.7419 3.8863 0.1831  -0.2057 -0.0631 227  THR X OG1 
12334 C CG2 . THR B 99   ? 3.9683 3.6488 3.8156 0.1369  -0.1946 -0.0477 227  THR X CG2 
12335 N N   . LEU B 100  ? 5.0298 4.7593 4.9401 0.0912  -0.2218 -0.0274 228  LEU X N   
12336 C CA  . LEU B 100  ? 5.0014 4.7195 4.9225 0.0682  -0.2288 -0.0198 228  LEU X CA  
12337 C C   . LEU B 100  ? 5.0486 4.7156 4.9309 0.0487  -0.2163 -0.0153 228  LEU X C   
12338 O O   . LEU B 100  ? 5.1124 4.7558 4.9497 0.0345  -0.2000 -0.0094 228  LEU X O   
12339 C CB  . LEU B 100  ? 2.5061 2.2540 2.4342 0.0414  -0.2328 -0.0053 228  LEU X CB  
12340 C CG  . LEU B 100  ? 2.4925 2.2933 2.4540 0.0570  -0.2427 -0.0071 228  LEU X CG  
12341 C CD1 . LEU B 100  ? 2.4427 2.2730 2.4225 0.0318  -0.2513 0.0068  228  LEU X CD1 
12342 C CD2 . LEU B 100  ? 2.4607 2.2780 2.4647 0.0934  -0.2572 -0.0229 228  LEU X CD2 
12343 N N   . LYS B 101  ? 5.1278 4.7777 5.0271 0.0477  -0.2241 -0.0179 229  LYS X N   
12344 C CA  . LYS B 101  ? 5.1411 4.7453 5.0067 0.0260  -0.2134 -0.0122 229  LYS X CA  
12345 C C   . LYS B 101  ? 4.9853 4.5894 4.8648 -0.0011 -0.2219 -0.0021 229  LYS X C   
12346 O O   . LYS B 101  ? 4.9022 4.5195 4.8216 0.0080  -0.2373 -0.0066 229  LYS X O   
12347 C CB  . LYS B 101  ? 2.6112 2.1848 2.4743 0.0482  -0.2108 -0.0242 229  LYS X CB  
12348 C CG  . LYS B 101  ? 2.5598 2.0914 2.3985 0.0258  -0.2034 -0.0182 229  LYS X CG  
12349 C CD  . LYS B 101  ? 2.5657 2.0637 2.3938 0.0453  -0.1972 -0.0285 229  LYS X CD  
12350 C CE  . LYS B 101  ? 2.5258 1.9803 2.3212 0.0211  -0.1863 -0.0212 229  LYS X CE  
12351 N NZ  . LYS B 101  ? 2.5369 1.9592 2.3205 0.0403  -0.1791 -0.0305 229  LYS X NZ  
12352 N N   . GLN B 102  ? 4.2279 3.8154 4.0729 -0.0350 -0.2119 0.0116  230  GLN X N   
12353 C CA  . GLN B 102  ? 4.0919 3.6727 3.9422 -0.0637 -0.2176 0.0221  230  GLN X CA  
12354 C C   . GLN B 102  ? 4.0571 3.5867 3.8743 -0.0762 -0.2065 0.0229  230  GLN X C   
12355 O O   . GLN B 102  ? 4.0150 3.5246 3.8072 -0.1082 -0.2008 0.0346  230  GLN X O   
12356 C CB  . GLN B 102  ? 4.0536 3.6517 3.8898 -0.0953 -0.2156 0.0376  230  GLN X CB  
12357 C CG  . GLN B 102  ? 3.9760 3.6288 3.8515 -0.0867 -0.2291 0.0389  230  GLN X CG  
12358 C CD  . GLN B 102  ? 3.9334 3.6042 3.7933 -0.1186 -0.2263 0.0551  230  GLN X CD  
12359 O OE1 . GLN B 102  ? 3.9266 3.5725 3.7575 -0.1509 -0.2197 0.0664  230  GLN X OE1 
12360 N NE2 . GLN B 102  ? 3.9166 3.6311 3.7954 -0.1097 -0.2311 0.0562  230  GLN X NE2 
12361 N N   . THR C 22   ? 4.8337 2.2875 2.4419 -0.3189 0.2102  -0.3203 22   THR B N   
12362 C CA  . THR C 22   ? 4.7785 2.2213 2.3987 -0.3098 0.2093  -0.3231 22   THR B CA  
12363 C C   . THR C 22   ? 4.7512 2.2139 2.3875 -0.3011 0.2125  -0.3291 22   THR B C   
12364 O O   . THR C 22   ? 4.7726 2.2573 2.4104 -0.3009 0.2164  -0.3329 22   THR B O   
12365 C CB  . THR C 22   ? 4.7393 2.1600 2.3581 -0.3044 0.2084  -0.3286 22   THR B CB  
12366 O OG1 . THR C 22   ? 4.7338 2.1591 2.3461 -0.3050 0.2110  -0.3347 22   THR B OG1 
12367 C CG2 . THR C 22   ? 4.7085 2.1050 2.3174 -0.3101 0.2044  -0.3212 22   THR B CG2 
12368 N N   . TYR C 23   ? 4.0419 1.4970 1.6909 -0.2940 0.2109  -0.3298 23   TYR B N   
12369 C CA  . TYR C 23   ? 4.1024 1.5750 1.7691 -0.2867 0.2129  -0.3326 23   TYR B CA  
12370 C C   . TYR C 23   ? 4.0734 1.5403 1.7548 -0.2744 0.2135  -0.3422 23   TYR B C   
12371 O O   . TYR C 23   ? 4.0147 1.4603 1.6954 -0.2714 0.2103  -0.3434 23   TYR B O   
12372 C CB  . TYR C 23   ? 4.1722 1.6463 1.8435 -0.2912 0.2096  -0.3219 23   TYR B CB  
12373 C CG  . TYR C 23   ? 4.2208 1.6704 1.8893 -0.2931 0.2045  -0.3164 23   TYR B CG  
12374 C CD1 . TYR C 23   ? 4.2063 1.6348 1.8707 -0.2895 0.2031  -0.3209 23   TYR B CD1 
12375 C CD2 . TYR C 23   ? 4.2698 1.7181 1.9396 -0.2987 0.2010  -0.3065 23   TYR B CD2 
12376 C CE1 . TYR C 23   ? 4.2032 1.6111 1.8652 -0.2910 0.1989  -0.3159 23   TYR B CE1 
12377 C CE2 . TYR C 23   ? 4.2519 1.6792 1.9185 -0.3006 0.1968  -0.3020 23   TYR B CE2 
12378 C CZ  . TYR C 23   ? 4.2292 1.6369 1.8922 -0.2966 0.1959  -0.3068 23   TYR B CZ  
12379 O OH  . TYR C 23   ? 4.2063 1.5943 1.8663 -0.2985 0.1920  -0.3021 23   TYR B OH  
12380 N N   . VAL C 24   ? 4.1606 1.6472 1.8559 -0.2671 0.2174  -0.3488 24   VAL B N   
12381 C CA  . VAL C 24   ? 4.1094 1.5930 1.8204 -0.2551 0.2181  -0.3585 24   VAL B CA  
12382 C C   . VAL C 24   ? 4.0870 1.5856 1.8188 -0.2493 0.2188  -0.3576 24   VAL B C   
12383 O O   . VAL C 24   ? 4.1205 1.6415 1.8566 -0.2508 0.2223  -0.3559 24   VAL B O   
12384 C CB  . VAL C 24   ? 4.1586 1.6498 1.8673 -0.2499 0.2231  -0.3710 24   VAL B CB  
12385 C CG1 . VAL C 24   ? 4.1695 1.6734 1.8989 -0.2381 0.2261  -0.3803 24   VAL B CG1 
12386 C CG2 . VAL C 24   ? 4.1240 1.5923 1.8220 -0.2493 0.2207  -0.3750 24   VAL B CG2 
12387 N N   . ILE C 25   ? 4.1548 1.6410 1.9003 -0.2426 0.2150  -0.3584 25   ILE B N   
12388 C CA  . ILE C 25   ? 4.2109 1.7078 1.9786 -0.2369 0.2143  -0.3567 25   ILE B CA  
12389 C C   . ILE C 25   ? 4.1718 1.6590 1.9541 -0.2254 0.2129  -0.3663 25   ILE B C   
12390 O O   . ILE C 25   ? 4.1347 1.6028 1.9193 -0.2242 0.2074  -0.3638 25   ILE B O   
12391 C CB  . ILE C 25   ? 4.2552 1.7434 2.0242 -0.2436 0.2085  -0.3435 25   ILE B CB  
12392 C CG1 . ILE C 25   ? 4.3271 1.8204 2.0789 -0.2561 0.2087  -0.3336 25   ILE B CG1 
12393 C CG2 . ILE C 25   ? 4.2773 1.7774 2.0707 -0.2384 0.2073  -0.3408 25   ILE B CG2 
12394 C CD1 . ILE C 25   ? 4.3937 1.9126 2.1533 -0.2580 0.2119  -0.3295 25   ILE B CD1 
12395 N N   . SER C 26   ? 3.8208 1.3212 1.6129 -0.2168 0.2179  -0.3776 26   SER B N   
12396 C CA  . SER C 26   ? 3.7727 1.2634 1.5788 -0.2058 0.2162  -0.3872 26   SER B CA  
12397 C C   . SER C 26   ? 3.7655 1.2613 1.5976 -0.1998 0.2131  -0.3839 26   SER B C   
12398 O O   . SER C 26   ? 3.7803 1.2918 1.6204 -0.2032 0.2142  -0.3762 26   SER B O   
12399 C CB  . SER C 26   ? 3.8492 1.3509 1.6551 -0.1990 0.2228  -0.4014 26   SER B CB  
12400 O OG  . SER C 26   ? 3.8889 1.3971 1.6732 -0.2071 0.2268  -0.4011 26   SER B OG  
12401 N N   . ALA C 27   ? 3.7783 1.2606 1.6237 -0.1916 0.2088  -0.3888 27   ALA B N   
12402 C CA  . ALA C 27   ? 3.7365 1.2249 1.6103 -0.1835 0.2062  -0.3890 27   ALA B CA  
12403 C C   . ALA C 27   ? 3.8907 1.3640 1.7752 -0.1735 0.2024  -0.3984 27   ALA B C   
12404 O O   . ALA C 27   ? 3.8433 1.2988 1.7122 -0.1745 0.2003  -0.4015 27   ALA B O   
12405 C CB  . ALA C 27   ? 3.7140 1.1995 1.5942 -0.1900 0.2003  -0.3746 27   ALA B CB  
12406 N N   . PRO C 28   ? 3.7589 1.2389 1.6707 -0.1639 0.2010  -0.4025 28   PRO B N   
12407 C CA  . PRO C 28   ? 3.7619 1.2286 1.6850 -0.1537 0.1973  -0.4126 28   PRO B CA  
12408 C C   . PRO C 28   ? 3.7644 1.2063 1.6768 -0.1573 0.1893  -0.4070 28   PRO B C   
12409 O O   . PRO C 28   ? 3.7720 1.2075 1.6673 -0.1674 0.1877  -0.3967 28   PRO B O   
12410 C CB  . PRO C 28   ? 3.7359 1.2121 1.6918 -0.1461 0.1945  -0.4116 28   PRO B CB  
12411 C CG  . PRO C 28   ? 3.7636 1.2630 1.7253 -0.1500 0.1999  -0.4056 28   PRO B CG  
12412 C CD  . PRO C 28   ? 3.7594 1.2583 1.6936 -0.1627 0.2019  -0.3967 28   PRO B CD  
12413 N N   . LYS C 29   ? 4.7140 2.1420 2.6360 -0.1491 0.1843  -0.4137 29   LYS B N   
12414 C CA  . LYS C 29   ? 4.6750 2.0811 2.5917 -0.1518 0.1757  -0.4069 29   LYS B CA  
12415 C C   . LYS C 29   ? 4.6603 2.0671 2.6002 -0.1513 0.1682  -0.3971 29   LYS B C   
12416 O O   . LYS C 29   ? 4.6003 1.9932 2.5367 -0.1558 0.1612  -0.3879 29   LYS B O   
12417 C CB  . LYS C 29   ? 4.6812 2.0710 2.5954 -0.1445 0.1729  -0.4173 29   LYS B CB  
12418 C CG  . LYS C 29   ? 4.6708 2.0406 2.5906 -0.1436 0.1624  -0.4110 29   LYS B CG  
12419 C CD  . LYS C 29   ? 5.1823 2.5408 3.0826 -0.1545 0.1597  -0.3983 29   LYS B CD  
12420 C CE  . LYS C 29   ? 5.0401 2.3847 2.9518 -0.1538 0.1493  -0.3898 29   LYS B CE  
12421 N NZ  . LYS C 29   ? 4.9982 2.3338 2.8937 -0.1642 0.1469  -0.3770 29   LYS B NZ  
12422 N N   . ILE C 30   ? 3.6354 1.0593 1.5992 -0.1462 0.1698  -0.3985 30   ILE B N   
12423 C CA  . ILE C 30   ? 3.6002 1.0275 1.5881 -0.1464 0.1628  -0.3885 30   ILE B CA  
12424 C C   . ILE C 30   ? 3.6108 1.0612 1.6128 -0.1477 0.1676  -0.3848 30   ILE B C   
12425 O O   . ILE C 30   ? 3.6498 1.1138 1.6433 -0.1478 0.1764  -0.3903 30   ILE B O   
12426 C CB  . ILE C 30   ? 3.5467 0.9678 1.5609 -0.1354 0.1560  -0.3945 30   ILE B CB  
12427 C CG1 . ILE C 30   ? 3.5337 0.9327 1.5352 -0.1328 0.1513  -0.3995 30   ILE B CG1 
12428 C CG2 . ILE C 30   ? 3.5219 0.9463 1.5609 -0.1370 0.1477  -0.3826 30   ILE B CG2 
12429 C CD1 . ILE C 30   ? 3.5260 0.9100 1.5139 -0.1414 0.1447  -0.3874 30   ILE B CD1 
12430 N N   . PHE C 31   ? 3.5624 1.0177 1.5861 -0.1493 0.1616  -0.3745 31   PHE B N   
12431 C CA  . PHE C 31   ? 3.5581 1.0350 1.6007 -0.1494 0.1648  -0.3701 31   PHE B CA  
12432 C C   . PHE C 31   ? 3.5399 1.0210 1.6181 -0.1400 0.1595  -0.3720 31   PHE B C   
12433 O O   . PHE C 31   ? 3.5173 0.9841 1.6052 -0.1354 0.1518  -0.3737 31   PHE B O   
12434 C CB  . PHE C 31   ? 3.5264 1.0075 1.5627 -0.1623 0.1623  -0.3534 31   PHE B CB  
12435 C CG  . PHE C 31   ? 3.5480 1.0253 1.5503 -0.1726 0.1669  -0.3500 31   PHE B CG  
12436 C CD1 . PHE C 31   ? 3.5151 0.9744 1.4975 -0.1806 0.1620  -0.3431 31   PHE B CD1 
12437 C CD2 . PHE C 31   ? 3.5854 1.0776 1.5766 -0.1743 0.1759  -0.3533 31   PHE B CD2 
12438 C CE1 . PHE C 31   ? 3.5114 0.9669 1.4642 -0.1899 0.1661  -0.3401 31   PHE B CE1 
12439 C CE2 . PHE C 31   ? 3.5915 1.0803 1.5529 -0.1841 0.1793  -0.3497 31   PHE B CE2 
12440 C CZ  . PHE C 31   ? 3.5453 1.0152 1.4879 -0.1917 0.1743  -0.3432 31   PHE B CZ  
12441 N N   . ARG C 32   ? 3.5889 1.0904 1.6872 -0.1375 0.1637  -0.3710 32   ARG B N   
12442 C CA  . ARG C 32   ? 3.5664 1.0752 1.7016 -0.1294 0.1591  -0.3711 32   ARG B CA  
12443 C C   . ARG C 32   ? 3.5257 1.0526 1.6762 -0.1362 0.1589  -0.3571 32   ARG B C   
12444 O O   . ARG C 32   ? 3.5239 1.0612 1.6579 -0.1441 0.1649  -0.3515 32   ARG B O   
12445 C CB  . ARG C 32   ? 3.6657 1.1828 1.8148 -0.1157 0.1661  -0.3880 32   ARG B CB  
12446 C CG  . ARG C 32   ? 3.6785 1.1781 1.8296 -0.1054 0.1627  -0.4021 32   ARG B CG  
12447 C CD  . ARG C 32   ? 3.7499 1.2579 1.9112 -0.0922 0.1710  -0.4208 32   ARG B CD  
12448 N NE  . ARG C 32   ? 3.7169 1.2074 1.8814 -0.0827 0.1667  -0.4335 32   ARG B NE  
12449 C CZ  . ARG C 32   ? 3.7272 1.2094 1.8705 -0.0789 0.1719  -0.4475 32   ARG B CZ  
12450 N NH1 . ARG C 32   ? 3.7649 1.2553 1.8825 -0.0835 0.1818  -0.4511 32   ARG B NH1 
12451 N NH2 . ARG C 32   ? 3.6987 1.1644 1.8469 -0.0710 0.1666  -0.4573 32   ARG B NH2 
12452 N N   . VAL C 33   ? 3.5904 1.1206 1.7730 -0.1333 0.1515  -0.3510 33   VAL B N   
12453 C CA  . VAL C 33   ? 3.6133 1.1622 1.8183 -0.1376 0.1507  -0.3386 33   VAL B CA  
12454 C C   . VAL C 33   ? 3.6926 1.2620 1.9159 -0.1287 0.1598  -0.3466 33   VAL B C   
12455 O O   . VAL C 33   ? 3.7008 1.2701 1.9401 -0.1158 0.1620  -0.3604 33   VAL B O   
12456 C CB  . VAL C 33   ? 3.5784 1.1238 1.8142 -0.1363 0.1393  -0.3308 33   VAL B CB  
12457 C CG1 . VAL C 33   ? 3.6037 1.1642 1.8560 -0.1459 0.1360  -0.3130 33   VAL B CG1 
12458 C CG2 . VAL C 33   ? 3.5215 1.0444 1.7412 -0.1402 0.1309  -0.3288 33   VAL B CG2 
12459 N N   . GLY C 34   ? 3.6587 1.2459 1.8802 -0.1355 0.1650  -0.3375 34   GLY B N   
12460 C CA  . GLY C 34   ? 3.7699 1.3789 2.0092 -0.1279 0.1739  -0.3432 34   GLY B CA  
12461 C C   . GLY C 34   ? 3.8632 1.4728 2.0823 -0.1207 0.1843  -0.3605 34   GLY B C   
12462 O O   . GLY C 34   ? 3.9246 1.5474 2.1600 -0.1099 0.1916  -0.3715 34   GLY B O   
12463 N N   . ALA C 35   ? 3.5231 1.1185 1.7066 -0.1271 0.1850  -0.3626 35   ALA B N   
12464 C CA  . ALA C 35   ? 3.5770 1.1710 1.7380 -0.1221 0.1938  -0.3782 35   ALA B CA  
12465 C C   . ALA C 35   ? 3.6520 1.2576 1.7867 -0.1312 0.2013  -0.3737 35   ALA B C   
12466 O O   . ALA C 35   ? 3.6051 1.2030 1.7180 -0.1433 0.1978  -0.3626 35   ALA B O   
12467 C CB  . ALA C 35   ? 3.5339 1.1030 1.6753 -0.1218 0.1890  -0.3849 35   ALA B CB  
12468 N N   . SER C 36   ? 4.7942 2.4183 2.9310 -0.1253 0.2114  -0.3827 36   SER B N   
12469 C CA  . SER C 36   ? 4.8451 2.4816 2.9570 -0.1331 0.2188  -0.3799 36   SER B CA  
12470 C C   . SER C 36   ? 4.8357 2.4552 2.9116 -0.1384 0.2192  -0.3854 36   SER B C   
12471 O O   . SER C 36   ? 4.8782 2.5016 2.9404 -0.1342 0.2266  -0.3982 36   SER B O   
12472 C CB  . SER C 36   ? 4.8987 2.5586 3.0214 -0.1241 0.2298  -0.3905 36   SER B CB  
12473 O OG  . SER C 36   ? 4.8951 2.5659 3.0553 -0.1146 0.2295  -0.3912 36   SER B OG  
12474 N N   . GLU C 37   ? 4.1966 1.7978 2.2577 -0.1479 0.2113  -0.3754 37   GLU B N   
12475 C CA  . GLU C 37   ? 4.2029 1.7860 2.2320 -0.1530 0.2107  -0.3793 37   GLU B CA  
12476 C C   . GLU C 37   ? 4.2215 1.8152 2.2241 -0.1605 0.2179  -0.3787 37   GLU B C   
12477 O O   . GLU C 37   ? 4.2155 1.8165 2.2092 -0.1710 0.2173  -0.3658 37   GLU B O   
12478 C CB  . GLU C 37   ? 4.2032 1.7657 2.2237 -0.1615 0.2009  -0.3678 37   GLU B CB  
12479 C CG  . GLU C 37   ? 4.2308 1.7819 2.2757 -0.1552 0.1926  -0.3674 37   GLU B CG  
12480 C CD  . GLU C 37   ? 4.2862 1.8243 2.3332 -0.1444 0.1924  -0.3828 37   GLU B CD  
12481 O OE1 . GLU C 37   ? 4.3503 1.8947 2.3896 -0.1386 0.2002  -0.3958 37   GLU B OE1 
12482 O OE2 . GLU C 37   ? 4.2615 1.7834 2.3176 -0.1419 0.1841  -0.3817 37   GLU B OE2 
12483 N N   . ASN C 38   ? 4.0480 1.6423 2.0381 -0.1554 0.2242  -0.3929 38   ASN B N   
12484 C CA  . ASN C 38   ? 4.0572 1.6615 2.0224 -0.1620 0.2308  -0.3938 38   ASN B CA  
12485 C C   . ASN C 38   ? 3.9994 1.5844 1.9349 -0.1730 0.2265  -0.3879 38   ASN B C   
12486 O O   . ASN C 38   ? 3.9573 1.5211 1.8855 -0.1709 0.2225  -0.3930 38   ASN B O   
12487 C CB  . ASN C 38   ? 4.0824 1.6957 2.0460 -0.1529 0.2392  -0.4112 38   ASN B CB  
12488 C CG  . ASN C 38   ? 4.1073 1.7423 2.0992 -0.1423 0.2449  -0.4172 38   ASN B CG  
12489 O OD1 . ASN C 38   ? 4.0889 1.7290 2.1055 -0.1400 0.2415  -0.4095 38   ASN B OD1 
12490 N ND2 . ASN C 38   ? 4.1514 1.7997 2.1402 -0.1359 0.2538  -0.4310 38   ASN B ND2 
12491 N N   . ILE C 39   ? 3.6147 1.2069 1.5339 -0.1845 0.2272  -0.3767 39   ILE B N   
12492 C CA  . ILE C 39   ? 3.5506 1.1255 1.4427 -0.1954 0.2234  -0.3701 39   ILE B CA  
12493 C C   . ILE C 39   ? 3.5637 1.1499 1.4331 -0.2045 0.2281  -0.3672 39   ILE B C   
12494 O O   . ILE C 39   ? 3.5641 1.1606 1.4297 -0.2132 0.2275  -0.3553 39   ILE B O   
12495 C CB  . ILE C 39   ? 3.5406 1.1050 1.4351 -0.2031 0.2156  -0.3556 39   ILE B CB  
12496 C CG1 . ILE C 39   ? 3.5371 1.0927 1.4563 -0.1949 0.2102  -0.3567 39   ILE B CG1 
12497 C CG2 . ILE C 39   ? 3.5391 1.0837 1.4064 -0.2128 0.2121  -0.3508 39   ILE B CG2 
12498 C CD1 . ILE C 39   ? 3.5963 1.1343 1.5154 -0.1863 0.2086  -0.3691 39   ILE B CD1 
12499 N N   . VAL C 40   ? 4.1691 1.7528 2.0233 -0.2028 0.2322  -0.3780 40   VAL B N   
12500 C CA  . VAL C 40   ? 4.2460 1.8407 2.0792 -0.2107 0.2366  -0.3771 40   VAL B CA  
12501 C C   . VAL C 40   ? 4.2614 1.8394 2.0721 -0.2228 0.2315  -0.3671 40   VAL B C   
12502 O O   . VAL C 40   ? 4.1921 1.7465 1.9973 -0.2233 0.2263  -0.3666 40   VAL B O   
12503 C CB  . VAL C 40   ? 4.3365 1.9332 2.1604 -0.2056 0.2423  -0.3921 40   VAL B CB  
12504 C CG1 . VAL C 40   ? 4.3610 1.9696 2.2069 -0.1921 0.2472  -0.4047 40   VAL B CG1 
12505 C CG2 . VAL C 40   ? 4.2859 1.8558 2.0948 -0.2069 0.2380  -0.3956 40   VAL B CG2 
12506 N N   . ILE C 41   ? 4.1756 1.7666 1.9735 -0.2324 0.2332  -0.3592 41   ILE B N   
12507 C CA  . ILE C 41   ? 4.1854 1.7632 1.9605 -0.2442 0.2294  -0.3507 41   ILE B CA  
12508 C C   . ILE C 41   ? 4.2100 1.8021 1.9691 -0.2495 0.2341  -0.3533 41   ILE B C   
12509 O O   . ILE C 41   ? 4.2321 1.8490 1.9965 -0.2495 0.2386  -0.3526 41   ILE B O   
12510 C CB  . ILE C 41   ? 4.2518 1.8312 2.0274 -0.2530 0.2249  -0.3355 41   ILE B CB  
12511 C CG1 . ILE C 41   ? 4.2714 1.8465 2.0230 -0.2659 0.2231  -0.3274 41   ILE B CG1 
12512 C CG2 . ILE C 41   ? 4.3040 1.9098 2.0966 -0.2508 0.2282  -0.3319 41   ILE B CG2 
12513 C CD1 . ILE C 41   ? 4.2974 1.8766 2.0474 -0.2756 0.2191  -0.3126 41   ILE B CD1 
12514 N N   . GLN C 42   ? 4.8809 2.4579 2.6210 -0.2542 0.2329  -0.3556 42   GLN B N   
12515 C CA  . GLN C 42   ? 4.9875 2.5758 2.7110 -0.2606 0.2363  -0.3573 42   GLN B CA  
12516 C C   . GLN C 42   ? 5.0134 2.5810 2.7169 -0.2708 0.2313  -0.3503 42   GLN B C   
12517 O O   . GLN C 42   ? 4.9517 2.4956 2.6545 -0.2696 0.2269  -0.3490 42   GLN B O   
12518 C CB  . GLN C 42   ? 5.0290 2.6213 2.7534 -0.2525 0.2416  -0.3723 42   GLN B CB  
12519 C CG  . GLN C 42   ? 5.0452 2.6281 2.7492 -0.2588 0.2414  -0.3751 42   GLN B CG  
12520 C CD  . GLN C 42   ? 5.0443 2.6148 2.7495 -0.2503 0.2428  -0.3882 42   GLN B CD  
12521 O OE1 . GLN C 42   ? 5.0575 2.6146 2.7478 -0.2545 0.2415  -0.3902 42   GLN B OE1 
12522 N NE2 . GLN C 42   ? 5.0332 2.6074 2.7567 -0.2385 0.2452  -0.3969 42   GLN B NE2 
12523 N N   . VAL C 43   ? 3.9802 1.5563 1.6680 -0.2808 0.2318  -0.3453 43   VAL B N   
12524 C CA  . VAL C 43   ? 3.9256 1.4821 1.5968 -0.2909 0.2265  -0.3369 43   VAL B CA  
12525 C C   . VAL C 43   ? 4.0081 1.5719 1.6623 -0.3009 0.2270  -0.3342 43   VAL B C   
12526 O O   . VAL C 43   ? 4.0693 1.6577 1.7234 -0.3034 0.2303  -0.3339 43   VAL B O   
12527 C CB  . VAL C 43   ? 3.8294 1.3799 1.5030 -0.2962 0.2216  -0.3244 43   VAL B CB  
12528 C CG1 . VAL C 43   ? 3.8487 1.4234 1.5232 -0.3025 0.2224  -0.3161 43   VAL B CG1 
12529 C CG2 . VAL C 43   ? 3.7465 1.2722 1.4048 -0.3043 0.2164  -0.3179 43   VAL B CG2 
12530 N N   . TYR C 44   ? 5.1601 2.7024 2.8006 -0.3066 0.2235  -0.3318 44   TYR B N   
12531 C CA  . TYR C 44   ? 5.2545 2.8000 2.8792 -0.3169 0.2228  -0.3283 44   TYR B CA  
12532 C C   . TYR C 44   ? 5.4873 3.0320 3.1036 -0.3283 0.2182  -0.3149 44   TYR B C   
12533 O O   . TYR C 44   ? 5.4428 2.9798 3.0457 -0.3375 0.2154  -0.3100 44   TYR B O   
12534 C CB  . TYR C 44   ? 5.3377 2.8604 2.9531 -0.3170 0.2215  -0.3325 44   TYR B CB  
12535 C CG  . TYR C 44   ? 5.5188 3.0490 3.1215 -0.3251 0.2223  -0.3327 44   TYR B CG  
12536 C CD1 . TYR C 44   ? 5.6142 3.1618 3.2179 -0.3218 0.2272  -0.3421 44   TYR B CD1 
12537 C CD2 . TYR C 44   ? 5.5789 3.0993 3.1689 -0.3363 0.2180  -0.3235 44   TYR B CD2 
12538 C CE1 . TYR C 44   ? 5.6694 3.2251 3.2617 -0.3301 0.2276  -0.3417 44   TYR B CE1 
12539 C CE2 . TYR C 44   ? 5.6337 3.1617 3.2134 -0.3443 0.2182  -0.3229 44   TYR B CE2 
12540 C CZ  . TYR C 44   ? 5.6708 3.2168 3.2515 -0.3414 0.2228  -0.3317 44   TYR B CZ  
12541 O OH  . TYR C 44   ? 5.6928 3.2474 3.2634 -0.3503 0.2226  -0.3305 44   TYR B OH  
12542 N N   . GLY C 45   ? 4.4368 1.9892 2.0614 -0.3281 0.2170  -0.3087 45   GLY B N   
12543 C CA  . GLY C 45   ? 4.4625 2.0134 2.0793 -0.3388 0.2122  -0.2960 45   GLY B CA  
12544 C C   . GLY C 45   ? 4.5058 2.0778 2.1145 -0.3477 0.2125  -0.2915 45   GLY B C   
12545 O O   . GLY C 45   ? 4.5120 2.1049 2.1242 -0.3445 0.2171  -0.2978 45   GLY B O   
12546 N N   . TYR C 46   ? 4.9687 2.5351 2.5665 -0.3589 0.2073  -0.2807 46   TYR B N   
12547 C CA  . TYR C 46   ? 5.0521 2.6375 2.6419 -0.3689 0.2059  -0.2744 46   TYR B CA  
12548 C C   . TYR C 46   ? 5.0919 2.7034 2.6885 -0.3712 0.2060  -0.2672 46   TYR B C   
12549 O O   . TYR C 46   ? 5.1471 2.7611 2.7548 -0.3652 0.2070  -0.2666 46   TYR B O   
12550 C CB  . TYR C 46   ? 5.0900 2.6567 2.6657 -0.3802 0.1997  -0.2658 46   TYR B CB  
12551 C CG  . TYR C 46   ? 5.1069 2.6532 2.6821 -0.3812 0.1958  -0.2599 46   TYR B CG  
12552 C CD1 . TYR C 46   ? 5.1524 2.7090 2.7304 -0.3852 0.1931  -0.2508 46   TYR B CD1 
12553 C CD2 . TYR C 46   ? 5.0764 2.5939 2.6486 -0.3781 0.1948  -0.2632 46   TYR B CD2 
12554 C CE1 . TYR C 46   ? 5.1454 2.6835 2.7222 -0.3869 0.1894  -0.2455 46   TYR B CE1 
12555 C CE2 . TYR C 46   ? 5.0677 2.5674 2.6390 -0.3793 0.1915  -0.2581 46   TYR B CE2 
12556 C CZ  . TYR C 46   ? 5.1067 2.6167 2.6799 -0.3839 0.1888  -0.2494 46   TYR B CZ  
12557 O OH  . TYR C 46   ? 5.0996 2.5922 2.6711 -0.3860 0.1853  -0.2443 46   TYR B OH  
12558 N N   . THR C 47   ? 6.7739 4.4045 4.3639 -0.3803 0.2043  -0.2609 47   THR B N   
12559 C CA  . THR C 47   ? 6.7651 4.4261 4.3615 -0.3823 0.2052  -0.2548 47   THR B CA  
12560 C C   . THR C 47   ? 6.7371 4.3978 4.3420 -0.3807 0.2033  -0.2477 47   THR B C   
12561 O O   . THR C 47   ? 6.7539 4.4385 4.3698 -0.3772 0.2062  -0.2459 47   THR B O   
12562 C CB  . THR C 47   ? 6.8994 5.1064 5.0284 -0.3003 0.1472  -0.2352 47   THR B CB  
12563 O OG1 . THR C 47   ? 6.8981 5.0984 5.0115 -0.3036 0.1489  -0.2408 47   THR B OG1 
12564 C CG2 . THR C 47   ? 6.9005 5.1919 5.0886 -0.2907 0.1433  -0.2284 47   THR B CG2 
12565 N N   . GLU C 48   ? 5.8773 3.5112 3.4774 -0.3834 0.1986  -0.2433 48   GLU B N   
12566 C CA  . GLU C 48   ? 5.8606 3.4921 3.4674 -0.3834 0.1960  -0.2358 48   GLU B CA  
12567 C C   . GLU C 48   ? 5.7998 3.4380 3.4244 -0.3707 0.2014  -0.2431 48   GLU B C   
12568 O O   . GLU C 48   ? 5.7545 3.3738 3.3829 -0.3631 0.2030  -0.2512 48   GLU B O   
12569 C CB  . GLU C 48   ? 5.8374 3.4373 3.4345 -0.3885 0.1904  -0.2315 48   GLU B CB  
12570 C CG  . GLU C 48   ? 5.8454 3.4433 3.4452 -0.3927 0.1862  -0.2210 48   GLU B CG  
12571 C CD  . GLU C 48   ? 5.8906 3.5104 3.4875 -0.4021 0.1827  -0.2092 48   GLU B CD  
12572 O OE1 . GLU C 48   ? 5.9021 3.5324 3.4910 -0.4080 0.1818  -0.2077 48   GLU B OE1 
12573 O OE2 . GLU C 48   ? 5.9076 3.5346 3.5106 -0.4041 0.1805  -0.2007 48   GLU B OE2 
12574 N N   . ALA C 49   ? 5.5905 3.2558 3.2267 -0.3685 0.2039  -0.2398 49   ALA B N   
12575 C CA  . ALA C 49   ? 5.5394 3.2120 3.1946 -0.3571 0.2084  -0.2450 49   ALA B CA  
12576 C C   . ALA C 49   ? 5.4766 3.1263 3.1344 -0.3575 0.2039  -0.2401 49   ALA B C   
12577 O O   . ALA C 49   ? 5.4825 3.1192 3.1287 -0.3677 0.1977  -0.2302 49   ALA B O   
12578 C CB  . ALA C 49   ? 5.5870 3.2921 3.2537 -0.3567 0.2109  -0.2391 49   ALA B CB  
12579 N N   . PHE C 50   ? 5.7628 3.4074 3.4358 -0.3468 0.2068  -0.2471 50   PHE B N   
12580 C CA  . PHE C 50   ? 5.7328 3.3562 3.4086 -0.3474 0.2023  -0.2426 50   PHE B CA  
12581 C C   . PHE C 50   ? 5.6541 3.2804 3.3518 -0.3363 0.2049  -0.2472 50   PHE B C   
12582 O O   . PHE C 50   ? 5.6242 3.2583 3.3329 -0.3255 0.2105  -0.2585 50   PHE B O   
12583 C CB  . PHE C 50   ? 5.7862 3.3789 3.4468 -0.3504 0.1992  -0.2457 50   PHE B CB  
12584 C CG  . PHE C 50   ? 5.8627 3.4457 3.5256 -0.3406 0.2033  -0.2596 50   PHE B CG  
12585 C CD1 . PHE C 50   ? 5.8677 3.4302 3.5365 -0.3343 0.2024  -0.2644 50   PHE B CD1 
12586 C CD2 . PHE C 50   ? 5.9384 3.5328 3.5972 -0.3385 0.2076  -0.2674 50   PHE B CD2 
12587 C CE1 . PHE C 50   ? 5.8683 3.4214 3.5390 -0.3256 0.2055  -0.2764 50   PHE B CE1 
12588 C CE2 . PHE C 50   ? 5.9325 3.5170 3.5926 -0.3301 0.2110  -0.2797 50   PHE B CE2 
12589 C CZ  . PHE C 50   ? 5.8980 3.4616 3.5640 -0.3236 0.2098  -0.2841 50   PHE B CZ  
12590 N N   . ASP C 51   ? 4.5929 2.2126 2.2965 -0.3395 0.2005  -0.2381 51   ASP B N   
12591 C CA  . ASP C 51   ? 4.5604 2.1849 2.2865 -0.3309 0.2017  -0.2393 51   ASP B CA  
12592 C C   . ASP C 51   ? 4.5043 2.1080 2.2364 -0.3222 0.2019  -0.2493 51   ASP B C   
12593 O O   . ASP C 51   ? 4.4813 2.0621 2.1985 -0.3250 0.1995  -0.2520 51   ASP B O   
12594 C CB  . ASP C 51   ? 4.5424 2.1678 2.2725 -0.3389 0.1962  -0.2248 51   ASP B CB  
12595 C CG  . ASP C 51   ? 4.5628 2.2175 2.3075 -0.3387 0.1982  -0.2175 51   ASP B CG  
12596 O OD1 . ASP C 51   ? 4.5727 2.2476 2.3162 -0.3374 0.2026  -0.2201 51   ASP B OD1 
12597 O OD2 . ASP C 51   ? 4.5647 2.2230 2.3225 -0.3403 0.1953  -0.2086 51   ASP B OD2 
12598 N N   . ALA C 52   ? 5.1049 2.7170 2.8596 -0.3117 0.2045  -0.2542 52   ALA B N   
12599 C CA  . ALA C 52   ? 5.0132 2.6085 2.7770 -0.3022 0.2045  -0.2638 52   ALA B CA  
12600 C C   . ALA C 52   ? 4.9878 2.5902 2.7781 -0.2947 0.2039  -0.2627 52   ALA B C   
12601 O O   . ALA C 52   ? 5.0175 2.6393 2.8257 -0.2860 0.2088  -0.2679 52   ALA B O   
12602 C CB  . ALA C 52   ? 4.9820 2.5780 2.7435 -0.2935 0.2100  -0.2785 52   ALA B CB  
12603 N N   . THR C 53   ? 4.6415 2.2280 2.4347 -0.2982 0.1980  -0.2560 53   THR B N   
12604 C CA  . THR C 53   ? 4.5995 2.1895 2.4182 -0.2919 0.1962  -0.2545 53   THR B CA  
12605 C C   . THR C 53   ? 4.5160 2.0850 2.3395 -0.2852 0.1937  -0.2620 53   THR B C   
12606 O O   . THR C 53   ? 4.4701 2.0179 2.2788 -0.2912 0.1893  -0.2592 53   THR B O   
12607 C CB  . THR C 53   ? 4.6736 2.2656 2.4961 -0.3019 0.1905  -0.2387 53   THR B CB  
12608 O OG1 . THR C 53   ? 4.7287 2.3457 2.5594 -0.3042 0.1929  -0.2315 53   THR B OG1 
12609 C CG2 . THR C 53   ? 4.6328 2.2195 2.4773 -0.2971 0.1866  -0.2371 53   THR B CG2 
12610 N N   . ILE C 54   ? 3.9379 1.5131 1.7827 -0.2729 0.1963  -0.2711 54   ILE B N   
12611 C CA  . ILE C 54   ? 3.8693 1.4268 1.7220 -0.2655 0.1934  -0.2781 54   ILE B CA  
12612 C C   . ILE C 54   ? 3.8205 1.3819 1.6983 -0.2637 0.1888  -0.2712 54   ILE B C   
12613 O O   . ILE C 54   ? 3.8089 1.3892 1.7008 -0.2653 0.1895  -0.2638 54   ILE B O   
12614 C CB  . ILE C 54   ? 3.9074 1.4684 1.7683 -0.2525 0.1988  -0.2938 54   ILE B CB  
12615 C CG1 . ILE C 54   ? 3.9385 1.5040 1.7786 -0.2542 0.2045  -0.3002 54   ILE B CG1 
12616 C CG2 . ILE C 54   ? 3.8483 1.3884 1.7129 -0.2459 0.1952  -0.3009 54   ILE B CG2 
12617 C CD1 . ILE C 54   ? 3.9446 1.5177 1.7924 -0.2422 0.2106  -0.3156 54   ILE B CD1 
12618 N N   . SER C 55   ? 3.7551 1.2993 1.6391 -0.2606 0.1839  -0.2730 55   SER B N   
12619 C CA  . SER C 55   ? 3.7703 1.3175 1.6805 -0.2579 0.1789  -0.2675 55   SER B CA  
12620 C C   . SER C 55   ? 3.7507 1.2784 1.6659 -0.2529 0.1739  -0.2721 55   SER B C   
12621 O O   . SER C 55   ? 3.7064 1.2165 1.6029 -0.2529 0.1738  -0.2780 55   SER B O   
12622 C CB  . SER C 55   ? 3.8019 1.3536 1.7118 -0.2703 0.1742  -0.2511 55   SER B CB  
12623 O OG  . SER C 55   ? 3.7998 1.3328 1.6847 -0.2810 0.1705  -0.2455 55   SER B OG  
12624 N N   . ILE C 56   ? 4.5402 2.0719 2.4818 -0.2492 0.1693  -0.2683 56   ILE B N   
12625 C CA  . ILE C 56   ? 4.5874 2.1050 2.5404 -0.2424 0.1643  -0.2732 56   ILE B CA  
12626 C C   . ILE C 56   ? 4.6154 2.1249 2.5725 -0.2511 0.1559  -0.2605 56   ILE B C   
12627 O O   . ILE C 56   ? 4.6072 2.1291 2.5841 -0.2541 0.1527  -0.2510 56   ILE B O   
12628 C CB  . ILE C 56   ? 4.6490 2.1791 2.6327 -0.2294 0.1657  -0.2809 56   ILE B CB  
12629 C CG1 . ILE C 56   ? 4.7222 2.2746 2.7270 -0.2315 0.1664  -0.2718 56   ILE B CG1 
12630 C CG2 . ILE C 56   ? 4.7694 2.3030 2.7463 -0.2200 0.1737  -0.2959 56   ILE B CG2 
12631 C CD1 . ILE C 56   ? 4.7752 2.3437 2.8074 -0.2183 0.1708  -0.2809 56   ILE B CD1 
12632 N N   . LYS C 57   ? 4.8537 2.3430 2.7922 -0.2555 0.1524  -0.2600 57   LYS B N   
12633 C CA  . LYS C 57   ? 4.8753 2.3566 2.8132 -0.2652 0.1450  -0.2480 57   LYS B CA  
12634 C C   . LYS C 57   ? 4.8445 2.3102 2.7892 -0.2605 0.1390  -0.2507 57   LYS B C   
12635 O O   . LYS C 57   ? 4.8443 2.2989 2.7824 -0.2526 0.1408  -0.2614 57   LYS B O   
12636 C CB  . LYS C 57   ? 4.8780 2.3511 2.7857 -0.2784 0.1458  -0.2410 57   LYS B CB  
12637 C CG  . LYS C 57   ? 4.9150 2.4047 2.8197 -0.2856 0.1490  -0.2338 57   LYS B CG  
12638 C CD  . LYS C 57   ? 4.9178 2.3986 2.7913 -0.2975 0.1502  -0.2289 57   LYS B CD  
12639 C CE  . LYS C 57   ? 4.9675 2.4657 2.8385 -0.3036 0.1534  -0.2224 57   LYS B CE  
12640 N NZ  . LYS C 57   ? 4.9904 2.4798 2.8310 -0.3147 0.1545  -0.2186 57   LYS B NZ  
12641 N N   . SER C 58   ? 5.2493 2.7151 3.2072 -0.2661 0.1315  -0.2402 58   SER B N   
12642 C CA  . SER C 58   ? 5.2161 2.6727 3.1890 -0.2615 0.1243  -0.2406 58   SER B CA  
12643 C C   . SER C 58   ? 5.1564 2.5923 3.1066 -0.2662 0.1216  -0.2400 58   SER B C   
12644 O O   . SER C 58   ? 5.1670 2.5971 3.0952 -0.2774 0.1221  -0.2333 58   SER B O   
12645 C CB  . SER C 58   ? 5.2310 2.6990 3.2300 -0.2661 0.1170  -0.2286 58   SER B CB  
12646 O OG  . SER C 58   ? 5.2648 2.7350 3.2504 -0.2806 0.1157  -0.2162 58   SER B OG  
12647 N N   . TYR C 59   ? 4.4901 1.9153 2.4473 -0.2577 0.1183  -0.2464 59   TYR B N   
12648 C CA  . TYR C 59   ? 4.4443 1.8495 2.3807 -0.2591 0.1168  -0.2484 59   TYR B CA  
12649 C C   . TYR C 59   ? 4.8205 2.2156 2.7255 -0.2713 0.1193  -0.2428 59   TYR B C   
12650 O O   . TYR C 59   ? 4.8783 2.2741 2.7651 -0.2734 0.1262  -0.2464 59   TYR B O   
12651 C CB  . TYR C 59   ? 4.3718 1.7706 2.3259 -0.2550 0.1081  -0.2462 59   TYR B CB  
12652 C CG  . TYR C 59   ? 4.3155 1.6954 2.2535 -0.2507 0.1081  -0.2527 59   TYR B CG  
12653 C CD1 . TYR C 59   ? 4.3254 1.6986 2.2467 -0.2452 0.1152  -0.2634 59   TYR B CD1 
12654 C CD2 . TYR C 59   ? 4.2492 1.6186 2.1886 -0.2525 0.1009  -0.2475 59   TYR B CD2 
12655 C CE1 . TYR C 59   ? 4.2834 1.6395 2.1902 -0.2416 0.1153  -0.2685 59   TYR B CE1 
12656 C CE2 . TYR C 59   ? 4.2078 1.5602 2.1325 -0.2485 0.1011  -0.2527 59   TYR B CE2 
12657 C CZ  . TYR C 59   ? 4.2254 1.5709 2.1340 -0.2430 0.1083  -0.2631 59   TYR B CZ  
12658 O OH  . TYR C 59   ? 4.1880 1.5169 2.0824 -0.2393 0.1085  -0.2676 59   TYR B OH  
12659 N N   . PRO C 60   ? 4.4277 1.8135 2.3261 -0.2792 0.1139  -0.2346 60   PRO B N   
12660 C CA  . PRO C 60   ? 4.3959 1.7701 2.2633 -0.2893 0.1171  -0.2316 60   PRO B CA  
12661 C C   . PRO C 60   ? 4.3778 1.7605 2.2350 -0.3015 0.1191  -0.2234 60   PRO B C   
12662 O O   . PRO C 60   ? 4.3859 1.7615 2.2179 -0.3072 0.1240  -0.2244 60   PRO B O   
12663 C CB  . PRO C 60   ? 4.3637 1.7254 2.2281 -0.2927 0.1111  -0.2266 60   PRO B CB  
12664 C CG  . PRO C 60   ? 4.3301 1.6940 2.2205 -0.2821 0.1054  -0.2296 60   PRO B CG  
12665 C CD  . PRO C 60   ? 4.3655 1.7480 2.2802 -0.2785 0.1053  -0.2294 60   PRO B CD  
12666 N N   . ASP C 61   ? 4.4236 1.8211 2.3007 -0.3055 0.1148  -0.2148 61   ASP B N   
12667 C CA  . ASP C 61   ? 4.4327 1.8396 2.3029 -0.3169 0.1158  -0.2061 61   ASP B CA  
12668 C C   . ASP C 61   ? 4.4552 1.8767 2.3317 -0.3125 0.1214  -0.2098 61   ASP B C   
12669 O O   . ASP C 61   ? 4.4525 1.8892 2.3555 -0.3066 0.1200  -0.2093 61   ASP B O   
12670 C CB  . ASP C 61   ? 4.4326 1.8496 2.3223 -0.3241 0.1083  -0.1940 61   ASP B CB  
12671 C CG  . ASP C 61   ? 4.4481 1.8809 2.3729 -0.3150 0.1054  -0.1944 61   ASP B CG  
12672 O OD1 . ASP C 61   ? 4.4968 1.9455 2.4337 -0.3157 0.1072  -0.1911 61   ASP B OD1 
12673 O OD2 . ASP C 61   ? 4.3999 1.8287 2.3404 -0.3069 0.1012  -0.1980 61   ASP B OD2 
12674 N N   . LYS C 62   ? 5.0269 2.4449 2.8803 -0.3152 0.1276  -0.2134 62   LYS B N   
12675 C CA  . LYS C 62   ? 5.0637 2.4970 2.9220 -0.3119 0.1328  -0.2162 62   LYS B CA  
12676 C C   . LYS C 62   ? 5.0995 2.5498 2.9702 -0.3200 0.1304  -0.2044 62   LYS B C   
12677 O O   . LYS C 62   ? 5.1713 2.6293 3.0313 -0.3258 0.1337  -0.2011 62   LYS B O   
12678 C CB  . LYS C 62   ? 5.0494 2.4757 2.8801 -0.3140 0.1392  -0.2217 62   LYS B CB  
12679 C CG  . LYS C 62   ? 4.9735 2.3909 2.7994 -0.3029 0.1433  -0.2349 62   LYS B CG  
12680 C CD  . LYS C 62   ? 4.9185 2.3237 2.7148 -0.3075 0.1477  -0.2382 62   LYS B CD  
12681 C CE  . LYS C 62   ? 4.8365 2.2305 2.6279 -0.2978 0.1506  -0.2497 62   LYS B CE  
12682 N NZ  . LYS C 62   ? 4.8049 2.1843 2.5684 -0.3032 0.1537  -0.2515 62   LYS B NZ  
12683 N N   . LYS C 63   ? 5.3127 2.7691 3.2065 -0.3208 0.1240  -0.1974 63   LYS B N   
12684 C CA  . LYS C 63   ? 5.3271 2.7994 3.2349 -0.3292 0.1207  -0.1847 63   LYS B CA  
12685 C C   . LYS C 63   ? 5.3254 2.8186 3.2607 -0.3209 0.1229  -0.1858 63   LYS B C   
12686 O O   . LYS C 63   ? 5.3744 2.8799 3.3067 -0.3245 0.1265  -0.1821 63   LYS B O   
12687 C CB  . LYS C 63   ? 5.3052 2.7748 3.2237 -0.3365 0.1122  -0.1746 63   LYS B CB  
12688 C CG  . LYS C 63   ? 5.3255 2.7779 3.2157 -0.3480 0.1102  -0.1707 63   LYS B CG  
12689 C CD  . LYS C 63   ? 5.4106 2.8623 3.2755 -0.3588 0.1138  -0.1663 63   LYS B CD  
12690 C CE  . LYS C 63   ? 5.4595 2.9291 3.3378 -0.3673 0.1110  -0.1536 63   LYS B CE  
12691 N NZ  . LYS C 63   ? 5.5200 2.9899 3.3749 -0.3771 0.1142  -0.1494 63   LYS B NZ  
12692 N N   . PHE C 64   ? 4.4086 1.9060 2.3709 -0.3098 0.1207  -0.1907 64   PHE B N   
12693 C CA  . PHE C 64   ? 4.3904 1.9069 2.3797 -0.3006 0.1235  -0.1932 64   PHE B CA  
12694 C C   . PHE C 64   ? 4.4242 1.9431 2.4015 -0.2922 0.1326  -0.2056 64   PHE B C   
12695 O O   . PHE C 64   ? 4.4084 1.9128 2.3676 -0.2876 0.1355  -0.2160 64   PHE B O   
12696 C CB  . PHE C 64   ? 4.3172 1.8358 2.3380 -0.2902 0.1188  -0.1967 64   PHE B CB  
12697 C CG  . PHE C 64   ? 4.2825 1.8186 2.3356 -0.2927 0.1137  -0.1853 64   PHE B CG  
12698 C CD1 . PHE C 64   ? 4.2203 1.7535 2.2876 -0.2984 0.1044  -0.1758 64   PHE B CD1 
12699 C CD2 . PHE C 64   ? 4.3020 1.8578 2.3721 -0.2894 0.1180  -0.1837 64   PHE B CD2 
12700 C CE1 . PHE C 64   ? 4.2031 1.7525 2.3013 -0.3013 0.0991  -0.1645 64   PHE B CE1 
12701 C CE2 . PHE C 64   ? 4.2859 1.8577 2.3872 -0.2917 0.1132  -0.1725 64   PHE B CE2 
12702 C CZ  . PHE C 64   ? 4.2375 1.8059 2.3532 -0.2979 0.1035  -0.1628 64   PHE B CZ  
12703 N N   . SER C 65   ? 5.0932 2.6310 3.0807 -0.2908 0.1370  -0.2038 65   SER B N   
12704 C CA  . SER C 65   ? 5.1419 2.6861 3.1223 -0.2825 0.1456  -0.2151 65   SER B CA  
12705 C C   . SER C 65   ? 5.1657 2.7318 3.1773 -0.2737 0.1483  -0.2162 65   SER B C   
12706 O O   . SER C 65   ? 5.2143 2.7968 3.2354 -0.2794 0.1484  -0.2058 65   SER B O   
12707 C CB  . SER C 65   ? 5.2113 2.7562 3.1629 -0.2924 0.1495  -0.2112 65   SER B CB  
12708 O OG  . SER C 65   ? 5.2726 2.8362 3.2333 -0.2989 0.1497  -0.1999 65   SER B OG  
12709 N N   . TYR C 66   ? 4.7937 2.3594 2.8214 -0.2597 0.1503  -0.2289 66   TYR B N   
12710 C CA  . TYR C 66   ? 4.7474 2.3314 2.8080 -0.2496 0.1524  -0.2315 66   TYR B CA  
12711 C C   . TYR C 66   ? 4.8126 2.4158 2.8710 -0.2477 0.1610  -0.2335 66   TYR B C   
12712 O O   . TYR C 66   ? 4.8332 2.4555 2.9127 -0.2483 0.1616  -0.2256 66   TYR B O   
12713 C CB  . TYR C 66   ? 4.6234 2.1991 2.6980 -0.2355 0.1522  -0.2457 66   TYR B CB  
12714 C CG  . TYR C 66   ? 4.4751 2.0302 2.5449 -0.2381 0.1441  -0.2442 66   TYR B CG  
12715 C CD1 . TYR C 66   ? 4.4022 1.9581 2.4960 -0.2404 0.1355  -0.2347 66   TYR B CD1 
12716 C CD2 . TYR C 66   ? 4.4149 1.9505 2.4566 -0.2388 0.1449  -0.2513 66   TYR B CD2 
12717 C CE1 . TYR C 66   ? 4.3071 1.8458 2.3969 -0.2432 0.1279  -0.2326 66   TYR B CE1 
12718 C CE2 . TYR C 66   ? 4.3252 1.8430 2.3630 -0.2411 0.1376  -0.2493 66   TYR B CE2 
12719 C CZ  . TYR C 66   ? 4.2594 1.7792 2.3212 -0.2433 0.1291  -0.2400 66   TYR B CZ  
12720 O OH  . TYR C 66   ? 4.1521 1.6560 2.2111 -0.2459 0.1216  -0.2373 66   TYR B OH  
12721 N N   . SER C 67   ? 4.0940 1.6926 2.1269 -0.2461 0.1673  -0.2431 67   SER B N   
12722 C CA  . SER C 67   ? 4.1287 1.7452 2.1550 -0.2459 0.1753  -0.2445 67   SER B CA  
12723 C C   . SER C 67   ? 4.1051 1.7119 2.0969 -0.2493 0.1796  -0.2511 67   SER B C   
12724 O O   . SER C 67   ? 4.0527 1.6387 2.0269 -0.2505 0.1771  -0.2558 67   SER B O   
12725 C CB  . SER C 67   ? 4.1480 1.7816 2.2002 -0.2315 0.1815  -0.2549 67   SER B CB  
12726 O OG  . SER C 67   ? 4.1141 1.7372 2.1617 -0.2206 0.1847  -0.2718 67   SER B OG  
12727 N N   . SER C 68   ? 4.4900 2.1128 2.4731 -0.2510 0.1858  -0.2509 68   SER B N   
12728 C CA  . SER C 68   ? 4.5330 2.1494 2.4842 -0.2568 0.1890  -0.2540 68   SER B CA  
12729 C C   . SER C 68   ? 4.6090 2.2468 2.5599 -0.2527 0.1973  -0.2590 68   SER B C   
12730 O O   . SER C 68   ? 4.5981 2.2538 2.5734 -0.2436 0.2012  -0.2625 68   SER B O   
12731 C CB  . SER C 68   ? 4.5588 2.1703 2.4916 -0.2724 0.1843  -0.2391 68   SER B CB  
12732 O OG  . SER C 68   ? 4.6149 2.2485 2.5577 -0.2767 0.1856  -0.2286 68   SER B OG  
12733 N N   . GLY C 69   ? 4.4358 2.0728 2.3599 -0.2596 0.1998  -0.2589 69   GLY B N   
12734 C CA  . GLY C 69   ? 4.5419 2.1996 2.4631 -0.2568 0.2074  -0.2635 69   GLY B CA  
12735 C C   . GLY C 69   ? 4.5929 2.2488 2.4842 -0.2675 0.2080  -0.2595 69   GLY B C   
12736 O O   . GLY C 69   ? 4.5672 2.2050 2.4373 -0.2698 0.2071  -0.2651 69   GLY B O   
12737 N N   . HIS C 70   ? 5.6752 3.3505 3.5659 -0.2742 0.2091  -0.2491 70   HIS B N   
12738 C CA  . HIS C 70   ? 5.7318 3.4073 3.5961 -0.2853 0.2086  -0.2433 70   HIS B CA  
12739 C C   . HIS C 70   ? 5.7226 3.4123 3.5798 -0.2801 0.2161  -0.2541 70   HIS B C   
12740 O O   . HIS C 70   ? 5.7455 3.4598 3.6086 -0.2799 0.2203  -0.2508 70   HIS B O   
12741 C CB  . HIS C 70   ? 5.8466 3.5367 3.7136 -0.2955 0.2055  -0.2263 70   HIS B CB  
12742 C CG  . HIS C 70   ? 5.9460 3.6263 3.7857 -0.3099 0.2008  -0.2167 70   HIS B CG  
12743 N ND1 . HIS C 70   ? 5.9523 3.6114 3.7815 -0.3192 0.1936  -0.2085 70   HIS B ND1 
12744 C CD2 . HIS C 70   ? 6.0354 3.7242 3.8566 -0.3167 0.2022  -0.2140 70   HIS B CD2 
12745 C CE1 . HIS C 70   ? 5.9959 3.6499 3.8012 -0.3308 0.1909  -0.2018 70   HIS B CE1 
12746 N NE2 . HIS C 70   ? 6.0469 3.7188 3.8474 -0.3296 0.1957  -0.2046 70   HIS B NE2 
12747 N N   . VAL C 71   ? 4.6743 2.3489 2.5188 -0.2760 0.2179  -0.2665 71   VAL B N   
12748 C CA  . VAL C 71   ? 4.6926 2.3800 2.5313 -0.2706 0.2250  -0.2780 71   VAL B CA  
12749 C C   . VAL C 71   ? 4.7070 2.3890 2.5171 -0.2807 0.2242  -0.2762 71   VAL B C   
12750 O O   . VAL C 71   ? 4.6622 2.3233 2.4569 -0.2817 0.2226  -0.2823 71   VAL B O   
12751 C CB  . VAL C 71   ? 4.6334 2.3120 2.4817 -0.2575 0.2285  -0.2944 71   VAL B CB  
12752 C CG1 . VAL C 71   ? 4.6282 2.3213 2.5074 -0.2465 0.2313  -0.2973 71   VAL B CG1 
12753 C CG2 . VAL C 71   ? 4.5638 2.2120 2.4037 -0.2589 0.2225  -0.2959 71   VAL B CG2 
12754 N N   . HIS C 72   ? 4.6674 2.3690 2.4715 -0.2882 0.2250  -0.2672 72   HIS B N   
12755 C CA  . HIS C 72   ? 4.7288 2.4272 2.5076 -0.2993 0.2230  -0.2628 72   HIS B CA  
12756 C C   . HIS C 72   ? 4.7461 2.4526 2.5153 -0.2959 0.2288  -0.2746 72   HIS B C   
12757 O O   . HIS C 72   ? 4.7843 2.5154 2.5632 -0.2901 0.2351  -0.2794 72   HIS B O   
12758 C CB  . HIS C 72   ? 4.8482 2.5645 2.6240 -0.3096 0.2205  -0.2475 72   HIS B CB  
12759 C CG  . HIS C 72   ? 4.9439 2.6618 2.6964 -0.3202 0.2189  -0.2435 72   HIS B CG  
12760 N ND1 . HIS C 72   ? 4.9570 2.6542 2.6902 -0.3316 0.2120  -0.2357 72   HIS B ND1 
12761 C CD2 . HIS C 72   ? 5.0178 2.7558 2.7637 -0.3212 0.2231  -0.2464 72   HIS B CD2 
12762 C CE1 . HIS C 72   ? 5.0024 2.7066 2.7191 -0.3390 0.2117  -0.2336 72   HIS B CE1 
12763 N NE2 . HIS C 72   ? 5.0388 2.7681 2.7626 -0.3332 0.2182  -0.2397 72   HIS B NE2 
12764 N N   . LEU C 73   ? 4.7219 2.4080 2.4718 -0.3001 0.2266  -0.2785 73   LEU B N   
12765 C CA  . LEU C 73   ? 4.7652 2.4564 2.5034 -0.2989 0.2309  -0.2885 73   LEU B CA  
12766 C C   . LEU C 73   ? 4.8532 2.5531 2.5726 -0.3115 0.2288  -0.2800 73   LEU B C   
12767 O O   . LEU C 73   ? 4.8508 2.5458 2.5627 -0.3216 0.2230  -0.2670 73   LEU B O   
12768 C CB  . LEU C 73   ? 4.6718 2.3358 2.4020 -0.2954 0.2298  -0.2983 73   LEU B CB  
12769 C CG  . LEU C 73   ? 4.5957 2.2312 2.3196 -0.3003 0.2227  -0.2915 73   LEU B CG  
12770 C CD1 . LEU C 73   ? 4.5417 2.1534 2.2505 -0.3010 0.2215  -0.2984 73   LEU B CD1 
12771 C CD2 . LEU C 73   ? 4.5570 2.1872 2.3011 -0.2926 0.2215  -0.2916 73   LEU B CD2 
12772 N N   . SER C 74   ? 5.4470 3.1600 3.1589 -0.3111 0.2333  -0.2873 74   SER B N   
12773 C CA  . SER C 74   ? 5.5296 3.2527 3.2248 -0.3228 0.2312  -0.2799 74   SER B CA  
12774 C C   . SER C 74   ? 5.5925 3.3246 3.2801 -0.3208 0.2363  -0.2911 74   SER B C   
12775 O O   . SER C 74   ? 5.6195 3.3522 3.3155 -0.3100 0.2419  -0.3044 74   SER B O   
12776 C CB  . SER C 74   ? 5.5666 3.3177 3.2683 -0.3272 0.2313  -0.2687 74   SER B CB  
12777 O OG  . SER C 74   ? 5.5845 3.3639 3.2976 -0.3194 0.2392  -0.2762 74   SER B OG  
12778 N N   . SER C 75   ? 4.9855 2.7242 2.6573 -0.3315 0.2339  -0.2856 75   SER B N   
12779 C CA  . SER C 75   ? 5.0496 2.8000 2.7136 -0.3316 0.2383  -0.2945 75   SER B CA  
12780 C C   . SER C 75   ? 5.1022 2.8843 2.7792 -0.3237 0.2464  -0.3014 75   SER B C   
12781 O O   . SER C 75   ? 5.1012 2.8933 2.7754 -0.3202 0.2518  -0.3125 75   SER B O   
12782 C CB  . SER C 75   ? 5.1255 2.8799 2.7721 -0.3458 0.2333  -0.2851 75   SER B CB  
12783 O OG  . SER C 75   ? 5.1127 2.8370 2.7465 -0.3514 0.2277  -0.2835 75   SER B OG  
12784 N N   . GLU C 76   ? 5.8084 3.6064 3.4996 -0.3210 0.2473  -0.2946 76   GLU B N   
12785 C CA  . GLU C 76   ? 5.8198 3.6473 3.5264 -0.3120 0.2554  -0.3009 76   GLU B CA  
12786 C C   . GLU C 76   ? 5.7175 3.5347 3.4382 -0.2975 0.2607  -0.3157 76   GLU B C   
12787 O O   . GLU C 76   ? 5.7499 3.5845 3.4787 -0.2888 0.2686  -0.3275 76   GLU B O   
12788 C CB  . GLU C 76   ? 5.8785 3.7242 3.5975 -0.3136 0.2542  -0.2880 76   GLU B CB  
12789 C CG  . GLU C 76   ? 5.9199 3.7945 3.6580 -0.3028 0.2631  -0.2944 76   GLU B CG  
12790 C CD  . GLU C 76   ? 5.9418 3.8317 3.6946 -0.3035 0.2617  -0.2812 76   GLU B CD  
12791 O OE1 . GLU C 76   ? 5.9187 3.7955 3.6660 -0.3125 0.2536  -0.2673 76   GLU B OE1 
12792 O OE2 . GLU C 76   ? 5.9780 3.8929 3.7479 -0.2950 0.2688  -0.2846 76   GLU B OE2 
12793 N N   . ASN C 77   ? 5.1954 2.9843 2.9193 -0.2952 0.2560  -0.3147 77   ASN B N   
12794 C CA  . ASN C 77   ? 5.0636 2.8383 2.8000 -0.2824 0.2591  -0.3276 77   ASN B CA  
12795 C C   . ASN C 77   ? 4.8570 2.6054 2.5792 -0.2830 0.2570  -0.3359 77   ASN B C   
12796 O O   . ASN C 77   ? 4.7592 2.4870 2.4882 -0.2752 0.2563  -0.3431 77   ASN B O   
12797 C CB  . ASN C 77   ? 5.0952 2.8576 2.8469 -0.2790 0.2551  -0.3208 77   ASN B CB  
12798 C CG  . ASN C 77   ? 5.1814 2.9457 2.9551 -0.2644 0.2601  -0.3320 77   ASN B CG  
12799 O OD1 . ASN C 77   ? 5.2314 3.0023 3.0075 -0.2562 0.2664  -0.3462 77   ASN B OD1 
12800 N ND2 . ASN C 77   ? 5.1888 2.9473 2.9787 -0.2612 0.2571  -0.3257 77   ASN B ND2 
12801 N N   . LYS C 78   ? 4.6142 2.3638 2.3174 -0.2927 0.2556  -0.3339 78   LYS B N   
12802 C CA  . LYS C 78   ? 4.4710 2.1967 2.1594 -0.2952 0.2532  -0.3396 78   LYS B CA  
12803 C C   . LYS C 78   ? 4.3313 2.0252 2.0218 -0.2928 0.2479  -0.3380 78   LYS B C   
12804 O O   . LYS C 78   ? 4.2778 1.9513 1.9641 -0.2890 0.2474  -0.3463 78   LYS B O   
12805 C CB  . LYS C 78   ? 4.3783 2.1094 2.0676 -0.2870 0.2599  -0.3559 78   LYS B CB  
12806 C CG  . LYS C 78   ? 4.3048 2.0683 1.9911 -0.2892 0.2659  -0.3591 78   LYS B CG  
12807 C CD  . LYS C 78   ? 4.1741 1.9445 1.8428 -0.3041 0.2618  -0.3481 78   LYS B CD  
12808 C CE  . LYS C 78   ? 4.1156 1.9185 1.7805 -0.3068 0.2676  -0.3519 78   LYS B CE  
12809 N NZ  . LYS C 78   ? 4.1058 1.9183 1.7567 -0.3217 0.2624  -0.3386 78   LYS B NZ  
12810 N N   . PHE C 79   ? 4.4046 2.0953 2.1019 -0.2952 0.2437  -0.3269 79   PHE B N   
12811 C CA  . PHE C 79   ? 4.3385 2.0013 2.0384 -0.2937 0.2384  -0.3239 79   PHE B CA  
12812 C C   . PHE C 79   ? 4.3332 1.9860 2.0473 -0.2806 0.2410  -0.3359 79   PHE B C   
12813 O O   . PHE C 79   ? 4.3087 1.9394 2.0169 -0.2783 0.2393  -0.3421 79   PHE B O   
12814 C CB  . PHE C 79   ? 4.2897 1.9284 1.9702 -0.3027 0.2330  -0.3199 79   PHE B CB  
12815 C CG  . PHE C 79   ? 4.3402 1.9832 2.0085 -0.3158 0.2286  -0.3064 79   PHE B CG  
12816 C CD1 . PHE C 79   ? 4.3564 2.0102 2.0110 -0.3240 0.2289  -0.3049 79   PHE B CD1 
12817 C CD2 . PHE C 79   ? 4.3412 1.9787 2.0125 -0.3203 0.2238  -0.2949 79   PHE B CD2 
12818 C CE1 . PHE C 79   ? 4.3711 2.0289 2.0153 -0.3361 0.2242  -0.2922 79   PHE B CE1 
12819 C CE2 . PHE C 79   ? 4.3602 2.0011 2.0200 -0.3324 0.2193  -0.2826 79   PHE B CE2 
12820 C CZ  . PHE C 79   ? 4.3724 2.0232 2.0191 -0.3402 0.2193  -0.2812 79   PHE B CZ  
12821 N N   . GLN C 80   ? 5.0042 2.6740 2.7380 -0.2720 0.2448  -0.3388 80   GLN B N   
12822 C CA  . GLN C 80   ? 5.0081 2.6700 2.7588 -0.2592 0.2467  -0.3494 80   GLN B CA  
12823 C C   . GLN C 80   ? 5.0121 2.6897 2.7851 -0.2538 0.2480  -0.3451 80   GLN B C   
12824 O O   . GLN C 80   ? 5.0569 2.7575 2.8324 -0.2579 0.2500  -0.3379 80   GLN B O   
12825 C CB  . GLN C 80   ? 5.0579 2.7281 2.8085 -0.2514 0.2534  -0.3652 80   GLN B CB  
12826 C CG  . GLN C 80   ? 5.0675 2.7248 2.7966 -0.2569 0.2527  -0.3698 80   GLN B CG  
12827 C CD  . GLN C 80   ? 5.0785 2.7350 2.8094 -0.2476 0.2577  -0.3863 80   GLN B CD  
12828 O OE1 . GLN C 80   ? 5.1113 2.7850 2.8564 -0.2384 0.2637  -0.3953 80   GLN B OE1 
12829 N NE2 . GLN C 80   ? 5.0469 2.6832 2.7635 -0.2502 0.2554  -0.3903 80   GLN B NE2 
12830 N N   . ASN C 81   ? 4.1214 1.7870 1.9115 -0.2450 0.2463  -0.3487 81   ASN B N   
12831 C CA  . ASN C 81   ? 4.0703 1.7505 1.8846 -0.2391 0.2474  -0.3452 81   ASN B CA  
12832 C C   . ASN C 81   ? 4.0677 1.7323 1.9013 -0.2294 0.2446  -0.3497 81   ASN B C   
12833 O O   . ASN C 81   ? 3.9868 1.6261 1.8136 -0.2300 0.2396  -0.3508 81   ASN B O   
12834 C CB  . ASN C 81   ? 4.1355 1.8233 1.9482 -0.2496 0.2434  -0.3279 81   ASN B CB  
12835 C CG  . ASN C 81   ? 4.2306 1.9488 2.0596 -0.2470 0.2481  -0.3242 81   ASN B CG  
12836 O OD1 . ASN C 81   ? 4.2350 1.9614 2.0877 -0.2370 0.2507  -0.3281 81   ASN B OD1 
12837 N ND2 . ASN C 81   ? 4.2949 2.0303 2.1122 -0.2560 0.2491  -0.3160 81   ASN B ND2 
12838 N N   . SER C 82   ? 4.0798 1.7604 1.9383 -0.2206 0.2478  -0.3518 82   SER B N   
12839 C CA  . SER C 82   ? 4.0559 1.7256 1.9364 -0.2102 0.2456  -0.3573 82   SER B CA  
12840 C C   . SER C 82   ? 4.0727 1.7430 1.9716 -0.2122 0.2403  -0.3442 82   SER B C   
12841 O O   . SER C 82   ? 4.1195 1.8059 2.0204 -0.2188 0.2404  -0.3324 82   SER B O   
12842 C CB  . SER C 82   ? 4.0956 1.7810 1.9936 -0.1968 0.2533  -0.3721 82   SER B CB  
12843 O OG  . SER C 82   ? 4.1006 1.7809 1.9836 -0.1937 0.2574  -0.3860 82   SER B OG  
12844 N N   . ALA C 83   ? 3.6620 1.3157 1.5752 -0.2064 0.2354  -0.3462 83   ALA B N   
12845 C CA  . ALA C 83   ? 3.6388 1.2926 1.5716 -0.2079 0.2299  -0.3344 83   ALA B CA  
12846 C C   . ALA C 83   ? 3.6380 1.2862 1.5983 -0.1961 0.2279  -0.3412 83   ALA B C   
12847 O O   . ALA C 83   ? 3.6259 1.2547 1.5835 -0.1912 0.2253  -0.3498 83   ALA B O   
12848 C CB  . ALA C 83   ? 3.5976 1.2322 1.5137 -0.2200 0.2220  -0.3221 83   ALA B CB  
12849 N N   . ILE C 84   ? 4.1932 1.8586 2.1803 -0.1918 0.2289  -0.3366 84   ILE B N   
12850 C CA  . ILE C 84   ? 4.1389 1.7995 2.1552 -0.1827 0.2251  -0.3390 84   ILE B CA  
12851 C C   . ILE C 84   ? 4.0807 1.7302 2.1035 -0.1909 0.2155  -0.3235 84   ILE B C   
12852 O O   . ILE C 84   ? 4.0803 1.7434 2.1206 -0.1942 0.2138  -0.3116 84   ILE B O   
12853 C CB  . ILE C 84   ? 4.9274 2.6121 2.9734 -0.1722 0.2313  -0.3435 84   ILE B CB  
12854 C CG1 . ILE C 84   ? 4.9666 2.6742 3.0172 -0.1795 0.2335  -0.3294 84   ILE B CG1 
12855 C CG2 . ILE C 84   ? 4.9558 2.6477 2.9980 -0.1619 0.2403  -0.3617 84   ILE B CG2 
12856 C CD1 . ILE C 84   ? 4.9896 2.7198 3.0739 -0.1699 0.2380  -0.3303 84   ILE B CD1 
12857 N N   . LEU C 85   ? 4.5387 2.1639 2.5469 -0.1946 0.2093  -0.3235 85   LEU B N   
12858 C CA  . LEU C 85   ? 4.4551 2.0673 2.4708 -0.2004 0.2000  -0.3119 85   LEU B CA  
12859 C C   . LEU C 85   ? 4.3721 1.9878 2.4224 -0.1895 0.1976  -0.3156 85   LEU B C   
12860 O O   . LEU C 85   ? 4.4033 2.0336 2.4705 -0.1791 0.2037  -0.3250 85   LEU B O   
12861 C CB  . LEU C 85   ? 4.4038 1.9896 2.3970 -0.2044 0.1950  -0.3139 85   LEU B CB  
12862 C CG  . LEU C 85   ? 4.4222 2.0017 2.3810 -0.2142 0.1975  -0.3123 85   LEU B CG  
12863 C CD1 . LEU C 85   ? 4.4639 2.0555 2.4162 -0.2260 0.1971  -0.2976 85   LEU B CD1 
12864 C CD2 . LEU C 85   ? 4.4457 2.0317 2.3927 -0.2083 0.2057  -0.3259 85   LEU B CD2 
12865 N N   . THR C 86   ? 4.6816 2.2843 2.7428 -0.1919 0.1886  -0.3083 86   THR B N   
12866 C CA  . THR C 86   ? 4.6186 2.2222 2.7131 -0.1817 0.1849  -0.3117 86   THR B CA  
12867 C C   . THR C 86   ? 4.5635 2.1566 2.6700 -0.1879 0.1741  -0.2992 86   THR B C   
12868 O O   . THR C 86   ? 4.5443 2.1476 2.6608 -0.1959 0.1710  -0.2848 86   THR B O   
12869 C CB  . THR C 86   ? 4.4816 2.1105 2.6046 -0.1747 0.1903  -0.3122 86   THR B CB  
12870 O OG1 . THR C 86   ? 4.4705 2.0988 2.6262 -0.1637 0.1868  -0.3174 86   THR B OG1 
12871 C CG2 . THR C 86   ? 4.4921 2.1359 2.6207 -0.1856 0.1887  -0.2943 86   THR B CG2 
12872 N N   . ILE C 87   ? 3.8533 1.4269 1.9591 -0.1844 0.1682  -0.3041 87   ILE B N   
12873 C CA  . ILE C 87   ? 3.8195 1.3849 1.9410 -0.1887 0.1576  -0.2934 87   ILE B CA  
12874 C C   . ILE C 87   ? 4.0226 1.6009 2.1848 -0.1804 0.1549  -0.2925 87   ILE B C   
12875 O O   . ILE C 87   ? 4.0686 1.6438 2.2470 -0.1679 0.1550  -0.3047 87   ILE B O   
12876 C CB  . ILE C 87   ? 3.6049 1.1468 1.7176 -0.1860 0.1515  -0.2991 87   ILE B CB  
12877 C CG1 . ILE C 87   ? 3.5358 1.0621 1.6108 -0.1952 0.1523  -0.2976 87   ILE B CG1 
12878 C CG2 . ILE C 87   ? 3.4884 1.0256 1.6231 -0.1886 0.1406  -0.2888 87   ILE B CG2 
12879 C CD1 . ILE C 87   ? 3.4891 0.9934 1.5577 -0.1936 0.1455  -0.3004 87   ILE B CD1 
12880 N N   . GLN C 88   ? 4.2358 1.8282 2.4152 -0.1873 0.1520  -0.2782 88   GLN B N   
12881 C CA  . GLN C 88   ? 4.3271 1.9307 2.5472 -0.1805 0.1480  -0.2754 88   GLN B CA  
12882 C C   . GLN C 88   ? 4.3960 1.9860 2.6270 -0.1846 0.1359  -0.2674 88   GLN B C   
12883 O O   . GLN C 88   ? 4.3670 1.9390 2.5734 -0.1901 0.1323  -0.2672 88   GLN B O   
12884 C CB  . GLN C 88   ? 4.3828 2.0092 2.6183 -0.1856 0.1508  -0.2635 88   GLN B CB  
12885 C CG  . GLN C 88   ? 4.4511 2.0909 2.6716 -0.1832 0.1625  -0.2701 88   GLN B CG  
12886 C CD  . GLN C 88   ? 4.5025 2.1667 2.7536 -0.1771 0.1674  -0.2681 88   GLN B CD  
12887 O OE1 . GLN C 88   ? 4.5595 2.2391 2.8018 -0.1791 0.1752  -0.2668 88   GLN B OE1 
12888 N NE2 . GLN C 88   ? 4.4699 2.1382 2.7581 -0.1697 0.1626  -0.2676 88   GLN B NE2 
12889 N N   . PRO C 89   ? 4.2868 1.8855 2.5552 -0.1815 0.1295  -0.2611 89   PRO B N   
12890 C CA  . PRO C 89   ? 4.2802 1.8695 2.5636 -0.1861 0.1171  -0.2517 89   PRO B CA  
12891 C C   . PRO C 89   ? 4.2097 1.7994 2.4853 -0.2034 0.1101  -0.2321 89   PRO B C   
12892 O O   . PRO C 89   ? 4.1498 1.7531 2.4525 -0.2081 0.1051  -0.2192 89   PRO B O   
12893 C CB  . PRO C 89   ? 4.2929 1.8945 2.6217 -0.1760 0.1139  -0.2525 89   PRO B CB  
12894 C CG  . PRO C 89   ? 4.3277 1.9373 2.6598 -0.1625 0.1250  -0.2688 89   PRO B CG  
12895 C CD  . PRO C 89   ? 4.3490 1.9642 2.6493 -0.1692 0.1344  -0.2681 89   PRO B CD  
12896 N N   . LYS C 90   ? 3.4568 1.0317 1.6969 -0.2126 0.1095  -0.2301 90   LYS B N   
12897 C CA  . LYS C 90   ? 3.4520 1.0230 1.6825 -0.2283 0.1020  -0.2138 90   LYS B CA  
12898 C C   . LYS C 90   ? 3.4459 1.0086 1.6964 -0.2272 0.0907  -0.2104 90   LYS B C   
12899 O O   . LYS C 90   ? 3.4415 1.0153 1.7281 -0.2247 0.0849  -0.2045 90   LYS B O   
12900 C CB  . LYS C 90   ? 3.4552 1.0111 1.6423 -0.2369 0.1051  -0.2148 90   LYS B CB  
12901 C CG  . LYS C 90   ? 3.8871 1.4483 2.0513 -0.2369 0.1159  -0.2205 90   LYS B CG  
12902 C CD  . LYS C 90   ? 3.8249 1.4064 1.9998 -0.2434 0.1184  -0.2094 90   LYS B CD  
12903 C CE  . LYS C 90   ? 3.8445 1.4362 2.0107 -0.2366 0.1296  -0.2191 90   LYS B CE  
12904 N NZ  . LYS C 90   ? 3.8881 1.4957 2.0491 -0.2460 0.1332  -0.2080 90   LYS B NZ  
12905 N N   . GLN C 91   ? 5.3180 2.8616 3.5457 -0.2287 0.0878  -0.2143 91   GLN B N   
12906 C CA  . GLN C 91   ? 5.4740 3.0079 3.7147 -0.2291 0.0767  -0.2103 91   GLN B CA  
12907 C C   . GLN C 91   ? 5.6611 3.2000 3.9411 -0.2165 0.0715  -0.2153 91   GLN B C   
12908 O O   . GLN C 91   ? 5.6808 3.2138 3.9627 -0.2031 0.0754  -0.2305 91   GLN B O   
12909 C CB  . GLN C 91   ? 5.4739 2.9865 3.6835 -0.2284 0.0770  -0.2180 91   GLN B CB  
12910 C CG  . GLN C 91   ? 5.5262 3.0314 3.6989 -0.2417 0.0800  -0.2118 91   GLN B CG  
12911 C CD  . GLN C 91   ? 5.5569 3.0685 3.7352 -0.2565 0.0726  -0.1941 91   GLN B CD  
12912 O OE1 . GLN C 91   ? 5.6080 3.1296 3.7797 -0.2659 0.0757  -0.1858 91   GLN B OE1 
12913 N NE2 . GLN C 91   ? 5.5217 3.0283 3.7128 -0.2590 0.0624  -0.1878 91   GLN B NE2 
12914 N N   . LEU C 92   ? 4.5404 2.0896 2.8515 -0.2213 0.0622  -0.2024 92   LEU B N   
12915 C CA  . LEU C 92   ? 4.7099 2.2643 3.0618 -0.2105 0.0556  -0.2052 92   LEU B CA  
12916 C C   . LEU C 92   ? 4.7847 2.3325 3.1527 -0.2143 0.0415  -0.1965 92   LEU B C   
12917 O O   . LEU C 92   ? 4.7668 2.3194 3.1712 -0.2068 0.0343  -0.1967 92   LEU B O   
12918 C CB  . LEU C 92   ? 4.7957 2.3718 3.1808 -0.2094 0.0571  -0.1988 92   LEU B CB  
12919 C CG  . LEU C 92   ? 4.8981 2.4860 3.2779 -0.2043 0.0701  -0.2060 92   LEU B CG  
12920 C CD1 . LEU C 92   ? 4.9366 2.5465 3.3486 -0.2076 0.0694  -0.1939 92   LEU B CD1 
12921 C CD2 . LEU C 92   ? 4.9225 2.5057 3.3052 -0.1869 0.0771  -0.2262 92   LEU B CD2 
12922 N N   . PRO C 93   ? 5.3414 2.8783 3.6832 -0.2258 0.0374  -0.1891 93   PRO B N   
12923 C CA  . PRO C 93   ? 5.3584 2.8912 3.7161 -0.2300 0.0239  -0.1800 93   PRO B CA  
12924 C C   . PRO C 93   ? 5.3947 2.9140 3.7595 -0.2167 0.0197  -0.1921 93   PRO B C   
12925 O O   . PRO C 93   ? 5.4018 2.9048 3.7368 -0.2154 0.0221  -0.1992 93   PRO B O   
12926 C CB  . PRO C 93   ? 5.3266 2.8504 3.6490 -0.2445 0.0231  -0.1717 93   PRO B CB  
12927 C CG  . PRO C 93   ? 5.3714 2.8978 3.6656 -0.2498 0.0348  -0.1732 93   PRO B CG  
12928 C CD  . PRO C 93   ? 5.3941 2.9222 3.6924 -0.2351 0.0443  -0.1887 93   PRO B CD  
12929 N N   . GLY C 94   ? 5.4290 2.9547 3.8329 -0.2073 0.0132  -0.1939 94   GLY B N   
12930 C CA  . GLY C 94   ? 5.4326 2.9457 3.8463 -0.1950 0.0077  -0.2043 94   GLY B CA  
12931 C C   . GLY C 94   ? 5.4082 2.9092 3.8088 -0.2022 -0.0020 -0.1970 94   GLY B C   
12932 O O   . GLY C 94   ? 5.3956 2.9033 3.8003 -0.2154 -0.0093 -0.1812 94   GLY B O   
12933 N N   . GLY C 95   ? 5.4002 2.8842 3.7852 -0.1939 -0.0020 -0.2082 95   GLY B N   
12934 C CA  . GLY C 95   ? 5.3511 2.8231 3.7206 -0.1999 -0.0099 -0.2020 95   GLY B CA  
12935 C C   . GLY C 95   ? 5.3724 2.8331 3.6957 -0.2065 -0.0008 -0.2044 95   GLY B C   
12936 O O   . GLY C 95   ? 5.3568 2.8013 3.6591 -0.2014 0.0005  -0.2126 95   GLY B O   
12937 N N   . GLN C 96   ? 5.4228 2.8917 3.7306 -0.2180 0.0052  -0.1969 96   GLN B N   
12938 C CA  . GLN C 96   ? 5.4225 2.8813 3.6874 -0.2236 0.0151  -0.2003 96   GLN B CA  
12939 C C   . GLN C 96   ? 5.4779 2.9267 3.7295 -0.2104 0.0244  -0.2181 96   GLN B C   
12940 O O   . GLN C 96   ? 5.5331 2.9888 3.8057 -0.2001 0.0270  -0.2263 96   GLN B O   
12941 C CB  . GLN C 96   ? 5.4136 2.8845 3.6687 -0.2349 0.0217  -0.1926 96   GLN B CB  
12942 C CG  . GLN C 96   ? 5.4094 2.8709 3.6219 -0.2399 0.0327  -0.1972 96   GLN B CG  
12943 C CD  . GLN C 96   ? 5.4405 2.9141 3.6449 -0.2504 0.0386  -0.1898 96   GLN B CD  
12944 O OE1 . GLN C 96   ? 5.4424 2.9312 3.6713 -0.2561 0.0338  -0.1790 96   GLN B OE1 
12945 N NE2 . GLN C 96   ? 5.4709 2.9379 3.6414 -0.2534 0.0486  -0.1949 96   GLN B NE2 
12946 N N   . ASN C 97   ? 5.6977 3.1307 3.9157 -0.2104 0.0292  -0.2241 97   ASN B N   
12947 C CA  . ASN C 97   ? 5.7011 3.1247 3.9027 -0.1997 0.0385  -0.2403 97   ASN B CA  
12948 C C   . ASN C 97   ? 5.6761 3.1056 3.8564 -0.2037 0.0509  -0.2435 97   ASN B C   
12949 O O   . ASN C 97   ? 5.6935 3.1128 3.8406 -0.2072 0.0577  -0.2468 97   ASN B O   
12950 C CB  . ASN C 97   ? 5.7239 3.1279 3.8996 -0.1983 0.0379  -0.2445 97   ASN B CB  
12951 C CG  . ASN C 97   ? 5.6985 3.0964 3.8928 -0.1952 0.0250  -0.2402 97   ASN B CG  
12952 O OD1 . ASN C 97   ? 5.6989 3.1054 3.9272 -0.1909 0.0170  -0.2376 97   ASN B OD1 
12953 N ND2 . ASN C 97   ? 5.6728 3.0560 3.8457 -0.1974 0.0229  -0.2390 97   ASN B ND2 
12954 N N   . PRO C 98   ? 6.1995 3.6459 4.3998 -0.2031 0.0537  -0.2420 98   PRO B N   
12955 C CA  . PRO C 98   ? 6.1404 3.5947 4.3218 -0.2097 0.0638  -0.2409 98   PRO B CA  
12956 C C   . PRO C 98   ? 5.9959 3.4454 4.1601 -0.2005 0.0745  -0.2566 98   PRO B C   
12957 O O   . PRO C 98   ? 5.9988 3.4407 4.1699 -0.1890 0.0738  -0.2678 98   PRO B O   
12958 C CB  . PRO C 98   ? 6.2178 3.6924 4.4317 -0.2101 0.0622  -0.2345 98   PRO B CB  
12959 C CG  . PRO C 98   ? 6.2130 3.6891 4.4638 -0.2012 0.0523  -0.2353 98   PRO B CG  
12960 C CD  . PRO C 98   ? 6.1995 3.6570 4.4381 -0.1934 0.0501  -0.2453 98   PRO B CD  
12961 N N   . VAL C 99   ? 5.9010 3.3550 4.0429 -0.2060 0.0838  -0.2571 99   VAL B N   
12962 C CA  . VAL C 99   ? 5.7476 3.2033 3.8794 -0.1976 0.0942  -0.2709 99   VAL B CA  
12963 C C   . VAL C 99   ? 5.5006 2.9381 3.6085 -0.1919 0.0971  -0.2825 99   VAL B C   
12964 O O   . VAL C 99   ? 5.5374 2.9747 3.6288 -0.1881 0.1062  -0.2927 99   VAL B O   
12965 C CB  . VAL C 99   ? 5.8135 3.2820 3.9791 -0.1859 0.0945  -0.2777 99   VAL B CB  
12966 C CG1 . VAL C 99   ? 5.8857 3.3575 4.0409 -0.1774 0.1057  -0.2924 99   VAL B CG1 
12967 C CG2 . VAL C 99   ? 5.8391 3.3264 4.0299 -0.1916 0.0918  -0.2655 99   VAL B CG2 
12968 N N   . SER C 100  ? 4.0418 1.4646 2.1480 -0.1916 0.0893  -0.2806 100  SER B N   
12969 C CA  . SER C 100  ? 3.7952 1.2004 1.8798 -0.1866 0.0914  -0.2903 100  SER B CA  
12970 C C   . SER C 100  ? 3.6212 1.0185 1.6686 -0.1952 0.0984  -0.2892 100  SER B C   
12971 O O   . SER C 100  ? 3.6252 1.0132 1.6589 -0.2034 0.0945  -0.2808 100  SER B O   
12972 C CB  . SER C 100  ? 3.6812 1.0736 1.7740 -0.1849 0.0806  -0.2866 100  SER B CB  
12973 O OG  . SER C 100  ? 3.6370 1.0389 1.7638 -0.1833 0.0716  -0.2799 100  SER B OG  
12974 N N   . TYR C 101  ? 4.3099 1.7110 2.3417 -0.1935 0.1084  -0.2976 101  TYR B N   
12975 C CA  . TYR C 101  ? 4.1527 1.5473 2.1501 -0.2015 0.1155  -0.2973 101  TYR B CA  
12976 C C   . TYR C 101  ? 4.0942 1.5030 2.0846 -0.2103 0.1211  -0.2911 101  TYR B C   
12977 O O   . TYR C 101  ? 4.0818 1.4983 2.0819 -0.2178 0.1170  -0.2797 101  TYR B O   
12978 C CB  . TYR C 101  ? 4.0508 1.4291 2.0293 -0.2090 0.1111  -0.2900 101  TYR B CB  
12979 C CG  . TYR C 101  ? 3.9850 1.3461 1.9578 -0.2025 0.1079  -0.2960 101  TYR B CG  
12980 C CD1 . TYR C 101  ? 4.0017 1.3491 1.9462 -0.2045 0.1126  -0.2997 101  TYR B CD1 
12981 C CD2 . TYR C 101  ? 3.9318 1.2902 1.9282 -0.1947 0.0997  -0.2972 101  TYR B CD2 
12982 C CE1 . TYR C 101  ? 3.9748 1.3065 1.9142 -0.1989 0.1094  -0.3041 101  TYR B CE1 
12983 C CE2 . TYR C 101  ? 3.9073 1.2499 1.8985 -0.1891 0.0961  -0.3017 101  TYR B CE2 
12984 C CZ  . TYR C 101  ? 3.9346 1.2640 1.8971 -0.1913 0.1011  -0.3051 101  TYR B CZ  
12985 O OH  . TYR C 101  ? 3.9095 1.2231 1.8670 -0.1860 0.0974  -0.3087 101  TYR B OH  
12986 N N   . VAL C 102  ? 4.2997 1.7116 2.2719 -0.2103 0.1299  -0.2978 102  VAL B N   
12987 C CA  . VAL C 102  ? 4.2925 1.7170 2.2561 -0.2191 0.1348  -0.2914 102  VAL B CA  
12988 C C   . VAL C 102  ? 4.3353 1.7534 2.2664 -0.2257 0.1413  -0.2929 102  VAL B C   
12989 O O   . VAL C 102  ? 4.3147 1.7193 2.2291 -0.2227 0.1434  -0.3002 102  VAL B O   
12990 C CB  . VAL C 102  ? 4.2872 1.7324 2.2705 -0.2136 0.1393  -0.2951 102  VAL B CB  
12991 C CG1 . VAL C 102  ? 4.2332 1.6856 2.2514 -0.2066 0.1331  -0.2938 102  VAL B CG1 
12992 C CG2 . VAL C 102  ? 4.3126 1.7593 2.2869 -0.2055 0.1473  -0.3091 102  VAL B CG2 
12993 N N   . TYR C 103  ? 4.6060 2.0340 2.5294 -0.2350 0.1438  -0.2850 103  TYR B N   
12994 C CA  . TYR C 103  ? 4.6456 2.0701 2.5403 -0.2427 0.1494  -0.2845 103  TYR B CA  
12995 C C   . TYR C 103  ? 4.6792 2.1226 2.5760 -0.2419 0.1561  -0.2871 103  TYR B C   
12996 O O   . TYR C 103  ? 4.6335 2.0926 2.5438 -0.2451 0.1557  -0.2800 103  TYR B O   
12997 C CB  . TYR C 103  ? 4.7769 2.1950 2.6574 -0.2558 0.1460  -0.2721 103  TYR B CB  
12998 C CG  . TYR C 103  ? 4.8214 2.2183 2.6876 -0.2580 0.1422  -0.2713 103  TYR B CG  
12999 C CD1 . TYR C 103  ? 4.8453 2.2349 2.7271 -0.2520 0.1360  -0.2720 103  TYR B CD1 
13000 C CD2 . TYR C 103  ? 4.8840 2.2686 2.7222 -0.2661 0.1447  -0.2693 103  TYR B CD2 
13001 C CE1 . TYR C 103  ? 4.8433 2.2147 2.7125 -0.2539 0.1327  -0.2706 103  TYR B CE1 
13002 C CE2 . TYR C 103  ? 4.8814 2.2472 2.7072 -0.2677 0.1418  -0.2684 103  TYR B CE2 
13003 C CZ  . TYR C 103  ? 4.8665 2.2262 2.7078 -0.2616 0.1359  -0.2689 103  TYR B CZ  
13004 O OH  . TYR C 103  ? 4.8463 2.1884 2.6759 -0.2631 0.1331  -0.2675 103  TYR B OH  
13005 N N   . LEU C 104  ? 3.6028 1.0449 1.4867 -0.2375 0.1621  -0.2972 104  LEU B N   
13006 C CA  . LEU C 104  ? 3.6695 1.1287 1.5511 -0.2370 0.1692  -0.3008 104  LEU B CA  
13007 C C   . LEU C 104  ? 3.6930 1.1488 1.5482 -0.2490 0.1709  -0.2938 104  LEU B C   
13008 O O   . LEU C 104  ? 3.6279 1.0658 1.4639 -0.2532 0.1695  -0.2934 104  LEU B O   
13009 C CB  . LEU C 104  ? 3.6717 1.1285 1.5492 -0.2275 0.1740  -0.3150 104  LEU B CB  
13010 C CG  . LEU C 104  ? 3.6915 1.1668 1.5763 -0.2206 0.1812  -0.3242 104  LEU B CG  
13011 C CD1 . LEU C 104  ? 3.7010 1.1940 1.6160 -0.2146 0.1808  -0.3230 104  LEU B CD1 
13012 C CD2 . LEU C 104  ? 3.6712 1.1371 1.5516 -0.2117 0.1835  -0.3378 104  LEU B CD2 
13013 N N   . GLU C 105  ? 4.2642 1.7367 2.1186 -0.2546 0.1739  -0.2883 105  GLU B N   
13014 C CA  . GLU C 105  ? 4.3325 1.8015 2.1626 -0.2667 0.1746  -0.2808 105  GLU B CA  
13015 C C   . GLU C 105  ? 4.3965 1.8825 2.2193 -0.2685 0.1808  -0.2824 105  GLU B C   
13016 O O   . GLU C 105  ? 4.4248 1.9304 2.2647 -0.2635 0.1838  -0.2839 105  GLU B O   
13017 C CB  . GLU C 105  ? 4.3577 1.8263 2.1902 -0.2767 0.1691  -0.2671 105  GLU B CB  
13018 C CG  . GLU C 105  ? 4.3916 1.8485 2.1971 -0.2896 0.1680  -0.2595 105  GLU B CG  
13019 C CD  . GLU C 105  ? 4.3968 1.8467 2.2032 -0.2985 0.1615  -0.2479 105  GLU B CD  
13020 O OE1 . GLU C 105  ? 4.4283 1.8919 2.2471 -0.3029 0.1595  -0.2391 105  GLU B OE1 
13021 O OE2 . GLU C 105  ? 4.3682 1.7990 2.1626 -0.3015 0.1586  -0.2473 105  GLU B OE2 
13022 N N   . VAL C 106  ? 4.7828 2.2617 2.5807 -0.2758 0.1826  -0.2816 106  VAL B N   
13023 C CA  . VAL C 106  ? 4.8415 2.3366 2.6308 -0.2795 0.1875  -0.2812 106  VAL B CA  
13024 C C   . VAL C 106  ? 4.8632 2.3526 2.6317 -0.2930 0.1852  -0.2707 106  VAL B C   
13025 O O   . VAL C 106  ? 4.8333 2.3038 2.5910 -0.2985 0.1811  -0.2665 106  VAL B O   
13026 C CB  . VAL C 106  ? 4.8507 2.3454 2.6306 -0.2739 0.1927  -0.2930 106  VAL B CB  
13027 C CG1 . VAL C 106  ? 4.9164 2.4311 2.6894 -0.2776 0.1975  -0.2923 106  VAL B CG1 
13028 C CG2 . VAL C 106  ? 4.8434 2.3403 2.6424 -0.2606 0.1943  -0.3040 106  VAL B CG2 
13029 N N   . VAL C 107  ? 4.1728 1.6788 1.9360 -0.2984 0.1878  -0.2664 107  VAL B N   
13030 C CA  . VAL C 107  ? 4.1912 1.6931 1.9357 -0.3115 0.1851  -0.2559 107  VAL B CA  
13031 C C   . VAL C 107  ? 4.2208 1.7343 1.9518 -0.3153 0.1890  -0.2570 107  VAL B C   
13032 O O   . VAL C 107  ? 4.2437 1.7738 1.9829 -0.3082 0.1939  -0.2641 107  VAL B O   
13033 C CB  . VAL C 107  ? 4.2841 1.7961 2.0392 -0.3178 0.1814  -0.2435 107  VAL B CB  
13034 C CG1 . VAL C 107  ? 4.2987 1.8021 2.0331 -0.3318 0.1776  -0.2329 107  VAL B CG1 
13035 C CG2 . VAL C 107  ? 4.2375 1.7425 2.0103 -0.3133 0.1776  -0.2426 107  VAL B CG2 
13036 N N   . SER C 108  ? 4.0920 1.5968 1.8025 -0.3265 0.1866  -0.2502 108  SER B N   
13037 C CA  . SER C 108  ? 4.1685 1.6847 1.8660 -0.3321 0.1888  -0.2488 108  SER B CA  
13038 C C   . SER C 108  ? 4.2564 1.7584 1.9323 -0.3449 0.1845  -0.2404 108  SER B C   
13039 O O   . SER C 108  ? 4.2453 1.7280 1.9156 -0.3487 0.1807  -0.2369 108  SER B O   
13040 C CB  . SER C 108  ? 4.1673 1.6852 1.8612 -0.3251 0.1937  -0.2607 108  SER B CB  
13041 O OG  . SER C 108  ? 4.1215 1.6177 1.8125 -0.3200 0.1933  -0.2683 108  SER B OG  
13042 N N   . LYS C 109  ? 5.3117 2.8235 2.9758 -0.3516 0.1852  -0.2371 109  LYS B N   
13043 C CA  . LYS C 109  ? 5.3860 2.8855 3.0299 -0.3639 0.1810  -0.2293 109  LYS B CA  
13044 C C   . LYS C 109  ? 5.4067 2.8813 3.0360 -0.3644 0.1807  -0.2351 109  LYS B C   
13045 O O   . LYS C 109  ? 5.4015 2.8578 3.0172 -0.3723 0.1770  -0.2301 109  LYS B O   
13046 C CB  . LYS C 109  ? 5.4437 2.9620 3.0805 -0.3707 0.1812  -0.2241 109  LYS B CB  
13047 C CG  . LYS C 109  ? 5.4908 3.0238 3.1296 -0.3646 0.1866  -0.2330 109  LYS B CG  
13048 C CD  . LYS C 109  ? 5.4411 2.9568 3.0642 -0.3663 0.1869  -0.2389 109  LYS B CD  
13049 C CE  . LYS C 109  ? 5.4440 2.9751 3.0683 -0.3616 0.1918  -0.2471 109  LYS B CE  
13050 N NZ  . LYS C 109  ? 5.4821 3.0301 3.0974 -0.3705 0.1908  -0.2408 109  LYS B NZ  
13051 N N   . HIS C 110  ? 5.5424 3.0165 3.1748 -0.3559 0.1848  -0.2456 110  HIS B N   
13052 C CA  . HIS C 110  ? 5.5531 3.0072 3.1716 -0.3568 0.1850  -0.2506 110  HIS B CA  
13053 C C   . HIS C 110  ? 5.4527 2.8841 3.0730 -0.3516 0.1841  -0.2547 110  HIS B C   
13054 O O   . HIS C 110  ? 5.4332 2.8448 3.0414 -0.3535 0.1835  -0.2568 110  HIS B O   
13055 C CB  . HIS C 110  ? 5.6492 3.1147 3.2682 -0.3518 0.1895  -0.2589 110  HIS B CB  
13056 C CG  . HIS C 110  ? 5.7229 3.1698 3.3293 -0.3527 0.1898  -0.2636 110  HIS B CG  
13057 N ND1 . HIS C 110  ? 5.7568 3.2059 3.3654 -0.3459 0.1936  -0.2731 110  HIS B ND1 
13058 C CD2 . HIS C 110  ? 5.7470 3.1726 3.3386 -0.3598 0.1868  -0.2600 110  HIS B CD2 
13059 C CE1 . HIS C 110  ? 5.7565 3.1869 3.3530 -0.3489 0.1927  -0.2743 110  HIS B CE1 
13060 N NE2 . HIS C 110  ? 5.7497 3.1656 3.3361 -0.3570 0.1888  -0.2666 110  HIS B NE2 
13061 N N   . PHE C 111  ? 5.0055 2.4402 2.6416 -0.3453 0.1837  -0.2553 111  PHE B N   
13062 C CA  . PHE C 111  ? 4.8891 2.3059 2.5303 -0.3390 0.1828  -0.2597 111  PHE B CA  
13063 C C   . PHE C 111  ? 4.7645 2.1915 2.4268 -0.3321 0.1821  -0.2596 111  PHE B C   
13064 O O   . PHE C 111  ? 4.7478 2.1941 2.4199 -0.3333 0.1823  -0.2551 111  PHE B O   
13065 C CB  . PHE C 111  ? 4.8990 2.3083 2.5386 -0.3314 0.1859  -0.2700 111  PHE B CB  
13066 C CG  . PHE C 111  ? 4.8720 2.2571 2.5081 -0.3286 0.1843  -0.2726 111  PHE B CG  
13067 C CD1 . PHE C 111  ? 4.8763 2.2424 2.4949 -0.3354 0.1830  -0.2700 111  PHE B CD1 
13068 C CD2 . PHE C 111  ? 4.8417 2.2235 2.4926 -0.3189 0.1839  -0.2775 111  PHE B CD2 
13069 C CE1 . PHE C 111  ? 4.8375 2.1823 2.4532 -0.3325 0.1819  -0.2720 111  PHE B CE1 
13070 C CE2 . PHE C 111  ? 4.7969 2.1576 2.4448 -0.3164 0.1820  -0.2791 111  PHE B CE2 
13071 C CZ  . PHE C 111  ? 4.7951 2.1377 2.4253 -0.3231 0.1813  -0.2763 111  PHE B CZ  
13072 N N   . SER C 112  ? 4.3018 1.7160 1.9720 -0.3250 0.1811  -0.2642 112  SER B N   
13073 C CA  . SER C 112  ? 4.2269 1.6496 1.9192 -0.3172 0.1802  -0.2654 112  SER B CA  
13074 C C   . SER C 112  ? 4.1695 1.5765 1.8679 -0.3086 0.1793  -0.2723 112  SER B C   
13075 O O   . SER C 112  ? 4.1435 1.5304 1.8297 -0.3115 0.1774  -0.2716 112  SER B O   
13076 C CB  . SER C 112  ? 4.1804 1.6066 1.8779 -0.3242 0.1760  -0.2546 112  SER B CB  
13077 O OG  . SER C 112  ? 4.1612 1.6069 1.8810 -0.3189 0.1763  -0.2537 112  SER B OG  
13078 N N   . LYS C 113  ? 4.1546 1.5709 1.8723 -0.2980 0.1804  -0.2789 113  LYS B N   
13079 C CA  . LYS C 113  ? 4.0638 1.4664 1.7881 -0.2895 0.1791  -0.2856 113  LYS B CA  
13080 C C   . LYS C 113  ? 3.9993 1.4124 1.7485 -0.2785 0.1789  -0.2910 113  LYS B C   
13081 O O   . LYS C 113  ? 4.0131 1.4458 1.7745 -0.2749 0.1818  -0.2932 113  LYS B O   
13082 C CB  . LYS C 113  ? 4.0761 1.4677 1.7857 -0.2876 0.1820  -0.2930 113  LYS B CB  
13083 C CG  . LYS C 113  ? 4.0660 1.4419 1.7801 -0.2795 0.1803  -0.2992 113  LYS B CG  
13084 C CD  . LYS C 113  ? 4.0641 1.4190 1.7686 -0.2841 0.1764  -0.2936 113  LYS B CD  
13085 C CE  . LYS C 113  ? 4.0343 1.3739 1.7410 -0.2764 0.1751  -0.2996 113  LYS B CE  
13086 N NZ  . LYS C 113  ? 4.0199 1.3494 1.7094 -0.2776 0.1782  -0.3038 113  LYS B NZ  
13087 N N   . SER C 114  ? 4.3251 1.7244 2.0814 -0.2730 0.1753  -0.2933 114  SER B N   
13088 C CA  . SER C 114  ? 4.3648 1.7699 2.1460 -0.2647 0.1724  -0.2951 114  SER B CA  
13089 C C   . SER C 114  ? 4.3357 1.7234 2.1200 -0.2578 0.1691  -0.3001 114  SER B C   
13090 O O   . SER C 114  ? 4.3018 1.6738 2.0689 -0.2594 0.1697  -0.3022 114  SER B O   
13091 C CB  . SER C 114  ? 4.3932 1.8030 2.1835 -0.2711 0.1679  -0.2839 114  SER B CB  
13092 O OG  . SER C 114  ? 4.4056 1.8041 2.1755 -0.2824 0.1664  -0.2760 114  SER B OG  
13093 N N   . LYS C 115  ? 4.3408 1.7312 2.1477 -0.2504 0.1653  -0.3013 115  LYS B N   
13094 C CA  . LYS C 115  ? 4.3020 1.6789 2.1144 -0.2422 0.1623  -0.3075 115  LYS B CA  
13095 C C   . LYS C 115  ? 4.2713 1.6501 2.1098 -0.2358 0.1561  -0.3062 115  LYS B C   
13096 O O   . LYS C 115  ? 4.2651 1.6589 2.1212 -0.2359 0.1550  -0.3022 115  LYS B O   
13097 C CB  . LYS C 115  ? 4.3254 1.7049 2.1347 -0.2347 0.1675  -0.3195 115  LYS B CB  
13098 C CG  . LYS C 115  ? 4.2653 1.6365 2.0865 -0.2243 0.1647  -0.3273 115  LYS B CG  
13099 C CD  . LYS C 115  ? 4.2208 1.5801 2.0247 -0.2224 0.1676  -0.3347 115  LYS B CD  
13100 C CE  . LYS C 115  ? 4.1743 1.5283 1.9918 -0.2112 0.1651  -0.3438 115  LYS B CE  
13101 N NZ  . LYS C 115  ? 4.1455 1.4849 1.9467 -0.2098 0.1664  -0.3496 115  LYS B NZ  
13102 N N   . ARG C 116  ? 4.5409 1.9049 2.3823 -0.2306 0.1516  -0.3087 116  ARG B N   
13103 C CA  . ARG C 116  ? 4.5623 1.9273 2.4294 -0.2235 0.1451  -0.3084 116  ARG B CA  
13104 C C   . ARG C 116  ? 4.5713 1.9336 2.4482 -0.2115 0.1453  -0.3202 116  ARG B C   
13105 O O   . ARG C 116  ? 4.5842 1.9333 2.4458 -0.2096 0.1468  -0.3256 116  ARG B O   
13106 C CB  . ARG C 116  ? 4.5570 1.9075 2.4219 -0.2275 0.1381  -0.3004 116  ARG B CB  
13107 C CG  . ARG C 116  ? 4.5717 1.9176 2.4582 -0.2188 0.1308  -0.3023 116  ARG B CG  
13108 C CD  . ARG C 116  ? 4.6119 1.9425 2.4898 -0.2118 0.1308  -0.3106 116  ARG B CD  
13109 N NE  . ARG C 116  ? 4.6139 1.9314 2.4968 -0.2107 0.1228  -0.3057 116  ARG B NE  
13110 C CZ  . ARG C 116  ? 4.6221 1.9258 2.5020 -0.2045 0.1203  -0.3105 116  ARG B CZ  
13111 N NH1 . ARG C 116  ? 4.6509 1.9515 2.5224 -0.1991 0.1253  -0.3208 116  ARG B NH1 
13112 N NH2 . ARG C 116  ? 4.5849 1.8784 2.4701 -0.2042 0.1127  -0.3046 116  ARG B NH2 
13113 N N   . MET C 117  ? 4.4552 1.8290 2.3581 -0.2037 0.1435  -0.3239 117  MET B N   
13114 C CA  . MET C 117  ? 4.4420 1.8160 2.3553 -0.1920 0.1448  -0.3365 117  MET B CA  
13115 C C   . MET C 117  ? 4.3941 1.7774 2.3401 -0.1842 0.1398  -0.3374 117  MET B C   
13116 O O   . MET C 117  ? 4.3890 1.7888 2.3496 -0.1855 0.1411  -0.3336 117  MET B O   
13117 C CB  . MET C 117  ? 4.5074 1.8926 2.4104 -0.1909 0.1542  -0.3451 117  MET B CB  
13118 C CG  . MET C 117  ? 4.5537 1.9589 2.4632 -0.1956 0.1580  -0.3398 117  MET B CG  
13119 S SD  . MET C 117  ? 4.6331 2.0523 2.5248 -0.1984 0.1687  -0.3456 117  MET B SD  
13120 C CE  . MET C 117  ? 4.1324 1.5321 1.9919 -0.2036 0.1702  -0.3474 117  MET B CE  
13121 N N   . PRO C 118  ? 4.0659 1.4388 2.0242 -0.1759 0.1339  -0.3423 118  PRO B N   
13122 C CA  . PRO C 118  ? 4.0245 1.4035 2.0153 -0.1691 0.1270  -0.3415 118  PRO B CA  
13123 C C   . PRO C 118  ? 4.0484 1.4475 2.0591 -0.1639 0.1319  -0.3465 118  PRO B C   
13124 O O   . PRO C 118  ? 4.0698 1.4763 2.0690 -0.1627 0.1407  -0.3542 118  PRO B O   
13125 C CB  . PRO C 118  ? 3.9921 1.3566 1.9869 -0.1597 0.1226  -0.3503 118  PRO B CB  
13126 C CG  . PRO C 118  ? 3.9867 1.3343 1.9517 -0.1647 0.1239  -0.3495 118  PRO B CG  
13127 C CD  . PRO C 118  ? 4.0438 1.3983 1.9862 -0.1729 0.1329  -0.3482 118  PRO B CD  
13128 N N   . ILE C 119  ? 4.0256 1.4342 2.0658 -0.1614 0.1263  -0.3415 119  ILE B N   
13129 C CA  . ILE C 119  ? 4.0445 1.4721 2.1068 -0.1553 0.1308  -0.3465 119  ILE B CA  
13130 C C   . ILE C 119  ? 4.0115 1.4412 2.1087 -0.1466 0.1231  -0.3475 119  ILE B C   
13131 O O   . ILE C 119  ? 3.9352 1.3548 2.0404 -0.1482 0.1133  -0.3405 119  ILE B O   
13132 C CB  . ILE C 119  ? 4.0455 1.4901 2.1084 -0.1643 0.1344  -0.3361 119  ILE B CB  
13133 C CG1 . ILE C 119  ? 3.9908 1.4468 2.0874 -0.1637 0.1277  -0.3273 119  ILE B CG1 
13134 C CG2 . ILE C 119  ? 4.0383 1.4749 2.0724 -0.1772 0.1346  -0.3261 119  ILE B CG2 
13135 C CD1 . ILE C 119  ? 4.0255 1.5026 2.1310 -0.1682 0.1327  -0.3209 119  ILE B CD1 
13136 N N   . THR C 120  ? 3.5020 0.9453 1.6205 -0.1375 0.1272  -0.3561 120  THR B N   
13137 C CA  . THR C 120  ? 3.5006 0.9465 1.6550 -0.1288 0.1198  -0.3574 120  THR B CA  
13138 C C   . THR C 120  ? 3.5051 0.9726 1.6875 -0.1252 0.1233  -0.3568 120  THR B C   
13139 O O   . THR C 120  ? 3.5463 1.0284 1.7207 -0.1294 0.1318  -0.3550 120  THR B O   
13140 C CB  . THR C 120  ? 3.5080 0.9403 1.6669 -0.1167 0.1175  -0.3721 120  THR B CB  
13141 O OG1 . THR C 120  ? 3.5070 0.9194 1.6416 -0.1205 0.1135  -0.3709 120  THR B OG1 
13142 C CG2 . THR C 120  ? 3.5059 0.9390 1.7031 -0.1085 0.1079  -0.3719 120  THR B CG2 
13143 N N   . TYR C 121  ? 4.1891 1.8249 1.8794 -0.2506 -0.5436 -0.0021 121  TYR B N   
13144 C CA  . TYR C 121  ? 4.1675 1.8641 1.9082 -0.2729 -0.5223 -0.0193 121  TYR B CA  
13145 C C   . TYR C 121  ? 4.0781 1.7522 1.8089 -0.2845 -0.5202 -0.0173 121  TYR B C   
13146 O O   . TYR C 121  ? 4.0492 1.7904 1.8405 -0.2895 -0.5182 -0.0203 121  TYR B O   
13147 C CB  . TYR C 121  ? 4.1413 1.9494 1.9742 -0.2534 -0.5388 -0.0106 121  TYR B CB  
13148 C CG  . TYR C 121  ? 4.1775 2.0264 2.0343 -0.2359 -0.5463 -0.0092 121  TYR B CG  
13149 C CD1 . TYR C 121  ? 4.2359 2.1228 2.1136 -0.2513 -0.5238 -0.0318 121  TYR B CD1 
13150 C CD2 . TYR C 121  ? 4.1446 1.9984 2.0070 -0.2037 -0.5763 0.0135  121  TYR B CD2 
13151 C CE1 . TYR C 121  ? 4.2510 2.1769 2.1507 -0.2351 -0.5308 -0.0316 121  TYR B CE1 
13152 C CE2 . TYR C 121  ? 4.1515 2.0445 2.0365 -0.1877 -0.5826 0.0141  121  TYR B CE2 
13153 C CZ  . TYR C 121  ? 4.2235 2.1518 2.1260 -0.2035 -0.5598 -0.0084 121  TYR B CZ  
13154 O OH  . TYR C 121  ? 4.2669 2.2346 2.1911 -0.1875 -0.5660 -0.0090 121  TYR B OH  
13155 N N   . ASP C 122  ? 4.4080 1.9880 2.0623 -0.2878 -0.5212 -0.0123 122  ASP B N   
13156 C CA  . ASP C 122  ? 4.3315 1.8839 1.9702 -0.2954 -0.5228 -0.0086 122  ASP B CA  
13157 C C   . ASP C 122  ? 4.3541 1.8436 1.9373 -0.3308 -0.4885 -0.0296 122  ASP B C   
13158 O O   . ASP C 122  ? 4.4419 1.8453 1.9521 -0.3348 -0.4876 -0.0255 122  ASP B O   
13159 C CB  . ASP C 122  ? 4.3380 1.8339 1.9334 -0.2704 -0.5528 0.0142  122  ASP B CB  
13160 C CG  . ASP C 122  ? 4.2838 1.8182 1.9231 -0.2576 -0.5747 0.0279  122  ASP B CG  
13161 O OD1 . ASP C 122  ? 4.2607 1.7761 1.8895 -0.2315 -0.6048 0.0476  122  ASP B OD1 
13162 O OD2 . ASP C 122  ? 4.2597 1.8446 1.9461 -0.2733 -0.5620 0.0182  122  ASP B OD2 
13163 N N   . ASN C 123  ? 4.2520 1.7857 1.8705 -0.3558 -0.4606 -0.0520 123  ASN B N   
13164 C CA  . ASN C 123  ? 4.3045 1.7841 1.8759 -0.3913 -0.4247 -0.0745 123  ASN B CA  
13165 C C   . ASN C 123  ? 4.2964 1.7892 1.8854 -0.4046 -0.4192 -0.0785 123  ASN B C   
13166 O O   . ASN C 123  ? 4.2487 1.8264 1.9138 -0.4064 -0.4194 -0.0839 123  ASN B O   
13167 C CB  . ASN C 123  ? 4.3391 1.8576 1.9388 -0.4129 -0.3958 -0.1000 123  ASN B CB  
13168 C CG  . ASN C 123  ? 4.4195 1.8740 1.9648 -0.4504 -0.3562 -0.1246 123  ASN B CG  
13169 O OD1 . ASN C 123  ? 4.4816 1.9293 2.0183 -0.4677 -0.3320 -0.1441 123  ASN B OD1 
13170 N ND2 . ASN C 123  ? 4.4424 1.8504 1.9518 -0.4634 -0.3486 -0.1245 123  ASN B ND2 
13171 N N   . GLY C 124  ? 3.8582 1.2665 1.3758 -0.4137 -0.4138 -0.0763 124  GLY B N   
13172 C CA  . GLY C 124  ? 3.8852 1.2950 1.4091 -0.4293 -0.4049 -0.0829 124  GLY B CA  
13173 C C   . GLY C 124  ? 3.7609 1.2062 1.3236 -0.4056 -0.4376 -0.0631 124  GLY B C   
13174 O O   . GLY C 124  ? 3.7191 1.1585 1.2785 -0.3761 -0.4692 -0.0410 124  GLY B O   
13175 N N   . PHE C 125  ? 3.9793 1.4616 1.5804 -0.4184 -0.4302 -0.0716 125  PHE B N   
13176 C CA  . PHE C 125  ? 3.8942 1.4071 1.5319 -0.3972 -0.4600 -0.0541 125  PHE B CA  
13177 C C   . PHE C 125  ? 3.8495 1.4347 1.5582 -0.4093 -0.4513 -0.0653 125  PHE B C   
13178 O O   . PHE C 125  ? 3.8911 1.4827 1.6027 -0.4383 -0.4196 -0.0887 125  PHE B O   
13179 C CB  . PHE C 125  ? 3.9411 1.3660 1.5019 -0.3972 -0.4653 -0.0477 125  PHE B CB  
13180 C CG  . PHE C 125  ? 4.0180 1.3495 1.4870 -0.3992 -0.4579 -0.0461 125  PHE B CG  
13181 C CD1 . PHE C 125  ? 4.1210 1.3952 1.5327 -0.4304 -0.4205 -0.0661 125  PHE B CD1 
13182 C CD2 . PHE C 125  ? 3.9940 1.2951 1.4355 -0.3698 -0.4875 -0.0249 125  PHE B CD2 
13183 C CE1 . PHE C 125  ? 4.2010 1.3850 1.5259 -0.4322 -0.4126 -0.0638 125  PHE B CE1 
13184 C CE2 . PHE C 125  ? 4.0880 1.3001 1.4431 -0.3704 -0.4813 -0.0228 125  PHE B CE2 
13185 C CZ  . PHE C 125  ? 4.1886 1.3408 1.4843 -0.4015 -0.4436 -0.0417 125  PHE B CZ  
13186 N N   . LEU C 126  ? 3.3735 1.0130 1.1409 -0.3868 -0.4798 -0.0488 126  LEU B N   
13187 C CA  . LEU C 126  ? 3.3102 1.0228 1.1517 -0.3943 -0.4755 -0.0566 126  LEU B CA  
13188 C C   . LEU C 126  ? 3.3204 1.0105 1.1543 -0.3903 -0.4892 -0.0498 126  LEU B C   
13189 O O   . LEU C 126  ? 3.3177 0.9960 1.1484 -0.3649 -0.5197 -0.0290 126  LEU B O   
13190 C CB  . LEU C 126  ? 3.2188 1.0320 1.1526 -0.3737 -0.4929 -0.0459 126  LEU B CB  
13191 C CG  . LEU C 126  ? 3.1824 1.0537 1.1565 -0.3828 -0.4747 -0.0600 126  LEU B CG  
13192 C CD1 . LEU C 126  ? 3.2222 1.0680 1.1662 -0.4189 -0.4356 -0.0902 126  LEU B CD1 
13193 C CD2 . LEU C 126  ? 3.1864 1.0524 1.1458 -0.3641 -0.4870 -0.0481 126  LEU B CD2 
13194 N N   . PHE C 127  ? 3.5440 1.2282 1.3751 -0.4160 -0.4658 -0.0691 127  PHE B N   
13195 C CA  . PHE C 127  ? 3.5506 1.2169 1.3768 -0.4160 -0.4746 -0.0671 127  PHE B CA  
13196 C C   . PHE C 127  ? 3.5163 1.2708 1.4342 -0.4186 -0.4743 -0.0730 127  PHE B C   
13197 O O   . PHE C 127  ? 3.4943 1.2879 1.4438 -0.4393 -0.4490 -0.0925 127  PHE B O   
13198 C CB  . PHE C 127  ? 3.6812 1.2649 1.4258 -0.4441 -0.4466 -0.0852 127  PHE B CB  
13199 C CG  . PHE C 127  ? 3.7114 1.1972 1.3571 -0.4399 -0.4490 -0.0771 127  PHE B CG  
13200 C CD1 . PHE C 127  ? 3.7327 1.1973 1.3618 -0.4089 -0.4836 -0.0532 127  PHE B CD1 
13201 C CD2 . PHE C 127  ? 3.8486 1.2625 1.4181 -0.4666 -0.4163 -0.0937 127  PHE B CD2 
13202 C CE1 . PHE C 127  ? 3.8113 1.1850 1.3486 -0.4037 -0.4867 -0.0459 127  PHE B CE1 
13203 C CE2 . PHE C 127  ? 3.9236 1.2446 1.4001 -0.4619 -0.4182 -0.0852 127  PHE B CE2 
13204 C CZ  . PHE C 127  ? 3.9046 1.2058 1.3647 -0.4298 -0.4541 -0.0613 127  PHE B CZ  
13205 N N   . ILE C 128  ? 3.2520 1.0381 1.2142 -0.3973 -0.5025 -0.0568 128  ILE B N   
13206 C CA  . ILE C 128  ? 3.1948 1.0674 1.2493 -0.3957 -0.5056 -0.0590 128  ILE B CA  
13207 C C   . ILE C 128  ? 3.2065 1.0692 1.2673 -0.4015 -0.5084 -0.0639 128  ILE B C   
13208 O O   . ILE C 128  ? 3.1243 1.0041 1.2170 -0.3803 -0.5360 -0.0475 128  ILE B O   
13209 C CB  . ILE C 128  ? 3.0864 1.0236 1.2089 -0.3646 -0.5359 -0.0352 128  ILE B CB  
13210 C CG1 . ILE C 128  ? 3.1085 1.0139 1.1904 -0.3475 -0.5489 -0.0204 128  ILE B CG1 
13211 C CG2 . ILE C 128  ? 3.0459 1.0767 1.2547 -0.3669 -0.5276 -0.0408 128  ILE B CG2 
13212 C CD1 . ILE C 128  ? 3.0312 1.0101 1.1838 -0.3206 -0.5714 -0.0005 128  ILE B CD1 
13213 N N   . HIS C 129  ? 3.6763 1.5135 1.7091 -0.4309 -0.4787 -0.0878 129  HIS B N   
13214 C CA  . HIS C 129  ? 3.7184 1.5369 1.7455 -0.4406 -0.4764 -0.0967 129  HIS B CA  
13215 C C   . HIS C 129  ? 3.6776 1.5826 1.8035 -0.4344 -0.4853 -0.0964 129  HIS B C   
13216 O O   . HIS C 129  ? 3.7216 1.6662 1.8849 -0.4541 -0.4628 -0.1159 129  HIS B O   
13217 C CB  . HIS C 129  ? 3.7890 1.5511 1.7520 -0.4751 -0.4391 -0.1230 129  HIS B CB  
13218 C CG  . HIS C 129  ? 3.7672 1.5338 1.7446 -0.4917 -0.4273 -0.1396 129  HIS B CG  
13219 N ND1 . HIS C 129  ? 3.8205 1.5757 1.7807 -0.5243 -0.3907 -0.1670 129  HIS B ND1 
13220 C CD2 . HIS C 129  ? 3.7163 1.4971 1.7238 -0.4812 -0.4461 -0.1342 129  HIS B CD2 
13221 C CE1 . HIS C 129  ? 3.8323 1.5949 1.8108 -0.5325 -0.3878 -0.1774 129  HIS B CE1 
13222 N NE2 . HIS C 129  ? 3.7754 1.5535 1.7828 -0.5066 -0.4213 -0.1579 129  HIS B NE2 
13223 N N   . THR C 130  ? 3.1465 1.0810 1.3161 -0.4065 -0.5183 -0.0742 130  THR B N   
13224 C CA  . THR C 130  ? 3.0903 1.0938 1.3460 -0.3993 -0.5291 -0.0721 130  THR B CA  
13225 C C   . THR C 130  ? 3.1440 1.1123 1.3751 -0.4180 -0.5171 -0.0901 130  THR B C   
13226 O O   . THR C 130  ? 3.2150 1.1101 1.3745 -0.4191 -0.5213 -0.0899 130  THR B O   
13227 C CB  . THR C 130  ? 2.9948 1.0259 1.2944 -0.3659 -0.5668 -0.0444 130  THR B CB  
13228 O OG1 . THR C 130  ? 2.9403 1.0134 1.3042 -0.3615 -0.5768 -0.0442 130  THR B OG1 
13229 C CG2 . THR C 130  ? 3.0346 0.9888 1.2598 -0.3532 -0.5854 -0.0327 130  THR B CG2 
13230 N N   . ASP C 131  ? 3.8092 1.8286 2.0976 -0.4319 -0.5026 -0.1058 131  ASP B N   
13231 C CA  . ASP C 131  ? 3.8585 1.8457 2.1229 -0.4521 -0.4876 -0.1259 131  ASP B CA  
13232 C C   . ASP C 131  ? 3.8850 1.8328 2.1272 -0.4368 -0.5131 -0.1147 131  ASP B C   
13233 O O   . ASP C 131  ? 3.9758 1.8474 2.1371 -0.4465 -0.5070 -0.1221 131  ASP B O   
13234 C CB  . ASP C 131  ? 3.8192 1.8782 2.1642 -0.4630 -0.4751 -0.1411 131  ASP B CB  
13235 C CG  . ASP C 131  ? 3.7530 1.8515 2.1638 -0.4449 -0.5003 -0.1300 131  ASP B CG  
13236 O OD1 . ASP C 131  ? 3.6788 1.8100 2.1314 -0.4181 -0.5278 -0.1057 131  ASP B OD1 
13237 O OD2 . ASP C 131  ? 3.7809 1.8775 2.2023 -0.4572 -0.4925 -0.1456 131  ASP B OD2 
13238 N N   . LYS C 132  ? 3.0717 1.0719 1.3861 -0.4129 -0.5411 -0.0974 132  LYS B N   
13239 C CA  . LYS C 132  ? 3.0713 1.0417 1.3739 -0.3940 -0.5699 -0.0844 132  LYS B CA  
13240 C C   . LYS C 132  ? 3.0385 1.0345 1.3722 -0.3636 -0.5998 -0.0566 132  LYS B C   
13241 O O   . LYS C 132  ? 2.9557 0.9922 1.3186 -0.3591 -0.5961 -0.0488 132  LYS B O   
13242 C CB  . LYS C 132  ? 2.9987 1.0019 1.3583 -0.3955 -0.5750 -0.0926 132  LYS B CB  
13243 C CG  . LYS C 132  ? 2.9107 1.0069 1.3797 -0.3864 -0.5808 -0.0863 132  LYS B CG  
13244 C CD  . LYS C 132  ? 2.9792 1.1015 1.4855 -0.4058 -0.5628 -0.1089 132  LYS B CD  
13245 C CE  . LYS C 132  ? 2.8716 1.0783 1.4875 -0.3918 -0.5759 -0.1000 132  LYS B CE  
13246 N NZ  . LYS C 132  ? 2.9280 1.1674 1.5835 -0.4121 -0.5542 -0.1237 132  LYS B NZ  
13247 N N   . PRO C 133  ? 3.0960 1.0675 1.4210 -0.3428 -0.6290 -0.0425 133  PRO B N   
13248 C CA  . PRO C 133  ? 2.9787 0.9643 1.3208 -0.3153 -0.6556 -0.0174 133  PRO B CA  
13249 C C   . PRO C 133  ? 2.9262 0.9576 1.3442 -0.2946 -0.6826 -0.0043 133  PRO B C   
13250 O O   . PRO C 133  ? 2.9306 0.9469 1.3436 -0.2721 -0.7099 0.0122  133  PRO B O   
13251 C CB  . PRO C 133  ? 3.0569 0.9556 1.3035 -0.3102 -0.6658 -0.0150 133  PRO B CB  
13252 C CG  . PRO C 133  ? 3.1468 1.0031 1.3578 -0.3253 -0.6588 -0.0335 133  PRO B CG  
13253 C CD  . PRO C 133  ? 3.1289 1.0434 1.4069 -0.3433 -0.6388 -0.0492 133  PRO B CD  
13254 N N   . VAL C 134  ? 3.2208 1.3047 1.7066 -0.3029 -0.6744 -0.0130 134  VAL B N   
13255 C CA  . VAL C 134  ? 3.1030 1.2504 1.6820 -0.2834 -0.6959 0.0016  134  VAL B CA  
13256 C C   . VAL C 134  ? 3.1290 1.3408 1.7839 -0.2952 -0.6803 -0.0087 134  VAL B C   
13257 O O   . VAL C 134  ? 3.2304 1.4268 1.8648 -0.3185 -0.6583 -0.0317 134  VAL B O   
13258 C CB  . VAL C 134  ? 3.0625 1.1787 1.6350 -0.2684 -0.7231 0.0066  134  VAL B CB  
13259 C CG1 . VAL C 134  ? 2.9955 1.1763 1.6675 -0.2568 -0.7372 0.0139  134  VAL B CG1 
13260 C CG2 . VAL C 134  ? 3.0444 1.1308 1.5833 -0.2460 -0.7471 0.0257  134  VAL B CG2 
13261 N N   . TYR C 135  ? 2.7096 0.9933 1.4516 -0.2784 -0.6916 0.0087  135  TYR B N   
13262 C CA  . TYR C 135  ? 2.7089 1.0589 1.5252 -0.2862 -0.6777 0.0022  135  TYR B CA  
13263 C C   . TYR C 135  ? 2.6292 1.0371 1.5378 -0.2650 -0.6991 0.0206  135  TYR B C   
13264 O O   . TYR C 135  ? 2.5870 1.0027 1.5144 -0.2422 -0.7220 0.0429  135  TYR B O   
13265 C CB  . TYR C 135  ? 2.6585 1.0463 1.4848 -0.2902 -0.6610 0.0042  135  TYR B CB  
13266 C CG  . TYR C 135  ? 2.7312 1.0712 1.4764 -0.3124 -0.6364 -0.0143 135  TYR B CG  
13267 C CD1 . TYR C 135  ? 2.7785 1.1272 1.5212 -0.3379 -0.6079 -0.0391 135  TYR B CD1 
13268 C CD2 . TYR C 135  ? 2.8147 1.1032 1.4895 -0.3078 -0.6410 -0.0071 135  TYR B CD2 
13269 C CE1 . TYR C 135  ? 2.8459 1.1520 1.5180 -0.3590 -0.5839 -0.0564 135  TYR B CE1 
13270 C CE2 . TYR C 135  ? 2.8203 1.0644 1.4230 -0.3282 -0.6176 -0.0234 135  TYR B CE2 
13271 C CZ  . TYR C 135  ? 2.8669 1.1196 1.4685 -0.3543 -0.5886 -0.0481 135  TYR B CZ  
13272 O OH  . TYR C 135  ? 2.9370 1.1439 1.4674 -0.3755 -0.5639 -0.0648 135  TYR B OH  
13273 N N   . THR C 136  ? 2.8075 1.2569 1.7751 -0.2731 -0.6900 0.0105  136  THR B N   
13274 C CA  . THR C 136  ? 2.7531 1.2573 1.8117 -0.2560 -0.7065 0.0252  136  THR B CA  
13275 C C   . THR C 136  ? 2.7520 1.3288 1.8769 -0.2562 -0.6931 0.0291  136  THR B C   
13276 O O   . THR C 136  ? 2.7647 1.3444 1.8639 -0.2737 -0.6699 0.0132  136  THR B O   
13277 C CB  . THR C 136  ? 2.8061 1.2964 1.8784 -0.2660 -0.7064 0.0077  136  THR B CB  
13278 O OG1 . THR C 136  ? 2.8745 1.3535 1.9166 -0.2925 -0.6787 -0.0192 136  THR B OG1 
13279 C CG2 . THR C 136  ? 2.8215 1.2445 1.8354 -0.2622 -0.7236 0.0050  136  THR B CG2 
13280 N N   . PRO C 137  ? 2.6623 1.2979 1.8732 -0.2367 -0.7071 0.0493  137  PRO B N   
13281 C CA  . PRO C 137  ? 2.5952 1.3021 1.8700 -0.2321 -0.6975 0.0574  137  PRO B CA  
13282 C C   . PRO C 137  ? 2.6509 1.3685 1.9156 -0.2559 -0.6703 0.0311  137  PRO B C   
13283 O O   . PRO C 137  ? 2.6806 1.3810 1.9415 -0.2721 -0.6611 0.0095  137  PRO B O   
13284 C CB  . PRO C 137  ? 2.5693 1.3214 1.9336 -0.2168 -0.7119 0.0714  137  PRO B CB  
13285 C CG  . PRO C 137  ? 2.5153 1.2300 1.8665 -0.2035 -0.7355 0.0833  137  PRO B CG  
13286 C CD  . PRO C 137  ? 2.5988 1.2373 1.8542 -0.2191 -0.7316 0.0638  137  PRO B CD  
13287 N N   . ASP C 138  ? 2.8959 1.6420 2.1558 -0.2578 -0.6573 0.0317  138  ASP B N   
13288 C CA  . ASP C 138  ? 2.9375 1.7162 2.2136 -0.2752 -0.6337 0.0105  138  ASP B CA  
13289 C C   . ASP C 138  ? 3.0618 1.7883 2.2606 -0.3037 -0.6107 -0.0200 138  ASP B C   
13290 O O   . ASP C 138  ? 3.0935 1.8431 2.3012 -0.3204 -0.5895 -0.0409 138  ASP B O   
13291 C CB  . ASP C 138  ? 3.0545 1.8777 2.4087 -0.2736 -0.6344 0.0071  138  ASP B CB  
13292 C CG  . ASP C 138  ? 3.0471 1.9413 2.4863 -0.2485 -0.6473 0.0346  138  ASP B CG  
13293 O OD1 . ASP C 138  ? 3.0572 1.9955 2.5129 -0.2443 -0.6392 0.0389  138  ASP B OD1 
13294 O OD2 . ASP C 138  ? 3.0065 1.9119 2.4949 -0.2329 -0.6651 0.0515  138  ASP B OD2 
13295 N N   . GLN C 139  ? 2.7223 1.3784 1.8447 -0.3093 -0.6142 -0.0228 139  GLN B N   
13296 C CA  . GLN C 139  ? 2.8054 1.4112 1.8529 -0.3362 -0.5906 -0.0501 139  GLN B CA  
13297 C C   . GLN C 139  ? 2.8526 1.4718 1.8761 -0.3411 -0.5759 -0.0524 139  GLN B C   
13298 O O   . GLN C 139  ? 2.8087 1.4649 1.8608 -0.3215 -0.5877 -0.0307 139  GLN B O   
13299 C CB  . GLN C 139  ? 2.8633 1.3861 1.8316 -0.3410 -0.5976 -0.0532 139  GLN B CB  
13300 C CG  . GLN C 139  ? 2.8555 1.3621 1.8426 -0.3395 -0.6097 -0.0569 139  GLN B CG  
13301 C CD  . GLN C 139  ? 2.9184 1.3404 1.8179 -0.3498 -0.6104 -0.0679 139  GLN B CD  
13302 O OE1 . GLN C 139  ? 2.8717 1.2607 1.7471 -0.3336 -0.6328 -0.0520 139  GLN B OE1 
13303 N NE2 . GLN C 139  ? 3.0075 1.3946 1.8591 -0.3763 -0.5858 -0.0955 139  GLN B NE2 
13304 N N   . SER C 140  ? 2.6837 1.2764 1.6593 -0.3674 -0.5495 -0.0796 140  SER B N   
13305 C CA  . SER C 140  ? 2.7245 1.3139 1.6620 -0.3751 -0.5345 -0.0853 140  SER B CA  
13306 C C   . SER C 140  ? 2.7429 1.2468 1.5821 -0.3843 -0.5312 -0.0884 140  SER B C   
13307 O O   . SER C 140  ? 2.7951 1.2438 1.5794 -0.4060 -0.5157 -0.1091 140  SER B O   
13308 C CB  . SER C 140  ? 2.7813 1.4008 1.7336 -0.3984 -0.5058 -0.1142 140  SER B CB  
13309 O OG  . SER C 140  ? 2.7801 1.4356 1.7397 -0.3964 -0.4978 -0.1139 140  SER B OG  
13310 N N   . VAL C 141  ? 2.7887 1.2818 1.6057 -0.3672 -0.5457 -0.0676 141  VAL B N   
13311 C CA  . VAL C 141  ? 2.8769 1.2923 1.6021 -0.3731 -0.5435 -0.0685 141  VAL B CA  
13312 C C   . VAL C 141  ? 2.8922 1.2819 1.5650 -0.3998 -0.5125 -0.0935 141  VAL B C   
13313 O O   . VAL C 141  ? 2.8928 1.3068 1.5681 -0.3979 -0.5062 -0.0919 141  VAL B O   
13314 C CB  . VAL C 141  ? 2.7985 1.2165 1.5198 -0.3471 -0.5662 -0.0405 141  VAL B CB  
13315 C CG1 . VAL C 141  ? 2.8378 1.1789 1.4645 -0.3541 -0.5611 -0.0432 141  VAL B CG1 
13316 C CG2 . VAL C 141  ? 2.7225 1.1518 1.4835 -0.3223 -0.5963 -0.0169 141  VAL B CG2 
13317 N N   . LYS C 142  ? 2.9736 1.3150 1.6002 -0.4250 -0.4923 -0.1172 142  LYS B N   
13318 C CA  . LYS C 142  ? 3.1050 1.4042 1.6670 -0.4509 -0.4630 -0.1396 142  LYS B CA  
13319 C C   . LYS C 142  ? 3.1621 1.4028 1.6524 -0.4430 -0.4704 -0.1259 142  LYS B C   
13320 O O   . LYS C 142  ? 3.1729 1.3716 1.6318 -0.4275 -0.4920 -0.1085 142  LYS B O   
13321 C CB  . LYS C 142  ? 3.1611 1.4100 1.6790 -0.4781 -0.4411 -0.1650 142  LYS B CB  
13322 C CG  . LYS C 142  ? 3.1925 1.4910 1.7598 -0.4986 -0.4170 -0.1913 142  LYS B CG  
13323 C CD  . LYS C 142  ? 3.2987 1.5381 1.8011 -0.5319 -0.3848 -0.2209 142  LYS B CD  
13324 C CE  . LYS C 142  ? 3.3336 1.6248 1.8864 -0.5529 -0.3596 -0.2490 142  LYS B CE  
13325 N NZ  . LYS C 142  ? 3.2617 1.6183 1.9005 -0.5394 -0.3753 -0.2443 142  LYS B NZ  
13326 N N   . VAL C 143  ? 3.1586 1.3974 1.6246 -0.4528 -0.4533 -0.1344 143  VAL B N   
13327 C CA  . VAL C 143  ? 3.1618 1.3460 1.5616 -0.4453 -0.4596 -0.1222 143  VAL B CA  
13328 C C   . VAL C 143  ? 3.1957 1.3689 1.5626 -0.4657 -0.4317 -0.1411 143  VAL B C   
13329 O O   . VAL C 143  ? 3.2121 1.4440 1.6286 -0.4757 -0.4161 -0.1563 143  VAL B O   
13330 C CB  . VAL C 143  ? 3.0764 1.3022 1.5182 -0.4127 -0.4897 -0.0928 143  VAL B CB  
13331 C CG1 . VAL C 143  ? 3.0250 1.3436 1.5517 -0.4065 -0.4881 -0.0930 143  VAL B CG1 
13332 C CG2 . VAL C 143  ? 3.1262 1.3040 1.5051 -0.4062 -0.4931 -0.0834 143  VAL B CG2 
13333 N N   . ARG C 144  ? 3.1829 1.2797 1.4660 -0.4716 -0.4257 -0.1407 144  ARG B N   
13334 C CA  . ARG C 144  ? 3.2389 1.3194 1.4870 -0.4879 -0.4020 -0.1553 144  ARG B CA  
13335 C C   . ARG C 144  ? 3.2366 1.2571 1.4188 -0.4750 -0.4138 -0.1385 144  ARG B C   
13336 O O   . ARG C 144  ? 3.1524 1.1626 1.3327 -0.4496 -0.4434 -0.1139 144  ARG B O   
13337 C CB  . ARG C 144  ? 3.2430 1.2825 1.4487 -0.5238 -0.3656 -0.1862 144  ARG B CB  
13338 C CG  . ARG C 144  ? 3.2979 1.2757 1.4563 -0.5337 -0.3630 -0.1901 144  ARG B CG  
13339 C CD  . ARG C 144  ? 3.4239 1.3401 1.5151 -0.5689 -0.3246 -0.2176 144  ARG B CD  
13340 N NE  . ARG C 144  ? 3.4809 1.3343 1.5196 -0.5809 -0.3180 -0.2237 144  ARG B NE  
13341 C CZ  . ARG C 144  ? 3.5325 1.3950 1.5856 -0.6037 -0.2962 -0.2468 144  ARG B CZ  
13342 N NH1 . ARG C 144  ? 3.5218 1.4536 1.6411 -0.6168 -0.2792 -0.2663 144  ARG B NH1 
13343 N NH2 . ARG C 144  ? 3.5849 1.3877 1.5857 -0.6128 -0.2915 -0.2511 144  ARG B NH2 
13344 N N   . VAL C 145  ? 3.4753 1.4572 1.6060 -0.4926 -0.3905 -0.1526 145  VAL B N   
13345 C CA  . VAL C 145  ? 3.4137 1.3359 1.4793 -0.4823 -0.3987 -0.1391 145  VAL B CA  
13346 C C   . VAL C 145  ? 3.5686 1.4190 1.5559 -0.5095 -0.3669 -0.1587 145  VAL B C   
13347 O O   . VAL C 145  ? 3.5552 1.4278 1.5562 -0.5323 -0.3387 -0.1824 145  VAL B O   
13348 C CB  . VAL C 145  ? 3.3764 1.3544 1.4864 -0.4586 -0.4169 -0.1233 145  VAL B CB  
13349 C CG1 . VAL C 145  ? 3.4243 1.3434 1.4662 -0.4595 -0.4109 -0.1219 145  VAL B CG1 
13350 C CG2 . VAL C 145  ? 3.3023 1.3088 1.4507 -0.4261 -0.4539 -0.0947 145  VAL B CG2 
13351 N N   . TYR C 146  ? 3.5838 1.3465 1.4884 -0.5062 -0.3721 -0.1486 146  TYR B N   
13352 C CA  . TYR C 146  ? 3.6848 1.3675 1.5057 -0.5282 -0.3450 -0.1620 146  TYR B CA  
13353 C C   . TYR C 146  ? 3.7204 1.3860 1.5174 -0.5097 -0.3588 -0.1465 146  TYR B C   
13354 O O   . TYR C 146  ? 3.6864 1.3480 1.4827 -0.4806 -0.3913 -0.1215 146  TYR B O   
13355 C CB  . TYR C 146  ? 3.6587 1.2526 1.4002 -0.5354 -0.3422 -0.1602 146  TYR B CB  
13356 C CG  . TYR C 146  ? 3.7513 1.3711 1.5268 -0.5437 -0.3403 -0.1687 146  TYR B CG  
13357 C CD1 . TYR C 146  ? 3.8067 1.4651 1.6194 -0.5706 -0.3110 -0.1951 146  TYR B CD1 
13358 C CD2 . TYR C 146  ? 3.7362 1.3442 1.5100 -0.5243 -0.3680 -0.1517 146  TYR B CD2 
13359 C CE1 . TYR C 146  ? 3.7930 1.4761 1.6386 -0.5781 -0.3090 -0.2038 146  TYR B CE1 
13360 C CE2 . TYR C 146  ? 3.7110 1.3432 1.5176 -0.5320 -0.3661 -0.1607 146  TYR B CE2 
13361 C CZ  . TYR C 146  ? 3.7330 1.4023 1.5751 -0.5589 -0.3363 -0.1865 146  TYR B CZ  
13362 O OH  . TYR C 146  ? 3.6953 1.3892 1.5713 -0.5665 -0.3340 -0.1965 146  TYR B OH  
13363 N N   . SER C 147  ? 3.5333 1.1913 1.3141 -0.5264 -0.3343 -0.1623 147  SER B N   
13364 C CA  . SER C 147  ? 3.5653 1.2142 1.3298 -0.5104 -0.3449 -0.1508 147  SER B CA  
13365 C C   . SER C 147  ? 3.6863 1.2541 1.3702 -0.5322 -0.3164 -0.1646 147  SER B C   
13366 O O   . SER C 147  ? 3.7558 1.3195 1.4345 -0.5627 -0.2818 -0.1908 147  SER B O   
13367 C CB  . SER C 147  ? 3.5345 1.2828 1.3851 -0.5004 -0.3510 -0.1530 147  SER B CB  
13368 O OG  . SER C 147  ? 3.6053 1.3797 1.4748 -0.5285 -0.3178 -0.1821 147  SER B OG  
13369 N N   . LEU C 148  ? 4.4979 2.0017 2.1207 -0.5159 -0.3313 -0.1469 148  LEU B N   
13370 C CA  . LEU C 148  ? 4.5968 2.0138 2.1362 -0.5332 -0.3072 -0.1558 148  LEU B CA  
13371 C C   . LEU C 148  ? 4.6636 2.0798 2.1974 -0.5142 -0.3208 -0.1447 148  LEU B C   
13372 O O   . LEU C 148  ? 4.6354 2.0954 2.2087 -0.4835 -0.3541 -0.1241 148  LEU B O   
13373 C CB  . LEU C 148  ? 4.6267 1.9444 2.0770 -0.5336 -0.3092 -0.1457 148  LEU B CB  
13374 C CG  . LEU C 148  ? 4.6959 1.9604 2.0981 -0.5705 -0.2693 -0.1691 148  LEU B CG  
13375 C CD1 . LEU C 148  ? 4.6531 1.9983 2.1325 -0.5889 -0.2535 -0.1898 148  LEU B CD1 
13376 C CD2 . LEU C 148  ? 4.7384 1.9190 2.0635 -0.5686 -0.2747 -0.1583 148  LEU B CD2 
13377 N N   . ASN C 149  ? 4.7761 2.1427 2.2619 -0.5334 -0.2937 -0.1593 149  ASN B N   
13378 C CA  . ASN C 149  ? 4.7737 2.1227 2.2397 -0.5186 -0.3024 -0.1513 149  ASN B CA  
13379 C C   . ASN C 149  ? 4.8068 2.0478 2.1760 -0.5097 -0.3099 -0.1350 149  ASN B C   
13380 O O   . ASN C 149  ? 4.8316 2.0052 2.1417 -0.5224 -0.2989 -0.1358 149  ASN B O   
13381 C CB  . ASN C 149  ? 4.8823 2.2383 2.3530 -0.5451 -0.2679 -0.1782 149  ASN B CB  
13382 C CG  . ASN C 149  ? 5.0343 2.3134 2.4399 -0.5811 -0.2283 -0.1985 149  ASN B CG  
13383 O OD1 . ASN C 149  ? 5.0592 2.3005 2.4331 -0.5901 -0.2234 -0.1969 149  ASN B OD1 
13384 N ND2 . ASN C 149  ? 5.1319 2.3875 2.5176 -0.6024 -0.1990 -0.2184 149  ASN B ND2 
13385 N N   . ASP C 150  ? 4.3145 1.5404 1.6680 -0.4868 -0.3292 -0.1203 150  ASP B N   
13386 C CA  . ASP C 150  ? 4.4100 1.5331 1.6711 -0.4776 -0.3353 -0.1064 150  ASP B CA  
13387 C C   . ASP C 150  ? 4.4804 1.5111 1.6598 -0.5082 -0.3007 -0.1199 150  ASP B C   
13388 O O   . ASP C 150  ? 4.5249 1.4723 1.6283 -0.5012 -0.3081 -0.1065 150  ASP B O   
13389 C CB  . ASP C 150  ? 4.4581 1.5729 1.7105 -0.4699 -0.3349 -0.1068 150  ASP B CB  
13390 C CG  . ASP C 150  ? 4.6889 1.8302 1.9656 -0.5002 -0.2980 -0.1356 150  ASP B CG  
13391 O OD1 . ASP C 150  ? 4.7575 1.8385 1.9825 -0.5121 -0.2778 -0.1443 150  ASP B OD1 
13392 O OD2 . ASP C 150  ? 4.6618 1.8843 2.0102 -0.5124 -0.2888 -0.1503 150  ASP B OD2 
13393 N N   . ASP C 151  ? 4.7980 1.8424 1.9917 -0.5417 -0.2626 -0.1468 151  ASP B N   
13394 C CA  . ASP C 151  ? 4.9546 1.9129 2.0732 -0.5747 -0.2239 -0.1625 151  ASP B CA  
13395 C C   . ASP C 151  ? 4.9404 1.9071 2.0662 -0.5916 -0.2128 -0.1705 151  ASP B C   
13396 O O   . ASP C 151  ? 5.0355 1.9626 2.1278 -0.6244 -0.1755 -0.1903 151  ASP B O   
13397 C CB  . ASP C 151  ? 5.0639 2.0296 2.1937 -0.6040 -0.1861 -0.1899 151  ASP B CB  
13398 C CG  . ASP C 151  ? 5.2138 2.0674 2.2473 -0.6185 -0.1611 -0.1926 151  ASP B CG  
13399 O OD1 . ASP C 151  ? 5.2837 2.1375 2.3235 -0.6409 -0.1313 -0.2142 151  ASP B OD1 
13400 O OD2 . ASP C 151  ? 5.2533 2.0192 2.2060 -0.6076 -0.1706 -0.1738 151  ASP B OD2 
13401 N N   . LEU C 152  ? 4.3985 1.4182 1.5705 -0.5692 -0.2449 -0.1556 152  LEU B N   
13402 C CA  . LEU C 152  ? 4.4233 1.4503 1.6022 -0.5800 -0.2404 -0.1602 152  LEU B CA  
13403 C C   . LEU C 152  ? 4.5082 1.5502 1.7035 -0.6199 -0.1971 -0.1912 152  LEU B C   
13404 O O   . LEU C 152  ? 4.5626 1.5503 1.7083 -0.6407 -0.1753 -0.1996 152  LEU B O   
13405 C CB  . LEU C 152  ? 4.4818 1.4125 1.5697 -0.5714 -0.2503 -0.1436 152  LEU B CB  
13406 C CG  . LEU C 152  ? 4.4461 1.3625 1.5189 -0.5312 -0.2960 -0.1138 152  LEU B CG  
13407 C CD1 . LEU C 152  ? 4.3149 1.3378 1.4880 -0.5072 -0.3284 -0.1045 152  LEU B CD1 
13408 C CD2 . LEU C 152  ? 4.5160 1.3722 1.5328 -0.5174 -0.3026 -0.1021 152  LEU B CD2 
13409 N N   . LYS C 153  ? 4.7818 1.8980 2.0464 -0.6298 -0.1847 -0.2088 153  LYS B N   
13410 C CA  . LYS C 153  ? 4.8101 1.9621 2.1106 -0.6643 -0.1483 -0.2396 153  LYS B CA  
13411 C C   . LYS C 153  ? 4.7219 1.9956 2.1329 -0.6547 -0.1641 -0.2446 153  LYS B C   
13412 O O   . LYS C 153  ? 4.6149 1.9388 2.0690 -0.6230 -0.2002 -0.2241 153  LYS B O   
13413 C CB  . LYS C 153  ? 4.9229 2.0419 2.1967 -0.6904 -0.1121 -0.2612 153  LYS B CB  
13414 C CG  . LYS C 153  ? 5.0408 2.0509 2.2190 -0.7189 -0.0765 -0.2703 153  LYS B CG  
13415 C CD  . LYS C 153  ? 5.1516 2.1261 2.3040 -0.7442 -0.0406 -0.2910 153  LYS B CD  
13416 C CE  . LYS C 153  ? 5.2816 2.1522 2.3446 -0.7765 0.0002  -0.3025 153  LYS B CE  
13417 N NZ  . LYS C 153  ? 5.3398 2.1035 2.3016 -0.7619 -0.0114 -0.2763 153  LYS B NZ  
13418 N N   . PRO C 154  ? 4.2611 1.5823 1.7183 -0.6816 -0.1373 -0.2715 154  PRO B N   
13419 C CA  . PRO C 154  ? 4.2262 1.6552 1.7820 -0.6734 -0.1517 -0.2756 154  PRO B CA  
13420 C C   . PRO C 154  ? 4.1765 1.6798 1.7954 -0.6395 -0.1876 -0.2571 154  PRO B C   
13421 O O   . PRO C 154  ? 4.1236 1.6839 1.7954 -0.6176 -0.2159 -0.2418 154  PRO B O   
13422 C CB  . PRO C 154  ? 4.2408 1.7092 1.8347 -0.7065 -0.1141 -0.3113 154  PRO B CB  
13423 C CG  . PRO C 154  ? 4.3426 1.7137 1.8517 -0.7373 -0.0772 -0.3257 154  PRO B CG  
13424 C CD  . PRO C 154  ? 4.3676 1.6475 1.7913 -0.7212 -0.0905 -0.3012 154  PRO B CD  
13425 N N   . ALA C 155  ? 4.8752 2.3768 2.4880 -0.6361 -0.1848 -0.2592 155  ALA B N   
13426 C CA  . ALA C 155  ? 4.8359 2.3991 2.4984 -0.6046 -0.2162 -0.2421 155  ALA B CA  
13427 C C   . ALA C 155  ? 4.8141 2.4937 2.5784 -0.6010 -0.2208 -0.2531 155  ALA B C   
13428 O O   . ALA C 155  ? 4.7436 2.4864 2.5610 -0.5715 -0.2520 -0.2342 155  ALA B O   
13429 C CB  . ALA C 155  ? 4.7585 2.3029 2.4047 -0.5712 -0.2551 -0.2082 155  ALA B CB  
13430 N N   . LYS C 156  ? 4.1707 1.8776 1.9615 -0.6307 -0.1893 -0.2838 156  LYS B N   
13431 C CA  . LYS C 156  ? 4.1078 1.9230 1.9927 -0.6294 -0.1910 -0.2975 156  LYS B CA  
13432 C C   . LYS C 156  ? 4.0174 1.8947 1.9482 -0.5974 -0.2206 -0.2800 156  LYS B C   
13433 O O   . LYS C 156  ? 4.0532 1.8965 1.9482 -0.5904 -0.2230 -0.2747 156  LYS B O   
13434 C CB  . LYS C 156  ? 4.1965 2.0242 2.0930 -0.6641 -0.1515 -0.3359 156  LYS B CB  
13435 C CG  . LYS C 156  ? 4.2686 2.0417 2.1258 -0.6977 -0.1191 -0.3556 156  LYS B CG  
13436 C CD  . LYS C 156  ? 4.3883 2.1262 2.2168 -0.7337 -0.0766 -0.3891 156  LYS B CD  
13437 C CE  . LYS C 156  ? 4.4733 2.1424 2.2495 -0.7658 -0.0445 -0.4044 156  LYS B CE  
13438 N NZ  . LYS C 156  ? 4.5952 2.2165 2.3340 -0.8019 -0.0013 -0.4349 156  LYS B NZ  
13439 N N   . ARG C 157  ? 4.1095 2.0750 2.1175 -0.5774 -0.2431 -0.2701 157  ARG B N   
13440 C CA  . ARG C 157  ? 4.0235 2.0562 2.0814 -0.5464 -0.2709 -0.2530 157  ARG B CA  
13441 C C   . ARG C 157  ? 3.9662 2.0932 2.1093 -0.5304 -0.2892 -0.2454 157  ARG B C   
13442 O O   . ARG C 157  ? 3.9612 2.0995 2.1238 -0.5432 -0.2808 -0.2540 157  ARG B O   
13443 C CB  . ARG C 157  ? 3.9410 1.9242 1.9550 -0.5192 -0.2990 -0.2207 157  ARG B CB  
13444 C CG  . ARG C 157  ? 3.9491 1.8494 1.8861 -0.5261 -0.2878 -0.2231 157  ARG B CG  
13445 C CD  . ARG C 157  ? 3.8509 1.7093 1.7512 -0.4966 -0.3186 -0.1908 157  ARG B CD  
13446 N NE  . ARG C 157  ? 3.9152 1.6706 1.7255 -0.5057 -0.3074 -0.1907 157  ARG B NE  
13447 C CZ  . ARG C 157  ? 3.8959 1.5971 1.6593 -0.4834 -0.3306 -0.1656 157  ARG B CZ  
13448 N NH1 . ARG C 157  ? 3.7908 1.5326 1.5909 -0.4518 -0.3657 -0.1396 157  ARG B NH1 
13449 N NH2 . ARG C 157  ? 3.9801 1.5861 1.6603 -0.4926 -0.3186 -0.1668 157  ARG B NH2 
13450 N N   . GLU C 158  ? 4.3366 2.5306 2.5298 -0.5019 -0.3137 -0.2292 158  GLU B N   
13451 C CA  . GLU C 158  ? 4.2757 2.5537 2.5459 -0.4809 -0.3357 -0.2147 158  GLU B CA  
13452 C C   . GLU C 158  ? 4.1918 2.4581 2.4579 -0.4496 -0.3698 -0.1778 158  GLU B C   
13453 O O   . GLU C 158  ? 4.2033 2.4504 2.4453 -0.4313 -0.3848 -0.1616 158  GLU B O   
13454 C CB  . GLU C 158  ? 4.3153 2.6888 2.6545 -0.4711 -0.3378 -0.2236 158  GLU B CB  
13455 C CG  . GLU C 158  ? 4.4038 2.8156 2.7742 -0.4984 -0.3093 -0.2596 158  GLU B CG  
13456 C CD  . GLU C 158  ? 4.4151 2.9364 2.8726 -0.4830 -0.3195 -0.2617 158  GLU B CD  
13457 O OE1 . GLU C 158  ? 4.3727 2.9359 2.8743 -0.4626 -0.3413 -0.2398 158  GLU B OE1 
13458 O OE2 . GLU C 158  ? 4.4651 3.0303 2.9470 -0.4911 -0.3059 -0.2856 158  GLU B OE2 
13459 N N   . THR C 159  ? 3.5556 1.8345 1.8474 -0.4435 -0.3819 -0.1657 159  THR B N   
13460 C CA  . THR C 159  ? 3.4047 1.6707 1.6948 -0.4160 -0.4132 -0.1329 159  THR B CA  
13461 C C   . THR C 159  ? 3.2094 1.5588 1.5817 -0.3974 -0.4317 -0.1191 159  THR B C   
13462 O O   . THR C 159  ? 3.1929 1.5926 1.6125 -0.4096 -0.4191 -0.1354 159  THR B O   
13463 C CB  . THR C 159  ? 3.4661 1.6468 1.6945 -0.4264 -0.4116 -0.1293 159  THR B CB  
13464 O OG1 . THR C 159  ? 3.5679 1.6644 1.7149 -0.4464 -0.3909 -0.1431 159  THR B OG1 
13465 C CG2 . THR C 159  ? 3.4072 1.5735 1.6329 -0.3969 -0.4452 -0.0968 159  THR B CG2 
13466 N N   . VAL C 160  ? 3.1100 1.4720 1.4988 -0.3673 -0.4616 -0.0888 160  VAL B N   
13467 C CA  . VAL C 160  ? 2.9806 1.4098 1.4416 -0.3466 -0.4825 -0.0698 160  VAL B CA  
13468 C C   . VAL C 160  ? 2.9298 1.3165 1.3713 -0.3299 -0.5065 -0.0447 160  VAL B C   
13469 O O   . VAL C 160  ? 2.9278 1.2608 1.3188 -0.3192 -0.5181 -0.0319 160  VAL B O   
13470 C CB  . VAL C 160  ? 2.9341 1.4408 1.4521 -0.3199 -0.4992 -0.0535 160  VAL B CB  
13471 C CG1 . VAL C 160  ? 2.8531 1.3783 1.4035 -0.2902 -0.5299 -0.0204 160  VAL B CG1 
13472 C CG2 . VAL C 160  ? 2.9423 1.5324 1.5269 -0.3244 -0.4885 -0.0676 160  VAL B CG2 
13473 N N   . LEU C 161  ? 3.2672 1.6811 1.7524 -0.3267 -0.5146 -0.0383 161  LEU B N   
13474 C CA  . LEU C 161  ? 3.2034 1.6053 1.6980 -0.3052 -0.5418 -0.0123 161  LEU B CA  
13475 C C   . LEU C 161  ? 3.1323 1.6200 1.7118 -0.2787 -0.5623 0.0096  161  LEU B C   
13476 O O   . LEU C 161  ? 3.1316 1.6899 1.7625 -0.2760 -0.5560 0.0053  161  LEU B O   
13477 C CB  . LEU C 161  ? 3.2064 1.5634 1.6798 -0.3204 -0.5373 -0.0201 161  LEU B CB  
13478 C CG  . LEU C 161  ? 3.2373 1.6054 1.7199 -0.3494 -0.5095 -0.0486 161  LEU B CG  
13479 C CD1 . LEU C 161  ? 3.1896 1.6370 1.7583 -0.3434 -0.5142 -0.0464 161  LEU B CD1 
13480 C CD2 . LEU C 161  ? 3.2685 1.5536 1.6837 -0.3694 -0.4986 -0.0606 161  LEU B CD2 
13481 N N   . THR C 162  ? 3.3291 1.8086 1.9218 -0.2593 -0.5865 0.0327  162  THR B N   
13482 C CA  . THR C 162  ? 3.2347 1.7824 1.8976 -0.2313 -0.6081 0.0579  162  THR B CA  
13483 C C   . THR C 162  ? 3.1763 1.7099 1.8572 -0.2178 -0.6300 0.0765  162  THR B C   
13484 O O   . THR C 162  ? 3.1564 1.6609 1.8175 -0.2000 -0.6500 0.0946  162  THR B O   
13485 C CB  . THR C 162  ? 3.5145 2.0707 2.1662 -0.2124 -0.6183 0.0717  162  THR B CB  
13486 O OG1 . THR C 162  ? 3.4522 2.0171 2.1279 -0.1850 -0.6456 0.1001  162  THR B OG1 
13487 C CG2 . THR C 162  ? 3.5576 2.0353 2.1231 -0.2255 -0.6084 0.0586  162  THR B CG2 
13488 N N   . PHE C 163  ? 3.0742 1.6295 1.7943 -0.2261 -0.6262 0.0708  163  PHE B N   
13489 C CA  . PHE C 163  ? 3.0180 1.5609 1.7588 -0.2160 -0.6451 0.0845  163  PHE B CA  
13490 C C   . PHE C 163  ? 2.9540 1.5364 1.7426 -0.1853 -0.6705 0.1143  163  PHE B C   
13491 O O   . PHE C 163  ? 2.9451 1.5845 1.7718 -0.1724 -0.6714 0.1243  163  PHE B O   
13492 C CB  . PHE C 163  ? 3.0018 1.5822 1.7959 -0.2261 -0.6374 0.0756  163  PHE B CB  
13493 C CG  . PHE C 163  ? 3.0566 1.6169 1.8206 -0.2563 -0.6099 0.0452  163  PHE B CG  
13494 C CD1 . PHE C 163  ? 3.1174 1.6801 1.8545 -0.2696 -0.5900 0.0288  163  PHE B CD1 
13495 C CD2 . PHE C 163  ? 3.0423 1.5841 1.8081 -0.2717 -0.6031 0.0319  163  PHE B CD2 
13496 C CE1 . PHE C 163  ? 3.1959 1.7418 1.9084 -0.2982 -0.5634 -0.0003 163  PHE B CE1 
13497 C CE2 . PHE C 163  ? 3.1079 1.6330 1.8478 -0.3000 -0.5764 0.0031  163  PHE B CE2 
13498 C CZ  . PHE C 163  ? 3.1921 1.7195 1.9060 -0.3135 -0.5563 -0.0130 163  PHE B CZ  
13499 N N   . ILE C 164  ? 2.8055 1.3598 1.5941 -0.1734 -0.6907 0.1280  164  ILE B N   
13500 C CA  . ILE C 164  ? 2.7874 1.3696 1.6138 -0.1447 -0.7150 0.1555  164  ILE B CA  
13501 C C   . ILE C 164  ? 2.7691 1.3540 1.6361 -0.1342 -0.7336 0.1680  164  ILE B C   
13502 O O   . ILE C 164  ? 2.7758 1.3010 1.6016 -0.1353 -0.7443 0.1656  164  ILE B O   
13503 C CB  . ILE C 164  ? 2.8562 1.3874 1.6208 -0.1353 -0.7250 0.1616  164  ILE B CB  
13504 C CG1 . ILE C 164  ? 2.9294 1.4620 1.6596 -0.1445 -0.7069 0.1497  164  ILE B CG1 
13505 C CG2 . ILE C 164  ? 2.8099 1.3711 1.6156 -0.1058 -0.7496 0.1890  164  ILE B CG2 
13506 C CD1 . ILE C 164  ? 2.9539 1.4426 1.6294 -0.1334 -0.7168 0.1566  164  ILE B CD1 
13507 N N   . ASP C 165  ? 3.3054 1.9604 2.2541 -0.1229 -0.7377 0.1814  165  ASP B N   
13508 C CA  . ASP C 165  ? 3.3082 1.9737 2.3058 -0.1141 -0.7529 0.1919  165  ASP B CA  
13509 C C   . ASP C 165  ? 3.2212 1.8439 2.1960 -0.0984 -0.7765 0.2049  165  ASP B C   
13510 O O   . ASP C 165  ? 3.1884 1.7912 2.1279 -0.0880 -0.7839 0.2124  165  ASP B O   
13511 C CB  . ASP C 165  ? 3.3667 2.1154 2.4564 -0.0992 -0.7558 0.2101  165  ASP B CB  
13512 C CG  . ASP C 165  ? 3.4383 2.2173 2.5628 -0.0718 -0.7745 0.2381  165  ASP B CG  
13513 O OD1 . ASP C 165  ? 3.4903 2.2301 2.5698 -0.0634 -0.7857 0.2431  165  ASP B OD1 
13514 O OD2 . ASP C 165  ? 3.4262 2.2695 2.6247 -0.0583 -0.7774 0.2552  165  ASP B OD2 
13515 N N   . PRO C 166  ? 2.8044 1.4125 1.7994 -0.0968 -0.7886 0.2059  166  PRO B N   
13516 C CA  . PRO C 166  ? 2.7830 1.3494 1.7609 -0.0831 -0.8124 0.2146  166  PRO B CA  
13517 C C   . PRO C 166  ? 2.7111 1.3075 1.7248 -0.0558 -0.8320 0.2404  166  PRO B C   
13518 O O   . PRO C 166  ? 2.6745 1.2471 1.6893 -0.0424 -0.8532 0.2486  166  PRO B O   
13519 C CB  . PRO C 166  ? 2.7914 1.3627 1.8113 -0.0871 -0.8179 0.2105  166  PRO B CB  
13520 C CG  . PRO C 166  ? 2.8464 1.4243 1.8605 -0.1119 -0.7928 0.1893  166  PRO B CG  
13521 C CD  . PRO C 166  ? 2.8378 1.4587 1.8610 -0.1134 -0.7767 0.1915  166  PRO B CD  
13522 N N   . GLU C 167  ? 3.2517 1.8996 2.2939 -0.0474 -0.8251 0.2522  167  GLU B N   
13523 C CA  . GLU C 167  ? 3.2327 1.9077 2.3048 -0.0221 -0.8419 0.2758  167  GLU B CA  
13524 C C   . GLU C 167  ? 3.2660 1.9354 2.2934 -0.0195 -0.8352 0.2758  167  GLU B C   
13525 O O   . GLU C 167  ? 3.2677 1.9514 2.3055 0.0001  -0.8477 0.2925  167  GLU B O   
13526 C CB  . GLU C 167  ? 3.2175 1.9708 2.3839 -0.0081 -0.8438 0.2963  167  GLU B CB  
13527 C CG  . GLU C 167  ? 3.2179 1.9786 2.4387 -0.0039 -0.8562 0.3019  167  GLU B CG  
13528 C CD  . GLU C 167  ? 3.2186 2.0552 2.5335 0.0111  -0.8575 0.3246  167  GLU B CD  
13529 O OE1 . GLU C 167  ? 3.2009 2.0629 2.5483 0.0320  -0.8699 0.3460  167  GLU B OE1 
13530 O OE2 . GLU C 167  ? 3.2264 2.0963 2.5830 0.0024  -0.8459 0.3211  167  GLU B OE2 
13531 N N   . GLY C 168  ? 3.1985 1.8474 2.1772 -0.0400 -0.8149 0.2558  168  GLY B N   
13532 C CA  . GLY C 168  ? 3.2514 1.8782 2.1737 -0.0413 -0.8081 0.2506  168  GLY B CA  
13533 C C   . GLY C 168  ? 3.2902 1.9828 2.2488 -0.0393 -0.7938 0.2546  168  GLY B C   
13534 O O   . GLY C 168  ? 3.3054 2.0082 2.2500 -0.0291 -0.7946 0.2608  168  GLY B O   
13535 N N   . SER C 169  ? 2.5416 1.2799 1.5477 -0.0483 -0.7813 0.2504  169  SER B N   
13536 C CA  . SER C 169  ? 2.5971 1.4002 1.6381 -0.0469 -0.7673 0.2520  169  SER B CA  
13537 C C   . SER C 169  ? 2.6163 1.4143 1.6336 -0.0728 -0.7436 0.2256  169  SER B C   
13538 O O   . SER C 169  ? 2.5927 1.3872 1.6255 -0.0862 -0.7376 0.2153  169  SER B O   
13539 C CB  . SER C 169  ? 2.5962 1.4714 1.7258 -0.0299 -0.7743 0.2740  169  SER B CB  
13540 O OG  . SER C 169  ? 2.6420 1.5740 1.8067 -0.0358 -0.7577 0.2686  169  SER B OG  
13541 N N   . GLU C 170  ? 2.7796 1.5783 1.7616 -0.0801 -0.7298 0.2135  170  GLU B N   
13542 C CA  . GLU C 170  ? 2.8329 1.6263 1.7922 -0.1055 -0.7063 0.1865  170  GLU B CA  
13543 C C   . GLU C 170  ? 2.7497 1.5911 1.7716 -0.1103 -0.7007 0.1849  170  GLU B C   
13544 O O   . GLU C 170  ? 2.6633 1.5526 1.7488 -0.0919 -0.7130 0.2064  170  GLU B O   
13545 C CB  . GLU C 170  ? 2.9526 1.7784 1.9033 -0.1061 -0.6934 0.1791  170  GLU B CB  
13546 C CG  . GLU C 170  ? 3.0543 1.8328 1.9408 -0.1038 -0.6957 0.1769  170  GLU B CG  
13547 C CD  . GLU C 170  ? 3.1884 1.9879 2.0570 -0.1128 -0.6776 0.1600  170  GLU B CD  
13548 O OE1 . GLU C 170  ? 3.2199 2.0869 2.1381 -0.1118 -0.6689 0.1574  170  GLU B OE1 
13549 O OE2 . GLU C 170  ? 3.2596 2.0077 2.0648 -0.1206 -0.6723 0.1488  170  GLU B OE2 
13550 N N   . VAL C 171  ? 2.6542 1.4834 1.6601 -0.1347 -0.6816 0.1596  171  VAL B N   
13551 C CA  . VAL C 171  ? 2.6396 1.5173 1.7066 -0.1389 -0.6757 0.1566  171  VAL B CA  
13552 C C   . VAL C 171  ? 2.6534 1.5438 1.7108 -0.1623 -0.6510 0.1278  171  VAL B C   
13553 O O   . VAL C 171  ? 2.6507 1.5858 1.7580 -0.1665 -0.6439 0.1221  171  VAL B O   
13554 C CB  . VAL C 171  ? 2.6669 1.5165 1.7487 -0.1403 -0.6865 0.1609  171  VAL B CB  
13555 C CG1 . VAL C 171  ? 2.6712 1.5659 1.8122 -0.1474 -0.6782 0.1541  171  VAL B CG1 
13556 C CG2 . VAL C 171  ? 2.6061 1.4631 1.7184 -0.1146 -0.7109 0.1904  171  VAL B CG2 
13557 N N   . ASP C 172  ? 2.5729 1.4265 1.5688 -0.1769 -0.6377 0.1095  172  ASP B N   
13558 C CA  . ASP C 172  ? 2.6482 1.5122 1.6345 -0.2002 -0.6134 0.0804  172  ASP B CA  
13559 C C   . ASP C 172  ? 2.7088 1.5326 1.6290 -0.2102 -0.6028 0.0666  172  ASP B C   
13560 O O   . ASP C 172  ? 2.6820 1.4940 1.5823 -0.1942 -0.6152 0.0826  172  ASP B O   
13561 C CB  . ASP C 172  ? 2.6941 1.5183 1.6644 -0.2233 -0.6026 0.0609  172  ASP B CB  
13562 C CG  . ASP C 172  ? 2.7847 1.6409 1.7734 -0.2443 -0.5793 0.0332  172  ASP B CG  
13563 O OD1 . ASP C 172  ? 2.7656 1.6504 1.8017 -0.2468 -0.5785 0.0307  172  ASP B OD1 
13564 O OD2 . ASP C 172  ? 2.8603 1.7122 1.8176 -0.2584 -0.5619 0.0131  172  ASP B OD2 
13565 N N   . MET C 173  ? 2.8468 1.6480 1.7336 -0.2372 -0.5793 0.0365  173  MET B N   
13566 C CA  . MET C 173  ? 2.8996 1.6607 1.7240 -0.2504 -0.5655 0.0199  173  MET B CA  
13567 C C   . MET C 173  ? 2.9326 1.6965 1.7501 -0.2790 -0.5383 -0.0134 173  MET B C   
13568 O O   . MET C 173  ? 2.9438 1.7498 1.8102 -0.2842 -0.5329 -0.0210 173  MET B O   
13569 C CB  . MET C 173  ? 2.9205 1.7311 1.7650 -0.2309 -0.5721 0.0312  173  MET B CB  
13570 C CG  . MET C 173  ? 2.9675 1.7263 1.7525 -0.2248 -0.5782 0.0378  173  MET B CG  
13571 S SD  . MET C 173  ? 3.1249 1.9486 1.9481 -0.1929 -0.5948 0.0614  173  MET B SD  
13572 C CE  . MET C 173  ? 2.9410 1.8117 1.8354 -0.1667 -0.6188 0.0944  173  MET B CE  
13573 N N   . VAL C 174  ? 3.0408 1.7596 1.7988 -0.2975 -0.5208 -0.0338 174  VAL B N   
13574 C CA  . VAL C 174  ? 3.1256 1.8513 1.8782 -0.3249 -0.4931 -0.0674 174  VAL B CA  
13575 C C   . VAL C 174  ? 3.1944 1.8419 1.8651 -0.3462 -0.4757 -0.0854 174  VAL B C   
13576 O O   . VAL C 174  ? 3.2137 1.7935 1.8300 -0.3427 -0.4847 -0.0730 174  VAL B O   
13577 C CB  . VAL C 174  ? 3.1592 1.8923 1.9392 -0.3405 -0.4839 -0.0805 174  VAL B CB  
13578 C CG1 . VAL C 174  ? 3.1436 1.8100 1.8875 -0.3422 -0.4932 -0.0696 174  VAL B CG1 
13579 C CG2 . VAL C 174  ? 3.2395 1.9662 2.0035 -0.3720 -0.4531 -0.1177 174  VAL B CG2 
13580 N N   . GLU C 175  ? 3.3917 2.0493 2.0549 -0.3675 -0.4511 -0.1146 175  GLU B N   
13581 C CA  . GLU C 175  ? 3.4708 2.0577 2.0602 -0.3897 -0.4311 -0.1339 175  GLU B CA  
13582 C C   . GLU C 175  ? 3.5137 2.0768 2.0882 -0.4232 -0.4026 -0.1654 175  GLU B C   
13583 O O   . GLU C 175  ? 3.4751 2.0688 2.0912 -0.4266 -0.4022 -0.1687 175  GLU B O   
13584 C CB  . GLU C 175  ? 3.5565 2.1778 2.1512 -0.3856 -0.4257 -0.1426 175  GLU B CB  
13585 C CG  . GLU C 175  ? 3.5545 2.2772 2.2286 -0.3609 -0.4408 -0.1313 175  GLU B CG  
13586 C CD  . GLU C 175  ? 3.5713 2.3163 2.2414 -0.3444 -0.4481 -0.1247 175  GLU B CD  
13587 O OE1 . GLU C 175  ? 3.6123 2.3345 2.2471 -0.3611 -0.4296 -0.1477 175  GLU B OE1 
13588 O OE2 . GLU C 175  ? 3.5114 2.2970 2.2146 -0.3147 -0.4719 -0.0970 175  GLU B OE2 
13589 N N   . GLU C 176  ? 3.0884 1.5964 1.6045 -0.4480 -0.3783 -0.1884 176  GLU B N   
13590 C CA  . GLU C 176  ? 3.1502 1.6556 1.6654 -0.4805 -0.3473 -0.2233 176  GLU B CA  
13591 C C   . GLU C 176  ? 3.2841 1.7287 1.7342 -0.5048 -0.3215 -0.2457 176  GLU B C   
13592 O O   . GLU C 176  ? 3.2901 1.7025 1.7018 -0.4947 -0.3288 -0.2343 176  GLU B O   
13593 C CB  . GLU C 176  ? 3.1209 1.5966 1.6304 -0.4932 -0.3427 -0.2260 176  GLU B CB  
13594 C CG  . GLU C 176  ? 3.3382 1.8593 1.8928 -0.5152 -0.3206 -0.2560 176  GLU B CG  
13595 C CD  . GLU C 176  ? 3.4525 2.0451 2.0847 -0.4981 -0.3384 -0.2443 176  GLU B CD  
13596 O OE1 . GLU C 176  ? 3.4208 2.0598 2.0936 -0.4677 -0.3653 -0.2172 176  GLU B OE1 
13597 O OE2 . GLU C 176  ? 3.4336 2.0364 2.0874 -0.5150 -0.3248 -0.2623 176  GLU B OE2 
13598 N N   . ILE C 177  ? 3.7683 2.1983 2.2081 -0.5368 -0.2907 -0.2779 177  ILE B N   
13599 C CA  . ILE C 177  ? 3.8939 2.2671 2.2757 -0.5637 -0.2618 -0.3025 177  ILE B CA  
13600 C C   . ILE C 177  ? 3.9861 2.2563 2.2869 -0.5848 -0.2460 -0.3051 177  ILE B C   
13601 O O   . ILE C 177  ? 3.9575 2.2133 2.2584 -0.5956 -0.2404 -0.3089 177  ILE B O   
13602 C CB  . ILE C 177  ? 3.9425 2.3668 2.3648 -0.5879 -0.2341 -0.3406 177  ILE B CB  
13603 C CG1 . ILE C 177  ? 3.9754 2.3689 2.3846 -0.6186 -0.2080 -0.3639 177  ILE B CG1 
13604 C CG2 . ILE C 177  ? 3.8901 2.4239 2.4019 -0.5665 -0.2513 -0.3378 177  ILE B CG2 
13605 C CD1 . ILE C 177  ? 4.0393 2.3474 2.3738 -0.6522 -0.1740 -0.3870 177  ILE B CD1 
13606 N N   . ASP C 178  ? 4.3398 2.5374 2.5704 -0.5907 -0.2381 -0.3036 178  ASP B N   
13607 C CA  . ASP C 178  ? 4.4452 2.5415 2.5932 -0.6106 -0.2216 -0.3061 178  ASP B CA  
13608 C C   . ASP C 178  ? 4.5638 2.6283 2.6836 -0.6490 -0.1799 -0.3425 178  ASP B C   
13609 O O   . ASP C 178  ? 4.6356 2.6651 2.7178 -0.6595 -0.1644 -0.3529 178  ASP B O   
13610 C CB  . ASP C 178  ? 4.4373 2.4625 2.5180 -0.5944 -0.2372 -0.2817 178  ASP B CB  
13611 C CG  . ASP C 178  ? 4.4213 2.3465 2.4205 -0.6065 -0.2291 -0.2763 178  ASP B CG  
13612 O OD1 . ASP C 178  ? 4.4193 2.2843 2.3631 -0.5907 -0.2454 -0.2540 178  ASP B OD1 
13613 O OD2 . ASP C 178  ? 4.4198 2.3279 2.4107 -0.6313 -0.2065 -0.2950 178  ASP B OD2 
13614 N N   . HIS C 179  ? 4.5534 2.6298 2.6927 -0.6703 -0.1614 -0.3622 179  HIS B N   
13615 C CA  . HIS C 179  ? 4.6518 2.6980 2.7668 -0.7087 -0.1200 -0.3978 179  HIS B CA  
13616 C C   . HIS C 179  ? 4.6953 2.6250 2.7107 -0.7273 -0.1014 -0.3957 179  HIS B C   
13617 O O   . HIS C 179  ? 4.7613 2.6417 2.7317 -0.7518 -0.0717 -0.4153 179  HIS B O   
13618 C CB  . HIS C 179  ? 4.7063 2.8112 2.8817 -0.7236 -0.1074 -0.4201 179  HIS B CB  
13619 C CG  . HIS C 179  ? 4.8553 2.9722 3.0423 -0.7581 -0.0686 -0.4612 179  HIS B CG  
13620 N ND1 . HIS C 179  ? 4.8645 3.0741 3.1299 -0.7587 -0.0656 -0.4826 179  HIS B ND1 
13621 C CD2 . HIS C 179  ? 4.9757 3.0241 3.1069 -0.7932 -0.0310 -0.4853 179  HIS B CD2 
13622 C CE1 . HIS C 179  ? 4.9597 3.1592 3.2194 -0.7928 -0.0283 -0.5195 179  HIS B CE1 
13623 N NE2 . HIS C 179  ? 5.0271 3.1290 3.2065 -0.8148 -0.0059 -0.5216 179  HIS B NE2 
13624 N N   . ILE C 180  ? 4.6342 2.5199 2.6152 -0.7153 -0.1187 -0.3724 180  ILE B N   
13625 C CA  . ILE C 180  ? 4.6753 2.4498 2.5589 -0.7297 -0.1041 -0.3679 180  ILE B CA  
13626 C C   . ILE C 180  ? 4.5983 2.3170 2.4284 -0.7011 -0.1350 -0.3321 180  ILE B C   
13627 O O   . ILE C 180  ? 4.6048 2.2400 2.3567 -0.7066 -0.1257 -0.3273 180  ILE B O   
13628 C CB  . ILE C 180  ? 4.4893 2.2403 2.3602 -0.7498 -0.0875 -0.3796 180  ILE B CB  
13629 C CG1 . ILE C 180  ? 4.3774 2.1982 2.3170 -0.7286 -0.1158 -0.3669 180  ILE B CG1 
13630 C CG2 . ILE C 180  ? 4.5549 2.3201 2.4421 -0.7868 -0.0460 -0.4185 180  ILE B CG2 
13631 C CD1 . ILE C 180  ? 4.3608 2.1930 2.3194 -0.7519 -0.0947 -0.3892 180  ILE B CD1 
13632 N N   . GLY C 181  ? 3.4210 1.1854 1.2942 -0.6707 -0.1714 -0.3077 181  GLY B N   
13633 C CA  . GLY C 181  ? 3.4457 1.1688 1.2800 -0.6413 -0.2037 -0.2745 181  GLY B CA  
13634 C C   . GLY C 181  ? 3.3916 1.1468 1.2632 -0.6217 -0.2314 -0.2569 181  GLY B C   
13635 O O   . GLY C 181  ? 3.3955 1.1431 1.2615 -0.5928 -0.2641 -0.2288 181  GLY B O   
13636 N N   . ILE C 182  ? 4.4850 2.2760 2.3960 -0.6385 -0.2171 -0.2749 182  ILE B N   
13637 C CA  . ILE C 182  ? 4.4060 2.2374 2.3639 -0.6223 -0.2405 -0.2622 182  ILE B CA  
13638 C C   . ILE C 182  ? 4.3057 2.2470 2.3650 -0.6074 -0.2546 -0.2618 182  ILE B C   
13639 O O   . ILE C 182  ? 4.2938 2.2893 2.4058 -0.6233 -0.2377 -0.2840 182  ILE B O   
13640 C CB  . ILE C 182  ? 4.4215 2.2315 2.3672 -0.6484 -0.2170 -0.2828 182  ILE B CB  
13641 C CG1 . ILE C 182  ? 4.5203 2.2275 2.3667 -0.6744 -0.1873 -0.2948 182  ILE B CG1 
13642 C CG2 . ILE C 182  ? 4.3674 2.1885 2.3347 -0.6305 -0.2433 -0.2660 182  ILE B CG2 
13643 C CD1 . ILE C 182  ? 4.5725 2.2559 2.4023 -0.7041 -0.1582 -0.3185 182  ILE B CD1 
13644 N N   . ILE C 183  ? 3.9575 1.9313 2.0435 -0.5764 -0.2853 -0.2366 183  ILE B N   
13645 C CA  . ILE C 183  ? 3.8599 1.9359 2.0378 -0.5591 -0.3002 -0.2326 183  ILE B CA  
13646 C C   . ILE C 183  ? 3.7887 1.9194 2.0311 -0.5498 -0.3147 -0.2270 183  ILE B C   
13647 O O   . ILE C 183  ? 3.7585 1.8767 1.9998 -0.5294 -0.3406 -0.2034 183  ILE B O   
13648 C CB  . ILE C 183  ? 3.8064 1.8995 1.9928 -0.5275 -0.3292 -0.2054 183  ILE B CB  
13649 C CG1 . ILE C 183  ? 3.8604 1.9067 1.9902 -0.5362 -0.3145 -0.2128 183  ILE B CG1 
13650 C CG2 . ILE C 183  ? 3.7438 1.9418 2.0237 -0.5087 -0.3445 -0.1997 183  ILE B CG2 
13651 C CD1 . ILE C 183  ? 3.8338 1.8726 1.9504 -0.5068 -0.3418 -0.1859 183  ILE B CD1 
13652 N N   . SER C 184  ? 4.0737 2.2663 2.3745 -0.5641 -0.2984 -0.2492 184  SER B N   
13653 C CA  . SER C 184  ? 4.0054 2.2446 2.3646 -0.5602 -0.3067 -0.2489 184  SER B CA  
13654 C C   . SER C 184  ? 4.0225 2.3541 2.4687 -0.5315 -0.3329 -0.2311 184  SER B C   
13655 O O   . SER C 184  ? 4.0134 2.4163 2.5199 -0.5351 -0.3244 -0.2459 184  SER B O   
13656 C CB  . SER C 184  ? 4.0396 2.2947 2.4153 -0.5918 -0.2740 -0.2841 184  SER B CB  
13657 O OG  . SER C 184  ? 4.0955 2.2818 2.3995 -0.6202 -0.2433 -0.3051 184  SER B OG  
13658 N N   . PHE C 185  ? 3.5145 1.8446 1.9670 -0.5030 -0.3643 -0.1996 185  PHE B N   
13659 C CA  . PHE C 185  ? 3.4338 1.8463 1.9669 -0.4746 -0.3898 -0.1793 185  PHE B CA  
13660 C C   . PHE C 185  ? 3.3729 1.8372 1.9714 -0.4767 -0.3902 -0.1859 185  PHE B C   
13661 O O   . PHE C 185  ? 3.3774 1.8139 1.9578 -0.5007 -0.3703 -0.2076 185  PHE B O   
13662 C CB  . PHE C 185  ? 3.3763 1.7667 1.8959 -0.4458 -0.4215 -0.1453 185  PHE B CB  
13663 C CG  . PHE C 185  ? 3.3937 1.7524 1.8670 -0.4374 -0.4258 -0.1357 185  PHE B CG  
13664 C CD1 . PHE C 185  ? 3.3655 1.7792 1.8805 -0.4121 -0.4444 -0.1170 185  PHE B CD1 
13665 C CD2 . PHE C 185  ? 3.4576 1.7308 1.8448 -0.4546 -0.4106 -0.1455 185  PHE B CD2 
13666 C CE1 . PHE C 185  ? 3.3978 1.7828 1.8707 -0.4042 -0.4482 -0.1093 185  PHE B CE1 
13667 C CE2 . PHE C 185  ? 3.4892 1.7316 1.8340 -0.4463 -0.4149 -0.1368 185  PHE B CE2 
13668 C CZ  . PHE C 185  ? 3.4673 1.7662 1.8557 -0.4212 -0.4339 -0.1192 185  PHE B CZ  
13669 N N   . PRO C 186  ? 2.6652 1.2043 1.3397 -0.4514 -0.4121 -0.1672 186  PRO B N   
13670 C CA  . PRO C 186  ? 2.6162 1.2152 1.3632 -0.4493 -0.4145 -0.1712 186  PRO B CA  
13671 C C   . PRO C 186  ? 2.5898 1.1936 1.3659 -0.4260 -0.4427 -0.1434 186  PRO B C   
13672 O O   . PRO C 186  ? 2.5665 1.1834 1.3546 -0.4000 -0.4663 -0.1155 186  PRO B O   
13673 C CB  . PRO C 186  ? 2.5578 1.2432 1.3699 -0.4368 -0.4167 -0.1708 186  PRO B CB  
13674 C CG  . PRO C 186  ? 2.5694 1.2401 1.3462 -0.4240 -0.4245 -0.1568 186  PRO B CG  
13675 C CD  . PRO C 186  ? 2.6273 1.2092 1.3280 -0.4259 -0.4301 -0.1461 186  PRO B CD  
13676 N N   . ASP C 187  ? 3.3140 1.9105 2.1048 -0.4358 -0.4393 -0.1523 187  ASP B N   
13677 C CA  . ASP C 187  ? 3.2427 1.8344 2.0562 -0.4180 -0.4634 -0.1306 187  ASP B CA  
13678 C C   . ASP C 187  ? 3.1401 1.7855 2.0087 -0.3847 -0.4912 -0.0985 187  ASP B C   
13679 O O   . ASP C 187  ? 3.0924 1.8043 2.0114 -0.3753 -0.4910 -0.0960 187  ASP B O   
13680 C CB  . ASP C 187  ? 3.2711 1.8889 2.1311 -0.4284 -0.4564 -0.1457 187  ASP B CB  
13681 C CG  . ASP C 187  ? 3.3812 1.9336 2.1813 -0.4587 -0.4334 -0.1728 187  ASP B CG  
13682 O OD1 . ASP C 187  ? 3.4504 1.9450 2.1773 -0.4754 -0.4170 -0.1844 187  ASP B OD1 
13683 O OD2 . ASP C 187  ? 3.3904 1.9494 2.2175 -0.4657 -0.4310 -0.1825 187  ASP B OD2 
13684 N N   . PHE C 188  ? 2.9306 1.5466 1.7882 -0.3667 -0.5147 -0.0746 188  PHE B N   
13685 C CA  . PHE C 188  ? 2.8091 1.4731 1.7214 -0.3356 -0.5409 -0.0435 188  PHE B CA  
13686 C C   . PHE C 188  ? 2.7688 1.4454 1.7281 -0.3270 -0.5554 -0.0343 188  PHE B C   
13687 O O   . PHE C 188  ? 2.7720 1.3918 1.6933 -0.3312 -0.5614 -0.0349 188  PHE B O   
13688 C CB  . PHE C 188  ? 2.7655 1.3839 1.6268 -0.3211 -0.5568 -0.0239 188  PHE B CB  
13689 C CG  . PHE C 188  ? 2.6571 1.3110 1.5675 -0.2896 -0.5853 0.0089  188  PHE B CG  
13690 C CD1 . PHE C 188  ? 2.6137 1.2686 1.5583 -0.2787 -0.6027 0.0216  188  PHE B CD1 
13691 C CD2 . PHE C 188  ? 2.6615 1.3456 1.5825 -0.2713 -0.5942 0.0262  188  PHE B CD2 
13692 C CE1 . PHE C 188  ? 2.5434 1.2297 1.5343 -0.2508 -0.6275 0.0511  188  PHE B CE1 
13693 C CE2 . PHE C 188  ? 2.6002 1.3152 1.5649 -0.2430 -0.6188 0.0561  188  PHE B CE2 
13694 C CZ  . PHE C 188  ? 2.5411 1.2571 1.5415 -0.2332 -0.6351 0.0687  188  PHE B CZ  
13695 N N   . LYS C 189  ? 3.1274 1.8778 2.1687 -0.3147 -0.5608 -0.0264 189  LYS B N   
13696 C CA  . LYS C 189  ? 3.0580 1.8257 2.1519 -0.3070 -0.5732 -0.0187 189  LYS B CA  
13697 C C   . LYS C 189  ? 2.9925 1.7669 2.1133 -0.2789 -0.6014 0.0141  189  LYS B C   
13698 O O   . LYS C 189  ? 2.9561 1.7606 2.0934 -0.2597 -0.6119 0.0348  189  LYS B O   
13699 C CB  . LYS C 189  ? 3.0890 1.9308 2.2601 -0.3070 -0.5653 -0.0259 189  LYS B CB  
13700 C CG  . LYS C 189  ? 3.0578 1.9468 2.3079 -0.2840 -0.5856 -0.0022 189  LYS B CG  
13701 C CD  . LYS C 189  ? 3.0877 1.9843 2.3740 -0.2956 -0.5794 -0.0185 189  LYS B CD  
13702 C CE  . LYS C 189  ? 3.0593 2.0330 2.4402 -0.2782 -0.5871 -0.0050 189  LYS B CE  
13703 N NZ  . LYS C 189  ? 3.0022 2.0005 2.4258 -0.2487 -0.6116 0.0310  189  LYS B NZ  
13704 N N   . ILE C 190  ? 3.0938 1.8398 2.2191 -0.2770 -0.6133 0.0175  190  ILE B N   
13705 C CA  . ILE C 190  ? 3.0429 1.7954 2.2006 -0.2519 -0.6399 0.0459  190  ILE B CA  
13706 C C   . ILE C 190  ? 3.0382 1.8692 2.2911 -0.2353 -0.6467 0.0616  190  ILE B C   
13707 O O   . ILE C 190  ? 3.1279 1.9913 2.4198 -0.2453 -0.6347 0.0472  190  ILE B O   
13708 C CB  . ILE C 190  ? 3.0050 1.7025 2.1380 -0.2566 -0.6496 0.0408  190  ILE B CB  
13709 C CG1 . ILE C 190  ? 2.9746 1.5948 2.0116 -0.2774 -0.6372 0.0203  190  ILE B CG1 
13710 C CG2 . ILE C 190  ? 2.8613 1.5562 2.0165 -0.2315 -0.6775 0.0682  190  ILE B CG2 
13711 C CD1 . ILE C 190  ? 2.9716 1.5684 1.9542 -0.2734 -0.6366 0.0275  190  ILE B CD1 
13712 N N   . PRO C 191  ? 3.0829 1.9445 2.3732 -0.2095 -0.6655 0.0913  191  PRO B N   
13713 C CA  . PRO C 191  ? 3.0193 1.9522 2.3991 -0.1914 -0.6730 0.1101  191  PRO B CA  
13714 C C   . PRO C 191  ? 3.0617 1.9974 2.4874 -0.1935 -0.6780 0.1066  191  PRO B C   
13715 O O   . PRO C 191  ? 3.0423 1.9258 2.4382 -0.1992 -0.6856 0.1005  191  PRO B O   
13716 C CB  . PRO C 191  ? 2.9534 1.8962 2.3486 -0.1654 -0.6937 0.1419  191  PRO B CB  
13717 C CG  . PRO C 191  ? 2.9769 1.8741 2.2952 -0.1697 -0.6920 0.1379  191  PRO B CG  
13718 C CD  . PRO C 191  ? 3.0373 1.8703 2.2870 -0.1960 -0.6790 0.1085  191  PRO B CD  
13719 N N   . SER C 192  ? 2.7684 1.7650 2.2665 -0.1879 -0.6742 0.1102  192  SER B N   
13720 C CA  . SER C 192  ? 2.7365 1.7434 2.2887 -0.1874 -0.6795 0.1089  192  SER B CA  
13721 C C   . SER C 192  ? 2.6075 1.5915 2.1717 -0.1711 -0.7023 0.1303  192  SER B C   
13722 O O   . SER C 192  ? 2.5564 1.5201 2.1373 -0.1742 -0.7093 0.1248  192  SER B O   
13723 C CB  . SER C 192  ? 2.7448 1.8271 2.3800 -0.1755 -0.6766 0.1195  192  SER B CB  
13724 O OG  . SER C 192  ? 2.7966 1.9124 2.4235 -0.1815 -0.6604 0.1090  192  SER B OG  
13725 N N   . ASN C 193  ? 2.3576 1.3462 1.9133 -0.1538 -0.7135 0.1533  193  ASN B N   
13726 C CA  . ASN C 193  ? 2.3406 1.3090 1.9033 -0.1369 -0.7353 0.1744  193  ASN B CA  
13727 C C   . ASN C 193  ? 2.3434 1.3000 1.8608 -0.1271 -0.7402 0.1876  193  ASN B C   
13728 O O   . ASN C 193  ? 2.3339 1.3392 1.8850 -0.1114 -0.7409 0.2074  193  ASN B O   
13729 C CB  . ASN C 193  ? 2.3051 1.3274 1.9603 -0.1170 -0.7461 0.1986  193  ASN B CB  
13730 C CG  . ASN C 193  ? 2.2761 1.2888 1.9471 -0.0970 -0.7676 0.2234  193  ASN B CG  
13731 O OD1 . ASN C 193  ? 2.2769 1.2413 1.8900 -0.0975 -0.7763 0.2214  193  ASN B OD1 
13732 N ND2 . ASN C 193  ? 2.2440 1.3027 1.9944 -0.0790 -0.7761 0.2468  193  ASN B ND2 
13733 N N   . PRO C 194  ? 2.6962 1.5872 2.1345 -0.1367 -0.7425 0.1756  194  PRO B N   
13734 C CA  . PRO C 194  ? 2.6800 1.5468 2.0635 -0.1298 -0.7470 0.1839  194  PRO B CA  
13735 C C   . PRO C 194  ? 2.6148 1.4576 1.9952 -0.1110 -0.7707 0.2038  194  PRO B C   
13736 O O   . PRO C 194  ? 2.5670 1.4071 1.9850 -0.1040 -0.7845 0.2101  194  PRO B O   
13737 C CB  . PRO C 194  ? 2.7592 1.5623 2.0548 -0.1538 -0.7337 0.1558  194  PRO B CB  
13738 C CG  . PRO C 194  ? 2.8118 1.6053 2.1167 -0.1727 -0.7231 0.1332  194  PRO B CG  
13739 C CD  . PRO C 194  ? 2.7526 1.5881 2.1420 -0.1589 -0.7354 0.1478  194  PRO B CD  
13740 N N   . ARG C 195  ? 2.9748 1.7999 2.3107 -0.1033 -0.7752 0.2120  195  ARG B N   
13741 C CA  . ARG C 195  ? 2.9797 1.7755 2.3021 -0.0868 -0.7971 0.2272  195  ARG B CA  
13742 C C   . ARG C 195  ? 3.0211 1.7400 2.2735 -0.0986 -0.8031 0.2089  195  ARG B C   
13743 O O   . ARG C 195  ? 3.0785 1.7529 2.2576 -0.1151 -0.7908 0.1903  195  ARG B O   
13744 C CB  . ARG C 195  ? 3.0207 1.8254 2.3203 -0.0737 -0.7998 0.2417  195  ARG B CB  
13745 C CG  . ARG C 195  ? 2.9919 1.8691 2.3651 -0.0531 -0.8030 0.2682  195  ARG B CG  
13746 C CD  . ARG C 195  ? 3.0699 1.9849 2.4364 -0.0563 -0.7853 0.2663  195  ARG B CD  
13747 N NE  . ARG C 195  ? 3.1141 2.0399 2.4664 -0.0401 -0.7914 0.2826  195  ARG B NE  
13748 C CZ  . ARG C 195  ? 3.0908 2.0518 2.4923 -0.0169 -0.8051 0.3095  195  ARG B CZ  
13749 N NH1 . ARG C 195  ? 3.0335 2.0213 2.5025 -0.0072 -0.8141 0.3237  195  ARG B NH1 
13750 N NH2 . ARG C 195  ? 3.1158 2.0847 2.4996 -0.0035 -0.8093 0.3218  195  ARG B NH2 
13751 N N   . TYR C 196  ? 3.0317 1.7346 2.3065 -0.0896 -0.8220 0.2141  196  TYR B N   
13752 C CA  . TYR C 196  ? 3.0250 1.6587 2.2401 -0.1003 -0.8284 0.1955  196  TYR B CA  
13753 C C   . TYR C 196  ? 3.0050 1.5807 2.1472 -0.0934 -0.8417 0.1968  196  TYR B C   
13754 O O   . TYR C 196  ? 2.9537 1.5361 2.1153 -0.0728 -0.8611 0.2151  196  TYR B O   
13755 C CB  . TYR C 196  ? 3.0344 1.6746 2.3036 -0.0967 -0.8412 0.1948  196  TYR B CB  
13756 C CG  . TYR C 196  ? 3.0499 1.7245 2.3647 -0.1110 -0.8244 0.1832  196  TYR B CG  
13757 C CD1 . TYR C 196  ? 3.0945 1.7404 2.3587 -0.1352 -0.8045 0.1575  196  TYR B CD1 
13758 C CD2 . TYR C 196  ? 2.9984 1.7335 2.4064 -0.1005 -0.8277 0.1978  196  TYR B CD2 
13759 C CE1 . TYR C 196  ? 3.1064 1.7842 2.4120 -0.1483 -0.7890 0.1453  196  TYR B CE1 
13760 C CE2 . TYR C 196  ? 2.9994 1.7653 2.4483 -0.1129 -0.8126 0.1866  196  TYR B CE2 
13761 C CZ  . TYR C 196  ? 3.0488 1.7863 2.4460 -0.1367 -0.7936 0.1597  196  TYR B CZ  
13762 O OH  . TYR C 196  ? 3.0482 1.8148 2.4834 -0.1495 -0.7784 0.1464  196  TYR B OH  
13763 N N   . GLY C 197  ? 3.2434 1.7612 2.3012 -0.1107 -0.8305 0.1770  197  GLY B N   
13764 C CA  . GLY C 197  ? 3.2891 1.7458 2.2737 -0.1045 -0.8432 0.1769  197  GLY B CA  
13765 C C   . GLY C 197  ? 3.3505 1.7561 2.2459 -0.1231 -0.8246 0.1597  197  GLY B C   
13766 O O   . GLY C 197  ? 3.4161 1.8014 2.2833 -0.1452 -0.8059 0.1392  197  GLY B O   
13767 N N   . MET C 198  ? 2.7331 1.1179 1.5855 -0.1139 -0.8293 0.1681  198  MET B N   
13768 C CA  . MET C 198  ? 2.8065 1.1311 1.5666 -0.1286 -0.8153 0.1536  198  MET B CA  
13769 C C   . MET C 198  ? 2.7664 1.1204 1.5228 -0.1361 -0.7943 0.1531  198  MET B C   
13770 O O   . MET C 198  ? 2.7818 1.1609 1.5519 -0.1204 -0.8012 0.1690  198  MET B O   
13771 C CB  . MET C 198  ? 2.8784 1.1465 1.5815 -0.1133 -0.8366 0.1605  198  MET B CB  
13772 C CG  . MET C 198  ? 3.2671 1.4639 1.8703 -0.1275 -0.8238 0.1463  198  MET B CG  
13773 S SD  . MET C 198  ? 3.4898 1.6586 2.0584 -0.1604 -0.7958 0.1187  198  MET B SD  
13774 C CE  . MET C 198  ? 3.0042 1.1323 1.5625 -0.1553 -0.8169 0.1135  198  MET B CE  
13775 N N   . TRP C 199  ? 3.0256 1.3758 1.7622 -0.1604 -0.7685 0.1334  199  TRP B N   
13776 C CA  . TRP C 199  ? 3.0541 1.4329 1.7882 -0.1696 -0.7474 0.1290  199  TRP B CA  
13777 C C   . TRP C 199  ? 3.1299 1.4481 1.7757 -0.1776 -0.7384 0.1206  199  TRP B C   
13778 O O   . TRP C 199  ? 3.2075 1.4541 1.7833 -0.1854 -0.7396 0.1109  199  TRP B O   
13779 C CB  . TRP C 199  ? 3.1035 1.5080 1.8602 -0.1922 -0.7235 0.1100  199  TRP B CB  
13780 C CG  . TRP C 199  ? 3.0884 1.5707 1.9413 -0.1827 -0.7278 0.1207  199  TRP B CG  
13781 C CD1 . TRP C 199  ? 3.0648 1.5655 1.9710 -0.1721 -0.7442 0.1298  199  TRP B CD1 
13782 C CD2 . TRP C 199  ? 3.0844 1.6368 1.9919 -0.1823 -0.7153 0.1235  199  TRP B CD2 
13783 N NE1 . TRP C 199  ? 3.0464 1.6229 2.0371 -0.1654 -0.7417 0.1392  199  TRP B NE1 
13784 C CE2 . TRP C 199  ? 3.0448 1.6542 2.0362 -0.1710 -0.7244 0.1356  199  TRP B CE2 
13785 C CE3 . TRP C 199  ? 3.1144 1.6867 2.0075 -0.1902 -0.6972 0.1161  199  TRP B CE3 
13786 C CZ2 . TRP C 199  ? 2.9950 1.6786 2.0530 -0.1665 -0.7164 0.1418  199  TRP B CZ2 
13787 C CZ3 . TRP C 199  ? 3.0771 1.7252 2.0372 -0.1858 -0.6900 0.1209  199  TRP B CZ3 
13788 C CH2 . TRP C 199  ? 3.0280 1.7305 2.0683 -0.1735 -0.6997 0.1342  199  TRP B CH2 
13789 N N   . THR C 200  ? 2.7239 1.0695 1.3715 -0.1757 -0.7290 0.1239  200  THR B N   
13790 C CA  . THR C 200  ? 2.7303 1.0198 1.2975 -0.1829 -0.7200 0.1161  200  THR B CA  
13791 C C   . THR C 200  ? 2.7842 1.0922 1.3423 -0.2034 -0.6910 0.0990  200  THR B C   
13792 O O   . THR C 200  ? 2.7807 1.1518 1.3884 -0.1959 -0.6880 0.1058  200  THR B O   
13793 C CB  . THR C 200  ? 2.7033 0.9971 1.2697 -0.1573 -0.7403 0.1371  200  THR B CB  
13794 O OG1 . THR C 200  ? 2.7292 1.0345 1.3348 -0.1353 -0.7677 0.1553  200  THR B OG1 
13795 C CG2 . THR C 200  ? 2.7721 0.9880 1.2466 -0.1613 -0.7385 0.1308  200  THR B CG2 
13796 N N   . ILE C 201  ? 2.9752 1.2301 1.4712 -0.2290 -0.6692 0.0763  201  ILE B N   
13797 C CA  . ILE C 201  ? 2.9623 1.2281 1.4430 -0.2478 -0.6421 0.0591  201  ILE B CA  
13798 C C   . ILE C 201  ? 3.0482 1.2575 1.4549 -0.2479 -0.6392 0.0583  201  ILE B C   
13799 O O   . ILE C 201  ? 3.1705 1.3010 1.5036 -0.2539 -0.6399 0.0537  201  ILE B O   
13800 C CB  . ILE C 201  ? 3.0850 1.3296 1.5438 -0.2787 -0.6151 0.0322  201  ILE B CB  
13801 C CG1 . ILE C 201  ? 3.0405 1.3344 1.5680 -0.2795 -0.6178 0.0313  201  ILE B CG1 
13802 C CG2 . ILE C 201  ? 3.0938 1.3610 1.5498 -0.2975 -0.5875 0.0135  201  ILE B CG2 
13803 C CD1 . ILE C 201  ? 3.0237 1.3147 1.5440 -0.3091 -0.5892 0.0039  201  ILE B CD1 
13804 N N   . LYS C 202  ? 3.2414 1.4910 1.6679 -0.2401 -0.6364 0.0628  202  LYS B N   
13805 C CA  . LYS C 202  ? 3.2821 1.4874 1.6457 -0.2427 -0.6291 0.0586  202  LYS B CA  
13806 C C   . LYS C 202  ? 3.3253 1.5453 1.6813 -0.2663 -0.5986 0.0355  202  LYS B C   
13807 O O   . LYS C 202  ? 3.2993 1.5838 1.7138 -0.2733 -0.5878 0.0274  202  LYS B O   
13808 C CB  . LYS C 202  ? 3.3144 1.5514 1.7030 -0.2142 -0.6506 0.0808  202  LYS B CB  
13809 C CG  . LYS C 202  ? 3.3161 1.5401 1.7137 -0.1905 -0.6805 0.1025  202  LYS B CG  
13810 C CD  . LYS C 202  ? 3.3476 1.5936 1.7595 -0.1647 -0.6990 0.1218  202  LYS B CD  
13811 C CE  . LYS C 202  ? 3.3223 1.5735 1.7634 -0.1402 -0.7288 0.1434  202  LYS B CE  
13812 N NZ  . LYS C 202  ? 3.3180 1.6013 1.7841 -0.1144 -0.7461 0.1627  202  LYS B NZ  
13813 N N   . ALA C 203  ? 2.9791 1.1402 1.2648 -0.2778 -0.5851 0.0245  203  ALA B N   
13814 C CA  . ALA C 203  ? 3.0046 1.1744 1.2806 -0.3021 -0.5549 0.0001  203  ALA B CA  
13815 C C   . ALA C 203  ? 3.0835 1.2205 1.3115 -0.3003 -0.5503 -0.0016 203  ALA B C   
13816 O O   . ALA C 203  ? 3.0965 1.1632 1.2616 -0.2935 -0.5599 0.0068  203  ALA B O   
13817 C CB  . ALA C 203  ? 3.0680 1.1858 1.3000 -0.3323 -0.5308 -0.0225 203  ALA B CB  
13818 N N   . LYS C 204  ? 3.3836 1.5717 1.6416 -0.3066 -0.5352 -0.0138 204  LYS B N   
13819 C CA  . LYS C 204  ? 3.4719 1.6415 1.6947 -0.3065 -0.5278 -0.0193 204  LYS B CA  
13820 C C   . LYS C 204  ? 3.5084 1.6964 1.7332 -0.3325 -0.4965 -0.0482 204  LYS B C   
13821 O O   . LYS C 204  ? 3.4666 1.7159 1.7462 -0.3419 -0.4860 -0.0601 204  LYS B O   
13822 C CB  . LYS C 204  ? 3.4668 1.6969 1.7374 -0.2763 -0.5505 0.0015  204  LYS B CB  
13823 C CG  . LYS C 204  ? 3.4862 1.8164 1.8460 -0.2678 -0.5540 0.0049  204  LYS B CG  
13824 C CD  . LYS C 204  ? 3.4834 1.8645 1.8873 -0.2347 -0.5806 0.0314  204  LYS B CD  
13825 C CE  . LYS C 204  ? 3.4493 1.9168 1.9386 -0.2220 -0.5901 0.0430  204  LYS B CE  
13826 N NZ  . LYS C 204  ? 3.4328 1.9548 1.9648 -0.1919 -0.6107 0.0662  204  LYS B NZ  
13827 N N   . TYR C 205  ? 3.7479 1.8830 1.9139 -0.3436 -0.4821 -0.0601 205  TYR B N   
13828 C CA  . TYR C 205  ? 3.8856 2.0390 2.0548 -0.3669 -0.4532 -0.0882 205  TYR B CA  
13829 C C   . TYR C 205  ? 3.9477 2.1968 2.1885 -0.3513 -0.4602 -0.0867 205  TYR B C   
13830 O O   . TYR C 205  ? 3.9592 2.2302 2.2139 -0.3247 -0.4823 -0.0664 205  TYR B O   
13831 C CB  . TYR C 205  ? 3.9621 2.0359 2.0533 -0.3801 -0.4376 -0.0993 205  TYR B CB  
13832 C CG  . TYR C 205  ? 4.0271 2.0148 2.0508 -0.4052 -0.4185 -0.1109 205  TYR B CG  
13833 C CD1 . TYR C 205  ? 4.0457 1.9448 1.9959 -0.3993 -0.4279 -0.0972 205  TYR B CD1 
13834 C CD2 . TYR C 205  ? 4.0765 2.0728 2.1109 -0.4340 -0.3917 -0.1354 205  TYR B CD2 
13835 C CE1 . TYR C 205  ? 4.1013 1.9207 1.9869 -0.4216 -0.4101 -0.1070 205  TYR B CE1 
13836 C CE2 . TYR C 205  ? 4.1273 2.0456 2.0997 -0.4574 -0.3729 -0.1459 205  TYR B CE2 
13837 C CZ  . TYR C 205  ? 4.1413 1.9705 2.0379 -0.4511 -0.3820 -0.1312 205  TYR B CZ  
13838 O OH  . TYR C 205  ? 4.1898 1.9403 2.0215 -0.4740 -0.3626 -0.1413 205  TYR B OH  
13839 N N   . LYS C 206  ? 3.6526 1.9592 1.9385 -0.3674 -0.4416 -0.1085 206  LYS B N   
13840 C CA  . LYS C 206  ? 3.6477 2.0476 2.0009 -0.3532 -0.4469 -0.1093 206  LYS B CA  
13841 C C   . LYS C 206  ? 3.7058 2.0915 2.0303 -0.3447 -0.4483 -0.1095 206  LYS B C   
13842 O O   . LYS C 206  ? 3.6602 2.0700 2.0007 -0.3166 -0.4718 -0.0865 206  LYS B O   
13843 C CB  . LYS C 206  ? 3.7015 2.1505 2.0922 -0.3763 -0.4221 -0.1394 206  LYS B CB  
13844 C CG  . LYS C 206  ? 3.6884 2.2428 2.1582 -0.3590 -0.4310 -0.1377 206  LYS B CG  
13845 C CD  . LYS C 206  ? 3.7192 2.3216 2.2295 -0.3804 -0.4095 -0.1662 206  LYS B CD  
13846 C CE  . LYS C 206  ? 3.8160 2.3827 2.2869 -0.4108 -0.3789 -0.2010 206  LYS B CE  
13847 N NZ  . LYS C 206  ? 3.8278 2.4651 2.3523 -0.4247 -0.3617 -0.2296 206  LYS B NZ  
13848 N N   . GLU C 207  ? 3.6646 2.0069 1.9449 -0.3702 -0.4221 -0.1362 207  GLU B N   
13849 C CA  . GLU C 207  ? 3.7273 2.0490 1.9759 -0.3679 -0.4180 -0.1426 207  GLU B CA  
13850 C C   . GLU C 207  ? 3.6774 1.9388 1.8769 -0.3475 -0.4388 -0.1174 207  GLU B C   
13851 O O   . GLU C 207  ? 3.5889 1.8523 1.7995 -0.3262 -0.4634 -0.0907 207  GLU B O   
13852 C CB  . GLU C 207  ? 3.8727 2.1438 2.0763 -0.4027 -0.3836 -0.1760 207  GLU B CB  
13853 C CG  . GLU C 207  ? 3.9164 2.2504 2.1699 -0.4236 -0.3615 -0.2056 207  GLU B CG  
13854 C CD  . GLU C 207  ? 3.9159 2.3426 2.2305 -0.4090 -0.3673 -0.2121 207  GLU B CD  
13855 O OE1 . GLU C 207  ? 3.8949 2.3394 2.2149 -0.3824 -0.3884 -0.1927 207  GLU B OE1 
13856 O OE2 . GLU C 207  ? 3.9397 2.4222 2.2970 -0.4237 -0.3510 -0.2374 207  GLU B OE2 
13857 N N   . ASP C 208  ? 4.0261 2.2361 2.1741 -0.3537 -0.4290 -0.1270 208  ASP B N   
13858 C CA  . ASP C 208  ? 3.9585 2.1083 2.0567 -0.3349 -0.4473 -0.1061 208  ASP B CA  
13859 C C   . ASP C 208  ? 3.9300 1.9884 1.9645 -0.3451 -0.4458 -0.0992 208  ASP B C   
13860 O O   . ASP C 208  ? 3.9730 2.0058 1.9920 -0.3714 -0.4243 -0.1158 208  ASP B O   
13861 C CB  . ASP C 208  ? 3.9911 2.1098 2.0519 -0.3413 -0.4342 -0.1214 208  ASP B CB  
13862 C CG  . ASP C 208  ? 4.0506 2.1233 2.0740 -0.3780 -0.3987 -0.1530 208  ASP B CG  
13863 O OD1 . ASP C 208  ? 4.0427 2.0477 2.0199 -0.3959 -0.3873 -0.1552 208  ASP B OD1 
13864 O OD2 . ASP C 208  ? 4.1061 2.2118 2.1476 -0.3890 -0.3818 -0.1763 208  ASP B OD2 
13865 N N   . PHE C 209  ? 3.8191 1.8286 1.8157 -0.3239 -0.4682 -0.0759 209  PHE B N   
13866 C CA  . PHE C 209  ? 3.7809 1.7115 1.7224 -0.3243 -0.4760 -0.0630 209  PHE B CA  
13867 C C   . PHE C 209  ? 3.6843 1.6504 1.6658 -0.2960 -0.5088 -0.0347 209  PHE B C   
13868 O O   . PHE C 209  ? 3.6398 1.6766 1.6866 -0.2932 -0.5133 -0.0320 209  PHE B O   
13869 C CB  . PHE C 209  ? 3.7773 1.6712 1.6937 -0.3564 -0.4497 -0.0822 209  PHE B CB  
13870 C CG  . PHE C 209  ? 3.8421 1.6734 1.7001 -0.3855 -0.4172 -0.1072 209  PHE B CG  
13871 C CD1 . PHE C 209  ? 3.8709 1.7078 1.7352 -0.4174 -0.3865 -0.1335 209  PHE B CD1 
13872 C CD2 . PHE C 209  ? 3.8556 1.6216 1.6535 -0.3813 -0.4169 -0.1049 209  PHE B CD2 
13873 C CE1 . PHE C 209  ? 3.9356 1.7145 1.7481 -0.4453 -0.3549 -0.1571 209  PHE B CE1 
13874 C CE2 . PHE C 209  ? 3.9519 1.6576 1.6964 -0.4087 -0.3857 -0.1278 209  PHE B CE2 
13875 C CZ  . PHE C 209  ? 3.9838 1.6958 1.7358 -0.4413 -0.3541 -0.1539 209  PHE B CZ  
13876 N N   . SER C 210  ? 4.0123 1.9277 1.9545 -0.2753 -0.5313 -0.0144 210  SER B N   
13877 C CA  . SER C 210  ? 3.9231 1.8627 1.8976 -0.2481 -0.5631 0.0121  210  SER B CA  
13878 C C   . SER C 210  ? 3.8837 1.7987 1.8514 -0.2570 -0.5647 0.0147  210  SER B C   
13879 O O   . SER C 210  ? 3.7807 1.7295 1.7896 -0.2380 -0.5880 0.0332  210  SER B O   
13880 C CB  . SER C 210  ? 3.9326 1.8194 1.8623 -0.2243 -0.5859 0.0300  210  SER B CB  
13881 O OG  . SER C 210  ? 3.8572 1.7704 1.8217 -0.1976 -0.6168 0.0544  210  SER B OG  
13882 N N   . THR C 211  ? 3.5956 1.4533 1.5131 -0.2861 -0.5390 -0.0045 211  THR B N   
13883 C CA  . THR C 211  ? 3.6006 1.4054 1.4834 -0.2951 -0.5396 -0.0028 211  THR B CA  
13884 C C   . THR C 211  ? 3.5129 1.3758 1.4602 -0.2866 -0.5546 0.0072  211  THR B C   
13885 O O   . THR C 211  ? 3.4731 1.4080 1.4841 -0.2944 -0.5453 -0.0011 211  THR B O   
13886 C CB  . THR C 211  ? 3.7011 1.4444 1.5263 -0.3309 -0.5046 -0.0278 211  THR B CB  
13887 O OG1 . THR C 211  ? 3.7362 1.5360 1.6041 -0.3513 -0.4791 -0.0498 211  THR B OG1 
13888 C CG2 . THR C 211  ? 3.7663 1.4147 1.5018 -0.3354 -0.4967 -0.0301 211  THR B CG2 
13889 N N   . THR C 212  ? 3.3088 1.1362 1.2365 -0.2707 -0.5780 0.0244  212  THR B N   
13890 C CA  . THR C 212  ? 3.2417 1.1165 1.2274 -0.2584 -0.5969 0.0369  212  THR B CA  
13891 C C   . THR C 212  ? 3.2817 1.1240 1.2478 -0.2787 -0.5853 0.0259  212  THR B C   
13892 O O   . THR C 212  ? 3.3697 1.1297 1.2636 -0.2842 -0.5851 0.0247  212  THR B O   
13893 C CB  . THR C 212  ? 3.1944 1.0512 1.1739 -0.2270 -0.6319 0.0617  212  THR B CB  
13894 O OG1 . THR C 212  ? 3.2232 1.0691 1.1821 -0.2124 -0.6390 0.0684  212  THR B OG1 
13895 C CG2 . THR C 212  ? 3.0970 1.0321 1.1621 -0.2071 -0.6542 0.0782  212  THR B CG2 
13896 N N   . GLY C 213  ? 4.4295 2.3366 2.4597 -0.2885 -0.5766 0.0183  213  GLY B N   
13897 C CA  . GLY C 213  ? 4.4210 2.3112 2.4490 -0.3003 -0.5735 0.0126  213  GLY B CA  
13898 C C   . GLY C 213  ? 4.3274 2.2635 2.4160 -0.2761 -0.6034 0.0328  213  GLY B C   
13899 O O   . GLY C 213  ? 4.2756 2.2928 2.4412 -0.2627 -0.6123 0.0419  213  GLY B O   
13900 N N   . THR C 214  ? 3.6218 1.5074 1.6770 -0.2696 -0.6191 0.0400  214  THR B N   
13901 C CA  . THR C 214  ? 3.5198 1.4493 1.6366 -0.2509 -0.6442 0.0551  214  THR B CA  
13902 C C   . THR C 214  ? 3.4726 1.3775 1.5783 -0.2673 -0.6367 0.0433  214  THR B C   
13903 O O   . THR C 214  ? 3.5320 1.3725 1.5693 -0.2893 -0.6164 0.0269  214  THR B O   
13904 C CB  . THR C 214  ? 3.5198 1.4268 1.6253 -0.2208 -0.6780 0.0775  214  THR B CB  
13905 O OG1 . THR C 214  ? 3.5149 1.4491 1.6351 -0.2043 -0.6856 0.0887  214  THR B OG1 
13906 C CG2 . THR C 214  ? 3.4145 1.3710 1.5904 -0.2035 -0.7017 0.0912  214  THR B CG2 
13907 N N   . ALA C 215  ? 3.4093 1.3660 1.5832 -0.2570 -0.6520 0.0514  215  ALA B N   
13908 C CA  . ALA C 215  ? 3.3815 1.3216 1.5541 -0.2690 -0.6488 0.0415  215  ALA B CA  
13909 C C   . ALA C 215  ? 3.2906 1.2920 1.5453 -0.2481 -0.6740 0.0575  215  ALA B C   
13910 O O   . ALA C 215  ? 3.2171 1.2731 1.5258 -0.2279 -0.6885 0.0744  215  ALA B O   
13911 C CB  . ALA C 215  ? 3.3934 1.3517 1.5758 -0.2986 -0.6163 0.0183  215  ALA B CB  
13912 N N   . TYR C 216  ? 3.4312 1.4234 1.6952 -0.2525 -0.6786 0.0523  216  TYR B N   
13913 C CA  . TYR C 216  ? 3.3209 1.3727 1.6682 -0.2354 -0.6998 0.0653  216  TYR B CA  
13914 C C   . TYR C 216  ? 3.3189 1.3884 1.6979 -0.2514 -0.6891 0.0509  216  TYR B C   
13915 O O   . TYR C 216  ? 3.4286 1.4593 1.7609 -0.2760 -0.6663 0.0302  216  TYR B O   
13916 C CB  . TYR C 216  ? 3.3493 1.3713 1.6850 -0.2111 -0.7321 0.0813  216  TYR B CB  
13917 C CG  . TYR C 216  ? 3.4095 1.4144 1.7179 -0.1921 -0.7466 0.0965  216  TYR B CG  
13918 C CD1 . TYR C 216  ? 3.3841 1.4356 1.7512 -0.1652 -0.7717 0.1179  216  TYR B CD1 
13919 C CD2 . TYR C 216  ? 3.5452 1.4860 1.7688 -0.2013 -0.7344 0.0891  216  TYR B CD2 
13920 C CE1 . TYR C 216  ? 3.4199 1.4562 1.7622 -0.1476 -0.7847 0.1308  216  TYR B CE1 
13921 C CE2 . TYR C 216  ? 3.5847 1.5085 1.7826 -0.1838 -0.7473 0.1020  216  TYR B CE2 
13922 C CZ  . TYR C 216  ? 3.5238 1.4961 1.7811 -0.1568 -0.7728 0.1225  216  TYR B CZ  
13923 O OH  . TYR C 216  ? 3.5548 1.5099 1.7860 -0.1393 -0.7855 0.1344  216  TYR B OH  
13924 N N   . PHE C 217  ? 3.1380 1.2671 1.5988 -0.2364 -0.7060 0.0627  217  PHE B N   
13925 C CA  . PHE C 217  ? 3.0941 1.2450 1.5964 -0.2464 -0.7018 0.0523  217  PHE B CA  
13926 C C   . PHE C 217  ? 3.0368 1.2513 1.6311 -0.2247 -0.7248 0.0702  217  PHE B C   
13927 O O   . PHE C 217  ? 2.9965 1.2706 1.6491 -0.2103 -0.7306 0.0862  217  PHE B O   
13928 C CB  . PHE C 217  ? 3.1055 1.2821 1.6195 -0.2723 -0.6700 0.0319  217  PHE B CB  
13929 C CG  . PHE C 217  ? 3.0559 1.3215 1.6586 -0.2664 -0.6666 0.0392  217  PHE B CG  
13930 C CD1 . PHE C 217  ? 2.9956 1.3149 1.6751 -0.2638 -0.6706 0.0401  217  PHE B CD1 
13931 C CD2 . PHE C 217  ? 3.0654 1.3603 1.6737 -0.2635 -0.6586 0.0441  217  PHE B CD2 
13932 C CE1 . PHE C 217  ? 3.0174 1.4167 1.7760 -0.2575 -0.6674 0.0473  217  PHE B CE1 
13933 C CE2 . PHE C 217  ? 2.9540 1.3300 1.6407 -0.2572 -0.6557 0.0505  217  PHE B CE2 
13934 C CZ  . PHE C 217  ? 2.9259 1.3537 1.6872 -0.2539 -0.6601 0.0527  217  PHE B CZ  
13935 N N   . GLU C 218  ? 3.5559 1.7559 2.1613 -0.2228 -0.7371 0.0669  218  GLU B N   
13936 C CA  . GLU C 218  ? 3.5349 1.7812 2.2188 -0.2020 -0.7610 0.0832  218  GLU B CA  
13937 C C   . GLU C 218  ? 3.4850 1.7905 2.2444 -0.2111 -0.7498 0.0764  218  GLU B C   
13938 O O   . GLU C 218  ? 3.5121 1.8018 2.2518 -0.2333 -0.7304 0.0550  218  GLU B O   
13939 C CB  . GLU C 218  ? 3.6464 1.8382 2.2952 -0.1944 -0.7821 0.0814  218  GLU B CB  
13940 C CG  . GLU C 218  ? 3.6760 1.8975 2.3861 -0.1677 -0.8129 0.1010  218  GLU B CG  
13941 C CD  . GLU C 218  ? 3.7796 1.9383 2.4391 -0.1588 -0.8351 0.0979  218  GLU B CD  
13942 O OE1 . GLU C 218  ? 3.7649 1.9431 2.4744 -0.1406 -0.8594 0.1080  218  GLU B OE1 
13943 O OE2 . GLU C 218  ? 3.8773 1.9665 2.4464 -0.1699 -0.8280 0.0848  218  GLU B OE2 
13944 N N   . VAL C 219  ? 2.8086 1.1820 1.6547 -0.1937 -0.7617 0.0949  219  VAL B N   
13945 C CA  . VAL C 219  ? 2.7639 1.1928 1.6871 -0.1982 -0.7554 0.0913  219  VAL B CA  
13946 C C   . VAL C 219  ? 2.7163 1.1554 1.6899 -0.1817 -0.7797 0.1021  219  VAL B C   
13947 O O   . VAL C 219  ? 2.6888 1.1399 1.6866 -0.1595 -0.8009 0.1230  219  VAL B O   
13948 C CB  . VAL C 219  ? 2.6883 1.1932 1.6809 -0.1900 -0.7493 0.1053  219  VAL B CB  
13949 C CG1 . VAL C 219  ? 2.7011 1.2610 1.7787 -0.1894 -0.7487 0.1058  219  VAL B CG1 
13950 C CG2 . VAL C 219  ? 2.7272 1.2338 1.6831 -0.2072 -0.7238 0.0922  219  VAL B CG2 
13951 N N   . LYS C 220  ? 2.8609 1.2972 1.8534 -0.1928 -0.7760 0.0870  220  LYS B N   
13952 C CA  . LYS C 220  ? 2.8151 1.2579 1.8550 -0.1795 -0.7981 0.0933  220  LYS B CA  
13953 C C   . LYS C 220  ? 2.7570 1.2572 1.8809 -0.1838 -0.7906 0.0902  220  LYS B C   
13954 O O   . LYS C 220  ? 2.8811 1.3972 2.0072 -0.2020 -0.7677 0.0751  220  LYS B O   
13955 C CB  . LYS C 220  ? 2.8573 1.2274 1.8286 -0.1865 -0.8061 0.0763  220  LYS B CB  
13956 C CG  . LYS C 220  ? 2.8999 1.2081 1.7901 -0.1776 -0.8197 0.0811  220  LYS B CG  
13957 C CD  . LYS C 220  ? 3.0393 1.2732 1.8516 -0.1886 -0.8216 0.0606  220  LYS B CD  
13958 C CE  . LYS C 220  ? 3.0668 1.2366 1.7985 -0.1776 -0.8376 0.0654  220  LYS B CE  
13959 N NZ  . LYS C 220  ? 3.0217 1.1954 1.7865 -0.1526 -0.8703 0.0791  220  LYS B NZ  
13960 N N   . GLU C 221  ? 3.1831 1.7143 2.3777 -0.1666 -0.8101 0.1045  221  GLU B N   
13961 C CA  . GLU C 221  ? 3.2713 1.8564 2.5510 -0.1674 -0.8058 0.1044  221  GLU B CA  
13962 C C   . GLU C 221  ? 3.2769 1.8341 2.5521 -0.1804 -0.8055 0.0817  221  GLU B C   
13963 O O   . GLU C 221  ? 3.2496 1.7814 2.5262 -0.1717 -0.8255 0.0815  221  GLU B O   
13964 C CB  . GLU C 221  ? 3.3314 1.9649 2.6942 -0.1430 -0.8252 0.1313  221  GLU B CB  
13965 C CG  . GLU C 221  ? 3.4298 2.1103 2.8797 -0.1426 -0.8238 0.1312  221  GLU B CG  
13966 C CD  . GLU C 221  ? 3.4493 2.1761 2.9834 -0.1193 -0.8411 0.1582  221  GLU B CD  
13967 O OE1 . GLU C 221  ? 3.4368 2.1652 2.9641 -0.1033 -0.8528 0.1776  221  GLU B OE1 
13968 O OE2 . GLU C 221  ? 3.4615 2.2228 3.0691 -0.1172 -0.8421 0.1595  221  GLU B OE2 
13969 N N   . TYR C 222  ? 3.0215 1.5860 2.2944 -0.2009 -0.7832 0.0616  222  TYR B N   
13970 C CA  . TYR C 222  ? 3.0448 1.5862 2.3150 -0.2143 -0.7804 0.0384  222  TYR B CA  
13971 C C   . TYR C 222  ? 3.0078 1.5876 2.3682 -0.2015 -0.7961 0.0462  222  TYR B C   
13972 O O   . TYR C 222  ? 2.9665 1.6073 2.4065 -0.1934 -0.7939 0.0602  222  TYR B O   
13973 C CB  . TYR C 222  ? 3.0660 1.6139 2.3230 -0.2388 -0.7518 0.0152  222  TYR B CB  
13974 C CG  . TYR C 222  ? 3.0845 1.6143 2.3456 -0.2522 -0.7482 -0.0087 222  TYR B CG  
13975 C CD1 . TYR C 222  ? 3.1379 1.5993 2.3172 -0.2647 -0.7470 -0.0286 222  TYR B CD1 
13976 C CD2 . TYR C 222  ? 3.0698 1.6500 2.4159 -0.2515 -0.7464 -0.0111 222  TYR B CD2 
13977 C CE1 . TYR C 222  ? 3.1836 1.6289 2.3653 -0.2766 -0.7436 -0.0511 222  TYR B CE1 
13978 C CE2 . TYR C 222  ? 3.1107 1.6751 2.4620 -0.2634 -0.7433 -0.0339 222  TYR B CE2 
13979 C CZ  . TYR C 222  ? 3.1663 1.6639 2.4353 -0.2761 -0.7418 -0.0542 222  TYR B CZ  
13980 O OH  . TYR C 222  ? 3.1992 1.6821 2.4725 -0.2878 -0.7383 -0.0777 222  TYR B OH  
13981 N N   . VAL C 223  ? 2.7756 1.3185 2.1226 -0.1993 -0.8120 0.0369  223  VAL B N   
13982 C CA  . VAL C 223  ? 2.7059 1.2792 2.1342 -0.1913 -0.8242 0.0379  223  VAL B CA  
13983 C C   . VAL C 223  ? 2.7706 1.3180 2.1799 -0.2105 -0.8142 0.0077  223  VAL B C   
13984 O O   . VAL C 223  ? 2.8144 1.3113 2.1397 -0.2271 -0.8025 -0.0119 223  VAL B O   
13985 C CB  . VAL C 223  ? 2.6430 1.2046 2.0893 -0.1701 -0.8537 0.0525  223  VAL B CB  
13986 C CG1 . VAL C 223  ? 2.5845 1.1817 2.1238 -0.1618 -0.8654 0.0542  223  VAL B CG1 
13987 C CG2 . VAL C 223  ? 2.5916 1.1742 2.0467 -0.1522 -0.8618 0.0811  223  VAL B CG2 
13988 N N   . LEU C 224  ? 3.3152 1.8968 2.8020 -0.2088 -0.8174 0.0036  224  LEU B N   
13989 C CA  . LEU C 224  ? 3.3966 1.9555 2.8701 -0.2257 -0.8094 -0.0256 224  LEU B CA  
13990 C C   . LEU C 224  ? 3.4249 1.9444 2.8831 -0.2178 -0.8328 -0.0329 224  LEU B C   
13991 O O   . LEU C 224  ? 3.3813 1.9229 2.9010 -0.1991 -0.8541 -0.0173 224  LEU B O   
13992 C CB  . LEU C 224  ? 3.3516 1.9661 2.9138 -0.2295 -0.7991 -0.0298 224  LEU B CB  
13993 C CG  . LEU C 224  ? 3.4262 2.0271 2.9667 -0.2531 -0.7785 -0.0618 224  LEU B CG  
13994 C CD1 . LEU C 224  ? 3.4784 2.0353 2.9938 -0.2573 -0.7900 -0.0831 224  LEU B CD1 
13995 C CD2 . LEU C 224  ? 3.4664 2.0407 2.9251 -0.2722 -0.7547 -0.0743 224  LEU B CD2 
13996 N N   . PRO C 225  ? 3.8733 2.7945 2.5472 0.7689  -0.6130 -0.5115 225  PRO B N   
13997 C CA  . PRO C 225  ? 3.7727 2.6650 2.4917 0.7505  -0.6067 -0.4976 225  PRO B CA  
13998 C C   . PRO C 225  ? 3.7609 2.6703 2.5528 0.7575  -0.6298 -0.4954 225  PRO B C   
13999 O O   . PRO C 225  ? 3.7716 2.7157 2.5828 0.7518  -0.6480 -0.5366 225  PRO B O   
14000 C CB  . PRO C 225  ? 3.7267 2.6169 2.4269 0.7098  -0.6002 -0.5499 225  PRO B CB  
14001 C CG  . PRO C 225  ? 3.7583 2.6696 2.3978 0.7080  -0.5986 -0.5842 225  PRO B CG  
14002 C CD  . PRO C 225  ? 3.8457 2.7878 2.4861 0.7423  -0.6157 -0.5712 225  PRO B CD  
14003 N N   . HIS C 226  ? 3.5622 2.4467 2.3952 0.7698  -0.6286 -0.4470 226  HIS B N   
14004 C CA  . HIS C 226  ? 3.5934 2.4829 2.4969 0.7710  -0.6481 -0.4440 226  HIS B CA  
14005 C C   . HIS C 226  ? 3.4815 2.3498 2.4081 0.7326  -0.6454 -0.4701 226  HIS B C   
14006 O O   . HIS C 226  ? 3.4541 2.3385 2.4173 0.7199  -0.6609 -0.5052 226  HIS B O   
14007 C CB  . HIS C 226  ? 3.6443 2.5156 2.5827 0.8004  -0.6497 -0.3794 226  HIS B CB  
14008 C CG  . HIS C 226  ? 3.8110 2.7031 2.7309 0.8385  -0.6535 -0.3516 226  HIS B CG  
14009 N ND1 . HIS C 226  ? 3.8638 2.7361 2.7487 0.8590  -0.6352 -0.3040 226  HIS B ND1 
14010 C CD2 . HIS C 226  ? 3.9128 2.8434 2.8445 0.8605  -0.6733 -0.3628 226  HIS B CD2 
14011 C CE1 . HIS C 226  ? 3.9682 2.8651 2.8411 0.8910  -0.6437 -0.2883 226  HIS B CE1 
14012 N NE2 . HIS C 226  ? 3.9993 2.9324 2.9010 0.8923  -0.6678 -0.3229 226  HIS B NE2 
14013 N N   . PHE C 227  ? 3.5930 2.4250 2.4975 0.7143  -0.6252 -0.4526 227  PHE B N   
14014 C CA  . PHE C 227  ? 3.5008 2.3108 2.4201 0.6763  -0.6216 -0.4751 227  PHE B CA  
14015 C C   . PHE C 227  ? 3.4795 2.2656 2.3479 0.6543  -0.5972 -0.4773 227  PHE B C   
14016 O O   . PHE C 227  ? 3.5202 2.2882 2.3600 0.6695  -0.5803 -0.4381 227  PHE B O   
14017 C CB  . PHE C 227  ? 3.3797 2.1603 2.3549 0.6759  -0.6287 -0.4360 227  PHE B CB  
14018 C CG  . PHE C 227  ? 3.2790 2.0332 2.2551 0.6974  -0.6170 -0.3700 227  PHE B CG  
14019 C CD1 . PHE C 227  ? 3.1918 1.9146 2.1404 0.6828  -0.5948 -0.3473 227  PHE B CD1 
14020 C CD2 . PHE C 227  ? 3.2948 2.0561 2.3013 0.7326  -0.6276 -0.3290 227  PHE B CD2 
14021 C CE1 . PHE C 227  ? 3.1674 1.8672 2.1198 0.7037  -0.5825 -0.2848 227  PHE B CE1 
14022 C CE2 . PHE C 227  ? 3.2604 1.9988 2.2694 0.7528  -0.6158 -0.2668 227  PHE B CE2 
14023 C CZ  . PHE C 227  ? 3.2038 1.9118 2.1862 0.7387  -0.5928 -0.2447 227  PHE B CZ  
14024 N N   . SER C 228  ? 3.7902 2.5756 2.6480 0.6186  -0.5945 -0.5228 228  SER B N   
14025 C CA  . SER C 228  ? 3.7911 2.5573 2.5998 0.5960  -0.5722 -0.5316 228  SER B CA  
14026 C C   . SER C 228  ? 3.6588 2.3810 2.4797 0.5850  -0.5580 -0.4865 228  SER B C   
14027 O O   . SER C 228  ? 3.5888 2.2945 2.4443 0.5608  -0.5644 -0.4899 228  SER B O   
14028 C CB  . SER C 228  ? 3.8465 2.6281 2.6437 0.5607  -0.5749 -0.5942 228  SER B CB  
14029 O OG  . SER C 228  ? 3.8391 2.5957 2.6014 0.5329  -0.5548 -0.5999 228  SER B OG  
14030 N N   . VAL C 229  ? 3.0705 1.7734 1.8637 0.6030  -0.5390 -0.4432 229  VAL B N   
14031 C CA  . VAL C 229  ? 2.8549 1.5174 1.6541 0.5899  -0.5219 -0.4026 229  VAL B CA  
14032 C C   . VAL C 229  ? 2.9031 1.5522 1.6493 0.5669  -0.4989 -0.4232 229  VAL B C   
14033 O O   . VAL C 229  ? 2.9272 1.5844 1.6219 0.5800  -0.4860 -0.4328 229  VAL B O   
14034 C CB  . VAL C 229  ? 2.7897 1.4340 1.6025 0.6233  -0.5130 -0.3331 229  VAL B CB  
14035 C CG1 . VAL C 229  ? 2.7015 1.3110 1.4914 0.6151  -0.4855 -0.2985 229  VAL B CG1 
14036 C CG2 . VAL C 229  ? 2.7271 1.3641 1.6067 0.6289  -0.5324 -0.3012 229  VAL B CG2 
14037 N N   . SER C 230  ? 3.5058 2.1336 2.2638 0.5317  -0.4950 -0.4314 230  SER B N   
14038 C CA  . SER C 230  ? 3.4650 2.0751 2.1804 0.5072  -0.4728 -0.4447 230  SER B CA  
14039 C C   . SER C 230  ? 3.3996 1.9723 2.1232 0.5113  -0.4536 -0.3845 230  SER B C   
14040 O O   . SER C 230  ? 3.3815 1.9448 2.1405 0.5340  -0.4575 -0.3342 230  SER B O   
14041 C CB  . SER C 230  ? 3.4231 2.0340 2.1468 0.4641  -0.4802 -0.4909 230  SER B CB  
14042 O OG  . SER C 230  ? 3.3543 1.9448 2.1283 0.4476  -0.4909 -0.4682 230  SER B OG  
14043 N N   . ILE C 231  ? 2.6858 1.2377 1.3787 0.4890  -0.4327 -0.3887 231  ILE B N   
14044 C CA  . ILE C 231  ? 2.6367 1.1527 1.3453 0.4844  -0.4156 -0.3352 231  ILE B CA  
14045 C C   . ILE C 231  ? 2.5908 1.0898 1.2672 0.4508  -0.3973 -0.3575 231  ILE B C   
14046 O O   . ILE C 231  ? 2.6603 1.1631 1.2831 0.4523  -0.3813 -0.3840 231  ILE B O   
14047 C CB  . ILE C 231  ? 2.6103 1.1156 1.3093 0.5248  -0.3979 -0.2796 231  ILE B CB  
14048 C CG1 . ILE C 231  ? 2.5694 1.0395 1.2604 0.5194  -0.3695 -0.2364 231  ILE B CG1 
14049 C CG2 . ILE C 231  ? 2.6859 1.2124 1.3314 0.5489  -0.3922 -0.3068 231  ILE B CG2 
14050 C CD1 . ILE C 231  ? 2.6046 1.0629 1.2812 0.5589  -0.3477 -0.1836 231  ILE B CD1 
14051 N N   . GLU C 232  ? 3.0343 1.5148 1.7438 0.4191  -0.4021 -0.3488 232  GLU B N   
14052 C CA  . GLU C 232  ? 3.0671 1.5300 1.7559 0.3836  -0.3876 -0.3653 232  GLU B CA  
14053 C C   . GLU C 232  ? 3.0021 1.4302 1.7149 0.3808  -0.3719 -0.3031 232  GLU B C   
14054 O O   . GLU C 232  ? 2.9428 1.3598 1.7062 0.3816  -0.3846 -0.2627 232  GLU B O   
14055 C CB  . GLU C 232  ? 3.1310 1.6030 1.8366 0.3444  -0.4077 -0.4115 232  GLU B CB  
14056 C CG  . GLU C 232  ? 3.2767 1.7842 1.9856 0.3495  -0.4308 -0.4607 232  GLU B CG  
14057 C CD  . GLU C 232  ? 3.3293 1.8379 2.0883 0.3330  -0.4568 -0.4662 232  GLU B CD  
14058 O OE1 . GLU C 232  ? 3.3096 1.7922 2.0949 0.3086  -0.4591 -0.4426 232  GLU B OE1 
14059 O OE2 . GLU C 232  ? 3.3836 1.9188 2.1549 0.3446  -0.4754 -0.4946 232  GLU B OE2 
14060 N N   . PRO C 233  ? 2.9521 1.3623 1.6292 0.3767  -0.3444 -0.2956 233  PRO B N   
14061 C CA  . PRO C 233  ? 2.9402 1.3181 1.6310 0.3771  -0.3225 -0.2378 233  PRO B CA  
14062 C C   . PRO C 233  ? 2.8807 1.2429 1.5945 0.3329  -0.3280 -0.2417 233  PRO B C   
14063 O O   . PRO C 233  ? 2.9115 1.2868 1.6105 0.3036  -0.3398 -0.2969 233  PRO B O   
14064 C CB  . PRO C 233  ? 2.9916 1.3614 1.6222 0.3891  -0.2913 -0.2478 233  PRO B CB  
14065 C CG  . PRO C 233  ? 3.0127 1.4116 1.5989 0.3887  -0.3013 -0.3156 233  PRO B CG  
14066 C CD  . PRO C 233  ? 2.9931 1.4140 1.6125 0.3668  -0.3332 -0.3498 233  PRO B CD  
14067 N N   . GLU C 234  ? 3.4149 1.7507 2.1634 0.3276  -0.3194 -0.1843 234  GLU B N   
14068 C CA  . GLU C 234  ? 3.3288 1.6485 2.0974 0.2848  -0.3247 -0.1846 234  GLU B CA  
14069 C C   . GLU C 234  ? 3.3031 1.6233 2.0232 0.2587  -0.3103 -0.2344 234  GLU B C   
14070 O O   . GLU C 234  ? 3.3146 1.6444 2.0310 0.2256  -0.3263 -0.2807 234  GLU B O   
14071 C CB  . GLU C 234  ? 3.3018 1.5930 2.1106 0.2854  -0.3131 -0.1115 234  GLU B CB  
14072 C CG  . GLU C 234  ? 3.4499 1.7293 2.3072 0.2486  -0.3374 -0.0966 234  GLU B CG  
14073 C CD  . GLU C 234  ? 3.4337 1.6853 2.3304 0.2437  -0.3258 -0.0252 234  GLU B CD  
14074 O OE1 . GLU C 234  ? 3.4584 1.7014 2.3532 0.2751  -0.3000 0.0190  234  GLU B OE1 
14075 O OE2 . GLU C 234  ? 3.3951 1.6333 2.3243 0.2086  -0.3422 -0.0124 234  GLU B OE2 
14076 N N   . TYR C 235  ? 3.0556 1.3646 1.7376 0.2739  -0.2797 -0.2256 235  TYR B N   
14077 C CA  . TYR C 235  ? 3.0333 1.3424 1.6658 0.2525  -0.2655 -0.2740 235  TYR B CA  
14078 C C   . TYR C 235  ? 3.0558 1.3711 1.6367 0.2869  -0.2462 -0.2881 235  TYR B C   
14079 O O   . TYR C 235  ? 3.0713 1.3965 1.6565 0.3220  -0.2500 -0.2702 235  TYR B O   
14080 C CB  . TYR C 235  ? 3.0186 1.2986 1.6550 0.2289  -0.2445 -0.2463 235  TYR B CB  
14081 C CG  . TYR C 235  ? 3.0020 1.2686 1.6935 0.1999  -0.2598 -0.2117 235  TYR B CG  
14082 C CD1 . TYR C 235  ? 3.0252 1.2771 1.7176 0.1605  -0.2550 -0.2172 235  TYR B CD1 
14083 C CD2 . TYR C 235  ? 2.9949 1.2622 1.7374 0.2112  -0.2797 -0.1716 235  TYR B CD2 
14084 C CE1 . TYR C 235  ? 3.0218 1.2602 1.7633 0.1321  -0.2709 -0.1836 235  TYR B CE1 
14085 C CE2 . TYR C 235  ? 2.9887 1.2414 1.7802 0.1829  -0.2958 -0.1391 235  TYR B CE2 
14086 C CZ  . TYR C 235  ? 3.0091 1.2475 1.7991 0.1434  -0.2916 -0.1450 235  TYR B CZ  
14087 O OH  . TYR C 235  ? 2.9945 1.2181 1.8310 0.1151  -0.3092 -0.1115 235  TYR B OH  
14088 N N   . ASN C 236  ? 3.6239 1.9316 2.1551 0.2771  -0.2256 -0.3182 236  ASN B N   
14089 C CA  . ASN C 236  ? 3.6785 1.9903 2.1532 0.3064  -0.2091 -0.3380 236  ASN B CA  
14090 C C   . ASN C 236  ? 3.6503 1.9317 2.1016 0.3332  -0.1734 -0.2934 236  ASN B C   
14091 O O   . ASN C 236  ? 3.7641 2.0459 2.1714 0.3639  -0.1603 -0.2994 236  ASN B O   
14092 C CB  . ASN C 236  ? 3.7603 2.0854 2.1871 0.2830  -0.2110 -0.4068 236  ASN B CB  
14093 C CG  . ASN C 236  ? 3.8481 2.2110 2.2698 0.2859  -0.2389 -0.4554 236  ASN B CG  
14094 O OD1 . ASN C 236  ? 3.8626 2.2422 2.3282 0.2867  -0.2632 -0.4487 236  ASN B OD1 
14095 N ND2 . ASN C 236  ? 3.8995 2.2755 2.2686 0.2876  -0.2360 -0.5039 236  ASN B ND2 
14096 N N   . PHE C 237  ? 2.9257 1.1803 1.4047 0.3211  -0.1571 -0.2496 237  PHE B N   
14097 C CA  . PHE C 237  ? 2.9247 1.1491 1.3897 0.3468  -0.1213 -0.2013 237  PHE B CA  
14098 C C   . PHE C 237  ? 2.8366 1.0500 1.3666 0.3515  -0.1227 -0.1336 237  PHE B C   
14099 O O   . PHE C 237  ? 2.7563 0.9864 1.3319 0.3436  -0.1517 -0.1271 237  PHE B O   
14100 C CB  . PHE C 237  ? 2.8577 1.0580 1.2912 0.3243  -0.0963 -0.2155 237  PHE B CB  
14101 C CG  . PHE C 237  ? 2.9194 1.1284 1.2881 0.3157  -0.0951 -0.2832 237  PHE B CG  
14102 C CD1 . PHE C 237  ? 2.9648 1.1506 1.2748 0.3338  -0.0634 -0.2885 237  PHE B CD1 
14103 C CD2 . PHE C 237  ? 2.8991 1.1384 1.2651 0.2896  -0.1252 -0.3414 237  PHE B CD2 
14104 C CE1 . PHE C 237  ? 2.9878 1.1800 1.2372 0.3247  -0.0636 -0.3505 237  PHE B CE1 
14105 C CE2 . PHE C 237  ? 2.9758 1.2246 1.2851 0.2810  -0.1248 -0.4019 237  PHE B CE2 
14106 C CZ  . PHE C 237  ? 2.9477 1.1728 1.1984 0.2979  -0.0950 -0.4066 237  PHE B CZ  
14107 N N   . ILE C 238  ? 2.5111 0.6956 1.0475 0.3637  -0.0916 -0.0823 238  ILE B N   
14108 C CA  . ILE C 238  ? 2.4767 0.6513 1.0795 0.3653  -0.0935 -0.0152 238  ILE B CA  
14109 C C   . ILE C 238  ? 2.5400 0.6847 1.1440 0.3535  -0.0631 0.0138  238  ILE B C   
14110 O O   . ILE C 238  ? 2.5810 0.7050 1.1641 0.3831  -0.0285 0.0456  238  ILE B O   
14111 C CB  . ILE C 238  ? 2.4753 0.6495 1.0921 0.4112  -0.0840 0.0354  238  ILE B CB  
14112 C CG1 . ILE C 238  ? 2.4627 0.6677 1.0877 0.4221  -0.1172 0.0114  238  ILE B CG1 
14113 C CG2 . ILE C 238  ? 2.4604 0.6197 1.1443 0.4134  -0.0788 0.1112  238  ILE B CG2 
14114 C CD1 . ILE C 238  ? 2.4610 0.6687 1.1327 0.4538  -0.1215 0.0724  238  ILE B CD1 
14115 N N   . GLY C 239  ? 3.4859 1.6282 2.1109 0.3100  -0.0755 -0.0003 239  GLY B N   
14116 C CA  . GLY C 239  ? 3.4944 1.6100 2.1299 0.2914  -0.0515 0.0277  239  GLY B CA  
14117 C C   . GLY C 239  ? 3.4860 1.5924 2.1945 0.2890  -0.0555 0.1007  239  GLY B C   
14118 O O   . GLY C 239  ? 3.4574 1.5792 2.2097 0.2856  -0.0857 0.1157  239  GLY B O   
14119 N N   . TYR C 240  ? 3.2077 1.2882 1.9305 0.2899  -0.0253 0.1464  240  TYR B N   
14120 C CA  . TYR C 240  ? 3.2224 1.2924 2.0119 0.2989  -0.0208 0.2260  240  TYR B CA  
14121 C C   . TYR C 240  ? 3.2065 1.2884 2.0576 0.2665  -0.0608 0.2422  240  TYR B C   
14122 O O   . TYR C 240  ? 3.1583 1.2325 2.0694 0.2690  -0.0619 0.3087  240  TYR B O   
14123 C CB  . TYR C 240  ? 3.2215 1.2638 2.0202 0.2923  0.0130  0.2633  240  TYR B CB  
14124 C CG  . TYR C 240  ? 3.1323 1.1741 1.9550 0.2412  -0.0071 0.2501  240  TYR B CG  
14125 C CD1 . TYR C 240  ? 3.0348 1.0750 1.9279 0.2200  -0.0255 0.3031  240  TYR B CD1 
14126 C CD2 . TYR C 240  ? 3.1424 1.1865 1.9167 0.2127  -0.0107 0.1829  240  TYR B CD2 
14127 C CE1 . TYR C 240  ? 2.9858 1.0252 1.8971 0.1714  -0.0461 0.2893  240  TYR B CE1 
14128 C CE2 . TYR C 240  ? 3.0997 1.1440 1.8933 0.1650  -0.0295 0.1691  240  TYR B CE2 
14129 C CZ  . TYR C 240  ? 3.0370 1.0787 1.8974 0.1440  -0.0474 0.2215  240  TYR B CZ  
14130 O OH  . TYR C 240  ? 3.0495 1.0904 1.9241 0.0951  -0.0665 0.2061  240  TYR B OH  
14131 N N   . LYS C 241  ? 3.5237 1.6227 2.3607 0.2346  -0.0928 0.1834  241  LYS B N   
14132 C CA  . LYS C 241  ? 3.5391 1.6464 2.4285 0.2034  -0.1313 0.1950  241  LYS B CA  
14133 C C   . LYS C 241  ? 3.5807 1.6984 2.5111 0.2293  -0.1499 0.2322  241  LYS B C   
14134 O O   . LYS C 241  ? 3.5674 1.6775 2.5584 0.2229  -0.1608 0.2911  241  LYS B O   
14135 C CB  . LYS C 241  ? 3.3282 1.4509 2.1894 0.1664  -0.1588 0.1214  241  LYS B CB  
14136 C CG  . LYS C 241  ? 3.1022 1.2130 1.9381 0.1335  -0.1444 0.0963  241  LYS B CG  
14137 C CD  . LYS C 241  ? 3.2811 1.4081 2.0879 0.0972  -0.1692 0.0237  241  LYS B CD  
14138 C CE  . LYS C 241  ? 3.6707 1.7843 2.4715 0.0563  -0.1618 0.0137  241  LYS B CE  
14139 N NZ  . LYS C 241  ? 3.6806 1.7790 2.4412 0.0676  -0.1231 0.0077  241  LYS B NZ  
14140 N N   . ASN C 242  ? 2.8715 1.0065 1.7703 0.2581  -0.1543 0.1995  242  ASN B N   
14141 C CA  . ASN C 242  ? 2.8775 1.0210 1.8100 0.2908  -0.1647 0.2388  242  ASN B CA  
14142 C C   . ASN C 242  ? 2.9537 1.0896 1.8637 0.3374  -0.1269 0.2696  242  ASN B C   
14143 O O   . ASN C 242  ? 2.9691 1.1036 1.8181 0.3499  -0.1042 0.2305  242  ASN B O   
14144 C CB  . ASN C 242  ? 2.8180 0.9865 1.7331 0.2950  -0.1945 0.1864  242  ASN B CB  
14145 C CG  . ASN C 242  ? 2.7422 0.9210 1.6299 0.2552  -0.2156 0.1156  242  ASN B CG  
14146 O OD1 . ASN C 242  ? 2.7027 0.8939 1.6106 0.2371  -0.2497 0.0933  242  ASN B OD1 
14147 N ND2 . ASN C 242  ? 2.8073 0.9802 1.6485 0.2415  -0.1948 0.0795  242  ASN B ND2 
14148 N N   . PHE C 243  ? 3.3625 1.4924 2.3199 0.3630  -0.1196 0.3399  243  PHE B N   
14149 C CA  . PHE C 243  ? 3.4954 1.6173 2.4310 0.4094  -0.0820 0.3720  243  PHE B CA  
14150 C C   . PHE C 243  ? 3.5507 1.6778 2.5441 0.4348  -0.0914 0.4358  243  PHE B C   
14151 O O   . PHE C 243  ? 3.5871 1.7147 2.5703 0.4779  -0.0700 0.4642  243  PHE B O   
14152 C CB  . PHE C 243  ? 3.5178 1.6139 2.4466 0.4088  -0.0419 0.4023  243  PHE B CB  
14153 C CG  . PHE C 243  ? 3.6011 1.6851 2.4929 0.4555  0.0012  0.4243  243  PHE B CG  
14154 C CD1 . PHE C 243  ? 3.6544 1.7446 2.4741 0.4775  0.0106  0.3711  243  PHE B CD1 
14155 C CD2 . PHE C 243  ? 3.6237 1.6895 2.5523 0.4768  0.0326  0.4987  243  PHE B CD2 
14156 C CE1 . PHE C 243  ? 3.7149 1.7912 2.4958 0.5197  0.0500  0.3906  243  PHE B CE1 
14157 C CE2 . PHE C 243  ? 3.6848 1.7375 2.5769 0.5204  0.0740  0.5187  243  PHE B CE2 
14158 C CZ  . PHE C 243  ? 3.7325 1.7892 2.5485 0.5416  0.0825  0.4640  243  PHE B CZ  
14159 N N   . LYS C 244  ? 4.4454 2.5757 3.4988 0.4062  -0.1250 0.4572  244  LYS B N   
14160 C CA  . LYS C 244  ? 4.5304 2.6687 3.6412 0.4219  -0.1459 0.5061  244  LYS B CA  
14161 C C   . LYS C 244  ? 4.5366 2.6942 3.6435 0.4067  -0.1882 0.4540  244  LYS B C   
14162 O O   . LYS C 244  ? 4.5977 2.7627 3.7504 0.4136  -0.2135 0.4823  244  LYS B O   
14163 C CB  . LYS C 244  ? 4.5485 2.6733 3.7334 0.4006  -0.1539 0.5740  244  LYS B CB  
14164 C CG  . LYS C 244  ? 4.6023 2.7096 3.8023 0.4200  -0.1116 0.6356  244  LYS B CG  
14165 C CD  . LYS C 244  ? 4.6093 2.7101 3.8937 0.4149  -0.1213 0.7179  244  LYS B CD  
14166 C CE  . LYS C 244  ? 4.6295 2.7208 3.9346 0.4294  -0.0775 0.7756  244  LYS B CE  
14167 N NZ  . LYS C 244  ? 4.6037 2.6736 3.8781 0.4018  -0.0624 0.7506  244  LYS B NZ  
14168 N N   . ASN C 245  ? 3.3024 1.4678 2.3560 0.3862  -0.1954 0.3783  245  ASN B N   
14169 C CA  . ASN C 245  ? 3.2773 1.4632 2.3210 0.3778  -0.2309 0.3243  245  ASN B CA  
14170 C C   . ASN C 245  ? 3.2250 1.4247 2.2021 0.3676  -0.2323 0.2400  245  ASN B C   
14171 O O   . ASN C 245  ? 3.2301 1.4218 2.1739 0.3458  -0.2176 0.2105  245  ASN B O   
14172 C CB  . ASN C 245  ? 3.2562 1.4386 2.3515 0.3390  -0.2683 0.3316  245  ASN B CB  
14173 C CG  . ASN C 245  ? 3.2697 1.4440 2.3485 0.2942  -0.2724 0.2953  245  ASN B CG  
14174 O OD1 . ASN C 245  ? 3.2886 1.4536 2.3358 0.2912  -0.2430 0.2895  245  ASN B OD1 
14175 N ND2 . ASN C 245  ? 3.2887 1.4651 2.3858 0.2587  -0.3082 0.2688  245  ASN B ND2 
14176 N N   . PHE C 246  ? 2.5158 0.7373 1.4782 0.3830  -0.2519 0.2033  246  PHE B N   
14177 C CA  . PHE C 246  ? 2.4143 0.6542 1.3219 0.3741  -0.2598 0.1238  246  PHE B CA  
14178 C C   . PHE C 246  ? 2.5261 0.7864 1.4561 0.3727  -0.2975 0.0984  246  PHE B C   
14179 O O   . PHE C 246  ? 2.5100 0.7742 1.4744 0.3989  -0.3067 0.1374  246  PHE B O   
14180 C CB  . PHE C 246  ? 2.5278 0.7735 1.3794 0.4117  -0.2315 0.1104  246  PHE B CB  
14181 C CG  . PHE C 246  ? 2.5395 0.7965 1.3283 0.3987  -0.2283 0.0362  246  PHE B CG  
14182 C CD1 . PHE C 246  ? 2.4562 0.6979 1.2126 0.3783  -0.2060 0.0195  246  PHE B CD1 
14183 C CD2 . PHE C 246  ? 2.5355 0.8190 1.2992 0.4080  -0.2472 -0.0148 246  PHE B CD2 
14184 C CE1 . PHE C 246  ? 2.5092 0.7612 1.2096 0.3659  -0.2038 -0.0472 246  PHE B CE1 
14185 C CE2 . PHE C 246  ? 2.5206 0.8158 1.2296 0.3957  -0.2449 -0.0804 246  PHE B CE2 
14186 C CZ  . PHE C 246  ? 2.5483 0.8275 1.2256 0.3743  -0.2236 -0.0966 246  PHE B CZ  
14187 N N   . GLU C 247  ? 3.6793 1.9521 2.5917 0.3431  -0.3186 0.0350  247  GLU B N   
14188 C CA  . GLU C 247  ? 3.6838 1.9735 2.6196 0.3414  -0.3530 0.0115  247  GLU B CA  
14189 C C   . GLU C 247  ? 3.7831 2.1009 2.6756 0.3546  -0.3589 -0.0524 247  GLU B C   
14190 O O   . GLU C 247  ? 3.8053 2.1332 2.6636 0.3304  -0.3620 -0.1123 247  GLU B O   
14191 C CB  . GLU C 247  ? 4.2163 2.4971 3.1829 0.2972  -0.3799 -0.0015 247  GLU B CB  
14192 C CG  . GLU C 247  ? 3.9713 2.2623 2.9725 0.2987  -0.4147 -0.0107 247  GLU B CG  
14193 C CD  . GLU C 247  ? 3.2942 1.5738 2.3175 0.2532  -0.4413 -0.0306 247  GLU B CD  
14194 O OE1 . GLU C 247  ? 3.2214 1.4862 2.2366 0.2221  -0.4328 -0.0305 247  GLU B OE1 
14195 O OE2 . GLU C 247  ? 3.2164 1.5008 2.2632 0.2497  -0.4693 -0.0454 247  GLU B OE2 
14196 N N   . ILE C 248  ? 2.8924 1.2237 1.7914 0.3927  -0.3626 -0.0364 248  ILE B N   
14197 C CA  . ILE C 248  ? 2.8681 1.2275 1.7316 0.4112  -0.3687 -0.0866 248  ILE B CA  
14198 C C   . ILE C 248  ? 2.8347 1.2095 1.7348 0.4110  -0.4026 -0.1011 248  ILE B C   
14199 O O   . ILE C 248  ? 2.8357 1.2044 1.7818 0.4268  -0.4140 -0.0541 248  ILE B O   
14200 C CB  . ILE C 248  ? 2.8898 1.2540 1.7319 0.4571  -0.3486 -0.0572 248  ILE B CB  
14201 C CG1 . ILE C 248  ? 2.8744 1.2140 1.6968 0.4636  -0.3126 -0.0180 248  ILE B CG1 
14202 C CG2 . ILE C 248  ? 2.9477 1.3396 1.7397 0.4715  -0.3508 -0.1150 248  ILE B CG2 
14203 C CD1 . ILE C 248  ? 2.9075 1.2456 1.7148 0.5112  -0.2898 0.0251  248  ILE B CD1 
14204 N N   . THR C 249  ? 2.9720 1.3673 1.8513 0.3946  -0.4176 -0.1664 249  THR B N   
14205 C CA  . THR C 249  ? 2.9896 1.4016 1.8980 0.3956  -0.4479 -0.1891 249  THR B CA  
14206 C C   . THR C 249  ? 3.0787 1.5212 1.9602 0.4290  -0.4487 -0.2164 249  THR B C   
14207 O O   . THR C 249  ? 3.1065 1.5606 1.9377 0.4332  -0.4320 -0.2472 249  THR B O   
14208 C CB  . THR C 249  ? 3.0644 1.4803 1.9670 0.3544  -0.4625 -0.2460 249  THR B CB  
14209 O OG1 . THR C 249  ? 3.0357 1.4357 1.9117 0.3263  -0.4434 -0.2517 249  THR B OG1 
14210 C CG2 . THR C 249  ? 3.0349 1.4375 1.9888 0.3361  -0.4895 -0.2333 249  THR B CG2 
14211 N N   . ILE C 250  ? 2.5878 1.0429 1.5024 0.4523  -0.4684 -0.2045 250  ILE B N   
14212 C CA  . ILE C 250  ? 2.6684 1.1547 1.5624 0.4835  -0.4729 -0.2294 250  ILE B CA  
14213 C C   . ILE C 250  ? 2.7251 1.2297 1.6514 0.4798  -0.5030 -0.2612 250  ILE B C   
14214 O O   . ILE C 250  ? 2.6930 1.1860 1.6687 0.4823  -0.5199 -0.2300 250  ILE B O   
14215 C CB  . ILE C 250  ? 2.6750 1.1599 1.5770 0.5264  -0.4636 -0.1729 250  ILE B CB  
14216 C CG1 . ILE C 250  ? 2.6682 1.1325 1.6330 0.5291  -0.4760 -0.1149 250  ILE B CG1 
14217 C CG2 . ILE C 250  ? 2.6531 1.1260 1.5086 0.5380  -0.4301 -0.1525 250  ILE B CG2 
14218 C CD1 . ILE C 250  ? 2.7033 1.1678 1.6855 0.5718  -0.4697 -0.0556 250  ILE B CD1 
14219 N N   . LYS C 251  ? 3.5436 2.0765 2.4430 0.4746  -0.5094 -0.3222 251  LYS B N   
14220 C CA  . LYS C 251  ? 3.6451 2.1935 2.5719 0.4626  -0.5349 -0.3622 251  LYS B CA  
14221 C C   . LYS C 251  ? 3.7989 2.3841 2.7225 0.4916  -0.5467 -0.3886 251  LYS B C   
14222 O O   . LYS C 251  ? 3.8476 2.4582 2.7325 0.4904  -0.5418 -0.4339 251  LYS B O   
14223 C CB  . LYS C 251  ? 3.6525 2.2016 2.5589 0.4210  -0.5343 -0.4166 251  LYS B CB  
14224 C CG  . LYS C 251  ? 3.6145 2.1313 2.5124 0.3911  -0.5193 -0.3962 251  LYS B CG  
14225 C CD  . LYS C 251  ? 3.6181 2.1313 2.5110 0.3475  -0.5255 -0.4434 251  LYS B CD  
14226 C CE  . LYS C 251  ? 3.6617 2.2054 2.5133 0.3391  -0.5205 -0.5072 251  LYS B CE  
14227 N NZ  . LYS C 251  ? 3.6354 2.1690 2.4699 0.2953  -0.5153 -0.5405 251  LYS B NZ  
14228 N N   . ALA C 252  ? 3.4345 2.0225 2.4007 0.5160  -0.5634 -0.3603 252  ALA B N   
14229 C CA  . ALA C 252  ? 3.5276 2.1501 2.4970 0.5469  -0.5757 -0.3767 252  ALA B CA  
14230 C C   . ALA C 252  ? 3.5530 2.1936 2.5502 0.5352  -0.5983 -0.4238 252  ALA B C   
14231 O O   . ALA C 252  ? 3.5284 2.1490 2.5557 0.5112  -0.6087 -0.4280 252  ALA B O   
14232 C CB  . ALA C 252  ? 3.5412 2.1588 2.5399 0.5842  -0.5795 -0.3170 252  ALA B CB  
14233 N N   . ARG C 253  ? 4.0964 2.7744 3.0838 0.5532  -0.6059 -0.4575 253  ARG B N   
14234 C CA  . ARG C 253  ? 4.1436 2.8421 3.1570 0.5445  -0.6248 -0.5039 253  ARG B CA  
14235 C C   . ARG C 253  ? 4.1507 2.8932 3.1559 0.5714  -0.6327 -0.5293 253  ARG B C   
14236 O O   . ARG C 253  ? 4.1954 2.9568 3.1556 0.5781  -0.6214 -0.5425 253  ARG B O   
14237 C CB  . ARG C 253  ? 4.2081 2.9034 3.2017 0.5030  -0.6197 -0.5540 253  ARG B CB  
14238 C CG  . ARG C 253  ? 4.3317 3.0450 3.2693 0.4938  -0.6027 -0.5852 253  ARG B CG  
14239 C CD  . ARG C 253  ? 4.4455 3.1710 3.3726 0.4590  -0.6038 -0.6460 253  ARG B CD  
14240 N NE  . ARG C 253  ? 4.5670 3.3130 3.5322 0.4621  -0.6230 -0.6766 253  ARG B NE  
14241 C CZ  . ARG C 253  ? 4.5948 3.3193 3.5985 0.4490  -0.6343 -0.6748 253  ARG B CZ  
14242 N NH1 . ARG C 253  ? 4.5470 3.2304 3.5574 0.4305  -0.6305 -0.6430 253  ARG B NH1 
14243 N NH2 . ARG C 253  ? 4.6517 3.3949 3.6875 0.4541  -0.6496 -0.7042 253  ARG B NH2 
14244 N N   . TYR C 254  ? 3.4438 2.2015 2.4928 0.5866  -0.6526 -0.5357 254  TYR B N   
14245 C CA  . TYR C 254  ? 3.4302 2.2315 2.4791 0.6121  -0.6627 -0.5585 254  TYR B CA  
14246 C C   . TYR C 254  ? 3.4024 2.2324 2.4296 0.5890  -0.6621 -0.6243 254  TYR B C   
14247 O O   . TYR C 254  ? 3.3402 2.1551 2.3602 0.5545  -0.6560 -0.6521 254  TYR B O   
14248 C CB  . TYR C 254  ? 3.4475 2.2554 2.5538 0.6360  -0.6837 -0.5432 254  TYR B CB  
14249 C CG  . TYR C 254  ? 3.4126 2.1899 2.5478 0.6552  -0.6861 -0.4780 254  TYR B CG  
14250 C CD1 . TYR C 254  ? 3.4002 2.1552 2.5885 0.6534  -0.7010 -0.4625 254  TYR B CD1 
14251 C CD2 . TYR C 254  ? 3.4136 2.1834 2.5227 0.6748  -0.6729 -0.4318 254  TYR B CD2 
14252 C CE1 . TYR C 254  ? 3.3705 2.0982 2.5877 0.6699  -0.7043 -0.4017 254  TYR B CE1 
14253 C CE2 . TYR C 254  ? 3.3852 2.1288 2.5232 0.6924  -0.6742 -0.3705 254  TYR B CE2 
14254 C CZ  . TYR C 254  ? 3.3600 2.0836 2.5534 0.6894  -0.6906 -0.3551 254  TYR B CZ  
14255 O OH  . TYR C 254  ? 3.3383 2.0366 2.5626 0.7059  -0.6928 -0.2928 254  TYR B OH  
14256 N N   . PHE C 255  ? 3.7047 2.5766 2.7217 0.6075  -0.6687 -0.6477 255  PHE B N   
14257 C CA  . PHE C 255  ? 3.7736 2.6770 2.7718 0.5877  -0.6686 -0.7076 255  PHE B CA  
14258 C C   . PHE C 255  ? 3.8688 2.7798 2.9097 0.5720  -0.6800 -0.7451 255  PHE B C   
14259 O O   . PHE C 255  ? 3.8656 2.7888 2.8931 0.5445  -0.6754 -0.7924 255  PHE B O   
14260 C CB  . PHE C 255  ? 3.8432 2.7896 2.8193 0.6116  -0.6742 -0.7193 255  PHE B CB  
14261 C CG  . PHE C 255  ? 3.8256 2.7653 2.7421 0.6152  -0.6587 -0.7032 255  PHE B CG  
14262 C CD1 . PHE C 255  ? 3.8142 2.7790 2.6859 0.6032  -0.6539 -0.7420 255  PHE B CD1 
14263 C CD2 . PHE C 255  ? 3.7765 2.6826 2.6816 0.6294  -0.6480 -0.6491 255  PHE B CD2 
14264 C CE1 . PHE C 255  ? 3.7948 2.7488 2.6083 0.6062  -0.6389 -0.7284 255  PHE B CE1 
14265 C CE2 . PHE C 255  ? 3.7766 2.6734 2.6252 0.6334  -0.6313 -0.6346 255  PHE B CE2 
14266 C CZ  . PHE C 255  ? 3.7947 2.7141 2.5957 0.6219  -0.6267 -0.6752 255  PHE B CZ  
14267 N N   . TYR C 256  ? 4.2864 3.1885 3.3780 0.5892  -0.6939 -0.7235 256  TYR B N   
14268 C CA  . TYR C 256  ? 4.4206 3.3248 3.5536 0.5770  -0.7040 -0.7568 256  TYR B CA  
14269 C C   . TYR C 256  ? 4.5371 3.3973 3.6745 0.5431  -0.6982 -0.7599 256  TYR B C   
14270 O O   . TYR C 256  ? 4.5940 3.4337 3.7715 0.5421  -0.7083 -0.7560 256  TYR B O   
14271 C CB  . TYR C 256  ? 4.4102 3.3253 3.5961 0.6098  -0.7222 -0.7386 256  TYR B CB  
14272 C CG  . TYR C 256  ? 4.3174 3.2066 3.5193 0.6349  -0.7266 -0.6758 256  TYR B CG  
14273 C CD1 . TYR C 256  ? 4.2547 3.1006 3.4874 0.6277  -0.7308 -0.6481 256  TYR B CD1 
14274 C CD2 . TYR C 256  ? 4.3186 3.2266 3.5047 0.6656  -0.7270 -0.6436 256  TYR B CD2 
14275 C CE1 . TYR C 256  ? 4.2016 3.0252 3.4522 0.6503  -0.7351 -0.5890 256  TYR B CE1 
14276 C CE2 . TYR C 256  ? 4.2672 3.1530 3.4689 0.6892  -0.7297 -0.5850 256  TYR B CE2 
14277 C CZ  . TYR C 256  ? 4.2022 3.0468 3.4381 0.6815  -0.7336 -0.5573 256  TYR B CZ  
14278 O OH  . TYR C 256  ? 4.1560 2.9797 3.4103 0.7046  -0.7365 -0.4972 256  TYR B OH  
14279 N N   . ASN C 257  ? 5.5769 4.4224 4.6714 0.5151  -0.6823 -0.7676 257  ASN B N   
14280 C CA  . ASN C 257  ? 5.5977 4.4040 4.6878 0.4788  -0.6757 -0.7727 257  ASN B CA  
14281 C C   . ASN C 257  ? 5.5036 4.2668 4.6295 0.4803  -0.6847 -0.7321 257  ASN B C   
14282 O O   . ASN C 257  ? 5.4715 4.2123 4.6158 0.4582  -0.6898 -0.7497 257  ASN B O   
14283 C CB  . ASN C 257  ? 5.7675 4.5881 4.8564 0.4503  -0.6742 -0.8331 257  ASN B CB  
14284 C CG  . ASN C 257  ? 5.9648 4.8072 5.0973 0.4661  -0.6885 -0.8574 257  ASN B CG  
14285 O OD1 . ASN C 257  ? 6.0663 4.9457 5.2118 0.4954  -0.6959 -0.8595 257  ASN B OD1 
14286 N ND2 . ASN C 257  ? 5.9936 4.8122 5.1485 0.4468  -0.6924 -0.8757 257  ASN B ND2 
14287 N N   . LYS C 258  ? 3.8393 2.5902 2.9733 0.5060  -0.6866 -0.6772 258  LYS B N   
14288 C CA  . LYS C 258  ? 3.7962 2.5047 2.9615 0.5069  -0.6942 -0.6305 258  LYS B CA  
14289 C C   . LYS C 258  ? 3.6610 2.3528 2.8089 0.5187  -0.6836 -0.5744 258  LYS B C   
14290 O O   . LYS C 258  ? 3.6956 2.4082 2.8368 0.5504  -0.6816 -0.5512 258  LYS B O   
14291 C CB  . LYS C 258  ? 3.8878 2.6007 3.1047 0.5346  -0.7136 -0.6188 258  LYS B CB  
14292 C CG  . LYS C 258  ? 3.9530 2.6468 3.2006 0.5153  -0.7253 -0.6488 258  LYS B CG  
14293 C CD  . LYS C 258  ? 3.9284 2.5683 3.1919 0.4955  -0.7306 -0.6143 258  LYS B CD  
14294 C CE  . LYS C 258  ? 3.9796 2.5975 3.2708 0.4787  -0.7433 -0.6440 258  LYS B CE  
14295 N NZ  . LYS C 258  ? 3.9435 2.5075 3.2462 0.4557  -0.7505 -0.6126 258  LYS B NZ  
14296 N N   . VAL C 259  ? 3.7810 2.4350 2.9208 0.4929  -0.6763 -0.5525 259  VAL B N   
14297 C CA  . VAL C 259  ? 3.6607 2.2950 2.7880 0.5016  -0.6643 -0.4972 259  VAL B CA  
14298 C C   . VAL C 259  ? 3.6188 2.2453 2.7853 0.5354  -0.6752 -0.4426 259  VAL B C   
14299 O O   . VAL C 259  ? 3.6239 2.2466 2.8322 0.5433  -0.6937 -0.4426 259  VAL B O   
14300 C CB  . VAL C 259  ? 3.5261 2.1186 2.6509 0.4666  -0.6588 -0.4797 259  VAL B CB  
14301 C CG1 . VAL C 259  ? 3.5248 2.1195 2.6212 0.4279  -0.6528 -0.5358 259  VAL B CG1 
14302 C CG2 . VAL C 259  ? 3.5117 2.0713 2.6858 0.4636  -0.6774 -0.4488 259  VAL B CG2 
14303 N N   . VAL C 260  ? 3.6042 2.2267 2.7571 0.5552  -0.6628 -0.3950 260  VAL B N   
14304 C CA  . VAL C 260  ? 3.6080 2.2189 2.7979 0.5849  -0.6706 -0.3354 260  VAL B CA  
14305 C C   . VAL C 260  ? 3.6032 2.1712 2.8294 0.5643  -0.6793 -0.3017 260  VAL B C   
14306 O O   . VAL C 260  ? 3.5592 2.1046 2.7719 0.5292  -0.6736 -0.3134 260  VAL B O   
14307 C CB  . VAL C 260  ? 3.5729 2.1872 2.7357 0.6095  -0.6515 -0.2908 260  VAL B CB  
14308 C CG1 . VAL C 260  ? 3.5674 2.1708 2.7710 0.6405  -0.6590 -0.2268 260  VAL B CG1 
14309 C CG2 . VAL C 260  ? 3.6147 2.2686 2.7350 0.6279  -0.6434 -0.3235 260  VAL B CG2 
14310 N N   . THR C 261  ? 2.7533 1.3099 2.0260 0.5854  -0.6942 -0.2596 261  THR B N   
14311 C CA  . THR C 261  ? 2.7643 1.2796 2.0710 0.5715  -0.7011 -0.2116 261  THR B CA  
14312 C C   . THR C 261  ? 2.7663 1.2782 2.0790 0.5997  -0.6895 -0.1438 261  THR B C   
14313 O O   . THR C 261  ? 2.7581 1.2736 2.0330 0.5998  -0.6670 -0.1334 261  THR B O   
14314 C CB  . THR C 261  ? 2.8139 1.3123 2.1710 0.5690  -0.7277 -0.2136 261  THR B CB  
14315 O OG1 . THR C 261  ? 2.8585 1.3699 2.2053 0.5525  -0.7348 -0.2813 261  THR B OG1 
14316 C CG2 . THR C 261  ? 2.7955 1.2470 2.1798 0.5415  -0.7367 -0.1773 261  THR B CG2 
14317 N N   . GLU C 262  ? 4.5851 3.0901 3.9434 0.6245  -0.7030 -0.0977 262  GLU B N   
14318 C CA  . GLU C 262  ? 4.6274 3.1284 3.9918 0.6505  -0.6899 -0.0308 262  GLU B CA  
14319 C C   . GLU C 262  ? 4.6380 3.1722 3.9566 0.6789  -0.6693 -0.0363 262  GLU B C   
14320 O O   . GLU C 262  ? 4.6602 3.2262 3.9657 0.6963  -0.6748 -0.0727 262  GLU B O   
14321 C CB  . GLU C 262  ? 4.7419 3.2328 4.1641 0.6746  -0.7079 0.0212  262  GLU B CB  
14322 C CG  . GLU C 262  ? 4.8293 3.3160 4.2581 0.7007  -0.6919 0.0931  262  GLU B CG  
14323 C CD  . GLU C 262  ? 4.9484 3.4308 4.4328 0.7288  -0.7083 0.1456  262  GLU B CD  
14324 O OE1 . GLU C 262  ? 5.0046 3.5019 4.4872 0.7638  -0.6965 0.1879  262  GLU B OE1 
14325 O OE2 . GLU C 262  ? 4.9827 3.4452 4.5114 0.7156  -0.7328 0.1450  262  GLU B OE2 
14326 N N   . ALA C 263  ? 3.8325 2.3574 3.1269 0.6828  -0.6457 0.0010  263  ALA B N   
14327 C CA  . ALA C 263  ? 3.8677 2.4159 3.1156 0.7099  -0.6238 0.0049  263  ALA B CA  
14328 C C   . ALA C 263  ? 3.8120 2.3389 3.0539 0.7165  -0.6004 0.0649  263  ALA B C   
14329 O O   . ALA C 263  ? 3.7841 2.2840 3.0328 0.6888  -0.5940 0.0789  263  ALA B O   
14330 C CB  . ALA C 263  ? 3.8953 2.4619 3.0866 0.6925  -0.6135 -0.0606 263  ALA B CB  
14331 N N   . ASP C 264  ? 4.7930 3.3320 4.0223 0.7538  -0.5868 0.1024  264  ASP B N   
14332 C CA  . ASP C 264  ? 4.7740 3.2949 3.9921 0.7635  -0.5598 0.1580  264  ASP B CA  
14333 C C   . ASP C 264  ? 4.7576 3.2796 3.9099 0.7497  -0.5343 0.1230  264  ASP B C   
14334 O O   . ASP C 264  ? 4.7629 3.3092 3.8699 0.7534  -0.5331 0.0715  264  ASP B O   
14335 C CB  . ASP C 264  ? 4.8922 3.4242 4.1171 0.8092  -0.5520 0.2117  264  ASP B CB  
14336 C CG  . ASP C 264  ? 4.9637 3.4705 4.2346 0.8162  -0.5455 0.2875  264  ASP B CG  
14337 O OD1 . ASP C 264  ? 4.9341 3.4160 4.2104 0.7912  -0.5342 0.3036  264  ASP B OD1 
14338 O OD2 . ASP C 264  ? 5.0503 3.5631 4.3536 0.8474  -0.5511 0.3341  264  ASP B OD2 
14339 N N   . VAL C 265  ? 3.2480 1.7440 2.3966 0.7354  -0.5137 0.1545  265  VAL B N   
14340 C CA  . VAL C 265  ? 3.2009 1.6923 2.2917 0.7198  -0.4884 0.1262  265  VAL B CA  
14341 C C   . VAL C 265  ? 3.2390 1.7204 2.3027 0.7471  -0.4548 0.1770  265  VAL B C   
14342 O O   . VAL C 265  ? 3.2450 1.7072 2.3461 0.7548  -0.4465 0.2400  265  VAL B O   
14343 C CB  . VAL C 265  ? 3.0282 1.4964 2.1339 0.6744  -0.4922 0.1112  265  VAL B CB  
14344 C CG1 . VAL C 265  ? 2.9845 1.4441 2.0365 0.6583  -0.4646 0.0910  265  VAL B CG1 
14345 C CG2 . VAL C 265  ? 2.9977 1.4769 2.1164 0.6496  -0.5210 0.0532  265  VAL B CG2 
14346 N N   . TYR C 266  ? 4.3767 2.8707 3.3758 0.7625  -0.4352 0.1510  266  TYR B N   
14347 C CA  . TYR C 266  ? 4.4297 2.9101 3.3969 0.7866  -0.4005 0.1950  266  TYR B CA  
14348 C C   . TYR C 266  ? 4.3735 2.8445 3.2779 0.7688  -0.3758 0.1581  266  TYR B C   
14349 O O   . TYR C 266  ? 4.4082 2.8969 3.2629 0.7652  -0.3786 0.1007  266  TYR B O   
14350 C CB  . TYR C 266  ? 4.6068 3.1058 3.5521 0.8313  -0.3956 0.2145  266  TYR B CB  
14351 C CG  . TYR C 266  ? 4.7331 3.2341 3.7404 0.8557  -0.4091 0.2736  266  TYR B CG  
14352 C CD1 . TYR C 266  ? 4.7830 3.2954 3.8445 0.8468  -0.4443 0.2627  266  TYR B CD1 
14353 C CD2 . TYR C 266  ? 4.8355 3.3262 3.8471 0.8882  -0.3858 0.3405  266  TYR B CD2 
14354 C CE1 . TYR C 266  ? 4.8386 3.3516 3.9580 0.8685  -0.4577 0.3165  266  TYR B CE1 
14355 C CE2 . TYR C 266  ? 4.8933 3.3867 3.9641 0.9102  -0.3986 0.3960  266  TYR B CE2 
14356 C CZ  . TYR C 266  ? 4.8956 3.3999 4.0204 0.8997  -0.4353 0.3836  266  TYR B CZ  
14357 O OH  . TYR C 266  ? 4.9238 3.4294 4.1080 0.9207  -0.4488 0.4384  266  TYR B OH  
14358 N N   . ILE C 267  ? 2.9250 1.3681 1.8333 0.7574  -0.3520 0.1921  267  ILE B N   
14359 C CA  . ILE C 267  ? 2.8492 1.2802 1.7025 0.7378  -0.3287 0.1583  267  ILE B CA  
14360 C C   . ILE C 267  ? 2.8655 1.2743 1.6860 0.7589  -0.2881 0.2012  267  ILE B C   
14361 O O   . ILE C 267  ? 2.8672 1.2541 1.7249 0.7583  -0.2735 0.2573  267  ILE B O   
14362 C CB  . ILE C 267  ? 2.8019 1.2182 1.6827 0.6928  -0.3376 0.1415  267  ILE B CB  
14363 C CG1 . ILE C 267  ? 2.7455 1.1803 1.6572 0.6706  -0.3757 0.0979  267  ILE B CG1 
14364 C CG2 . ILE C 267  ? 2.8116 1.2190 1.6341 0.6727  -0.3163 0.1003  267  ILE B CG2 
14365 C CD1 . ILE C 267  ? 2.7066 1.1261 1.6436 0.6263  -0.3857 0.0819  267  ILE B CD1 
14366 N N   . THR C 268  ? 3.6599 2.0733 2.4100 0.7770  -0.2694 0.1748  268  THR B N   
14367 C CA  . THR C 268  ? 3.6786 2.0671 2.3903 0.7948  -0.2283 0.2087  268  THR B CA  
14368 C C   . THR C 268  ? 3.6685 2.0381 2.3459 0.7625  -0.2112 0.1744  268  THR B C   
14369 O O   . THR C 268  ? 3.6579 2.0376 2.3316 0.7294  -0.2313 0.1190  268  THR B O   
14370 C CB  . THR C 268  ? 3.8094 2.2056 2.4598 0.8357  -0.2122 0.2095  268  THR B CB  
14371 O OG1 . THR C 268  ? 3.8637 2.2797 2.4593 0.8273  -0.2265 0.1388  268  THR B OG1 
14372 C CG2 . THR C 268  ? 3.8361 2.2479 2.5271 0.8688  -0.2256 0.2556  268  THR B CG2 
14373 N N   . PHE C 269  ? 4.0609 2.4027 2.7159 0.7724  -0.1733 0.2089  269  PHE B N   
14374 C CA  . PHE C 269  ? 3.9985 2.3206 2.6129 0.7466  -0.1530 0.1773  269  PHE B CA  
14375 C C   . PHE C 269  ? 3.9812 2.2838 2.5282 0.7748  -0.1135 0.1872  269  PHE B C   
14376 O O   . PHE C 269  ? 4.0513 2.3537 2.5885 0.8134  -0.1004 0.2254  269  PHE B O   
14377 C CB  . PHE C 269  ? 3.9379 2.2386 2.6055 0.7225  -0.1450 0.2155  269  PHE B CB  
14378 C CG  . PHE C 269  ? 3.8710 2.1843 2.6084 0.6973  -0.1811 0.2188  269  PHE B CG  
14379 C CD1 . PHE C 269  ? 3.8456 2.1604 2.6470 0.7131  -0.1908 0.2788  269  PHE B CD1 
14380 C CD2 . PHE C 269  ? 3.8285 2.1511 2.5669 0.6573  -0.2055 0.1614  269  PHE B CD2 
14381 C CE1 . PHE C 269  ? 3.7930 2.1158 2.6565 0.6889  -0.2250 0.2809  269  PHE B CE1 
14382 C CE2 . PHE C 269  ? 3.7733 2.1042 2.5724 0.6336  -0.2382 0.1630  269  PHE B CE2 
14383 C CZ  . PHE C 269  ? 3.7590 2.0888 2.6200 0.6490  -0.2486 0.2222  269  PHE B CZ  
14384 N N   . GLY C 270  ? 3.9467 2.2305 2.4462 0.7558  -0.0933 0.1546  270  GLY B N   
14385 C CA  . GLY C 270  ? 3.9954 2.2567 2.4237 0.7818  -0.0552 0.1587  270  GLY B CA  
14386 C C   . GLY C 270  ? 3.9322 2.1627 2.3288 0.7618  -0.0255 0.1468  270  GLY B C   
14387 O O   . GLY C 270  ? 3.9089 2.1394 2.3275 0.7230  -0.0378 0.1199  270  GLY B O   
14388 N N   . ILE C 271  ? 3.4063 1.6091 1.7519 0.7897  0.0150  0.1695  271  ILE B N   
14389 C CA  . ILE C 271  ? 3.3265 1.4989 1.6191 0.7765  0.0451  0.1457  271  ILE B CA  
14390 C C   . ILE C 271  ? 3.4422 1.6163 1.6432 0.7863  0.0458  0.0874  271  ILE B C   
14391 O O   . ILE C 271  ? 3.4922 1.6948 1.6822 0.7972  0.0190  0.0652  271  ILE B O   
14392 C CB  . ILE C 271  ? 3.2586 1.3950 1.5588 0.7980  0.0912  0.2100  271  ILE B CB  
14393 C CG1 . ILE C 271  ? 3.1564 1.3000 1.5500 0.8021  0.0848  0.2795  271  ILE B CG1 
14394 C CG2 . ILE C 271  ? 3.2375 1.3464 1.5214 0.7697  0.1124  0.1917  271  ILE B CG2 
14395 C CD1 . ILE C 271  ? 3.0195 1.1684 1.4778 0.7586  0.0630  0.2765  271  ILE B CD1 
14396 N N   . ARG C 272  ? 3.7421 1.8863 1.8788 0.7810  0.0744  0.0617  272  ARG B N   
14397 C CA  . ARG C 272  ? 3.9223 2.0686 1.9751 0.7798  0.0688  -0.0020 272  ARG B CA  
14398 C C   . ARG C 272  ? 4.0578 2.1629 2.0528 0.7725  0.1054  -0.0172 272  ARG B C   
14399 O O   . ARG C 272  ? 4.0153 2.0916 2.0330 0.7769  0.1376  0.0277  272  ARG B O   
14400 C CB  . ARG C 272  ? 3.8574 2.0384 1.9257 0.7427  0.0253  -0.0633 272  ARG B CB  
14401 C CG  . ARG C 272  ? 3.9135 2.1067 1.9074 0.7414  0.0108  -0.1271 272  ARG B CG  
14402 C CD  . ARG C 272  ? 3.8535 2.0934 1.8873 0.7230  -0.0366 -0.1617 272  ARG B CD  
14403 N NE  . ARG C 272  ? 3.8724 2.1317 1.8466 0.7198  -0.0567 -0.2221 272  ARG B NE  
14404 C CZ  . ARG C 272  ? 3.8743 2.1760 1.8735 0.7096  -0.0966 -0.2550 272  ARG B CZ  
14405 N NH1 . ARG C 272  ? 3.8542 2.1798 1.9334 0.7022  -0.1196 -0.2343 272  ARG B NH1 
14406 N NH2 . ARG C 272  ? 3.8929 2.2121 1.8376 0.7068  -0.1136 -0.3078 272  ARG B NH2 
14407 N N   . GLU C 273  ? 3.9591 2.0612 1.8812 0.7610  0.1004  -0.0796 273  GLU B N   
14408 C CA  . GLU C 273  ? 4.0447 2.1075 1.9146 0.7483  0.1316  -0.1003 273  GLU B CA  
14409 C C   . GLU C 273  ? 3.9857 2.0640 1.8402 0.7059  0.1048  -0.1703 273  GLU B C   
14410 O O   . GLU C 273  ? 3.9315 1.9968 1.8054 0.6751  0.1117  -0.1802 273  GLU B O   
14411 C CB  . GLU C 273  ? 4.2447 2.2730 2.0234 0.7826  0.1652  -0.0998 273  GLU B CB  
14412 C CG  . GLU C 273  ? 4.3703 2.3615 2.1561 0.8155  0.2125  -0.0309 273  GLU B CG  
14413 C CD  . GLU C 273  ? 4.3267 2.3140 2.1989 0.7977  0.2213  0.0130  273  GLU B CD  
14414 O OE1 . GLU C 273  ? 4.2887 2.2592 2.1614 0.7666  0.2291  -0.0097 273  GLU B OE1 
14415 O OE2 . GLU C 273  ? 4.2876 2.2891 2.2278 0.8141  0.2193  0.0709  273  GLU B OE2 
14416 N N   . ASP C 274  ? 4.9240 3.0320 2.7467 0.7040  0.0734  -0.2173 274  ASP B N   
14417 C CA  . ASP C 274  ? 4.8661 2.9928 2.6732 0.6651  0.0464  -0.2853 274  ASP B CA  
14418 C C   . ASP C 274  ? 4.8750 3.0519 2.7046 0.6623  0.0016  -0.3128 274  ASP B C   
14419 O O   . ASP C 274  ? 4.8724 3.0691 2.7427 0.6859  -0.0096 -0.2756 274  ASP B O   
14420 C CB  . ASP C 274  ? 4.9343 3.0310 2.6464 0.6624  0.0644  -0.3299 274  ASP B CB  
14421 C CG  . ASP C 274  ? 5.4428 3.5291 3.0830 0.7012  0.0737  -0.3268 274  ASP B CG  
14422 O OD1 . ASP C 274  ? 5.4864 3.5694 3.0547 0.6948  0.0660  -0.3780 274  ASP B OD1 
14423 O OD2 . ASP C 274  ? 5.4974 3.5783 3.1516 0.7372  0.0886  -0.2728 274  ASP B OD2 
14424 N N   . LEU C 275  ? 3.7609 1.9586 1.5675 0.6329  -0.0236 -0.3766 275  LEU B N   
14425 C CA  . LEU C 275  ? 3.8008 2.0470 1.6232 0.6298  -0.0656 -0.4087 275  LEU B CA  
14426 C C   . LEU C 275  ? 3.9885 2.2390 1.7332 0.6526  -0.0715 -0.4357 275  LEU B C   
14427 O O   . LEU C 275  ? 4.0015 2.2918 1.7548 0.6562  -0.1047 -0.4573 275  LEU B O   
14428 C CB  . LEU C 275  ? 3.6532 1.9281 1.5114 0.5846  -0.0943 -0.4582 275  LEU B CB  
14429 C CG  . LEU C 275  ? 3.5189 1.8016 1.4594 0.5584  -0.1016 -0.4396 275  LEU B CG  
14430 C CD1 . LEU C 275  ? 3.4343 1.7605 1.4089 0.5273  -0.1403 -0.4883 275  LEU B CD1 
14431 C CD2 . LEU C 275  ? 3.5191 1.8009 1.5205 0.5828  -0.0974 -0.3734 275  LEU B CD2 
14432 N N   . LYS C 276  ? 4.1244 2.3328 1.7938 0.6683  -0.0391 -0.4328 276  LYS B N   
14433 C CA  . LYS C 276  ? 4.2911 2.4957 1.8788 0.6899  -0.0414 -0.4550 276  LYS B CA  
14434 C C   . LYS C 276  ? 4.4916 2.6824 2.0671 0.7370  -0.0222 -0.3984 276  LYS B C   
14435 O O   . LYS C 276  ? 4.6360 2.8157 2.1395 0.7608  -0.0171 -0.4050 276  LYS B O   
14436 C CB  . LYS C 276  ? 4.2578 2.4211 1.7624 0.6770  -0.0183 -0.4911 276  LYS B CB  
14437 C CG  . LYS C 276  ? 4.2749 2.4452 1.6995 0.6770  -0.0367 -0.5420 276  LYS B CG  
14438 C CD  . LYS C 276  ? 4.2363 2.3623 1.5826 0.6599  -0.0143 -0.5787 276  LYS B CD  
14439 C CE  . LYS C 276  ? 4.2360 2.3029 1.5199 0.6919  0.0326  -0.5427 276  LYS B CE  
14440 N NZ  . LYS C 276  ? 4.3264 2.3903 1.5517 0.7303  0.0323  -0.5289 276  LYS B NZ  
14441 N N   . ASP C 277  ? 4.4417 2.6328 2.0879 0.7491  -0.0116 -0.3420 277  ASP B N   
14442 C CA  . ASP C 277  ? 4.6237 2.8037 2.2724 0.7926  0.0078  -0.2812 277  ASP B CA  
14443 C C   . ASP C 277  ? 4.6550 2.8826 2.3627 0.8050  -0.0275 -0.2649 277  ASP B C   
14444 O O   . ASP C 277  ? 4.5923 2.8431 2.3831 0.7903  -0.0448 -0.2494 277  ASP B O   
14445 C CB  . ASP C 277  ? 4.6783 2.8255 2.3690 0.7994  0.0448  -0.2238 277  ASP B CB  
14446 C CG  . ASP C 277  ? 4.8598 2.9886 2.5431 0.8456  0.0729  -0.1600 277  ASP B CG  
14447 O OD1 . ASP C 277  ? 4.9887 3.1237 2.6218 0.8725  0.0677  -0.1630 277  ASP B OD1 
14448 O OD2 . ASP C 277  ? 4.8671 2.9755 2.5951 0.8551  0.1004  -0.1057 277  ASP B OD2 
14449 N N   . ASP C 278  ? 5.8025 4.0430 3.4652 0.8317  -0.0385 -0.2686 278  ASP B N   
14450 C CA  . ASP C 278  ? 5.7972 4.0813 3.5100 0.8474  -0.0708 -0.2518 278  ASP B CA  
14451 C C   . ASP C 278  ? 5.7639 4.0420 3.5331 0.8772  -0.0541 -0.1777 278  ASP B C   
14452 O O   . ASP C 278  ? 5.7606 4.0715 3.5797 0.8914  -0.0783 -0.1557 278  ASP B O   
14453 C CB  . ASP C 278  ? 6.3002 4.6012 3.9470 0.8659  -0.0892 -0.2783 278  ASP B CB  
14454 C CG  . ASP C 278  ? 6.3877 4.6449 3.9373 0.8922  -0.0543 -0.2690 278  ASP B CG  
14455 O OD1 . ASP C 278  ? 6.3780 4.5929 3.9172 0.9033  -0.0133 -0.2331 278  ASP B OD1 
14456 O OD2 . ASP C 278  ? 6.4631 4.7275 3.9458 0.9020  -0.0680 -0.2973 278  ASP B OD2 
14457 N N   . GLN C 279  ? 4.1832 2.4195 1.9469 0.8859  -0.0127 -0.1388 279  GLN B N   
14458 C CA  . GLN C 279  ? 4.1443 2.3713 1.9587 0.9147  0.0079  -0.0648 279  GLN B CA  
14459 C C   . GLN C 279  ? 3.9584 2.1614 1.8270 0.8991  0.0320  -0.0315 279  GLN B C   
14460 O O   . GLN C 279  ? 3.8956 2.0618 1.7264 0.8897  0.0630  -0.0392 279  GLN B O   
14461 C CB  . GLN C 279  ? 4.3327 2.5323 2.0805 0.9580  0.0405  -0.0308 279  GLN B CB  
14462 C CG  . GLN C 279  ? 4.3855 2.5745 2.1856 0.9885  0.0655  0.0485  279  GLN B CG  
14463 C CD  . GLN C 279  ? 4.3642 2.5956 2.2464 0.9949  0.0312  0.0763  279  GLN B CD  
14464 O OE1 . GLN C 279  ? 4.2641 2.4983 2.2267 0.9932  0.0337  0.1227  279  GLN B OE1 
14465 N NE2 . GLN C 279  ? 4.4590 2.7233 2.3224 1.0018  -0.0018 0.0482  279  GLN B NE2 
14466 N N   . LYS C 280  ? 4.3746 2.5983 2.3331 0.8981  0.0170  0.0087  280  LYS B N   
14467 C CA  . LYS C 280  ? 4.1909 2.4017 2.2173 0.8785  0.0282  0.0405  280  LYS B CA  
14468 C C   . LYS C 280  ? 4.1496 2.3612 2.2398 0.9068  0.0381  0.1175  280  LYS B C   
14469 O O   . LYS C 280  ? 4.1734 2.4150 2.3015 0.9205  0.0117  0.1334  280  LYS B O   
14470 C CB  . LYS C 280  ? 4.0296 2.2699 2.1101 0.8361  -0.0109 0.0001  280  LYS B CB  
14471 C CG  . LYS C 280  ? 3.9498 2.2350 2.0716 0.8385  -0.0547 -0.0106 280  LYS B CG  
14472 C CD  . LYS C 280  ? 4.0001 2.3074 2.0587 0.8389  -0.0766 -0.0713 280  LYS B CD  
14473 C CE  . LYS C 280  ? 3.9594 2.3125 2.0639 0.8389  -0.1205 -0.0847 280  LYS B CE  
14474 N NZ  . LYS C 280  ? 4.0186 2.3954 2.0668 0.8359  -0.1430 -0.1444 280  LYS B NZ  
14475 N N   . GLU C 281  ? 3.7822 1.9609 1.8870 0.9150  0.0762  0.1662  281  GLU B N   
14476 C CA  . GLU C 281  ? 3.7776 1.9526 1.9338 0.9460  0.0927  0.2436  281  GLU B CA  
14477 C C   . GLU C 281  ? 3.5753 1.7698 1.8357 0.9264  0.0679  0.2763  281  GLU B C   
14478 O O   . GLU C 281  ? 3.4617 1.6386 1.7663 0.9102  0.0831  0.3054  281  GLU B O   
14479 C CB  . GLU C 281  ? 3.9130 2.0442 2.0396 0.9658  0.1464  0.2843  281  GLU B CB  
14480 C CG  . GLU C 281  ? 4.1652 2.2684 2.1858 0.9706  0.1708  0.2375  281  GLU B CG  
14481 C CD  . GLU C 281  ? 4.4250 2.5422 2.3778 0.9946  0.1578  0.2098  281  GLU B CD  
14482 O OE1 . GLU C 281  ? 4.4835 2.6224 2.4637 1.0213  0.1463  0.2458  281  GLU B OE1 
14483 O OE2 . GLU C 281  ? 4.5597 2.6662 2.4320 0.9861  0.1581  0.1526  281  GLU B OE2 
14484 N N   . MET C 282  ? 3.4135 1.6434 1.7117 0.9286  0.0295  0.2725  282  MET B N   
14485 C CA  . MET C 282  ? 3.3153 1.5638 1.7086 0.9120  0.0019  0.3014  282  MET B CA  
14486 C C   . MET C 282  ? 3.2843 1.5125 1.7385 0.9187  0.0264  0.3749  282  MET B C   
14487 O O   . MET C 282  ? 3.3270 1.5256 1.7559 0.9375  0.0690  0.4095  282  MET B O   
14488 C CB  . MET C 282  ? 3.3381 1.6192 1.7617 0.9322  -0.0293 0.3135  282  MET B CB  
14489 C CG  . MET C 282  ? 3.3756 1.6859 1.7642 0.9229  -0.0637 0.2463  282  MET B CG  
14490 S SD  . MET C 282  ? 3.3549 1.6918 1.7992 0.8754  -0.1106 0.1960  282  MET B SD  
14491 C CE  . MET C 282  ? 3.1231 1.4535 1.4816 0.8505  -0.1047 0.1153  282  MET B CE  
14492 N N   . MET C 283  ? 3.6616 1.9076 2.1992 0.9032  -0.0034 0.3986  283  MET B N   
14493 C CA  . MET C 283  ? 3.6807 1.9144 2.2943 0.8979  0.0059  0.4633  283  MET B CA  
14494 C C   . MET C 283  ? 3.8022 2.0592 2.4781 0.9148  -0.0205 0.5035  283  MET B C   
14495 O O   . MET C 283  ? 3.8055 2.0889 2.4779 0.9139  -0.0542 0.4674  283  MET B O   
14496 C CB  . MET C 283  ? 3.5683 1.7990 2.2198 0.8485  -0.0127 0.4370  283  MET B CB  
14497 C CG  . MET C 283  ? 3.7498 1.9560 2.3434 0.8288  0.0140  0.3983  283  MET B CG  
14498 S SD  . MET C 283  ? 2.8728 1.0758 1.4871 0.7695  -0.0056 0.3513  283  MET B SD  
14499 C CE  . MET C 283  ? 2.8040 1.0444 1.4148 0.7505  -0.0572 0.2825  283  MET B CE  
14500 N N   . GLN C 284  ? 4.5194 2.7666 3.2518 0.9319  -0.0038 0.5795  284  GLN B N   
14501 C CA  . GLN C 284  ? 4.5915 2.8574 3.3976 0.9419  -0.0299 0.6249  284  GLN B CA  
14502 C C   . GLN C 284  ? 4.5458 2.8119 3.4290 0.9011  -0.0577 0.6332  284  GLN B C   
14503 O O   . GLN C 284  ? 4.5090 2.7608 3.3864 0.8689  -0.0526 0.6092  284  GLN B O   
14504 C CB  . GLN C 284  ? 4.6555 2.9117 3.4809 0.9837  0.0029  0.7049  284  GLN B CB  
14505 C CG  . GLN C 284  ? 4.6208 2.8476 3.4610 0.9840  0.0444  0.7535  284  GLN B CG  
14506 C CD  . GLN C 284  ? 4.6656 2.8682 3.4172 0.9962  0.0873  0.7266  284  GLN B CD  
14507 O OE1 . GLN C 284  ? 4.6637 2.8684 3.3454 0.9862  0.0803  0.6566  284  GLN B OE1 
14508 N NE2 . GLN C 284  ? 4.7132 2.8916 3.4688 1.0178  0.1324  0.7833  284  GLN B NE2 
14509 N N   . THR C 285  ? 4.4980 2.7794 3.4511 0.9014  -0.0883 0.6654  285  THR B N   
14510 C CA  . THR C 285  ? 4.4374 2.7176 3.4623 0.8627  -0.1181 0.6738  285  THR B CA  
14511 C C   . THR C 285  ? 4.3711 2.6576 3.3722 0.8214  -0.1456 0.5947  285  THR B C   
14512 O O   . THR C 285  ? 4.2898 2.5651 3.3202 0.7843  -0.1542 0.5897  285  THR B O   
14513 C CB  . THR C 285  ? 4.4422 2.6983 3.5070 0.8521  -0.0924 0.7297  285  THR B CB  
14514 O OG1 . THR C 285  ? 4.5179 2.7654 3.5824 0.8937  -0.0543 0.7940  285  THR B OG1 
14515 C CG2 . THR C 285  ? 4.4003 2.6568 3.5535 0.8233  -0.1253 0.7634  285  THR B CG2 
14516 N N   . ALA C 286  ? 4.8924 3.1975 3.8399 0.8284  -0.1585 0.5344  286  ALA B N   
14517 C CA  . ALA C 286  ? 4.8226 3.1396 3.7515 0.7931  -0.1881 0.4589  286  ALA B CA  
14518 C C   . ALA C 286  ? 4.7629 3.1003 3.7449 0.7860  -0.2320 0.4529  286  ALA B C   
14519 O O   . ALA C 286  ? 4.7749 3.1314 3.7517 0.8137  -0.2433 0.4522  286  ALA B O   
14520 C CB  . ALA C 286  ? 4.8844 3.2107 3.7279 0.8033  -0.1780 0.3972  286  ALA B CB  
14521 N N   . MET C 287  ? 4.0419 2.3738 3.0726 0.7481  -0.2567 0.4470  287  MET B N   
14522 C CA  . MET C 287  ? 3.9850 2.3268 3.0792 0.7395  -0.2955 0.4577  287  MET B CA  
14523 C C   . MET C 287  ? 4.0295 2.3980 3.1125 0.7495  -0.3243 0.4119  287  MET B C   
14524 O O   . MET C 287  ? 4.0309 2.4117 3.0765 0.7312  -0.3367 0.3430  287  MET B O   
14525 C CB  . MET C 287  ? 3.8744 2.2025 3.0088 0.6927  -0.3161 0.4486  287  MET B CB  
14526 C CG  . MET C 287  ? 3.8119 2.1154 2.9824 0.6839  -0.2960 0.5110  287  MET B CG  
14527 S SD  . MET C 287  ? 4.2549 2.5405 3.4376 0.6261  -0.3079 0.4830  287  MET B SD  
14528 C CE  . MET C 287  ? 3.7978 2.0893 2.8911 0.6166  -0.2882 0.4033  287  MET B CE  
14529 N N   . GLN C 288  ? 6.6454 5.0866 5.8380 0.7519  -0.3245 0.4584  288  GLN B N   
14530 C CA  . GLN C 288  ? 6.6406 5.1860 5.9319 0.7283  -0.3373 0.4364  288  GLN B CA  
14531 C C   . GLN C 288  ? 6.6395 5.1535 5.9524 0.7119  -0.3733 0.4248  288  GLN B C   
14532 O O   . GLN C 288  ? 6.6461 5.0851 5.9403 0.7090  -0.3889 0.4497  288  GLN B O   
14533 C CB  . GLN C 288  ? 6.6395 5.2969 6.0732 0.7210  -0.3199 0.4972  288  GLN B CB  
14534 C CG  . GLN C 288  ? 6.6506 5.3258 6.1920 0.7111  -0.3145 0.5800  288  GLN B CG  
14535 C CD  . GLN C 288  ? 6.6513 5.4376 6.3460 0.6911  -0.3134 0.6344  288  GLN B CD  
14536 O OE1 . GLN C 288  ? 6.6486 5.5173 6.4026 0.6753  -0.3142 0.6166  288  GLN B OE1 
14537 N NE2 . GLN C 288  ? 6.6575 5.4428 6.4198 0.6851  -0.3191 0.6993  288  GLN B NE2 
14538 N N   . ASN C 289  ? 4.3653 2.7833 3.5554 0.7563  -0.4316 0.3703  289  ASN B N   
14539 C CA  . ASN C 289  ? 4.3694 2.7844 3.6152 0.7336  -0.4685 0.3618  289  ASN B CA  
14540 C C   . ASN C 289  ? 4.2407 2.6308 3.5152 0.6884  -0.4788 0.3596  289  ASN B C   
14541 O O   . ASN C 289  ? 4.1747 2.5432 3.4846 0.6817  -0.4706 0.4163  289  ASN B O   
14542 C CB  . ASN C 289  ? 4.4919 2.9091 3.7954 0.7615  -0.4831 0.4198  289  ASN B CB  
14543 C CG  . ASN C 289  ? 4.6258 3.0678 3.9027 0.8065  -0.4743 0.4257  289  ASN B CG  
14544 O OD1 . ASN C 289  ? 4.6843 3.1429 3.8998 0.8156  -0.4617 0.3814  289  ASN B OD1 
14545 N ND2 . ASN C 289  ? 4.6690 3.1130 3.9920 0.8339  -0.4818 0.4818  289  ASN B ND2 
14546 N N   . THR C 290  ? 2.9644 1.3586 2.2233 0.6576  -0.4969 0.2943  290  THR B N   
14547 C CA  . THR C 290  ? 2.8930 1.2662 2.1888 0.6162  -0.5198 0.2873  290  THR B CA  
14548 C C   . THR C 290  ? 2.8615 1.2479 2.1623 0.6056  -0.5508 0.2292  290  THR B C   
14549 O O   . THR C 290  ? 2.8550 1.2280 2.1704 0.5696  -0.5709 0.2006  290  THR B O   
14550 C CB  . THR C 290  ? 2.6490 1.0044 1.9204 0.5803  -0.5034 0.2745  290  THR B CB  
14551 O OG1 . THR C 290  ? 2.6237 0.9567 1.9306 0.5795  -0.4909 0.3456  290  THR B OG1 
14552 C CG2 . THR C 290  ? 2.6778 1.0230 1.9561 0.5353  -0.5283 0.2267  290  THR B CG2 
14553 N N   . MET C 291  ? 4.3242 2.7370 3.6126 0.6387  -0.5538 0.2139  291  MET B N   
14554 C CA  . MET C 291  ? 4.3010 2.7299 3.5990 0.6376  -0.5813 0.1660  291  MET B CA  
14555 C C   . MET C 291  ? 4.2113 2.6421 3.4796 0.6008  -0.5879 0.0945  291  MET B C   
14556 O O   . MET C 291  ? 4.1764 2.5839 3.4618 0.5646  -0.5982 0.0888  291  MET B O   
14557 C CB  . MET C 291  ? 4.3357 2.7492 3.7003 0.6375  -0.6096 0.2011  291  MET B CB  
14558 C CG  . MET C 291  ? 4.3844 2.8012 3.7818 0.6770  -0.6062 0.2681  291  MET B CG  
14559 S SD  . MET C 291  ? 4.7011 3.1023 4.1748 0.6772  -0.6429 0.2993  291  MET B SD  
14560 C CE  . MET C 291  ? 4.6101 2.9746 4.1020 0.6224  -0.6574 0.2886  291  MET B CE  
14561 N N   . LEU C 292  ? 4.3722 2.8314 3.5947 0.6100  -0.5816 0.0412  292  LEU B N   
14562 C CA  . LEU C 292  ? 4.2969 2.7636 3.4931 0.5790  -0.5886 -0.0291 292  LEU B CA  
14563 C C   . LEU C 292  ? 4.2246 2.6775 3.4681 0.5603  -0.6181 -0.0374 292  LEU B C   
14564 O O   . LEU C 292  ? 4.2533 2.7118 3.5333 0.5826  -0.6357 -0.0211 292  LEU B O   
14565 C CB  . LEU C 292  ? 4.3451 2.8489 3.5040 0.5985  -0.5874 -0.0796 292  LEU B CB  
14566 C CG  . LEU C 292  ? 4.3364 2.8536 3.4629 0.5690  -0.5905 -0.1540 292  LEU B CG  
14567 C CD1 . LEU C 292  ? 4.3247 2.8339 3.4876 0.5450  -0.6165 -0.1825 292  LEU B CD1 
14568 C CD2 . LEU C 292  ? 4.2816 2.7839 3.3700 0.5412  -0.5687 -0.1627 292  LEU B CD2 
14569 N N   . ILE C 293  ? 3.5355 1.9684 2.7780 0.5194  -0.6237 -0.0619 293  ILE B N   
14570 C CA  . ILE C 293  ? 3.4686 1.8830 2.7512 0.4988  -0.6516 -0.0715 293  ILE B CA  
14571 C C   . ILE C 293  ? 3.4353 1.8529 2.6949 0.4652  -0.6593 -0.1427 293  ILE B C   
14572 O O   . ILE C 293  ? 3.3994 1.8006 2.6401 0.4299  -0.6533 -0.1576 293  ILE B O   
14573 C CB  . ILE C 293  ? 3.4123 1.7891 2.7367 0.4837  -0.6592 -0.0106 293  ILE B CB  
14574 C CG1 . ILE C 293  ? 3.3957 1.7739 2.7536 0.5224  -0.6568 0.0572  293  ILE B CG1 
14575 C CG2 . ILE C 293  ? 3.4177 1.7708 2.7741 0.4560  -0.6882 -0.0282 293  ILE B CG2 
14576 C CD1 . ILE C 293  ? 3.3521 1.6999 2.7449 0.5138  -0.6545 0.1278  293  ILE B CD1 
14577 N N   . ASN C 294  ? 2.8083 1.2479 2.0724 0.4778  -0.6728 -0.1843 294  ASN B N   
14578 C CA  . ASN C 294  ? 2.8248 1.2776 2.0653 0.4555  -0.6773 -0.2560 294  ASN B CA  
14579 C C   . ASN C 294  ? 2.7417 1.2147 1.9275 0.4428  -0.6555 -0.2963 294  ASN B C   
14580 O O   . ASN C 294  ? 2.7092 1.1696 1.8746 0.4063  -0.6512 -0.3240 294  ASN B O   
14581 C CB  . ASN C 294  ? 2.8906 1.3117 2.1503 0.4183  -0.6949 -0.2722 294  ASN B CB  
14582 C CG  . ASN C 294  ? 2.9950 1.4323 2.2369 0.4022  -0.7004 -0.3449 294  ASN B CG  
14583 O OD1 . ASN C 294  ? 3.0056 1.4483 2.2105 0.3756  -0.6887 -0.3842 294  ASN B OD1 
14584 N ND2 . ASN C 294  ? 3.0624 1.5095 2.3317 0.4200  -0.7171 -0.3627 294  ASN B ND2 
14585 N N   . GLY C 295  ? 3.9294 2.4338 3.0909 0.4729  -0.6429 -0.3002 295  GLY B N   
14586 C CA  . GLY C 295  ? 3.9036 2.4298 3.0128 0.4641  -0.6244 -0.3420 295  GLY B CA  
14587 C C   . GLY C 295  ? 3.8299 2.3352 2.9127 0.4462  -0.6032 -0.3174 295  GLY B C   
14588 O O   . GLY C 295  ? 3.8095 2.3253 2.8488 0.4315  -0.5876 -0.3515 295  GLY B O   
14589 N N   . ILE C 296  ? 3.1539 1.6293 2.2653 0.4468  -0.6030 -0.2574 296  ILE B N   
14590 C CA  . ILE C 296  ? 3.0675 1.5239 2.1592 0.4373  -0.5806 -0.2230 296  ILE B CA  
14591 C C   . ILE C 296  ? 3.0883 1.5231 2.2158 0.4574  -0.5779 -0.1451 296  ILE B C   
14592 O O   . ILE C 296  ? 3.1177 1.5537 2.2833 0.4813  -0.5929 -0.1161 296  ILE B O   
14593 C CB  . ILE C 296  ? 2.9101 1.3448 1.9903 0.3891  -0.5790 -0.2460 296  ILE B CB  
14594 C CG1 . ILE C 296  ? 2.8997 1.3483 1.9691 0.3654  -0.5929 -0.3159 296  ILE B CG1 
14595 C CG2 . ILE C 296  ? 2.8166 1.2477 1.8552 0.3805  -0.5509 -0.2410 296  ILE B CG2 
14596 C CD1 . ILE C 296  ? 2.8919 1.3633 1.9099 0.3533  -0.5768 -0.3700 296  ILE B CD1 
14597 N N   . ALA C 297  ? 3.0129 1.4303 2.1263 0.4493  -0.5565 -0.1118 297  ALA B N   
14598 C CA  . ALA C 297  ? 2.9704 1.3609 2.1202 0.4533  -0.5525 -0.0395 297  ALA B CA  
14599 C C   . ALA C 297  ? 2.9703 1.3505 2.0851 0.4388  -0.5245 -0.0326 297  ALA B C   
14600 O O   . ALA C 297  ? 2.9918 1.3825 2.0623 0.4215  -0.5151 -0.0853 297  ALA B O   
14601 C CB  . ALA C 297  ? 2.9772 1.3760 2.1478 0.4982  -0.5490 0.0109  297  ALA B CB  
14602 N N   . GLN C 298  ? 3.3931 1.7531 2.5283 0.4458  -0.5105 0.0319  298  GLN B N   
14603 C CA  . GLN C 298  ? 3.3732 1.7215 2.4782 0.4330  -0.4824 0.0415  298  GLN B CA  
14604 C C   . GLN C 298  ? 3.3245 1.6548 2.4532 0.4504  -0.4628 0.1174  298  GLN B C   
14605 O O   . GLN C 298  ? 3.3291 1.6533 2.5047 0.4686  -0.4732 0.1693  298  GLN B O   
14606 C CB  . GLN C 298  ? 3.3874 1.7186 2.4935 0.3845  -0.4912 0.0170  298  GLN B CB  
14607 C CG  . GLN C 298  ? 3.4725 1.8195 2.5336 0.3628  -0.4923 -0.0591 298  GLN B CG  
14608 C CD  . GLN C 298  ? 3.5170 1.8448 2.5816 0.3148  -0.5005 -0.0760 298  GLN B CD  
14609 O OE1 . GLN C 298  ? 3.5252 1.8274 2.6205 0.2984  -0.5016 -0.0282 298  GLN B OE1 
14610 N NE2 . GLN C 298  ? 3.5412 1.8817 2.5755 0.2914  -0.5069 -0.1426 298  GLN B NE2 
14611 N N   . VAL C 299  ? 2.4949 0.8160 1.5919 0.4432  -0.4342 0.1228  299  VAL B N   
14612 C CA  . VAL C 299  ? 2.4592 0.7616 1.5754 0.4557  -0.4105 0.1923  299  VAL B CA  
14613 C C   . VAL C 299  ? 2.4593 0.7479 1.5432 0.4344  -0.3840 0.1859  299  VAL B C   
14614 O O   . VAL C 299  ? 2.5225 0.8166 1.5672 0.4093  -0.3844 0.1262  299  VAL B O   
14615 C CB  . VAL C 299  ? 2.4938 0.8063 1.6022 0.5055  -0.3907 0.2288  299  VAL B CB  
14616 C CG1 . VAL C 299  ? 2.4762 0.7880 1.6448 0.5253  -0.4104 0.2814  299  VAL B CG1 
14617 C CG2 . VAL C 299  ? 2.5415 0.8793 1.5925 0.5253  -0.3856 0.1712  299  VAL B CG2 
14618 N N   . THR C 300  ? 3.4300 1.7008 2.5337 0.4445  -0.3609 0.2494  300  THR B N   
14619 C CA  . THR C 300  ? 3.4023 1.6568 2.4839 0.4273  -0.3333 0.2557  300  THR B CA  
14620 C C   . THR C 300  ? 3.4717 1.7167 2.5545 0.4627  -0.2979 0.3164  300  THR B C   
14621 O O   . THR C 300  ? 3.4445 1.6837 2.5767 0.4814  -0.2988 0.3808  300  THR B O   
14622 C CB  . THR C 300  ? 3.8381 2.0730 2.9598 0.3835  -0.3489 0.2736  300  THR B CB  
14623 O OG1 . THR C 300  ? 3.8387 2.0655 3.0261 0.3873  -0.3689 0.3322  300  THR B OG1 
14624 C CG2 . THR C 300  ? 3.8214 2.0626 2.9244 0.3445  -0.3748 0.2039  300  THR B CG2 
14625 N N   . PHE C 301  ? 2.8105 1.0530 1.8383 0.4718  -0.2659 0.2957  301  PHE B N   
14626 C CA  . PHE C 301  ? 2.9485 1.1875 1.9584 0.5151  -0.2322 0.3352  301  PHE B CA  
14627 C C   . PHE C 301  ? 3.0482 1.2632 2.0536 0.5113  -0.1960 0.3715  301  PHE B C   
14628 O O   . PHE C 301  ? 3.1112 1.3201 2.0611 0.5085  -0.1720 0.3370  301  PHE B O   
14629 C CB  . PHE C 301  ? 2.9577 1.2164 1.9032 0.5393  -0.2279 0.2799  301  PHE B CB  
14630 C CG  . PHE C 301  ? 2.9510 1.2018 1.8457 0.5731  -0.1875 0.2920  301  PHE B CG  
14631 C CD1 . PHE C 301  ? 2.9611 1.2130 1.8635 0.6162  -0.1726 0.3413  301  PHE B CD1 
14632 C CD2 . PHE C 301  ? 2.9519 1.1939 1.7865 0.5616  -0.1650 0.2496  301  PHE B CD2 
14633 C CE1 . PHE C 301  ? 3.0067 1.2489 1.8561 0.6468  -0.1347 0.3491  301  PHE B CE1 
14634 C CE2 . PHE C 301  ? 2.9835 1.2147 1.7654 0.5917  -0.1279 0.2565  301  PHE B CE2 
14635 C CZ  . PHE C 301  ? 3.0237 1.2543 1.8114 0.6343  -0.1123 0.3056  301  PHE B CZ  
14636 N N   . ASP C 302  ? 3.1855 1.3867 2.2533 0.5097  -0.1939 0.4422  302  ASP B N   
14637 C CA  . ASP C 302  ? 3.2028 1.3817 2.2799 0.5102  -0.1591 0.4901  302  ASP B CA  
14638 C C   . ASP C 302  ? 3.2273 1.4013 2.2480 0.5497  -0.1165 0.4912  302  ASP B C   
14639 O O   . ASP C 302  ? 3.2356 1.4106 2.2670 0.5891  -0.1004 0.5376  302  ASP B O   
14640 C CB  . ASP C 302  ? 3.2576 1.4275 2.4148 0.5139  -0.1632 0.5748  302  ASP B CB  
14641 C CG  . ASP C 302  ? 3.3505 1.5003 2.5202 0.5272  -0.1212 0.6346  302  ASP B CG  
14642 O OD1 . ASP C 302  ? 3.3825 1.5264 2.6165 0.5356  -0.1191 0.7084  302  ASP B OD1 
14643 O OD2 . ASP C 302  ? 3.3910 1.5305 2.5080 0.5296  -0.0899 0.6089  302  ASP B OD2 
14644 N N   . SER C 303  ? 3.7313 1.8985 2.6909 0.5382  -0.0984 0.4403  303  SER B N   
14645 C CA  . SER C 303  ? 3.7774 1.9383 2.6693 0.5714  -0.0616 0.4251  303  SER B CA  
14646 C C   . SER C 303  ? 3.8130 1.9526 2.7181 0.6032  -0.0187 0.4965  303  SER B C   
14647 O O   . SER C 303  ? 3.8870 2.0218 2.7471 0.6422  0.0108  0.5027  303  SER B O   
14648 C CB  . SER C 303  ? 3.7464 1.9015 2.5771 0.5456  -0.0539 0.3573  303  SER B CB  
14649 O OG  . SER C 303  ? 3.6804 1.8574 2.4971 0.5204  -0.0909 0.2918  303  SER B OG  
14650 N N   . GLU C 304  ? 3.7604 1.8874 2.7279 0.5856  -0.0161 0.5508  304  GLU B N   
14651 C CA  . GLU C 304  ? 3.7280 1.8365 2.7255 0.6114  0.0217  0.6268  304  GLU B CA  
14652 C C   . GLU C 304  ? 3.7278 1.8430 2.7316 0.6602  0.0349  0.6708  304  GLU B C   
14653 O O   . GLU C 304  ? 3.7444 1.8514 2.6927 0.6962  0.0696  0.6681  304  GLU B O   
14654 C CB  . GLU C 304  ? 3.6922 1.7968 2.7753 0.5836  0.0045  0.6822  304  GLU B CB  
14655 C CG  . GLU C 304  ? 3.7168 1.7989 2.8128 0.5665  0.0321  0.7090  304  GLU B CG  
14656 C CD  . GLU C 304  ? 3.7022 1.7835 2.8795 0.5325  0.0065  0.7544  304  GLU B CD  
14657 O OE1 . GLU C 304  ? 3.6988 1.7951 2.9208 0.5266  -0.0303 0.7683  304  GLU B OE1 
14658 O OE2 . GLU C 304  ? 3.6945 1.7595 2.8900 0.5116  0.0224  0.7758  304  GLU B OE2 
14659 N N   . THR C 305  ? 3.0936 1.2216 2.1674 0.6594  0.0070  0.7147  305  THR B N   
14660 C CA  . THR C 305  ? 3.1653 1.3064 2.2530 0.6988  0.0056  0.7486  305  THR B CA  
14661 C C   . THR C 305  ? 3.2382 1.3842 2.2404 0.7278  0.0215  0.6975  305  THR B C   
14662 O O   . THR C 305  ? 3.2630 1.3937 2.2231 0.7583  0.0639  0.7129  305  THR B O   
14663 C CB  . THR C 305  ? 3.1080 1.2703 2.2446 0.6814  -0.0463 0.7417  305  THR B CB  
14664 O OG1 . THR C 305  ? 3.0631 1.2194 2.2617 0.6396  -0.0702 0.7615  305  THR B OG1 
14665 C CG2 . THR C 305  ? 3.1483 1.3218 2.3224 0.7196  -0.0483 0.7974  305  THR B CG2 
14666 N N   . ALA C 306  ? 3.4650 1.6309 2.4400 0.7160  -0.0129 0.6344  306  ALA B N   
14667 C CA  . ALA C 306  ? 3.6416 1.8199 2.5514 0.7465  -0.0094 0.5955  306  ALA B CA  
14668 C C   . ALA C 306  ? 3.7976 1.9611 2.6180 0.7601  0.0263  0.5550  306  ALA B C   
14669 O O   . ALA C 306  ? 3.8456 2.0200 2.6081 0.7533  0.0130  0.4864  306  ALA B O   
14670 C CB  . ALA C 306  ? 3.5872 1.7916 2.4965 0.7281  -0.0563 0.5390  306  ALA B CB  
14671 N N   . VAL C 307  ? 6.2530 4.3913 5.0639 0.7799  0.0712  0.5989  307  VAL B N   
14672 C CA  . VAL C 307  ? 6.4981 4.6179 5.2241 0.8049  0.1109  0.5756  307  VAL B CA  
14673 C C   . VAL C 307  ? 6.6035 4.8339 5.4970 0.7621  0.1158  0.6266  307  VAL B C   
14674 O O   . VAL C 307  ? 6.5897 4.8653 5.4943 0.7652  0.1270  0.6230  307  VAL B O   
14675 C CB  . VAL C 307  ? 5.7222 3.8298 4.3921 0.7729  0.1146  0.5074  307  VAL B CB  
14676 C CG1 . VAL C 307  ? 5.8059 3.8879 4.3927 0.8003  0.1593  0.4939  307  VAL B CG1 
14677 C CG2 . VAL C 307  ? 5.7009 3.8339 4.3464 0.7476  0.0720  0.4325  307  VAL B CG2 
14678 N N   . LYS C 308  ? 4.2229 2.3080 3.0317 0.8191  0.1652  0.6989  308  LYS B N   
14679 C CA  . LYS C 308  ? 4.4959 2.5561 3.3217 0.8440  0.2134  0.7660  308  LYS B CA  
14680 C C   . LYS C 308  ? 4.8038 2.8643 3.6117 0.8965  0.2390  0.8073  308  LYS B C   
14681 O O   . LYS C 308  ? 4.9065 2.9493 3.6382 0.9242  0.2739  0.7896  308  LYS B O   
14682 C CB  . LYS C 308  ? 4.4378 2.4981 3.3618 0.8220  0.2047  0.8287  308  LYS B CB  
14683 C CG  . LYS C 308  ? 4.3288 2.3827 3.2667 0.7715  0.1883  0.7957  308  LYS B CG  
14684 C CD  . LYS C 308  ? 4.2966 2.3486 3.3295 0.7526  0.1826  0.8645  308  LYS B CD  
14685 C CE  . LYS C 308  ? 4.2666 2.3430 3.3681 0.7508  0.1421  0.8974  308  LYS B CE  
14686 N NZ  . LYS C 308  ? 4.2770 2.3852 3.4794 0.7335  0.1477  0.9598  308  LYS B NZ  
14687 N N   . GLU C 309  ? 5.6846 3.7640 4.5602 0.9096  0.2214  0.8613  309  GLU B N   
14688 C CA  . GLU C 309  ? 5.9231 4.0059 4.7828 0.9588  0.2424  0.8996  309  GLU B CA  
14689 C C   . GLU C 309  ? 5.8217 3.9194 4.6070 0.9711  0.2238  0.8358  309  GLU B C   
14690 O O   . GLU C 309  ? 6.0654 4.1640 4.8159 1.0119  0.2424  0.8538  309  GLU B O   
14691 C CB  . GLU C 309  ? 6.2078 4.3082 5.1626 0.9685  0.2261  0.9748  309  GLU B CB  
14692 C CG  . GLU C 309  ? 6.3860 4.6428 5.5061 0.8892  0.1386  0.9574  309  GLU B CG  
14693 C CD  . GLU C 309  ? 6.4545 4.8243 5.7098 0.7935  0.0812  0.9376  309  GLU B CD  
14694 O OE1 . GLU C 309  ? 6.4768 4.8517 5.7679 0.7568  0.0770  0.9383  309  GLU B OE1 
14695 O OE2 . GLU C 309  ? 6.4863 4.9269 5.7958 0.7600  0.0414  0.9209  309  GLU B OE2 
14696 N N   . LEU C 310  ? 5.1926 3.3021 3.9529 0.9361  0.1877  0.7624  310  LEU B N   
14697 C CA  . LEU C 310  ? 5.0893 3.2186 3.7923 0.9445  0.1630  0.7042  310  LEU B CA  
14698 C C   . LEU C 310  ? 4.9493 3.0621 3.5457 0.9523  0.1859  0.6431  310  LEU B C   
14699 O O   . LEU C 310  ? 4.9562 3.0846 3.4993 0.9599  0.1674  0.5943  310  LEU B O   
14700 C CB  . LEU C 310  ? 5.0534 3.2105 3.7948 0.9072  0.1068  0.6623  310  LEU B CB  
14701 C CG  . LEU C 310  ? 4.9824 3.1527 3.8267 0.8920  0.0784  0.7143  310  LEU B CG  
14702 C CD1 . LEU C 310  ? 4.9314 3.1305 3.7979 0.8712  0.0251  0.6728  310  LEU B CD1 
14703 C CD2 . LEU C 310  ? 5.0310 3.2005 3.9204 0.9306  0.0986  0.7979  310  LEU B CD2 
14704 N N   . SER C 311  ? 4.9166 2.9976 3.4848 0.9500  0.2256  0.6478  311  SER B N   
14705 C CA  . SER C 311  ? 4.8332 2.8896 3.3004 0.9620  0.2563  0.6022  311  SER B CA  
14706 C C   . SER C 311  ? 4.7596 2.7790 3.2220 0.9570  0.3006  0.6238  311  SER B C   
14707 O O   . SER C 311  ? 4.6722 2.6893 3.2113 0.9418  0.3028  0.6709  311  SER B O   
14708 C CB  . SER C 311  ? 4.7423 2.8129 3.1555 0.9332  0.2224  0.5131  311  SER B CB  
14709 O OG  . SER C 311  ? 4.7289 2.8271 3.1203 0.9498  0.1945  0.4912  311  SER B OG  
14710 N N   . TYR C 312  ? 4.4496 2.4395 2.8227 0.9696  0.3347  0.5905  312  TYR B N   
14711 C CA  . TYR C 312  ? 4.4568 2.4068 2.8122 0.9690  0.3815  0.6056  312  TYR B CA  
14712 C C   . TYR C 312  ? 3.8152 1.7621 2.2174 0.9212  0.3687  0.5913  312  TYR B C   
14713 O O   . TYR C 312  ? 3.8069 1.7212 2.1940 0.9174  0.4051  0.5986  312  TYR B O   
14714 C CB  . TYR C 312  ? 4.5821 2.5008 2.8222 0.9858  0.4124  0.5561  312  TYR B CB  
14715 C CG  . TYR C 312  ? 4.7303 2.6202 2.9213 1.0375  0.4637  0.5979  312  TYR B CG  
14716 C CD1 . TYR C 312  ? 4.8644 2.7376 2.9499 1.0596  0.4771  0.5547  312  TYR B CD1 
14717 C CD2 . TYR C 312  ? 4.7442 2.6225 2.9924 1.0633  0.4990  0.6801  312  TYR B CD2 
14718 C CE1 . TYR C 312  ? 4.9943 2.8386 3.0295 1.1064  0.5249  0.5913  312  TYR B CE1 
14719 C CE2 . TYR C 312  ? 4.8675 2.7190 3.0696 1.1111  0.5481  0.7180  312  TYR B CE2 
14720 C CZ  . TYR C 312  ? 4.9881 2.8218 3.0821 1.1325  0.5612  0.6728  312  TYR B CZ  
14721 O OH  . TYR C 312  ? 5.1131 2.9179 3.1581 1.1797  0.6108  0.7103  312  TYR B OH  
14722 N N   . TYR C 313  ? 4.6087 2.5880 3.0644 0.8858  0.3181  0.5705  313  TYR B N   
14723 C CA  . TYR C 313  ? 4.4587 2.4397 2.9605 0.8378  0.2990  0.5552  313  TYR B CA  
14724 C C   . TYR C 313  ? 4.4174 2.4131 3.0273 0.8251  0.2822  0.6204  313  TYR B C   
14725 O O   . TYR C 313  ? 4.3894 2.4149 3.0443 0.8184  0.2425  0.6249  313  TYR B O   
14726 C CB  . TYR C 313  ? 4.3084 2.3129 2.7850 0.8009  0.2527  0.4747  313  TYR B CB  
14727 C CG  . TYR C 313  ? 4.2930 2.2992 2.6762 0.8150  0.2507  0.4114  313  TYR B CG  
14728 C CD1 . TYR C 313  ? 4.2874 2.3252 2.6639 0.8249  0.2166  0.3898  313  TYR B CD1 
14729 C CD2 . TYR C 313  ? 4.3249 2.3003 2.6268 0.8179  0.2820  0.3739  313  TYR B CD2 
14730 C CE1 . TYR C 313  ? 4.3649 2.4056 2.6568 0.8374  0.2130  0.3337  313  TYR B CE1 
14731 C CE2 . TYR C 313  ? 4.4005 2.3764 2.6149 0.8296  0.2784  0.3165  313  TYR B CE2 
14732 C CZ  . TYR C 313  ? 4.4138 2.4235 2.6239 0.8391  0.2432  0.2971  313  TYR B CZ  
14733 O OH  . TYR C 313  ? 4.4909 2.5029 2.6164 0.8498  0.2375  0.2420  313  TYR B OH  
14734 N N   . SER C 314  ? 4.6828 2.6570 3.3346 0.8208  0.3113  0.6702  314  SER B N   
14735 C CA  . SER C 314  ? 4.5963 2.5822 3.3508 0.8044  0.2949  0.7324  314  SER B CA  
14736 C C   . SER C 314  ? 4.4373 2.4174 3.2189 0.7553  0.2812  0.7121  314  SER B C   
14737 O O   . SER C 314  ? 4.3382 2.3313 3.1982 0.7281  0.2539  0.7435  314  SER B O   
14738 C CB  . SER C 314  ? 4.7220 2.6910 3.5160 0.8407  0.3390  0.8189  314  SER B CB  
14739 O OG  . SER C 314  ? 4.8152 2.7491 3.5653 0.8515  0.3887  0.8201  314  SER B OG  
14740 N N   . LEU C 315  ? 4.1547 2.1141 2.8685 0.7442  0.3002  0.6592  315  LEU B N   
14741 C CA  . LEU C 315  ? 4.0716 2.0212 2.7986 0.7005  0.2947  0.6369  315  LEU B CA  
14742 C C   . LEU C 315  ? 3.9385 1.9065 2.6344 0.6612  0.2522  0.5556  315  LEU B C   
14743 O O   . LEU C 315  ? 3.9689 1.9423 2.5940 0.6703  0.2463  0.4967  315  LEU B O   
14744 C CB  . LEU C 315  ? 4.2067 2.1186 2.8825 0.7123  0.3459  0.6337  315  LEU B CB  
14745 C CG  . LEU C 315  ? 4.2747 2.1653 3.0095 0.7184  0.3814  0.7086  315  LEU B CG  
14746 C CD1 . LEU C 315  ? 4.3554 2.2071 3.0265 0.7468  0.4385  0.7077  315  LEU B CD1 
14747 C CD2 . LEU C 315  ? 4.1805 2.0758 2.9743 0.6681  0.3575  0.7113  315  LEU B CD2 
14748 N N   . GLU C 316  ? 3.0614 1.0387 1.8107 0.6173  0.2231  0.5541  316  GLU B N   
14749 C CA  . GLU C 316  ? 2.9681 0.9582 1.6893 0.5760  0.1893  0.4792  316  GLU B CA  
14750 C C   . GLU C 316  ? 2.9622 0.9302 1.5963 0.5822  0.2197  0.4273  316  GLU B C   
14751 O O   . GLU C 316  ? 2.9828 0.9527 1.5509 0.6075  0.2251  0.3903  316  GLU B O   
14752 C CB  . GLU C 316  ? 2.9209 0.9114 1.7027 0.5293  0.1701  0.4927  316  GLU B CB  
14753 C CG  . GLU C 316  ? 2.9408 0.9565 1.7289 0.4869  0.1193  0.4364  316  GLU B CG  
14754 C CD  . GLU C 316  ? 3.0197 1.0317 1.7443 0.4601  0.1179  0.3598  316  GLU B CD  
14755 O OE1 . GLU C 316  ? 3.0554 1.0423 1.7582 0.4544  0.1492  0.3606  316  GLU B OE1 
14756 O OE2 . GLU C 316  ? 3.0342 1.0684 1.7336 0.4440  0.0852  0.3001  316  GLU B OE2 
14757 N N   . ASP C 317  ? 3.0471 0.9933 1.6825 0.5582  0.2381  0.4263  317  ASP B N   
14758 C CA  . ASP C 317  ? 3.1310 1.0469 1.6947 0.5675  0.2764  0.3961  317  ASP B CA  
14759 C C   . ASP C 317  ? 3.2420 1.1572 1.7316 0.6057  0.2873  0.3661  317  ASP B C   
14760 O O   . ASP C 317  ? 3.2457 1.1698 1.6753 0.5940  0.2696  0.2955  317  ASP B O   
14761 C CB  . ASP C 317  ? 3.1646 1.0496 1.7599 0.5839  0.3220  0.4641  317  ASP B CB  
14762 C CG  . ASP C 317  ? 3.3836 1.2347 1.9290 0.5735  0.3555  0.4359  317  ASP B CG  
14763 O OD1 . ASP C 317  ? 3.4484 1.2946 1.9185 0.5662  0.3528  0.3658  317  ASP B OD1 
14764 O OD2 . ASP C 317  ? 3.3688 1.1977 1.9524 0.5732  0.3852  0.4860  317  ASP B OD2 
14765 N N   . LEU C 318  ? 4.4579 2.3649 2.9554 0.6503  0.3140  0.4216  318  LEU B N   
14766 C CA  . LEU C 318  ? 4.5788 2.4797 3.0051 0.6922  0.3316  0.4054  318  LEU B CA  
14767 C C   . LEU C 318  ? 4.5533 2.4868 2.9490 0.6852  0.2885  0.3469  318  LEU B C   
14768 O O   . LEU C 318  ? 4.5767 2.5187 2.9422 0.7188  0.2887  0.3483  318  LEU B O   
14769 C CB  . LEU C 318  ? 4.6477 2.5428 3.1047 0.7383  0.3591  0.4818  318  LEU B CB  
14770 C CG  . LEU C 318  ? 4.7939 2.6484 3.2074 0.7776  0.4192  0.5139  318  LEU B CG  
14771 C CD1 . LEU C 318  ? 4.8225 2.6770 3.2953 0.8136  0.4419  0.6010  318  LEU B CD1 
14772 C CD2 . LEU C 318  ? 4.9397 2.7792 3.2471 0.8023  0.4341  0.4612  318  LEU B CD2 
14773 N N   . ASN C 319  ? 2.8497 0.8019 1.2539 0.6418  0.2521  0.2961  319  ASN B N   
14774 C CA  . ASN C 319  ? 2.8001 0.7814 1.1715 0.6334  0.2146  0.2355  319  ASN B CA  
14775 C C   . ASN C 319  ? 2.7885 0.7729 1.1238 0.5928  0.1973  0.1630  319  ASN B C   
14776 O O   . ASN C 319  ? 2.7487 0.7363 1.1264 0.5555  0.1837  0.1608  319  ASN B O   
14777 C CB  . ASN C 319  ? 2.7487 0.7642 1.1913 0.6267  0.1750  0.2587  319  ASN B CB  
14778 C CG  . ASN C 319  ? 2.7746 0.8191 1.1855 0.6351  0.1441  0.2133  319  ASN B CG  
14779 O OD1 . ASN C 319  ? 2.8795 0.9180 1.2174 0.6589  0.1573  0.1824  319  ASN B OD1 
14780 N ND2 . ASN C 319  ? 2.7426 0.8182 1.2060 0.6152  0.1017  0.2074  319  ASN B ND2 
14781 N N   . ASN C 320  ? 3.2705 1.2533 1.5265 0.6001  0.1983  0.1052  320  ASN B N   
14782 C CA  . ASN C 320  ? 3.2585 1.2483 1.4770 0.5630  0.1793  0.0324  320  ASN B CA  
14783 C C   . ASN C 320  ? 3.3448 1.3526 1.5005 0.5760  0.1617  -0.0214 320  ASN B C   
14784 O O   . ASN C 320  ? 3.3805 1.3915 1.4860 0.5545  0.1511  -0.0854 320  ASN B O   
14785 C CB  . ASN C 320  ? 3.2975 1.2490 1.4774 0.5517  0.2142  0.0212  320  ASN B CB  
14786 C CG  . ASN C 320  ? 3.2582 1.1985 1.5049 0.5279  0.2229  0.0637  320  ASN B CG  
14787 O OD1 . ASN C 320  ? 3.2161 1.1612 1.4758 0.4866  0.2074  0.0328  320  ASN B OD1 
14788 N ND2 . ASN C 320  ? 3.2626 1.1898 1.5553 0.5531  0.2462  0.1369  320  ASN B ND2 
14789 N N   . LYS C 321  ? 4.3413 2.3606 2.5022 0.6123  0.1594  0.0092  321  LYS B N   
14790 C CA  . LYS C 321  ? 4.4165 2.4614 2.5372 0.6271  0.1353  -0.0294 321  LYS B CA  
14791 C C   . LYS C 321  ? 4.2999 2.3873 2.4852 0.6105  0.0899  -0.0330 321  LYS B C   
14792 O O   . LYS C 321  ? 4.2013 2.2961 2.4445 0.5788  0.0747  -0.0261 321  LYS B O   
14793 C CB  . LYS C 321  ? 4.5834 2.6151 2.6732 0.6771  0.1604  0.0097  321  LYS B CB  
14794 C CG  . LYS C 321  ? 4.6028 2.6332 2.7637 0.6992  0.1717  0.0892  321  LYS B CG  
14795 C CD  . LYS C 321  ? 4.7741 2.7875 2.8974 0.7502  0.2029  0.1286  321  LYS B CD  
14796 C CE  . LYS C 321  ? 4.8679 2.8339 2.9270 0.7659  0.2530  0.1329  321  LYS B CE  
14797 N NZ  . LYS C 321  ? 4.9798 2.9264 2.9993 0.8161  0.2862  0.1723  321  LYS B NZ  
14798 N N   . TYR C 322  ? 3.4354 1.5489 1.6111 0.6322  0.0684  -0.0422 322  TYR B N   
14799 C CA  . TYR C 322  ? 3.3687 1.5234 1.5896 0.6131  0.0224  -0.0661 322  TYR B CA  
14800 C C   . TYR C 322  ? 3.3451 1.5170 1.6405 0.6278  0.0060  -0.0116 322  TYR B C   
14801 O O   . TYR C 322  ? 3.3758 1.5298 1.6953 0.6539  0.0303  0.0519  322  TYR B O   
14802 C CB  . TYR C 322  ? 3.4194 1.5982 1.5842 0.6172  0.0005  -0.1269 322  TYR B CB  
14803 C CG  . TYR C 322  ? 3.4224 1.5929 1.5302 0.5895  0.0036  -0.1896 322  TYR B CG  
14804 C CD1 . TYR C 322  ? 3.3741 1.5751 1.4591 0.5708  -0.0279 -0.2536 322  TYR B CD1 
14805 C CD2 . TYR C 322  ? 3.4784 1.6106 1.5592 0.5812  0.0382  -0.1831 322  TYR B CD2 
14806 C CE1 . TYR C 322  ? 3.3985 1.5921 1.4342 0.5439  -0.0254 -0.3094 322  TYR B CE1 
14807 C CE2 . TYR C 322  ? 3.4896 1.6124 1.5206 0.5549  0.0411  -0.2384 322  TYR B CE2 
14808 C CZ  . TYR C 322  ? 3.4674 1.6211 1.4758 0.5356  0.0090  -0.3015 322  TYR B CZ  
14809 O OH  . TYR C 322  ? 3.4802 1.6243 1.4407 0.5084  0.0122  -0.3552 322  TYR B OH  
14810 N N   . LEU C 323  ? 2.7535 0.9599 1.0850 0.6099  -0.0352 -0.0384 323  LEU B N   
14811 C CA  . LEU C 323  ? 2.6784 0.9055 1.0793 0.6198  -0.0595 0.0011  323  LEU B CA  
14812 C C   . LEU C 323  ? 2.6922 0.9571 1.0873 0.6228  -0.0966 -0.0425 323  LEU B C   
14813 O O   . LEU C 323  ? 2.6739 0.9585 1.0799 0.5906  -0.1242 -0.0905 323  LEU B O   
14814 C CB  . LEU C 323  ? 2.6402 0.8651 1.1122 0.5851  -0.0730 0.0218  323  LEU B CB  
14815 C CG  . LEU C 323  ? 2.5835 0.8171 1.1381 0.5858  -0.0929 0.0745  323  LEU B CG  
14816 C CD1 . LEU C 323  ? 2.5546 0.8211 1.1355 0.5740  -0.1359 0.0405  323  LEU B CD1 
14817 C CD2 . LEU C 323  ? 2.5896 0.8135 1.1621 0.6278  -0.0728 0.1425  323  LEU B CD2 
14818 N N   . TYR C 324  ? 3.3902 1.6650 1.7689 0.6617  -0.0962 -0.0244 324  TYR B N   
14819 C CA  . TYR C 324  ? 3.4829 1.7930 1.8517 0.6705  -0.1281 -0.0615 324  TYR B CA  
14820 C C   . TYR C 324  ? 3.4370 1.7687 1.8797 0.6757  -0.1568 -0.0308 324  TYR B C   
14821 O O   . TYR C 324  ? 3.4071 1.7279 1.8896 0.6973  -0.1461 0.0329  324  TYR B O   
14822 C CB  . TYR C 324  ? 3.6525 1.9612 1.9565 0.7096  -0.1128 -0.0612 324  TYR B CB  
14823 C CG  . TYR C 324  ? 3.7569 2.1003 2.0666 0.7313  -0.1422 -0.0705 324  TYR B CG  
14824 C CD1 . TYR C 324  ? 3.8690 2.2338 2.1254 0.7308  -0.1582 -0.1282 324  TYR B CD1 
14825 C CD2 . TYR C 324  ? 3.7540 2.1085 2.1229 0.7531  -0.1536 -0.0192 324  TYR B CD2 
14826 C CE1 . TYR C 324  ? 3.9279 2.3254 2.1911 0.7516  -0.1850 -0.1345 324  TYR B CE1 
14827 C CE2 . TYR C 324  ? 3.8116 2.1974 2.1870 0.7740  -0.1799 -0.0260 324  TYR B CE2 
14828 C CZ  . TYR C 324  ? 3.8882 2.2957 2.2110 0.7735  -0.1953 -0.0832 324  TYR B CZ  
14829 O OH  . TYR C 324  ? 3.9232 2.3623 2.2554 0.7941  -0.2213 -0.0876 324  TYR B OH  
14830 N N   . ILE C 325  ? 3.2032 1.5653 1.6636 0.6565  -0.1926 -0.0765 325  ILE B N   
14831 C CA  . ILE C 325  ? 3.1242 1.5062 1.6532 0.6575  -0.2230 -0.0564 325  ILE B CA  
14832 C C   . ILE C 325  ? 3.1585 1.5751 1.6769 0.6745  -0.2498 -0.0883 325  ILE B C   
14833 O O   . ILE C 325  ? 3.2044 1.6370 1.6744 0.6676  -0.2565 -0.1447 325  ILE B O   
14834 C CB  . ILE C 325  ? 3.0054 1.3897 1.5831 0.6136  -0.2445 -0.0766 325  ILE B CB  
14835 C CG1 . ILE C 325  ? 2.9757 1.3291 1.5552 0.5897  -0.2207 -0.0593 325  ILE B CG1 
14836 C CG2 . ILE C 325  ? 2.9409 1.3318 1.5932 0.6159  -0.2678 -0.0377 325  ILE B CG2 
14837 C CD1 . ILE C 325  ? 2.8847 1.2371 1.5197 0.5514  -0.2416 -0.0619 325  ILE B CD1 
14838 N N   . ALA C 326  ? 2.9517 1.3804 1.5194 0.6959  -0.2660 -0.0504 326  ALA B N   
14839 C CA  . ALA C 326  ? 2.9923 1.4548 1.5651 0.7106  -0.2948 -0.0749 326  ALA B CA  
14840 C C   . ALA C 326  ? 2.9473 1.4180 1.5961 0.7183  -0.3175 -0.0353 326  ALA B C   
14841 O O   . ALA C 326  ? 2.9097 1.3628 1.5921 0.7354  -0.3052 0.0279  326  ALA B O   
14842 C CB  . ALA C 326  ? 3.0726 1.5407 1.5893 0.7479  -0.2816 -0.0699 326  ALA B CB  
14843 N N   . VAL C 327  ? 3.2161 1.7129 1.8928 0.7047  -0.3504 -0.0733 327  VAL B N   
14844 C CA  . VAL C 327  ? 3.2031 1.7086 1.9489 0.7104  -0.3759 -0.0455 327  VAL B CA  
14845 C C   . VAL C 327  ? 3.2922 1.8284 2.0322 0.7413  -0.3934 -0.0550 327  VAL B C   
14846 O O   . VAL C 327  ? 3.3847 1.9382 2.0698 0.7498  -0.3910 -0.0935 327  VAL B O   
14847 C CB  . VAL C 327  ? 3.0882 1.5983 1.8747 0.6707  -0.4017 -0.0825 327  VAL B CB  
14848 C CG1 . VAL C 327  ? 3.0547 1.5642 1.9130 0.6750  -0.4248 -0.0464 327  VAL B CG1 
14849 C CG2 . VAL C 327  ? 3.0053 1.4902 1.7854 0.6348  -0.3869 -0.0891 327  VAL B CG2 
14850 N N   . THR C 328  ? 3.4081 1.9504 2.2051 0.7580  -0.4113 -0.0179 328  THR B N   
14851 C CA  . THR C 328  ? 3.4803 2.0545 2.2906 0.7784  -0.4369 -0.0336 328  THR B CA  
14852 C C   . THR C 328  ? 3.4371 2.0107 2.3231 0.7659  -0.4639 -0.0210 328  THR B C   
14853 O O   . THR C 328  ? 3.3492 1.8997 2.2790 0.7658  -0.4603 0.0316  328  THR B O   
14854 C CB  . THR C 328  ? 3.5806 2.1621 2.3717 0.8241  -0.4269 0.0083  328  THR B CB  
14855 O OG1 . THR C 328  ? 3.6632 2.2406 2.3782 0.8335  -0.4014 -0.0063 328  THR B OG1 
14856 C CG2 . THR C 328  ? 3.6276 2.2435 2.4364 0.8435  -0.4555 -0.0081 328  THR B CG2 
14857 N N   . VAL C 329  ? 3.7325 2.3300 2.6330 0.7536  -0.4904 -0.0707 329  VAL B N   
14858 C CA  . VAL C 329  ? 3.7313 2.3275 2.6976 0.7401  -0.5171 -0.0689 329  VAL B CA  
14859 C C   . VAL C 329  ? 3.8941 2.5209 2.8830 0.7649  -0.5414 -0.0793 329  VAL B C   
14860 O O   . VAL C 329  ? 3.9855 2.6372 2.9667 0.7552  -0.5571 -0.1347 329  VAL B O   
14861 C CB  . VAL C 329  ? 3.6217 2.2145 2.5899 0.6966  -0.5263 -0.1233 329  VAL B CB  
14862 C CG1 . VAL C 329  ? 3.5482 2.1314 2.5812 0.6816  -0.5514 -0.1166 329  VAL B CG1 
14863 C CG2 . VAL C 329  ? 3.5594 2.1260 2.4977 0.6716  -0.5018 -0.1200 329  VAL B CG2 
14864 N N   . ILE C 330  ? 3.8294 2.4554 2.8473 0.7974  -0.5439 -0.0244 330  ILE B N   
14865 C CA  . ILE C 330  ? 3.9495 2.6025 2.9959 0.8223  -0.5675 -0.0265 330  ILE B CA  
14866 C C   . ILE C 330  ? 4.0062 2.6525 3.1184 0.8046  -0.5941 -0.0329 330  ILE B C   
14867 O O   . ILE C 330  ? 3.9262 2.5436 3.0786 0.7940  -0.5950 0.0060  330  ILE B O   
14868 C CB  . ILE C 330  ? 4.1329 2.7880 3.1837 0.8648  -0.5597 0.0355  330  ILE B CB  
14869 C CG1 . ILE C 330  ? 4.0799 2.7030 3.1748 0.8667  -0.5518 0.1023  330  ILE B CG1 
14870 C CG2 . ILE C 330  ? 4.1763 2.8360 3.1561 0.8820  -0.5336 0.0369  330  ILE B CG2 
14871 C CD1 . ILE C 330  ? 4.1260 2.7475 3.2111 0.9057  -0.5340 0.1641  330  ILE B CD1 
14872 N N   . GLU C 331  ? 4.5617 3.2337 3.6837 0.8006  -0.6153 -0.0826 331  GLU B N   
14873 C CA  . GLU C 331  ? 4.6574 3.3225 3.8346 0.7825  -0.6396 -0.0989 331  GLU B CA  
14874 C C   . GLU C 331  ? 4.7746 3.4307 4.0117 0.8058  -0.6550 -0.0455 331  GLU B C   
14875 O O   . GLU C 331  ? 4.8431 3.5180 4.0836 0.8411  -0.6574 -0.0189 331  GLU B O   
14876 C CB  . GLU C 331  ? 4.7106 3.4084 3.8825 0.7770  -0.6557 -0.1643 331  GLU B CB  
14877 C CG  . GLU C 331  ? 4.7239 3.4218 3.9561 0.7754  -0.6823 -0.1735 331  GLU B CG  
14878 C CD  . GLU C 331  ? 4.8023 3.5407 4.0368 0.7892  -0.6976 -0.2181 331  GLU B CD  
14879 O OE1 . GLU C 331  ? 4.8434 3.6104 4.0318 0.7981  -0.6893 -0.2424 331  GLU B OE1 
14880 O OE2 . GLU C 331  ? 4.8257 3.5665 4.1085 0.7912  -0.7183 -0.2284 331  GLU B OE2 
14881 N N   . SER C 332  ? 3.7122 2.3389 2.9959 0.7851  -0.6666 -0.0301 332  SER B N   
14882 C CA  . SER C 332  ? 3.8175 2.4304 3.1603 0.8038  -0.6815 0.0241  332  SER B CA  
14883 C C   . SER C 332  ? 3.9549 2.5896 3.3339 0.8229  -0.7064 0.0073  332  SER B C   
14884 O O   . SER C 332  ? 3.9909 2.6301 3.4027 0.8535  -0.7144 0.0519  332  SER B O   
14885 C CB  . SER C 332  ? 3.7818 2.3546 3.1631 0.7736  -0.6888 0.0452  332  SER B CB  
14886 O OG  . SER C 332  ? 3.8141 2.3743 3.2555 0.7894  -0.7076 0.0904  332  SER B OG  
14887 N N   . THR C 333  ? 3.9378 2.5856 3.3133 0.8048  -0.7181 -0.0556 333  THR B N   
14888 C CA  . THR C 333  ? 4.0504 2.7182 3.4625 0.8209  -0.7409 -0.0758 333  THR B CA  
14889 C C   . THR C 333  ? 4.1406 2.8498 3.5333 0.8575  -0.7398 -0.0759 333  THR B C   
14890 O O   . THR C 333  ? 4.1911 2.9079 3.6170 0.8884  -0.7502 -0.0372 333  THR B O   
14891 C CB  . THR C 333  ? 4.0674 2.7382 3.4810 0.7916  -0.7514 -0.1438 333  THR B CB  
14892 O OG1 . THR C 333  ? 4.1368 2.8501 3.5380 0.8080  -0.7569 -0.1861 333  THR B OG1 
14893 C CG2 . THR C 333  ? 4.0107 2.6666 3.3816 0.7544  -0.7349 -0.1730 333  THR B CG2 
14894 N N   . GLY C 334  ? 4.1710 2.9065 3.5095 0.8534  -0.7280 -0.1179 334  GLY B N   
14895 C CA  . GLY C 334  ? 4.2307 3.0069 3.5466 0.8837  -0.7297 -0.1261 334  GLY B CA  
14896 C C   . GLY C 334  ? 4.2168 2.9958 3.5081 0.9146  -0.7156 -0.0717 334  GLY B C   
14897 O O   . GLY C 334  ? 4.3242 3.1308 3.6172 0.9465  -0.7232 -0.0585 334  GLY B O   
14898 N N   . GLY C 335  ? 4.2066 2.9571 3.4754 0.9056  -0.6947 -0.0390 335  GLY B N   
14899 C CA  . GLY C 335  ? 4.1188 2.8695 3.3574 0.9336  -0.6765 0.0105  335  GLY B CA  
14900 C C   . GLY C 335  ? 4.0360 2.8043 3.1995 0.9327  -0.6584 -0.0220 335  GLY B C   
14901 O O   . GLY C 335  ? 4.0677 2.8419 3.1938 0.9582  -0.6437 0.0077  335  GLY B O   
14902 N N   . PHE C 336  ? 3.6220 2.3977 2.7626 0.9029  -0.6597 -0.0836 336  PHE B N   
14903 C CA  . PHE C 336  ? 3.5256 2.3150 2.5956 0.8957  -0.6438 -0.1205 336  PHE B CA  
14904 C C   . PHE C 336  ? 3.3933 2.1516 2.4229 0.8879  -0.6143 -0.0927 336  PHE B C   
14905 O O   . PHE C 336  ? 3.3390 2.0673 2.3980 0.8872  -0.6066 -0.0449 336  PHE B O   
14906 C CB  . PHE C 336  ? 3.4458 2.2467 2.5081 0.8616  -0.6514 -0.1900 336  PHE B CB  
14907 C CG  . PHE C 336  ? 3.4303 2.2711 2.5085 0.8698  -0.6743 -0.2310 336  PHE B CG  
14908 C CD1 . PHE C 336  ? 3.3587 2.2029 2.4871 0.8533  -0.6930 -0.2609 336  PHE B CD1 
14909 C CD2 . PHE C 336  ? 3.4931 2.3673 2.5347 0.8926  -0.6767 -0.2410 336  PHE B CD2 
14910 C CE1 . PHE C 336  ? 3.4037 2.2848 2.5499 0.8610  -0.7122 -0.2981 336  PHE B CE1 
14911 C CE2 . PHE C 336  ? 3.5465 2.4591 2.6065 0.8993  -0.6982 -0.2772 336  PHE B CE2 
14912 C CZ  . PHE C 336  ? 3.5065 2.4233 2.6206 0.8840  -0.7152 -0.3055 336  PHE B CZ  
14913 N N   . SER C 337  ? 3.8612 2.6265 2.8244 0.8810  -0.5983 -0.1236 337  SER B N   
14914 C CA  . SER C 337  ? 3.7423 2.4780 2.6630 0.8701  -0.5689 -0.1071 337  SER B CA  
14915 C C   . SER C 337  ? 3.7467 2.4893 2.6119 0.8436  -0.5604 -0.1671 337  SER B C   
14916 O O   . SER C 337  ? 3.8175 2.5908 2.6520 0.8487  -0.5697 -0.2070 337  SER B O   
14917 C CB  . SER C 337  ? 3.7424 2.4725 2.6287 0.9052  -0.5496 -0.0568 337  SER B CB  
14918 O OG  . SER C 337  ? 3.6478 2.3468 2.4969 0.8959  -0.5191 -0.0382 337  SER B OG  
14919 N N   . GLU C 338  ? 3.7003 2.4149 2.5550 0.8145  -0.5438 -0.1719 338  GLU B N   
14920 C CA  . GLU C 338  ? 3.7065 2.4226 2.5074 0.7882  -0.5324 -0.2236 338  GLU B CA  
14921 C C   . GLU C 338  ? 3.6300 2.3108 2.3954 0.7803  -0.5011 -0.1974 338  GLU B C   
14922 O O   . GLU C 338  ? 3.5462 2.1994 2.3445 0.7796  -0.4921 -0.1503 338  GLU B O   
14923 C CB  . GLU C 338  ? 3.7057 2.4286 2.5342 0.7517  -0.5483 -0.2744 338  GLU B CB  
14924 C CG  . GLU C 338  ? 3.8017 2.5476 2.5832 0.7333  -0.5490 -0.3388 338  GLU B CG  
14925 C CD  . GLU C 338  ? 3.9562 2.7402 2.7184 0.7592  -0.5629 -0.3567 338  GLU B CD  
14926 O OE1 . GLU C 338  ? 3.9966 2.7976 2.8015 0.7819  -0.5817 -0.3384 338  GLU B OE1 
14927 O OE2 . GLU C 338  ? 4.0383 2.8348 2.7428 0.7563  -0.5558 -0.3885 338  GLU B OE2 
14928 N N   . GLU C 339  ? 4.1354 2.8168 2.8343 0.7746  -0.4846 -0.2269 339  GLU B N   
14929 C CA  . GLU C 339  ? 4.1163 2.7639 2.7770 0.7697  -0.4527 -0.2037 339  GLU B CA  
14930 C C   . GLU C 339  ? 4.0038 2.6459 2.6319 0.7319  -0.4454 -0.2560 339  GLU B C   
14931 O O   . GLU C 339  ? 3.9832 2.6516 2.6012 0.7162  -0.4621 -0.3116 339  GLU B O   
14932 C CB  . GLU C 339  ? 4.3019 2.9473 2.9061 0.8038  -0.4340 -0.1796 339  GLU B CB  
14933 C CG  . GLU C 339  ? 4.4295 3.0745 3.0664 0.8410  -0.4358 -0.1181 339  GLU B CG  
14934 C CD  . GLU C 339  ? 4.6603 3.3144 3.2417 0.8762  -0.4264 -0.1056 339  GLU B CD  
14935 O OE1 . GLU C 339  ? 4.7666 3.4201 3.2793 0.8714  -0.4147 -0.1403 339  GLU B OE1 
14936 O OE2 . GLU C 339  ? 4.7258 3.3865 3.3313 0.9081  -0.4314 -0.0609 339  GLU B OE2 
14937 N N   . ALA C 340  ? 3.2653 1.8738 1.8802 0.7173  -0.4204 -0.2363 340  ALA B N   
14938 C CA  . ALA C 340  ? 3.2275 1.8264 1.8153 0.6800  -0.4115 -0.2799 340  ALA B CA  
14939 C C   . ALA C 340  ? 3.1708 1.7315 1.7301 0.6767  -0.3776 -0.2479 340  ALA B C   
14940 O O   . ALA C 340  ? 3.1212 1.6593 1.7120 0.6882  -0.3660 -0.1908 340  ALA B O   
14941 C CB  . ALA C 340  ? 3.1828 1.7861 1.8241 0.6466  -0.4318 -0.3029 340  ALA B CB  
14942 N N   . GLU C 341  ? 3.4400 1.9933 1.9412 0.6612  -0.3615 -0.2838 341  GLU B N   
14943 C CA  . GLU C 341  ? 3.4495 1.9664 1.9176 0.6626  -0.3270 -0.2544 341  GLU B CA  
14944 C C   . GLU C 341  ? 3.1021 1.6064 1.5439 0.6248  -0.3168 -0.2949 341  GLU B C   
14945 O O   . GLU C 341  ? 3.1103 1.6368 1.5381 0.6024  -0.3331 -0.3527 341  GLU B O   
14946 C CB  . GLU C 341  ? 3.5698 2.0816 1.9735 0.6962  -0.3078 -0.2439 341  GLU B CB  
14947 C CG  . GLU C 341  ? 3.6849 2.2138 2.0236 0.6884  -0.3128 -0.3060 341  GLU B CG  
14948 C CD  . GLU C 341  ? 3.7736 2.2923 2.0428 0.7209  -0.2935 -0.2943 341  GLU B CD  
14949 O OE1 . GLU C 341  ? 3.7973 2.2960 2.0682 0.7504  -0.2739 -0.2380 341  GLU B OE1 
14950 O OE2 . GLU C 341  ? 3.8079 2.3381 2.0199 0.7167  -0.2979 -0.3409 341  GLU B OE2 
14951 N N   . ILE C 342  ? 3.2417 1.7112 1.6788 0.6184  -0.2891 -0.2623 342  ILE B N   
14952 C CA  . ILE C 342  ? 3.1983 1.6502 1.6024 0.5869  -0.2730 -0.2935 342  ILE B CA  
14953 C C   . ILE C 342  ? 3.2746 1.6974 1.6176 0.6053  -0.2375 -0.2761 342  ILE B C   
14954 O O   . ILE C 342  ? 3.2778 1.6783 1.6293 0.6304  -0.2164 -0.2188 342  ILE B O   
14955 C CB  . ILE C 342  ? 3.0342 1.4684 1.4892 0.5558  -0.2723 -0.2752 342  ILE B CB  
14956 C CG1 . ILE C 342  ? 3.0009 1.4600 1.5137 0.5380  -0.3071 -0.2925 342  ILE B CG1 
14957 C CG2 . ILE C 342  ? 2.9659 1.3833 1.3855 0.5228  -0.2560 -0.3088 342  ILE B CG2 
14958 C CD1 . ILE C 342  ? 2.9116 1.3540 1.4726 0.5047  -0.3108 -0.2780 342  ILE B CD1 
14959 N N   . PRO C 343  ? 3.5042 1.9255 1.7856 0.5919  -0.2300 -0.3255 343  PRO B N   
14960 C CA  . PRO C 343  ? 3.5527 1.9484 1.7648 0.6138  -0.1994 -0.3171 343  PRO B CA  
14961 C C   . PRO C 343  ? 3.5180 1.8749 1.7435 0.6194  -0.1666 -0.2621 343  PRO B C   
14962 O O   . PRO C 343  ? 3.5896 1.9315 1.8188 0.6527  -0.1487 -0.2083 343  PRO B O   
14963 C CB  . PRO C 343  ? 3.5214 1.9151 1.6825 0.5834  -0.1970 -0.3783 343  PRO B CB  
14964 C CG  . PRO C 343  ? 3.4753 1.9024 1.6749 0.5514  -0.2297 -0.4224 343  PRO B CG  
14965 C CD  . PRO C 343  ? 3.4458 1.8801 1.7229 0.5509  -0.2438 -0.3847 343  PRO B CD  
14966 N N   . GLY C 344  ? 3.9013 2.2432 2.1362 0.5848  -0.1591 -0.2765 344  GLY B N   
14967 C CA  . GLY C 344  ? 3.8451 2.1511 2.0966 0.5826  -0.1292 -0.2295 344  GLY B CA  
14968 C C   . GLY C 344  ? 3.7095 2.0138 2.0053 0.5397  -0.1385 -0.2407 344  GLY B C   
14969 O O   . GLY C 344  ? 3.7070 2.0367 2.0165 0.5116  -0.1664 -0.2873 344  GLY B O   
14970 N N   . ILE C 345  ? 2.6983 0.9719 1.0158 0.5353  -0.1137 -0.1962 345  ILE B N   
14971 C CA  . ILE C 345  ? 2.6189 0.8866 0.9835 0.4971  -0.1201 -0.1927 345  ILE B CA  
14972 C C   . ILE C 345  ? 2.6124 0.8409 0.9611 0.4973  -0.0813 -0.1602 345  ILE B C   
14973 O O   . ILE C 345  ? 2.6118 0.8217 0.9927 0.5161  -0.0629 -0.0973 345  ILE B O   
14974 C CB  . ILE C 345  ? 2.5454 0.8249 0.9878 0.4974  -0.1426 -0.1505 345  ILE B CB  
14975 C CG1 . ILE C 345  ? 2.6256 0.9416 1.0862 0.4849  -0.1822 -0.1946 345  ILE B CG1 
14976 C CG2 . ILE C 345  ? 2.5147 0.7765 1.0060 0.4673  -0.1397 -0.1218 345  ILE B CG2 
14977 C CD1 . ILE C 345  ? 2.5555 0.8794 1.0894 0.4781  -0.2060 -0.1615 345  ILE B CD1 
14978 N N   . LYS C 346  ? 3.2651 1.4813 1.5632 0.4777  -0.0680 -0.2031 346  LYS B N   
14979 C CA  . LYS C 346  ? 3.1452 1.3226 1.4172 0.4798  -0.0288 -0.1801 346  LYS B CA  
14980 C C   . LYS C 346  ? 3.0564 1.2183 1.3939 0.4631  -0.0219 -0.1283 346  LYS B C   
14981 O O   . LYS C 346  ? 3.0678 1.2391 1.4376 0.4249  -0.0415 -0.1472 346  LYS B O   
14982 C CB  . LYS C 346  ? 3.1565 1.3278 1.3734 0.4519  -0.0243 -0.2422 346  LYS B CB  
14983 C CG  . LYS C 346  ? 3.2259 1.3551 1.3989 0.4573  0.0176  -0.2302 346  LYS B CG  
14984 C CD  . LYS C 346  ? 3.2198 1.3419 1.3559 0.4197  0.0190  -0.2868 346  LYS B CD  
14985 C CE  . LYS C 346  ? 3.2803 1.3984 1.3324 0.4291  0.0250  -0.3398 346  LYS B CE  
14986 N NZ  . LYS C 346  ? 3.2766 1.3699 1.2861 0.4023  0.0426  -0.3755 346  LYS B NZ  
14987 N N   . TYR C 347  ? 2.8946 1.0343 1.2539 0.4909  0.0044  -0.0620 347  TYR B N   
14988 C CA  . TYR C 347  ? 2.8330 0.9548 1.2511 0.4749  0.0150  -0.0100 347  TYR B CA  
14989 C C   . TYR C 347  ? 2.8342 0.9311 1.2229 0.4501  0.0376  -0.0305 347  TYR B C   
14990 O O   . TYR C 347  ? 2.8584 0.9421 1.1796 0.4593  0.0570  -0.0650 347  TYR B O   
14991 C CB  . TYR C 347  ? 2.8276 0.9276 1.2640 0.5127  0.0465  0.0626  347  TYR B CB  
14992 C CG  . TYR C 347  ? 2.8002 0.9172 1.2997 0.5287  0.0275  0.1115  347  TYR B CG  
14993 C CD1 . TYR C 347  ? 2.7618 0.8639 1.3201 0.5374  0.0426  0.1851  347  TYR B CD1 
14994 C CD2 . TYR C 347  ? 2.8419 0.9900 1.3442 0.5353  -0.0058 0.0856  347  TYR B CD2 
14995 C CE1 . TYR C 347  ? 2.7573 0.8742 1.3740 0.5520  0.0245  0.2311  347  TYR B CE1 
14996 C CE2 . TYR C 347  ? 2.8343 0.9964 1.3938 0.5502  -0.0234 0.1299  347  TYR B CE2 
14997 C CZ  . TYR C 347  ? 2.8043 0.9505 1.4206 0.5579  -0.0088 0.2024  347  TYR B CZ  
14998 O OH  . TYR C 347  ? 2.7996 0.9599 1.4746 0.5716  -0.0285 0.2465  347  TYR B OH  
14999 N N   . VAL C 348  ? 2.7677 0.8555 1.2051 0.4197  0.0367  -0.0068 348  VAL B N   
15000 C CA  . VAL C 348  ? 2.8262 0.8858 1.2395 0.4006  0.0640  -0.0148 348  VAL B CA  
15001 C C   . VAL C 348  ? 2.7981 0.8360 1.2683 0.3968  0.0831  0.0532  348  VAL B C   
15002 O O   . VAL C 348  ? 2.7617 0.8097 1.2982 0.3937  0.0663  0.0986  348  VAL B O   
15003 C CB  . VAL C 348  ? 2.6613 0.7322 1.0574 0.3542  0.0433  -0.0797 348  VAL B CB  
15004 C CG1 . VAL C 348  ? 2.6749 0.7153 1.0571 0.3342  0.0716  -0.0775 348  VAL B CG1 
15005 C CG2 . VAL C 348  ? 2.6811 0.7693 1.0132 0.3577  0.0312  -0.1487 348  VAL B CG2 
15006 N N   . LEU C 349  ? 2.8490 0.8557 1.2931 0.3971  0.1189  0.0609  349  LEU B N   
15007 C CA  . LEU C 349  ? 2.8169 0.8024 1.3134 0.3922  0.1392  0.1236  349  LEU B CA  
15008 C C   . LEU C 349  ? 2.7151 0.7042 1.2402 0.3410  0.1205  0.1051  349  LEU B C   
15009 O O   . LEU C 349  ? 2.6223 0.6196 1.2140 0.3218  0.1016  0.1431  349  LEU B O   
15010 C CB  . LEU C 349  ? 2.9354 0.8841 1.3883 0.4187  0.1887  0.1399  349  LEU B CB  
15011 C CG  . LEU C 349  ? 2.9336 0.8574 1.4380 0.4225  0.2182  0.2110  349  LEU B CG  
15012 C CD1 . LEU C 349  ? 2.9488 0.8450 1.4246 0.3995  0.2425  0.1891  349  LEU B CD1 
15013 C CD2 . LEU C 349  ? 2.8580 0.8022 1.4506 0.4003  0.1874  0.2557  349  LEU B CD2 
15014 N N   . SER C 350  ? 2.4129 1.1750 1.5603 0.6347  0.2063  0.2599  350  SER B N   
15015 C CA  . SER C 350  ? 2.3320 1.1383 1.5326 0.6307  0.2050  0.2579  350  SER B CA  
15016 C C   . SER C 350  ? 2.3408 1.2074 1.5144 0.6195  0.1778  0.2230  350  SER B C   
15017 O O   . SER C 350  ? 2.4348 1.2919 1.5628 0.5963  0.1965  0.1995  350  SER B O   
15018 C CB  . SER C 350  ? 2.3317 1.0976 1.5566 0.6107  0.2622  0.2681  350  SER B CB  
15019 O OG  . SER C 350  ? 2.2833 1.0910 1.5556 0.6049  0.2642  0.2647  350  SER B OG  
15020 N N   . PRO C 351  ? 2.2074 1.1372 1.4111 0.6363  0.1339  0.2200  351  PRO B N   
15021 C CA  . PRO C 351  ? 2.2399 1.2348 1.4171 0.6349  0.0937  0.1903  351  PRO B CA  
15022 C C   . PRO C 351  ? 2.2980 1.3113 1.4636 0.6056  0.1166  0.1663  351  PRO B C   
15023 O O   . PRO C 351  ? 2.3596 1.4262 1.5027 0.6005  0.0881  0.1408  351  PRO B O   
15024 C CB  . PRO C 351  ? 2.1425 1.1922 1.3757 0.6605  0.0548  0.2022  351  PRO B CB  
15025 C CG  . PRO C 351  ? 2.0954 1.1029 1.3706 0.6791  0.0656  0.2367  351  PRO B CG  
15026 C CD  . PRO C 351  ? 2.1181 1.0613 1.3918 0.6578  0.1245  0.2472  351  PRO B CD  
15027 N N   . TYR C 352  ? 2.3319 1.2998 1.5130 0.5863  0.1685  0.1750  352  TYR B N   
15028 C CA  . TYR C 352  ? 2.3766 1.3521 1.5513 0.5568  0.1965  0.1550  352  TYR B CA  
15029 C C   . TYR C 352  ? 2.4408 1.3517 1.5651 0.5334  0.2392  0.1460  352  TYR B C   
15030 O O   . TYR C 352  ? 2.4179 1.2718 1.5312 0.5398  0.2598  0.1638  352  TYR B O   
15031 C CB  . TYR C 352  ? 2.3423 1.3209 1.5851 0.5530  0.2253  0.1732  352  TYR B CB  
15032 C CG  . TYR C 352  ? 2.2858 1.3242 1.5907 0.5746  0.1944  0.1857  352  TYR B CG  
15033 C CD1 . TYR C 352  ? 2.2989 1.3992 1.6228 0.5666  0.1810  0.1698  352  TYR B CD1 
15034 C CD2 . TYR C 352  ? 2.2356 1.2661 1.5833 0.6019  0.1830  0.2144  352  TYR B CD2 
15035 C CE1 . TYR C 352  ? 2.2396 1.3940 1.6186 0.5865  0.1554  0.1809  352  TYR B CE1 
15036 C CE2 . TYR C 352  ? 2.1925 1.2759 1.5958 0.6216  0.1566  0.2246  352  TYR B CE2 
15037 C CZ  . TYR C 352  ? 2.1930 1.3391 1.6110 0.6144  0.1429  0.2076  352  TYR B CZ  
15038 O OH  . TYR C 352  ? 2.1367 1.3395 1.6093 0.6354  0.1159  0.2172  352  TYR B OH  
15039 N N   . LYS C 353  ? 2.1815 1.1009 1.2802 0.5064  0.2548  0.1200  353  LYS B N   
15040 C CA  . LYS C 353  ? 2.2803 1.1429 1.3288 0.4842  0.2922  0.1077  353  LYS B CA  
15041 C C   . LYS C 353  ? 2.2911 1.1599 1.3467 0.4547  0.3207  0.0904  353  LYS B C   
15042 O O   . LYS C 353  ? 2.2447 1.1629 1.2861 0.4429  0.2989  0.0647  353  LYS B O   
15043 C CB  . LYS C 353  ? 2.3365 1.2045 1.3134 0.4847  0.2647  0.0832  353  LYS B CB  
15044 C CG  . LYS C 353  ? 2.4294 1.3729 1.3951 0.4877  0.2155  0.0595  353  LYS B CG  
15045 C CD  . LYS C 353  ? 2.5351 1.4894 1.4568 0.5086  0.1745  0.0546  353  LYS B CD  
15046 C CE  . LYS C 353  ? 2.6727 1.6261 1.5206 0.4928  0.1687  0.0217  353  LYS B CE  
15047 N NZ  . LYS C 353  ? 2.7179 1.6855 1.5254 0.5151  0.1274  0.0180  353  LYS B NZ  
15048 N N   . LEU C 354  ? 2.3389 1.1572 1.4166 0.4425  0.3698  0.1048  354  LEU B N   
15049 C CA  . LEU C 354  ? 2.3613 1.1808 1.4501 0.4145  0.3997  0.0907  354  LEU B CA  
15050 C C   . LEU C 354  ? 2.4421 1.2416 1.4621 0.3916  0.4074  0.0589  354  LEU B C   
15051 O O   . LEU C 354  ? 2.4993 1.2700 1.4684 0.3982  0.4012  0.0539  354  LEU B O   
15052 C CB  . LEU C 354  ? 2.3553 1.1175 1.4781 0.4085  0.4523  0.1147  354  LEU B CB  
15053 C CG  . LEU C 354  ? 2.2608 1.0075 1.4387 0.4327  0.4597  0.1527  354  LEU B CG  
15054 C CD1 . LEU C 354  ? 2.2154 0.9967 1.4648 0.4326  0.4678  0.1660  354  LEU B CD1 
15055 C CD2 . LEU C 354  ? 2.2208 0.9854 1.3946 0.4630  0.4167  0.1648  354  LEU B CD2 
15056 N N   . ASN C 355  ? 2.3932 1.2072 1.4123 0.3650  0.4213  0.0375  355  ASN B N   
15057 C CA  . ASN C 355  ? 2.5117 1.2882 1.4727 0.3400  0.4437  0.0112  355  ASN B CA  
15058 C C   . ASN C 355  ? 2.5141 1.2993 1.4946 0.3111  0.4676  -0.0035 355  ASN B C   
15059 O O   . ASN C 355  ? 2.4444 1.2919 1.4461 0.3051  0.4425  -0.0158 355  ASN B O   
15060 C CB  . ASN C 355  ? 2.6947 1.4972 1.5929 0.3411  0.4058  -0.0169 355  ASN B CB  
15061 C CG  . ASN C 355  ? 2.7545 1.6373 1.6635 0.3385  0.3638  -0.0356 355  ASN B CG  
15062 O OD1 . ASN C 355  ? 2.7340 1.6635 1.6589 0.3617  0.3236  -0.0272 355  ASN B OD1 
15063 N ND2 . ASN C 355  ? 2.8344 1.7341 1.7339 0.3104  0.3718  -0.0614 355  ASN B ND2 
15064 N N   . LEU C 356  ? 2.2300 0.9526 1.2040 0.2939  0.5163  -0.0012 356  LEU B N   
15065 C CA  . LEU C 356  ? 2.2259 0.9484 1.2186 0.2653  0.5436  -0.0140 356  LEU B CA  
15066 C C   . LEU C 356  ? 2.2957 1.0760 1.2680 0.2483  0.5122  -0.0472 356  LEU B C   
15067 O O   . LEU C 356  ? 2.3769 1.1781 1.3016 0.2538  0.4787  -0.0658 356  LEU B O   
15068 C CB  . LEU C 356  ? 2.3251 0.9710 1.2810 0.2471  0.5903  -0.0206 356  LEU B CB  
15069 C CG  . LEU C 356  ? 2.2639 0.8508 1.2462 0.2588  0.6299  0.0126  356  LEU B CG  
15070 C CD1 . LEU C 356  ? 2.3352 0.8499 1.2766 0.2401  0.6743  0.0027  356  LEU B CD1 
15071 C CD2 . LEU C 356  ? 2.1984 0.8113 1.2548 0.2582  0.6417  0.0321  356  LEU B CD2 
15072 N N   . VAL C 357  ? 2.1662 0.9735 1.1740 0.2275  0.5225  -0.0547 357  VAL B N   
15073 C CA  . VAL C 357  ? 2.2383 1.1034 1.2294 0.2105  0.4924  -0.0855 357  VAL B CA  
15074 C C   . VAL C 357  ? 2.3625 1.2199 1.3604 0.1760  0.5199  -0.1040 357  VAL B C   
15075 O O   . VAL C 357  ? 2.2469 1.1064 1.2995 0.1694  0.5437  -0.0886 357  VAL B O   
15076 C CB  . VAL C 357  ? 2.1996 1.1466 1.2349 0.2269  0.4510  -0.0774 357  VAL B CB  
15077 C CG1 . VAL C 357  ? 2.1824 1.1876 1.1940 0.2096  0.4194  -0.1096 357  VAL B CG1 
15078 C CG2 . VAL C 357  ? 2.1509 1.1097 1.1822 0.2613  0.4199  -0.0599 357  VAL B CG2 
15079 N N   . ALA C 358  ? 2.7093 1.5593 1.6525 0.1544  0.5157  -0.1373 358  ALA B N   
15080 C CA  . ALA C 358  ? 2.8058 1.6402 1.7510 0.1203  0.5433  -0.1564 358  ALA B CA  
15081 C C   . ALA C 358  ? 2.7712 1.5485 1.7551 0.1136  0.5956  -0.1341 358  ALA B C   
15082 O O   . ALA C 358  ? 2.7015 1.4962 1.7327 0.0976  0.6112  -0.1307 358  ALA B O   
15083 C CB  . ALA C 358  ? 2.8468 1.7592 1.8242 0.1077  0.5158  -0.1688 358  ALA B CB  
15084 N N   . THR C 359  ? 2.5148 1.2246 1.4776 0.1261  0.6225  -0.1188 359  THR B N   
15085 C CA  . THR C 359  ? 2.4992 1.1498 1.4935 0.1236  0.6727  -0.0953 359  THR B CA  
15086 C C   . THR C 359  ? 2.5221 1.0866 1.4647 0.1169  0.7103  -0.1007 359  THR B C   
15087 O O   . THR C 359  ? 2.4450 0.9690 1.3799 0.1381  0.7233  -0.0785 359  THR B O   
15088 C CB  . THR C 359  ? 2.4317 1.0910 1.4784 0.1538  0.6723  -0.0561 359  THR B CB  
15089 O OG1 . THR C 359  ? 2.4272 1.0972 1.4466 0.1804  0.6400  -0.0501 359  THR B OG1 
15090 C CG2 . THR C 359  ? 2.3536 1.0831 1.4657 0.1562  0.6539  -0.0461 359  THR B CG2 
15091 N N   . PRO C 360  ? 2.9954 1.5319 1.9048 0.0878  0.7287  -0.1292 360  PRO B N   
15092 C CA  . PRO C 360  ? 3.0562 1.5143 1.9111 0.0793  0.7623  -0.1400 360  PRO B CA  
15093 C C   . PRO C 360  ? 3.0165 1.4124 1.8870 0.0959  0.8021  -0.1066 360  PRO B C   
15094 O O   . PRO C 360  ? 2.8582 1.2632 1.7904 0.1012  0.8173  -0.0801 360  PRO B O   
15095 C CB  . PRO C 360  ? 3.1285 1.5729 1.9861 0.0446  0.7853  -0.1631 360  PRO B CB  
15096 C CG  . PRO C 360  ? 3.1290 1.6532 2.0114 0.0330  0.7477  -0.1790 360  PRO B CG  
15097 C CD  . PRO C 360  ? 3.0246 1.6057 1.9522 0.0606  0.7186  -0.1521 360  PRO B CD  
15098 N N   . LEU C 361  ? 2.6959 1.0318 1.5130 0.1040  0.8191  -0.1075 361  LEU B N   
15099 C CA  . LEU C 361  ? 2.4925 0.7688 1.3212 0.1207  0.8568  -0.0750 361  LEU B CA  
15100 C C   . LEU C 361  ? 2.6603 0.8620 1.4704 0.1033  0.9083  -0.0793 361  LEU B C   
15101 O O   . LEU C 361  ? 2.6711 0.8129 1.4507 0.1146  0.9347  -0.0676 361  LEU B O   
15102 C CB  . LEU C 361  ? 2.6548 0.9180 1.4489 0.1489  0.8412  -0.0621 361  LEU B CB  
15103 C CG  . LEU C 361  ? 2.5510 0.8775 1.3733 0.1725  0.7965  -0.0472 361  LEU B CG  
15104 C CD1 . LEU C 361  ? 2.5240 0.9225 1.3385 0.1628  0.7498  -0.0760 361  LEU B CD1 
15105 C CD2 . LEU C 361  ? 2.5747 0.8742 1.3619 0.1992  0.7894  -0.0321 361  LEU B CD2 
15106 N N   . PHE C 362  ? 3.5879 1.7958 2.4176 0.0760  0.9213  -0.0958 362  PHE B N   
15107 C CA  . PHE C 362  ? 3.7068 1.8518 2.5377 0.0590  0.9708  -0.0953 362  PHE B CA  
15108 C C   . PHE C 362  ? 3.5562 1.7290 2.4566 0.0452  0.9831  -0.0847 362  PHE B C   
15109 O O   . PHE C 362  ? 3.5135 1.7404 2.4342 0.0282  0.9594  -0.1028 362  PHE B O   
15110 C CB  . PHE C 362  ? 3.9870 2.0986 2.7559 0.0355  0.9772  -0.1340 362  PHE B CB  
15111 C CG  . PHE C 362  ? 4.1801 2.2898 2.8839 0.0468  0.9515  -0.1513 362  PHE B CG  
15112 C CD1 . PHE C 362  ? 4.2572 2.4223 2.9391 0.0390  0.9080  -0.1797 362  PHE B CD1 
15113 C CD2 . PHE C 362  ? 4.2510 2.3070 2.9173 0.0669  0.9699  -0.1372 362  PHE B CD2 
15114 C CE1 . PHE C 362  ? 4.3575 2.5224 2.9794 0.0507  0.8841  -0.1951 362  PHE B CE1 
15115 C CE2 . PHE C 362  ? 4.3422 2.3978 2.9492 0.0788  0.9464  -0.1517 362  PHE B CE2 
15116 C CZ  . PHE C 362  ? 4.3916 2.5015 2.9757 0.0709  0.9033  -0.1811 362  PHE B CZ  
15117 N N   . LEU C 363  ? 2.7331 0.8697 1.6708 0.0535  1.0206  -0.0541 363  LEU B N   
15118 C CA  . LEU C 363  ? 2.6400 0.7955 1.6428 0.0426  1.0380  -0.0411 363  LEU B CA  
15119 C C   . LEU C 363  ? 2.6693 0.7686 1.6567 0.0157  1.0787  -0.0569 363  LEU B C   
15120 O O   . LEU C 363  ? 2.6850 0.7159 1.6502 0.0197  1.1165  -0.0472 363  LEU B O   
15121 C CB  . LEU C 363  ? 2.5122 0.6591 1.5630 0.0683  1.0560  0.0016  363  LEU B CB  
15122 C CG  . LEU C 363  ? 2.5553 0.6372 1.5656 0.0870  1.0784  0.0168  363  LEU B CG  
15123 C CD1 . LEU C 363  ? 2.6117 0.6228 1.6231 0.0766  1.1339  0.0256  363  LEU B CD1 
15124 C CD2 . LEU C 363  ? 2.4515 0.5540 1.4920 0.1194  1.0639  0.0510  363  LEU B CD2 
15125 N N   . LYS C 364  ? 2.8154 0.9430 1.8119 -0.0115 1.0698  -0.0824 364  LYS B N   
15126 C CA  . LYS C 364  ? 2.8172 0.8992 1.8178 -0.0374 1.1090  -0.0924 364  LYS B CA  
15127 C C   . LYS C 364  ? 2.7904 0.8564 1.8528 -0.0271 1.1452  -0.0545 364  LYS B C   
15128 O O   . LYS C 364  ? 2.6766 0.7877 1.7861 -0.0067 1.1301  -0.0282 364  LYS B O   
15129 C CB  . LYS C 364  ? 2.8843 1.0113 1.8972 -0.0672 1.0892  -0.1218 364  LYS B CB  
15130 C CG  . LYS C 364  ? 2.9957 1.1545 1.9566 -0.0742 1.0467  -0.1562 364  LYS B CG  
15131 C CD  . LYS C 364  ? 2.9537 1.1672 1.9154 -0.0469 1.0049  -0.1446 364  LYS B CD  
15132 C CE  . LYS C 364  ? 3.0300 1.2909 1.9555 -0.0574 0.9608  -0.1782 364  LYS B CE  
15133 N NZ  . LYS C 364  ? 3.1690 1.3819 2.0417 -0.0833 0.9759  -0.2125 364  LYS B NZ  
15134 N N   . PRO C 365  ? 3.4676 1.4676 2.5276 -0.0392 1.1931  -0.0512 365  PRO B N   
15135 C CA  . PRO C 365  ? 3.4228 1.4052 2.5385 -0.0286 1.2293  -0.0150 365  PRO B CA  
15136 C C   . PRO C 365  ? 3.4365 1.4634 2.6194 -0.0437 1.2322  -0.0097 365  PRO B C   
15137 O O   . PRO C 365  ? 3.5168 1.5716 2.6995 -0.0687 1.2170  -0.0365 365  PRO B O   
15138 C CB  . PRO C 365  ? 3.4844 1.3773 2.5635 -0.0367 1.2781  -0.0173 365  PRO B CB  
15139 C CG  . PRO C 365  ? 3.5661 1.4290 2.5682 -0.0429 1.2654  -0.0487 365  PRO B CG  
15140 C CD  . PRO C 365  ? 3.5793 1.5100 2.5774 -0.0562 1.2171  -0.0769 365  PRO B CD  
15141 N N   . GLY C 366  ? 3.2465 1.2801 2.4873 -0.0283 1.2526  0.0252  366  GLY B N   
15142 C CA  . GLY C 366  ? 3.3119 1.3906 2.6201 -0.0388 1.2561  0.0341  366  GLY B CA  
15143 C C   . GLY C 366  ? 3.1819 1.3510 2.5201 -0.0330 1.2060  0.0307  366  GLY B C   
15144 O O   . GLY C 366  ? 3.1147 1.3312 2.5153 -0.0210 1.2017  0.0544  366  GLY B O   
15145 N N   . ILE C 367  ? 3.1441 1.3381 2.4376 -0.0404 1.1680  0.0015  367  ILE B N   
15146 C CA  . ILE C 367  ? 3.0486 1.3283 2.3647 -0.0325 1.1181  -0.0019 367  ILE B CA  
15147 C C   . ILE C 367  ? 2.9273 1.2321 2.2628 0.0037  1.1001  0.0274  367  ILE B C   
15148 O O   . ILE C 367  ? 2.9214 1.1753 2.2346 0.0211  1.1188  0.0432  367  ILE B O   
15149 C CB  . ILE C 367  ? 3.1317 1.4313 2.3924 -0.0486 1.0817  -0.0408 367  ILE B CB  
15150 C CG1 . ILE C 367  ? 3.1960 1.5013 2.4638 -0.0841 1.0893  -0.0660 367  ILE B CG1 
15151 C CG2 . ILE C 367  ? 3.0685 1.4468 2.3375 -0.0316 1.0284  -0.0413 367  ILE B CG2 
15152 C CD1 . ILE C 367  ? 3.2715 1.6039 2.4933 -0.1019 1.0530  -0.1039 367  ILE B CD1 
15153 N N   . PRO C 368  ? 2.4563 0.8395 1.8370 0.0156  1.0652  0.0365  368  PRO B N   
15154 C CA  . PRO C 368  ? 2.3511 0.7658 1.7467 0.0493  1.0391  0.0593  368  PRO B CA  
15155 C C   . PRO C 368  ? 2.3258 0.7615 1.6673 0.0557  0.9954  0.0382  368  PRO B C   
15156 O O   . PRO C 368  ? 2.3977 0.8683 1.7163 0.0383  0.9678  0.0090  368  PRO B O   
15157 C CB  . PRO C 368  ? 2.2305 0.7234 1.6964 0.0569  1.0192  0.0739  368  PRO B CB  
15158 C CG  . PRO C 368  ? 2.2899 0.7881 1.7797 0.0278  1.0394  0.0620  368  PRO B CG  
15159 C CD  . PRO C 368  ? 2.4278 0.8726 1.8557 -0.0002 1.0529  0.0302  368  PRO B CD  
15160 N N   . TYR C 369  ? 2.4296 0.8443 1.7522 0.0815  0.9896  0.0543  369  TYR B N   
15161 C CA  . TYR C 369  ? 2.4366 0.8649 1.7075 0.0916  0.9512  0.0386  369  TYR B CA  
15162 C C   . TYR C 369  ? 2.3323 0.8436 1.6352 0.1118  0.9013  0.0456  369  TYR B C   
15163 O O   . TYR C 369  ? 2.3189 0.8524 1.6720 0.1348  0.8990  0.0751  369  TYR B O   
15164 C CB  . TYR C 369  ? 2.4217 0.7837 1.6555 0.1085  0.9713  0.0527  369  TYR B CB  
15165 C CG  . TYR C 369  ? 2.5109 0.8715 1.6816 0.1162  0.9399  0.0347  369  TYR B CG  
15166 C CD1 . TYR C 369  ? 2.6491 1.0194 1.7710 0.0948  0.9214  -0.0027 369  TYR B CD1 
15167 C CD2 . TYR C 369  ? 2.5108 0.8599 1.6707 0.1448  0.9290  0.0551  369  TYR B CD2 
15168 C CE1 . TYR C 369  ? 2.6893 1.0600 1.7532 0.1027  0.8928  -0.0192 369  TYR B CE1 
15169 C CE2 . TYR C 369  ? 2.5708 0.9199 1.6743 0.1526  0.9005  0.0397  369  TYR B CE2 
15170 C CZ  . TYR C 369  ? 2.6772 1.0374 1.7322 0.1320  0.8827  0.0025  369  TYR B CZ  
15171 O OH  . TYR C 369  ? 2.7538 1.1154 1.7519 0.1408  0.8544  -0.0130 369  TYR B OH  
15172 N N   . PRO C 370  ? 2.3269 0.8855 1.6014 0.1027  0.8612  0.0175  370  PRO B N   
15173 C CA  . PRO C 370  ? 2.2656 0.9058 1.5599 0.1186  0.8099  0.0171  370  PRO B CA  
15174 C C   . PRO C 370  ? 2.1910 0.8345 1.4509 0.1451  0.7781  0.0214  370  PRO B C   
15175 O O   . PRO C 370  ? 2.2558 0.8938 1.4570 0.1381  0.7590  -0.0040 370  PRO B O   
15176 C CB  . PRO C 370  ? 2.3427 1.0195 1.6100 0.0921  0.7871  -0.0190 370  PRO B CB  
15177 C CG  . PRO C 370  ? 2.2972 0.9143 1.5429 0.0616  0.8288  -0.0350 370  PRO B CG  
15178 C CD  . PRO C 370  ? 2.4401 0.9777 1.6669 0.0716  0.8672  -0.0178 370  PRO B CD  
15179 N N   . ILE C 371  ? 2.4527 1.1076 1.7477 0.1747  0.7701  0.0514  371  ILE B N   
15180 C CA  . ILE C 371  ? 2.4345 1.0912 1.6969 0.1995  0.7390  0.0555  371  ILE B CA  
15181 C C   . ILE C 371  ? 2.4141 1.1509 1.6957 0.2198  0.6842  0.0562  371  ILE B C   
15182 O O   . ILE C 371  ? 2.3153 1.0807 1.6489 0.2425  0.6750  0.0821  371  ILE B O   
15183 C CB  . ILE C 371  ? 2.4080 1.0130 1.6836 0.2217  0.7641  0.0881  371  ILE B CB  
15184 C CG1 . ILE C 371  ? 2.4217 0.9567 1.7001 0.2057  0.8216  0.0961  371  ILE B CG1 
15185 C CG2 . ILE C 371  ? 2.3975 0.9798 1.6192 0.2377  0.7440  0.0855  371  ILE B CG2 
15186 C CD1 . ILE C 371  ? 2.3803 0.8632 1.6684 0.2267  0.8474  0.1279  371  ILE B CD1 
15187 N N   . LYS C 372  ? 2.1437 0.9151 1.3817 0.2133  0.6476  0.0280  372  LYS B N   
15188 C CA  . LYS C 372  ? 2.0778 0.9267 1.3291 0.2314  0.5946  0.0257  372  LYS B CA  
15189 C C   . LYS C 372  ? 2.0723 0.9191 1.2836 0.2556  0.5619  0.0270  372  LYS B C   
15190 O O   . LYS C 372  ? 2.2079 1.0661 1.3651 0.2492  0.5368  0.0010  372  LYS B O   
15191 C CB  . LYS C 372  ? 2.1366 1.0379 1.3714 0.2093  0.5706  -0.0059 372  LYS B CB  
15192 C CG  . LYS C 372  ? 2.2514 1.1442 1.5086 0.1786  0.6043  -0.0148 372  LYS B CG  
15193 C CD  . LYS C 372  ? 2.3547 1.2902 1.5867 0.1542  0.5820  -0.0483 372  LYS B CD  
15194 C CE  . LYS C 372  ? 2.4099 1.3006 1.6324 0.1189  0.6232  -0.0644 372  LYS B CE  
15195 N NZ  . LYS C 372  ? 2.4012 1.3446 1.6672 0.0990  0.6213  -0.0713 372  LYS B NZ  
15196 N N   . VAL C 373  ? 2.1068 0.9399 1.3447 0.2830  0.5617  0.0567  373  VAL B N   
15197 C CA  . VAL C 373  ? 2.2508 1.0874 1.4590 0.3083  0.5277  0.0610  373  VAL B CA  
15198 C C   . VAL C 373  ? 2.1724 1.0911 1.3903 0.3222  0.4726  0.0521  373  VAL B C   
15199 O O   . VAL C 373  ? 2.1596 1.1305 1.4131 0.3141  0.4641  0.0468  373  VAL B O   
15200 C CB  . VAL C 373  ? 2.0271 0.8245 1.2644 0.3327  0.5439  0.0963  373  VAL B CB  
15201 C CG1 . VAL C 373  ? 1.9873 0.7619 1.2798 0.3258  0.5876  0.1171  373  VAL B CG1 
15202 C CG2 . VAL C 373  ? 1.9574 0.8029 1.2192 0.3649  0.4983  0.1114  373  VAL B CG2 
15203 N N   . GLN C 374  ? 2.1149 1.0457 1.3019 0.3434  0.4356  0.0510  374  GLN B N   
15204 C CA  . GLN C 374  ? 2.1265 1.1334 1.3106 0.3555  0.3814  0.0380  374  GLN B CA  
15205 C C   . GLN C 374  ? 2.1877 1.2034 1.3601 0.3875  0.3445  0.0501  374  GLN B C   
15206 O O   . GLN C 374  ? 2.3117 1.3092 1.4266 0.3898  0.3300  0.0368  374  GLN B O   
15207 C CB  . GLN C 374  ? 2.1986 1.2251 1.3285 0.3314  0.3681  0.0008  374  GLN B CB  
15208 C CG  . GLN C 374  ? 2.2638 1.3546 1.3678 0.3445  0.3124  -0.0158 374  GLN B CG  
15209 C CD  . GLN C 374  ? 2.4276 1.5387 1.4843 0.3183  0.3034  -0.0518 374  GLN B CD  
15210 O OE1 . GLN C 374  ? 2.5144 1.5906 1.5102 0.3101  0.3060  -0.0698 374  GLN B OE1 
15211 N NE2 . GLN C 374  ? 2.4483 1.6158 1.5339 0.3047  0.2941  -0.0622 374  GLN B NE2 
15212 N N   . VAL C 375  ? 1.8806 0.9249 1.1080 0.4126  0.3288  0.0750  375  VAL B N   
15213 C CA  . VAL C 375  ? 1.8927 0.9417 1.1167 0.4439  0.2955  0.0897  375  VAL B CA  
15214 C C   . VAL C 375  ? 1.8935 0.9949 1.0769 0.4515  0.2443  0.0668  375  VAL B C   
15215 O O   . VAL C 375  ? 1.9210 1.0760 1.1022 0.4394  0.2269  0.0462  375  VAL B O   
15216 C CB  . VAL C 375  ? 1.8786 0.9543 1.1734 0.4694  0.2858  0.1190  375  VAL B CB  
15217 C CG1 . VAL C 375  ? 1.8209 0.9308 1.1132 0.5009  0.2350  0.1251  375  VAL B CG1 
15218 C CG2 . VAL C 375  ? 1.8145 0.8261 1.1389 0.4717  0.3300  0.1470  375  VAL B CG2 
15219 N N   . LYS C 376  ? 2.0368 1.1214 1.1874 0.4711  0.2214  0.0710  376  LYS B N   
15220 C CA  . LYS C 376  ? 2.0442 1.1776 1.1582 0.4838  0.1699  0.0531  376  LYS B CA  
15221 C C   . LYS C 376  ? 1.9606 1.0840 1.0786 0.5159  0.1440  0.0738  376  LYS B C   
15222 O O   . LYS C 376  ? 1.9850 1.0609 1.1286 0.5258  0.1673  0.1000  376  LYS B O   
15223 C CB  . LYS C 376  ? 2.1656 1.2805 1.2052 0.4641  0.1714  0.0234  376  LYS B CB  
15224 C CG  . LYS C 376  ? 2.1423 1.2740 1.1681 0.4312  0.1879  -0.0034 376  LYS B CG  
15225 C CD  . LYS C 376  ? 2.2538 1.3499 1.2053 0.4119  0.1980  -0.0301 376  LYS B CD  
15226 C CE  . LYS C 376  ? 2.3274 1.4522 1.2606 0.3813  0.2022  -0.0609 376  LYS B CE  
15227 N NZ  . LYS C 376  ? 2.4356 1.5007 1.3152 0.3573  0.2359  -0.0790 376  LYS B NZ  
15228 N N   . ASP C 377  ? 2.0721 1.2404 1.1626 0.5317  0.0952  0.0612  377  ASP B N   
15229 C CA  . ASP C 377  ? 2.0853 1.2527 1.1793 0.5631  0.0636  0.0784  377  ASP B CA  
15230 C C   . ASP C 377  ? 2.2195 1.3620 1.2438 0.5654  0.0494  0.0649  377  ASP B C   
15231 O O   . ASP C 377  ? 2.3119 1.4524 1.2840 0.5447  0.0551  0.0384  377  ASP B O   
15232 C CB  . ASP C 377  ? 2.0565 1.3018 1.1730 0.5831  0.0127  0.0741  377  ASP B CB  
15233 C CG  . ASP C 377  ? 2.1645 1.4586 1.2324 0.5719  -0.0151 0.0411  377  ASP B CG  
15234 O OD1 . ASP C 377  ? 2.2321 1.5208 1.2804 0.5422  0.0113  0.0221  377  ASP B OD1 
15235 O OD2 . ASP C 377  ? 2.2056 1.5413 1.2541 0.5928  -0.0631 0.0343  377  ASP B OD2 
15236 N N   . SER C 378  ? 2.4103 1.5377 1.4353 0.5920  0.0278  0.0829  378  SER B N   
15237 C CA  . SER C 378  ? 2.4943 1.5999 1.4586 0.5999  0.0104  0.0748  378  SER B CA  
15238 C C   . SER C 378  ? 2.2678 1.4197 1.1758 0.5930  -0.0218 0.0407  378  SER B C   
15239 O O   . SER C 378  ? 2.3305 1.4658 1.1826 0.5972  -0.0343 0.0306  378  SER B O   
15240 C CB  . SER C 378  ? 2.4767 1.5854 1.4638 0.6337  -0.0230 0.0981  378  SER B CB  
15241 O OG  . SER C 378  ? 2.3925 1.5402 1.4471 0.6479  -0.0372 0.1136  378  SER B OG  
15242 N N   . LEU C 379  ? 2.2524 1.4629 1.1759 0.5828  -0.0347 0.0240  379  LEU B N   
15243 C CA  . LEU C 379  ? 2.3670 1.6326 1.2455 0.5783  -0.0701 -0.0068 379  LEU B CA  
15244 C C   . LEU C 379  ? 2.5109 1.7906 1.3750 0.5449  -0.0472 -0.0320 379  LEU B C   
15245 O O   . LEU C 379  ? 2.6014 1.9315 1.4338 0.5376  -0.0738 -0.0583 379  LEU B O   
15246 C CB  . LEU C 379  ? 2.3072 1.6444 1.2172 0.6027  -0.1193 -0.0037 379  LEU B CB  
15247 C CG  . LEU C 379  ? 2.3330 1.6832 1.2063 0.6292  -0.1646 -0.0056 379  LEU B CG  
15248 C CD1 . LEU C 379  ? 2.2685 1.6679 1.1863 0.6613  -0.2080 0.0098  379  LEU B CD1 
15249 C CD2 . LEU C 379  ? 2.4081 1.7896 1.2141 0.6173  -0.1854 -0.0397 379  LEU B CD2 
15250 N N   . ASP C 380  ? 2.9555 2.1913 1.8458 0.5251  0.0017  -0.0229 380  ASP B N   
15251 C CA  . ASP C 380  ? 3.0688 2.3006 1.9443 0.4911  0.0316  -0.0447 380  ASP B CA  
15252 C C   . ASP C 380  ? 3.0899 2.3931 1.9937 0.4813  0.0144  -0.0582 380  ASP B C   
15253 O O   . ASP C 380  ? 3.1592 2.4835 2.0304 0.4585  0.0139  -0.0858 380  ASP B O   
15254 C CB  . ASP C 380  ? 3.2486 2.4563 2.0474 0.4765  0.0340  -0.0716 380  ASP B CB  
15255 C CG  . ASP C 380  ? 3.3561 2.4804 2.1308 0.4719  0.0746  -0.0609 380  ASP B CG  
15256 O OD1 . ASP C 380  ? 3.3474 2.4296 2.1486 0.4555  0.1194  -0.0509 380  ASP B OD1 
15257 O OD2 . ASP C 380  ? 3.4573 2.5585 2.1861 0.4853  0.0618  -0.0621 380  ASP B OD2 
15258 N N   . GLN C 381  ? 2.8994 2.2406 1.8638 0.4994  -0.0007 -0.0385 381  GLN B N   
15259 C CA  . GLN C 381  ? 2.8964 2.2949 1.9021 0.4886  -0.0036 -0.0439 381  GLN B CA  
15260 C C   . GLN C 381  ? 2.8000 2.1623 1.8618 0.4791  0.0422  -0.0221 381  GLN B C   
15261 O O   . GLN C 381  ? 2.7395 2.0470 1.8163 0.4896  0.0641  0.0007  381  GLN B O   
15262 C CB  . GLN C 381  ? 2.9021 2.3731 1.9394 0.5172  -0.0522 -0.0365 381  GLN B CB  
15263 C CG  . GLN C 381  ? 3.0209 2.5369 2.0078 0.5300  -0.1020 -0.0566 381  GLN B CG  
15264 C CD  . GLN C 381  ? 3.0365 2.5708 2.0381 0.5684  -0.1417 -0.0387 381  GLN B CD  
15265 O OE1 . GLN C 381  ? 3.0367 2.6362 2.0676 0.5875  -0.1776 -0.0357 381  GLN B OE1 
15266 N NE2 . GLN C 381  ? 3.0337 2.5098 2.0161 0.5807  -0.1352 -0.0258 381  GLN B NE2 
15267 N N   . LEU C 382  ? 2.4087 1.8022 1.5024 0.4598  0.0568  -0.0283 382  LEU B N   
15268 C CA  . LEU C 382  ? 2.3071 1.6736 1.4584 0.4523  0.0984  -0.0071 382  LEU B CA  
15269 C C   . LEU C 382  ? 2.2310 1.6253 1.4398 0.4845  0.0787  0.0205  382  LEU B C   
15270 O O   . LEU C 382  ? 2.2663 1.7204 1.4781 0.5061  0.0323  0.0178  382  LEU B O   
15271 C CB  . LEU C 382  ? 2.3161 1.7182 1.4890 0.4259  0.1130  -0.0206 382  LEU B CB  
15272 C CG  . LEU C 382  ? 2.4038 1.7672 1.5272 0.3910  0.1414  -0.0459 382  LEU B CG  
15273 C CD1 . LEU C 382  ? 2.4443 1.8455 1.5900 0.3643  0.1529  -0.0598 382  LEU B CD1 
15274 C CD2 . LEU C 382  ? 2.3748 1.6508 1.4941 0.3828  0.1901  -0.0323 382  LEU B CD2 
15275 N N   . VAL C 383  ? 2.1045 1.4563 1.3580 0.4891  0.1125  0.0468  383  VAL B N   
15276 C CA  . VAL C 383  ? 1.9786 1.3584 1.2919 0.5193  0.0953  0.0730  383  VAL B CA  
15277 C C   . VAL C 383  ? 1.9395 1.3055 1.3130 0.5106  0.1366  0.0916  383  VAL B C   
15278 O O   . VAL C 383  ? 1.9471 1.2468 1.3227 0.4974  0.1815  0.1021  383  VAL B O   
15279 C CB  . VAL C 383  ? 1.8859 1.2291 1.1932 0.5468  0.0814  0.0919  383  VAL B CB  
15280 C CG1 . VAL C 383  ? 1.9665 1.2432 1.2144 0.5335  0.1014  0.0836  383  VAL B CG1 
15281 C CG2 . VAL C 383  ? 1.9009 1.2203 1.2725 0.5621  0.1036  0.1245  383  VAL B CG2 
15282 N N   . GLY C 384  ? 2.0199 1.4504 1.4416 0.5186  0.1211  0.0957  384  GLY B N   
15283 C CA  . GLY C 384  ? 1.9889 1.4171 1.4663 0.5073  0.1593  0.1094  384  GLY B CA  
15284 C C   . GLY C 384  ? 1.9355 1.3505 1.4704 0.5329  0.1674  0.1413  384  GLY B C   
15285 O O   . GLY C 384  ? 1.9288 1.3487 1.4655 0.5618  0.1361  0.1522  384  GLY B O   
15286 N N   . GLY C 385  ? 1.8508 1.2485 1.4325 0.5222  0.2094  0.1560  385  GLY B N   
15287 C CA  . GLY C 385  ? 1.7643 1.1643 1.4098 0.5462  0.2164  0.1855  385  GLY B CA  
15288 C C   . GLY C 385  ? 1.7272 1.0607 1.3711 0.5592  0.2312  0.2058  385  GLY B C   
15289 O O   . GLY C 385  ? 1.6814 1.0272 1.3511 0.5900  0.2048  0.2229  385  GLY B O   
15290 N N   . VAL C 386  ? 1.7574 1.0199 1.3719 0.5361  0.2737  0.2045  386  VAL B N   
15291 C CA  . VAL C 386  ? 1.7163 0.9148 1.3220 0.5469  0.2875  0.2225  386  VAL B CA  
15292 C C   . VAL C 386  ? 1.6508 0.7841 1.2665 0.5260  0.3476  0.2338  386  VAL B C   
15293 O O   . VAL C 386  ? 1.6961 0.8164 1.2906 0.4970  0.3749  0.2174  386  VAL B O   
15294 C CB  . VAL C 386  ? 1.6477 0.8229 1.1827 0.5452  0.2651  0.2055  386  VAL B CB  
15295 C CG1 . VAL C 386  ? 1.5937 0.7446 1.1315 0.5740  0.2449  0.2255  386  VAL B CG1 
15296 C CG2 . VAL C 386  ? 1.6891 0.9291 1.1919 0.5443  0.2197  0.1781  386  VAL B CG2 
15297 N N   . PRO C 387  ? 1.7911 0.8828 1.4381 0.5411  0.3674  0.2618  387  PRO B N   
15298 C CA  . PRO C 387  ? 1.8487 0.8735 1.5094 0.5277  0.4241  0.2787  387  PRO B CA  
15299 C C   . PRO C 387  ? 1.9461 0.9039 1.5420 0.5034  0.4532  0.2655  387  PRO B C   
15300 O O   . PRO C 387  ? 1.9994 0.9506 1.5444 0.5063  0.4276  0.2525  387  PRO B O   
15301 C CB  . PRO C 387  ? 1.8311 0.8366 1.5309 0.5566  0.4204  0.3099  387  PRO B CB  
15302 C CG  . PRO C 387  ? 1.7116 0.7702 1.4147 0.5842  0.3615  0.3077  387  PRO B CG  
15303 C CD  . PRO C 387  ? 1.7323 0.8342 1.3905 0.5737  0.3295  0.2768  387  PRO B CD  
15304 N N   . VAL C 388  ? 1.9509 0.8592 1.5490 0.4815  0.5060  0.2695  388  VAL B N   
15305 C CA  . VAL C 388  ? 2.0170 0.8708 1.5548 0.4556  0.5341  0.2521  388  VAL B CA  
15306 C C   . VAL C 388  ? 2.0598 0.8444 1.6072 0.4420  0.5938  0.2681  388  VAL B C   
15307 O O   . VAL C 388  ? 2.1102 0.8760 1.6442 0.4157  0.6256  0.2544  388  VAL B O   
15308 C CB  . VAL C 388  ? 2.0691 0.9588 1.5818 0.4302  0.5273  0.2201  388  VAL B CB  
15309 C CG1 . VAL C 388  ? 2.1646 0.9988 1.6180 0.4028  0.5576  0.2008  388  VAL B CG1 
15310 C CG2 . VAL C 388  ? 2.0544 1.0092 1.5485 0.4419  0.4698  0.2021  388  VAL B CG2 
15311 N N   . THR C 389  ? 2.3686 1.1146 1.9381 0.4598  0.6089  0.2970  389  THR B N   
15312 C CA  . THR C 389  ? 2.4058 1.0878 1.9878 0.4499  0.6655  0.3152  389  THR B CA  
15313 C C   . THR C 389  ? 2.4955 1.1174 2.0160 0.4237  0.6999  0.2982  389  THR B C   
15314 O O   . THR C 389  ? 2.5878 1.1807 2.0564 0.4257  0.6904  0.2914  389  THR B O   
15315 C CB  . THR C 389  ? 2.5553 1.2038 2.1637 0.4742  0.6724  0.3487  389  THR B CB  
15316 O OG1 . THR C 389  ? 2.5189 1.2128 2.1439 0.5010  0.6214  0.3546  389  THR B OG1 
15317 C CG2 . THR C 389  ? 2.5252 1.1811 2.1946 0.4728  0.7102  0.3708  389  THR B CG2 
15318 N N   . LEU C 390  ? 2.0624 0.6644 1.5897 0.4002  0.7404  0.2921  390  LEU B N   
15319 C CA  . LEU C 390  ? 2.1021 0.6458 1.5740 0.3753  0.7752  0.2755  390  LEU B CA  
15320 C C   . LEU C 390  ? 2.1902 0.6656 1.6736 0.3725  0.8299  0.2988  390  LEU B C   
15321 O O   . LEU C 390  ? 2.2485 0.7169 1.7640 0.3602  0.8631  0.3035  390  LEU B O   
15322 C CB  . LEU C 390  ? 2.0904 0.6580 1.5503 0.3470  0.7796  0.2459  390  LEU B CB  
15323 C CG  . LEU C 390  ? 2.1970 0.7046 1.6015 0.3203  0.8156  0.2268  390  LEU B CG  
15324 C CD1 . LEU C 390  ? 2.3060 0.7877 1.6473 0.3264  0.7979  0.2168  390  LEU B CD1 
15325 C CD2 . LEU C 390  ? 2.2049 0.7379 1.5976 0.2921  0.8159  0.1964  390  LEU B CD2 
15326 N N   . ASN C 391  ? 2.5367 0.9623 1.9938 0.3841  0.8398  0.3137  391  ASN B N   
15327 C CA  . ASN C 391  ? 2.6214 0.9773 2.0774 0.3796  0.8932  0.3327  391  ASN B CA  
15328 C C   . ASN C 391  ? 2.7383 1.0443 2.1319 0.3548  0.9220  0.3097  391  ASN B C   
15329 O O   . ASN C 391  ? 2.8052 1.1098 2.1427 0.3501  0.9005  0.2873  391  ASN B O   
15330 C CB  . ASN C 391  ? 2.6695 0.9939 2.1275 0.4034  0.8931  0.3613  391  ASN B CB  
15331 C CG  . ASN C 391  ? 2.6425 1.0340 2.1680 0.4231  0.8758  0.3818  391  ASN B CG  
15332 O OD1 . ASN C 391  ? 2.5840 1.0281 2.1326 0.4337  0.8326  0.3768  391  ASN B OD1 
15333 N ND2 . ASN C 391  ? 2.6713 1.0759 2.2306 0.4272  0.9096  0.4017  391  ASN B ND2 
15334 N N   . ALA C 392  ? 2.6077 0.8709 2.0097 0.3400  0.9710  0.3152  392  ALA B N   
15335 C CA  . ALA C 392  ? 2.6759 0.8916 2.0207 0.3161  0.9990  0.2920  392  ALA B CA  
15336 C C   . ALA C 392  ? 2.7058 0.8460 2.0388 0.3179  1.0496  0.3134  392  ALA B C   
15337 O O   . ALA C 392  ? 2.6856 0.8144 2.0632 0.3345  1.0666  0.3462  392  ALA B O   
15338 C CB  . ALA C 392  ? 2.6759 0.9142 2.0333 0.2905  1.0085  0.2696  392  ALA B CB  
15339 N N   . GLN C 393  ? 2.8214 0.9118 2.0928 0.3020  1.0716  0.2944  393  GLN B N   
15340 C CA  . GLN C 393  ? 2.9484 0.9639 2.1978 0.2999  1.1224  0.3086  393  GLN B CA  
15341 C C   . GLN C 393  ? 3.0339 1.0146 2.2305 0.2729  1.1448  0.2766  393  GLN B C   
15342 O O   . GLN C 393  ? 3.0216 1.0261 2.1807 0.2599  1.1173  0.2441  393  GLN B O   
15343 C CB  . GLN C 393  ? 2.9937 0.9754 2.2115 0.3209  1.1197  0.3266  393  GLN B CB  
15344 C CG  . GLN C 393  ? 3.0541 0.9639 2.2620 0.3252  1.1715  0.3508  393  GLN B CG  
15345 C CD  . GLN C 393  ? 3.1513 1.0051 2.2831 0.3145  1.1926  0.3314  393  GLN B CD  
15346 O OE1 . GLN C 393  ? 3.2133 1.0120 2.3312 0.3068  1.2386  0.3368  393  GLN B OE1 
15347 N NE2 . GLN C 393  ? 3.1633 1.0312 2.2452 0.3154  1.1589  0.3091  393  GLN B NE2 
15348 N N   . THR C 394  ? 3.4475 1.3716 2.6412 0.2645  1.1946  0.2856  394  THR B N   
15349 C CA  . THR C 394  ? 3.5555 1.4459 2.7053 0.2385  1.2174  0.2560  394  THR B CA  
15350 C C   . THR C 394  ? 3.7400 1.5570 2.8770 0.2386  1.2718  0.2733  394  THR B C   
15351 O O   . THR C 394  ? 3.7708 1.5712 2.9403 0.2574  1.2903  0.3084  394  THR B O   
15352 C CB  . THR C 394  ? 3.4482 1.3791 2.6336 0.2168  1.2131  0.2378  394  THR B CB  
15353 O OG1 . THR C 394  ? 3.4370 1.3926 2.5801 0.1992  1.1833  0.1991  394  THR B OG1 
15354 C CG2 . THR C 394  ? 3.4916 1.3755 2.6895 0.2004  1.2652  0.2417  394  THR B CG2 
15355 N N   . ILE C 395  ? 3.3622 1.1349 2.4500 0.2186  1.2962  0.2486  395  ILE B N   
15356 C CA  . ILE C 395  ? 3.4715 1.1742 2.5461 0.2163  1.3497  0.2618  395  ILE B CA  
15357 C C   . ILE C 395  ? 3.5833 1.2644 2.6447 0.1875  1.3737  0.2348  395  ILE B C   
15358 O O   . ILE C 395  ? 3.5932 1.3060 2.6411 0.1686  1.3486  0.2021  395  ILE B O   
15359 C CB  . ILE C 395  ? 3.5373 1.1874 2.5493 0.2285  1.3610  0.2648  395  ILE B CB  
15360 C CG1 . ILE C 395  ? 3.5893 1.2211 2.5321 0.2098  1.3542  0.2234  395  ILE B CG1 
15361 C CG2 . ILE C 395  ? 3.4973 1.1755 2.5151 0.2543  1.3278  0.2845  395  ILE B CG2 
15362 C CD1 . ILE C 395  ? 3.7006 1.2571 2.5842 0.2127  1.3919  0.2236  395  ILE B CD1 
15363 N N   . ASP C 396  ? 3.1737 0.8011 2.2412 0.1847  1.4227  0.2497  396  ASP B N   
15364 C CA  . ASP C 396  ? 3.2411 0.8421 2.3019 0.1587  1.4505  0.2287  396  ASP B CA  
15365 C C   . ASP C 396  ? 3.3370 0.8920 2.3192 0.1487  1.4553  0.1991  396  ASP B C   
15366 O O   . ASP C 396  ? 3.3737 0.9134 2.3141 0.1648  1.4450  0.2023  396  ASP B O   
15367 C CB  . ASP C 396  ? 3.3107 0.8655 2.4009 0.1634  1.5021  0.2579  396  ASP B CB  
15368 C CG  . ASP C 396  ? 3.3778 0.9406 2.5090 0.1418  1.5217  0.2507  396  ASP B CG  
15369 O OD1 . ASP C 396  ? 3.4434 0.9669 2.5960 0.1435  1.5655  0.2718  396  ASP B OD1 
15370 O OD2 . ASP C 396  ? 3.3583 0.9672 2.5016 0.1235  1.4942  0.2253  396  ASP B OD2 
15371 N N   . VAL C 397  ? 3.8645 1.3984 2.8270 0.1226  1.4703  0.1702  397  VAL B N   
15372 C CA  . VAL C 397  ? 4.0006 1.4724 2.8917 0.1140  1.4908  0.1472  397  VAL B CA  
15373 C C   . VAL C 397  ? 4.0781 1.4864 2.9654 0.1300  1.5391  0.1786  397  VAL B C   
15374 O O   . VAL C 397  ? 4.1554 1.5108 2.9849 0.1378  1.5564  0.1757  397  VAL B O   
15375 C CB  . VAL C 397  ? 4.0584 1.5189 2.9385 0.0816  1.5000  0.1121  397  VAL B CB  
15376 C CG1 . VAL C 397  ? 4.0902 1.5080 3.0006 0.0736  1.5494  0.1276  397  VAL B CG1 
15377 C CG2 . VAL C 397  ? 4.1814 1.6039 2.9820 0.0719  1.4964  0.0765  397  VAL B CG2 
15378 N N   . ASN C 398  ? 4.3409 1.7576 3.2914 0.1360  1.5599  0.2097  398  ASN B N   
15379 C CA  . ASN C 398  ? 4.3926 1.7586 3.3521 0.1527  1.6044  0.2446  398  ASN B CA  
15380 C C   . ASN C 398  ? 4.3655 1.7279 3.3124 0.1820  1.5957  0.2716  398  ASN B C   
15381 O O   . ASN C 398  ? 4.3438 1.6795 3.3121 0.1996  1.6254  0.3071  398  ASN B O   
15382 C CB  . ASN C 398  ? 4.3632 1.7525 3.4000 0.1531  1.6212  0.2710  398  ASN B CB  
15383 C CG  . ASN C 398  ? 4.4703 1.8010 3.5098 0.1453  1.6752  0.2797  398  ASN B CG  
15384 O OD1 . ASN C 398  ? 4.5952 1.8685 3.5789 0.1369  1.6989  0.2624  398  ASN B OD1 
15385 N ND2 . ASN C 398  ? 4.4180 1.7968 3.5243 0.1530  1.6938  0.2969  398  ASN B ND2 
15386 N N   . GLN C 399  ? 3.9860 1.3758 2.8991 0.1871  1.5552  0.2555  399  GLN B N   
15387 C CA  . GLN C 399  ? 3.9837 1.3841 2.8941 0.2145  1.5378  0.2809  399  GLN B CA  
15388 C C   . GLN C 399  ? 3.9140 1.3355 2.8959 0.2313  1.5463  0.3228  399  GLN B C   
15389 O O   . GLN C 399  ? 3.9194 1.3279 2.9044 0.2532  1.5685  0.3502  399  GLN B O   
15390 C CB  . GLN C 399  ? 4.1013 1.4394 2.9472 0.2277  1.5616  0.2859  399  GLN B CB  
15391 C CG  . GLN C 399  ? 4.1862 1.5105 2.9579 0.2172  1.5447  0.2460  399  GLN B CG  
15392 C CD  . GLN C 399  ? 4.1380 1.5184 2.9002 0.2220  1.4907  0.2317  399  GLN B CD  
15393 O OE1 . GLN C 399  ? 4.1171 1.5116 2.8839 0.2448  1.4745  0.2551  399  GLN B OE1 
15394 N NE2 . GLN C 399  ? 4.1157 1.5282 2.8644 0.2005  1.4626  0.1934  399  GLN B NE2 
15395 N N   . GLU C 400  ? 4.1081 1.5832 3.1486 0.2224  1.5286  0.3214  400  GLU B N   
15396 C CA  . GLU C 400  ? 4.0240 1.5714 3.1402 0.2406  1.5280  0.3457  400  GLU B CA  
15397 C C   . GLU C 400  ? 3.8709 1.4816 3.0175 0.2452  1.4738  0.3446  400  GLU B C   
15398 O O   . GLU C 400  ? 3.8310 1.4529 2.9766 0.2259  1.4480  0.3230  400  GLU B O   
15399 C CB  . GLU C 400  ? 4.0440 1.6095 3.2082 0.2291  1.5595  0.3439  400  GLU B CB  
15400 C CG  . GLU C 400  ? 4.0627 1.6889 3.2935 0.2533  1.5803  0.3671  400  GLU B CG  
15401 C CD  . GLU C 400  ? 4.1499 1.7697 3.4105 0.2452  1.6248  0.3657  400  GLU B CD  
15402 O OE1 . GLU C 400  ? 4.2148 1.8136 3.4739 0.2587  1.6657  0.3776  400  GLU B OE1 
15403 O OE2 . GLU C 400  ? 4.1489 1.7839 3.4345 0.2258  1.6192  0.3528  400  GLU B OE2 
15404 N N   . THR C 401  ? 3.9368 1.5974 3.1101 0.2713  1.4557  0.3644  401  THR B N   
15405 C CA  . THR C 401  ? 3.7922 1.5099 2.9898 0.2782  1.4029  0.3640  401  THR B CA  
15406 C C   . THR C 401  ? 3.6564 1.4472 2.9285 0.2775  1.3935  0.3670  401  THR B C   
15407 O O   . THR C 401  ? 3.6859 1.4888 2.9961 0.2754  1.4290  0.3722  401  THR B O   
15408 C CB  . THR C 401  ? 3.7623 1.5140 2.9691 0.3067  1.3843  0.3847  401  THR B CB  
15409 O OG1 . THR C 401  ? 3.7255 1.5308 2.9965 0.3244  1.4061  0.4055  401  THR B OG1 
15410 C CG2 . THR C 401  ? 3.8613 1.5475 3.0008 0.3128  1.3969  0.3873  401  THR B CG2 
15411 N N   . SER C 402  ? 3.4594 1.2988 2.7514 0.2814  1.3449  0.3640  402  SER B N   
15412 C CA  . SER C 402  ? 3.3028 1.2199 2.6669 0.2861  1.3281  0.3695  402  SER B CA  
15413 C C   . SER C 402  ? 3.1640 1.1333 2.5423 0.3031  1.2752  0.3746  402  SER B C   
15414 O O   . SER C 402  ? 3.1202 1.0669 2.4551 0.2976  1.2403  0.3607  402  SER B O   
15415 C CB  . SER C 402  ? 3.3044 1.2160 2.6774 0.2598  1.3282  0.3509  402  SER B CB  
15416 O OG  . SER C 402  ? 3.3404 1.2140 2.6536 0.2401  1.3091  0.3235  402  SER B OG  
15417 N N   . ASP C 403  ? 3.3715 1.4084 2.8095 0.3247  1.2697  0.3939  403  ASP B N   
15418 C CA  . ASP C 403  ? 3.2857 1.3841 2.7509 0.3397  1.2186  0.3982  403  ASP B CA  
15419 C C   . ASP C 403  ? 3.1811 1.3345 2.6984 0.3339  1.2006  0.3930  403  ASP B C   
15420 O O   . ASP C 403  ? 3.1594 1.3565 2.7356 0.3389  1.2211  0.4035  403  ASP B O   
15421 C CB  . ASP C 403  ? 3.3109 1.4548 2.8133 0.3654  1.2174  0.4211  403  ASP B CB  
15422 C CG  . ASP C 403  ? 3.3730 1.5088 2.8382 0.3782  1.1827  0.4240  403  ASP B CG  
15423 O OD1 . ASP C 403  ? 3.3305 1.4720 2.7743 0.3761  1.1385  0.4116  403  ASP B OD1 
15424 O OD2 . ASP C 403  ? 3.4496 1.5733 2.9078 0.3914  1.2004  0.4388  403  ASP B OD2 
15425 N N   . LEU C 404  ? 2.5540 0.7046 2.0488 0.3242  1.1619  0.3764  404  LEU B N   
15426 C CA  . LEU C 404  ? 2.4514 0.6513 1.9908 0.3189  1.1417  0.3708  404  LEU B CA  
15427 C C   . LEU C 404  ? 2.3837 0.6697 1.9850 0.3426  1.1109  0.3860  404  LEU B C   
15428 O O   . LEU C 404  ? 2.3934 0.7042 2.0076 0.3625  1.1053  0.4015  404  LEU B O   
15429 C CB  . LEU C 404  ? 2.3808 0.5712 1.8788 0.3027  1.1076  0.3433  404  LEU B CB  
15430 C CG  . LEU C 404  ? 2.3934 0.5583 1.8633 0.2720  1.1358  0.3176  404  LEU B CG  
15431 C CD1 . LEU C 404  ? 2.3332 0.5436 1.7738 0.2580  1.0957  0.2826  404  LEU B CD1 
15432 C CD2 . LEU C 404  ? 2.3234 0.4975 1.8507 0.2647  1.1656  0.3295  404  LEU B CD2 
15433 N N   . ASP C 405  ? 2.4622 0.7928 2.1017 0.3390  1.0906  0.3808  405  ASP B N   
15434 C CA  . ASP C 405  ? 2.3599 0.7736 2.0622 0.3588  1.0639  0.3936  405  ASP B CA  
15435 C C   . ASP C 405  ? 2.2602 0.7000 1.9532 0.3640  1.0081  0.3822  405  ASP B C   
15436 O O   . ASP C 405  ? 2.2523 0.6705 1.9250 0.3483  0.9968  0.3647  405  ASP B O   
15437 C CB  . ASP C 405  ? 2.3873 0.8376 2.1494 0.3542  1.0912  0.3997  405  ASP B CB  
15438 C CG  . ASP C 405  ? 2.6080 1.0605 2.3989 0.3610  1.1382  0.4159  405  ASP B CG  
15439 O OD1 . ASP C 405  ? 2.6277 1.0984 2.4248 0.3788  1.1318  0.4290  405  ASP B OD1 
15440 O OD2 . ASP C 405  ? 2.6055 1.0410 2.4123 0.3490  1.1803  0.4150  405  ASP B OD2 
15441 N N   . PRO C 406  ? 2.1581 0.6476 1.8694 0.3865  0.9728  0.3920  406  PRO B N   
15442 C CA  . PRO C 406  ? 2.1117 0.6289 1.8091 0.3994  0.9146  0.3832  406  PRO B CA  
15443 C C   . PRO C 406  ? 2.1278 0.6780 1.8490 0.3956  0.8911  0.3717  406  PRO B C   
15444 O O   . PRO C 406  ? 2.1391 0.7472 1.9205 0.4015  0.8949  0.3823  406  PRO B O   
15445 C CB  . PRO C 406  ? 2.0612 0.6446 1.8031 0.4228  0.8950  0.4020  406  PRO B CB  
15446 C CG  . PRO C 406  ? 2.1052 0.6746 1.8647 0.4216  0.9443  0.4190  406  PRO B CG  
15447 C CD  . PRO C 406  ? 2.1301 0.6611 1.8890 0.4017  0.9911  0.4140  406  PRO B CD  
15448 N N   . SER C 407  ? 2.2055 0.7676 1.8824 0.3793  0.8695  0.3415  407  SER B N   
15449 C CA  . SER C 407  ? 2.2131 0.8478 1.9140 0.3758  0.8388  0.3256  407  SER B CA  
15450 C C   . SER C 407  ? 2.1937 0.8771 1.8824 0.3953  0.7811  0.3185  407  SER B C   
15451 O O   . SER C 407  ? 2.2362 0.8912 1.8792 0.4007  0.7679  0.3148  407  SER B O   
15452 C CB  . SER C 407  ? 2.2844 0.9168 1.9510 0.3434  0.8510  0.2953  407  SER B CB  
15453 O OG  . SER C 407  ? 2.3504 0.9357 2.0291 0.3260  0.9047  0.3024  407  SER B OG  
15454 N N   . LYS C 408  ? 2.3489 1.1052 2.0787 0.4070  0.7473  0.3175  408  LYS B N   
15455 C CA  . LYS C 408  ? 2.2673 1.0774 1.9899 0.4272  0.6896  0.3104  408  LYS B CA  
15456 C C   . LYS C 408  ? 2.1832 1.0659 1.9225 0.4212  0.6626  0.2924  408  LYS B C   
15457 O O   . LYS C 408  ? 2.1607 1.0769 1.9555 0.4258  0.6711  0.3041  408  LYS B O   
15458 C CB  . LYS C 408  ? 2.2242 1.0518 1.9959 0.4609  0.6715  0.3392  408  LYS B CB  
15459 C CG  . LYS C 408  ? 2.2298 1.1259 2.0073 0.4828  0.6109  0.3320  408  LYS B CG  
15460 C CD  . LYS C 408  ? 2.2398 1.1608 2.0702 0.5140  0.5934  0.3591  408  LYS B CD  
15461 C CE  . LYS C 408  ? 2.2839 1.1768 2.1104 0.5094  0.6218  0.3764  408  LYS B CE  
15462 N NZ  . LYS C 408  ? 2.2603 1.2161 2.1220 0.5256  0.5952  0.3905  408  LYS B NZ  
15463 N N   . SER C 409  ? 1.9195 0.8273 1.6113 0.4112  0.6310  0.2645  409  SER B N   
15464 C CA  . SER C 409  ? 1.9462 0.9320 1.6533 0.4106  0.5958  0.2486  409  SER B CA  
15465 C C   . SER C 409  ? 1.8847 0.9137 1.5836 0.4376  0.5405  0.2477  409  SER B C   
15466 O O   . SER C 409  ? 1.8133 0.8126 1.5054 0.4570  0.5331  0.2626  409  SER B O   
15467 C CB  . SER C 409  ? 2.0796 1.0694 1.7412 0.3785  0.5982  0.2162  409  SER B CB  
15468 O OG  . SER C 409  ? 1.9505 1.0200 1.6304 0.3790  0.5632  0.2028  409  SER B OG  
15469 N N   . VAL C 410  ? 1.7435 0.8432 1.4438 0.4388  0.5021  0.2306  410  VAL B N   
15470 C CA  . VAL C 410  ? 1.7800 0.9233 1.4601 0.4604  0.4466  0.2228  410  VAL B CA  
15471 C C   . VAL C 410  ? 1.9004 1.0877 1.5412 0.4425  0.4205  0.1909  410  VAL B C   
15472 O O   . VAL C 410  ? 1.9432 1.1552 1.5977 0.4215  0.4349  0.1801  410  VAL B O   
15473 C CB  . VAL C 410  ? 1.7058 0.9043 1.4447 0.4932  0.4174  0.2428  410  VAL B CB  
15474 C CG1 . VAL C 410  ? 1.7347 0.9850 1.4504 0.5144  0.3568  0.2312  410  VAL B CG1 
15475 C CG2 . VAL C 410  ? 1.6347 0.7856 1.4075 0.5115  0.4408  0.2737  410  VAL B CG2 
15476 N N   . THR C 411  ? 1.6596 0.8545 1.2513 0.4506  0.3830  0.1765  411  THR B N   
15477 C CA  . THR C 411  ? 1.7129 0.9337 1.2535 0.4320  0.3615  0.1449  411  THR B CA  
15478 C C   . THR C 411  ? 1.6839 0.9912 1.2505 0.4365  0.3273  0.1355  411  THR B C   
15479 O O   . THR C 411  ? 1.5804 0.9359 1.1808 0.4655  0.2942  0.1483  411  THR B O   
15480 C CB  . THR C 411  ? 1.7605 0.9687 1.2461 0.4450  0.3286  0.1357  411  THR B CB  
15481 O OG1 . THR C 411  ? 1.8517 1.1153 1.3024 0.4400  0.2889  0.1088  411  THR B OG1 
15482 C CG2 . THR C 411  ? 1.6667 0.8878 1.1832 0.4806  0.3024  0.1590  411  THR B CG2 
15483 N N   . ARG C 412  ? 1.9934 1.3207 1.5421 0.4082  0.3336  0.1125  412  ARG B N   
15484 C CA  . ARG C 412  ? 2.1129 1.5241 1.6837 0.4090  0.3030  0.1023  412  ARG B CA  
15485 C C   . ARG C 412  ? 2.1254 1.5927 1.6746 0.4346  0.2434  0.0943  412  ARG B C   
15486 O O   . ARG C 412  ? 2.1558 1.5936 1.6629 0.4455  0.2270  0.0910  412  ARG B O   
15487 C CB  . ARG C 412  ? 2.3127 1.7280 1.8586 0.3716  0.3194  0.0766  412  ARG B CB  
15488 C CG  . ARG C 412  ? 2.4418 1.9392 2.0228 0.3679  0.3000  0.0707  412  ARG B CG  
15489 C CD  . ARG C 412  ? 2.6383 2.1367 2.1942 0.3293  0.3159  0.0451  412  ARG B CD  
15490 N NE  . ARG C 412  ? 2.7169 2.2076 2.3208 0.3100  0.3578  0.0547  412  ARG B NE  
15491 C CZ  . ARG C 412  ? 2.8541 2.3340 2.4463 0.2746  0.3814  0.0367  412  ARG B CZ  
15492 N NH1 . ARG C 412  ? 2.9584 2.4346 2.4921 0.2544  0.3671  0.0073  412  ARG B NH1 
15493 N NH2 . ARG C 412  ? 2.8664 2.3389 2.5059 0.2595  0.4192  0.0481  412  ARG B NH2 
15494 N N   . VAL C 413  ? 1.8413 1.3896 1.4199 0.4448  0.2119  0.0918  413  VAL B N   
15495 C CA  . VAL C 413  ? 1.8481 1.4584 1.4133 0.4718  0.1539  0.0859  413  VAL B CA  
15496 C C   . VAL C 413  ? 1.9420 1.5793 1.4486 0.4545  0.1281  0.0544  413  VAL B C   
15497 O O   . VAL C 413  ? 1.9582 1.6091 1.4236 0.4700  0.0892  0.0443  413  VAL B O   
15498 C CB  . VAL C 413  ? 1.8284 1.5200 1.4524 0.4916  0.1309  0.0973  413  VAL B CB  
15499 C CG1 . VAL C 413  ? 1.8162 1.5679 1.4261 0.5230  0.0706  0.0928  413  VAL B CG1 
15500 C CG2 . VAL C 413  ? 1.7454 1.4214 1.4359 0.5071  0.1584  0.1279  413  VAL B CG2 
15501 N N   . ASP C 414  ? 2.6720 2.3199 2.1777 0.4228  0.1492  0.0395  414  ASP B N   
15502 C CA  . ASP C 414  ? 2.7736 2.4456 2.2274 0.4010  0.1310  0.0086  414  ASP B CA  
15503 C C   . ASP C 414  ? 2.7979 2.3933 2.1938 0.3750  0.1592  -0.0081 414  ASP B C   
15504 O O   . ASP C 414  ? 2.8716 2.4719 2.2100 0.3651  0.1385  -0.0329 414  ASP B O   
15505 C CB  . ASP C 414  ? 2.8543 2.5747 2.3397 0.3782  0.1415  0.0015  414  ASP B CB  
15506 C CG  . ASP C 414  ? 2.8947 2.5641 2.4136 0.3542  0.1984  0.0119  414  ASP B CG  
15507 O OD1 . ASP C 414  ? 2.8359 2.4991 2.4094 0.3703  0.2163  0.0384  414  ASP B OD1 
15508 O OD2 . ASP C 414  ? 2.9751 2.6104 2.4654 0.3198  0.2248  -0.0067 414  ASP B OD2 
15509 N N   . ASP C 415  ? 2.5174 2.0430 1.9290 0.3649  0.2068  0.0060  415  ASP B N   
15510 C CA  . ASP C 415  ? 2.5679 2.0197 1.9333 0.3367  0.2425  -0.0084 415  ASP B CA  
15511 C C   . ASP C 415  ? 2.4661 1.8588 1.7895 0.3513  0.2417  -0.0040 415  ASP B C   
15512 O O   . ASP C 415  ? 2.4974 1.8527 1.7611 0.3362  0.2459  -0.0241 415  ASP B O   
15513 C CB  . ASP C 415  ? 2.6430 2.0504 2.0490 0.3179  0.2969  0.0054  415  ASP B CB  
15514 C CG  . ASP C 415  ? 2.8031 2.1423 2.1649 0.2853  0.3344  -0.0123 415  ASP B CG  
15515 O OD1 . ASP C 415  ? 2.9096 2.2296 2.2088 0.2804  0.3197  -0.0329 415  ASP B OD1 
15516 O OD2 . ASP C 415  ? 2.8131 2.1178 2.2020 0.2655  0.3784  -0.0059 415  ASP B OD2 
15517 N N   . GLY C 416  ? 2.0167 1.4020 1.3730 0.3811  0.2364  0.0229  416  GLY B N   
15518 C CA  . GLY C 416  ? 1.9964 1.3218 1.3239 0.3956  0.2411  0.0330  416  GLY B CA  
15519 C C   . GLY C 416  ? 2.0441 1.2899 1.3726 0.3763  0.2978  0.0415  416  GLY B C   
15520 O O   . GLY C 416  ? 2.0801 1.2650 1.3852 0.3830  0.3133  0.0509  416  GLY B O   
15521 N N   . VAL C 417  ? 2.1993 1.4462 1.5555 0.3523  0.3293  0.0386  417  VAL B N   
15522 C CA  . VAL C 417  ? 2.2143 1.3875 1.5688 0.3313  0.3839  0.0437  417  VAL B CA  
15523 C C   . VAL C 417  ? 2.1180 1.2738 1.5375 0.3404  0.4160  0.0746  417  VAL B C   
15524 O O   . VAL C 417  ? 2.0692 1.2741 1.5425 0.3435  0.4133  0.0835  417  VAL B O   
15525 C CB  . VAL C 417  ? 2.3386 1.5116 1.6761 0.2950  0.4038  0.0189  417  VAL B CB  
15526 C CG1 . VAL C 417  ? 2.3485 1.4543 1.7025 0.2754  0.4622  0.0288  417  VAL B CG1 
15527 C CG2 . VAL C 417  ? 2.4527 1.6175 1.7167 0.2820  0.3852  -0.0120 417  VAL B CG2 
15528 N N   . ALA C 418  ? 2.2914 1.3763 1.7045 0.3445  0.4480  0.0910  418  ALA B N   
15529 C CA  . ALA C 418  ? 2.2611 1.3184 1.7302 0.3514  0.4845  0.1202  418  ALA B CA  
15530 C C   . ALA C 418  ? 2.3142 1.3143 1.7762 0.3205  0.5384  0.1152  418  ALA B C   
15531 O O   . ALA C 418  ? 2.3428 1.2723 1.7768 0.3158  0.5691  0.1202  418  ALA B O   
15532 C CB  . ALA C 418  ? 2.2228 1.2403 1.6932 0.3775  0.4845  0.1441  418  ALA B CB  
15533 N N   . SER C 419  ? 2.0885 1.1186 1.5775 0.3005  0.5503  0.1067  419  SER B N   
15534 C CA  . SER C 419  ? 2.1716 1.1518 1.6483 0.2684  0.5967  0.0965  419  SER B CA  
15535 C C   . SER C 419  ? 2.0941 1.0184 1.6073 0.2699  0.6467  0.1233  419  SER B C   
15536 O O   . SER C 419  ? 2.0286 0.9765 1.5990 0.2896  0.6476  0.1486  419  SER B O   
15537 C CB  . SER C 419  ? 2.2487 1.2827 1.7450 0.2472  0.5906  0.0796  419  SER B CB  
15538 O OG  . SER C 419  ? 2.2836 1.3785 1.7550 0.2524  0.5401  0.0602  419  SER B OG  
15539 N N   . PHE C 420  ? 2.1257 0.9771 1.6053 0.2500  0.6877  0.1176  420  PHE B N   
15540 C CA  . PHE C 420  ? 2.1749 0.9699 1.6846 0.2492  0.7381  0.1414  420  PHE B CA  
15541 C C   . PHE C 420  ? 2.3060 1.0627 1.8044 0.2156  0.7792  0.1266  420  PHE B C   
15542 O O   . PHE C 420  ? 2.4535 1.2232 1.9176 0.1931  0.7681  0.0974  420  PHE B O   
15543 C CB  . PHE C 420  ? 2.1693 0.8968 1.6432 0.2604  0.7539  0.1525  420  PHE B CB  
15544 C CG  . PHE C 420  ? 2.0358 0.7816 1.5222 0.2935  0.7236  0.1721  420  PHE B CG  
15545 C CD1 . PHE C 420  ? 1.9672 0.6915 1.4980 0.3134  0.7439  0.2051  420  PHE B CD1 
15546 C CD2 . PHE C 420  ? 2.0434 0.8245 1.4955 0.3048  0.6755  0.1578  420  PHE B CD2 
15547 C CE1 . PHE C 420  ? 1.9459 0.6843 1.4889 0.3436  0.7156  0.2234  420  PHE B CE1 
15548 C CE2 . PHE C 420  ? 2.0546 0.8497 1.5178 0.3356  0.6470  0.1761  420  PHE B CE2 
15549 C CZ  . PHE C 420  ? 1.9776 0.7511 1.4868 0.3548  0.6664  0.2088  420  PHE B CZ  
15550 N N   . VAL C 421  ? 2.6887 1.3966 2.2151 0.2126  0.8266  0.1468  421  VAL B N   
15551 C CA  . VAL C 421  ? 2.6985 1.3470 2.2034 0.1835  0.8722  0.1353  421  VAL B CA  
15552 C C   . VAL C 421  ? 2.6715 1.2576 2.1979 0.1911  0.9198  0.1634  421  VAL B C   
15553 O O   . VAL C 421  ? 2.6172 1.2227 2.2027 0.2071  0.9286  0.1901  421  VAL B O   
15554 C CB  . VAL C 421  ? 2.6770 1.3597 2.2109 0.1578  0.8804  0.1216  421  VAL B CB  
15555 C CG1 . VAL C 421  ? 2.6813 1.3097 2.2386 0.1423  0.9368  0.1332  421  VAL B CG1 
15556 C CG2 . VAL C 421  ? 2.7383 1.4311 2.2203 0.1324  0.8608  0.0841  421  VAL B CG2 
15557 N N   . LEU C 422  ? 2.1681 0.6805 1.6454 0.1813  0.9495  0.1577  422  LEU B N   
15558 C CA  . LEU C 422  ? 2.1664 0.6144 1.6590 0.1823  1.0009  0.1805  422  LEU B CA  
15559 C C   . LEU C 422  ? 2.3078 0.7106 1.7787 0.1499  1.0394  0.1616  422  LEU B C   
15560 O O   . LEU C 422  ? 2.3905 0.7725 1.8044 0.1313  1.0341  0.1325  422  LEU B O   
15561 C CB  . LEU C 422  ? 2.1484 0.5439 1.6104 0.2026  1.0091  0.1973  422  LEU B CB  
15562 C CG  . LEU C 422  ? 2.0699 0.4714 1.4802 0.2150  0.9703  0.1857  422  LEU B CG  
15563 C CD1 . LEU C 422  ? 2.1714 0.5612 1.5194 0.1900  0.9631  0.1482  422  LEU B CD1 
15564 C CD2 . LEU C 422  ? 2.0516 0.4013 1.4430 0.2368  0.9830  0.2088  422  LEU B CD2 
15565 N N   . ASN C 423  ? 2.9444 1.3348 2.4622 0.1434  1.0767  0.1776  423  ASN B N   
15566 C CA  . ASN C 423  ? 3.0243 1.3731 2.5303 0.1134  1.1148  0.1625  423  ASN B CA  
15567 C C   . ASN C 423  ? 3.0527 1.3152 2.5230 0.1144  1.1568  0.1714  423  ASN B C   
15568 O O   . ASN C 423  ? 2.9721 1.2133 2.4691 0.1351  1.1769  0.2022  423  ASN B O   
15569 C CB  . ASN C 423  ? 2.9733 1.3496 2.5485 0.1086  1.1356  0.1783  423  ASN B CB  
15570 C CG  . ASN C 423  ? 2.8794 1.3379 2.5103 0.1298  1.0990  0.1934  423  ASN B CG  
15571 O OD1 . ASN C 423  ? 2.9060 1.4262 2.5523 0.1205  1.0700  0.1780  423  ASN B OD1 
15572 N ND2 . ASN C 423  ? 2.7776 1.2379 2.4389 0.1591  1.0997  0.2235  423  ASN B ND2 
15573 N N   . LEU C 424  ? 2.3811 0.5944 1.7915 0.0935  1.1701  0.1455  424  LEU B N   
15574 C CA  . LEU C 424  ? 2.4398 0.5743 1.8058 0.0994  1.2023  0.1529  424  LEU B CA  
15575 C C   . LEU C 424  ? 2.5345 0.5973 1.8851 0.0800  1.2553  0.1498  424  LEU B C   
15576 O O   . LEU C 424  ? 2.6076 0.6592 1.9353 0.0528  1.2613  0.1216  424  LEU B O   
15577 C CB  . LEU C 424  ? 2.4774 0.6025 1.7760 0.1035  1.1733  0.1327  424  LEU B CB  
15578 C CG  . LEU C 424  ? 2.3962 0.5654 1.7094 0.1334  1.1347  0.1505  424  LEU B CG  
15579 C CD1 . LEU C 424  ? 2.4584 0.6257 1.7077 0.1399  1.1019  0.1319  424  LEU B CD1 
15580 C CD2 . LEU C 424  ? 2.3255 0.4668 1.6733 0.1578  1.1608  0.1902  424  LEU B CD2 
15581 N N   . PRO C 425  ? 3.0417 1.0548 2.4035 0.0949  1.2931  0.1788  425  PRO B N   
15582 C CA  . PRO C 425  ? 3.1443 1.0883 2.4980 0.0817  1.3466  0.1825  425  PRO B CA  
15583 C C   . PRO C 425  ? 3.3292 1.2192 2.6104 0.0614  1.3570  0.1506  425  PRO B C   
15584 O O   . PRO C 425  ? 3.4227 1.2581 2.6593 0.0719  1.3735  0.1559  425  PRO B O   
15585 C CB  . PRO C 425  ? 3.1098 1.0153 2.4727 0.1083  1.3721  0.2185  425  PRO B CB  
15586 C CG  . PRO C 425  ? 2.9858 0.9532 2.3914 0.1330  1.3364  0.2390  425  PRO B CG  
15587 C CD  . PRO C 425  ? 2.9342 0.9562 2.3177 0.1269  1.2847  0.2109  425  PRO B CD  
15588 N N   . SER C 426  ? 3.3142 1.2193 2.5857 0.0335  1.3482  0.1193  426  SER B N   
15589 C CA  . SER C 426  ? 3.4749 1.3374 2.6786 0.0121  1.3513  0.0837  426  SER B CA  
15590 C C   . SER C 426  ? 3.6298 1.4229 2.7679 0.0230  1.3694  0.0831  426  SER B C   
15591 O O   . SER C 426  ? 3.6661 1.4522 2.7456 0.0184  1.3475  0.0564  426  SER B O   
15592 C CB  . SER C 426  ? 3.5808 1.4203 2.7958 -0.0181 1.3802  0.0676  426  SER B CB  
15593 O OG  . SER C 426  ? 3.5634 1.3651 2.8148 -0.0138 1.4265  0.0951  426  SER B OG  
15594 N N   . GLY C 427  ? 3.1620 0.9055 2.3099 0.0379  1.4092  0.1125  427  GLY B N   
15595 C CA  . GLY C 427  ? 3.2227 0.9031 2.3149 0.0518  1.4285  0.1180  427  GLY B CA  
15596 C C   . GLY C 427  ? 3.1541 0.8577 2.2253 0.0765  1.3947  0.1266  427  GLY B C   
15597 O O   . GLY C 427  ? 3.1732 0.8312 2.2063 0.0931  1.4091  0.1384  427  GLY B O   
15598 N N   . VAL C 428  ? 2.9989 0.7743 2.0949 0.0799  1.3493  0.1217  428  VAL B N   
15599 C CA  . VAL C 428  ? 2.9159 0.7158 1.9925 0.1026  1.3144  0.1284  428  VAL B CA  
15600 C C   . VAL C 428  ? 2.9803 0.7565 1.9793 0.0949  1.2999  0.0958  428  VAL B C   
15601 O O   . VAL C 428  ? 3.0699 0.8157 2.0360 0.0716  1.3149  0.0680  428  VAL B O   
15602 C CB  . VAL C 428  ? 2.8182 0.7017 1.9410 0.1091  1.2688  0.1311  428  VAL B CB  
15603 C CG1 . VAL C 428  ? 2.8735 0.7974 1.9736 0.0864  1.2351  0.0916  428  VAL B CG1 
15604 C CG2 . VAL C 428  ? 2.7503 0.6532 1.8721 0.1391  1.2421  0.1522  428  VAL B CG2 
15605 N N   . THR C 429  ? 2.5663 0.3596 1.5380 0.1144  1.2689  0.0984  429  THR B N   
15606 C CA  . THR C 429  ? 2.6332 0.3851 1.5299 0.1186  1.2678  0.0821  429  THR B CA  
15607 C C   . THR C 429  ? 2.6176 0.4166 1.4891 0.1300  1.2175  0.0704  429  THR B C   
15608 O O   . THR C 429  ? 2.6423 0.4639 1.4772 0.1157  1.1898  0.0358  429  THR B O   
15609 C CB  . THR C 429  ? 2.6664 0.3622 1.5554 0.1418  1.3020  0.1160  429  THR B CB  
15610 O OG1 . THR C 429  ? 2.5964 0.3267 1.5159 0.1683  1.2786  0.1452  429  THR B OG1 
15611 C CG2 . THR C 429  ? 2.6474 0.3047 1.5745 0.1358  1.3508  0.1361  429  THR B CG2 
15612 N N   . VAL C 430  ? 3.5298 1.3412 2.4218 0.1569  1.2071  0.1011  430  VAL B N   
15613 C CA  . VAL C 430  ? 3.4487 1.3078 2.3305 0.1722  1.1602  0.0986  430  VAL B CA  
15614 C C   . VAL C 430  ? 3.3628 1.2690 2.3164 0.1872  1.1460  0.1284  430  VAL B C   
15615 O O   . VAL C 430  ? 3.3199 1.2017 2.3116 0.1985  1.1757  0.1608  430  VAL B O   
15616 C CB  . VAL C 430  ? 3.4101 1.2306 2.2492 0.1944  1.1649  0.1129  430  VAL B CB  
15617 C CG1 . VAL C 430  ? 3.3441 1.2147 2.1762 0.2122  1.1154  0.1132  430  VAL B CG1 
15618 C CG2 . VAL C 430  ? 3.5241 1.2927 2.2936 0.1825  1.1839  0.0868  430  VAL B CG2 
15619 N N   . LEU C 431  ? 3.0275 1.0021 1.9990 0.1882  1.1001  0.1176  431  LEU B N   
15620 C CA  . LEU C 431  ? 2.8601 0.8839 1.8974 0.2042  1.0817  0.1436  431  LEU B CA  
15621 C C   . LEU C 431  ? 2.8349 0.8853 1.8541 0.2272  1.0416  0.1492  431  LEU B C   
15622 O O   . LEU C 431  ? 2.7402 0.8229 1.7238 0.2228  1.0053  0.1226  431  LEU B O   
15623 C CB  . LEU C 431  ? 2.7649 0.8489 1.8386 0.1867  1.0606  0.1258  431  LEU B CB  
15624 C CG  . LEU C 431  ? 2.6304 0.7622 1.7804 0.1999  1.0511  0.1526  431  LEU B CG  
15625 C CD1 . LEU C 431  ? 2.5654 0.7770 1.7381 0.1940  1.0057  0.1343  431  LEU B CD1 
15626 C CD2 . LEU C 431  ? 2.5634 0.6895 1.7266 0.2310  1.0431  0.1848  431  LEU B CD2 
15627 N N   . GLU C 432  ? 3.2258 1.2605 2.2675 0.2518  1.0486  0.1839  432  GLU B N   
15628 C CA  . GLU C 432  ? 3.1953 1.2608 2.2313 0.2751  1.0080  0.1930  432  GLU B CA  
15629 C C   . GLU C 432  ? 3.1065 1.2306 2.2139 0.2884  0.9832  0.2130  432  GLU B C   
15630 O O   . GLU C 432  ? 3.1003 1.2166 2.2602 0.2909  1.0096  0.2367  432  GLU B O   
15631 C CB  . GLU C 432  ? 3.2135 1.2257 2.2274 0.2952  1.0277  0.2190  432  GLU B CB  
15632 C CG  . GLU C 432  ? 3.3753 1.3199 2.3286 0.2850  1.0644  0.2076  432  GLU B CG  
15633 C CD  . GLU C 432  ? 3.4806 1.4191 2.3656 0.2902  1.0409  0.1880  432  GLU B CD  
15634 O OE1 . GLU C 432  ? 3.4057 1.3954 2.2878 0.2981  0.9945  0.1786  432  GLU B OE1 
15635 O OE2 . GLU C 432  ? 3.6078 1.4902 2.4412 0.2872  1.0692  0.1822  432  GLU B OE2 
15636 N N   . PHE C 433  ? 2.4795 0.6620 1.5883 0.2981  0.9327  0.2037  433  PHE B N   
15637 C CA  . PHE C 433  ? 2.3534 0.5938 1.5271 0.3130  0.9055  0.2213  433  PHE B CA  
15638 C C   . PHE C 433  ? 2.3733 0.6571 1.5422 0.3355  0.8536  0.2239  433  PHE B C   
15639 O O   . PHE C 433  ? 2.4477 0.7408 1.5636 0.3332  0.8272  0.2004  433  PHE B O   
15640 C CB  . PHE C 433  ? 2.2951 0.5809 1.5033 0.2938  0.9018  0.2046  433  PHE B CB  
15641 C CG  . PHE C 433  ? 2.3549 0.6711 1.5200 0.2733  0.8763  0.1643  433  PHE B CG  
15642 C CD1 . PHE C 433  ? 2.3928 0.7059 1.5566 0.2451  0.8973  0.1430  433  PHE B CD1 
15643 C CD2 . PHE C 433  ? 2.3937 0.7443 1.5232 0.2822  0.8306  0.1484  433  PHE B CD2 
15644 C CE1 . PHE C 433  ? 2.4398 0.7831 1.5681 0.2258  0.8733  0.1067  433  PHE B CE1 
15645 C CE2 . PHE C 433  ? 2.4552 0.8363 1.5475 0.2636  0.8072  0.1120  433  PHE B CE2 
15646 C CZ  . PHE C 433  ? 2.5223 0.9001 1.6148 0.2353  0.8284  0.0913  433  PHE B CZ  
15647 N N   . ASN C 434  ? 2.5993 0.9081 1.8234 0.3578  0.8397  0.2526  434  ASN B N   
15648 C CA  . ASN C 434  ? 2.5355 0.8896 1.7641 0.3803  0.7888  0.2566  434  ASN B CA  
15649 C C   . ASN C 434  ? 2.5079 0.9390 1.7863 0.3859  0.7507  0.2528  434  ASN B C   
15650 O O   . ASN C 434  ? 2.4941 0.9425 1.8334 0.3903  0.7617  0.2710  434  ASN B O   
15651 C CB  . ASN C 434  ? 2.5004 0.8234 1.7449 0.4056  0.7938  0.2915  434  ASN B CB  
15652 C CG  . ASN C 434  ? 2.5353 0.7848 1.7332 0.4019  0.8320  0.2977  434  ASN B CG  
15653 O OD1 . ASN C 434  ? 2.5458 0.7797 1.6929 0.4083  0.8174  0.2908  434  ASN B OD1 
15654 N ND2 . ASN C 434  ? 2.5672 0.7719 1.7807 0.3920  0.8816  0.3105  434  ASN B ND2 
15655 N N   . VAL C 435  ? 1.8792 0.3574 1.1299 0.3870  0.7056  0.2292  435  VAL B N   
15656 C CA  . VAL C 435  ? 1.8172 0.3701 1.1075 0.3964  0.6637  0.2256  435  VAL B CA  
15657 C C   . VAL C 435  ? 2.0435 0.6161 1.3423 0.4262  0.6248  0.2422  435  VAL B C   
15658 O O   . VAL C 435  ? 2.0763 0.6145 1.3351 0.4347  0.6217  0.2457  435  VAL B O   
15659 C CB  . VAL C 435  ? 1.8877 0.4812 1.1402 0.3795  0.6369  0.1891  435  VAL B CB  
15660 C CG1 . VAL C 435  ? 1.8400 0.5074 1.1121 0.3961  0.5826  0.1844  435  VAL B CG1 
15661 C CG2 . VAL C 435  ? 1.9108 0.5041 1.1775 0.3523  0.6677  0.1758  435  VAL B CG2 
15662 N N   . LYS C 436  ? 2.6058 1.2341 1.9569 0.4429  0.5946  0.2525  436  LYS B N   
15663 C CA  . LYS C 436  ? 2.5472 1.1974 1.9104 0.4720  0.5546  0.2677  436  LYS B CA  
15664 C C   . LYS C 436  ? 2.5263 1.2475 1.9460 0.4864  0.5206  0.2716  436  LYS B C   
15665 O O   . LYS C 436  ? 2.4910 1.2267 1.9585 0.4805  0.5410  0.2790  436  LYS B O   
15666 C CB  . LYS C 436  ? 2.5063 1.1012 1.8865 0.4875  0.5791  0.3011  436  LYS B CB  
15667 C CG  . LYS C 436  ? 2.4157 1.0060 1.8658 0.4954  0.6046  0.3300  436  LYS B CG  
15668 C CD  . LYS C 436  ? 2.6045 1.2238 2.0985 0.5264  0.5688  0.3530  436  LYS B CD  
15669 C CE  . LYS C 436  ? 2.6457 1.2791 2.1944 0.5252  0.6028  0.3784  436  LYS B CE  
15670 N NZ  . LYS C 436  ? 2.6829 1.2576 2.2032 0.5182  0.6418  0.3897  436  LYS B NZ  
15671 N N   . THR C 437  ? 2.0479 0.8147 1.4613 0.5055  0.4687  0.2662  437  THR B N   
15672 C CA  . THR C 437  ? 2.0711 0.9043 1.5378 0.5231  0.4347  0.2719  437  THR B CA  
15673 C C   . THR C 437  ? 1.9809 0.7971 1.5034 0.5460  0.4427  0.3070  437  THR B C   
15674 O O   . THR C 437  ? 1.9292 0.6950 1.4400 0.5549  0.4539  0.3247  437  THR B O   
15675 C CB  . THR C 437  ? 1.9865 0.8707 1.4287 0.5388  0.3765  0.2566  437  THR B CB  
15676 O OG1 . THR C 437  ? 2.0192 0.8658 1.4280 0.5525  0.3653  0.2653  437  THR B OG1 
15677 C CG2 . THR C 437  ? 2.0490 0.9620 1.4436 0.5167  0.3653  0.2213  437  THR B CG2 
15678 N N   . ASP C 438  ? 2.1844 1.0429 1.7683 0.5557  0.4376  0.3177  438  ASP B N   
15679 C CA  . ASP C 438  ? 2.2511 1.1216 1.8895 0.5722  0.4401  0.3456  438  ASP B CA  
15680 C C   . ASP C 438  ? 2.2030 1.1554 1.8706 0.5908  0.3881  0.3420  438  ASP B C   
15681 O O   . ASP C 438  ? 2.1441 1.1533 1.8674 0.5923  0.3876  0.3528  438  ASP B O   
15682 C CB  . ASP C 438  ? 2.3265 1.1973 2.0117 0.5563  0.4893  0.3588  438  ASP B CB  
15683 C CG  . ASP C 438  ? 2.4251 1.2887 2.1333 0.5521  0.5197  0.3806  438  ASP B CG  
15684 O OD1 . ASP C 438  ? 2.4421 1.3279 2.1510 0.5642  0.4929  0.3869  438  ASP B OD1 
15685 O OD2 . ASP C 438  ? 2.4714 1.3081 2.1975 0.5372  0.5699  0.3906  438  ASP B OD2 
15686 N N   . ALA C 439  ? 2.5743 1.5319 2.2012 0.6049  0.3440  0.3257  439  ALA B N   
15687 C CA  . ALA C 439  ? 2.5855 1.6181 2.2295 0.6238  0.2902  0.3210  439  ALA B CA  
15688 C C   . ALA C 439  ? 2.6003 1.6660 2.2920 0.6221  0.2981  0.3400  439  ALA B C   
15689 O O   . ALA C 439  ? 2.6527 1.6786 2.3436 0.6134  0.3296  0.3542  439  ALA B O   
15690 C CB  . ALA C 439  ? 2.6353 1.6562 2.2257 0.6381  0.2500  0.3096  439  ALA B CB  
15691 N N   . PRO C 440  ? 2.1056 1.2451 1.8405 0.6300  0.2710  0.3401  440  PRO B N   
15692 C CA  . PRO C 440  ? 2.0429 1.2119 1.8309 0.6250  0.2866  0.3580  440  PRO B CA  
15693 C C   . PRO C 440  ? 2.0113 1.1974 1.7929 0.6351  0.2523  0.3594  440  PRO B C   
15694 O O   . PRO C 440  ? 2.0145 1.2034 1.8275 0.6303  0.2680  0.3749  440  PRO B O   
15695 C CB  . PRO C 440  ? 1.9995 1.2384 1.8331 0.6282  0.2721  0.3551  440  PRO B CB  
15696 C CG  . PRO C 440  ? 2.0766 1.3304 1.8776 0.6387  0.2393  0.3339  440  PRO B CG  
15697 C CD  . PRO C 440  ? 2.1044 1.3040 1.8429 0.6431  0.2278  0.3242  440  PRO B CD  
15698 N N   . ASP C 441  ? 2.1942 1.3914 1.9358 0.6490  0.2062  0.3428  441  ASP B N   
15699 C CA  . ASP C 441  ? 2.2340 1.4480 1.9634 0.6600  0.1672  0.3400  441  ASP B CA  
15700 C C   . ASP C 441  ? 2.2344 1.3847 1.9167 0.6604  0.1745  0.3438  441  ASP B C   
15701 O O   . ASP C 441  ? 2.2410 1.3964 1.9193 0.6669  0.1520  0.3464  441  ASP B O   
15702 C CB  . ASP C 441  ? 2.3434 1.6118 2.0571 0.6758  0.1111  0.3195  441  ASP B CB  
15703 C CG  . ASP C 441  ? 2.4372 1.7026 2.1225 0.6794  0.1067  0.3052  441  ASP B CG  
15704 O OD1 . ASP C 441  ? 2.5111 1.8035 2.1649 0.6934  0.0631  0.2878  441  ASP B OD1 
15705 O OD2 . ASP C 441  ? 2.4189 1.6556 2.1136 0.6681  0.1467  0.3108  441  ASP B OD2 
15706 N N   . LEU C 442  ? 1.8748 0.9628 1.5207 0.6531  0.2066  0.3441  442  LEU B N   
15707 C CA  . LEU C 442  ? 1.8735 0.9010 1.4686 0.6544  0.2121  0.3461  442  LEU B CA  
15708 C C   . LEU C 442  ? 1.9180 0.9089 1.5304 0.6437  0.2536  0.3671  442  LEU B C   
15709 O O   . LEU C 442  ? 1.9181 0.8953 1.5599 0.6304  0.2977  0.3785  442  LEU B O   
15710 C CB  . LEU C 442  ? 1.8189 0.7932 1.3620 0.6513  0.2258  0.3347  442  LEU B CB  
15711 C CG  . LEU C 442  ? 1.7428 0.7577 1.2677 0.6647  0.1804  0.3137  442  LEU B CG  
15712 C CD1 . LEU C 442  ? 1.7546 0.7258 1.2269 0.6586  0.1906  0.2971  442  LEU B CD1 
15713 C CD2 . LEU C 442  ? 1.7139 0.7674 1.2227 0.6825  0.1262  0.3064  442  LEU B CD2 
15714 N N   . PRO C 443  ? 3.7234 2.6983 3.3172 0.6501  0.2401  0.3726  443  PRO B N   
15715 C CA  . PRO C 443  ? 3.7786 2.7118 3.3831 0.6401  0.2845  0.3927  443  PRO B CA  
15716 C C   . PRO C 443  ? 3.8960 2.7729 3.4774 0.6268  0.3327  0.3936  443  PRO B C   
15717 O O   . PRO C 443  ? 3.9357 2.7843 3.4699 0.6279  0.3255  0.3783  443  PRO B O   
15718 C CB  . PRO C 443  ? 3.7660 2.6672 3.3260 0.6494  0.2657  0.3934  443  PRO B CB  
15719 C CG  . PRO C 443  ? 3.7416 2.6899 3.2926 0.6646  0.2064  0.3776  443  PRO B CG  
15720 C CD  . PRO C 443  ? 3.7073 2.6923 3.2652 0.6656  0.1912  0.3617  443  PRO B CD  
15721 N N   . GLU C 444  ? 2.5582 1.4204 2.1731 0.6142  0.3806  0.4100  444  GLU B N   
15722 C CA  . GLU C 444  ? 2.6281 1.4272 2.2150 0.6010  0.4293  0.4119  444  GLU B CA  
15723 C C   . GLU C 444  ? 2.5758 1.3177 2.0916 0.6058  0.4202  0.4043  444  GLU B C   
15724 O O   . GLU C 444  ? 2.5202 1.2351 1.9918 0.6051  0.4120  0.3873  444  GLU B O   
15725 C CB  . GLU C 444  ? 2.8080 1.5930 2.4301 0.5917  0.4776  0.4333  444  GLU B CB  
15726 C CG  . GLU C 444  ? 2.9828 1.7296 2.6038 0.5757  0.5301  0.4348  444  GLU B CG  
15727 C CD  . GLU C 444  ? 3.1562 1.8290 2.7071 0.5697  0.5460  0.4242  444  GLU B CD  
15728 O OE1 . GLU C 444  ? 3.2305 1.8721 2.7375 0.5773  0.5320  0.4242  444  GLU B OE1 
15729 O OE2 . GLU C 444  ? 3.1938 1.8385 2.7336 0.5568  0.5731  0.4159  444  GLU B OE2 
15730 N N   . GLU C 445  ? 2.5380 1.2631 2.0437 0.6116  0.4201  0.4166  445  GLU B N   
15731 C CA  . GLU C 445  ? 2.5954 1.2694 2.0347 0.6181  0.4099  0.4115  445  GLU B CA  
15732 C C   . GLU C 445  ? 2.5214 1.1846 1.9133 0.6221  0.3824  0.3885  445  GLU B C   
15733 O O   . GLU C 445  ? 2.5550 1.1608 1.9000 0.6146  0.4043  0.3805  445  GLU B O   
15734 C CB  . GLU C 445  ? 2.6798 1.3797 2.1216 0.6329  0.3718  0.4170  445  GLU B CB  
15735 C CG  . GLU C 445  ? 2.7949 1.4894 2.2666 0.6316  0.3958  0.4396  445  GLU B CG  
15736 C CD  . GLU C 445  ? 2.9044 1.6180 2.3715 0.6459  0.3549  0.4424  445  GLU B CD  
15737 O OE1 . GLU C 445  ? 2.9100 1.6616 2.3712 0.6560  0.3061  0.4273  445  GLU B OE1 
15738 O OE2 . GLU C 445  ? 2.9729 1.6640 2.4419 0.6473  0.3714  0.4593  445  GLU B OE2 
15739 N N   . ASN C 446  ? 1.9094 0.6303 1.3158 0.6340  0.3338  0.3772  446  ASN B N   
15740 C CA  . ASN C 446  ? 1.9131 0.6316 1.2722 0.6439  0.2970  0.3563  446  ASN B CA  
15741 C C   . ASN C 446  ? 1.9136 0.6355 1.2741 0.6368  0.3025  0.3410  446  ASN B C   
15742 O O   . ASN C 446  ? 1.8879 0.6573 1.2315 0.6394  0.2658  0.3184  446  ASN B O   
15743 C CB  . ASN C 446  ? 1.8976 0.6793 1.2703 0.6615  0.2407  0.3511  446  ASN B CB  
15744 C CG  . ASN C 446  ? 1.9840 0.7611 1.3578 0.6678  0.2341  0.3655  446  ASN B CG  
15745 O OD1 . ASN C 446  ? 1.9685 0.7835 1.3948 0.6671  0.2328  0.3777  446  ASN B OD1 
15746 N ND2 . ASN C 446  ? 2.0774 0.8051 1.3931 0.6738  0.2315  0.3646  446  ASN B ND2 
15747 N N   . GLN C 447  ? 2.2867 0.9813 1.6666 0.6191  0.3509  0.3470  447  GLN B N   
15748 C CA  . GLN C 447  ? 2.3165 1.0368 1.7005 0.6006  0.3626  0.3266  447  GLN B CA  
15749 C C   . GLN C 447  ? 2.3546 1.0503 1.6717 0.5752  0.3832  0.3002  447  GLN B C   
15750 O O   . GLN C 447  ? 2.3687 1.0037 1.6599 0.5655  0.4217  0.3080  447  GLN B O   
15751 C CB  . GLN C 447  ? 2.3207 1.0203 1.7582 0.5935  0.4069  0.3463  447  GLN B CB  
15752 C CG  . GLN C 447  ? 2.3114 1.0886 1.8179 0.5990  0.3925  0.3571  447  GLN B CG  
15753 C CD  . GLN C 447  ? 2.2942 1.1235 1.8247 0.6033  0.3666  0.3433  447  GLN B CD  
15754 O OE1 . GLN C 447  ? 2.2997 1.1318 1.7921 0.5992  0.3507  0.3203  447  GLN B OE1 
15755 N NE2 . GLN C 447  ? 2.2727 1.1640 1.8651 0.6041  0.3643  0.3522  447  GLN B NE2 
15756 N N   . ALA C 448  ? 2.0156 0.7587 1.3056 0.5645  0.3588  0.2692  448  ALA B N   
15757 C CA  . ALA C 448  ? 2.0768 0.8013 1.3036 0.5392  0.3760  0.2409  448  ALA B CA  
15758 C C   . ALA C 448  ? 2.2240 0.9078 1.4573 0.5144  0.4320  0.2413  448  ALA B C   
15759 O O   . ALA C 448  ? 2.1478 0.8509 1.4314 0.5094  0.4460  0.2479  448  ALA B O   
15760 C CB  . ALA C 448  ? 2.1011 0.8890 1.3043 0.5323  0.3383  0.2086  448  ALA B CB  
15761 N N   . ARG C 449  ? 2.2558 0.8851 1.4365 0.4993  0.4627  0.2331  449  ARG B N   
15762 C CA  . ARG C 449  ? 2.2942 0.8753 1.4745 0.4768  0.5178  0.2342  449  ARG B CA  
15763 C C   . ARG C 449  ? 2.4064 0.9488 1.5156 0.4554  0.5394  0.2091  449  ARG B C   
15764 O O   . ARG C 449  ? 2.4534 0.9955 1.5097 0.4599  0.5163  0.1949  449  ARG B O   
15765 C CB  . ARG C 449  ? 2.2798 0.8103 1.4960 0.4884  0.5515  0.2709  449  ARG B CB  
15766 C CG  . ARG C 449  ? 2.3502 0.8402 1.5358 0.5043  0.5488  0.2861  449  ARG B CG  
15767 C CD  . ARG C 449  ? 2.4065 0.8546 1.6354 0.5144  0.5812  0.3223  449  ARG B CD  
15768 N NE  . ARG C 449  ? 2.4036 0.8756 1.6750 0.5415  0.5482  0.3459  449  ARG B NE  
15769 C CZ  . ARG C 449  ? 2.4140 0.8756 1.7448 0.5532  0.5637  0.3768  449  ARG B CZ  
15770 N NH1 . ARG C 449  ? 2.4315 0.8746 1.7858 0.5369  0.6131  0.3848  449  ARG B NH1 
15771 N NH2 . ARG C 449  ? 2.3797 0.8989 1.7455 0.5683  0.5321  0.3872  449  ARG B NH2 
15772 N N   . GLU C 450  ? 2.3784 0.8877 1.4874 0.4328  0.5841  0.2040  450  GLU B N   
15773 C CA  . GLU C 450  ? 2.4832 0.9546 1.5295 0.4111  0.6079  0.1793  450  GLU B CA  
15774 C C   . GLU C 450  ? 2.4799 0.8927 1.5379 0.3978  0.6646  0.1923  450  GLU B C   
15775 O O   . GLU C 450  ? 2.4242 0.8244 1.5357 0.4067  0.6848  0.2213  450  GLU B O   
15776 C CB  . GLU C 450  ? 2.4702 0.9867 1.4993 0.3895  0.5912  0.1435  450  GLU B CB  
15777 C CG  . GLU C 450  ? 2.4413 1.0119 1.4434 0.3984  0.5380  0.1240  450  GLU B CG  
15778 C CD  . GLU C 450  ? 2.5999 1.1396 1.5295 0.3984  0.5339  0.1086  450  GLU B CD  
15779 O OE1 . GLU C 450  ? 2.7055 1.1934 1.6005 0.3814  0.5721  0.0997  450  GLU B OE1 
15780 O OE2 . GLU C 450  ? 2.6106 1.1766 1.5181 0.4162  0.4938  0.1059  450  GLU B OE2 
15781 N N   . GLY C 451  ? 2.4140 0.7914 1.4215 0.3766  0.6901  0.1698  451  GLY B N   
15782 C CA  . GLY C 451  ? 2.4061 0.7286 1.4205 0.3619  0.7439  0.1780  451  GLY B CA  
15783 C C   . GLY C 451  ? 2.4762 0.7850 1.4339 0.3366  0.7539  0.1418  451  GLY B C   
15784 O O   . GLY C 451  ? 2.5588 0.8894 1.4694 0.3366  0.7221  0.1181  451  GLY B O   
15785 N N   . TYR C 452  ? 2.3165 0.5906 1.2784 0.3156  0.7961  0.1368  452  TYR B N   
15786 C CA  . TYR C 452  ? 2.4094 0.6654 1.3185 0.2897  0.8086  0.1014  452  TYR B CA  
15787 C C   . TYR C 452  ? 2.4958 0.6839 1.3954 0.2738  0.8651  0.1043  452  TYR B C   
15788 O O   . TYR C 452  ? 2.4712 0.6123 1.3825 0.2862  0.8962  0.1332  452  TYR B O   
15789 C CB  . TYR C 452  ? 2.3949 0.7140 1.3175 0.2719  0.7802  0.0737  452  TYR B CB  
15790 C CG  . TYR C 452  ? 2.3792 0.7645 1.2996 0.2857  0.7239  0.0652  452  TYR B CG  
15791 C CD1 . TYR C 452  ? 2.4940 0.9022 1.3597 0.2768  0.6952  0.0315  452  TYR B CD1 
15792 C CD2 . TYR C 452  ? 2.2937 0.7182 1.2659 0.3083  0.6993  0.0904  452  TYR B CD2 
15793 C CE1 . TYR C 452  ? 2.4981 0.9664 1.3601 0.2901  0.6443  0.0239  452  TYR B CE1 
15794 C CE2 . TYR C 452  ? 2.2904 0.7735 1.2589 0.3221  0.6477  0.0826  452  TYR B CE2 
15795 C CZ  . TYR C 452  ? 2.3795 0.8844 1.2927 0.3128  0.6209  0.0496  452  TYR B CZ  
15796 O OH  . TYR C 452  ? 2.3369 0.9004 1.2451 0.3271  0.5698  0.0419  452  TYR B OH  
15797 N N   . ARG C 453  ? 2.5827 0.7661 1.4607 0.2466  0.8774  0.0742  453  ARG B N   
15798 C CA  . ARG C 453  ? 2.6112 0.7319 1.4775 0.2301  0.9286  0.0731  453  ARG B CA  
15799 C C   . ARG C 453  ? 2.6781 0.8065 1.5311 0.1984  0.9346  0.0381  453  ARG B C   
15800 O O   . ARG C 453  ? 2.7347 0.8896 1.5476 0.1878  0.9062  0.0061  453  ARG B O   
15801 C CB  . ARG C 453  ? 2.6881 0.7470 1.4931 0.2390  0.9481  0.0743  453  ARG B CB  
15802 C CG  . ARG C 453  ? 2.7588 0.7467 1.5513 0.2283  1.0029  0.0796  453  ARG B CG  
15803 C CD  . ARG C 453  ? 2.8811 0.8156 1.5991 0.2318  1.0166  0.0678  453  ARG B CD  
15804 N NE  . ARG C 453  ? 2.9038 0.7937 1.6220 0.2552  1.0404  0.1030  453  ARG B NE  
15805 C CZ  . ARG C 453  ? 2.9292 0.8316 1.6426 0.2799  1.0168  0.1215  453  ARG B CZ  
15806 N NH1 . ARG C 453  ? 2.9336 0.8910 1.6395 0.2853  0.9684  0.1074  453  ARG B NH1 
15807 N NH2 . ARG C 453  ? 2.9284 0.7881 1.6447 0.2996  1.0417  0.1546  453  ARG B NH2 
15808 N N   . ALA C 454  ? 2.8348 0.9399 1.7218 0.1832  0.9717  0.0445  454  ALA B N   
15809 C CA  . ALA C 454  ? 2.9702 1.0761 1.8474 0.1521  0.9815  0.0134  454  ALA B CA  
15810 C C   . ALA C 454  ? 3.0851 1.1150 1.9379 0.1394  1.0329  0.0119  454  ALA B C   
15811 O O   . ALA C 454  ? 3.0866 1.0711 1.9521 0.1530  1.0659  0.0410  454  ALA B O   
15812 C CB  . ALA C 454  ? 2.8620 1.0201 1.8054 0.1423  0.9740  0.0179  454  ALA B CB  
15813 N N   . ILE C 455  ? 3.6774 1.6932 2.4952 0.1133  1.0395  -0.0222 455  ILE B N   
15814 C CA  . ILE C 455  ? 3.7793 1.7209 2.5655 0.1018  1.0855  -0.0274 455  ILE B CA  
15815 C C   . ILE C 455  ? 3.8140 1.7523 2.6019 0.0693  1.0979  -0.0557 455  ILE B C   
15816 O O   . ILE C 455  ? 3.8362 1.8173 2.6121 0.0528  1.0668  -0.0859 455  ILE B O   
15817 C CB  . ILE C 455  ? 3.7379 1.6395 2.4481 0.1096  1.0843  -0.0425 455  ILE B CB  
15818 C CG1 . ILE C 455  ? 3.6861 1.5770 2.3951 0.1420  1.0817  -0.0097 455  ILE B CG1 
15819 C CG2 . ILE C 455  ? 3.8445 1.6736 2.5169 0.0950  1.1279  -0.0550 455  ILE B CG2 
15820 C CD1 . ILE C 455  ? 3.7869 1.6603 2.4240 0.1537  1.0659  -0.0245 455  ILE B CD1 
15821 N N   . ALA C 456  ? 2.7722 0.6578 1.5742 0.0603  1.1440  -0.0455 456  ALA B N   
15822 C CA  . ALA C 456  ? 2.8049 0.6828 1.6186 0.0297  1.1613  -0.0670 456  ALA B CA  
15823 C C   . ALA C 456  ? 2.9583 0.8018 1.7046 0.0085  1.1632  -0.1082 456  ALA B C   
15824 O O   . ALA C 456  ? 3.0231 0.8000 1.7214 0.0122  1.1919  -0.1110 456  ALA B O   
15825 C CB  . ALA C 456  ? 2.7858 0.6186 1.6384 0.0288  1.2102  -0.0407 456  ALA B CB  
15826 N N   . TYR C 457  ? 2.7812 0.6718 1.5255 -0.0131 1.1324  -0.1395 457  TYR B N   
15827 C CA  . TYR C 457  ? 2.8902 0.7559 1.5842 -0.0393 1.1338  -0.1809 457  TYR B CA  
15828 C C   . TYR C 457  ? 2.9732 0.7649 1.6616 -0.0522 1.1846  -0.1801 457  TYR B C   
15829 O O   . TYR C 457  ? 2.9606 0.7525 1.6816 -0.0760 1.1992  -0.1878 457  TYR B O   
15830 C CB  . TYR C 457  ? 2.9491 0.8796 1.6695 -0.0642 1.1021  -0.2056 457  TYR B CB  
15831 C CG  . TYR C 457  ? 3.1413 1.0515 1.8239 -0.0956 1.1040  -0.2474 457  TYR B CG  
15832 C CD1 . TYR C 457  ? 3.1940 1.1638 1.8899 -0.1180 1.0708  -0.2735 457  TYR B CD1 
15833 C CD2 . TYR C 457  ? 3.2690 1.1015 1.9030 -0.1025 1.1381  -0.2610 457  TYR B CD2 
15834 C CE1 . TYR C 457  ? 3.3159 1.2672 1.9788 -0.1475 1.0716  -0.3121 457  TYR B CE1 
15835 C CE2 . TYR C 457  ? 3.3953 1.2077 1.9950 -0.1308 1.1389  -0.3001 457  TYR B CE2 
15836 C CZ  . TYR C 457  ? 3.4062 1.2774 2.0209 -0.1539 1.1057  -0.3258 457  TYR B CZ  
15837 O OH  . TYR C 457  ? 3.5134 1.3622 2.0942 -0.1825 1.1067  -0.3649 457  TYR B OH  
15838 N N   . SER C 458  ? 3.4784 1.2070 2.1250 -0.0356 1.2116  -0.1699 458  SER B N   
15839 C CA  . SER C 458  ? 3.6017 1.2564 2.2359 -0.0444 1.2597  -0.1688 458  SER B CA  
15840 C C   . SER C 458  ? 3.7238 1.3654 2.3245 -0.0759 1.2564  -0.2129 458  SER B C   
15841 O O   . SER C 458  ? 3.7334 1.4077 2.2999 -0.0834 1.2202  -0.2431 458  SER B O   
15842 C CB  . SER C 458  ? 3.6618 1.2570 2.2469 -0.0194 1.2824  -0.1542 458  SER B CB  
15843 O OG  . SER C 458  ? 3.5623 1.1863 2.1696 0.0096  1.2683  -0.1210 458  SER B OG  
15844 N N   . SER C 459  ? 3.5163 1.1119 2.1295 -0.0943 1.2935  -0.2160 459  SER B N   
15845 C CA  . SER C 459  ? 3.6459 1.2278 2.2400 -0.1270 1.2938  -0.2550 459  SER B CA  
15846 C C   . SER C 459  ? 3.7129 1.2334 2.3258 -0.1376 1.3433  -0.2447 459  SER B C   
15847 O O   . SER C 459  ? 3.6227 1.1569 2.2989 -0.1374 1.3604  -0.2167 459  SER B O   
15848 C CB  . SER C 459  ? 3.5953 1.2539 2.2344 -0.1481 1.2582  -0.2688 459  SER B CB  
15849 O OG  . SER C 459  ? 3.6934 1.3426 2.3121 -0.1801 1.2541  -0.3081 459  SER B OG  
15850 N N   . LEU C 460  ? 4.6582 2.1110 3.2158 -0.1457 1.3665  -0.2672 460  LEU B N   
15851 C CA  . LEU C 460  ? 4.8030 2.1893 3.3705 -0.1505 1.4163  -0.2547 460  LEU B CA  
15852 C C   . LEU C 460  ? 4.8827 2.2789 3.5039 -0.1808 1.4277  -0.2609 460  LEU B C   
15853 O O   . LEU C 460  ? 4.8824 2.2490 3.5413 -0.1800 1.4648  -0.2360 460  LEU B O   
15854 C CB  . LEU C 460  ? 5.0005 2.3090 3.4925 -0.1481 1.4391  -0.2756 460  LEU B CB  
15855 C CG  . LEU C 460  ? 5.0761 2.3161 3.5726 -0.1351 1.4912  -0.2468 460  LEU B CG  
15856 C CD1 . LEU C 460  ? 5.0106 2.2465 3.5003 -0.0984 1.4978  -0.2102 460  LEU B CD1 
15857 C CD2 . LEU C 460  ? 5.2635 2.4256 3.7011 -0.1455 1.5187  -0.2740 460  LEU B CD2 
15858 N N   . SER C 461  ? 3.9938 1.4909 2.4924 0.4435  0.7567  -0.2160 461  SER B N   
15859 C CA  . SER C 461  ? 4.0672 1.5358 2.5332 0.4212  0.6936  -0.2062 461  SER B CA  
15860 C C   . SER C 461  ? 3.9305 1.4972 2.5103 0.4156  0.6843  -0.2073 461  SER B C   
15861 O O   . SER C 461  ? 3.9397 1.5024 2.5101 0.3938  0.6337  -0.1974 461  SER B O   
15862 C CB  . SER C 461  ? 4.1362 1.5701 2.5217 0.3724  0.6502  -0.1776 461  SER B CB  
15863 O OG  . SER C 461  ? 4.3106 1.6258 2.5697 0.3753  0.6261  -0.1771 461  SER B OG  
15864 N N   . GLN C 462  ? 3.4103 1.0651 2.0968 0.4348  0.7334  -0.2192 462  GLN B N   
15865 C CA  . GLN C 462  ? 3.2510 1.0076 2.0543 0.4318  0.7319  -0.2219 462  GLN B CA  
15866 C C   . GLN C 462  ? 3.1767 0.9943 2.0034 0.3812  0.6997  -0.1959 462  GLN B C   
15867 O O   . GLN C 462  ? 3.0813 0.9921 2.0053 0.3717  0.6971  -0.1948 462  GLN B O   
15868 C CB  . GLN C 462  ? 3.2846 1.0145 2.0919 0.4520  0.7017  -0.2357 462  GLN B CB  
15869 C CG  . GLN C 462  ? 3.2890 1.0259 2.1493 0.5050  0.7449  -0.2663 462  GLN B CG  
15870 C CD  . GLN C 462  ? 3.1724 1.0298 2.1702 0.5153  0.7870  -0.2752 462  GLN B CD  
15871 O OE1 . GLN C 462  ? 3.0882 1.0217 2.1389 0.4850  0.7913  -0.2593 462  GLN B OE1 
15872 N NE2 . GLN C 462  ? 3.1685 1.0431 2.2248 0.5587  0.8176  -0.3015 462  GLN B NE2 
15873 N N   . SER C 463  ? 3.6640 1.4291 2.4004 0.3494  0.6757  -0.1756 463  SER B N   
15874 C CA  . SER C 463  ? 3.5761 1.3827 2.3136 0.2990  0.6373  -0.1500 463  SER B CA  
15875 C C   . SER C 463  ? 3.3958 1.2932 2.2060 0.2817  0.6698  -0.1413 463  SER B C   
15876 O O   . SER C 463  ? 3.4262 1.3096 2.2219 0.2940  0.7105  -0.1440 463  SER B O   
15877 C CB  . SER C 463  ? 3.7157 1.4235 2.3222 0.2730  0.5975  -0.1326 463  SER B CB  
15878 O OG  . SER C 463  ? 3.6883 1.4357 2.2908 0.2245  0.5694  -0.1078 463  SER B OG  
15879 N N   . TYR C 464  ? 3.1071 1.0962 1.9931 0.2526  0.6507  -0.1305 464  TYR B N   
15880 C CA  . TYR C 464  ? 2.9505 1.0259 1.9034 0.2321  0.6745  -0.1208 464  TYR B CA  
15881 C C   . TYR C 464  ? 2.9066 1.0171 1.8497 0.1812  0.6281  -0.0971 464  TYR B C   
15882 O O   . TYR C 464  ? 2.9620 1.0283 1.8430 0.1600  0.5774  -0.0866 464  TYR B O   
15883 C CB  . TYR C 464  ? 2.8167 0.9963 1.9047 0.2541  0.7130  -0.1368 464  TYR B CB  
15884 C CG  . TYR C 464  ? 2.8675 1.0180 1.9726 0.3038  0.7466  -0.1621 464  TYR B CG  
15885 C CD1 . TYR C 464  ? 2.9529 1.0381 2.0059 0.3322  0.7849  -0.1718 464  TYR B CD1 
15886 C CD2 . TYR C 464  ? 2.8383 1.0254 2.0092 0.3227  0.7395  -0.1767 464  TYR B CD2 
15887 C CE1 . TYR C 464  ? 3.0065 1.0653 2.0742 0.3788  0.8162  -0.1964 464  TYR B CE1 
15888 C CE2 . TYR C 464  ? 2.8972 1.0574 2.0840 0.3696  0.7700  -0.2012 464  TYR B CE2 
15889 C CZ  . TYR C 464  ? 2.9833 1.0799 2.1187 0.3977  0.8087  -0.2113 464  TYR B CZ  
15890 O OH  . TYR C 464  ? 3.0246 1.0961 2.1757 0.4447  0.8399  -0.2368 464  TYR B OH  
15891 N N   . LEU C 465  ? 2.7674 0.9576 1.7720 0.1614  0.6455  -0.0886 465  LEU B N   
15892 C CA  . LEU C 465  ? 2.7104 0.9543 1.7269 0.1144  0.6055  -0.0687 465  LEU B CA  
15893 C C   . LEU C 465  ? 2.5876 0.9560 1.7342 0.1120  0.6335  -0.0730 465  LEU B C   
15894 O O   . LEU C 465  ? 2.5607 0.9579 1.7671 0.1422  0.6849  -0.0873 465  LEU B O   
15895 C CB  . LEU C 465  ? 2.7600 0.9494 1.6813 0.0835  0.5886  -0.0486 465  LEU B CB  
15896 C CG  . LEU C 465  ? 2.7479 0.9545 1.6379 0.0331  0.5335  -0.0264 465  LEU B CG  
15897 C CD1 . LEU C 465  ? 2.8832 0.9988 1.6742 0.0251  0.4862  -0.0204 465  LEU B CD1 
15898 C CD2 . LEU C 465  ? 2.7800 0.9819 1.6290 0.0050  0.5344  -0.0098 465  LEU B CD2 
15899 N N   . TYR C 466  ? 2.6660 1.1079 1.8562 0.0764  0.5992  -0.0614 466  TYR B N   
15900 C CA  . TYR C 466  ? 2.4833 1.0462 1.7904 0.0652  0.6164  -0.0624 466  TYR B CA  
15901 C C   . TYR C 466  ? 2.5203 1.1225 1.8162 0.0161  0.5681  -0.0427 466  TYR B C   
15902 O O   . TYR C 466  ? 2.5453 1.1399 1.8169 -0.0013 0.5239  -0.0367 466  TYR B O   
15903 C CB  . TYR C 466  ? 2.4117 1.0505 1.8304 0.0907  0.6330  -0.0813 466  TYR B CB  
15904 C CG  . TYR C 466  ? 2.2900 1.0578 1.8302 0.0754  0.6417  -0.0823 466  TYR B CG  
15905 C CD1 . TYR C 466  ? 2.3623 1.1723 1.9128 0.0453  0.6410  -0.0688 466  TYR B CD1 
15906 C CD2 . TYR C 466  ? 2.2844 1.1319 1.9302 0.0923  0.6506  -0.0977 466  TYR B CD2 
15907 C CE1 . TYR C 466  ? 2.2322 1.1601 1.8947 0.0323  0.6482  -0.0709 466  TYR B CE1 
15908 C CE2 . TYR C 466  ? 2.1601 1.1265 1.9185 0.0791  0.6584  -0.0998 466  TYR B CE2 
15909 C CZ  . TYR C 466  ? 2.1198 1.1262 1.8863 0.0490  0.6569  -0.0866 466  TYR B CZ  
15910 O OH  . TYR C 466  ? 2.0336 1.1567 1.9104 0.0360  0.6634  -0.0894 466  TYR B OH  
15911 N N   . ILE C 467  ? 2.5533 1.1973 1.8660 -0.0066 0.5763  -0.0324 467  ILE B N   
15912 C CA  . ILE C 467  ? 2.5209 1.2164 1.8364 -0.0526 0.5343  -0.0156 467  ILE B CA  
15913 C C   . ILE C 467  ? 2.3944 1.2179 1.8385 -0.0586 0.5533  -0.0213 467  ILE B C   
15914 O O   . ILE C 467  ? 2.3253 1.1793 1.8297 -0.0348 0.6007  -0.0319 467  ILE B O   
15915 C CB  . ILE C 467  ? 2.5761 1.2076 1.7891 -0.0812 0.5158  0.0036  467  ILE B CB  
15916 C CG1 . ILE C 467  ? 2.5552 1.2232 1.8046 -0.0812 0.5527  0.0050  467  ILE B CG1 
15917 C CG2 . ILE C 467  ? 2.7230 1.2242 1.8160 -0.0650 0.5117  0.0048  467  ILE B CG2 
15918 C CD1 . ILE C 467  ? 2.6089 1.2335 1.7713 -0.1150 0.5293  0.0248  467  ILE B CD1 
15919 N N   . ASP C 468  ? 2.1931 1.0906 1.6787 -0.0900 0.5159  -0.0148 468  ASP B N   
15920 C CA  . ASP C 468  ? 2.0836 1.1072 1.6881 -0.1015 0.5252  -0.0193 468  ASP B CA  
15921 C C   . ASP C 468  ? 2.0924 1.1592 1.6809 -0.1511 0.4779  -0.0019 468  ASP B C   
15922 O O   . ASP C 468  ? 2.1717 1.1685 1.6567 -0.1758 0.4461  0.0146  468  ASP B O   
15923 C CB  . ASP C 468  ? 2.0970 1.1913 1.8039 -0.0783 0.5365  -0.0373 468  ASP B CB  
15924 C CG  . ASP C 468  ? 1.8853 1.0846 1.7209 -0.0644 0.5769  -0.0509 468  ASP B CG  
15925 O OD1 . ASP C 468  ? 1.8772 1.0953 1.7262 -0.0716 0.5973  -0.0466 468  ASP B OD1 
15926 O OD2 . ASP C 468  ? 1.8425 1.1053 1.7672 -0.0458 0.5876  -0.0661 468  ASP B OD2 
15927 N N   . TRP C 469  ? 2.6801 1.8635 2.3728 -0.1648 0.4747  -0.0064 469  TRP B N   
15928 C CA  . TRP C 469  ? 2.7813 2.0268 2.4799 -0.2102 0.4328  0.0067  469  TRP B CA  
15929 C C   . TRP C 469  ? 2.8188 2.1957 2.6552 -0.2084 0.4484  -0.0064 469  TRP B C   
15930 O O   . TRP C 469  ? 2.7470 2.1527 2.6580 -0.1752 0.4934  -0.0222 469  TRP B O   
15931 C CB  . TRP C 469  ? 2.7967 2.0068 2.4269 -0.2361 0.4251  0.0226  469  TRP B CB  
15932 C CG  . TRP C 469  ? 2.6930 1.9516 2.3848 -0.2294 0.4635  0.0180  469  TRP B CG  
15933 C CD1 . TRP C 469  ? 2.6626 1.9714 2.3673 -0.2607 0.4506  0.0274  469  TRP B CD1 
15934 C CD2 . TRP C 469  ? 2.6377 1.8948 2.3810 -0.1903 0.5189  0.0041  469  TRP B CD2 
15935 N NE1 . TRP C 469  ? 2.5764 1.9133 2.3372 -0.2434 0.4929  0.0204  469  TRP B NE1 
15936 C CE2 . TRP C 469  ? 2.5685 1.8752 2.3538 -0.2011 0.5354  0.0068  469  TRP B CE2 
15937 C CE3 . TRP C 469  ? 2.6473 1.8674 2.4061 -0.1476 0.5555  -0.0104 469  TRP B CE3 
15938 C CZ2 . TRP C 469  ? 2.5158 1.8341 2.3562 -0.1717 0.5866  -0.0033 469  TRP B CZ2 
15939 C CZ3 . TRP C 469  ? 2.5784 1.8128 2.3926 -0.1187 0.6075  -0.0210 469  TRP B CZ3 
15940 C CH2 . TRP C 469  ? 2.5131 1.7954 2.3668 -0.1313 0.6223  -0.0168 469  TRP B CH2 
15941 N N   . THR C 470  ? 2.9413 2.4003 2.8155 -0.2425 0.4127  -0.0012 470  THR B N   
15942 C CA  . THR C 470  ? 2.9620 2.5455 2.9659 -0.2410 0.4303  -0.0141 470  THR B CA  
15943 C C   . THR C 470  ? 3.1277 2.7879 3.1568 -0.2808 0.4056  -0.0055 470  THR B C   
15944 O O   . THR C 470  ? 3.2185 2.8719 3.1888 -0.3172 0.3607  0.0092  470  THR B O   
15945 C CB  . THR C 470  ? 2.8605 2.5109 2.9497 -0.2254 0.4300  -0.0289 470  THR B CB  
15946 O OG1 . THR C 470  ? 2.8790 2.4563 2.9447 -0.1867 0.4541  -0.0379 470  THR B OG1 
15947 C CG2 . THR C 470  ? 2.6858 2.4545 2.9114 -0.2150 0.4591  -0.0453 470  THR B CG2 
15948 N N   . ASP C 471  ? 2.3190 2.0498 2.4361 -0.2721 0.4369  -0.0154 471  ASP B N   
15949 C CA  . ASP C 471  ? 2.4790 2.3086 2.6571 -0.3018 0.4219  -0.0143 471  ASP B CA  
15950 C C   . ASP C 471  ? 2.5116 2.4461 2.8311 -0.2789 0.4567  -0.0350 471  ASP B C   
15951 O O   . ASP C 471  ? 2.4726 2.3846 2.8241 -0.2434 0.5017  -0.0452 471  ASP B O   
15952 C CB  . ASP C 471  ? 2.5979 2.3840 2.7163 -0.3171 0.4243  -0.0016 471  ASP B CB  
15953 C CG  . ASP C 471  ? 2.6806 2.5481 2.8234 -0.3587 0.3914  0.0051  471  ASP B CG  
15954 O OD1 . ASP C 471  ? 2.7746 2.6567 2.8778 -0.3932 0.3450  0.0154  471  ASP B OD1 
15955 O OD2 . ASP C 471  ? 2.6627 2.5726 2.8552 -0.3586 0.4109  0.0014  471  ASP B OD2 
15956 N N   . ASN C 472  ? 4.1707 4.2190 4.5729 -0.3000 0.4357  -0.0409 472  ASN B N   
15957 C CA  . ASN C 472  ? 4.1676 4.3258 4.7074 -0.2835 0.4624  -0.0606 472  ASN B CA  
15958 C C   . ASN C 472  ? 4.1962 4.3927 4.7849 -0.2844 0.4860  -0.0634 472  ASN B C   
15959 O O   . ASN C 472  ? 4.0954 4.3637 4.7915 -0.2644 0.5161  -0.0797 472  ASN B O   
15960 C CB  . ASN C 472  ? 4.1201 4.3874 4.7328 -0.3031 0.4310  -0.0680 472  ASN B CB  
15961 C CG  . ASN C 472  ? 4.1438 4.4407 4.7131 -0.3506 0.3819  -0.0538 472  ASN B CG  
15962 O OD1 . ASN C 472  ? 4.1947 4.4339 4.6825 -0.3697 0.3703  -0.0387 472  ASN B OD1 
15963 N ND2 . ASN C 472  ? 4.1062 4.4954 4.7307 -0.3698 0.3530  -0.0590 472  ASN B ND2 
15964 N N   . HIS C 473  ? 2.9840 3.1305 3.4930 -0.3073 0.4717  -0.0473 473  HIS B N   
15965 C CA  . HIS C 473  ? 3.0413 3.2137 3.5840 -0.3102 0.4905  -0.0475 473  HIS B CA  
15966 C C   . HIS C 473  ? 2.8969 2.9694 3.3801 -0.2871 0.5267  -0.0413 473  HIS B C   
15967 O O   . HIS C 473  ? 2.9798 2.9462 3.3515 -0.2866 0.5204  -0.0285 473  HIS B O   
15968 C CB  . HIS C 473  ? 3.3543 3.5592 3.8664 -0.3533 0.4499  -0.0358 473  HIS B CB  
15969 C CG  . HIS C 473  ? 3.6588 3.9021 4.1525 -0.3840 0.4022  -0.0313 473  HIS B CG  
15970 N ND1 . HIS C 473  ? 3.8636 4.0228 4.2411 -0.4011 0.3713  -0.0147 473  HIS B ND1 
15971 C CD2 . HIS C 473  ? 3.7390 4.0945 4.3116 -0.4024 0.3783  -0.0403 473  HIS B CD2 
15972 C CE1 . HIS C 473  ? 4.0706 4.2890 4.4583 -0.4287 0.3317  -0.0131 473  HIS B CE1 
15973 N NE2 . HIS C 473  ? 3.8809 4.2195 4.3855 -0.4301 0.3352  -0.0286 473  HIS B NE2 
15974 N N   . LYS C 474  ? 3.6656 3.7753 4.2240 -0.2697 0.5630  -0.0501 474  LYS B N   
15975 C CA  . LYS C 474  ? 3.5357 3.5675 4.0622 -0.2428 0.6053  -0.0475 474  LYS B CA  
15976 C C   . LYS C 474  ? 3.4704 3.4090 3.8751 -0.2614 0.5909  -0.0274 474  LYS B C   
15977 O O   . LYS C 474  ? 3.5241 3.3819 3.8771 -0.2426 0.6206  -0.0219 474  LYS B O   
15978 C CB  . LYS C 474  ? 3.4714 3.5728 4.1047 -0.2291 0.6393  -0.0585 474  LYS B CB  
15979 C CG  . LYS C 474  ? 3.4571 3.6460 4.1424 -0.2594 0.6139  -0.0582 474  LYS B CG  
15980 C CD  . LYS C 474  ? 3.3875 3.6305 4.1691 -0.2440 0.6487  -0.0678 474  LYS B CD  
15981 C CE  . LYS C 474  ? 3.4388 3.5917 4.1546 -0.2333 0.6767  -0.0555 474  LYS B CE  
15982 N NZ  . LYS C 474  ? 3.3619 3.5649 4.1697 -0.2198 0.7097  -0.0632 474  LYS B NZ  
15983 N N   . ALA C 475  ? 2.9144 2.8650 3.2727 -0.2985 0.5449  -0.0165 475  ALA B N   
15984 C CA  . ALA C 475  ? 2.7925 2.6554 3.0322 -0.3183 0.5269  0.0026  475  ALA B CA  
15985 C C   . ALA C 475  ? 2.6693 2.5256 2.8430 -0.3524 0.4748  0.0131  475  ALA B C   
15986 O O   . ALA C 475  ? 2.6034 2.5434 2.8372 -0.3662 0.4513  0.0059  475  ALA B O   
15987 C CB  . ALA C 475  ? 2.7686 2.6595 3.0301 -0.3311 0.5326  0.0070  475  ALA B CB  
15988 N N   . LEU C 476  ? 2.4122 2.1674 2.4622 -0.3648 0.4581  0.0299  476  LEU B N   
15989 C CA  . LEU C 476  ? 2.3371 2.0691 2.3117 -0.3955 0.4105  0.0415  476  LEU B CA  
15990 C C   . LEU C 476  ? 2.3254 2.0437 2.2426 -0.4279 0.3861  0.0561  476  LEU B C   
15991 O O   . LEU C 476  ? 2.4057 2.0395 2.2465 -0.4234 0.3981  0.0661  476  LEU B O   
15992 C CB  . LEU C 476  ? 2.3202 1.9384 2.1980 -0.3787 0.4131  0.0474  476  LEU B CB  
15993 C CG  . LEU C 476  ? 2.1980 1.7834 2.1107 -0.3313 0.4652  0.0344  476  LEU B CG  
15994 C CD1 . LEU C 476  ? 2.2706 1.7392 2.0787 -0.3168 0.4656  0.0406  476  LEU B CD1 
15995 C CD2 . LEU C 476  ? 2.1048 1.7740 2.1339 -0.3090 0.4844  0.0154  476  LEU B CD2 
15996 N N   . LEU C 477  ? 2.5029 2.3111 2.4636 -0.4598 0.3529  0.0558  477  LEU B N   
15997 C CA  . LEU C 477  ? 2.4684 2.2909 2.4018 -0.4906 0.3305  0.0658  477  LEU B CA  
15998 C C   . LEU C 477  ? 2.4982 2.2150 2.2928 -0.5105 0.3025  0.0852  477  LEU B C   
15999 O O   . LEU C 477  ? 2.5562 2.2094 2.2889 -0.5057 0.2928  0.0897  477  LEU B O   
16000 C CB  . LEU C 477  ? 2.4774 2.4222 2.4868 -0.5203 0.2978  0.0597  477  LEU B CB  
16001 C CG  . LEU C 477  ? 2.4408 2.4812 2.5794 -0.4974 0.3204  0.0391  477  LEU B CG  
16002 C CD1 . LEU C 477  ? 2.4531 2.6104 2.6605 -0.5253 0.2860  0.0322  477  LEU B CD1 
16003 C CD2 . LEU C 477  ? 2.3770 2.4478 2.5976 -0.4700 0.3645  0.0275  477  LEU B CD2 
16004 N N   . VAL C 478  ? 2.0303 1.7250 1.7760 -0.5312 0.2905  0.0963  478  VAL B N   
16005 C CA  . VAL C 478  ? 2.1650 1.7643 1.7802 -0.5532 0.2618  0.1148  478  VAL B CA  
16006 C C   . VAL C 478  ? 2.2180 1.8585 1.8120 -0.5929 0.2101  0.1217  478  VAL B C   
16007 O O   . VAL C 478  ? 2.1436 1.8908 1.8139 -0.6131 0.1930  0.1154  478  VAL B O   
16008 C CB  . VAL C 478  ? 2.1988 1.7692 1.7735 -0.5644 0.2638  0.1242  478  VAL B CB  
16009 C CG1 . VAL C 478  ? 2.2002 1.8637 1.8145 -0.6017 0.2294  0.1252  478  VAL B CG1 
16010 C CG2 . VAL C 478  ? 2.3152 1.7581 1.7497 -0.5711 0.2515  0.1413  478  VAL B CG2 
16011 N N   . GLY C 479  ? 1.8749 1.4294 1.3624 -0.6051 0.1845  0.1350  479  GLY B N   
16012 C CA  . GLY C 479  ? 1.9728 1.5563 1.4320 -0.6423 0.1353  0.1431  479  GLY B CA  
16013 C C   . GLY C 479  ? 1.9847 1.5681 1.4581 -0.6305 0.1311  0.1381  479  GLY B C   
16014 O O   . GLY C 479  ? 2.0856 1.6334 1.4904 -0.6530 0.0946  0.1494  479  GLY B O   
16015 N N   . GLU C 480  ? 2.5976 2.2206 2.1608 -0.5954 0.1681  0.1214  480  GLU B N   
16016 C CA  . GLU C 480  ? 2.5740 2.2035 2.1639 -0.5792 0.1689  0.1141  480  GLU B CA  
16017 C C   . GLU C 480  ? 2.6690 2.1717 2.1456 -0.5705 0.1617  0.1248  480  GLU B C   
16018 O O   . GLU C 480  ? 2.7429 2.1565 2.1178 -0.5809 0.1516  0.1385  480  GLU B O   
16019 C CB  . GLU C 480  ? 2.4983 2.1758 2.1950 -0.5385 0.2158  0.0943  480  GLU B CB  
16020 C CG  . GLU C 480  ? 2.5026 2.3201 2.3232 -0.5478 0.2115  0.0809  480  GLU B CG  
16021 C CD  . GLU C 480  ? 2.5031 2.3693 2.4321 -0.5070 0.2554  0.0606  480  GLU B CD  
16022 O OE1 . GLU C 480  ? 2.4553 2.4186 2.4783 -0.5060 0.2516  0.0478  480  GLU B OE1 
16023 O OE2 . GLU C 480  ? 2.5356 2.3443 2.4585 -0.4745 0.2955  0.0566  480  GLU B OE2 
16024 N N   . HIS C 481  ? 2.7614 2.2549 2.2557 -0.5504 0.1665  0.1178  481  HIS B N   
16025 C CA  . HIS C 481  ? 2.8911 2.2659 2.2828 -0.5399 0.1590  0.1261  481  HIS B CA  
16026 C C   . HIS C 481  ? 2.8028 2.1532 2.2326 -0.4942 0.1965  0.1114  481  HIS B C   
16027 O O   . HIS C 481  ? 2.7107 2.1384 2.2319 -0.4828 0.2040  0.0986  481  HIS B O   
16028 C CB  . HIS C 481  ? 3.0663 2.4360 2.4037 -0.5756 0.1059  0.1393  481  HIS B CB  
16029 C CG  . HIS C 481  ? 3.2238 2.5647 2.4772 -0.6168 0.0692  0.1576  481  HIS B CG  
16030 N ND1 . HIS C 481  ? 3.3706 2.5900 2.5031 -0.6191 0.0610  0.1709  481  HIS B ND1 
16031 C CD2 . HIS C 481  ? 3.2057 2.6235 2.4776 -0.6571 0.0384  0.1643  481  HIS B CD2 
16032 C CE1 . HIS C 481  ? 3.4241 2.6465 2.5052 -0.6591 0.0267  0.1853  481  HIS B CE1 
16033 N NE2 . HIS C 481  ? 3.3143 2.6570 2.4784 -0.6830 0.0124  0.1816  481  HIS B NE2 
16034 N N   . LEU C 482  ? 2.6744 1.9178 2.0342 -0.4677 0.2207  0.1125  482  LEU B N   
16035 C CA  . LEU C 482  ? 2.6340 1.8523 2.0296 -0.4220 0.2607  0.0973  482  LEU B CA  
16036 C C   . LEU C 482  ? 2.7174 1.8705 2.0616 -0.4113 0.2436  0.0978  482  LEU B C   
16037 O O   . LEU C 482  ? 2.8457 1.8887 2.0803 -0.4109 0.2310  0.1076  482  LEU B O   
16038 C CB  . LEU C 482  ? 2.6178 1.7670 1.9828 -0.3930 0.3037  0.0944  482  LEU B CB  
16039 C CG  . LEU C 482  ? 2.4974 1.6761 1.9520 -0.3483 0.3551  0.0748  482  LEU B CG  
16040 C CD1 . LEU C 482  ? 2.4381 1.5966 1.8985 -0.3297 0.3975  0.0724  482  LEU B CD1 
16041 C CD2 . LEU C 482  ? 2.5459 1.6574 1.9708 -0.3175 0.3634  0.0672  482  LEU B CD2 
16042 N N   . ASN C 483  ? 2.9338 2.1560 2.3593 -0.4018 0.2431  0.0866  483  ASN B N   
16043 C CA  . ASN C 483  ? 2.9737 2.1415 2.3692 -0.3835 0.2346  0.0833  483  ASN B CA  
16044 C C   . ASN C 483  ? 2.9142 2.0431 2.3366 -0.3325 0.2833  0.0664  483  ASN B C   
16045 O O   . ASN C 483  ? 2.8176 2.0248 2.3480 -0.3097 0.3136  0.0499  483  ASN B O   
16046 C CB  . ASN C 483  ? 2.9762 2.2311 2.4391 -0.3980 0.2077  0.0802  483  ASN B CB  
16047 C CG  . ASN C 483  ? 3.0992 2.2843 2.4980 -0.3955 0.1795  0.0852  483  ASN B CG  
16048 O OD1 . ASN C 483  ? 3.2182 2.3065 2.5051 -0.4095 0.1533  0.0997  483  ASN B OD1 
16049 N ND2 . ASN C 483  ? 3.0645 2.2962 2.5331 -0.3772 0.1839  0.0731  483  ASN B ND2 
16050 N N   . ILE C 484  ? 2.6123 1.6211 1.9355 -0.3156 0.2891  0.0702  484  ILE B N   
16051 C CA  . ILE C 484  ? 2.5434 1.4976 1.8716 -0.2674 0.3330  0.0551  484  ILE B CA  
16052 C C   . ILE C 484  ? 2.5734 1.4473 1.8434 -0.2499 0.3172  0.0527  484  ILE B C   
16053 O O   . ILE C 484  ? 2.6786 1.4741 1.8465 -0.2696 0.2793  0.0667  484  ILE B O   
16054 C CB  . ILE C 484  ? 2.5654 1.4449 1.8313 -0.2550 0.3618  0.0581  484  ILE B CB  
16055 C CG1 . ILE C 484  ? 2.5914 1.3798 1.8169 -0.2113 0.3921  0.0468  484  ILE B CG1 
16056 C CG2 . ILE C 484  ? 2.6641 1.4868 1.8242 -0.2932 0.3234  0.0790  484  ILE B CG2 
16057 C CD1 . ILE C 484  ? 2.6502 1.3231 1.7584 -0.2079 0.3962  0.0556  484  ILE B CD1 
16058 N N   . ILE C 485  ? 2.6402 1.5344 1.9775 -0.2122 0.3466  0.0343  485  ILE B N   
16059 C CA  . ILE C 485  ? 2.6942 1.5279 1.9973 -0.1915 0.3344  0.0287  485  ILE B CA  
16060 C C   . ILE C 485  ? 2.7873 1.5198 2.0326 -0.1525 0.3681  0.0197  485  ILE B C   
16061 O O   . ILE C 485  ? 2.7448 1.4947 2.0394 -0.1239 0.4167  0.0071  485  ILE B O   
16062 C CB  . ILE C 485  ? 2.5806 1.5001 1.9954 -0.1720 0.3457  0.0124  485  ILE B CB  
16063 C CG1 . ILE C 485  ? 2.5584 1.5511 2.0021 -0.2101 0.2987  0.0224  485  ILE B CG1 
16064 C CG2 . ILE C 485  ? 2.6460 1.4968 2.0403 -0.1323 0.3577  -0.0007 485  ILE B CG2 
16065 C CD1 . ILE C 485  ? 2.5065 1.6064 2.0182 -0.2409 0.2964  0.0272  485  ILE B CD1 
16066 N N   . VAL C 486  ? 2.3836 1.0116 1.5254 -0.1516 0.3412  0.0260  486  VAL B N   
16067 C CA  . VAL C 486  ? 2.4582 0.9764 1.5216 -0.1207 0.3646  0.0201  486  VAL B CA  
16068 C C   . VAL C 486  ? 2.4996 0.9760 1.5639 -0.0857 0.3674  0.0053  486  VAL B C   
16069 O O   . VAL C 486  ? 2.5804 0.9762 1.5611 -0.0905 0.3325  0.0116  486  VAL B O   
16070 C CB  . VAL C 486  ? 2.5674 0.9882 1.4996 -0.1482 0.3279  0.0391  486  VAL B CB  
16071 C CG1 . VAL C 486  ? 2.6603 0.9634 1.5065 -0.1155 0.3481  0.0320  486  VAL B CG1 
16072 C CG2 . VAL C 486  ? 2.5641 1.0220 1.4898 -0.1832 0.3235  0.0539  486  VAL B CG2 
16073 N N   . THR C 487  ? 3.1604 1.6921 2.3205 -0.0506 0.4081  -0.0145 487  THR B N   
16074 C CA  . THR C 487  ? 3.1788 1.6857 2.3548 -0.0172 0.4105  -0.0300 487  THR B CA  
16075 C C   . THR C 487  ? 3.2600 1.6662 2.3745 0.0232  0.4411  -0.0426 487  THR B C   
16076 O O   . THR C 487  ? 3.1836 1.6116 2.3532 0.0566  0.4919  -0.0587 487  THR B O   
16077 C CB  . THR C 487  ? 3.0823 1.6993 2.3947 0.0029  0.4398  -0.0470 487  THR B CB  
16078 O OG1 . THR C 487  ? 3.0091 1.6644 2.3780 0.0218  0.4929  -0.0566 487  THR B OG1 
16079 C CG2 . THR C 487  ? 3.0012 1.7190 2.3762 -0.0349 0.4068  -0.0368 487  THR B CG2 
16080 N N   . PRO C 488  ? 2.6712 0.9672 1.6719 0.0208  0.4101  -0.0357 488  PRO B N   
16081 C CA  . PRO C 488  ? 2.7651 0.9628 1.7005 0.0582  0.4385  -0.0479 488  PRO B CA  
16082 C C   . PRO C 488  ? 2.8324 1.0279 1.8177 0.1049  0.4638  -0.0718 488  PRO B C   
16083 O O   . PRO C 488  ? 2.8491 0.9634 1.7816 0.1379  0.4849  -0.0840 488  PRO B O   
16084 C CB  . PRO C 488  ? 2.8865 0.9737 1.6909 0.0388  0.3907  -0.0335 488  PRO B CB  
16085 C CG  . PRO C 488  ? 2.8711 1.0023 1.6700 -0.0128 0.3430  -0.0111 488  PRO B CG  
16086 C CD  . PRO C 488  ? 2.7425 0.9973 1.6665 -0.0166 0.3488  -0.0165 488  PRO B CD  
16087 N N   . LYS C 489  ? 3.3564 1.6413 2.4419 0.1073  0.4619  -0.0789 489  LYS B N   
16088 C CA  . LYS C 489  ? 3.5016 1.7942 2.6427 0.1489  0.4803  -0.1012 489  LYS B CA  
16089 C C   . LYS C 489  ? 3.6680 1.8844 2.7741 0.1956  0.5205  -0.1204 489  LYS B C   
16090 O O   . LYS C 489  ? 3.6626 1.8786 2.7726 0.2081  0.5634  -0.1248 489  LYS B O   
16091 C CB  . LYS C 489  ? 3.3857 1.8063 2.6664 0.1553  0.5075  -0.1116 489  LYS B CB  
16092 C CG  . LYS C 489  ? 3.3795 1.8189 2.7279 0.1975  0.5271  -0.1351 489  LYS B CG  
16093 C CD  . LYS C 489  ? 3.2874 1.8542 2.7640 0.1914  0.5315  -0.1400 489  LYS B CD  
16094 C CE  . LYS C 489  ? 3.2875 1.8723 2.8280 0.2303  0.5437  -0.1622 489  LYS B CE  
16095 N NZ  . LYS C 489  ? 3.4193 1.9335 2.8943 0.2310  0.4972  -0.1597 489  LYS B NZ  
16096 N N   . SER C 490  ? 3.7045 1.8572 2.7760 0.2207  0.5048  -0.1317 490  SER B N   
16097 C CA  . SER C 490  ? 3.8190 1.9091 2.8718 0.2700  0.5410  -0.1544 490  SER B CA  
16098 C C   . SER C 490  ? 4.0064 1.9623 2.9258 0.2776  0.5219  -0.1527 490  SER B C   
16099 O O   . SER C 490  ? 4.1063 2.0020 2.9934 0.3010  0.5042  -0.1640 490  SER B O   
16100 C CB  . SER C 490  ? 3.7691 1.9136 2.8938 0.2949  0.6058  -0.1680 490  SER B CB  
16101 O OG  . SER C 490  ? 3.6582 1.9202 2.9099 0.2956  0.6223  -0.1743 490  SER B OG  
16102 N N   . PRO C 491  ? 3.7950 1.7034 2.6370 0.2581  0.5235  -0.1389 491  PRO B N   
16103 C CA  . PRO C 491  ? 3.8887 1.6705 2.6070 0.2685  0.5087  -0.1397 491  PRO B CA  
16104 C C   . PRO C 491  ? 3.8404 1.5581 2.5216 0.2858  0.4732  -0.1486 491  PRO B C   
16105 O O   . PRO C 491  ? 3.8003 1.5301 2.4811 0.2593  0.4248  -0.1360 491  PRO B O   
16106 C CB  . PRO C 491  ? 3.9922 1.7477 2.6340 0.2198  0.4724  -0.1123 491  PRO B CB  
16107 C CG  . PRO C 491  ? 3.8927 1.7527 2.6166 0.2007  0.5025  -0.1045 491  PRO B CG  
16108 C CD  . PRO C 491  ? 3.7595 1.7209 2.6153 0.2235  0.5317  -0.1211 491  PRO B CD  
16109 N N   . TYR C 492  ? 4.0545 1.7071 2.7076 0.3305  0.4981  -0.1708 492  TYR B N   
16110 C CA  . TYR C 492  ? 4.0927 1.6869 2.7193 0.3531  0.4697  -0.1830 492  TYR B CA  
16111 C C   . TYR C 492  ? 4.1753 1.7202 2.7248 0.3123  0.4030  -0.1598 492  TYR B C   
16112 O O   . TYR C 492  ? 4.2367 1.7622 2.7840 0.3150  0.3662  -0.1615 492  TYR B O   
16113 C CB  . TYR C 492  ? 4.1884 1.6871 2.7501 0.3972  0.4934  -0.2046 492  TYR B CB  
16114 C CG  . TYR C 492  ? 4.2922 1.6835 2.7234 0.3834  0.4732  -0.1938 492  TYR B CG  
16115 C CD1 . TYR C 492  ? 4.4003 1.6887 2.7537 0.4186  0.4777  -0.2116 492  TYR B CD1 
16116 C CD2 . TYR C 492  ? 4.2668 1.6600 2.6529 0.3363  0.4501  -0.1669 492  TYR B CD2 
16117 C CE1 . TYR C 492  ? 4.5103 1.6995 2.7434 0.4069  0.4594  -0.2027 492  TYR B CE1 
16118 C CE2 . TYR C 492  ? 4.3772 1.6719 2.6437 0.3237  0.4314  -0.1572 492  TYR B CE2 
16119 C CZ  . TYR C 492  ? 4.5081 1.7005 2.6980 0.3591  0.4363  -0.1751 492  TYR B CZ  
16120 O OH  . TYR C 492  ? 4.6496 1.7445 2.7208 0.3472  0.4177  -0.1663 492  TYR B OH  
16121 N N   . ILE C 493  ? 3.7541 1.2801 2.2413 0.2736  0.3865  -0.1374 493  ILE B N   
16122 C CA  . ILE C 493  ? 3.8771 1.3693 2.2992 0.2291  0.3222  -0.1130 493  ILE B CA  
16123 C C   . ILE C 493  ? 3.8854 1.4264 2.3018 0.1763  0.3049  -0.0859 493  ILE B C   
16124 O O   . ILE C 493  ? 3.8343 1.4204 2.2786 0.1716  0.3417  -0.0838 493  ILE B O   
16125 C CB  . ILE C 493  ? 4.9141 2.2694 3.2122 0.2377  0.2847  -0.1142 493  ILE B CB  
16126 C CG1 . ILE C 493  ? 4.9470 2.2847 3.2579 0.2489  0.2474  -0.1204 493  ILE B CG1 
16127 C CG2 . ILE C 493  ? 5.0047 2.3059 3.2043 0.1916  0.2423  -0.0878 493  ILE B CG2 
16128 C CD1 . ILE C 493  ? 5.1216 2.3318 3.3162 0.2499  0.2000  -0.1179 493  ILE B CD1 
16129 N N   . ASP C 494  ? 4.2516 1.7838 2.6335 0.1373  0.2472  -0.0656 494  ASP B N   
16130 C CA  . ASP C 494  ? 4.2132 1.8009 2.5983 0.0842  0.2201  -0.0397 494  ASP B CA  
16131 C C   . ASP C 494  ? 4.3498 1.8485 2.6120 0.0509  0.1806  -0.0194 494  ASP B C   
16132 O O   . ASP C 494  ? 4.3468 1.8805 2.5994 0.0042  0.1489  0.0032  494  ASP B O   
16133 C CB  . ASP C 494  ? 4.1856 1.8380 2.6268 0.0609  0.1808  -0.0305 494  ASP B CB  
16134 C CG  . ASP C 494  ? 4.2372 1.8006 2.6037 0.0588  0.1276  -0.0262 494  ASP B CG  
16135 O OD1 . ASP C 494  ? 4.3017 1.7767 2.6190 0.0962  0.1349  -0.0426 494  ASP B OD1 
16136 O OD2 . ASP C 494  ? 4.2610 1.8436 2.6185 0.0199  0.0782  -0.0066 494  ASP B OD2 
16137 N N   . LYS C 495  ? 4.1531 1.5384 2.3221 0.0741  0.1810  -0.0278 495  LYS B N   
16138 C CA  . LYS C 495  ? 4.2693 1.5591 2.3156 0.0449  0.1387  -0.0099 495  LYS B CA  
16139 C C   . LYS C 495  ? 4.1808 1.4937 2.2042 0.0125  0.1478  0.0066  495  LYS B C   
16140 O O   . LYS C 495  ? 4.2555 1.4850 2.1821 0.0065  0.1413  0.0123  495  LYS B O   
16141 C CB  . LYS C 495  ? 4.4388 1.6039 2.3941 0.0808  0.1411  -0.0254 495  LYS B CB  
16142 C CG  . LYS C 495  ? 4.5378 1.6500 2.4775 0.0996  0.1077  -0.0344 495  LYS B CG  
16143 C CD  . LYS C 495  ? 4.5422 1.6777 2.4810 0.0553  0.0481  -0.0115 495  LYS B CD  
16144 C CE  . LYS C 495  ? 4.3836 1.6325 2.4443 0.0575  0.0568  -0.0155 495  LYS B CE  
16145 N NZ  . LYS C 495  ? 4.3228 1.6307 2.4001 0.0047  0.0109  0.0106  495  LYS B NZ  
16146 N N   . ILE C 496  ? 4.0601 1.4877 2.1745 -0.0083 0.1619  0.0139  496  ILE B N   
16147 C CA  . ILE C 496  ? 3.9858 1.4510 2.0992 -0.0336 0.1786  0.0262  496  ILE B CA  
16148 C C   . ILE C 496  ? 4.0917 1.5283 2.1282 -0.0852 0.1265  0.0525  496  ILE B C   
16149 O O   . ILE C 496  ? 4.0911 1.5630 2.1421 -0.1174 0.0839  0.0665  496  ILE B O   
16150 C CB  . ILE C 496  ? 3.7701 1.3689 2.0080 -0.0396 0.2079  0.0248  496  ILE B CB  
16151 C CG1 . ILE C 496  ? 3.6218 1.2598 1.9486 0.0094  0.2537  -0.0011 496  ILE B CG1 
16152 C CG2 . ILE C 496  ? 3.7609 1.3906 1.9970 -0.0579 0.2325  0.0341  496  ILE B CG2 
16153 C CD1 . ILE C 496  ? 3.5193 1.2308 1.9316 0.0082  0.2364  -0.0044 496  ILE B CD1 
16154 N N   . THR C 497  ? 3.6091 0.9825 1.5634 -0.0932 0.1305  0.0592  497  THR B N   
16155 C CA  . THR C 497  ? 3.7349 1.0844 1.6170 -0.1424 0.0859  0.0839  497  THR B CA  
16156 C C   . THR C 497  ? 3.6323 1.0965 1.5884 -0.1770 0.0905  0.0970  497  THR B C   
16157 O O   . THR C 497  ? 3.6171 1.1445 1.6126 -0.2089 0.0574  0.1092  497  THR B O   
16158 C CB  . THR C 497  ? 3.9069 1.1585 1.6824 -0.1393 0.0918  0.0861  497  THR B CB  
16159 O OG1 . THR C 497  ? 3.9558 1.2136 1.6853 -0.1889 0.0593  0.1100  497  THR B OG1 
16160 C CG2 . THR C 497  ? 3.8531 1.1219 1.6636 -0.1035 0.1567  0.0697  497  THR B CG2 
16161 N N   . HIS C 498  ? 4.2408 1.7331 2.2166 -0.1705 0.1319  0.0941  498  HIS B N   
16162 C CA  . HIS C 498  ? 4.1190 1.7074 2.1496 -0.2055 0.1328  0.1076  498  HIS B CA  
16163 C C   . HIS C 498  ? 3.9198 1.5995 2.0602 -0.1802 0.1895  0.0932  498  HIS B C   
16164 O O   . HIS C 498  ? 3.9137 1.5669 2.0667 -0.1371 0.2333  0.0748  498  HIS B O   
16165 C CB  . HIS C 498  ? 4.2378 1.7744 2.1770 -0.2350 0.1175  0.1242  498  HIS B CB  
16166 C CG  . HIS C 498  ? 4.4237 1.8848 2.2619 -0.2686 0.0572  0.1415  498  HIS B CG  
16167 N ND1 . HIS C 498  ? 4.5837 1.9245 2.3050 -0.2634 0.0440  0.1436  498  HIS B ND1 
16168 C CD2 . HIS C 498  ? 4.4505 1.9419 2.2893 -0.3083 0.0069  0.1577  498  HIS B CD2 
16169 C CE1 . HIS C 498  ? 4.6966 1.9943 2.3500 -0.2988 -0.0129 0.1605  498  HIS B CE1 
16170 N NE2 . HIS C 498  ? 4.6188 2.0063 2.3410 -0.3268 -0.0360 0.1698  498  HIS B NE2 
16171 N N   . TYR C 499  ? 3.7035 1.4928 1.9256 -0.2073 0.1875  0.1011  499  TYR B N   
16172 C CA  . TYR C 499  ? 3.4795 1.3517 1.7927 -0.1925 0.2376  0.0921  499  TYR B CA  
16173 C C   . TYR C 499  ? 3.4228 1.2859 1.6910 -0.2169 0.2404  0.1055  499  TYR B C   
16174 O O   . TYR C 499  ? 3.4487 1.3030 1.6647 -0.2587 0.1976  0.1243  499  TYR B O   
16175 C CB  . TYR C 499  ? 3.3266 1.3258 1.7595 -0.2051 0.2365  0.0907  499  TYR B CB  
16176 C CG  . TYR C 499  ? 3.2969 1.3109 1.7841 -0.1761 0.2414  0.0752  499  TYR B CG  
16177 C CD1 . TYR C 499  ? 3.2456 1.2570 1.7795 -0.1276 0.2912  0.0535  499  TYR B CD1 
16178 C CD2 . TYR C 499  ? 3.3476 1.3767 1.8375 -0.1970 0.1958  0.0824  499  TYR B CD2 
16179 C CE1 . TYR C 499  ? 3.2302 1.2555 1.8148 -0.1001 0.2949  0.0385  499  TYR B CE1 
16180 C CE2 . TYR C 499  ? 3.3326 1.3748 1.8718 -0.1705 0.1984  0.0685  499  TYR B CE2 
16181 C CZ  . TYR C 499  ? 3.2735 1.3138 1.8606 -0.1216 0.2479  0.0461  499  TYR B CZ  
16182 O OH  . TYR C 499  ? 3.2472 1.3008 1.8837 -0.0951 0.2490  0.0319  499  TYR B OH  
16183 N N   . ASN C 500  ? 3.6625 1.5258 1.9497 -0.1903 0.2908  0.0959  500  ASN B N   
16184 C CA  . ASN C 500  ? 3.6419 1.4963 1.8920 -0.2072 0.3016  0.1067  500  ASN B CA  
16185 C C   . ASN C 500  ? 3.4424 1.3946 1.7964 -0.1992 0.3467  0.1010  500  ASN B C   
16186 O O   . ASN C 500  ? 3.3831 1.3615 1.8033 -0.1619 0.3916  0.0839  500  ASN B O   
16187 C CB  . ASN C 500  ? 3.7690 1.5050 1.9138 -0.1846 0.3169  0.1035  500  ASN B CB  
16188 C CG  . ASN C 500  ? 3.9123 1.5497 1.9734 -0.1743 0.2868  0.1003  500  ASN B CG  
16189 O OD1 . ASN C 500  ? 3.9615 1.6027 2.0138 -0.1971 0.2414  0.1080  500  ASN B OD1 
16190 N ND2 . ASN C 500  ? 3.9795 1.5266 1.9769 -0.1399 0.3115  0.0889  500  ASN B ND2 
16191 N N   . TYR C 501  ? 3.4335 1.4392 1.8018 -0.2342 0.3344  0.1151  501  TYR B N   
16192 C CA  . TYR C 501  ? 3.2800 1.3790 1.7475 -0.2289 0.3727  0.1104  501  TYR B CA  
16193 C C   . TYR C 501  ? 3.2861 1.3669 1.7160 -0.2387 0.3890  0.1197  501  TYR B C   
16194 O O   . TYR C 501  ? 3.3781 1.3811 1.7035 -0.2566 0.3654  0.1322  501  TYR B O   
16195 C CB  . TYR C 501  ? 3.2150 1.4312 1.7787 -0.2560 0.3521  0.1137  501  TYR B CB  
16196 C CG  . TYR C 501  ? 3.2912 1.5272 1.8182 -0.3066 0.3033  0.1333  501  TYR B CG  
16197 C CD1 . TYR C 501  ? 3.2678 1.5479 1.8108 -0.3286 0.3082  0.1422  501  TYR B CD1 
16198 C CD2 . TYR C 501  ? 3.3881 1.6063 1.8722 -0.3331 0.2519  0.1426  501  TYR B CD2 
16199 C CE1 . TYR C 501  ? 3.3213 1.6257 1.8358 -0.3749 0.2637  0.1590  501  TYR B CE1 
16200 C CE2 . TYR C 501  ? 3.4444 1.6871 1.8993 -0.3806 0.2074  0.1604  501  TYR B CE2 
16201 C CZ  . TYR C 501  ? 3.4126 1.6991 1.8832 -0.4009 0.2140  0.1679  501  TYR B CZ  
16202 O OH  . TYR C 501  ? 3.4614 1.7746 1.9048 -0.4473 0.1707  0.1843  501  TYR B OH  
16203 N N   . LEU C 502  ? 2.9734 1.1290 1.4924 -0.2272 0.4291  0.1135  502  LEU B N   
16204 C CA  . LEU C 502  ? 2.9454 1.0880 1.4425 -0.2289 0.4539  0.1198  502  LEU B CA  
16205 C C   . LEU C 502  ? 2.8240 1.0816 1.4400 -0.2328 0.4778  0.1170  502  LEU B C   
16206 O O   . LEU C 502  ? 2.7174 1.0312 1.4258 -0.2062 0.5104  0.1022  502  LEU B O   
16207 C CB  . LEU C 502  ? 2.9404 1.0077 1.3987 -0.1874 0.4980  0.1089  502  LEU B CB  
16208 C CG  . LEU C 502  ? 2.9946 0.9705 1.3428 -0.1918 0.5001  0.1193  502  LEU B CG  
16209 C CD1 . LEU C 502  ? 3.0492 0.9900 1.3136 -0.2347 0.4444  0.1377  502  LEU B CD1 
16210 C CD2 . LEU C 502  ? 3.0647 0.9425 1.3450 -0.1538 0.5233  0.1076  502  LEU B CD2 
16211 N N   . ILE C 503  ? 2.8989 1.1907 1.5129 -0.2652 0.4618  0.1305  503  ILE B N   
16212 C CA  . ILE C 503  ? 2.7853 1.1893 1.5121 -0.2727 0.4784  0.1283  503  ILE B CA  
16213 C C   . ILE C 503  ? 2.7808 1.1797 1.4933 -0.2784 0.4988  0.1367  503  ILE B C   
16214 O O   . ILE C 503  ? 2.8279 1.2143 1.4867 -0.3112 0.4681  0.1515  503  ILE B O   
16215 C CB  . ILE C 503  ? 2.7460 1.2291 1.5129 -0.3118 0.4331  0.1354  503  ILE B CB  
16216 C CG1 . ILE C 503  ? 2.7573 1.2560 1.5478 -0.3080 0.4121  0.1279  503  ILE B CG1 
16217 C CG2 . ILE C 503  ? 2.6136 1.2115 1.4957 -0.3190 0.4498  0.1320  503  ILE B CG2 
16218 C CD1 . ILE C 503  ? 2.7258 1.2876 1.5350 -0.3490 0.3621  0.1367  503  ILE B CD1 
16219 N N   . LEU C 504  ? 2.7536 1.1632 1.5155 -0.2464 0.5503  0.1271  504  LEU B N   
16220 C CA  . LEU C 504  ? 2.7530 1.1581 1.5107 -0.2453 0.5779  0.1337  504  LEU B CA  
16221 C C   . LEU C 504  ? 2.6870 1.2095 1.5651 -0.2559 0.5867  0.1314  504  LEU B C   
16222 O O   . LEU C 504  ? 2.6317 1.2330 1.6085 -0.2474 0.5930  0.1194  504  LEU B O   
16223 C CB  . LEU C 504  ? 2.7945 1.1491 1.5438 -0.2038 0.6312  0.1242  504  LEU B CB  
16224 C CG  . LEU C 504  ? 2.8800 1.1120 1.5096 -0.1855 0.6382  0.1250  504  LEU B CG  
16225 C CD1 . LEU C 504  ? 2.9542 1.1350 1.5173 -0.1943 0.5970  0.1252  504  LEU B CD1 
16226 C CD2 . LEU C 504  ? 2.8522 1.0722 1.5172 -0.1415 0.6918  0.1096  504  LEU B CD2 
16227 N N   . SER C 505  ? 3.6097 2.1430 2.4803 -0.2730 0.5879  0.1424  505  SER B N   
16228 C CA  . SER C 505  ? 3.5200 2.1613 2.4959 -0.2877 0.5892  0.1417  505  SER B CA  
16229 C C   . SER C 505  ? 3.5651 2.1890 2.5239 -0.2887 0.6110  0.1508  505  SER B C   
16230 O O   . SER C 505  ? 3.6273 2.1966 2.4970 -0.3103 0.5878  0.1651  505  SER B O   
16231 C CB  . SER C 505  ? 3.5087 2.1966 2.4829 -0.3290 0.5353  0.1496  505  SER B CB  
16232 O OG  . SER C 505  ? 3.4142 2.1933 2.4703 -0.3461 0.5339  0.1510  505  SER B OG  
16233 N N   . LYS C 506  ? 2.8041 1.4754 1.8485 -0.2665 0.6543  0.1432  506  LYS B N   
16234 C CA  . LYS C 506  ? 2.8353 1.4808 1.8591 -0.2636 0.6794  0.1522  506  LYS B CA  
16235 C C   . LYS C 506  ? 2.9864 1.5117 1.8890 -0.2485 0.6926  0.1582  506  LYS B C   
16236 O O   . LYS C 506  ? 3.0820 1.5508 1.8975 -0.2665 0.6755  0.1724  506  LYS B O   
16237 C CB  . LYS C 506  ? 2.8302 1.4991 1.8354 -0.3011 0.6438  0.1662  506  LYS B CB  
16238 C CG  . LYS C 506  ? 2.6942 1.4783 1.8033 -0.3225 0.6201  0.1613  506  LYS B CG  
16239 C CD  . LYS C 506  ? 2.7049 1.4965 1.7708 -0.3619 0.5759  0.1749  506  LYS B CD  
16240 C CE  . LYS C 506  ? 2.7884 1.5252 1.7581 -0.3833 0.5317  0.1817  506  LYS B CE  
16241 N NZ  . LYS C 506  ? 2.7262 1.5277 1.7542 -0.3905 0.5088  0.1718  506  LYS B NZ  
16242 N N   . GLY C 507  ? 3.3242 1.8104 2.2192 -0.2159 0.7211  0.1468  507  GLY B N   
16243 C CA  . GLY C 507  ? 3.4553 1.8302 2.2415 -0.1972 0.7387  0.1497  507  GLY B CA  
16244 C C   . GLY C 507  ? 3.6141 1.9013 2.2714 -0.2177 0.6972  0.1606  507  GLY B C   
16245 O O   . GLY C 507  ? 3.7053 1.8983 2.2654 -0.2053 0.7093  0.1645  507  GLY B O   
16246 N N   . LYS C 508  ? 3.6963 2.0154 2.3530 -0.2491 0.6484  0.1653  508  LYS B N   
16247 C CA  . LYS C 508  ? 3.8086 2.0526 2.3493 -0.2729 0.6037  0.1763  508  LYS B CA  
16248 C C   . LYS C 508  ? 3.7525 2.0034 2.2921 -0.2806 0.5688  0.1705  508  LYS B C   
16249 O O   . LYS C 508  ? 3.6558 1.9953 2.2783 -0.2959 0.5501  0.1671  508  LYS B O   
16250 C CB  . LYS C 508  ? 3.8332 2.1022 2.3566 -0.3117 0.5706  0.1918  508  LYS B CB  
16251 C CG  . LYS C 508  ? 3.9500 2.1281 2.3589 -0.3195 0.5665  0.2056  508  LYS B CG  
16252 C CD  . LYS C 508  ? 3.9420 2.1558 2.3466 -0.3575 0.5332  0.2194  508  LYS B CD  
16253 C CE  . LYS C 508  ? 3.9975 2.1539 2.3369 -0.3567 0.5495  0.2307  508  LYS B CE  
16254 N NZ  . LYS C 508  ? 3.9507 2.1662 2.3231 -0.3866 0.5294  0.2409  508  LYS B NZ  
16255 N N   . ILE C 509  ? 3.2471 1.4044 1.6919 -0.2706 0.5587  0.1695  509  ILE B N   
16256 C CA  . ILE C 509  ? 3.2195 1.3712 1.6448 -0.2839 0.5178  0.1680  509  ILE B CA  
16257 C C   . ILE C 509  ? 3.1984 1.3787 1.6023 -0.3298 0.4680  0.1830  509  ILE B C   
16258 O O   . ILE C 509  ? 3.2530 1.4015 1.5989 -0.3473 0.4598  0.1955  509  ILE B O   
16259 C CB  . ILE C 509  ? 3.3175 1.3520 1.6287 -0.2692 0.5101  0.1667  509  ILE B CB  
16260 C CG1 . ILE C 509  ? 3.3109 1.2978 1.6148 -0.2258 0.5632  0.1551  509  ILE B CG1 
16261 C CG2 . ILE C 509  ? 3.3490 1.3851 1.6633 -0.2725 0.4783  0.1609  509  ILE B CG2 
16262 C CD1 . ILE C 509  ? 3.3893 1.3026 1.6409 -0.1998 0.5635  0.1438  509  ILE B CD1 
16263 N N   . ILE C 510  ? 3.2362 1.4781 1.6872 -0.3495 0.4349  0.1816  510  ILE B N   
16264 C CA  . ILE C 510  ? 3.2409 1.5138 1.6728 -0.3941 0.3861  0.1951  510  ILE B CA  
16265 C C   . ILE C 510  ? 3.2926 1.5614 1.7020 -0.4115 0.3427  0.1962  510  ILE B C   
16266 O O   . ILE C 510  ? 3.3264 1.5846 1.6813 -0.4477 0.2977  0.2090  510  ILE B O   
16267 C CB  . ILE C 510  ? 3.2285 1.6215 1.7718 -0.4099 0.3890  0.1942  510  ILE B CB  
16268 C CG1 . ILE C 510  ? 3.1070 1.5774 1.7704 -0.3818 0.4229  0.1771  510  ILE B CG1 
16269 C CG2 . ILE C 510  ? 3.2219 1.6101 1.7546 -0.4133 0.4079  0.2018  510  ILE B CG2 
16270 C CD1 . ILE C 510  ? 2.9759 1.5701 1.7568 -0.3964 0.4236  0.1739  510  ILE B CD1 
16271 N N   . HIS C 511  ? 3.4659 1.7429 1.9169 -0.3863 0.3557  0.1831  511  HIS B N   
16272 C CA  . HIS C 511  ? 3.5763 1.8407 2.0010 -0.4005 0.3154  0.1845  511  HIS B CA  
16273 C C   . HIS C 511  ? 3.6649 1.8494 2.0470 -0.3663 0.3298  0.1745  511  HIS B C   
16274 O O   . HIS C 511  ? 3.6433 1.8107 2.0496 -0.3282 0.3758  0.1623  511  HIS B O   
16275 C CB  . HIS C 511  ? 3.5141 1.8970 2.0496 -0.4148 0.3019  0.1796  511  HIS B CB  
16276 C CG  . HIS C 511  ? 3.4754 1.9423 2.0572 -0.4482 0.2862  0.1876  511  HIS B CG  
16277 N ND1 . HIS C 511  ? 3.5304 2.0118 2.0741 -0.4915 0.2359  0.2011  511  HIS B ND1 
16278 C CD2 . HIS C 511  ? 3.3787 1.9186 2.0408 -0.4445 0.3140  0.1837  511  HIS B CD2 
16279 C CE1 . HIS C 511  ? 3.4509 2.0125 2.0507 -0.5123 0.2335  0.2042  511  HIS B CE1 
16280 N NE2 . HIS C 511  ? 3.3583 1.9557 2.0305 -0.4843 0.2799  0.1939  511  HIS B NE2 
16281 N N   . PHE C 512  ? 3.5324 1.6676 1.8495 -0.3809 0.2888  0.1799  512  PHE B N   
16282 C CA  . PHE C 512  ? 3.6421 1.6938 1.9074 -0.3522 0.2933  0.1713  512  PHE B CA  
16283 C C   . PHE C 512  ? 3.7085 1.7222 1.9059 -0.3824 0.2364  0.1823  512  PHE B C   
16284 O O   . PHE C 512  ? 3.7052 1.7351 1.8730 -0.4230 0.1991  0.1976  512  PHE B O   
16285 C CB  . PHE C 512  ? 3.8076 1.7541 1.9813 -0.3300 0.3176  0.1708  512  PHE B CB  
16286 C CG  . PHE C 512  ? 3.9856 1.8562 2.0434 -0.3602 0.2800  0.1876  512  PHE B CG  
16287 C CD1 . PHE C 512  ? 4.1366 1.8925 2.0845 -0.3517 0.2640  0.1885  512  PHE B CD1 
16288 C CD2 . PHE C 512  ? 3.9735 1.8897 2.0338 -0.3982 0.2579  0.2019  512  PHE B CD2 
16289 C CE1 . PHE C 512  ? 4.2595 1.9463 2.1012 -0.3806 0.2279  0.2039  512  PHE B CE1 
16290 C CE2 . PHE C 512  ? 4.0885 1.9375 2.0436 -0.4272 0.2222  0.2173  512  PHE B CE2 
16291 C CZ  . PHE C 512  ? 4.2294 1.9630 2.0746 -0.4188 0.2071  0.2186  512  PHE B CZ  
16292 N N   . GLY C 513  ? 3.9728 1.9361 2.1456 -0.3632 0.2288  0.1747  513  GLY B N   
16293 C CA  . GLY C 513  ? 4.0773 1.9999 2.1857 -0.3901 0.1748  0.1853  513  GLY B CA  
16294 C C   . GLY C 513  ? 4.1180 1.9994 2.2242 -0.3612 0.1749  0.1732  513  GLY B C   
16295 O O   . GLY C 513  ? 4.0816 1.9367 2.2054 -0.3186 0.2164  0.1571  513  GLY B O   
16296 N N   . THR C 514  ? 3.9897 1.8654 2.0742 -0.3842 0.1282  0.1808  514  THR B N   
16297 C CA  . THR C 514  ? 4.0380 1.8864 2.1321 -0.3587 0.1250  0.1695  514  THR B CA  
16298 C C   . THR C 514  ? 4.0090 1.9111 2.1364 -0.3873 0.0810  0.1772  514  THR B C   
16299 O O   . THR C 514  ? 4.0581 1.9637 2.1436 -0.4307 0.0358  0.1950  514  THR B O   
16300 C CB  . THR C 514  ? 4.2062 1.9190 2.1862 -0.3391 0.1167  0.1673  514  THR B CB  
16301 O OG1 . THR C 514  ? 4.2042 1.8784 2.1798 -0.2978 0.1682  0.1527  514  THR B OG1 
16302 C CG2 . THR C 514  ? 4.2713 1.9579 2.2533 -0.3245 0.0967  0.1601  514  THR B CG2 
16303 N N   . ARG C 515  ? 3.8906 1.8358 2.0948 -0.3622 0.0953  0.1633  515  ARG B N   
16304 C CA  . ARG C 515  ? 3.9329 1.9214 2.1678 -0.3828 0.0567  0.1686  515  ARG B CA  
16305 C C   . ARG C 515  ? 4.0067 1.9058 2.1918 -0.3551 0.0475  0.1606  515  ARG B C   
16306 O O   . ARG C 515  ? 3.9843 1.8601 2.1940 -0.3098 0.0872  0.1419  515  ARG B O   
16307 C CB  . ARG C 515  ? 3.8499 1.9672 2.2211 -0.3753 0.0807  0.1579  515  ARG B CB  
16308 C CG  . ARG C 515  ? 3.8031 2.0071 2.2373 -0.3884 0.1050  0.1593  515  ARG B CG  
16309 C CD  . ARG C 515  ? 3.8898 2.1320 2.3001 -0.4420 0.0615  0.1793  515  ARG B CD  
16310 N NE  . ARG C 515  ? 3.8251 2.1731 2.3205 -0.4539 0.0819  0.1781  515  ARG B NE  
16311 C CZ  . ARG C 515  ? 3.7689 2.2342 2.3753 -0.4594 0.0859  0.1718  515  ARG B CZ  
16312 N NH1 . ARG C 515  ? 3.7726 2.2662 2.4189 -0.4544 0.0716  0.1669  515  ARG B NH1 
16313 N NH2 . ARG C 515  ? 3.6907 2.2456 2.3690 -0.4696 0.1038  0.1702  515  ARG B NH2 
16314 N N   . GLU C 516  ? 3.8863 1.7339 2.0000 -0.3826 -0.0053 0.1747  516  GLU B N   
16315 C CA  . GLU C 516  ? 3.9465 1.7103 2.0126 -0.3601 -0.0216 0.1685  516  GLU B CA  
16316 C C   . GLU C 516  ? 3.8260 1.6567 1.9911 -0.3359 -0.0084 0.1542  516  GLU B C   
16317 O O   . GLU C 516  ? 3.7117 1.6440 1.9551 -0.3583 -0.0204 0.1590  516  GLU B O   
16318 C CB  . GLU C 516  ? 4.0996 1.8005 2.0722 -0.3993 -0.0844 0.1889  516  GLU B CB  
16319 C CG  . GLU C 516  ? 4.2100 1.8374 2.1448 -0.3811 -0.1090 0.1842  516  GLU B CG  
16320 C CD  . GLU C 516  ? 4.3928 1.8936 2.1948 -0.3959 -0.1496 0.1964  516  GLU B CD  
16321 O OE1 . GLU C 516  ? 4.4776 1.9299 2.2433 -0.4004 -0.1882 0.2010  516  GLU B OE1 
16322 O OE2 . GLU C 516  ? 4.4556 1.9054 2.1905 -0.4026 -0.1432 0.2013  516  GLU B OE2 
16323 N N   . LYS C 517  ? 3.6768 1.4500 1.8373 -0.2898 0.0161  0.1360  517  LYS B N   
16324 C CA  . LYS C 517  ? 3.6112 1.4409 1.8646 -0.2605 0.0343  0.1196  517  LYS B CA  
16325 C C   . LYS C 517  ? 3.7296 1.5728 1.9879 -0.2817 -0.0148 0.1287  517  LYS B C   
16326 O O   . LYS C 517  ? 3.8907 1.6468 2.0576 -0.2960 -0.0577 0.1397  517  LYS B O   
16327 C CB  . LYS C 517  ? 3.5857 1.3440 1.8252 -0.2058 0.0712  0.0975  517  LYS B CB  
16328 C CG  . LYS C 517  ? 3.4363 1.2717 1.7908 -0.1706 0.1079  0.0772  517  LYS B CG  
16329 C CD  . LYS C 517  ? 3.4599 1.2642 1.8160 -0.1524 0.0852  0.0696  517  LYS B CD  
16330 C CE  . LYS C 517  ? 3.3127 1.2047 1.7908 -0.1196 0.1222  0.0497  517  LYS B CE  
16331 N NZ  . LYS C 517  ? 3.3556 1.1815 1.8239 -0.0701 0.1406  0.0285  517  LYS B NZ  
16332 N N   . PHE C 518  ? 4.3650 2.3179 2.7317 -0.2829 -0.0077 0.1238  518  PHE B N   
16333 C CA  . PHE C 518  ? 4.4476 2.4285 2.8357 -0.2997 -0.0488 0.1306  518  PHE B CA  
16334 C C   . PHE C 518  ? 4.5479 2.4529 2.9130 -0.2618 -0.0512 0.1173  518  PHE B C   
16335 O O   . PHE C 518  ? 4.4395 2.3808 2.8816 -0.2230 -0.0171 0.0971  518  PHE B O   
16336 C CB  . PHE C 518  ? 4.3517 2.4733 2.8662 -0.3074 -0.0353 0.1263  518  PHE B CB  
16337 C CG  . PHE C 518  ? 4.3872 2.5818 2.9107 -0.3615 -0.0680 0.1468  518  PHE B CG  
16338 C CD1 . PHE C 518  ? 4.5096 2.6454 2.9351 -0.3978 -0.1004 0.1665  518  PHE B CD1 
16339 C CD2 . PHE C 518  ? 4.2978 2.6204 2.9271 -0.3764 -0.0670 0.1457  518  PHE B CD2 
16340 C CE1 . PHE C 518  ? 4.5107 2.7144 2.9436 -0.4479 -0.1308 0.1848  518  PHE B CE1 
16341 C CE2 . PHE C 518  ? 4.2991 2.6914 2.9367 -0.4263 -0.0975 0.1635  518  PHE B CE2 
16342 C CZ  . PHE C 518  ? 4.4028 2.7360 2.9422 -0.4622 -0.1293 0.1831  518  PHE B CZ  
16343 N N   . SER C 519  ? 3.6973 1.4974 1.9561 -0.2743 -0.0938 0.1289  519  SER B N   
16344 C CA  . SER C 519  ? 3.8430 1.5477 2.0571 -0.2382 -0.0992 0.1167  519  SER B CA  
16345 C C   . SER C 519  ? 3.8037 1.5694 2.1158 -0.2067 -0.0812 0.0993  519  SER B C   
16346 O O   . SER C 519  ? 3.7893 1.5637 2.1511 -0.1616 -0.0325 0.0765  519  SER B O   
16347 C CB  . SER C 519  ? 3.9879 1.6080 2.1022 -0.2690 -0.1624 0.1362  519  SER B CB  
16348 O OG  . SER C 519  ? 4.0451 1.6253 2.0773 -0.3054 -0.1829 0.1547  519  SER B OG  
16349 N N   . ASP C 520  ? 4.9468 2.7573 3.2871 -0.2317 -0.1207 0.1104  520  ASP B N   
16350 C CA  . ASP C 520  ? 4.9176 2.7801 3.3432 -0.2051 -0.1123 0.0960  520  ASP B CA  
16351 C C   . ASP C 520  ? 4.7355 2.6858 3.2718 -0.1706 -0.0512 0.0738  520  ASP B C   
16352 O O   . ASP C 520  ? 4.7297 2.6395 3.2714 -0.1245 -0.0109 0.0528  520  ASP B O   
16353 C CB  . ASP C 520  ? 5.0089 2.9462 3.4705 -0.2469 -0.1566 0.1139  520  ASP B CB  
16354 C CG  . ASP C 520  ? 5.0599 3.1005 3.5661 -0.2882 -0.1548 0.1273  520  ASP B CG  
16355 O OD1 . ASP C 520  ? 5.0786 3.1138 3.5659 -0.2906 -0.1288 0.1270  520  ASP B OD1 
16356 O OD2 . ASP C 520  ? 5.0724 3.2002 3.6328 -0.3179 -0.1795 0.1375  520  ASP B OD2 
16357 N N   . ALA C 521  ? 4.4906 2.5628 3.1154 -0.1940 -0.0454 0.0786  521  ALA B N   
16358 C CA  . ALA C 521  ? 4.2608 2.4308 3.0049 -0.1649 0.0054  0.0586  521  ALA B CA  
16359 C C   . ALA C 521  ? 4.0565 2.2164 2.8081 -0.1380 0.0602  0.0451  521  ALA B C   
16360 O O   . ALA C 521  ? 4.0980 2.1895 2.7667 -0.1482 0.0595  0.0535  521  ALA B O   
16361 C CB  . ALA C 521  ? 4.1882 2.4909 3.0208 -0.1997 -0.0045 0.0676  521  ALA B CB  
16362 N N   . SER C 522  ? 4.0890 2.3206 2.9433 -0.1041 0.1072  0.0244  522  SER B N   
16363 C CA  . SER C 522  ? 3.9293 2.1694 2.8135 -0.0749 0.1646  0.0095  522  SER B CA  
16364 C C   . SER C 522  ? 3.8284 2.0970 2.6962 -0.1084 0.1689  0.0241  522  SER B C   
16365 O O   . SER C 522  ? 3.9217 2.1150 2.6892 -0.1309 0.1456  0.0392  522  SER B O   
16366 C CB  . SER C 522  ? 3.7731 2.1155 2.7891 -0.0453 0.2061  -0.0109 522  SER B CB  
16367 O OG  . SER C 522  ? 3.6922 2.0594 2.7497 -0.0217 0.2619  -0.0237 522  SER B OG  
16368 N N   . TYR C 523  ? 3.0399 1.4199 2.0099 -0.1112 0.1982  0.0188  523  TYR B N   
16369 C CA  . TYR C 523  ? 2.9066 1.3241 1.8809 -0.1340 0.2134  0.0276  523  TYR B CA  
16370 C C   . TYR C 523  ? 2.8890 1.3305 1.8265 -0.1889 0.1655  0.0516  523  TYR B C   
16371 O O   . TYR C 523  ? 2.9333 1.3454 1.8221 -0.2125 0.1170  0.0643  523  TYR B O   
16372 C CB  . TYR C 523  ? 2.7514 1.2856 1.8540 -0.1198 0.2564  0.0137  523  TYR B CB  
16373 C CG  . TYR C 523  ? 2.6728 1.3025 1.8646 -0.1288 0.2385  0.0109  523  TYR B CG  
16374 C CD1 . TYR C 523  ? 2.6365 1.3460 1.8558 -0.1738 0.2058  0.0261  523  TYR B CD1 
16375 C CD2 . TYR C 523  ? 2.6226 1.2636 1.8704 -0.0923 0.2534  -0.0072 523  TYR B CD2 
16376 C CE1 . TYR C 523  ? 2.5657 1.3651 1.8663 -0.1824 0.1895  0.0233  523  TYR B CE1 
16377 C CE2 . TYR C 523  ? 2.5430 1.2720 1.8723 -0.1003 0.2370  -0.0099 523  TYR B CE2 
16378 C CZ  . TYR C 523  ? 2.5268 1.3350 1.8819 -0.1455 0.2052  0.0056  523  TYR B CZ  
16379 O OH  . TYR C 523  ? 2.4915 1.3902 1.9274 -0.1542 0.1884  0.0029  523  TYR B OH  
16380 N N   . GLN C 524  ? 2.5524 1.0485 1.5147 -0.2090 0.1803  0.0575  524  GLN B N   
16381 C CA  . GLN C 524  ? 2.6101 1.1449 1.5508 -0.2610 0.1403  0.0785  524  GLN B CA  
16382 C C   . GLN C 524  ? 2.5656 1.1641 1.5457 -0.2752 0.1650  0.0807  524  GLN B C   
16383 O O   . GLN C 524  ? 2.5174 1.1123 1.5228 -0.2464 0.2121  0.0688  524  GLN B O   
16384 C CB  . GLN C 524  ? 2.7632 1.1886 1.5715 -0.2853 0.0971  0.0967  524  GLN B CB  
16385 C CG  . GLN C 524  ? 2.8180 1.1620 1.5469 -0.2791 0.1157  0.0995  524  GLN B CG  
16386 C CD  . GLN C 524  ? 2.9894 1.2001 1.6020 -0.2698 0.0933  0.1034  524  GLN B CD  
16387 O OE1 . GLN C 524  ? 3.0219 1.1905 1.6349 -0.2368 0.0993  0.0906  524  GLN B OE1 
16388 N NE2 . GLN C 524  ? 3.0985 1.2420 1.6108 -0.2989 0.0654  0.1206  524  GLN B NE2 
16389 N N   . SER C 525  ? 3.7897 2.4475 2.7742 -0.3210 0.1310  0.0966  525  SER B N   
16390 C CA  . SER C 525  ? 3.7184 2.4500 2.7476 -0.3400 0.1462  0.0996  525  SER B CA  
16391 C C   . SER C 525  ? 3.8092 2.4597 2.7360 -0.3562 0.1400  0.1131  525  SER B C   
16392 O O   . SER C 525  ? 3.9032 2.4670 2.7258 -0.3743 0.1035  0.1270  525  SER B O   
16393 C CB  . SER C 525  ? 3.7150 2.5536 2.7999 -0.3815 0.1116  0.1088  525  SER B CB  
16394 O OG  . SER C 525  ? 3.6884 2.5839 2.8449 -0.3709 0.1058  0.0996  525  SER B OG  
16395 N N   . ILE C 526  ? 3.0556 1.7331 2.0125 -0.3490 0.1758  0.1088  526  ILE B N   
16396 C CA  . ILE C 526  ? 3.0734 1.6960 1.9476 -0.3695 0.1690  0.1223  526  ILE B CA  
16397 C C   . ILE C 526  ? 2.9671 1.6932 1.9073 -0.3975 0.1700  0.1267  526  ILE B C   
16398 O O   . ILE C 526  ? 2.7784 1.5838 1.8185 -0.3791 0.2072  0.1134  526  ILE B O   
16399 C CB  . ILE C 526  ? 3.0102 1.5563 1.8486 -0.3321 0.2140  0.1133  526  ILE B CB  
16400 C CG1 . ILE C 526  ? 3.0121 1.4600 1.7937 -0.2990 0.2179  0.1053  526  ILE B CG1 
16401 C CG2 . ILE C 526  ? 3.0829 1.5710 1.8327 -0.3543 0.2046  0.1280  526  ILE B CG2 
16402 C CD1 . ILE C 526  ? 3.0590 1.4158 1.7793 -0.2683 0.2534  0.0994  526  ILE B CD1 
16403 N N   . ASN C 527  ? 3.4304 2.1579 2.3175 -0.4418 0.1293  0.1447  527  ASN B N   
16404 C CA  . ASN C 527  ? 3.4221 2.2536 2.3764 -0.4685 0.1282  0.1474  527  ASN B CA  
16405 C C   . ASN C 527  ? 3.5018 2.3102 2.4055 -0.4879 0.1286  0.1580  527  ASN B C   
16406 O O   . ASN C 527  ? 3.6019 2.3768 2.4272 -0.5242 0.0889  0.1749  527  ASN B O   
16407 C CB  . ASN C 527  ? 3.4428 2.3604 2.4371 -0.5056 0.0860  0.1543  527  ASN B CB  
16408 C CG  . ASN C 527  ? 3.3464 2.3979 2.4598 -0.5133 0.1009  0.1456  527  ASN B CG  
16409 O OD1 . ASN C 527  ? 3.3052 2.3809 2.4342 -0.5179 0.1184  0.1458  527  ASN B OD1 
16410 N ND2 . ASN C 527  ? 3.3159 2.4546 2.5154 -0.5131 0.0950  0.1373  527  ASN B ND2 
16411 N N   . ILE C 528  ? 2.8436 1.6769 1.7997 -0.4638 0.1739  0.1477  528  ILE B N   
16412 C CA  . ILE C 528  ? 2.8809 1.6982 1.8028 -0.4760 0.1823  0.1554  528  ILE B CA  
16413 C C   . ILE C 528  ? 2.8037 1.7431 1.8222 -0.4954 0.1852  0.1529  528  ILE B C   
16414 O O   . ILE C 528  ? 2.6952 1.7130 1.8212 -0.4734 0.2182  0.1379  528  ILE B O   
16415 C CB  . ILE C 528  ? 2.9218 1.6689 1.8213 -0.4361 0.2310  0.1474  528  ILE B CB  
16416 C CG1 . ILE C 528  ? 2.9755 1.6528 1.8514 -0.3993 0.2467  0.1374  528  ILE B CG1 
16417 C CG2 . ILE C 528  ? 3.0067 1.6715 1.8010 -0.4514 0.2226  0.1616  528  ILE B CG2 
16418 C CD1 . ILE C 528  ? 2.8875 1.6443 1.8775 -0.3739 0.2691  0.1199  528  ILE B CD1 
16419 N N   . PRO C 529  ? 3.3397 2.2956 2.3199 -0.5372 0.1491  0.1673  529  PRO B N   
16420 C CA  . PRO C 529  ? 3.2894 2.3419 2.3345 -0.5603 0.1467  0.1678  529  PRO B CA  
16421 C C   . PRO C 529  ? 3.2318 2.2778 2.3044 -0.5345 0.1927  0.1609  529  PRO B C   
16422 O O   . PRO C 529  ? 3.3104 2.2650 2.2971 -0.5293 0.2009  0.1688  529  PRO B O   
16423 C CB  . PRO C 529  ? 3.3722 2.3863 2.3219 -0.6032 0.1019  0.1870  529  PRO B CB  
16424 C CG  . PRO C 529  ? 3.4792 2.4269 2.3532 -0.6124 0.0688  0.1954  529  PRO B CG  
16425 C CD  . PRO C 529  ? 3.4774 2.3572 2.3443 -0.5670 0.1024  0.1845  529  PRO B CD  
16426 N N   . VAL C 530  ? 2.8556 1.9971 2.0462 -0.5187 0.2219  0.1466  530  VAL B N   
16427 C CA  . VAL C 530  ? 2.7772 1.9232 2.0021 -0.4978 0.2633  0.1411  530  VAL B CA  
16428 C C   . VAL C 530  ? 2.7828 1.9333 1.9689 -0.5303 0.2427  0.1538  530  VAL B C   
16429 O O   . VAL C 530  ? 2.7543 1.9832 1.9740 -0.5635 0.2112  0.1569  530  VAL B O   
16430 C CB  . VAL C 530  ? 2.3482 1.6008 1.7121 -0.4766 0.2956  0.1231  530  VAL B CB  
16431 C CG1 . VAL C 530  ? 2.2773 1.6472 1.7177 -0.5079 0.2718  0.1219  530  VAL B CG1 
16432 C CG2 . VAL C 530  ? 2.2992 1.5305 1.6884 -0.4446 0.3455  0.1166  530  VAL B CG2 
16433 N N   . THR C 531  ? 3.1698 2.2342 2.2809 -0.5213 0.2589  0.1612  531  THR B N   
16434 C CA  . THR C 531  ? 3.2185 2.2757 2.2814 -0.5516 0.2375  0.1741  531  THR B CA  
16435 C C   . THR C 531  ? 3.1475 2.2434 2.2698 -0.5393 0.2714  0.1693  531  THR B C   
16436 O O   . THR C 531  ? 3.0935 2.1716 2.2484 -0.5035 0.3165  0.1606  531  THR B O   
16437 C CB  . THR C 531  ? 3.3586 2.2880 2.2799 -0.5586 0.2219  0.1890  531  THR B CB  
16438 O OG1 . THR C 531  ? 3.3990 2.3342 2.2734 -0.5975 0.1866  0.2025  531  THR B OG1 
16439 C CG2 . THR C 531  ? 3.3772 2.2270 2.2636 -0.5234 0.2666  0.1869  531  THR B CG2 
16440 N N   . GLN C 532  ? 2.7639 1.9122 1.8987 -0.5700 0.2486  0.1754  532  GLN B N   
16441 C CA  . GLN C 532  ? 2.7298 1.9133 1.9147 -0.5632 0.2743  0.1728  532  GLN B CA  
16442 C C   . GLN C 532  ? 2.7732 1.8617 1.9075 -0.5302 0.3159  0.1747  532  GLN B C   
16443 O O   . GLN C 532  ? 2.7150 1.8315 1.9166 -0.5060 0.3552  0.1667  532  GLN B O   
16444 C CB  . GLN C 532  ? 2.7757 1.9802 1.9272 -0.6024 0.2377  0.1842  532  GLN B CB  
16445 C CG  . GLN C 532  ? 2.7402 1.9694 1.9270 -0.5992 0.2581  0.1842  532  GLN B CG  
16446 C CD  . GLN C 532  ? 2.6042 1.9531 1.9319 -0.5899 0.2769  0.1686  532  GLN B CD  
16447 O OE1 . GLN C 532  ? 2.5573 1.9713 1.9602 -0.5827 0.2789  0.1567  532  GLN B OE1 
16448 N NE2 . GLN C 532  ? 2.5332 1.9105 1.8970 -0.5898 0.2900  0.1686  532  GLN B NE2 
16449 N N   . ASN C 533  ? 3.1057 2.0825 2.1228 -0.5286 0.3074  0.1846  533  ASN B N   
16450 C CA  . ASN C 533  ? 3.1518 2.0314 2.1041 -0.5017 0.3419  0.1880  533  ASN B CA  
16451 C C   . ASN C 533  ? 3.0779 1.9565 2.0885 -0.4585 0.3916  0.1742  533  ASN B C   
16452 O O   . ASN C 533  ? 3.1118 1.9186 2.0799 -0.4335 0.4251  0.1753  533  ASN B O   
16453 C CB  . ASN C 533  ? 3.3177 2.0798 2.1339 -0.5083 0.3199  0.1996  533  ASN B CB  
16454 C CG  . ASN C 533  ? 3.4298 2.1746 2.1724 -0.5491 0.2750  0.2150  533  ASN B CG  
16455 O OD1 . ASN C 533  ? 3.5147 2.2505 2.2133 -0.5742 0.2341  0.2209  533  ASN B OD1 
16456 N ND2 . ASN C 533  ? 3.4300 2.1693 2.1577 -0.5566 0.2818  0.2220  533  ASN B ND2 
16457 N N   . MET C 534  ? 2.7021 1.6595 1.8084 -0.4495 0.3966  0.1609  534  MET B N   
16458 C CA  . MET C 534  ? 2.6036 1.5628 1.7676 -0.4088 0.4427  0.1470  534  MET B CA  
16459 C C   . MET C 534  ? 2.4527 1.5186 1.7441 -0.4027 0.4658  0.1369  534  MET B C   
16460 O O   . MET C 534  ? 2.3629 1.4647 1.7345 -0.3732 0.5013  0.1232  534  MET B O   
16461 C CB  . MET C 534  ? 2.6021 1.5642 1.7754 -0.4012 0.4306  0.1391  534  MET B CB  
16462 C CG  . MET C 534  ? 2.7045 1.6057 1.7731 -0.4289 0.3831  0.1516  534  MET B CG  
16463 S SD  . MET C 534  ? 2.6599 1.5992 1.7569 -0.4360 0.3524  0.1453  534  MET B SD  
16464 C CE  . MET C 534  ? 2.4912 1.3737 1.5952 -0.3849 0.3968  0.1311  534  MET B CE  
16465 N N   . VAL C 535  ? 2.5772 1.6918 1.8847 -0.4311 0.4447  0.1437  535  VAL B N   
16466 C CA  . VAL C 535  ? 2.4574 1.6881 1.8889 -0.4345 0.4525  0.1341  535  VAL B CA  
16467 C C   . VAL C 535  ? 2.3650 1.6321 1.8926 -0.3976 0.5035  0.1200  535  VAL B C   
16468 O O   . VAL C 535  ? 2.2990 1.6528 1.9292 -0.3902 0.5095  0.1061  535  VAL B O   
16469 C CB  . VAL C 535  ? 2.4662 1.7190 1.8894 -0.4607 0.4359  0.1438  535  VAL B CB  
16470 C CG1 . VAL C 535  ? 2.4761 1.7972 1.9117 -0.5000 0.3855  0.1462  535  VAL B CG1 
16471 C CG2 . VAL C 535  ? 2.6165 1.7548 1.9165 -0.4622 0.4380  0.1596  535  VAL B CG2 
16472 N N   . PRO C 536  ? 2.0867 1.2896 1.5827 -0.3745 0.5409  0.1234  536  PRO B N   
16473 C CA  . PRO C 536  ? 2.0726 1.3303 1.6763 -0.3448 0.5858  0.1100  536  PRO B CA  
16474 C C   . PRO C 536  ? 2.0058 1.2558 1.6358 -0.3156 0.6073  0.0970  536  PRO B C   
16475 O O   . PRO C 536  ? 1.9237 1.2593 1.6568 -0.3080 0.6128  0.0829  536  PRO B O   
16476 C CB  . PRO C 536  ? 2.1395 1.3289 1.6970 -0.3303 0.6191  0.1189  536  PRO B CB  
16477 C CG  . PRO C 536  ? 2.1462 1.2749 1.5936 -0.3607 0.5836  0.1367  536  PRO B CG  
16478 C CD  . PRO C 536  ? 2.1984 1.3013 1.5850 -0.3767 0.5452  0.1385  536  PRO B CD  
16479 N N   . SER C 537  ? 2.0140 1.1618 1.5513 -0.2986 0.6192  0.1011  537  SER B N   
16480 C CA  . SER C 537  ? 1.9823 1.1125 1.5301 -0.2721 0.6342  0.0892  537  SER B CA  
16481 C C   . SER C 537  ? 2.1169 1.1466 1.5380 -0.2792 0.6077  0.0983  537  SER B C   
16482 O O   . SER C 537  ? 2.1990 1.2025 1.5477 -0.3108 0.5682  0.1116  537  SER B O   
16483 C CB  . SER C 537  ? 1.9821 1.0959 1.5702 -0.2319 0.6910  0.0795  537  SER B CB  
16484 O OG  . SER C 537  ? 2.0490 1.0588 1.5389 -0.2195 0.7110  0.0887  537  SER B OG  
16485 N N   . SER C 538  ? 2.2301 1.2054 1.6265 -0.2498 0.6286  0.0904  538  SER B N   
16486 C CA  . SER C 538  ? 2.2769 1.1519 1.5553 -0.2516 0.6065  0.0969  538  SER B CA  
16487 C C   . SER C 538  ? 2.2776 1.1196 1.5651 -0.2140 0.6349  0.0828  538  SER B C   
16488 O O   . SER C 538  ? 2.1910 1.1032 1.5825 -0.1939 0.6597  0.0682  538  SER B O   
16489 C CB  . SER C 538  ? 2.2954 1.1891 1.5450 -0.2873 0.5498  0.1040  538  SER B CB  
16490 O OG  . SER C 538  ? 2.2913 1.1735 1.4845 -0.3218 0.5194  0.1198  538  SER B OG  
16491 N N   . ARG C 539  ? 2.3674 1.1024 1.5470 -0.2034 0.6321  0.0864  539  ARG B N   
16492 C CA  . ARG C 539  ? 2.3801 1.0819 1.5560 -0.1746 0.6431  0.0736  539  ARG B CA  
16493 C C   . ARG C 539  ? 2.5012 1.1163 1.5625 -0.1882 0.6031  0.0820  539  ARG B C   
16494 O O   . ARG C 539  ? 2.5781 1.1413 1.5517 -0.2131 0.5774  0.0973  539  ARG B O   
16495 C CB  . ARG C 539  ? 2.3913 1.0459 1.5645 -0.1335 0.6965  0.0638  539  ARG B CB  
16496 C CG  . ARG C 539  ? 2.3646 1.0254 1.5534 -0.1289 0.7318  0.0687  539  ARG B CG  
16497 C CD  . ARG C 539  ? 2.4621 1.0537 1.6175 -0.0902 0.7792  0.0609  539  ARG B CD  
16498 N NE  . ARG C 539  ? 2.3471 0.9861 1.5955 -0.0571 0.8141  0.0420  539  ARG B NE  
16499 C CZ  . ARG C 539  ? 2.2899 0.9926 1.6337 -0.0412 0.8554  0.0350  539  ARG B CZ  
16500 N NH1 . ARG C 539  ? 2.2852 1.0107 1.6439 -0.0551 0.8664  0.0456  539  ARG B NH1 
16501 N NH2 . ARG C 539  ? 2.2674 1.0106 1.6921 -0.0116 0.8847  0.0174  539  ARG B NH2 
16502 N N   . LEU C 540  ? 2.4674 1.0690 1.5328 -0.1719 0.5969  0.0718  540  LEU B N   
16503 C CA  . LEU C 540  ? 2.6091 1.1198 1.5673 -0.1778 0.5631  0.0773  540  LEU B CA  
16504 C C   . LEU C 540  ? 2.6354 1.1043 1.5943 -0.1382 0.5864  0.0612  540  LEU B C   
16505 O O   . LEU C 540  ? 2.5108 1.0381 1.5651 -0.1116 0.6209  0.0460  540  LEU B O   
16506 C CB  . LEU C 540  ? 2.6652 1.2136 1.6225 -0.2144 0.5083  0.0857  540  LEU B CB  
16507 C CG  . LEU C 540  ? 2.6491 1.2770 1.6938 -0.2143 0.4940  0.0759  540  LEU B CG  
16508 C CD1 . LEU C 540  ? 2.6515 1.2765 1.7446 -0.1715 0.5267  0.0567  540  LEU B CD1 
16509 C CD2 . LEU C 540  ? 2.7382 1.3357 1.7126 -0.2467 0.4365  0.0881  540  LEU B CD2 
16510 N N   . LEU C 541  ? 2.7812 1.1489 1.6335 -0.1346 0.5662  0.0642  541  LEU B N   
16511 C CA  . LEU C 541  ? 2.8291 1.1436 1.6663 -0.0971 0.5844  0.0491  541  LEU B CA  
16512 C C   . LEU C 541  ? 3.0013 1.2361 1.7392 -0.1110 0.5368  0.0560  541  LEU B C   
16513 O O   . LEU C 541  ? 3.0622 1.2664 1.7284 -0.1457 0.4985  0.0730  541  LEU B O   
16514 C CB  . LEU C 541  ? 2.8359 1.0892 1.6379 -0.0645 0.6324  0.0425  541  LEU B CB  
16515 C CG  . LEU C 541  ? 3.0012 1.1315 1.6878 -0.0440 0.6344  0.0398  541  LEU B CG  
16516 C CD1 . LEU C 541  ? 2.9509 1.0582 1.6450 -0.0079 0.6930  0.0293  541  LEU B CD1 
16517 C CD2 . LEU C 541  ? 3.1101 1.1658 1.6786 -0.0763 0.5938  0.0586  541  LEU B CD2 
16518 N N   . VAL C 542  ? 2.8772 1.0778 1.6108 -0.0842 0.5383  0.0430  542  VAL B N   
16519 C CA  . VAL C 542  ? 3.0163 1.1578 1.6752 -0.0991 0.4890  0.0491  542  VAL B CA  
16520 C C   . VAL C 542  ? 3.1639 1.2207 1.7755 -0.0601 0.5033  0.0344  542  VAL B C   
16521 O O   . VAL C 542  ? 3.1056 1.1963 1.7895 -0.0281 0.5311  0.0169  542  VAL B O   
16522 C CB  . VAL C 542  ? 2.9292 1.1562 1.6647 -0.1180 0.4589  0.0496  542  VAL B CB  
16523 C CG1 . VAL C 542  ? 3.0112 1.1766 1.6884 -0.1178 0.4201  0.0495  542  VAL B CG1 
16524 C CG2 . VAL C 542  ? 2.8870 1.1792 1.6395 -0.1641 0.4295  0.0669  542  VAL B CG2 
16525 N N   . TYR C 543  ? 3.4042 1.3516 1.8951 -0.0625 0.4840  0.0408  543  TYR B N   
16526 C CA  . TYR C 543  ? 3.5405 1.3986 1.9756 -0.0255 0.4953  0.0264  543  TYR B CA  
16527 C C   . TYR C 543  ? 3.6695 1.4585 2.0255 -0.0398 0.4415  0.0325  543  TYR B C   
16528 O O   . TYR C 543  ? 3.7240 1.4928 2.0202 -0.0789 0.3983  0.0512  543  TYR B O   
16529 C CB  . TYR C 543  ? 3.6329 1.4115 1.9901 -0.0082 0.5254  0.0251  543  TYR B CB  
16530 C CG  . TYR C 543  ? 3.7487 1.4637 1.9990 -0.0426 0.4920  0.0452  543  TYR B CG  
16531 C CD1 . TYR C 543  ? 3.7175 1.4788 1.9821 -0.0712 0.4948  0.0599  543  TYR B CD1 
16532 C CD2 . TYR C 543  ? 3.8917 1.4990 2.0268 -0.0458 0.4576  0.0488  543  TYR B CD2 
16533 C CE1 . TYR C 543  ? 3.8044 1.5086 1.9724 -0.1021 0.4647  0.0776  543  TYR B CE1 
16534 C CE2 . TYR C 543  ? 3.9770 1.5263 2.0149 -0.0772 0.4272  0.0667  543  TYR B CE2 
16535 C CZ  . TYR C 543  ? 3.9189 1.5182 1.9744 -0.1052 0.4313  0.0811  543  TYR B CZ  
16536 O OH  . TYR C 543  ? 3.9740 1.5192 1.9361 -0.1363 0.4015  0.0985  543  TYR B OH  
16537 N N   . TYR C 544  ? 3.8847 1.6382 2.2417 -0.0081 0.4438  0.0166  544  TYR B N   
16538 C CA  . TYR C 544  ? 4.0228 1.6901 2.2922 -0.0142 0.3968  0.0201  544  TYR B CA  
16539 C C   . TYR C 544  ? 4.1252 1.6857 2.3170 0.0246  0.4170  0.0054  544  TYR B C   
16540 O O   . TYR C 544  ? 4.0870 1.6583 2.3261 0.0656  0.4634  -0.0145 544  TYR B O   
16541 C CB  . TYR C 544  ? 3.9953 1.7087 2.3272 -0.0131 0.3727  0.0148  544  TYR B CB  
16542 C CG  . TYR C 544  ? 3.9284 1.6777 2.3449 0.0327  0.4151  -0.0093 544  TYR B CG  
16543 C CD1 . TYR C 544  ? 3.8043 1.6309 2.3115 0.0501  0.4672  -0.0189 544  TYR B CD1 
16544 C CD2 . TYR C 544  ? 3.9709 1.6780 2.3783 0.0580  0.4020  -0.0225 544  TYR B CD2 
16545 C CE1 . TYR C 544  ? 3.7427 1.6044 2.3287 0.0907  0.5056  -0.0407 544  TYR B CE1 
16546 C CE2 . TYR C 544  ? 3.9029 1.6452 2.3896 0.0999  0.4404  -0.0451 544  TYR B CE2 
16547 C CZ  . TYR C 544  ? 3.7933 1.6137 2.3692 0.1158  0.4925  -0.0541 544  TYR B CZ  
16548 O OH  . TYR C 544  ? 3.7332 1.5917 2.3902 0.1565  0.5314  -0.0766 544  TYR B OH  
16549 N N   . ILE C 545  ? 3.7336 1.1927 1.8068 0.0109  0.3816  0.0148  545  ILE B N   
16550 C CA  . ILE C 545  ? 3.8306 1.1805 1.8146 0.0429  0.3962  0.0027  545  ILE B CA  
16551 C C   . ILE C 545  ? 3.9083 1.2048 1.8768 0.0718  0.3806  -0.0133 545  ILE B C   
16552 O O   . ILE C 545  ? 3.9746 1.2132 1.8776 0.0536  0.3294  -0.0047 545  ILE B O   
16553 C CB  . ILE C 545  ? 3.8927 1.1574 1.7547 0.0144  0.3649  0.0199  545  ILE B CB  
16554 C CG1 . ILE C 545  ? 3.7963 1.1232 1.6789 -0.0224 0.3676  0.0389  545  ILE B CG1 
16555 C CG2 . ILE C 545  ? 4.0167 1.1830 1.7963 0.0481  0.3910  0.0068  545  ILE B CG2 
16556 C CD1 . ILE C 545  ? 3.7654 1.0247 1.5389 -0.0591 0.3277  0.0590  545  ILE B CD1 
16557 N N   . VAL C 546  ? 4.0600 1.3767 2.0897 0.1167  0.4249  -0.0366 546  VAL B N   
16558 C CA  . VAL C 546  ? 4.1701 1.4547 2.2087 0.1489  0.4171  -0.0549 546  VAL B CA  
16559 C C   . VAL C 546  ? 4.4509 1.6149 2.3894 0.1801  0.4178  -0.0690 546  VAL B C   
16560 O O   . VAL C 546  ? 4.4786 1.6158 2.4003 0.2095  0.4623  -0.0822 546  VAL B O   
16561 C CB  . VAL C 546  ? 3.9739 1.3430 2.1334 0.1844  0.4652  -0.0754 546  VAL B CB  
16562 C CG1 . VAL C 546  ? 4.0192 1.3292 2.1654 0.2317  0.4761  -0.1005 546  VAL B CG1 
16563 C CG2 . VAL C 546  ? 3.8438 1.3194 2.1037 0.1610  0.4481  -0.0673 546  VAL B CG2 
16564 N N   . THR C 547  ? 4.4104 1.5034 2.2847 0.1742  0.3681  -0.0668 547  THR B N   
16565 C CA  . THR C 547  ? 4.7177 1.6947 2.4991 0.2046  0.3624  -0.0817 547  THR B CA  
16566 C C   . THR C 547  ? 4.8974 1.8731 2.7282 0.2528  0.3829  -0.1090 547  THR B C   
16567 O O   . THR C 547  ? 4.9743 1.9135 2.7896 0.2570  0.3447  -0.1126 547  THR B O   
16568 C CB  . THR C 547  ? 4.8440 1.7344 2.5231 0.1749  0.2965  -0.0660 547  THR B CB  
16569 O OG1 . THR C 547  ? 4.8451 1.7257 2.4675 0.1336  0.2800  -0.0427 547  THR B OG1 
16570 C CG2 . THR C 547  ? 4.9993 1.7704 2.5869 0.2086  0.2894  -0.0835 547  THR B CG2 
16571 N N   . GLY C 548  ? 5.9327 2.9498 3.8246 0.2887  0.4429  -0.1279 548  GLY B N   
16572 C CA  . GLY C 548  ? 6.1274 3.1279 4.0496 0.3393  0.4680  -0.1567 548  GLY B CA  
16573 C C   . GLY C 548  ? 6.4916 3.3645 4.2965 0.3598  0.4516  -0.1675 548  GLY B C   
16574 O O   . GLY C 548  ? 6.5995 3.4133 4.3181 0.3469  0.4495  -0.1585 548  GLY B O   
16575 N N   . GLU C 549  ? 6.4955 3.3247 4.2959 0.3918  0.4387  -0.1870 549  GLU B N   
16576 C CA  . GLU C 549  ? 6.7946 3.5002 4.4838 0.4112  0.4172  -0.1981 549  GLU B CA  
16577 C C   . GLU C 549  ? 6.8332 3.5242 4.5025 0.4366  0.4620  -0.2134 549  GLU B C   
16578 O O   . GLU C 549  ? 6.8471 3.5658 4.5340 0.4249  0.4255  -0.2174 549  GLU B O   
16579 C CB  . GLU C 549  ? 6.8540 3.6256 4.6559 0.4343  0.3852  -0.2219 549  GLU B CB  
16580 C CG  . GLU C 549  ? 6.8260 3.6979 4.7630 0.4768  0.4287  -0.2540 549  GLU B CG  
16581 C CD  . GLU C 549  ? 6.8087 3.7232 4.7950 0.4829  0.4653  -0.2497 549  GLU B CD  
16582 O OE1 . GLU C 549  ? 6.8250 3.7348 4.7876 0.4494  0.4428  -0.2249 549  GLU B OE1 
16583 O OE2 . GLU C 549  ? 6.7761 3.7297 4.8256 0.5210  0.5173  -0.2716 549  GLU B OE2 
16584 N N   . GLN C 550  ? 6.2849 3.0309 4.0142 0.4594  0.5256  -0.2232 550  GLN B N   
16585 C CA  . GLN C 550  ? 6.2925 3.0099 3.9897 0.4889  0.5768  -0.2385 550  GLN B CA  
16586 C C   . GLN C 550  ? 6.1881 2.9022 3.8362 0.4571  0.5860  -0.2172 550  GLN B C   
16587 O O   . GLN C 550  ? 6.3133 2.9550 3.8767 0.4693  0.5993  -0.2231 550  GLN B O   
16588 C CB  . GLN C 550  ? 6.2337 3.0315 4.0375 0.5265  0.6385  -0.2600 550  GLN B CB  
16589 C CG  . GLN C 550  ? 6.0864 3.0047 3.9976 0.5034  0.6628  -0.2453 550  GLN B CG  
16590 C CD  . GLN C 550  ? 6.0021 2.9891 4.0032 0.4959  0.6389  -0.2437 550  GLN B CD  
16591 O OE1 . GLN C 550  ? 6.0706 3.0164 4.0573 0.5102  0.6065  -0.2541 550  GLN B OE1 
16592 N NE2 . GLN C 550  ? 5.8467 2.9393 3.9417 0.4737  0.6542  -0.2308 550  GLN B NE2 
16593 N N   . THR C 551  ? 5.8856 2.6776 3.5858 0.4169  0.5784  -0.1932 551  THR B N   
16594 C CA  . THR C 551  ? 5.7512 2.5529 3.4195 0.3886  0.5922  -0.1739 551  THR B CA  
16595 C C   . THR C 551  ? 5.4910 2.3664 3.2039 0.3387  0.5660  -0.1459 551  THR B C   
16596 O O   . THR C 551  ? 5.3694 2.3263 3.1767 0.3323  0.5615  -0.1443 551  THR B O   
16597 C CB  . THR C 551  ? 5.7106 2.5610 3.4308 0.4160  0.6620  -0.1864 551  THR B CB  
16598 O OG1 . THR C 551  ? 5.8473 2.6262 3.5158 0.4606  0.6882  -0.2119 551  THR B OG1 
16599 C CG2 . THR C 551  ? 5.6894 2.5547 3.3823 0.3852  0.6751  -0.1650 551  THR B CG2 
16600 N N   . ALA C 552  ? 5.2534 2.1009 2.8978 0.3039  0.5489  -0.1246 552  ALA B N   
16601 C CA  . ALA C 552  ? 5.0090 1.9257 2.6899 0.2560  0.5267  -0.0982 552  ALA B CA  
16602 C C   . ALA C 552  ? 4.6895 1.7231 2.4908 0.2597  0.5748  -0.0992 552  ALA B C   
16603 O O   . ALA C 552  ? 4.6572 1.7017 2.4630 0.2727  0.6211  -0.1027 552  ALA B O   
16604 C CB  . ALA C 552  ? 5.0862 1.9477 2.6690 0.2238  0.5075  -0.0782 552  ALA B CB  
16605 N N   . GLU C 553  ? 4.7117 1.8315 2.6091 0.2482  0.5632  -0.0960 553  GLU B N   
16606 C CA  . GLU C 553  ? 4.4044 1.6403 2.4240 0.2508  0.6048  -0.0976 553  GLU B CA  
16607 C C   . GLU C 553  ? 4.2076 1.5251 2.2762 0.2037  0.5823  -0.0737 553  GLU B C   
16608 O O   . GLU C 553  ? 4.1576 1.5056 2.2521 0.1806  0.5411  -0.0652 553  GLU B O   
16609 C CB  . GLU C 553  ? 4.2679 1.5543 2.3818 0.2850  0.6243  -0.1192 553  GLU B CB  
16610 C CG  . GLU C 553  ? 4.1365 1.4946 2.3417 0.3138  0.6898  -0.1334 553  GLU B CG  
16611 C CD  . GLU C 553  ? 3.9634 1.4292 2.2991 0.3184  0.7008  -0.1397 553  GLU B CD  
16612 O OE1 . GLU C 553  ? 3.8860 1.4136 2.2639 0.2825  0.6716  -0.1229 553  GLU B OE1 
16613 O OE2 . GLU C 553  ? 3.9116 1.4023 2.3084 0.3579  0.7393  -0.1621 553  GLU B OE2 
16614 N N   . LEU C 554  ? 4.0940 1.4472 2.1751 0.1900  0.6098  -0.0634 554  LEU B N   
16615 C CA  . LEU C 554  ? 3.9421 1.3870 2.0885 0.1517  0.5990  -0.0449 554  LEU B CA  
16616 C C   . LEU C 554  ? 3.7725 1.3254 2.0552 0.1684  0.6305  -0.0569 554  LEU B C   
16617 O O   . LEU C 554  ? 3.7534 1.3129 2.0774 0.2089  0.6741  -0.0773 554  LEU B O   
16618 C CB  . LEU C 554  ? 3.9403 1.3867 2.0571 0.1338  0.6192  -0.0310 554  LEU B CB  
16619 C CG  . LEU C 554  ? 4.0477 1.4391 2.0650 0.0930  0.5752  -0.0085 554  LEU B CG  
16620 C CD1 . LEU C 554  ? 3.9955 1.4230 2.0191 0.0713  0.5953  0.0064  554  LEU B CD1 
16621 C CD2 . LEU C 554  ? 4.0578 1.4729 2.0817 0.0572  0.5171  0.0047  554  LEU B CD2 
16622 N N   . VAL C 555  ? 4.5732 2.2116 2.9255 0.1370  0.6079  -0.0447 555  VAL B N   
16623 C CA  . VAL C 555  ? 4.4072 2.1554 2.8920 0.1480  0.6354  -0.0542 555  VAL B CA  
16624 C C   . VAL C 555  ? 4.2517 2.0888 2.7931 0.1060  0.6166  -0.0359 555  VAL B C   
16625 O O   . VAL C 555  ? 4.2744 2.0968 2.7678 0.0689  0.5673  -0.0187 555  VAL B O   
16626 C CB  . VAL C 555  ? 4.4250 2.1836 2.9517 0.1677  0.6199  -0.0689 555  VAL B CB  
16627 C CG1 . VAL C 555  ? 4.2925 2.1730 2.9517 0.1639  0.6309  -0.0723 555  VAL B CG1 
16628 C CG2 . VAL C 555  ? 4.4834 2.1857 2.9940 0.2174  0.6543  -0.0926 555  VAL B CG2 
16629 N N   . SER C 556  ? 3.2797 1.2092 1.9233 0.1115  0.6556  -0.0399 556  SER B N   
16630 C CA  . SER C 556  ? 3.1699 1.1930 1.8799 0.0745  0.6385  -0.0256 556  SER B CA  
16631 C C   . SER C 556  ? 3.0431 1.1802 1.8882 0.0854  0.6772  -0.0348 556  SER B C   
16632 O O   . SER C 556  ? 3.0415 1.1964 1.9438 0.1232  0.7196  -0.0534 556  SER B O   
16633 C CB  . SER C 556  ? 3.1876 1.1845 1.8300 0.0418  0.6262  -0.0054 556  SER B CB  
16634 O OG  . SER C 556  ? 3.1126 1.1633 1.8134 0.0474  0.6703  -0.0058 556  SER B OG  
16635 N N   . ASP C 557  ? 3.3336 1.5488 2.2286 0.0504  0.6594  -0.0214 557  ASP B N   
16636 C CA  . ASP C 557  ? 3.1235 1.4463 2.1382 0.0528  0.6922  -0.0262 557  ASP B CA  
16637 C C   . ASP C 557  ? 3.0258 1.3975 2.0478 0.0103  0.6709  -0.0072 557  ASP B C   
16638 O O   . ASP C 557  ? 3.0637 1.3899 2.0019 -0.0210 0.6294  0.0091  557  ASP B O   
16639 C CB  . ASP C 557  ? 3.0583 1.4601 2.1771 0.0651  0.6914  -0.0401 557  ASP B CB  
16640 C CG  . ASP C 557  ? 2.9411 1.4509 2.1879 0.0739  0.7308  -0.0484 557  ASP B CG  
16641 O OD1 . ASP C 557  ? 2.9370 1.4449 2.1908 0.0846  0.7704  -0.0486 557  ASP B OD1 
16642 O OD2 . ASP C 557  ? 2.8484 1.4442 2.1878 0.0699  0.7217  -0.0545 557  ASP B OD2 
16643 N N   . SER C 558  ? 2.5629 1.0274 1.6860 0.0097  0.6995  -0.0098 558  SER B N   
16644 C CA  . SER C 558  ? 2.5298 1.0434 1.6676 -0.0256 0.6870  0.0058  558  SER B CA  
16645 C C   . SER C 558  ? 2.3842 1.0204 1.6593 -0.0254 0.7077  -0.0016 558  SER B C   
16646 O O   . SER C 558  ? 2.3075 0.9817 1.6610 0.0060  0.7417  -0.0186 558  SER B O   
16647 C CB  . SER C 558  ? 2.5865 1.0441 1.6641 -0.0216 0.7144  0.0132  558  SER B CB  
16648 O OG  . SER C 558  ? 2.5369 1.0181 1.6782 0.0127  0.7706  -0.0001 558  SER B OG  
16649 N N   . VAL C 559  ? 3.0561 1.7540 2.3605 -0.0598 0.6878  0.0106  559  VAL B N   
16650 C CA  . VAL C 559  ? 2.9059 1.7216 2.3395 -0.0623 0.7047  0.0040  559  VAL B CA  
16651 C C   . VAL C 559  ? 2.9060 1.7535 2.3491 -0.0860 0.7081  0.0164  559  VAL B C   
16652 O O   . VAL C 559  ? 3.0208 1.8182 2.3763 -0.1123 0.6808  0.0325  559  VAL B O   
16653 C CB  . VAL C 559  ? 2.7853 1.6761 2.2752 -0.0834 0.6659  0.0026  559  VAL B CB  
16654 C CG1 . VAL C 559  ? 2.7244 1.6162 2.2489 -0.0542 0.6727  -0.0139 559  VAL B CG1 
16655 C CG2 . VAL C 559  ? 2.8049 1.6549 2.2024 -0.1220 0.6110  0.0203  559  VAL B CG2 
16656 N N   . TRP C 560  ? 2.8627 1.7929 2.4125 -0.0764 0.7410  0.0086  560  TRP B N   
16657 C CA  . TRP C 560  ? 2.8197 1.7908 2.3911 -0.0995 0.7416  0.0194  560  TRP B CA  
16658 C C   . TRP C 560  ? 2.7104 1.7754 2.3443 -0.1323 0.7026  0.0219  560  TRP B C   
16659 O O   . TRP C 560  ? 2.6651 1.7867 2.3635 -0.1280 0.6928  0.0111  560  TRP B O   
16660 C CB  . TRP C 560  ? 2.8252 1.8331 2.4744 -0.0746 0.7953  0.0114  560  TRP B CB  
16661 C CG  . TRP C 560  ? 2.8708 1.9121 2.5357 -0.0974 0.7948  0.0230  560  TRP B CG  
16662 C CD1 . TRP C 560  ? 2.9849 1.9596 2.5658 -0.1071 0.7974  0.0376  560  TRP B CD1 
16663 C CD2 . TRP C 560  ? 2.7995 1.9498 2.5703 -0.1139 0.7892  0.0207  560  TRP B CD2 
16664 N NE1 . TRP C 560  ? 2.9413 1.9766 2.5701 -0.1286 0.7936  0.0449  560  TRP B NE1 
16665 C CE2 . TRP C 560  ? 2.8207 1.9644 2.5667 -0.1330 0.7882  0.0343  560  TRP B CE2 
16666 C CE3 . TRP C 560  ? 2.7274 1.9809 2.6123 -0.1139 0.7842  0.0077  560  TRP B CE3 
16667 C CZ2 . TRP C 560  ? 2.7403 1.9767 2.5728 -0.1514 0.7824  0.0348  560  TRP B CZ2 
16668 C CZ3 . TRP C 560  ? 2.6553 2.0017 2.6260 -0.1322 0.7791  0.0079  560  TRP B CZ3 
16669 C CH2 . TRP C 560  ? 2.6519 1.9891 2.5966 -0.1504 0.7781  0.0211  560  TRP B CH2 
16670 N N   . LEU C 561  ? 1.8673 0.9498 1.4819 -0.1647 0.6802  0.0357  561  LEU B N   
16671 C CA  . LEU C 561  ? 1.8048 0.9593 1.4497 -0.2006 0.6344  0.0403  561  LEU B CA  
16672 C C   . LEU C 561  ? 1.7245 0.9639 1.4358 -0.2245 0.6288  0.0442  561  LEU B C   
16673 O O   . LEU C 561  ? 1.7346 0.9689 1.3947 -0.2585 0.5922  0.0578  561  LEU B O   
16674 C CB  . LEU C 561  ? 1.8790 0.9618 1.4052 -0.2289 0.5876  0.0557  561  LEU B CB  
16675 C CG  . LEU C 561  ? 1.9521 0.9614 1.4040 -0.2213 0.5684  0.0553  561  LEU B CG  
16676 C CD1 . LEU C 561  ? 2.0094 0.9655 1.3548 -0.2585 0.5187  0.0735  561  LEU B CD1 
16677 C CD2 . LEU C 561  ? 1.8906 0.9686 1.4242 -0.2133 0.5605  0.0419  561  LEU B CD2 
16678 N N   . ASN C 562  ? 2.1152 1.4347 1.9408 -0.2082 0.6616  0.0322  562  ASN B N   
16679 C CA  . ASN C 562  ? 2.0548 1.4528 1.9448 -0.2290 0.6569  0.0350  562  ASN B CA  
16680 C C   . ASN C 562  ? 1.9115 1.3630 1.8018 -0.2675 0.6054  0.0406  562  ASN B C   
16681 O O   . ASN C 562  ? 1.9118 1.3953 1.8208 -0.2732 0.5820  0.0351  562  ASN B O   
16682 C CB  . ASN C 562  ? 1.8905 1.3863 1.9191 -0.2096 0.6891  0.0185  562  ASN B CB  
16683 C CG  . ASN C 562  ? 2.0057 1.5685 2.0949 -0.2263 0.6903  0.0213  562  ASN B CG  
16684 O OD1 . ASN C 562  ? 1.9949 1.5879 2.0691 -0.2597 0.6521  0.0295  562  ASN B OD1 
16685 N ND2 . ASN C 562  ? 1.9501 1.5363 2.1086 -0.2030 0.7339  0.0145  562  ASN B ND2 
16686 N N   . ILE C 563  ? 2.0823 1.5457 1.9524 -0.2946 0.5871  0.0517  563  ILE B N   
16687 C CA  . ILE C 563  ? 2.0795 1.6059 1.9617 -0.3309 0.5400  0.0552  563  ILE B CA  
16688 C C   . ILE C 563  ? 2.0578 1.6682 2.0093 -0.3503 0.5342  0.0550  563  ILE B C   
16689 O O   . ILE C 563  ? 2.0147 1.6443 2.0209 -0.3334 0.5689  0.0506  563  ILE B O   
16690 C CB  . ILE C 563  ? 2.1693 1.6152 1.9252 -0.3553 0.4998  0.0708  563  ILE B CB  
16691 C CG1 . ILE C 563  ? 2.2228 1.6387 1.9140 -0.3817 0.4820  0.0861  563  ILE B CG1 
16692 C CG2 . ILE C 563  ? 2.2166 1.5513 1.8866 -0.3301 0.5171  0.0729  563  ILE B CG2 
16693 C CD1 . ILE C 563  ? 2.3377 1.6999 1.9227 -0.4127 0.4348  0.1004  563  ILE B CD1 
16694 N N   . GLU C 564  ? 2.1203 1.7827 2.0711 -0.3858 0.4896  0.0593  564  GLU B N   
16695 C CA  . GLU C 564  ? 2.0834 1.8365 2.1064 -0.4058 0.4785  0.0567  564  GLU B CA  
16696 C C   . GLU C 564  ? 2.1665 1.8717 2.1329 -0.4163 0.4806  0.0699  564  GLU B C   
16697 O O   . GLU C 564  ? 2.2722 1.9075 2.1315 -0.4371 0.4546  0.0852  564  GLU B O   
16698 C CB  . GLU C 564  ? 2.1025 1.9278 2.1403 -0.4412 0.4296  0.0567  564  GLU B CB  
16699 C CG  . GLU C 564  ? 2.2412 1.9996 2.1567 -0.4731 0.3874  0.0746  564  GLU B CG  
16700 C CD  . GLU C 564  ? 2.2771 2.1197 2.2173 -0.5130 0.3437  0.0764  564  GLU B CD  
16701 O OE1 . GLU C 564  ? 2.3693 2.1847 2.2321 -0.5419 0.3037  0.0878  564  GLU B OE1 
16702 O OE2 . GLU C 564  ? 2.2070 2.1439 2.2448 -0.5156 0.3491  0.0660  564  GLU B OE2 
16703 N N   . GLU C 565  ? 1.8377 1.5828 1.8784 -0.4024 0.5107  0.0639  565  GLU B N   
16704 C CA  . GLU C 565  ? 1.9316 1.6423 1.9333 -0.4113 0.5141  0.0754  565  GLU B CA  
16705 C C   . GLU C 565  ? 1.9361 1.6934 1.9270 -0.4508 0.4687  0.0817  565  GLU B C   
16706 O O   . GLU C 565  ? 1.8673 1.6825 1.9180 -0.4581 0.4695  0.0791  565  GLU B O   
16707 C CB  . GLU C 565  ? 1.9287 1.6792 2.0239 -0.3865 0.5565  0.0665  565  GLU B CB  
16708 C CG  . GLU C 565  ? 1.9760 1.6962 2.0948 -0.3486 0.6000  0.0579  565  GLU B CG  
16709 C CD  . GLU C 565  ? 1.9642 1.7048 2.1556 -0.3253 0.6432  0.0528  565  GLU B CD  
16710 O OE1 . GLU C 565  ? 1.9398 1.7271 2.1718 -0.3396 0.6357  0.0547  565  GLU B OE1 
16711 O OE2 . GLU C 565  ? 1.9651 1.6755 2.1730 -0.2934 0.6836  0.0471  565  GLU B OE2 
16712 N N   . LYS C 566  ? 2.1326 1.8650 2.0483 -0.4761 0.4288  0.0898  566  LYS B N   
16713 C CA  . LYS C 566  ? 2.1967 1.9516 2.0749 -0.5153 0.3840  0.0988  566  LYS B CA  
16714 C C   . LYS C 566  ? 2.2888 1.9536 2.0708 -0.5209 0.3859  0.1152  566  LYS B C   
16715 O O   . LYS C 566  ? 2.3508 1.9102 2.0293 -0.5142 0.3904  0.1262  566  LYS B O   
16716 C CB  . LYS C 566  ? 2.2610 2.0016 2.0772 -0.5384 0.3441  0.1042  566  LYS B CB  
16717 C CG  . LYS C 566  ? 2.3082 2.0787 2.0861 -0.5817 0.2940  0.1130  566  LYS B CG  
16718 C CD  . LYS C 566  ? 2.3517 2.1601 2.1265 -0.6024 0.2584  0.1114  566  LYS B CD  
16719 C CE  . LYS C 566  ? 2.4113 2.2678 2.1635 -0.6468 0.2084  0.1180  566  LYS B CE  
16720 N NZ  . LYS C 566  ? 2.5258 2.2830 2.1429 -0.6688 0.1820  0.1377  566  LYS B NZ  
16721 N N   . CYS C 567  ? 3.2423 2.0041 2.7006 -0.1504 0.1103  -0.0422 567  CYS B N   
16722 C CA  . CYS C 567  ? 3.2685 2.0250 2.6927 -0.1676 0.1293  -0.0447 567  CYS B CA  
16723 C C   . CYS C 567  ? 3.2971 2.0617 2.6863 -0.1777 0.1391  -0.0415 567  CYS B C   
16724 O O   . CYS C 567  ? 3.3020 2.0764 2.6922 -0.1712 0.1304  -0.0371 567  CYS B O   
16725 C CB  . CYS C 567  ? 3.2779 2.0429 2.6742 -0.1629 0.1157  -0.0452 567  CYS B CB  
16726 S SG  . CYS C 567  ? 4.0756 2.8264 3.5053 -0.1576 0.1112  -0.0500 567  CYS B SG  
16727 N N   . GLY C 568  ? 2.8036 1.5637 2.1619 -0.1940 0.1574  -0.0437 568  GLY B N   
16728 C CA  . GLY C 568  ? 2.8329 1.6007 2.1550 -0.2049 0.1679  -0.0413 568  GLY B CA  
16729 C C   . GLY C 568  ? 2.8382 1.6292 2.1179 -0.1965 0.1476  -0.0374 568  GLY B C   
16730 O O   . GLY C 568  ? 2.8472 1.6539 2.1186 -0.1874 0.1329  -0.0329 568  GLY B O   
16731 N N   . ASN C 569  ? 3.4996 2.2928 2.7524 -0.1998 0.1464  -0.0393 569  ASN B N   
16732 C CA  . ASN C 569  ? 3.4993 2.3147 2.7152 -0.1902 0.1251  -0.0368 569  ASN B CA  
16733 C C   . ASN C 569  ? 3.4571 2.2804 2.6922 -0.1699 0.0980  -0.0363 569  ASN B C   
16734 O O   . ASN C 569  ? 3.4665 2.2788 2.7183 -0.1677 0.0963  -0.0393 569  ASN B O   
16735 C CB  . ASN C 569  ? 3.5253 2.3401 2.7027 -0.2021 0.1344  -0.0388 569  ASN B CB  
16736 C CG  . ASN C 569  ? 3.5610 2.3861 2.6977 -0.2138 0.1451  -0.0372 569  ASN B CG  
16737 O OD1 . ASN C 569  ? 3.5711 2.4097 2.7006 -0.2093 0.1384  -0.0339 569  ASN B OD1 
16738 N ND2 . ASN C 569  ? 3.5737 2.3927 2.6830 -0.2292 0.1617  -0.0394 569  ASN B ND2 
16739 N N   . GLN C 570  ? 4.1073 2.9495 3.3402 -0.1557 0.0769  -0.0327 570  GLN B N   
16740 C CA  . GLN C 570  ? 4.0775 2.9302 3.3248 -0.1363 0.0500  -0.0326 570  GLN B CA  
16741 C C   . GLN C 570  ? 4.1274 2.9898 3.3414 -0.1337 0.0392  -0.0344 570  GLN B C   
16742 O O   . GLN C 570  ? 4.1358 3.0181 3.3125 -0.1316 0.0296  -0.0331 570  GLN B O   
16743 C CB  . GLN C 570  ? 4.0266 2.8994 3.2751 -0.1227 0.0299  -0.0284 570  GLN B CB  
16744 C CG  . GLN C 570  ? 4.4598 3.3280 3.7554 -0.1095 0.0182  -0.0274 570  GLN B CG  
16745 C CD  . GLN C 570  ? 4.4459 3.3022 3.7669 -0.1162 0.0329  -0.0250 570  GLN B CD  
16746 O OE1 . GLN C 570  ? 4.4405 3.2821 3.7586 -0.1324 0.0576  -0.0263 570  GLN B OE1 
16747 N NE2 . GLN C 570  ? 4.4339 3.2966 3.7801 -0.1037 0.0176  -0.0217 570  GLN B NE2 
16748 N N   . LEU C 571  ? 3.1166 1.9647 2.3438 -0.1344 0.0413  -0.0377 571  LEU B N   
16749 C CA  . LEU C 571  ? 3.1284 1.9843 2.3291 -0.1296 0.0278  -0.0393 571  LEU B CA  
16750 C C   . LEU C 571  ? 3.1600 2.0235 2.3826 -0.1097 0.0015  -0.0400 571  LEU B C   
16751 O O   . LEU C 571  ? 3.1691 2.0185 2.4310 -0.1055 0.0017  -0.0413 571  LEU B O   
16752 C CB  . LEU C 571  ? 3.0400 1.8755 2.2364 -0.1437 0.0454  -0.0422 571  LEU B CB  
16753 C CG  . LEU C 571  ? 2.9497 1.7893 2.1299 -0.1358 0.0279  -0.0438 571  LEU B CG  
16754 C CD1 . LEU C 571  ? 2.8694 1.7359 2.0136 -0.1251 0.0067  -0.0427 571  LEU B CD1 
16755 C CD2 . LEU C 571  ? 2.8927 1.7147 2.0566 -0.1520 0.0452  -0.0457 571  LEU B CD2 
16756 N N   . GLN C 572  ? 3.2444 2.1305 2.4412 -0.0978 -0.0207 -0.0397 572  GLN B N   
16757 C CA  . GLN C 572  ? 3.2615 2.1572 2.4742 -0.0788 -0.0471 -0.0410 572  GLN B CA  
16758 C C   . GLN C 572  ? 3.2162 2.1233 2.3947 -0.0741 -0.0615 -0.0433 572  GLN B C   
16759 O O   . GLN C 572  ? 3.2018 2.1192 2.3411 -0.0813 -0.0575 -0.0431 572  GLN B O   
16760 C CB  . GLN C 572  ? 3.3914 2.3068 2.6151 -0.0652 -0.0642 -0.0386 572  GLN B CB  
16761 C CG  . GLN C 572  ? 3.5123 2.4372 2.7604 -0.0450 -0.0908 -0.0400 572  GLN B CG  
16762 C CD  . GLN C 572  ? 3.6080 2.5117 2.9029 -0.0423 -0.0871 -0.0411 572  GLN B CD  
16763 O OE1 . GLN C 572  ? 3.6366 2.5222 2.9541 -0.0527 -0.0671 -0.0401 572  GLN B OE1 
16764 N NE2 . GLN C 572  ? 3.6474 2.5540 2.9576 -0.0282 -0.1068 -0.0436 572  GLN B NE2 
16765 N N   . VAL C 573  ? 2.8526 1.7575 2.0472 -0.0621 -0.0783 -0.0456 573  VAL B N   
16766 C CA  . VAL C 573  ? 2.8127 1.7276 1.9803 -0.0553 -0.0949 -0.0481 573  VAL B CA  
16767 C C   . VAL C 573  ? 2.8299 1.7645 2.0080 -0.0334 -0.1255 -0.0500 573  VAL B C   
16768 O O   . VAL C 573  ? 2.8346 1.7623 2.0496 -0.0238 -0.1338 -0.0506 573  VAL B O   
16769 C CB  . VAL C 573  ? 2.6946 1.5856 1.8686 -0.0628 -0.0863 -0.0498 573  VAL B CB  
16770 C CG1 . VAL C 573  ? 2.6741 1.5577 1.8124 -0.0806 -0.0675 -0.0492 573  VAL B CG1 
16771 C CG2 . VAL C 573  ? 2.6352 1.5035 1.8534 -0.0671 -0.0724 -0.0495 573  VAL B CG2 
16772 N N   . HIS C 574  ? 3.0764 2.0362 2.2229 -0.0255 -0.1422 -0.0514 574  HIS B N   
16773 C CA  . HIS C 574  ? 3.0851 2.0660 2.2394 -0.0052 -0.1712 -0.0539 574  HIS B CA  
16774 C C   . HIS C 574  ? 3.1420 2.1333 2.2696 0.0021  -0.1883 -0.0580 574  HIS B C   
16775 O O   . HIS C 574  ? 3.1365 2.1347 2.2268 -0.0055 -0.1836 -0.0586 574  HIS B O   
16776 C CB  . HIS C 574  ? 3.1203 2.1272 2.2661 0.0006  -0.1797 -0.0525 574  HIS B CB  
16777 C CG  . HIS C 574  ? 3.1554 2.1557 2.3338 -0.0006 -0.1716 -0.0487 574  HIS B CG  
16778 N ND1 . HIS C 574  ? 3.1538 2.1400 2.3752 0.0062  -0.1747 -0.0485 574  HIS B ND1 
16779 C CD2 . HIS C 574  ? 3.1767 2.1829 2.3509 -0.0074 -0.1614 -0.0449 574  HIS B CD2 
16780 C CE1 . HIS C 574  ? 3.1558 2.1392 2.3985 0.0037  -0.1667 -0.0448 574  HIS B CE1 
16781 N NE2 . HIS C 574  ? 3.1726 2.1676 2.3873 -0.0045 -0.1587 -0.0424 574  HIS B NE2 
16782 N N   . LEU C 575  ? 2.7495 1.7425 1.8969 0.0172  -0.2088 -0.0611 575  LEU B N   
16783 C CA  . LEU C 575  ? 2.8593 1.8623 1.9858 0.0266  -0.2281 -0.0656 575  LEU B CA  
16784 C C   . LEU C 575  ? 3.0021 2.0396 2.1095 0.0407  -0.2512 -0.0692 575  LEU B C   
16785 O O   . LEU C 575  ? 3.0489 2.1010 2.1770 0.0530  -0.2653 -0.0699 575  LEU B O   
16786 C CB  . LEU C 575  ? 2.7902 1.7788 1.9473 0.0363  -0.2397 -0.0676 575  LEU B CB  
16787 C CG  . LEU C 575  ? 2.7082 1.6638 1.8789 0.0212  -0.2171 -0.0649 575  LEU B CG  
16788 C CD1 . LEU C 575  ? 2.6713 1.6124 1.8734 0.0301  -0.2280 -0.0669 575  LEU B CD1 
16789 C CD2 . LEU C 575  ? 2.7193 1.6687 1.8518 0.0088  -0.2074 -0.0648 575  LEU B CD2 
16790 N N   . SER C 576  ? 4.1848 3.2354 3.2535 0.0392  -0.2559 -0.0719 576  SER B N   
16791 C CA  . SER C 576  ? 4.2929 3.3780 3.3391 0.0501  -0.2751 -0.0759 576  SER B CA  
16792 C C   . SER C 576  ? 4.3125 3.4154 3.3821 0.0702  -0.3014 -0.0799 576  SER B C   
16793 O O   . SER C 576  ? 4.3093 3.4305 3.3869 0.0755  -0.3071 -0.0793 576  SER B O   
16794 C CB  . SER C 576  ? 4.3726 3.4674 3.3785 0.0484  -0.2802 -0.0797 576  SER B CB  
16795 O OG  . SER C 576  ? 4.4271 3.5245 3.4030 0.0329  -0.2613 -0.0770 576  SER B OG  
16796 N N   . PRO C 577  ? 3.5118 2.6100 2.5911 0.0813  -0.3179 -0.0841 577  PRO B N   
16797 C CA  . PRO C 577  ? 3.5177 2.6265 2.6279 0.0988  -0.3391 -0.0871 577  PRO B CA  
16798 C C   . PRO C 577  ? 3.4874 2.5721 2.6383 0.0957  -0.3276 -0.0824 577  PRO B C   
16799 O O   . PRO C 577  ? 3.4975 2.5552 2.6619 0.0903  -0.3187 -0.0811 577  PRO B O   
16800 C CB  . PRO C 577  ? 3.5633 2.6706 2.6707 0.1097  -0.3578 -0.0929 577  PRO B CB  
16801 C CG  . PRO C 577  ? 3.5820 2.6907 2.6491 0.1011  -0.3523 -0.0941 577  PRO B CG  
16802 C CD  . PRO C 577  ? 3.5424 2.6329 2.6009 0.0809  -0.3228 -0.0873 577  PRO B CD  
16803 N N   . ASP C 578  ? 3.5254 2.6200 2.6957 0.0987  -0.3279 -0.0799 578  ASP B N   
16804 C CA  . ASP C 578  ? 3.4609 2.5340 2.6703 0.0956  -0.3164 -0.0755 578  ASP B CA  
16805 C C   . ASP C 578  ? 3.4153 2.4843 2.6596 0.1104  -0.3341 -0.0786 578  ASP B C   
16806 O O   . ASP C 578  ? 3.3635 2.4188 2.6436 0.1110  -0.3289 -0.0759 578  ASP B O   
16807 C CB  . ASP C 578  ? 3.4839 2.5677 2.7010 0.0928  -0.3101 -0.0712 578  ASP B CB  
16808 C CG  . ASP C 578  ? 3.5038 2.5605 2.7487 0.0814  -0.2877 -0.0657 578  ASP B CG  
16809 O OD1 . ASP C 578  ? 3.4979 2.5314 2.7677 0.0809  -0.2832 -0.0661 578  ASP B OD1 
16810 O OD2 . ASP C 578  ? 3.5190 2.5774 2.7607 0.0727  -0.2744 -0.0613 578  ASP B OD2 
16811 N N   . ALA C 579  ? 3.4764 2.5576 2.7103 0.1225  -0.3552 -0.0846 579  ALA B N   
16812 C CA  . ALA C 579  ? 3.4649 2.5426 2.7286 0.1369  -0.3732 -0.0883 579  ALA B CA  
16813 C C   . ALA C 579  ? 3.3903 2.4334 2.6808 0.1289  -0.3579 -0.0853 579  ALA B C   
16814 O O   . ALA C 579  ? 3.4034 2.4258 2.6799 0.1140  -0.3386 -0.0826 579  ALA B O   
16815 C CB  . ALA C 579  ? 3.5112 2.6013 2.7546 0.1475  -0.3938 -0.0951 579  ALA B CB  
16816 N N   . ASP C 580  ? 3.3241 2.3616 2.6530 0.1385  -0.3667 -0.0861 580  ASP B N   
16817 C CA  . ASP C 580  ? 3.2858 2.2922 2.6445 0.1317  -0.3530 -0.0838 580  ASP B CA  
16818 C C   . ASP C 580  ? 3.2635 2.2566 2.6223 0.1361  -0.3630 -0.0876 580  ASP B C   
16819 O O   . ASP C 580  ? 3.2492 2.2235 2.6387 0.1378  -0.3626 -0.0880 580  ASP B O   
16820 C CB  . ASP C 580  ? 3.3283 2.3346 2.7295 0.1393  -0.3568 -0.0827 580  ASP B CB  
16821 C CG  . ASP C 580  ? 3.4239 2.4509 2.8391 0.1593  -0.3853 -0.0879 580  ASP B CG  
16822 O OD1 . ASP C 580  ? 3.4706 2.4976 2.8787 0.1668  -0.3997 -0.0926 580  ASP B OD1 
16823 O OD2 . ASP C 580  ? 3.4519 2.4949 2.8851 0.1673  -0.3936 -0.0872 580  ASP B OD2 
16824 N N   . ALA C 581  ? 3.3702 2.3734 2.6941 0.1377  -0.3721 -0.0906 581  ALA B N   
16825 C CA  . ALA C 581  ? 3.3500 2.3406 2.6685 0.1410  -0.3819 -0.0939 581  ALA B CA  
16826 C C   . ALA C 581  ? 3.3518 2.3527 2.6260 0.1380  -0.3852 -0.0956 581  ALA B C   
16827 O O   . ALA C 581  ? 3.3615 2.3885 2.6141 0.1414  -0.3909 -0.0971 581  ALA B O   
16828 C CB  . ALA C 581  ? 3.3731 2.3753 2.7151 0.1605  -0.4082 -0.0994 581  ALA B CB  
16829 N N   . TYR C 582  ? 2.9329 1.9135 2.1933 0.1314  -0.3820 -0.0955 582  TYR B N   
16830 C CA  . TYR C 582  ? 2.9026 1.8902 2.1207 0.1274  -0.3841 -0.0968 582  TYR B CA  
16831 C C   . TYR C 582  ? 2.8684 1.8519 2.0772 0.1365  -0.4037 -0.1013 582  TYR B C   
16832 O O   . TYR C 582  ? 2.8704 1.8327 2.1008 0.1381  -0.4070 -0.1013 582  TYR B O   
16833 C CB  . TYR C 582  ? 2.8724 1.8401 2.0713 0.1058  -0.3559 -0.0909 582  TYR B CB  
16834 C CG  . TYR C 582  ? 2.8380 1.8161 2.0342 0.0975  -0.3390 -0.0875 582  TYR B CG  
16835 C CD1 . TYR C 582  ? 2.8527 1.8546 2.0160 0.0965  -0.3401 -0.0884 582  TYR B CD1 
16836 C CD2 . TYR C 582  ? 2.7944 1.7589 2.0215 0.0908  -0.3226 -0.0836 582  TYR B CD2 
16837 C CE1 . TYR C 582  ? 2.8395 1.8505 1.9996 0.0886  -0.3250 -0.0850 582  TYR B CE1 
16838 C CE2 . TYR C 582  ? 2.7790 1.7520 2.0040 0.0834  -0.3078 -0.0803 582  TYR B CE2 
16839 C CZ  . TYR C 582  ? 2.8036 1.7996 1.9947 0.0822  -0.3091 -0.0808 582  TYR B CZ  
16840 O OH  . TYR C 582  ? 2.7929 1.7969 1.9809 0.0744  -0.2947 -0.0773 582  TYR B OH  
16841 N N   . SER C 583  ? 3.6769 2.6812 2.8535 0.1423  -0.4171 -0.1054 583  SER B N   
16842 C CA  . SER C 583  ? 3.6732 2.6746 2.8356 0.1500  -0.4355 -0.1098 583  SER B CA  
16843 C C   . SER C 583  ? 3.6637 2.6373 2.8042 0.1328  -0.4188 -0.1048 583  SER B C   
16844 O O   . SER C 583  ? 3.6069 2.5810 2.7219 0.1190  -0.4011 -0.1013 583  SER B O   
16845 C CB  . SER C 583  ? 3.7618 2.7968 2.8973 0.1617  -0.4546 -0.1164 583  SER B CB  
16846 O OG  . SER C 583  ? 3.7902 2.8378 2.8983 0.1507  -0.4392 -0.1139 583  SER B OG  
16847 N N   . PRO C 584  ? 2.8803 1.8301 2.0297 0.1333  -0.4249 -0.1046 584  PRO B N   
16848 C CA  . PRO C 584  ? 2.8953 1.8137 2.0311 0.1152  -0.4069 -0.0989 584  PRO B CA  
16849 C C   . PRO C 584  ? 2.8740 1.7973 1.9659 0.1088  -0.4065 -0.0987 584  PRO B C   
16850 O O   . PRO C 584  ? 2.9061 1.8303 1.9846 0.1174  -0.4259 -0.1022 584  PRO B O   
16851 C CB  . PRO C 584  ? 2.8989 1.7963 2.0546 0.1217  -0.4208 -0.1001 584  PRO B CB  
16852 C CG  . PRO C 584  ? 2.9093 1.8252 2.0959 0.1419  -0.4414 -0.1059 584  PRO B CG  
16853 C CD  . PRO C 584  ? 2.9266 1.8785 2.0976 0.1512  -0.4504 -0.1101 584  PRO B CD  
16854 N N   . GLY C 585  ? 3.3245 2.2504 2.3950 0.0938  -0.3851 -0.0948 585  GLY B N   
16855 C CA  . GLY C 585  ? 3.3633 2.2957 2.3918 0.0871  -0.3836 -0.0947 585  GLY B CA  
16856 C C   . GLY C 585  ? 3.3747 2.3398 2.3840 0.0902  -0.3834 -0.0974 585  GLY B C   
16857 O O   . GLY C 585  ? 3.3970 2.3712 2.3709 0.0845  -0.3810 -0.0978 585  GLY B O   
16858 N N   . GLN C 586  ? 3.0867 2.0693 2.1194 0.0989  -0.3862 -0.0993 586  GLN B N   
16859 C CA  . GLN C 586  ? 3.1241 2.1394 2.1425 0.1032  -0.3882 -0.1022 586  GLN B CA  
16860 C C   . GLN C 586  ? 3.1488 2.1610 2.1425 0.0839  -0.3622 -0.0970 586  GLN B C   
16861 O O   . GLN C 586  ? 3.1216 2.1122 2.1275 0.0693  -0.3390 -0.0910 586  GLN B O   
16862 C CB  . GLN C 586  ? 3.0923 2.1211 2.1442 0.1134  -0.3932 -0.1034 586  GLN B CB  
16863 C CG  . GLN C 586  ? 3.1193 2.1811 2.1599 0.1170  -0.3945 -0.1056 586  GLN B CG  
16864 C CD  . GLN C 586  ? 3.1335 2.2036 2.2086 0.1243  -0.3964 -0.1052 586  GLN B CD  
16865 O OE1 . GLN C 586  ? 3.1219 2.1809 2.2295 0.1324  -0.4046 -0.1057 586  GLN B OE1 
16866 N NE2 . GLN C 586  ? 3.1562 2.2458 2.2241 0.1210  -0.3889 -0.1039 586  GLN B NE2 
16867 N N   . THR C 587  ? 3.3096 2.3438 2.2689 0.0838  -0.3658 -0.0998 587  THR B N   
16868 C CA  . THR C 587  ? 3.3731 2.4106 2.3101 0.0676  -0.3429 -0.0958 587  THR B CA  
16869 C C   . THR C 587  ? 3.3739 2.4241 2.3332 0.0693  -0.3362 -0.0946 587  THR B C   
16870 O O   . THR C 587  ? 3.3438 2.4178 2.3149 0.0852  -0.3552 -0.0994 587  THR B O   
16871 C CB  . THR C 587  ? 3.4521 2.5145 2.3494 0.0697  -0.3516 -0.1002 587  THR B CB  
16872 O OG1 . THR C 587  ? 3.4786 2.5720 2.3804 0.0893  -0.3771 -0.1078 587  THR B OG1 
16873 C CG2 . THR C 587  ? 3.4991 2.5463 2.3746 0.0667  -0.3569 -0.1005 587  THR B CG2 
16874 N N   . VAL C 588  ? 3.1380 2.1716 2.1038 0.0529  -0.3098 -0.0883 588  VAL B N   
16875 C CA  . VAL C 588  ? 3.1350 2.1763 2.1226 0.0525  -0.3011 -0.0860 588  VAL B CA  
16876 C C   . VAL C 588  ? 3.1257 2.1574 2.1014 0.0324  -0.2719 -0.0804 588  VAL B C   
16877 O O   . VAL C 588  ? 3.1480 2.1526 2.1246 0.0176  -0.2525 -0.0763 588  VAL B O   
16878 C CB  . VAL C 588  ? 3.1116 2.1356 2.1440 0.0579  -0.3023 -0.0845 588  VAL B CB  
16879 C CG1 . VAL C 588  ? 3.0964 2.0885 2.1370 0.0508  -0.2957 -0.0824 588  VAL B CG1 
16880 C CG2 . VAL C 588  ? 3.0844 2.1031 2.1364 0.0488  -0.2824 -0.0797 588  VAL B CG2 
16881 N N   . SER C 589  ? 3.9583 3.0120 2.9238 0.0317  -0.2687 -0.0803 589  SER B N   
16882 C CA  . SER C 589  ? 3.9623 3.0099 2.9123 0.0131  -0.2422 -0.0757 589  SER B CA  
16883 C C   . SER C 589  ? 3.9022 2.9297 2.8851 0.0044  -0.2226 -0.0705 589  SER B C   
16884 O O   . SER C 589  ? 3.8682 2.9023 2.8796 0.0142  -0.2305 -0.0705 589  SER B O   
16885 C CB  . SER C 589  ? 4.0315 3.1107 2.9542 0.0148  -0.2466 -0.0777 589  SER B CB  
16886 O OG  . SER C 589  ? 4.0926 3.1968 3.0005 0.0305  -0.2728 -0.0843 589  SER B OG  
16887 N N   . LEU C 590  ? 3.0664 2.0697 2.0454 -0.0141 -0.1972 -0.0665 590  LEU B N   
16888 C CA  . LEU C 590  ? 2.9929 1.9772 2.0013 -0.0240 -0.1764 -0.0623 590  LEU B CA  
16889 C C   . LEU C 590  ? 2.9742 1.9637 1.9666 -0.0379 -0.1558 -0.0593 590  LEU B C   
16890 O O   . LEU C 590  ? 3.0273 2.0192 1.9850 -0.0494 -0.1451 -0.0590 590  LEU B O   
16891 C CB  . LEU C 590  ? 2.9242 1.8757 1.9461 -0.0354 -0.1610 -0.0605 590  LEU B CB  
16892 C CG  . LEU C 590  ? 2.8183 1.7505 1.8563 -0.0524 -0.1322 -0.0566 590  LEU B CG  
16893 C CD1 . LEU C 590  ? 2.7611 1.6924 1.8406 -0.0444 -0.1342 -0.0558 590  LEU B CD1 
16894 C CD2 . LEU C 590  ? 2.7793 1.6818 1.8204 -0.0672 -0.1146 -0.0554 590  LEU B CD2 
16895 N N   . ASN C 591  ? 3.1497 2.1398 2.1682 -0.0369 -0.1502 -0.0570 591  ASN B N   
16896 C CA  . ASN C 591  ? 3.1226 2.1189 2.1296 -0.0482 -0.1331 -0.0540 591  ASN B CA  
16897 C C   . ASN C 591  ? 3.0842 2.0541 2.1101 -0.0650 -0.1046 -0.0504 591  ASN B C   
16898 O O   . ASN C 591  ? 3.0603 2.0114 2.1227 -0.0637 -0.1009 -0.0498 591  ASN B O   
16899 C CB  . ASN C 591  ? 3.1268 2.1467 2.1440 -0.0355 -0.1483 -0.0539 591  ASN B CB  
16900 C CG  . ASN C 591  ? 3.1870 2.2384 2.1744 -0.0241 -0.1705 -0.0577 591  ASN B CG  
16901 O OD1 . ASN C 591  ? 3.2215 2.2885 2.1758 -0.0308 -0.1656 -0.0578 591  ASN B OD1 
16902 N ND2 . ASN C 591  ? 3.2018 2.2631 2.2010 -0.0068 -0.1950 -0.0615 591  ASN B ND2 
16903 N N   . MET C 592  ? 3.3232 2.2926 2.3246 -0.0808 -0.0846 -0.0486 592  MET B N   
16904 C CA  . MET C 592  ? 3.2786 2.2269 2.2967 -0.0967 -0.0576 -0.0457 592  MET B CA  
16905 C C   . MET C 592  ? 3.2950 2.2559 2.3118 -0.0991 -0.0517 -0.0431 592  MET B C   
16906 O O   . MET C 592  ? 3.3125 2.2978 2.3018 -0.0948 -0.0622 -0.0434 592  MET B O   
16907 C CB  . MET C 592  ? 3.2810 2.2134 2.2749 -0.1159 -0.0353 -0.0456 592  MET B CB  
16908 C CG  . MET C 592  ? 3.2532 2.1595 2.2655 -0.1209 -0.0282 -0.0465 592  MET B CG  
16909 S SD  . MET C 592  ? 3.5271 2.4376 2.5161 -0.1122 -0.0492 -0.0490 592  MET B SD  
16910 C CE  . MET C 592  ? 3.4044 2.3294 2.3388 -0.1239 -0.0413 -0.0490 592  MET B CE  
16911 N N   . ALA C 593  ? 2.9781 1.9222 2.0246 -0.1064 -0.0348 -0.0408 593  ALA B N   
16912 C CA  . ALA C 593  ? 3.0126 1.9653 2.0620 -0.1087 -0.0291 -0.0378 593  ALA B CA  
16913 C C   . ALA C 593  ? 3.0537 1.9838 2.1230 -0.1245 -0.0016 -0.0358 593  ALA B C   
16914 O O   . ALA C 593  ? 3.0194 1.9272 2.1196 -0.1278 0.0084  -0.0367 593  ALA B O   
16915 C CB  . ALA C 593  ? 2.9756 1.9423 2.0502 -0.0905 -0.0517 -0.0368 593  ALA B CB  
16916 N N   . THR C 594  ? 3.0751 2.0117 2.1271 -0.1340 0.0103  -0.0335 594  THR B N   
16917 C CA  . THR C 594  ? 3.1315 2.0489 2.2025 -0.1479 0.0352  -0.0319 594  THR B CA  
16918 C C   . THR C 594  ? 3.1929 2.1214 2.2505 -0.1532 0.0411  -0.0286 594  THR B C   
16919 O O   . THR C 594  ? 3.2464 2.1945 2.2659 -0.1548 0.0362  -0.0281 594  THR B O   
16920 C CB  . THR C 594  ? 3.1566 2.0552 2.2156 -0.1663 0.0598  -0.0340 594  THR B CB  
16921 O OG1 . THR C 594  ? 3.1598 2.0588 2.2035 -0.1630 0.0506  -0.0366 594  THR B OG1 
16922 C CG2 . THR C 594  ? 3.1339 2.0064 2.2335 -0.1740 0.0786  -0.0347 594  THR B CG2 
16923 N N   . GLY C 595  ? 3.5634 2.4787 2.6529 -0.1562 0.0516  -0.0264 595  GLY B N   
16924 C CA  . GLY C 595  ? 3.6306 2.5516 2.7115 -0.1630 0.0597  -0.0229 595  GLY B CA  
16925 C C   . GLY C 595  ? 3.7421 2.6552 2.7956 -0.1832 0.0854  -0.0240 595  GLY B C   
16926 O O   . GLY C 595  ? 3.7504 2.6711 2.7846 -0.1907 0.0926  -0.0216 595  GLY B O   
16927 N N   . MET C 596  ? 3.3065 2.2043 2.3583 -0.1923 0.0991  -0.0275 596  MET B N   
16928 C CA  . MET C 596  ? 3.3783 2.2678 2.4037 -0.2122 0.1240  -0.0291 596  MET B CA  
16929 C C   . MET C 596  ? 3.3852 2.2732 2.3882 -0.2155 0.1239  -0.0323 596  MET B C   
16930 O O   . MET C 596  ? 3.3919 2.2738 2.4133 -0.2063 0.1129  -0.0339 596  MET B O   
16931 C CB  . MET C 596  ? 3.3790 2.2430 2.4356 -0.2253 0.1496  -0.0303 596  MET B CB  
16932 C CG  . MET C 596  ? 3.3825 2.2450 2.4579 -0.2258 0.1542  -0.0272 596  MET B CG  
16933 S SD  . MET C 596  ? 3.7251 2.5978 2.7574 -0.2414 0.1693  -0.0254 596  MET B SD  
16934 C CE  . MET C 596  ? 3.1124 1.9700 2.1254 -0.2616 0.1960  -0.0303 596  MET B CE  
16935 N N   . ASP C 597  ? 3.8632 2.7560 2.8265 -0.2288 0.1360  -0.0332 597  ASP B N   
16936 C CA  . ASP C 597  ? 3.8555 2.7456 2.7959 -0.2335 0.1372  -0.0358 597  ASP B CA  
16937 C C   . ASP C 597  ? 3.7457 2.6102 2.7183 -0.2381 0.1482  -0.0380 597  ASP B C   
16938 O O   . ASP C 597  ? 3.7083 2.5552 2.7069 -0.2481 0.1681  -0.0387 597  ASP B O   
16939 C CB  . ASP C 597  ? 3.9642 2.8566 2.8644 -0.2517 0.1562  -0.0364 597  ASP B CB  
16940 C CG  . ASP C 597  ? 4.0749 2.9918 2.9430 -0.2496 0.1485  -0.0346 597  ASP B CG  
16941 O OD1 . ASP C 597  ? 4.1067 3.0442 2.9656 -0.2337 0.1236  -0.0340 597  ASP B OD1 
16942 O OD2 . ASP C 597  ? 4.1190 3.0348 2.9709 -0.2644 0.1678  -0.0342 597  ASP B OD2 
16943 N N   . SER C 598  ? 3.0545 1.9169 2.0259 -0.2311 0.1355  -0.0394 598  SER B N   
16944 C CA  . SER C 598  ? 2.9489 1.7874 1.9501 -0.2356 0.1449  -0.0416 598  SER B CA  
16945 C C   . SER C 598  ? 2.8445 1.6790 1.8323 -0.2337 0.1356  -0.0430 598  SER B C   
16946 O O   . SER C 598  ? 2.8454 1.6966 1.8066 -0.2237 0.1156  -0.0425 598  SER B O   
16947 C CB  . SER C 598  ? 2.9031 1.7342 1.9535 -0.2237 0.1377  -0.0414 598  SER B CB  
16948 O OG  . SER C 598  ? 2.8695 1.6767 1.9509 -0.2309 0.1515  -0.0441 598  SER B OG  
16949 N N   . TRP C 599  ? 3.3761 2.1875 2.3829 -0.2442 0.1508  -0.0450 599  TRP B N   
16950 C CA  . TRP C 599  ? 3.3213 2.1236 2.3187 -0.2459 0.1461  -0.0461 599  TRP B CA  
16951 C C   . TRP C 599  ? 3.2453 2.0415 2.2777 -0.2304 0.1285  -0.0467 599  TRP B C   
16952 O O   . TRP C 599  ? 3.2403 2.0214 2.3118 -0.2319 0.1377  -0.0482 599  TRP B O   
16953 C CB  . TRP C 599  ? 3.3551 2.1352 2.3533 -0.2681 0.1746  -0.0481 599  TRP B CB  
16954 C CG  . TRP C 599  ? 3.4500 2.2343 2.4060 -0.2845 0.1898  -0.0477 599  TRP B CG  
16955 C CD1 . TRP C 599  ? 3.4902 2.2691 2.4413 -0.3020 0.2159  -0.0487 599  TRP B CD1 
16956 C CD2 . TRP C 599  ? 3.5006 2.2958 2.4132 -0.2849 0.1798  -0.0465 599  TRP B CD2 
16957 N NE1 . TRP C 599  ? 3.5283 2.3144 2.4351 -0.3136 0.2230  -0.0481 599  TRP B NE1 
16958 C CE2 . TRP C 599  ? 3.5283 2.3244 2.4109 -0.3033 0.2010  -0.0467 599  TRP B CE2 
16959 C CE3 . TRP C 599  ? 3.5145 2.3188 2.4115 -0.2713 0.1547  -0.0455 599  TRP B CE3 
16960 C CZ2 . TRP C 599  ? 3.5496 2.3556 2.3870 -0.3084 0.1976  -0.0457 599  TRP B CZ2 
16961 C CZ3 . TRP C 599  ? 3.5379 2.3516 2.3907 -0.2762 0.1512  -0.0448 599  TRP B CZ3 
16962 C CH2 . TRP C 599  ? 3.5548 2.3694 2.3782 -0.2945 0.1724  -0.0448 599  TRP B CH2 
16963 N N   . VAL C 600  ? 3.2500 2.0576 2.2688 -0.2158 0.1033  -0.0461 600  VAL B N   
16964 C CA  . VAL C 600  ? 3.1517 1.9550 2.2017 -0.2001 0.0843  -0.0469 600  VAL B CA  
16965 C C   . VAL C 600  ? 3.1175 1.9023 2.1653 -0.2073 0.0872  -0.0480 600  VAL B C   
16966 O O   . VAL C 600  ? 3.1482 1.9267 2.1665 -0.2226 0.1005  -0.0478 600  VAL B O   
16967 C CB  . VAL C 600  ? 3.1380 1.9655 2.1788 -0.1781 0.0529  -0.0461 600  VAL B CB  
16968 C CG1 . VAL C 600  ? 3.1108 1.9360 2.1924 -0.1609 0.0353  -0.0469 600  VAL B CG1 
16969 C CG2 . VAL C 600  ? 3.1325 1.9815 2.1575 -0.1751 0.0511  -0.0446 600  VAL B CG2 
16970 N N   . ALA C 601  ? 2.9102 1.6865 1.9892 -0.1964 0.0746  -0.0491 601  ALA B N   
16971 C CA  . ALA C 601  ? 2.9017 1.6596 1.9826 -0.2020 0.0752  -0.0499 601  ALA B CA  
16972 C C   . ALA C 601  ? 2.8900 1.6488 1.9944 -0.1827 0.0496  -0.0506 601  ALA B C   
16973 O O   . ALA C 601  ? 2.8933 1.6389 2.0366 -0.1804 0.0520  -0.0522 601  ALA B O   
16974 C CB  . ALA C 601  ? 2.8791 1.6130 1.9827 -0.2208 0.1033  -0.0518 601  ALA B CB  
16975 N N   . LEU C 602  ? 2.7923 1.5669 1.8730 -0.1690 0.0252  -0.0499 602  LEU B N   
16976 C CA  . LEU C 602  ? 2.7708 1.5492 1.8705 -0.1495 -0.0011 -0.0509 602  LEU B CA  
16977 C C   . LEU C 602  ? 2.8019 1.5564 1.9189 -0.1545 0.0011  -0.0517 602  LEU B C   
16978 O O   . LEU C 602  ? 2.8211 1.5581 1.9261 -0.1730 0.0200  -0.0512 602  LEU B O   
16979 C CB  . LEU C 602  ? 2.7559 1.5555 1.8224 -0.1362 -0.0258 -0.0507 602  LEU B CB  
16980 C CG  . LEU C 602  ? 2.7401 1.5636 1.7778 -0.1351 -0.0263 -0.0500 602  LEU B CG  
16981 C CD1 . LEU C 602  ? 2.7466 1.5941 1.7608 -0.1176 -0.0550 -0.0512 602  LEU B CD1 
16982 C CD2 . LEU C 602  ? 2.7214 1.5520 1.7839 -0.1329 -0.0187 -0.0495 602  LEU B CD2 
16983 N N   . ALA C 603  ? 3.3261 2.0803 2.4709 -0.1384 -0.0183 -0.0530 603  ALA B N   
16984 C CA  . ALA C 603  ? 3.2679 2.0000 2.4320 -0.1417 -0.0181 -0.0540 603  ALA B CA  
16985 C C   . ALA C 603  ? 3.2345 1.9720 2.4239 -0.1202 -0.0451 -0.0555 603  ALA B C   
16986 O O   . ALA C 603  ? 3.1964 1.9336 2.4240 -0.1125 -0.0464 -0.0570 603  ALA B O   
16987 C CB  . ALA C 603  ? 3.2377 1.9501 2.4323 -0.1571 0.0083  -0.0552 603  ALA B CB  
16988 N N   . ALA C 604  ? 3.4107 2.1526 2.5795 -0.1109 -0.0665 -0.0554 604  ALA B N   
16989 C CA  . ALA C 604  ? 3.3910 2.1406 2.5799 -0.0895 -0.0941 -0.0573 604  ALA B CA  
16990 C C   . ALA C 604  ? 3.3886 2.1156 2.5992 -0.0910 -0.0969 -0.0581 604  ALA B C   
16991 O O   . ALA C 604  ? 3.4223 2.1424 2.6132 -0.0906 -0.1080 -0.0575 604  ALA B O   
16992 C CB  . ALA C 604  ? 3.3789 2.1496 2.5358 -0.0756 -0.1187 -0.0576 604  ALA B CB  
16993 N N   . VAL C 605  ? 2.4862 1.2017 1.7374 -0.0926 -0.0871 -0.0595 605  VAL B N   
16994 C CA  . VAL C 605  ? 2.4848 1.1797 1.7623 -0.0937 -0.0889 -0.0609 605  VAL B CA  
16995 C C   . VAL C 605  ? 2.5042 1.2076 1.7976 -0.0714 -0.1189 -0.0628 605  VAL B C   
16996 O O   . VAL C 605  ? 2.5080 1.2343 1.8009 -0.0542 -0.1372 -0.0636 605  VAL B O   
16997 C CB  . VAL C 605  ? 2.4641 1.1467 1.7827 -0.1015 -0.0688 -0.0627 605  VAL B CB  
16998 C CG1 . VAL C 605  ? 2.4703 1.1311 1.8150 -0.1047 -0.0686 -0.0645 605  VAL B CG1 
16999 C CG2 . VAL C 605  ? 2.4747 1.1503 1.7818 -0.1227 -0.0387 -0.0618 605  VAL B CG2 
17000 N N   . ASP C 606  ? 2.8205 1.5055 2.1276 -0.0723 -0.1240 -0.0636 606  ASP B N   
17001 C CA  . ASP C 606  ? 2.8197 1.5096 2.1534 -0.0527 -0.1482 -0.0661 606  ASP B CA  
17002 C C   . ASP C 606  ? 2.7779 1.4626 2.1579 -0.0518 -0.1384 -0.0683 606  ASP B C   
17003 O O   . ASP C 606  ? 2.7943 1.4572 2.1941 -0.0646 -0.1226 -0.0691 606  ASP B O   
17004 C CB  . ASP C 606  ? 2.8698 1.5418 2.1993 -0.0534 -0.1592 -0.0661 606  ASP B CB  
17005 C CG  . ASP C 606  ? 2.8502 1.5282 2.2064 -0.0324 -0.1852 -0.0691 606  ASP B CG  
17006 O OD1 . ASP C 606  ? 2.8390 1.5391 2.2083 -0.0158 -0.1985 -0.0710 606  ASP B OD1 
17007 O OD2 . ASP C 606  ? 2.8528 1.5136 2.2163 -0.0329 -0.1926 -0.0696 606  ASP B OD2 
17008 N N   . SER C 607  ? 2.7786 1.6912 2.5845 0.0963  -0.8160 -0.5242 607  SER B N   
17009 C CA  . SER C 607  ? 2.7379 1.6087 2.5829 0.0667  -0.7886 -0.4913 607  SER B CA  
17010 C C   . SER C 607  ? 2.6984 1.5135 2.5919 0.0852  -0.7805 -0.4186 607  SER B C   
17011 O O   . SER C 607  ? 2.6489 1.4227 2.5697 0.0680  -0.7521 -0.3792 607  SER B O   
17012 C CB  . SER C 607  ? 2.7534 1.6451 2.6437 0.0301  -0.8104 -0.5263 607  SER B CB  
17013 O OG  . SER C 607  ? 2.7767 1.6754 2.7153 0.0435  -0.8509 -0.5238 607  SER B OG  
17014 N N   . ALA C 608  ? 2.3157 1.1310 2.2203 0.1202  -0.8063 -0.4012 608  ALA B N   
17015 C CA  . ALA C 608  ? 2.2778 1.0445 2.2331 0.1391  -0.8060 -0.3351 608  ALA B CA  
17016 C C   . ALA C 608  ? 2.2384 0.9583 2.1811 0.1440  -0.7604 -0.2797 608  ALA B C   
17017 O O   . ALA C 608  ? 2.1772 0.8566 2.1657 0.1273  -0.7431 -0.2379 608  ALA B O   
17018 C CB  . ALA C 608  ? 2.3703 1.1476 2.3214 0.1805  -0.8355 -0.3278 608  ALA B CB  
17019 N N   . VAL C 609  ? 2.5013 1.2285 2.3809 0.1677  -0.7412 -0.2801 609  VAL B N   
17020 C CA  . VAL C 609  ? 2.4727 1.1598 2.3309 0.1755  -0.6970 -0.2315 609  VAL B CA  
17021 C C   . VAL C 609  ? 2.4082 1.0596 2.3057 0.1407  -0.6707 -0.2056 609  VAL B C   
17022 O O   . VAL C 609  ? 2.3647 0.9784 2.3224 0.1400  -0.6717 -0.1559 609  VAL B O   
17023 C CB  . VAL C 609  ? 2.4926 1.2052 2.2691 0.1814  -0.6749 -0.2652 609  VAL B CB  
17024 C CG1 . VAL C 609  ? 2.5932 1.3378 2.3301 0.2194  -0.6976 -0.2829 609  VAL B CG1 
17025 C CG2 . VAL C 609  ? 2.4591 1.2082 2.2140 0.1435  -0.6764 -0.3299 609  VAL B CG2 
17026 N N   . TYR C 610  ? 2.5349 1.1990 2.3986 0.1117  -0.6479 -0.2398 610  TYR B N   
17027 C CA  . TYR C 610  ? 2.4527 1.0868 2.3453 0.0772  -0.6198 -0.2208 610  TYR B CA  
17028 C C   . TYR C 610  ? 3.1079 1.7201 3.0835 0.0630  -0.6396 -0.1926 610  TYR B C   
17029 O O   . TYR C 610  ? 3.0252 1.5956 3.0392 0.0785  -0.6320 -0.1306 610  TYR B O   
17030 C CB  . TYR C 610  ? 2.4114 1.0796 2.2713 0.0415  -0.6136 -0.2833 610  TYR B CB  
17031 C CG  . TYR C 610  ? 2.5103 1.2173 2.2906 0.0525  -0.6104 -0.3321 610  TYR B CG  
17032 C CD1 . TYR C 610  ? 2.5836 1.2737 2.3076 0.0641  -0.5723 -0.3167 610  TYR B CD1 
17033 C CD2 . TYR C 610  ? 2.5013 1.2628 2.2628 0.0499  -0.6452 -0.3948 610  TYR B CD2 
17034 C CE1 . TYR C 610  ? 2.6921 1.4181 2.3427 0.0731  -0.5697 -0.3626 610  TYR B CE1 
17035 C CE2 . TYR C 610  ? 2.6134 1.4121 2.3024 0.0588  -0.6428 -0.4401 610  TYR B CE2 
17036 C CZ  . TYR C 610  ? 2.6948 1.4752 2.3284 0.0701  -0.6051 -0.4241 610  TYR B CZ  
17037 O OH  . TYR C 610  ? 2.7245 1.5408 2.2860 0.0786  -0.6024 -0.4685 610  TYR B OH  
17038 N N   . GLY C 611  ? 3.3255 1.9667 3.3275 0.0330  -0.6642 -0.2384 611  GLY B N   
17039 C CA  . GLY C 611  ? 3.3579 1.9940 3.4326 0.0232  -0.6961 -0.2295 611  GLY B CA  
17040 C C   . GLY C 611  ? 3.3846 1.9770 3.5263 0.0024  -0.6836 -0.1807 611  GLY B C   
17041 O O   . GLY C 611  ? 3.3537 1.9469 3.5124 -0.0340 -0.6716 -0.1957 611  GLY B O   
17042 N N   . VAL C 612  ? 3.0612 1.6174 3.2426 0.0259  -0.6887 -0.1228 612  VAL B N   
17043 C CA  . VAL C 612  ? 3.1013 1.6136 3.3500 0.0119  -0.6799 -0.0690 612  VAL B CA  
17044 C C   . VAL C 612  ? 3.2032 1.6920 3.4449 -0.0147 -0.6355 -0.0509 612  VAL B C   
17045 O O   . VAL C 612  ? 3.2495 1.7091 3.4648 -0.0003 -0.6001 -0.0102 612  VAL B O   
17046 C CB  . VAL C 612  ? 4.1492 2.6218 4.4222 0.0469  -0.6793 -0.0017 612  VAL B CB  
17047 C CG1 . VAL C 612  ? 4.1697 2.6555 4.4754 0.0662  -0.7267 -0.0100 612  VAL B CG1 
17048 C CG2 . VAL C 612  ? 4.2206 2.6865 4.4307 0.0780  -0.6515 0.0171  612  VAL B CG2 
17049 N N   . GLN C 613  ? 3.9833 2.4849 4.2496 -0.0532 -0.6376 -0.0807 613  GLN B N   
17050 C CA  . GLN C 613  ? 4.0814 2.5684 4.3353 -0.0816 -0.5975 -0.0758 613  GLN B CA  
17051 C C   . GLN C 613  ? 4.2579 2.7559 4.4319 -0.0703 -0.5692 -0.0953 613  GLN B C   
17052 O O   . GLN C 613  ? 4.2731 2.7388 4.4241 -0.0524 -0.5363 -0.0508 613  GLN B O   
17053 C CB  . GLN C 613  ? 4.0587 2.4919 4.3592 -0.0846 -0.5706 -0.0033 613  GLN B CB  
17054 C CG  . GLN C 613  ? 4.0021 2.4188 4.2898 -0.1133 -0.5276 0.0038  613  GLN B CG  
17055 C CD  . GLN C 613  ? 3.9184 2.2963 4.2723 -0.1327 -0.5139 0.0556  613  GLN B CD  
17056 O OE1 . GLN C 613  ? 3.8767 2.2499 4.2920 -0.1369 -0.5424 0.0690  613  GLN B OE1 
17057 N NE2 . GLN C 613  ? 3.8934 2.2437 4.2346 -0.1448 -0.4701 0.0844  613  GLN B NE2 
17058 N N   . ARG C 614  ? 3.6601 2.2049 3.7916 -0.0802 -0.5829 -0.1624 614  ARG B N   
17059 C CA  . ARG C 614  ? 3.7883 2.3468 3.8439 -0.0755 -0.5568 -0.1884 614  ARG B CA  
17060 C C   . ARG C 614  ? 3.8108 2.3481 3.8607 -0.1068 -0.5163 -0.1806 614  ARG B C   
17061 O O   . ARG C 614  ? 3.8008 2.3622 3.8513 -0.1407 -0.5186 -0.2249 614  ARG B O   
17062 C CB  . ARG C 614  ? 3.8283 2.4444 3.8447 -0.0803 -0.5848 -0.2632 614  ARG B CB  
17063 C CG  . ARG C 614  ? 3.8747 2.5083 3.8105 -0.0736 -0.5622 -0.2936 614  ARG B CG  
17064 C CD  . ARG C 614  ? 3.9238 2.6087 3.8224 -0.0575 -0.5961 -0.3479 614  ARG B CD  
17065 N NE  . ARG C 614  ? 3.9634 2.6828 3.8014 -0.0744 -0.5858 -0.4046 614  ARG B NE  
17066 C CZ  . ARG C 614  ? 3.9981 2.7702 3.8199 -0.0850 -0.6155 -0.4678 614  ARG B CZ  
17067 N NH1 . ARG C 614  ? 3.9878 2.7836 3.8486 -0.0793 -0.6571 -0.4825 614  ARG B NH1 
17068 N NH2 . ARG C 614  ? 4.0497 2.8505 3.8164 -0.1012 -0.6036 -0.5160 614  ARG B NH2 
17069 N N   . GLY C 615  ? 5.6908 4.1833 5.7354 -0.0947 -0.4794 -0.1236 615  GLY B N   
17070 C CA  . GLY C 615  ? 5.6793 4.1434 5.7283 -0.1215 -0.4397 -0.1034 615  GLY B CA  
17071 C C   . GLY C 615  ? 5.7152 4.2087 5.7375 -0.1577 -0.4332 -0.1627 615  GLY B C   
17072 O O   . GLY C 615  ? 5.7835 4.3113 5.7483 -0.1546 -0.4384 -0.2134 615  GLY B O   
17073 N N   . ALA C 616  ? 4.0588 2.5394 4.1237 -0.1921 -0.4218 -0.1556 616  ALA B N   
17074 C CA  . ALA C 616  ? 4.0701 2.5751 4.1156 -0.2290 -0.4132 -0.2067 616  ALA B CA  
17075 C C   . ALA C 616  ? 4.1385 2.6473 4.1044 -0.2236 -0.3835 -0.2294 616  ALA B C   
17076 O O   . ALA C 616  ? 4.1942 2.7444 4.1171 -0.2293 -0.3978 -0.2889 616  ALA B O   
17077 C CB  . ALA C 616  ? 4.0000 2.4774 4.0959 -0.2614 -0.3919 -0.1790 616  ALA B CB  
17078 N N   . LYS C 617  ? 4.2665 2.7327 4.2128 -0.2117 -0.3430 -0.1815 617  LYS B N   
17079 C CA  . LYS C 617  ? 4.3031 2.7665 4.1741 -0.2053 -0.3112 -0.1969 617  LYS B CA  
17080 C C   . LYS C 617  ? 4.2730 2.7804 4.1052 -0.2317 -0.3206 -0.2714 617  LYS B C   
17081 O O   . LYS C 617  ? 4.2375 2.7504 4.0928 -0.2683 -0.3159 -0.2913 617  LYS B O   
17082 C CB  . LYS C 617  ? 4.3980 2.8584 4.2257 -0.1608 -0.3123 -0.1797 617  LYS B CB  
17083 C CG  . LYS C 617  ? 4.4765 2.9169 4.2356 -0.1489 -0.2710 -0.1717 617  LYS B CG  
17084 C CD  . LYS C 617  ? 4.4421 2.8337 4.2206 -0.1614 -0.2287 -0.1206 617  LYS B CD  
17085 C CE  . LYS C 617  ? 4.5192 2.8860 4.2324 -0.1431 -0.1879 -0.1035 617  LYS B CE  
17086 N NZ  . LYS C 617  ? 4.4804 2.8016 4.2116 -0.1570 -0.1464 -0.0570 617  LYS B NZ  
17087 N N   . LYS C 618  ? 3.8933 2.4327 3.6679 -0.2132 -0.3341 -0.3115 618  LYS B N   
17088 C CA  . LYS C 618  ? 3.8579 2.4465 3.5978 -0.2353 -0.3510 -0.3854 618  LYS B CA  
17089 C C   . LYS C 618  ? 3.7917 2.4166 3.4762 -0.2071 -0.3727 -0.4216 618  LYS B C   
17090 O O   . LYS C 618  ? 3.8026 2.4099 3.4534 -0.1726 -0.3606 -0.3930 618  LYS B O   
17091 C CB  . LYS C 618  ? 3.9445 2.5241 3.6471 -0.2641 -0.3150 -0.4055 618  LYS B CB  
17092 C CG  . LYS C 618  ? 3.9250 2.4815 3.6780 -0.2999 -0.2973 -0.3875 618  LYS B CG  
17093 C CD  . LYS C 618  ? 3.9230 2.5201 3.7063 -0.3359 -0.3242 -0.4385 618  LYS B CD  
17094 C CE  . LYS C 618  ? 3.8662 2.4400 3.6822 -0.3728 -0.2977 -0.4256 618  LYS B CE  
17095 N NZ  . LYS C 618  ? 3.8106 2.3306 3.6667 -0.3639 -0.2717 -0.3530 618  LYS B NZ  
17096 N N   . PRO C 619  ? 5.1122 3.7895 4.7876 -0.2218 -0.4049 -0.4844 619  PRO B N   
17097 C CA  . PRO C 619  ? 5.1258 3.8441 4.7492 -0.1989 -0.4278 -0.5253 619  PRO B CA  
17098 C C   . PRO C 619  ? 5.1345 3.8582 4.6795 -0.2003 -0.4009 -0.5544 619  PRO B C   
17099 O O   . PRO C 619  ? 5.1842 3.8926 4.6855 -0.1687 -0.3857 -0.5334 619  PRO B O   
17100 C CB  . PRO C 619  ? 5.1377 3.9087 4.7852 -0.2213 -0.4683 -0.5817 619  PRO B CB  
17101 C CG  . PRO C 619  ? 5.0562 3.8099 4.7769 -0.2490 -0.4707 -0.5606 619  PRO B CG  
17102 C CD  . PRO C 619  ? 5.0338 3.7363 4.7540 -0.2597 -0.4244 -0.5174 619  PRO B CD  
17103 N N   . LEU C 620  ? 4.1827 2.9285 3.7105 -0.2365 -0.3957 -0.6022 620  LEU B N   
17104 C CA  . LEU C 620  ? 4.1952 2.9462 3.6498 -0.2424 -0.3707 -0.6338 620  LEU B CA  
17105 C C   . LEU C 620  ? 4.1804 2.8759 3.6203 -0.2453 -0.3216 -0.5904 620  LEU B C   
17106 O O   . LEU C 620  ? 4.2631 2.9507 3.6392 -0.2392 -0.2962 -0.6013 620  LEU B O   
17107 C CB  . LEU C 620  ? 4.1468 2.9415 3.5895 -0.2810 -0.3833 -0.7005 620  LEU B CB  
17108 C CG  . LEU C 620  ? 4.1689 2.9610 3.5480 -0.2994 -0.3525 -0.7308 620  LEU B CG  
17109 C CD1 . LEU C 620  ? 4.2746 3.0881 3.5805 -0.2724 -0.3552 -0.7566 620  LEU B CD1 
17110 C CD2 . LEU C 620  ? 4.1410 2.9668 3.5292 -0.3437 -0.3620 -0.7841 620  LEU B CD2 
17111 N N   . GLU C 621  ? 3.7421 2.3996 3.2409 -0.2544 -0.3085 -0.5418 621  GLU B N   
17112 C CA  . GLU C 621  ? 3.7279 2.3310 3.2209 -0.2558 -0.2625 -0.4941 621  GLU B CA  
17113 C C   . GLU C 621  ? 3.7092 2.2807 3.1757 -0.2116 -0.2456 -0.4443 621  GLU B C   
17114 O O   . GLU C 621  ? 3.7432 2.2842 3.1653 -0.2044 -0.2082 -0.4266 621  GLU B O   
17115 C CB  . GLU C 621  ? 3.6965 2.2728 3.2631 -0.2805 -0.2557 -0.4590 621  GLU B CB  
17116 C CG  . GLU C 621  ? 3.7377 2.2549 3.3142 -0.2765 -0.2121 -0.3962 621  GLU B CG  
17117 C CD  . GLU C 621  ? 3.6792 2.1746 3.3333 -0.2993 -0.2103 -0.3612 621  GLU B CD  
17118 O OE1 . GLU C 621  ? 3.6530 2.1693 3.3324 -0.3356 -0.2199 -0.3954 621  GLU B OE1 
17119 O OE2 . GLU C 621  ? 3.6492 2.1077 3.3398 -0.2809 -0.2000 -0.2993 621  GLU B OE2 
17120 N N   . ARG C 622  ? 3.2680 1.8480 2.7605 -0.1820 -0.2735 -0.4232 622  ARG B N   
17121 C CA  . ARG C 622  ? 3.2381 1.7960 2.7055 -0.1378 -0.2633 -0.3801 622  ARG B CA  
17122 C C   . ARG C 622  ? 3.2509 1.8076 2.6355 -0.1285 -0.2358 -0.4009 622  ARG B C   
17123 O O   . ARG C 622  ? 3.2725 1.7880 2.6338 -0.1160 -0.1980 -0.3608 622  ARG B O   
17124 C CB  . ARG C 622  ? 3.2683 1.8592 2.7476 -0.1102 -0.3059 -0.3892 622  ARG B CB  
17125 C CG  . ARG C 622  ? 3.2939 1.8596 2.7705 -0.0650 -0.3010 -0.3339 622  ARG B CG  
17126 C CD  . ARG C 622  ? 3.0875 1.6802 2.5967 -0.0429 -0.3453 -0.3355 622  ARG B CD  
17127 N NE  . ARG C 622  ? 3.1806 1.8238 2.6406 -0.0316 -0.3715 -0.3923 622  ARG B NE  
17128 C CZ  . ARG C 622  ? 3.2004 1.8714 2.6718 -0.0073 -0.4084 -0.3999 622  ARG B CZ  
17129 N NH1 . ARG C 622  ? 3.1547 1.8067 2.6850 0.0084  -0.4242 -0.3547 622  ARG B NH1 
17130 N NH2 . ARG C 622  ? 3.2638 1.9818 2.6873 0.0013  -0.4297 -0.4529 622  ARG B NH2 
17131 N N   . VAL C 623  ? 3.7356 2.3383 3.0761 -0.1362 -0.2551 -0.4652 623  VAL B N   
17132 C CA  . VAL C 623  ? 3.7716 2.3788 3.0333 -0.1334 -0.2327 -0.4952 623  VAL B CA  
17133 C C   . VAL C 623  ? 3.6963 2.2738 2.9450 -0.1653 -0.1944 -0.4965 623  VAL B C   
17134 O O   . VAL C 623  ? 3.7313 2.2713 2.9441 -0.1522 -0.1573 -0.4667 623  VAL B O   
17135 C CB  . VAL C 623  ? 3.2857 1.9523 2.5095 -0.1389 -0.2649 -0.5662 623  VAL B CB  
17136 C CG1 . VAL C 623  ? 3.3476 2.0204 2.5021 -0.1554 -0.2419 -0.6086 623  VAL B CG1 
17137 C CG2 . VAL C 623  ? 3.3139 2.0032 2.5203 -0.0966 -0.2902 -0.5617 623  VAL B CG2 
17138 N N   . PHE C 624  ? 4.0644 2.6578 3.3431 -0.2062 -0.2029 -0.5294 624  PHE B N   
17139 C CA  . PHE C 624  ? 3.9918 2.5603 3.2584 -0.2387 -0.1685 -0.5354 624  PHE B CA  
17140 C C   . PHE C 624  ? 4.0104 2.5179 3.2930 -0.2304 -0.1275 -0.4682 624  PHE B C   
17141 O O   . PHE C 624  ? 4.0407 2.5212 3.2916 -0.2446 -0.0918 -0.4674 624  PHE B O   
17142 C CB  . PHE C 624  ? 3.7945 2.3869 3.1062 -0.2828 -0.1855 -0.5704 624  PHE B CB  
17143 C CG  . PHE C 624  ? 3.7172 2.3459 2.9820 -0.3108 -0.1900 -0.6400 624  PHE B CG  
17144 C CD1 . PHE C 624  ? 3.6515 2.3334 2.9354 -0.3316 -0.2283 -0.6922 624  PHE B CD1 
17145 C CD2 . PHE C 624  ? 3.7250 2.3349 2.9273 -0.3166 -0.1561 -0.6532 624  PHE B CD2 
17146 C CE1 . PHE C 624  ? 3.6748 2.3915 2.9171 -0.3581 -0.2327 -0.7554 624  PHE B CE1 
17147 C CE2 . PHE C 624  ? 3.7457 2.3886 2.9058 -0.3433 -0.1607 -0.7169 624  PHE B CE2 
17148 C CZ  . PHE C 624  ? 3.7290 2.4257 2.9096 -0.3644 -0.1989 -0.7676 624  PHE B CZ  
17149 N N   . GLN C 625  ? 3.4543 1.9402 2.7863 -0.2077 -0.1326 -0.4119 625  GLN B N   
17150 C CA  . GLN C 625  ? 3.4995 1.9296 2.8448 -0.1948 -0.0948 -0.3446 625  GLN B CA  
17151 C C   . GLN C 625  ? 3.5776 1.9914 2.8507 -0.1636 -0.0689 -0.3350 625  GLN B C   
17152 O O   . GLN C 625  ? 3.6157 2.0114 2.8418 -0.1743 -0.0365 -0.3462 625  GLN B O   
17153 C CB  . GLN C 625  ? 3.5462 1.9606 2.9555 -0.1731 -0.1093 -0.2876 625  GLN B CB  
17154 C CG  . GLN C 625  ? 3.5556 1.9849 3.0409 -0.1999 -0.1376 -0.2921 625  GLN B CG  
17155 C CD  . GLN C 625  ? 3.5902 1.9876 3.1418 -0.1849 -0.1383 -0.2240 625  GLN B CD  
17156 O OE1 . GLN C 625  ? 3.6360 1.9924 3.1820 -0.1635 -0.1080 -0.1687 625  GLN B OE1 
17157 N NE2 . GLN C 625  ? 3.5609 1.9773 3.1758 -0.1965 -0.1729 -0.2278 625  GLN B NE2 
17158 N N   . PHE C 626  ? 3.6340 2.0551 2.8982 -0.1244 -0.0840 -0.3147 626  PHE B N   
17159 C CA  . PHE C 626  ? 3.7075 2.1203 2.9021 -0.0910 -0.0649 -0.3087 626  PHE B CA  
17160 C C   . PHE C 626  ? 3.6562 2.0828 2.7811 -0.1099 -0.0504 -0.3659 626  PHE B C   
17161 O O   . PHE C 626  ? 3.6440 2.0367 2.7336 -0.1128 -0.0114 -0.3525 626  PHE B O   
17162 C CB  . PHE C 626  ? 3.8224 2.2670 3.0090 -0.0561 -0.0986 -0.3136 626  PHE B CB  
17163 C CG  . PHE C 626  ? 4.0154 2.4646 3.1246 -0.0239 -0.0861 -0.3226 626  PHE B CG  
17164 C CD1 . PHE C 626  ? 4.0892 2.5065 3.1861 0.0149  -0.0645 -0.2650 626  PHE B CD1 
17165 C CD2 . PHE C 626  ? 4.1171 2.6041 3.1661 -0.0324 -0.0962 -0.3885 626  PHE B CD2 
17166 C CE1 . PHE C 626  ? 4.2179 2.6407 3.2426 0.0455  -0.0530 -0.2734 626  PHE B CE1 
17167 C CE2 . PHE C 626  ? 4.2473 2.7397 3.2243 -0.0029 -0.0852 -0.3978 626  PHE B CE2 
17168 C CZ  . PHE C 626  ? 4.2952 2.7555 3.2595 0.0365  -0.0635 -0.3404 626  PHE B CZ  
17169 N N   . LEU C 627  ? 2.9290 1.4054 2.0368 -0.1243 -0.0822 -0.4297 627  LEU B N   
17170 C CA  . LEU C 627  ? 2.9437 1.4408 1.9802 -0.1365 -0.0751 -0.4876 627  LEU B CA  
17171 C C   . LEU C 627  ? 2.9296 1.3941 1.9438 -0.1652 -0.0361 -0.4921 627  LEU B C   
17172 O O   . LEU C 627  ? 3.0499 1.5213 1.9998 -0.1715 -0.0233 -0.5313 627  LEU B O   
17173 C CB  . LEU C 627  ? 2.8769 1.4330 1.9166 -0.1568 -0.1171 -0.5535 627  LEU B CB  
17174 C CG  . LEU C 627  ? 2.8704 1.4583 1.8572 -0.1845 -0.1195 -0.6238 627  LEU B CG  
17175 C CD1 . LEU C 627  ? 2.8892 1.5390 1.8739 -0.1840 -0.1658 -0.6757 627  LEU B CD1 
17176 C CD2 . LEU C 627  ? 2.7841 1.3589 1.7962 -0.2309 -0.1041 -0.6384 627  LEU B CD2 
17177 N N   . GLU C 628  ? 3.5799 2.0089 2.6461 -0.1830 -0.0171 -0.4527 628  GLU B N   
17178 C CA  . GLU C 628  ? 3.5729 1.9665 2.6151 -0.2052 0.0232  -0.4506 628  GLU B CA  
17179 C C   . GLU C 628  ? 3.5402 1.8782 2.5982 -0.1849 0.0595  -0.3776 628  GLU B C   
17180 O O   . GLU C 628  ? 3.4780 1.7857 2.5783 -0.2065 0.0792  -0.3488 628  GLU B O   
17181 C CB  . GLU C 628  ? 3.5459 1.9495 2.6251 -0.2539 0.0184  -0.4819 628  GLU B CB  
17182 C CG  . GLU C 628  ? 3.8086 2.1974 2.9732 -0.2669 0.0126  -0.4404 628  GLU B CG  
17183 C CD  . GLU C 628  ? 3.7832 2.1624 2.9749 -0.3121 0.0269  -0.4549 628  GLU B CD  
17184 O OE1 . GLU C 628  ? 3.8419 2.1925 2.9938 -0.3234 0.0629  -0.4573 628  GLU B OE1 
17185 O OE2 . GLU C 628  ? 3.6980 2.0979 2.9506 -0.3354 0.0021  -0.4634 628  GLU B OE2 
17186 N N   . LYS C 629  ? 2.9859 1.3120 2.0108 -0.1427 0.0679  -0.3468 629  LYS B N   
17187 C CA  . LYS C 629  ? 2.9708 1.2442 1.9899 -0.1212 0.1087  -0.2834 629  LYS B CA  
17188 C C   . LYS C 629  ? 3.0352 1.2958 1.9713 -0.1164 0.1385  -0.3078 629  LYS B C   
17189 O O   . LYS C 629  ? 3.0156 1.2345 1.9257 -0.0988 0.1764  -0.2676 629  LYS B O   
17190 C CB  . LYS C 629  ? 2.9781 1.2441 2.0188 -0.0783 0.1006  -0.2288 629  LYS B CB  
17191 C CG  . LYS C 629  ? 2.8753 1.1509 2.0011 -0.0865 0.0711  -0.2055 629  LYS B CG  
17192 C CD  . LYS C 629  ? 3.0949 1.3704 2.2657 -0.1345 0.0704  -0.2258 629  LYS B CD  
17193 C CE  . LYS C 629  ? 2.8076 1.1015 2.0588 -0.1472 0.0353  -0.2173 629  LYS B CE  
17194 N NZ  . LYS C 629  ? 2.7169 1.0158 2.0028 -0.1940 0.0344  -0.2447 629  LYS B NZ  
17195 N N   . SER C 630  ? 2.5908 0.8899 1.4871 -0.1339 0.1195  -0.3764 630  SER B N   
17196 C CA  . SER C 630  ? 2.6806 0.9747 1.5009 -0.1409 0.1418  -0.4153 630  SER B CA  
17197 C C   . SER C 630  ? 2.6773 0.9387 1.5035 -0.1769 0.1731  -0.4167 630  SER B C   
17198 O O   . SER C 630  ? 2.6802 0.9314 1.4477 -0.1876 0.1949  -0.4475 630  SER B O   
17199 C CB  . SER C 630  ? 2.6880 1.0370 1.4746 -0.1542 0.1079  -0.4896 630  SER B CB  
17200 O OG  . SER C 630  ? 2.6476 1.0237 1.4822 -0.1942 0.0834  -0.5235 630  SER B OG  
17201 N N   . ASP C 631  ? 3.5089 1.7552 2.4063 -0.1972 0.1742  -0.3860 631  ASP B N   
17202 C CA  . ASP C 631  ? 3.4925 1.7043 2.3961 -0.2282 0.2071  -0.3804 631  ASP B CA  
17203 C C   . ASP C 631  ? 3.5424 1.7028 2.4176 -0.1987 0.2498  -0.3246 631  ASP B C   
17204 O O   . ASP C 631  ? 3.4891 1.6281 2.4019 -0.1737 0.2560  -0.2634 631  ASP B O   
17205 C CB  . ASP C 631  ? 3.4409 1.6516 2.4288 -0.2581 0.1972  -0.3622 631  ASP B CB  
17206 C CG  . ASP C 631  ? 3.5697 1.7678 2.5601 -0.3022 0.2166  -0.3880 631  ASP B CG  
17207 O OD1 . ASP C 631  ? 3.5876 1.7401 2.5892 -0.3066 0.2533  -0.3463 631  ASP B OD1 
17208 O OD2 . ASP C 631  ? 3.6165 1.8509 2.5984 -0.3323 0.1951  -0.4490 631  ASP B OD2 
17209 N N   . LEU C 632  ? 3.3169 1.4591 2.1229 -0.2004 0.2780  -0.3474 632  LEU B N   
17210 C CA  . LEU C 632  ? 3.3743 1.4693 2.1408 -0.1716 0.3199  -0.3020 632  LEU B CA  
17211 C C   . LEU C 632  ? 3.2796 1.3294 2.0972 -0.1839 0.3508  -0.2465 632  LEU B C   
17212 O O   . LEU C 632  ? 3.2830 1.3010 2.1152 -0.1550 0.3716  -0.1829 632  LEU B O   
17213 C CB  . LEU C 632  ? 3.5096 1.5979 2.1895 -0.1751 0.3404  -0.3475 632  LEU B CB  
17214 C CG  . LEU C 632  ? 3.5845 1.7188 2.2085 -0.1683 0.3114  -0.4098 632  LEU B CG  
17215 C CD1 . LEU C 632  ? 3.6475 1.7782 2.2015 -0.1891 0.3274  -0.4649 632  LEU B CD1 
17216 C CD2 . LEU C 632  ? 3.6550 1.7952 2.2485 -0.1187 0.3066  -0.3843 632  LEU B CD2 
17217 N N   . GLY C 633  ? 3.5011 1.5506 2.3480 -0.2271 0.3524  -0.2702 633  GLY B N   
17218 C CA  . GLY C 633  ? 3.3816 1.3907 2.2740 -0.2432 0.3819  -0.2243 633  GLY B CA  
17219 C C   . GLY C 633  ? 3.2030 1.2148 2.1809 -0.2414 0.3653  -0.1764 633  GLY B C   
17220 O O   . GLY C 633  ? 3.1870 1.2267 2.1878 -0.2217 0.3331  -0.1707 633  GLY B O   
17221 N N   . CYS C 634  ? 3.0070 0.9895 2.0323 -0.2627 0.3868  -0.1425 634  CYS B N   
17222 C CA  . CYS C 634  ? 2.9237 0.9031 2.0307 -0.2614 0.3753  -0.0917 634  CYS B CA  
17223 C C   . CYS C 634  ? 2.8662 0.8241 2.0285 -0.2964 0.3925  -0.0717 634  CYS B C   
17224 O O   . CYS C 634  ? 2.9452 0.8797 2.0799 -0.3165 0.4229  -0.0839 634  CYS B O   
17225 C CB  . CYS C 634  ? 2.9640 0.9148 2.0707 -0.2174 0.3928  -0.0242 634  CYS B CB  
17226 S SG  . CYS C 634  ? 3.3181 1.2660 2.5230 -0.2124 0.3760  0.0393  634  CYS B SG  
17227 N N   . GLY C 635  ? 3.1738 1.1400 2.4142 -0.3032 0.3726  -0.0409 635  GLY B N   
17228 C CA  . GLY C 635  ? 3.0704 1.0170 2.3702 -0.3328 0.3875  -0.0140 635  GLY B CA  
17229 C C   . GLY C 635  ? 3.0106 0.9912 2.3576 -0.3749 0.3584  -0.0568 635  GLY B C   
17230 O O   . GLY C 635  ? 3.0078 1.0321 2.3464 -0.3833 0.3219  -0.1111 635  GLY B O   
17231 N N   . ALA C 636  ? 3.1142 1.0754 2.5131 -0.4004 0.3746  -0.0298 636  ALA B N   
17232 C CA  . ALA C 636  ? 3.0560 1.0421 2.4906 -0.4443 0.3585  -0.0706 636  ALA B CA  
17233 C C   . ALA C 636  ? 3.0970 1.0799 2.4675 -0.4647 0.3786  -0.1215 636  ALA B C   
17234 O O   . ALA C 636  ? 3.0811 1.0887 2.4602 -0.5010 0.3659  -0.1699 636  ALA B O   
17235 C CB  . ALA C 636  ? 3.0166 1.0009 2.5191 -0.4577 0.3746  -0.0234 636  ALA B CB  
17236 N N   . GLY C 637  ? 3.1002 1.0518 2.4059 -0.4403 0.4104  -0.1091 637  GLY B N   
17237 C CA  . GLY C 637  ? 3.1973 1.1406 2.4337 -0.4536 0.4319  -0.1539 637  GLY B CA  
17238 C C   . GLY C 637  ? 3.2982 1.1867 2.5105 -0.4491 0.4837  -0.1139 637  GLY B C   
17239 O O   . GLY C 637  ? 3.2216 1.0810 2.4764 -0.4388 0.5028  -0.0512 637  GLY B O   
17240 N N   . GLY C 638  ? 2.9085 0.7832 2.0516 -0.4556 0.5061  -0.1496 638  GLY B N   
17241 C CA  . GLY C 638  ? 2.9573 0.7833 2.0767 -0.4620 0.5542  -0.1261 638  GLY B CA  
17242 C C   . GLY C 638  ? 2.9611 0.7410 2.0801 -0.4282 0.5897  -0.0531 638  GLY B C   
17243 O O   . GLY C 638  ? 2.9574 0.7357 2.1321 -0.4132 0.5825  -0.0017 638  GLY B O   
17244 N N   . GLY C 639  ? 3.6350 1.3766 2.6919 -0.4175 0.6290  -0.0481 639  GLY B N   
17245 C CA  . GLY C 639  ? 3.6393 1.3388 2.6814 -0.3805 0.6634  0.0163  639  GLY B CA  
17246 C C   . GLY C 639  ? 3.6178 1.2718 2.6872 -0.3869 0.7054  0.0707  639  GLY B C   
17247 O O   . GLY C 639  ? 3.4786 1.1352 2.6191 -0.4093 0.7014  0.0948  639  GLY B O   
17248 N N   . LEU C 640  ? 2.7759 0.3887 1.7861 -0.3659 0.7459  0.0895  640  LEU B N   
17249 C CA  . LEU C 640  ? 2.7731 0.3383 1.7973 -0.3562 0.7900  0.1538  640  LEU B CA  
17250 C C   . LEU C 640  ? 2.8549 0.3836 1.8013 -0.3553 0.8288  0.1335  640  LEU B C   
17251 O O   . LEU C 640  ? 2.8594 0.3497 1.8092 -0.3635 0.8667  0.1630  640  LEU B O   
17252 C CB  . LEU C 640  ? 2.7732 0.3282 1.8128 -0.3116 0.7940  0.2201  640  LEU B CB  
17253 C CG  . LEU C 640  ? 2.6194 0.1410 1.6846 -0.2858 0.8297  0.3009  640  LEU B CG  
17254 C CD1 . LEU C 640  ? 2.6101 0.1678 1.7141 -0.2995 0.8565  0.3067  640  LEU B CD1 
17255 C CD2 . LEU C 640  ? 2.5901 0.1484 1.7147 -0.2589 0.8036  0.3434  640  LEU B CD2 
17256 N N   . ASN C 641  ? 3.2992 0.8416 2.1763 -0.3462 0.8176  0.0812  641  ASN B N   
17257 C CA  . ASN C 641  ? 3.3841 0.9010 2.1833 -0.3515 0.8444  0.0430  641  ASN B CA  
17258 C C   . ASN C 641  ? 3.4285 0.9857 2.1966 -0.3716 0.8096  -0.0350 641  ASN B C   
17259 O O   . ASN C 641  ? 3.4284 1.0254 2.2078 -0.3605 0.7721  -0.0503 641  ASN B O   
17260 C CB  . ASN C 641  ? 3.5222 1.0121 2.2559 -0.3059 0.8687  0.0679  641  ASN B CB  
17261 C CG  . ASN C 641  ? 3.5400 1.0232 2.3127 -0.2702 0.8726  0.1401  641  ASN B CG  
17262 O OD1 . ASN C 641  ? 3.4974 0.9575 2.3207 -0.2733 0.8934  0.1945  641  ASN B OD1 
17263 N ND2 . ASN C 641  ? 3.6025 1.1071 2.3544 -0.2365 0.8518  0.1421  641  ASN B ND2 
17264 N N   . ASN C 642  ? 3.8998 1.4472 2.6281 -0.4004 0.8216  -0.0841 642  ASN B N   
17265 C CA  . ASN C 642  ? 3.9376 1.5244 2.6366 -0.4227 0.7888  -0.1602 642  ASN B CA  
17266 C C   . ASN C 642  ? 3.9837 1.5912 2.6367 -0.3860 0.7693  -0.1720 642  ASN B C   
17267 O O   . ASN C 642  ? 3.9374 1.5908 2.5869 -0.3926 0.7300  -0.2188 642  ASN B O   
17268 C CB  . ASN C 642  ? 4.0782 1.6422 2.7195 -0.4475 0.8115  -0.2065 642  ASN B CB  
17269 C CG  . ASN C 642  ? 4.1851 1.7881 2.7845 -0.4643 0.7796  -0.2837 642  ASN B CG  
17270 O OD1 . ASN C 642  ? 4.3253 1.9128 2.8509 -0.4616 0.7934  -0.3196 642  ASN B OD1 
17271 N ND2 . ASN C 642  ? 4.1247 1.7792 2.7706 -0.4809 0.7362  -0.3094 642  ASN B ND2 
17272 N N   . ALA C 643  ? 3.5924 1.1658 2.2110 -0.3459 0.7980  -0.1265 643  ALA B N   
17273 C CA  . ALA C 643  ? 3.6654 1.2553 2.2522 -0.3050 0.7828  -0.1199 643  ALA B CA  
17274 C C   . ALA C 643  ? 3.5022 1.1291 2.1607 -0.2971 0.7466  -0.0937 643  ALA B C   
17275 O O   . ALA C 643  ? 3.4559 1.1276 2.1137 -0.2982 0.7072  -0.1332 643  ALA B O   
17276 C CB  . ALA C 643  ? 3.8078 1.3516 2.3514 -0.2644 0.8238  -0.0688 643  ALA B CB  
17277 N N   . ASN C 644  ? 3.2927 0.9014 2.0134 -0.2899 0.7593  -0.0283 644  ASN B N   
17278 C CA  . ASN C 644  ? 3.1997 0.8393 1.9892 -0.2812 0.7264  0.0004  644  ASN B CA  
17279 C C   . ASN C 644  ? 3.1559 0.8449 1.9825 -0.3165 0.6818  -0.0542 644  ASN B C   
17280 O O   . ASN C 644  ? 3.1832 0.9106 2.0293 -0.3051 0.6444  -0.0639 644  ASN B O   
17281 C CB  . ASN C 644  ? 3.0874 0.6989 1.9436 -0.2778 0.7477  0.0746  644  ASN B CB  
17282 C CG  . ASN C 644  ? 3.0073 0.6444 1.9299 -0.2615 0.7172  0.1131  644  ASN B CG  
17283 O OD1 . ASN C 644  ? 2.9319 0.5497 1.9089 -0.2537 0.7305  0.1763  644  ASN B OD1 
17284 N ND2 . ASN C 644  ? 3.0283 0.7088 1.9465 -0.2564 0.6760  0.0751  644  ASN B ND2 
17285 N N   . VAL C 645  ? 3.8384 1.5270 2.6737 -0.3586 0.6860  -0.0901 645  VAL B N   
17286 C CA  . VAL C 645  ? 3.7760 1.5114 2.6434 -0.3946 0.6461  -0.1448 645  VAL B CA  
17287 C C   . VAL C 645  ? 3.8554 1.6294 2.6697 -0.3882 0.6153  -0.2062 645  VAL B C   
17288 O O   . VAL C 645  ? 3.8020 1.6214 2.6473 -0.3922 0.5738  -0.2289 645  VAL B O   
17289 C CB  . VAL C 645  ? 3.7795 1.5041 2.6527 -0.4395 0.6612  -0.1751 645  VAL B CB  
17290 C CG1 . VAL C 645  ? 3.7316 1.5070 2.6388 -0.4758 0.6197  -0.2306 645  VAL B CG1 
17291 C CG2 . VAL C 645  ? 3.7011 1.3893 2.6271 -0.4473 0.6918  -0.1160 645  VAL B CG2 
17292 N N   . PHE C 646  ? 3.2053 0.9607 1.9394 -0.3784 0.6361  -0.2330 646  PHE B N   
17293 C CA  . PHE C 646  ? 3.2588 1.0452 1.9318 -0.3676 0.6129  -0.2874 646  PHE B CA  
17294 C C   . PHE C 646  ? 3.3114 1.1145 1.9777 -0.3238 0.5950  -0.2627 646  PHE B C   
17295 O O   . PHE C 646  ? 3.3349 1.1793 1.9794 -0.3175 0.5615  -0.3042 646  PHE B O   
17296 C CB  . PHE C 646  ? 3.3483 1.1007 1.9383 -0.3621 0.6464  -0.3081 646  PHE B CB  
17297 C CG  . PHE C 646  ? 3.3148 1.0775 1.8788 -0.4029 0.6424  -0.3730 646  PHE B CG  
17298 C CD1 . PHE C 646  ? 3.2782 1.0013 1.8326 -0.4268 0.6774  -0.3715 646  PHE B CD1 
17299 C CD2 . PHE C 646  ? 3.2984 1.1117 1.8486 -0.4179 0.6030  -0.4358 646  PHE B CD2 
17300 C CE1 . PHE C 646  ? 3.2813 1.0139 1.8118 -0.4654 0.6734  -0.4322 646  PHE B CE1 
17301 C CE2 . PHE C 646  ? 3.2966 1.1214 1.8232 -0.4565 0.5984  -0.4965 646  PHE B CE2 
17302 C CZ  . PHE C 646  ? 3.2905 1.0744 1.8074 -0.4808 0.6336  -0.4948 646  PHE B CZ  
17303 N N   . HIS C 647  ? 3.6847 1.4547 2.3671 -0.2928 0.6195  -0.1942 647  HIS B N   
17304 C CA  . HIS C 647  ? 3.7349 1.5158 2.4162 -0.2497 0.6066  -0.1611 647  HIS B CA  
17305 C C   . HIS C 647  ? 3.5193 1.3444 2.2698 -0.2591 0.5621  -0.1645 647  HIS B C   
17306 O O   . HIS C 647  ? 3.5051 1.3729 2.2400 -0.2572 0.5267  -0.2089 647  HIS B O   
17307 C CB  . HIS C 647  ? 3.8648 1.6002 2.5592 -0.2193 0.6431  -0.0830 647  HIS B CB  
17308 C CG  . HIS C 647  ? 4.0758 1.8132 2.7426 -0.1701 0.6411  -0.0518 647  HIS B CG  
17309 N ND1 . HIS C 647  ? 4.1226 1.9027 2.7974 -0.1539 0.6015  -0.0672 647  HIS B ND1 
17310 C CD2 . HIS C 647  ? 4.2244 1.9251 2.8568 -0.1321 0.6755  -0.0025 647  HIS B CD2 
17311 C CE1 . HIS C 647  ? 4.2193 1.9900 2.8661 -0.1091 0.6106  -0.0304 647  HIS B CE1 
17312 N NE2 . HIS C 647  ? 4.2881 2.0118 2.9087 -0.0950 0.6549  0.0090  647  HIS B NE2 
17313 N N   . LEU C 648  ? 3.0248 0.8403 1.8515 -0.2706 0.5636  -0.1198 648  LEU B N   
17314 C CA  . LEU C 648  ? 2.9037 0.7563 1.8011 -0.2755 0.5230  -0.1136 648  LEU B CA  
17315 C C   . LEU C 648  ? 2.8584 0.7609 1.7544 -0.3034 0.4831  -0.1851 648  LEU B C   
17316 O O   . LEU C 648  ? 2.8048 0.7447 1.7453 -0.3043 0.4446  -0.1922 648  LEU B O   
17317 C CB  . LEU C 648  ? 2.7579 0.5927 1.7346 -0.2948 0.5319  -0.0671 648  LEU B CB  
17318 C CG  . LEU C 648  ? 2.7088 0.5177 1.7173 -0.2591 0.5464  0.0112  648  LEU B CG  
17319 C CD1 . LEU C 648  ? 2.6414 0.4081 1.6875 -0.2718 0.5830  0.0621  648  LEU B CD1 
17320 C CD2 . LEU C 648  ? 2.6306 0.4727 1.6981 -0.2478 0.5054  0.0273  648  LEU B CD2 
17321 N N   . ALA C 649  ? 2.9379 0.8405 1.7821 -0.3263 0.4927  -0.2382 649  ALA B N   
17322 C CA  . ALA C 649  ? 2.9164 0.8663 1.7474 -0.3518 0.4577  -0.3101 649  ALA B CA  
17323 C C   . ALA C 649  ? 2.9609 0.9409 1.7445 -0.3207 0.4336  -0.3346 649  ALA B C   
17324 O O   . ALA C 649  ? 2.9499 0.9716 1.7126 -0.3354 0.4039  -0.3948 649  ALA B O   
17325 C CB  . ALA C 649  ? 3.0071 0.9439 1.7914 -0.3830 0.4785  -0.3562 649  ALA B CB  
17326 N N   . GLY C 650  ? 3.7830 1.7432 2.5494 -0.2774 0.4466  -0.2875 650  GLY B N   
17327 C CA  . GLY C 650  ? 3.8913 1.8745 2.6026 -0.2449 0.4306  -0.3084 650  GLY B CA  
17328 C C   . GLY C 650  ? 4.0250 2.0001 2.6509 -0.2487 0.4487  -0.3554 650  GLY B C   
17329 O O   . GLY C 650  ? 4.0852 2.0829 2.6563 -0.2279 0.4350  -0.3859 650  GLY B O   
17330 N N   . LEU C 651  ? 3.4709 1.4136 2.0858 -0.2759 0.4791  -0.3619 651  LEU B N   
17331 C CA  . LEU C 651  ? 3.6211 1.5482 2.1559 -0.2804 0.5007  -0.4019 651  LEU B CA  
17332 C C   . LEU C 651  ? 3.7155 1.5891 2.2067 -0.2497 0.5461  -0.3562 651  LEU B C   
17333 O O   . LEU C 651  ? 3.6686 1.5110 2.1980 -0.2335 0.5674  -0.2916 651  LEU B O   
17334 C CB  . LEU C 651  ? 3.5842 1.5073 2.1254 -0.3297 0.5074  -0.4423 651  LEU B CB  
17335 C CG  . LEU C 651  ? 3.5431 1.5189 2.0887 -0.3631 0.4681  -0.5121 651  LEU B CG  
17336 C CD1 . LEU C 651  ? 3.5279 1.4895 2.0603 -0.4062 0.4849  -0.5494 651  LEU B CD1 
17337 C CD2 . LEU C 651  ? 3.6542 1.6629 2.1368 -0.3423 0.4463  -0.5551 651  LEU B CD2 
17338 N N   . THR C 652  ? 3.3188 1.1842 1.7286 -0.2413 0.5596  -0.3917 652  THR B N   
17339 C CA  . THR C 652  ? 3.3742 1.1858 1.7361 -0.2359 0.6065  -0.3748 652  THR B CA  
17340 C C   . THR C 652  ? 3.4203 1.2374 1.7130 -0.2593 0.6073  -0.4462 652  THR B C   
17341 O O   . THR C 652  ? 3.4425 1.3020 1.7064 -0.2616 0.5760  -0.4982 652  THR B O   
17342 C CB  . THR C 652  ? 3.4230 1.2019 1.7594 -0.1851 0.6340  -0.3138 652  THR B CB  
17343 O OG1 . THR C 652  ? 3.4243 1.1479 1.7612 -0.1858 0.6794  -0.2709 652  THR B OG1 
17344 C CG2 . THR C 652  ? 3.5683 1.3545 1.8202 -0.1563 0.6340  -0.3436 652  THR B CG2 
17345 N N   . PHE C 653  ? 3.5109 1.2850 1.7802 -0.2775 0.6431  -0.4472 653  PHE B N   
17346 C CA  . PHE C 653  ? 3.5973 1.3738 1.8316 -0.3166 0.6434  -0.5107 653  PHE B CA  
17347 C C   . PHE C 653  ? 3.7690 1.4990 1.9246 -0.3036 0.6826  -0.5146 653  PHE B C   
17348 O O   . PHE C 653  ? 3.7714 1.4586 1.9172 -0.2743 0.7167  -0.4602 653  PHE B O   
17349 C CB  . PHE C 653  ? 3.5308 1.2922 1.8257 -0.3558 0.6535  -0.4995 653  PHE B CB  
17350 C CG  . PHE C 653  ? 3.5505 1.2603 1.8721 -0.3400 0.6930  -0.4281 653  PHE B CG  
17351 C CD1 . PHE C 653  ? 3.5871 1.2527 1.9019 -0.3617 0.7291  -0.4214 653  PHE B CD1 
17352 C CD2 . PHE C 653  ? 3.5203 1.2258 1.8725 -0.3024 0.6945  -0.3668 653  PHE B CD2 
17353 C CE1 . PHE C 653  ? 3.5633 1.1831 1.9028 -0.3464 0.7656  -0.3548 653  PHE B CE1 
17354 C CE2 . PHE C 653  ? 3.4972 1.1574 1.8745 -0.2878 0.7304  -0.3004 653  PHE B CE2 
17355 C CZ  . PHE C 653  ? 3.5150 1.1331 1.8864 -0.3099 0.7658  -0.2944 653  PHE B CZ  
17356 N N   . LEU C 654  ? 4.1681 1.9049 2.2685 -0.3266 0.6789  -0.5784 654  LEU B N   
17357 C CA  . LEU C 654  ? 4.3803 2.0764 2.3983 -0.3126 0.7122  -0.5895 654  LEU B CA  
17358 C C   . LEU C 654  ? 4.5207 2.1814 2.5295 -0.3512 0.7380  -0.6103 654  LEU B C   
17359 O O   . LEU C 654  ? 4.6119 2.2928 2.6018 -0.3860 0.7219  -0.6717 654  LEU B O   
17360 C CB  . LEU C 654  ? 4.4291 2.1583 2.3790 -0.3027 0.6888  -0.6466 654  LEU B CB  
17361 C CG  . LEU C 654  ? 4.5477 2.2447 2.4230 -0.2589 0.7163  -0.6287 654  LEU B CG  
17362 C CD1 . LEU C 654  ? 4.5084 2.1714 2.4163 -0.2240 0.7432  -0.5479 654  LEU B CD1 
17363 C CD2 . LEU C 654  ? 4.6184 2.3588 2.4476 -0.2344 0.6865  -0.6627 654  LEU B CD2 
17364 N N   . THR C 655  ? 4.4724 2.0807 2.4946 -0.3450 0.7780  -0.5588 655  THR B N   
17365 C CA  . THR C 655  ? 4.5235 2.0947 2.5400 -0.3804 0.8053  -0.5732 655  THR B CA  
17366 C C   . THR C 655  ? 4.6877 2.1941 2.6680 -0.3571 0.8557  -0.5292 655  THR B C   
17367 O O   . THR C 655  ? 4.6153 2.0990 2.6282 -0.3305 0.8754  -0.4631 655  THR B O   
17368 C CB  . THR C 655  ? 4.6967 2.2801 2.7995 -0.4200 0.7956  -0.5634 655  THR B CB  
17369 O OG1 . THR C 655  ? 4.6260 2.2670 2.7522 -0.4496 0.7511  -0.6175 655  THR B OG1 
17370 C CG2 . THR C 655  ? 4.6960 2.2335 2.7928 -0.4507 0.8304  -0.5666 655  THR B CG2 
17371 N N   . ASN C 656  ? 4.3916 1.8683 2.3029 -0.3671 0.8764  -0.5669 656  ASN B N   
17372 C CA  . ASN C 656  ? 4.5809 1.9940 2.4613 -0.3534 0.9252  -0.5311 656  ASN B CA  
17373 C C   . ASN C 656  ? 4.5070 1.8952 2.4372 -0.3914 0.9437  -0.5189 656  ASN B C   
17374 O O   . ASN C 656  ? 4.5233 1.9196 2.4545 -0.4344 0.9346  -0.5686 656  ASN B O   
17375 C CB  . ASN C 656  ? 4.8085 2.1945 2.5906 -0.3410 0.9430  -0.5691 656  ASN B CB  
17376 C CG  . ASN C 656  ? 4.8876 2.2714 2.6218 -0.2868 0.9481  -0.5438 656  ASN B CG  
17377 O OD1 . ASN C 656  ? 5.0306 2.3914 2.6844 -0.2685 0.9642  -0.5658 656  ASN B OD1 
17378 N ND2 . ASN C 656  ? 4.7845 2.1922 2.5689 -0.2607 0.9344  -0.4964 656  ASN B ND2 
17379 N N   . ALA C 657  ? 5.0726 2.4329 3.0467 -0.3738 0.9687  -0.4497 657  ALA B N   
17380 C CA  . ALA C 657  ? 4.9641 2.2964 2.9911 -0.4007 0.9917  -0.4204 657  ALA B CA  
17381 C C   . ALA C 657  ? 4.8684 2.1962 2.9532 -0.3711 1.0000  -0.3437 657  ALA B C   
17382 O O   . ALA C 657  ? 4.8901 2.1717 2.9696 -0.3499 1.0392  -0.2912 657  ALA B O   
17383 C CB  . ALA C 657  ? 4.8407 2.2106 2.9207 -0.4511 0.9615  -0.4619 657  ALA B CB  
17384 N N   . ASN C 658  ? 4.8683 2.2450 3.0067 -0.3683 0.9625  -0.3374 658  ASN B N   
17385 C CA  . ASN C 658  ? 4.7687 2.1462 2.9671 -0.3425 0.9650  -0.2669 658  ASN B CA  
17386 C C   . ASN C 658  ? 4.8016 2.1949 2.9727 -0.2948 0.9536  -0.2472 658  ASN B C   
17387 O O   . ASN C 658  ? 4.8721 2.2872 2.9871 -0.2862 0.9349  -0.2944 658  ASN B O   
17388 C CB  . ASN C 658  ? 4.5893 2.0073 2.8769 -0.3731 0.9326  -0.2656 658  ASN B CB  
17389 C CG  . ASN C 658  ? 4.4587 1.8510 2.7957 -0.4060 0.9549  -0.2452 658  ASN B CG  
17390 O OD1 . ASN C 658  ? 4.3180 1.7395 2.7226 -0.4371 0.9318  -0.2512 658  ASN B OD1 
17391 N ND2 . ASN C 658  ? 4.5056 1.8433 2.8089 -0.3987 1.0002  -0.2204 658  ASN B ND2 
17392 N N   . ALA C 659  ? 4.1057 1.4884 2.3173 -0.2646 0.9651  -0.1770 659  ALA B N   
17393 C CA  . ALA C 659  ? 4.1450 1.5451 2.3460 -0.2190 0.9529  -0.1480 659  ALA B CA  
17394 C C   . ALA C 659  ? 4.0543 1.5144 2.2987 -0.2251 0.9018  -0.1700 659  ALA B C   
17395 O O   . ALA C 659  ? 3.9597 1.4354 2.2782 -0.2247 0.8882  -0.1292 659  ALA B O   
17396 C CB  . ALA C 659  ? 4.1243 1.4938 2.3604 -0.1874 0.9816  -0.0636 659  ALA B CB  
17397 N N   . ASP C 660  ? 4.0631 1.5563 2.2611 -0.2296 0.8740  -0.2333 660  ASP B N   
17398 C CA  . ASP C 660  ? 3.9819 1.5341 2.2149 -0.2355 0.8244  -0.2602 660  ASP B CA  
17399 C C   . ASP C 660  ? 3.9440 1.5138 2.1982 -0.1926 0.8107  -0.2133 660  ASP B C   
17400 O O   . ASP C 660  ? 3.8797 1.4963 2.1437 -0.1873 0.7716  -0.2373 660  ASP B O   
17401 C CB  . ASP C 660  ? 4.0845 1.6711 2.2662 -0.2549 0.7965  -0.3419 660  ASP B CB  
17402 C CG  . ASP C 660  ? 4.2961 1.8589 2.3821 -0.2338 0.8179  -0.3672 660  ASP B CG  
17403 O OD1 . ASP C 660  ? 4.3731 1.9267 2.4262 -0.1892 0.8282  -0.3355 660  ASP B OD1 
17404 O OD2 . ASP C 660  ? 4.3779 1.9330 2.4216 -0.2622 0.8230  -0.4206 660  ASP B OD2 
17405 N N   . ASP C 661  ? 3.8434 1.3754 2.1080 -0.1633 0.8434  -0.1448 661  ASP B N   
17406 C CA  . ASP C 661  ? 3.8305 1.3697 2.1072 -0.1182 0.8390  -0.0928 661  ASP B CA  
17407 C C   . ASP C 661  ? 3.7389 1.3213 2.0930 -0.1222 0.7986  -0.0788 661  ASP B C   
17408 O O   . ASP C 661  ? 3.6633 1.2813 2.0501 -0.1565 0.7655  -0.1225 661  ASP B O   
17409 C CB  . ASP C 661  ? 3.7765 1.2649 2.0553 -0.0909 0.8845  -0.0201 661  ASP B CB  
17410 C CG  . ASP C 661  ? 3.5296 1.0021 1.8891 -0.1137 0.8951  0.0249  661  ASP B CG  
17411 O OD1 . ASP C 661  ? 3.4414 0.8835 1.7997 -0.1412 0.9207  0.0184  661  ASP B OD1 
17412 O OD2 . ASP C 661  ? 3.4299 0.9202 1.8539 -0.1033 0.8778  0.0675  661  ASP B OD2 
17413 N N   . SER C 662  ? 5.1654 2.7448 3.5471 -0.0858 0.8012  -0.0173 662  SER B N   
17414 C CA  . SER C 662  ? 5.0985 2.7151 3.5497 -0.0833 0.7643  0.0016  662  SER B CA  
17415 C C   . SER C 662  ? 5.1642 2.7654 3.6304 -0.0374 0.7783  0.0755  662  SER B C   
17416 O O   . SER C 662  ? 5.1592 2.7848 3.6120 -0.0061 0.7583  0.0802  662  SER B O   
17417 C CB  . SER C 662  ? 5.1444 2.8130 3.5744 -0.0862 0.7202  -0.0596 662  SER B CB  
17418 O OG  . SER C 662  ? 5.2820 2.9501 3.6302 -0.0548 0.7273  -0.0794 662  SER B OG  
17419 N N   . GLN C 663  ? 3.9158 1.4767 2.4115 -0.0350 0.8130  0.1337  663  GLN B N   
17420 C CA  . GLN C 663  ? 4.0312 1.5659 2.5311 0.0078  0.8389  0.2081  663  GLN B CA  
17421 C C   . GLN C 663  ? 4.1908 1.7516 2.6890 0.0493  0.8168  0.2312  663  GLN B C   
17422 O O   . GLN C 663  ? 4.0951 1.6847 2.6542 0.0485  0.7849  0.2461  663  GLN B O   
17423 C CB  . GLN C 663  ? 3.8546 1.3651 2.4299 -0.0049 0.8563  0.2686  663  GLN B CB  
17424 C CG  . GLN C 663  ? 3.7362 1.2252 2.3224 -0.0484 0.8743  0.2463  663  GLN B CG  
17425 C CD  . GLN C 663  ? 3.7922 1.2443 2.2984 -0.0465 0.9128  0.2239  663  GLN B CD  
17426 O OE1 . GLN C 663  ? 3.8859 1.3234 2.3304 -0.0097 0.9310  0.2346  663  GLN B OE1 
17427 N NE2 . GLN C 663  ? 3.7455 1.1826 2.2529 -0.0857 0.9248  0.1933  663  GLN B NE2 
17428 N N   . GLU C 664  ? 5.2689 2.8176 3.6951 0.0865  0.8358  0.2349  664  GLU B N   
17429 C CA  . GLU C 664  ? 5.4711 3.0336 3.8870 0.1338  0.8276  0.2705  664  GLU B CA  
17430 C C   . GLU C 664  ? 5.5482 3.1611 3.9510 0.1393  0.7825  0.2229  664  GLU B C   
17431 O O   . GLU C 664  ? 5.5311 3.1545 3.8622 0.1598  0.7810  0.1887  664  GLU B O   
17432 C CB  . GLU C 664  ? 5.4690 3.0241 3.9629 0.1473  0.8295  0.3475  664  GLU B CB  
17433 C CG  . GLU C 664  ? 5.4418 2.9481 3.9501 0.1484  0.8753  0.4044  664  GLU B CG  
17434 C CD  . GLU C 664  ? 5.5251 3.0167 4.0555 0.1910  0.8924  0.4856  664  GLU B CD  
17435 O OE1 . GLU C 664  ? 5.5972 3.1112 4.1129 0.2252  0.8752  0.4953  664  GLU B OE1 
17436 O OE2 . GLU C 664  ? 5.5225 2.9804 4.0842 0.1906  0.9236  0.5403  664  GLU B OE2 
17437 N N   . ASN C 665  ? 3.8817 1.5256 2.3552 0.1215  0.7461  0.2223  665  ASN B N   
17438 C CA  . ASN C 665  ? 3.9527 1.6421 2.4310 0.1366  0.7046  0.2018  665  ASN B CA  
17439 C C   . ASN C 665  ? 3.9290 1.6531 2.4320 0.0928  0.6681  0.1372  665  ASN B C   
17440 O O   . ASN C 665  ? 3.9826 1.7118 2.4375 0.0701  0.6682  0.0762  665  ASN B O   
17441 C CB  . ASN C 665  ? 3.9015 1.5931 2.4479 0.1606  0.6959  0.2720  665  ASN B CB  
17442 C CG  . ASN C 665  ? 3.8695 1.6051 2.4251 0.1811  0.6545  0.2606  665  ASN B CG  
17443 O OD1 . ASN C 665  ? 3.7484 1.5085 2.3712 0.1657  0.6214  0.2628  665  ASN B OD1 
17444 N ND2 . ASN C 665  ? 3.9813 1.7268 2.4717 0.2166  0.6561  0.2503  665  ASN B ND2 
17445 N N   . ASP C 666  ? 5.7802 3.5277 4.3594 0.0813  0.6371  0.1522  666  ASP B N   
17446 C CA  . ASP C 666  ? 5.7088 3.4847 4.3288 0.0368  0.6056  0.1034  666  ASP B CA  
17447 C C   . ASP C 666  ? 5.5271 3.3242 4.2354 0.0308  0.5740  0.1328  666  ASP B C   
17448 O O   . ASP C 666  ? 5.4911 3.3291 4.2129 0.0347  0.5343  0.1074  666  ASP B O   
17449 C CB  . ASP C 666  ? 5.8680 3.6821 4.4338 0.0252  0.5786  0.0228  666  ASP B CB  
17450 C CG  . ASP C 666  ? 6.0092 3.8629 4.5659 0.0554  0.5445  0.0146  666  ASP B CG  
17451 O OD1 . ASP C 666  ? 6.0830 3.9266 4.6419 0.0957  0.5531  0.0685  666  ASP B OD1 
17452 O OD2 . ASP C 666  ? 6.0355 3.9310 4.5832 0.0391  0.5094  -0.0449 666  ASP B OD2 
17453 N N   . GLU C 667  ? 5.5962 3.3639 4.3627 0.0237  0.5932  0.1891  667  GLU B N   
17454 C CA  . GLU C 667  ? 5.3977 3.1789 4.2531 0.0025  0.5680  0.2091  667  GLU B CA  
17455 C C   . GLU C 667  ? 5.3529 3.1797 4.2406 0.0089  0.5189  0.1915  667  GLU B C   
17456 O O   . GLU C 667  ? 5.3283 3.1901 4.2148 -0.0169 0.4878  0.1298  667  GLU B O   
17457 C CB  . GLU C 667  ? 5.2344 3.0143 4.1130 -0.0478 0.5687  0.1715  667  GLU B CB  
17458 C CG  . GLU C 667  ? 5.2289 2.9934 4.0348 -0.0619 0.5945  0.1257  667  GLU B CG  
17459 C CD  . GLU C 667  ? 5.2171 2.9308 3.9888 -0.0421 0.6456  0.1725  667  GLU B CD  
17460 O OE1 . GLU C 667  ? 5.1957 2.8909 3.9839 -0.0083 0.6601  0.2373  667  GLU B OE1 
17461 O OE2 . GLU C 667  ? 5.2385 2.9306 3.9666 -0.0602 0.6715  0.1447  667  GLU B OE2 
17462 N N   . PRO C 668  ? 5.4372 3.2633 4.3554 0.0431  0.5118  0.2466  668  PRO B N   
17463 C CA  . PRO C 668  ? 5.3794 3.2427 4.3423 0.0507  0.4668  0.2440  668  PRO B CA  
17464 C C   . PRO C 668  ? 5.2355 3.1125 4.2800 0.0135  0.4405  0.2389  668  PRO B C   
17465 O O   . PRO C 668  ? 5.1730 3.0605 4.2767 0.0229  0.4165  0.2718  668  PRO B O   
17466 C CB  . PRO C 668  ? 5.4010 3.2463 4.3807 0.0943  0.4779  0.3182  668  PRO B CB  
17467 C CG  . PRO C 668  ? 5.5158 3.3285 4.4287 0.1182  0.5221  0.3379  668  PRO B CG  
17468 C CD  . PRO C 668  ? 5.5032 3.2941 4.4001 0.0821  0.5480  0.3108  668  PRO B CD  
17469 N N   . CYS C 669  ? 4.7619 2.6388 3.8080 -0.0279 0.4449  0.1977  669  CYS B N   
17470 C CA  . CYS C 669  ? 4.6429 2.5333 3.7611 -0.0664 0.4225  0.1873  669  CYS B CA  
17471 C C   . CYS C 669  ? 4.5859 2.5126 3.7569 -0.0610 0.3751  0.1854  669  CYS B C   
17472 O O   . CYS C 669  ? 4.6379 2.5930 3.7778 -0.0385 0.3509  0.1610  669  CYS B O   
17473 C CB  . CYS C 669  ? 4.6382 2.5433 3.7302 -0.1070 0.4196  0.1174  669  CYS B CB  
17474 S SG  . CYS C 669  ? 5.1432 3.0906 4.3025 -0.1483 0.3730  0.0739  669  CYS B SG  
17475 N N   . LYS C 670  ? 4.2254 2.1508 3.4757 -0.0814 0.3621  0.2111  670  LYS B N   
17476 C CA  . LYS C 670  ? 4.1484 2.1023 3.4549 -0.0753 0.3192  0.2175  670  LYS B CA  
17477 C C   . LYS C 670  ? 3.9839 1.9419 3.3728 -0.1105 0.3023  0.2244  670  LYS B C   
17478 O O   . LYS C 670  ? 3.9269 1.8596 3.3711 -0.1068 0.3129  0.2851  670  LYS B O   
17479 C CB  . LYS C 670  ? 4.2036 2.1413 3.5213 -0.0310 0.3238  0.2832  670  LYS B CB  
17480 C CG  . LYS C 670  ? 4.1573 2.1179 3.5371 -0.0221 0.2821  0.2993  670  LYS B CG  
17481 C CD  . LYS C 670  ? 4.2051 2.2096 3.5518 -0.0100 0.2443  0.2452  670  LYS B CD  
17482 C CE  . LYS C 670  ? 4.1489 2.1763 3.5581 -0.0028 0.2014  0.2576  670  LYS B CE  
17483 N NZ  . LYS C 670  ? 4.1809 2.1878 3.6123 0.0360  0.2067  0.3276  670  LYS B NZ  
17484 N N   . GLU C 671  ? 4.4673 2.4580 3.8632 -0.1444 0.2762  0.1622  671  GLU B N   
17485 C CA  . GLU C 671  ? 4.3124 2.3182 3.7847 -0.1768 0.2500  0.1570  671  GLU B CA  
17486 C C   . GLU C 671  ? 3.9777 1.9565 3.4945 -0.2105 0.2753  0.1802  671  GLU B C   
17487 O O   . GLU C 671  ? 3.9265 1.9006 3.5156 -0.2199 0.2644  0.2156  671  GLU B O   
17488 C CB  . GLU C 671  ? 4.2703 2.2873 3.7993 -0.1558 0.2173  0.1919  671  GLU B CB  
17489 C CG  . GLU C 671  ? 4.2949 2.3507 3.7952 -0.1332 0.1801  0.1547  671  GLU B CG  
17490 C CD  . GLU C 671  ? 4.2340 2.2972 3.7906 -0.1117 0.1493  0.1918  671  GLU B CD  
17491 O OE1 . GLU C 671  ? 4.1469 2.1926 3.7721 -0.1222 0.1488  0.2353  671  GLU B OE1 
17492 O OE2 . GLU C 671  ? 4.2728 2.3595 3.8052 -0.0845 0.1251  0.1775  671  GLU B OE2 
17493 N N   . ILE C 672  ? 3.6108 1.5735 3.0847 -0.2291 0.3075  0.1585  672  ILE B N   
17494 C CA  . ILE C 672  ? 3.4481 1.3857 2.9547 -0.2616 0.3344  0.1750  672  ILE B CA  
17495 C C   . ILE C 672  ? 3.3039 1.2705 2.8174 -0.3055 0.3174  0.1101  672  ILE B C   
17496 O O   . ILE C 672  ? 3.2198 1.1732 2.7666 -0.3364 0.3329  0.1163  672  ILE B O   
17497 C CB  . ILE C 672  ? 3.7502 1.6444 3.2028 -0.2522 0.3875  0.1994  672  ILE B CB  
17498 C CG1 . ILE C 672  ? 3.6697 1.5301 3.1647 -0.2750 0.4192  0.2398  672  ILE B CG1 
17499 C CG2 . ILE C 672  ? 3.8240 1.7280 3.2018 -0.2643 0.3962  0.1351  672  ILE B CG2 
17500 C CD1 . ILE C 672  ? 3.7380 1.5572 3.1770 -0.2675 0.4706  0.2579  672  ILE B CD1 
17501 N N   . LEU C 673  ? 2.9429 0.9499 2.4247 -0.3076 0.2857  0.0487  673  LEU B N   
17502 C CA  . LEU C 673  ? 2.8155 0.8489 2.2796 -0.3450 0.2763  -0.0191 673  LEU B CA  
17503 C C   . LEU C 673  ? 2.6827 0.7403 2.2174 -0.3803 0.2495  -0.0345 673  LEU B C   
17504 O O   . LEU C 673  ? 2.6552 0.7377 2.1813 -0.4126 0.2395  -0.0899 673  LEU B O   
17505 C CB  . LEU C 673  ? 2.7929 0.8629 2.1959 -0.3356 0.2525  -0.0807 673  LEU B CB  
17506 C CG  . LEU C 673  ? 2.6431 0.7649 2.0733 -0.3440 0.2013  -0.1244 673  LEU B CG  
17507 C CD1 . LEU C 673  ? 2.6793 0.8335 2.0421 -0.3478 0.1888  -0.1935 673  LEU B CD1 
17508 C CD2 . LEU C 673  ? 2.5962 0.7255 2.0612 -0.3107 0.1751  -0.0874 673  LEU B CD2 
17509 N N   . LEU C 679  ? 3.6760 4.2712 4.0315 -0.3290 -0.0397 0.7102  679  LEU B N   
17510 C CA  . LEU C 679  ? 3.6591 4.2636 4.0039 -0.3173 -0.1012 0.7323  679  LEU B CA  
17511 C C   . LEU C 679  ? 3.6697 4.2746 4.0366 -0.3087 -0.1169 0.6944  679  LEU B C   
17512 O O   . LEU C 679  ? 3.6644 4.2749 4.0101 -0.2980 -0.1565 0.7182  679  LEU B O   
17513 C CB  . LEU C 679  ? 3.6048 4.2156 3.9781 -0.3219 -0.1533 0.7232  679  LEU B CB  
17514 C CG  . LEU C 679  ? 3.5872 4.1973 3.9258 -0.3306 -0.1482 0.7730  679  LEU B CG  
17515 C CD1 . LEU C 679  ? 3.5550 4.1636 3.9324 -0.3388 -0.1792 0.7431  679  LEU B CD1 
17516 C CD2 . LEU C 679  ? 3.5840 4.2008 3.8615 -0.3246 -0.1766 0.8455  679  LEU B CD2 
17517 N N   . GLN C 680  ? 3.1085 3.7088 3.5162 -0.3155 -0.0856 0.6359  680  GLN B N   
17518 C CA  . GLN C 680  ? 3.1092 3.7077 3.5312 -0.3102 -0.0889 0.6014  680  GLN B CA  
17519 C C   . GLN C 680  ? 3.0628 3.6429 3.4309 -0.3048 -0.0408 0.6296  680  GLN B C   
17520 O O   . GLN C 680  ? 3.0599 3.6337 3.4256 -0.2998 -0.0394 0.6099  680  GLN B O   
17521 C CB  . GLN C 680  ? 3.1528 3.7581 3.6420 -0.3217 -0.0795 0.5255  680  GLN B CB  
17522 C CG  . GLN C 680  ? 3.1700 3.7601 3.6560 -0.3314 -0.0209 0.4969  680  GLN B CG  
17523 C CD  . GLN C 680  ? 3.1807 3.7559 3.6452 -0.3437 0.0377  0.5113  680  GLN B CD  
17524 O OE1 . GLN C 680  ? 3.1919 3.7731 3.6543 -0.3469 0.0356  0.5343  680  GLN B OE1 
17525 N NE2 . GLN C 680  ? 3.1818 3.7348 3.6275 -0.3516 0.0898  0.4981  680  GLN B NE2 
17526 N N   . LYS C 681  ? 3.8287 4.3994 4.1524 -0.3052 -0.0020 0.6754  681  LYS B N   
17527 C CA  . LYS C 681  ? 3.7694 4.3211 4.0349 -0.2957 0.0436  0.7099  681  LYS B CA  
17528 C C   . LYS C 681  ? 3.7653 4.3284 3.9807 -0.2770 0.0147  0.7666  681  LYS B C   
17529 O O   . LYS C 681  ? 3.7614 4.3130 3.9376 -0.2641 0.0358  0.7812  681  LYS B O   
17530 C CB  . LYS C 681  ? 3.7200 4.2596 3.9569 -0.3017 0.0949  0.7395  681  LYS B CB  
17531 C CG  . LYS C 681  ? 3.6853 4.2194 3.9666 -0.3231 0.1222  0.6941  681  LYS B CG  
17532 C CD  . LYS C 681  ? 3.6496 4.1738 3.8958 -0.3284 0.1663  0.7335  681  LYS B CD  
17533 C CE  . LYS C 681  ? 3.6397 4.1718 3.9300 -0.3496 0.1726  0.7027  681  LYS B CE  
17534 N NZ  . LYS C 681  ? 3.6427 4.1700 3.8973 -0.3550 0.2057  0.7483  681  LYS B NZ  
17535 N N   . LYS C 682  ? 3.8745 4.4599 4.0887 -0.2763 -0.0331 0.7987  682  LYS B N   
17536 C CA  . LYS C 682  ? 3.8769 4.4800 4.0454 -0.2629 -0.0666 0.8540  682  LYS B CA  
17537 C C   . LYS C 682  ? 3.9225 4.5266 4.0950 -0.2538 -0.0937 0.8323  682  LYS B C   
17538 O O   . LYS C 682  ? 3.9017 4.5168 4.0289 -0.2407 -0.1040 0.8727  682  LYS B O   
17539 C CB  . LYS C 682  ? 3.8604 4.4827 4.0336 -0.2698 -0.1192 0.8822  682  LYS B CB  
17540 C CG  . LYS C 682  ? 3.8448 4.4863 3.9909 -0.2621 -0.1742 0.9181  682  LYS B CG  
17541 C CD  . LYS C 682  ? 3.8102 4.4662 3.8901 -0.2489 -0.1518 0.9799  682  LYS B CD  
17542 C CE  . LYS C 682  ? 3.8008 4.4782 3.8555 -0.2426 -0.2036 1.0083  682  LYS B CE  
17543 N NZ  . LYS C 682  ? 3.7765 4.4744 3.7681 -0.2277 -0.1804 1.0653  682  LYS B NZ  
17544 N N   . ILE C 683  ? 4.4460 5.0421 4.6731 -0.2614 -0.1049 0.7680  683  ILE B N   
17545 C CA  . ILE C 683  ? 4.5093 5.1060 4.7460 -0.2556 -0.1304 0.7405  683  ILE B CA  
17546 C C   . ILE C 683  ? 4.5536 5.1266 4.7733 -0.2520 -0.0779 0.7172  683  ILE B C   
17547 O O   . ILE C 683  ? 4.5820 5.1532 4.7730 -0.2412 -0.0842 0.7251  683  ILE B O   
17548 C CB  . ILE C 683  ? 4.0442 4.6486 4.3492 -0.2646 -0.1759 0.6834  683  ILE B CB  
17549 C CG1 . ILE C 683  ? 4.0304 4.6466 4.3553 -0.2699 -0.2150 0.6969  683  ILE B CG1 
17550 C CG2 . ILE C 683  ? 4.0698 4.6823 4.3772 -0.2577 -0.2208 0.6727  683  ILE B CG2 
17551 C CD1 . ILE C 683  ? 3.9864 4.6079 4.3817 -0.2766 -0.2476 0.6358  683  ILE B CD1 
17552 N N   . GLU C 684  ? 3.8039 4.3567 4.0375 -0.2620 -0.0268 0.6895  684  GLU B N   
17553 C CA  . GLU C 684  ? 3.8274 4.3497 4.0445 -0.2625 0.0235  0.6627  684  GLU B CA  
17554 C C   . GLU C 684  ? 3.7824 4.2872 3.9254 -0.2440 0.0600  0.7130  684  GLU B C   
17555 O O   . GLU C 684  ? 3.7797 4.2524 3.8982 -0.2416 0.1009  0.6959  684  GLU B O   
17556 C CB  . GLU C 684  ? 3.8938 4.3989 4.1443 -0.2818 0.0664  0.6195  684  GLU B CB  
17557 C CG  . GLU C 684  ? 3.9628 4.4835 4.2876 -0.2987 0.0405  0.5535  684  GLU B CG  
17558 C CD  . GLU C 684  ? 4.0153 4.5180 4.3651 -0.3192 0.0891  0.5047  684  GLU B CD  
17559 O OE1 . GLU C 684  ? 4.0293 4.5023 4.3374 -0.3211 0.1420  0.5234  684  GLU B OE1 
17560 O OE2 . GLU C 684  ? 4.0400 4.5596 4.4503 -0.3336 0.0738  0.4478  684  GLU B OE2 
17561 N N   . GLU C 685  ? 3.1488 3.6751 3.2553 -0.2312 0.0445  0.7747  685  GLU B N   
17562 C CA  . GLU C 685  ? 3.1222 3.6445 3.1596 -0.2095 0.0703  0.8275  685  GLU B CA  
17563 C C   . GLU C 685  ? 3.0812 3.6105 3.0981 -0.1966 0.0433  0.8280  685  GLU B C   
17564 O O   . GLU C 685  ? 3.0904 3.6001 3.0613 -0.1807 0.0744  0.8370  685  GLU B O   
17565 C CB  . GLU C 685  ? 3.1310 3.6845 3.1407 -0.2030 0.0567  0.8931  685  GLU B CB  
17566 C CG  . GLU C 685  ? 3.1419 3.7324 3.1676 -0.2068 -0.0114 0.9109  685  GLU B CG  
17567 C CD  . GLU C 685  ? 3.1500 3.7701 3.1488 -0.2062 -0.0257 0.9737  685  GLU B CD  
17568 O OE1 . GLU C 685  ? 3.1477 3.7633 3.1208 -0.2030 0.0167  1.0026  685  GLU B OE1 
17569 O OE2 . GLU C 685  ? 3.1601 3.8072 3.1618 -0.2104 -0.0809 0.9949  685  GLU B OE2 
17570 N N   . ILE C 686  ? 3.4497 4.0054 3.4998 -0.2034 -0.0161 0.8180  686  ILE B N   
17571 C CA  . ILE C 686  ? 3.4146 3.9825 3.4482 -0.1942 -0.0501 0.8209  686  ILE B CA  
17572 C C   . ILE C 686  ? 3.3800 3.9187 3.4298 -0.1983 -0.0344 0.7626  686  ILE B C   
17573 O O   . ILE C 686  ? 3.4029 3.9500 3.4556 -0.1967 -0.0681 0.7485  686  ILE B O   
17574 C CB  . ILE C 686  ? 3.4191 4.0199 3.4822 -0.2020 -0.1208 0.8279  686  ILE B CB  
17575 C CG1 . ILE C 686  ? 3.4063 4.0281 3.4627 -0.2055 -0.1340 0.8744  686  ILE B CG1 
17576 C CG2 . ILE C 686  ? 3.4344 4.0547 3.4637 -0.1912 -0.1553 0.8520  686  ILE B CG2 
17577 C CD1 . ILE C 686  ? 3.3939 4.0344 3.3843 -0.1899 -0.1158 0.9437  686  ILE B CD1 
17578 N N   . ALA C 687  ? 3.4854 3.9898 3.5442 -0.2061 0.0160  0.7293  687  ALA B N   
17579 C CA  . ALA C 687  ? 3.4234 3.8932 3.4771 -0.2091 0.0435  0.6843  687  ALA B CA  
17580 C C   . ALA C 687  ? 3.3665 3.8248 3.3475 -0.1846 0.0648  0.7246  687  ALA B C   
17581 O O   . ALA C 687  ? 3.3636 3.7911 3.3193 -0.1805 0.0863  0.7010  687  ALA B O   
17582 C CB  . ALA C 687  ? 3.4162 3.8502 3.4826 -0.2234 0.0960  0.6508  687  ALA B CB  
17583 N N   . ALA C 688  ? 3.6542 4.1394 3.6012 -0.1688 0.0585  0.7859  688  ALA B N   
17584 C CA  . ALA C 688  ? 3.6121 4.1043 3.4919 -0.1424 0.0698  0.8345  688  ALA B CA  
17585 C C   . ALA C 688  ? 3.5928 4.0972 3.4622 -0.1370 0.0346  0.8249  688  ALA B C   
17586 O O   . ALA C 688  ? 3.5798 4.0820 3.3931 -0.1153 0.0502  0.8503  688  ALA B O   
17587 C CB  . ALA C 688  ? 3.5939 4.1284 3.4533 -0.1330 0.0550  0.8997  688  ALA B CB  
17588 N N   . LYS C 689  ? 3.9143 4.4327 3.8367 -0.1558 -0.0135 0.7885  689  LYS B N   
17589 C CA  . LYS C 689  ? 3.9425 4.4706 3.8594 -0.1542 -0.0487 0.7743  689  LYS B CA  
17590 C C   . LYS C 689  ? 4.0440 4.5320 3.9728 -0.1634 -0.0281 0.7133  689  LYS B C   
17591 O O   . LYS C 689  ? 4.0782 4.5740 4.0210 -0.1698 -0.0629 0.6878  689  LYS B O   
17592 C CB  . LYS C 689  ? 3.8538 4.4223 3.8127 -0.1666 -0.1192 0.7764  689  LYS B CB  
17593 C CG  . LYS C 689  ? 3.7745 4.3445 3.8025 -0.1869 -0.1388 0.7420  689  LYS B CG  
17594 C CD  . LYS C 689  ? 3.7215 4.3273 3.7780 -0.1941 -0.2091 0.7550  689  LYS B CD  
17595 C CE  . LYS C 689  ? 3.6694 4.3054 3.6784 -0.1833 -0.2259 0.8259  689  LYS B CE  
17596 N NZ  . LYS C 689  ? 3.6515 4.3168 3.6767 -0.1916 -0.2978 0.8402  689  LYS B NZ  
17597 N N   . TYR C 690  ? 3.6925 4.1370 3.6134 -0.1660 0.0273  0.6909  690  TYR B N   
17598 C CA  . TYR C 690  ? 3.8188 4.2206 3.7405 -0.1766 0.0515  0.6365  690  TYR B CA  
17599 C C   . TYR C 690  ? 3.8769 4.2668 3.7415 -0.1592 0.0536  0.6458  690  TYR B C   
17600 O O   . TYR C 690  ? 3.8704 4.2626 3.6761 -0.1335 0.0713  0.6931  690  TYR B O   
17601 C CB  . TYR C 690  ? 3.9090 4.2609 3.8182 -0.1822 0.1133  0.6181  690  TYR B CB  
17602 C CG  . TYR C 690  ? 4.0410 4.3402 3.9166 -0.1850 0.1458  0.5809  690  TYR B CG  
17603 C CD1 . TYR C 690  ? 4.0928 4.3865 4.0079 -0.2089 0.1271  0.5235  690  TYR B CD1 
17604 C CD2 . TYR C 690  ? 4.1039 4.3587 3.9058 -0.1630 0.1935  0.6036  690  TYR B CD2 
17605 C CE1 . TYR C 690  ? 4.1677 4.4117 4.0486 -0.2144 0.1552  0.4900  690  TYR B CE1 
17606 C CE2 . TYR C 690  ? 4.1813 4.3814 3.9468 -0.1659 0.2218  0.5694  690  TYR B CE2 
17607 C CZ  . TYR C 690  ? 4.2135 4.4076 4.0177 -0.1933 0.2025  0.5129  690  TYR B CZ  
17608 O OH  . TYR C 690  ? 4.2820 4.4198 4.0469 -0.1992 0.2298  0.4791  690  TYR B OH  
17609 N N   . LYS C 691  ? 4.4267 4.8066 4.3096 -0.1734 0.0355  0.5996  691  LYS B N   
17610 C CA  . LYS C 691  ? 4.4767 4.8454 4.3106 -0.1610 0.0327  0.6006  691  LYS B CA  
17611 C C   . LYS C 691  ? 4.5264 4.8775 4.3979 -0.1867 0.0204  0.5367  691  LYS B C   
17612 O O   . LYS C 691  ? 4.5624 4.9043 4.4101 -0.1863 0.0097  0.5206  691  LYS B O   
17613 C CB  . LYS C 691  ? 4.4629 4.8854 4.2868 -0.1484 -0.0180 0.6429  691  LYS B CB  
17614 C CG  . LYS C 691  ? 4.4152 4.8838 4.3067 -0.1663 -0.0790 0.6370  691  LYS B CG  
17615 C CD  . LYS C 691  ? 4.3779 4.8963 4.2497 -0.1535 -0.1213 0.6937  691  LYS B CD  
17616 C CE  . LYS C 691  ? 4.3397 4.8942 4.2728 -0.1695 -0.1774 0.6933  691  LYS B CE  
17617 N NZ  . LYS C 691  ? 4.3196 4.9181 4.2285 -0.1604 -0.2152 0.7532  691  LYS B NZ  
17618 N N   . HIS C 692  ? 3.1850 3.5352 3.1165 -0.2099 0.0221  0.5005  692  HIS B N   
17619 C CA  . HIS C 692  ? 3.2058 3.5450 3.1817 -0.2375 0.0145  0.4373  692  HIS B CA  
17620 C C   . HIS C 692  ? 3.1117 3.4684 3.1563 -0.2567 0.0119  0.4135  692  HIS B C   
17621 O O   . HIS C 692  ? 3.0491 3.4364 3.1149 -0.2492 -0.0044 0.4448  692  HIS B O   
17622 C CB  . HIS C 692  ? 3.2815 3.6558 3.2823 -0.2430 -0.0438 0.4228  692  HIS B CB  
17623 C CG  . HIS C 692  ? 3.3842 3.7509 3.4272 -0.2707 -0.0521 0.3585  692  HIS B CG  
17624 N ND1 . HIS C 692  ? 3.4651 3.7813 3.4735 -0.2817 -0.0115 0.3256  692  HIS B ND1 
17625 C CD2 . HIS C 692  ? 3.4163 3.8206 3.5316 -0.2894 -0.0973 0.3215  692  HIS B CD2 
17626 C CE1 . HIS C 692  ? 3.5075 3.8341 3.5660 -0.3086 -0.0307 0.2717  692  HIS B CE1 
17627 N NE2 . HIS C 692  ? 3.4767 3.8587 3.6023 -0.3123 -0.0826 0.2679  692  HIS B NE2 
17628 N N   . SER C 693  ? 3.3701 3.7083 3.4476 -0.2826 0.0284  0.3577  693  SER B N   
17629 C CA  . SER C 693  ? 3.2897 3.6492 3.4360 -0.3026 0.0262  0.3278  693  SER B CA  
17630 C C   . SER C 693  ? 3.1814 3.6001 3.3918 -0.3022 -0.0382 0.3265  693  SER B C   
17631 O O   . SER C 693  ? 3.1420 3.5855 3.3806 -0.2974 -0.0503 0.3469  693  SER B O   
17632 C CB  . SER C 693  ? 3.3310 3.6689 3.5016 -0.3328 0.0486  0.2651  693  SER B CB  
17633 O OG  . SER C 693  ? 3.3075 3.6774 3.5515 -0.3524 0.0409  0.2322  693  SER B OG  
17634 N N   . VAL C 694  ? 4.5016 4.9397 4.7310 -0.3072 -0.0802 0.3032  694  VAL B N   
17635 C CA  . VAL C 694  ? 4.4306 4.9199 4.7238 -0.3090 -0.1442 0.2923  694  VAL B CA  
17636 C C   . VAL C 694  ? 4.3496 4.8639 4.6357 -0.2887 -0.1770 0.3474  694  VAL B C   
17637 O O   . VAL C 694  ? 4.3345 4.8836 4.6748 -0.2901 -0.2215 0.3413  694  VAL B O   
17638 C CB  . VAL C 694  ? 4.3855 4.8879 4.6859 -0.3144 -0.1848 0.2680  694  VAL B CB  
17639 C CG1 . VAL C 694  ? 4.3763 4.9282 4.7477 -0.3171 -0.2501 0.2502  694  VAL B CG1 
17640 C CG2 . VAL C 694  ? 4.4234 4.8992 4.7236 -0.3368 -0.1519 0.2158  694  VAL B CG2 
17641 N N   . VAL C 695  ? 2.6817 3.1786 2.8999 -0.2700 -0.1560 0.4009  695  VAL B N   
17642 C CA  . VAL C 695  ? 2.6155 3.1373 2.8218 -0.2539 -0.1838 0.4561  695  VAL B CA  
17643 C C   . VAL C 695  ? 2.5570 3.0803 2.7909 -0.2576 -0.1623 0.4603  695  VAL B C   
17644 O O   . VAL C 695  ? 2.5274 3.0785 2.7907 -0.2553 -0.1998 0.4778  695  VAL B O   
17645 C CB  . VAL C 695  ? 2.6211 3.1327 2.7477 -0.2325 -0.1665 0.5136  695  VAL B CB  
17646 C CG1 . VAL C 695  ? 2.5841 3.1240 2.6996 -0.2202 -0.1904 0.5710  695  VAL B CG1 
17647 C CG2 . VAL C 695  ? 2.6511 3.1675 2.7510 -0.2289 -0.1946 0.5118  695  VAL B CG2 
17648 N N   . LYS C 696  ? 3.9078 4.3984 4.1302 -0.2645 -0.1029 0.4435  696  LYS B N   
17649 C CA  . LYS C 696  ? 3.8692 4.3602 4.1217 -0.2724 -0.0788 0.4389  696  LYS B CA  
17650 C C   . LYS C 696  ? 3.8629 4.3872 4.1969 -0.2871 -0.1188 0.3948  696  LYS B C   
17651 O O   . LYS C 696  ? 3.8427 4.3855 4.2062 -0.2868 -0.1316 0.4053  696  LYS B O   
17652 C CB  . LYS C 696  ? 3.8820 4.3300 4.1117 -0.2825 -0.0112 0.4184  696  LYS B CB  
17653 C CG  . LYS C 696  ? 3.8773 4.3287 4.1557 -0.3009 0.0116  0.3891  696  LYS B CG  
17654 C CD  . LYS C 696  ? 3.7902 4.2471 4.0562 -0.2913 0.0240  0.4352  696  LYS B CD  
17655 C CE  . LYS C 696  ? 3.7686 4.2251 4.0776 -0.3116 0.0531  0.4030  696  LYS B CE  
17656 N NZ  . LYS C 696  ? 3.7199 4.1794 4.0152 -0.3048 0.0685  0.4462  696  LYS B NZ  
17657 N N   . LYS C 697  ? 2.1779 2.7106 2.5471 -0.2990 -0.1393 0.3455  697  LYS B N   
17658 C CA  . LYS C 697  ? 2.1672 2.7368 2.6150 -0.3091 -0.1828 0.3019  697  LYS B CA  
17659 C C   . LYS C 697  ? 2.1496 2.7485 2.6105 -0.2950 -0.2517 0.3277  697  LYS B C   
17660 O O   . LYS C 697  ? 2.1591 2.7854 2.6771 -0.2962 -0.2894 0.3080  697  LYS B O   
17661 C CB  . LYS C 697  ? 2.1981 2.7717 2.6800 -0.3272 -0.1827 0.2408  697  LYS B CB  
17662 C CG  . LYS C 697  ? 2.2232 2.8406 2.7895 -0.3352 -0.2272 0.1927  697  LYS B CG  
17663 C CD  . LYS C 697  ? 2.2327 2.8603 2.8460 -0.3501 -0.1946 0.1576  697  LYS B CD  
17664 C CE  . LYS C 697  ? 2.2598 2.9351 2.9582 -0.3563 -0.2353 0.1045  697  LYS B CE  
17665 N NZ  . LYS C 697  ? 2.2661 2.9563 3.0104 -0.3738 -0.1989 0.0640  697  LYS B NZ  
17666 N N   . CYS C 698  ? 3.0072 3.5997 3.4134 -0.2819 -0.2683 0.3709  698  CYS B N   
17667 C CA  . CYS C 698  ? 2.9952 3.6114 3.4012 -0.2707 -0.3324 0.4038  698  CYS B CA  
17668 C C   . CYS C 698  ? 2.9510 3.5736 3.3541 -0.2636 -0.3391 0.4438  698  CYS B C   
17669 O O   . CYS C 698  ? 2.9305 3.5723 3.3570 -0.2598 -0.3940 0.4549  698  CYS B O   
17670 C CB  . CYS C 698  ? 2.9956 3.6052 3.3365 -0.2603 -0.3410 0.4441  698  CYS B CB  
17671 S SG  . CYS C 698  ? 3.4456 4.0633 3.7987 -0.2669 -0.3785 0.4066  698  CYS B SG  
17672 N N   . CYS C 699  ? 2.5688 3.1722 2.9400 -0.2625 -0.2831 0.4656  699  CYS B N   
17673 C CA  . CYS C 699  ? 2.5927 3.2001 2.9542 -0.2576 -0.2805 0.5060  699  CYS B CA  
17674 C C   . CYS C 699  ? 2.6319 3.2433 3.0516 -0.2686 -0.2675 0.4670  699  CYS B C   
17675 O O   . CYS C 699  ? 2.6299 3.2566 3.0779 -0.2674 -0.3030 0.4733  699  CYS B O   
17676 C CB  . CYS C 699  ? 2.5947 3.1819 2.8891 -0.2491 -0.2264 0.5531  699  CYS B CB  
17677 S SG  . CYS C 699  ? 2.5700 3.1734 2.8151 -0.2362 -0.2485 0.6334  699  CYS B SG  
17678 N N   . TYR C 700  ? 2.3541 2.9507 2.7885 -0.2802 -0.2165 0.4266  700  TYR B N   
17679 C CA  . TYR C 700  ? 2.4440 3.0461 2.9291 -0.2931 -0.1943 0.3890  700  TYR B CA  
17680 C C   . TYR C 700  ? 2.5052 3.1388 3.0582 -0.2936 -0.2513 0.3559  700  TYR B C   
17681 O O   . TYR C 700  ? 2.5106 3.1534 3.0689 -0.2862 -0.2826 0.3819  700  TYR B O   
17682 C CB  . TYR C 700  ? 2.5311 3.1164 3.0261 -0.3098 -0.1409 0.3420  700  TYR B CB  
17683 C CG  . TYR C 700  ? 2.6154 3.1885 3.1148 -0.3217 -0.0873 0.3355  700  TYR B CG  
17684 C CD1 . TYR C 700  ? 2.6709 3.2625 3.2332 -0.3392 -0.0787 0.2805  700  TYR B CD1 
17685 C CD2 . TYR C 700  ? 2.6402 3.1864 3.0806 -0.3153 -0.0458 0.3852  700  TYR B CD2 
17686 C CE1 . TYR C 700  ? 2.6970 3.2790 3.2617 -0.3521 -0.0302 0.2754  700  TYR B CE1 
17687 C CE2 . TYR C 700  ? 2.6692 3.2033 3.1117 -0.3272 0.0019  0.3810  700  TYR B CE2 
17688 C CZ  . TYR C 700  ? 2.6963 3.2473 3.2001 -0.3466 0.0096  0.3261  700  TYR B CZ  
17689 O OH  . TYR C 700  ? 2.7053 3.2455 3.2095 -0.3605 0.0568  0.3223  700  TYR B OH  
17690 N N   . ASP C 701  ? 2.6800 3.3296 3.2828 -0.3015 -0.2668 0.2994  701  ASP B N   
17691 C CA  . ASP C 701  ? 2.6943 3.3744 3.3594 -0.2972 -0.3255 0.2685  701  ASP B CA  
17692 C C   . ASP C 701  ? 2.6405 3.3205 3.2775 -0.2812 -0.3837 0.3171  701  ASP B C   
17693 O O   . ASP C 701  ? 2.6133 3.3090 3.2868 -0.2739 -0.4363 0.3087  701  ASP B O   
17694 C CB  . ASP C 701  ? 2.7336 3.4334 3.4445 -0.3051 -0.3412 0.2106  701  ASP B CB  
17695 C CG  . ASP C 701  ? 2.7722 3.4614 3.4426 -0.3014 -0.3591 0.2276  701  ASP B CG  
17696 O OD1 . ASP C 701  ? 2.7707 3.4464 3.3885 -0.2893 -0.3780 0.2827  701  ASP B OD1 
17697 O OD2 . ASP C 701  ? 2.7983 3.4949 3.4890 -0.3119 -0.3548 0.1857  701  ASP B OD2 
17698 N N   . GLY C 702  ? 3.0521 3.7138 3.6215 -0.2759 -0.3735 0.3679  702  GLY B N   
17699 C CA  . GLY C 702  ? 2.9811 3.6441 3.5139 -0.2644 -0.4242 0.4185  702  GLY B CA  
17700 C C   . GLY C 702  ? 2.8913 3.5603 3.4403 -0.2596 -0.4620 0.4371  702  GLY B C   
17701 O O   . GLY C 702  ? 2.8492 3.5286 3.4256 -0.2544 -0.5236 0.4277  702  GLY B O   
17702 N N   . ALA C 703  ? 1.8901 2.5501 2.4208 -0.2616 -0.4260 0.4628  703  ALA B N   
17703 C CA  . ALA C 703  ? 1.9423 2.6044 2.4858 -0.2591 -0.4576 0.4788  703  ALA B CA  
17704 C C   . ALA C 703  ? 1.8763 2.5516 2.4960 -0.2603 -0.4762 0.4162  703  ALA B C   
17705 O O   . ALA C 703  ? 1.8530 2.5310 2.4942 -0.2536 -0.5299 0.4151  703  ALA B O   
17706 C CB  . ALA C 703  ? 1.9568 2.6078 2.4633 -0.2628 -0.4097 0.5180  703  ALA B CB  
17707 N N   . CYS C 704  ? 1.9328 2.6164 2.5904 -0.2688 -0.4324 0.3644  704  CYS B N   
17708 C CA  . CYS C 704  ? 1.9378 2.6396 2.6650 -0.2729 -0.4269 0.3055  704  CYS B CA  
17709 C C   . CYS C 704  ? 1.8974 2.6012 2.6457 -0.2647 -0.4664 0.3107  704  CYS B C   
17710 O O   . CYS C 704  ? 1.8909 2.5802 2.6059 -0.2668 -0.4490 0.3499  704  CYS B O   
17711 C CB  . CYS C 704  ? 1.9272 2.6530 2.7113 -0.2748 -0.4418 0.2425  704  CYS B CB  
17712 S SG  . CYS C 704  ? 1.9351 2.6867 2.7861 -0.2901 -0.3911 0.1710  704  CYS B SG  
17713 N N   . VAL C 705  ? 2.5783 3.2984 3.3796 -0.2549 -0.5195 0.2716  705  VAL B N   
17714 C CA  . VAL C 705  ? 2.5578 3.2745 3.3780 -0.2452 -0.5583 0.2720  705  VAL B CA  
17715 C C   . VAL C 705  ? 2.5788 3.2990 3.4261 -0.2289 -0.6364 0.2564  705  VAL B C   
17716 O O   . VAL C 705  ? 2.6010 3.3412 3.5112 -0.2196 -0.6590 0.2026  705  VAL B O   
17717 C CB  . VAL C 705  ? 2.5158 3.2513 3.3901 -0.2499 -0.5229 0.2223  705  VAL B CB  
17718 C CG1 . VAL C 705  ? 2.5248 3.2435 3.3600 -0.2614 -0.4720 0.2586  705  VAL B CG1 
17719 C CG2 . VAL C 705  ? 2.5142 3.2801 3.4376 -0.2593 -0.4864 0.1629  705  VAL B CG2 
17720 N N   . ASN C 706  ? 2.9955 3.6975 3.7943 -0.2251 -0.6783 0.3035  706  ASN B N   
17721 C CA  . ASN C 706  ? 3.0125 3.7135 3.8307 -0.2110 -0.7543 0.2921  706  ASN B CA  
17722 C C   . ASN C 706  ? 2.9774 3.6474 3.7516 -0.2052 -0.8099 0.3427  706  ASN B C   
17723 O O   . ASN C 706  ? 2.9864 3.6401 3.6969 -0.2116 -0.8209 0.4015  706  ASN B O   
17724 C CB  . ASN C 706  ? 3.0748 3.7860 3.8862 -0.2127 -0.7675 0.2892  706  ASN B CB  
17725 C CG  . ASN C 706  ? 3.1095 3.8440 3.9872 -0.2013 -0.8101 0.2301  706  ASN B CG  
17726 O OD1 . ASN C 706  ? 3.1064 3.8475 4.0319 -0.1884 -0.8390 0.1954  706  ASN B OD1 
17727 N ND2 . ASN C 706  ? 3.1465 3.8947 4.0269 -0.2051 -0.8145 0.2177  706  ASN B ND2 
17728 N N   . ASN C 707  ? 2.5274 3.1903 3.3357 -0.1932 -0.8454 0.3176  707  ASN B N   
17729 C CA  . ASN C 707  ? 2.5068 3.1344 3.2763 -0.1883 -0.9009 0.3584  707  ASN B CA  
17730 C C   . ASN C 707  ? 2.4671 3.0818 3.2529 -0.1719 -0.9841 0.3443  707  ASN B C   
17731 O O   . ASN C 707  ? 2.4345 3.0143 3.1865 -0.1682 -1.0366 0.3758  707  ASN B O   
17732 C CB  . ASN C 707  ? 2.5259 3.1423 3.3047 -0.1875 -0.8825 0.3515  707  ASN B CB  
17733 C CG  . ASN C 707  ? 2.5240 3.1723 3.3783 -0.1813 -0.8440 0.2801  707  ASN B CG  
17734 O OD1 . ASN C 707  ? 2.5194 3.2003 3.4120 -0.1835 -0.8134 0.2421  707  ASN B OD1 
17735 N ND2 . ASN C 707  ? 2.5230 3.1630 3.3963 -0.1753 -0.8447 0.2621  707  ASN B ND2 
17736 N N   . ASP C 708  ? 2.0308 2.6719 2.8657 -0.1632 -0.9971 0.2979  708  ASP B N   
17737 C CA  . ASP C 708  ? 2.1047 2.7367 2.9605 -0.1458 -1.0759 0.2799  708  ASP B CA  
17738 C C   . ASP C 708  ? 2.1146 2.7348 2.9205 -0.1533 -1.1150 0.3238  708  ASP B C   
17739 O O   . ASP C 708  ? 2.1091 2.7151 2.9190 -0.1418 -1.1845 0.3202  708  ASP B O   
17740 C CB  . ASP C 708  ? 2.0345 2.7061 2.9757 -0.1307 -1.0759 0.2030  708  ASP B CB  
17741 C CG  . ASP C 708  ? 2.0455 2.7204 3.0401 -0.1117 -1.0852 0.1559  708  ASP B CG  
17742 O OD1 . ASP C 708  ? 1.9886 2.6284 2.9526 -0.1093 -1.0987 0.1820  708  ASP B OD1 
17743 O OD2 . ASP C 708  ? 2.0036 2.7185 3.0708 -0.0994 -1.0794 0.0918  708  ASP B OD2 
17744 N N   . GLU C 709  ? 2.2843 2.9108 3.0426 -0.1717 -1.0706 0.3645  709  GLU B N   
17745 C CA  . GLU C 709  ? 2.3278 2.9493 3.0376 -0.1799 -1.1006 0.4054  709  GLU B CA  
17746 C C   . GLU C 709  ? 2.3465 2.9678 2.9910 -0.1980 -1.0496 0.4625  709  GLU B C   
17747 O O   . GLU C 709  ? 2.3808 3.0170 3.0333 -0.2037 -0.9797 0.4527  709  GLU B O   
17748 C CB  . GLU C 709  ? 2.3632 3.0147 3.1166 -0.1760 -1.1035 0.3605  709  GLU B CB  
17749 C CG  . GLU C 709  ? 2.3691 3.0555 3.1794 -0.1771 -1.0361 0.3044  709  GLU B CG  
17750 C CD  . GLU C 709  ? 2.3819 3.0987 3.2356 -0.1754 -1.0433 0.2585  709  GLU B CD  
17751 O OE1 . GLU C 709  ? 2.3890 3.1004 3.2226 -0.1746 -1.0941 0.2751  709  GLU B OE1 
17752 O OE2 . GLU C 709  ? 2.3760 3.1232 3.2824 -0.1768 -0.9983 0.2065  709  GLU B OE2 
17753 N N   . THR C 710  ? 2.6656 3.2710 3.2446 -0.2068 -1.0852 0.5223  710  THR B N   
17754 C CA  . THR C 710  ? 2.6890 3.2960 3.2013 -0.2217 -1.0445 0.5831  710  THR B CA  
17755 C C   . THR C 710  ? 2.7422 3.3757 3.2569 -0.2259 -0.9731 0.5714  710  THR B C   
17756 O O   . THR C 710  ? 2.7424 3.3924 3.3106 -0.2204 -0.9523 0.5154  710  THR B O   
17757 C CB  . THR C 710  ? 2.9676 3.5637 3.4125 -0.2316 -1.0968 0.6445  710  THR B CB  
17758 O OG1 . THR C 710  ? 2.9824 3.6000 3.4156 -0.2347 -1.0895 0.6455  710  THR B OG1 
17759 C CG2 . THR C 710  ? 2.9746 3.5415 3.4258 -0.2259 -1.1818 0.6408  710  THR B CG2 
17760 N N   . CYS C 711  ? 2.8315 3.4691 3.2864 -0.2356 -0.9353 0.6245  711  CYS B N   
17761 C CA  . CYS C 711  ? 2.8912 3.5469 3.3404 -0.2378 -0.8678 0.6164  711  CYS B CA  
17762 C C   . CYS C 711  ? 2.9229 3.5902 3.3497 -0.2394 -0.8840 0.6231  711  CYS B C   
17763 O O   . CYS C 711  ? 2.9634 3.6419 3.4010 -0.2392 -0.8393 0.5964  711  CYS B O   
17764 C CB  . CYS C 711  ? 2.9174 3.5737 3.3181 -0.2435 -0.8107 0.6634  711  CYS B CB  
17765 S SG  . CYS C 711  ? 2.8967 3.5535 3.3407 -0.2425 -0.7326 0.6208  711  CYS B SG  
17766 N N   . GLU C 712  ? 2.5477 3.2107 2.9414 -0.2426 -0.9480 0.6577  712  GLU B N   
17767 C CA  . GLU C 712  ? 2.5732 3.2485 2.9489 -0.2449 -0.9682 0.6600  712  GLU B CA  
17768 C C   . GLU C 712  ? 2.5152 3.1890 2.9418 -0.2399 -1.0255 0.6123  712  GLU B C   
17769 O O   . GLU C 712  ? 2.5159 3.1996 2.9330 -0.2426 -1.0475 0.6093  712  GLU B O   
17770 C CB  . GLU C 712  ? 2.6686 3.3480 2.9689 -0.2541 -0.9941 0.7304  712  GLU B CB  
17771 C CG  . GLU C 712  ? 2.7302 3.3936 3.0032 -0.2599 -1.0354 0.7732  712  GLU B CG  
17772 C CD  . GLU C 712  ? 2.8061 3.4812 3.0024 -0.2721 -1.0530 0.8442  712  GLU B CD  
17773 O OE1 . GLU C 712  ? 2.8348 3.5271 2.9923 -0.2737 -0.9992 0.8790  712  GLU B OE1 
17774 O OE2 . GLU C 712  ? 2.8335 3.5022 3.0076 -0.2799 -1.1206 0.8651  712  GLU B OE2 
17775 N N   . GLN C 713  ? 2.9473 3.6100 3.4275 -0.2316 -1.0495 0.5752  713  GLN B N   
17776 C CA  . GLN C 713  ? 2.9144 3.5820 3.4574 -0.2225 -1.0894 0.5174  713  GLN B CA  
17777 C C   . GLN C 713  ? 2.8750 3.5654 3.4667 -0.2213 -1.0309 0.4610  713  GLN B C   
17778 O O   . GLN C 713  ? 2.9010 3.6062 3.5166 -0.2214 -1.0442 0.4292  713  GLN B O   
17779 C CB  . GLN C 713  ? 2.8965 3.5466 3.4803 -0.2110 -1.1305 0.4946  713  GLN B CB  
17780 C CG  . GLN C 713  ? 2.9000 3.5202 3.4384 -0.2130 -1.1986 0.5434  713  GLN B CG  
17781 C CD  . GLN C 713  ? 2.8848 3.4818 3.4611 -0.1995 -1.2356 0.5176  713  GLN B CD  
17782 O OE1 . GLN C 713  ? 2.8656 3.4651 3.4732 -0.1942 -1.1938 0.4931  713  GLN B OE1 
17783 N NE2 . GLN C 713  ? 2.8965 3.4693 3.4680 -0.1935 -1.3149 0.5228  713  GLN B NE2 
17784 N N   . ARG C 714  ? 3.1666 3.8588 3.7703 -0.2221 -0.9669 0.4499  714  ARG B N   
17785 C CA  . ARG C 714  ? 3.1401 3.8499 3.7801 -0.2252 -0.9044 0.4022  714  ARG B CA  
17786 C C   . ARG C 714  ? 3.1179 3.8317 3.7111 -0.2341 -0.8702 0.4221  714  ARG B C   
17787 O O   . ARG C 714  ? 3.1166 3.8424 3.7345 -0.2385 -0.8382 0.3812  714  ARG B O   
17788 C CB  . ARG C 714  ? 3.1431 3.8492 3.7929 -0.2267 -0.8437 0.3969  714  ARG B CB  
17789 C CG  . ARG C 714  ? 3.1429 3.8457 3.8391 -0.2178 -0.8683 0.3728  714  ARG B CG  
17790 C CD  . ARG C 714  ? 3.1659 3.8557 3.8379 -0.2213 -0.8253 0.4017  714  ARG B CD  
17791 N NE  . ARG C 714  ? 3.2190 3.9190 3.9071 -0.2288 -0.7485 0.3755  714  ARG B NE  
17792 C CZ  . ARG C 714  ? 3.2519 3.9446 3.9300 -0.2329 -0.7023 0.3885  714  ARG B CZ  
17793 N NH1 . ARG C 714  ? 3.2381 3.9147 3.8911 -0.2305 -0.7242 0.4267  714  ARG B NH1 
17794 N NH2 . ARG C 714  ? 3.2801 3.9797 3.9711 -0.2412 -0.6349 0.3634  714  ARG B NH2 
17795 N N   . ALA C 715  ? 2.3933 3.0977 2.9170 -0.2371 -0.8772 0.4853  715  ALA B N   
17796 C CA  . ALA C 715  ? 2.3932 3.1011 2.8625 -0.2426 -0.8449 0.5125  715  ALA B CA  
17797 C C   . ALA C 715  ? 2.3909 3.1079 2.8562 -0.2452 -0.8918 0.5046  715  ALA B C   
17798 O O   . ALA C 715  ? 2.4415 3.1626 2.8665 -0.2494 -0.8694 0.5182  715  ALA B O   
17799 C CB  . ALA C 715  ? 2.3417 3.0440 2.7401 -0.2438 -0.8345 0.5834  715  ALA B CB  
17800 N N   . ALA C 716  ? 2.6687 3.3875 3.1740 -0.2418 -0.9579 0.4828  716  ALA B N   
17801 C CA  . ALA C 716  ? 2.7163 3.4445 3.2272 -0.2444 -1.0068 0.4689  716  ALA B CA  
17802 C C   . ALA C 716  ? 2.7410 3.4843 3.3047 -0.2463 -0.9794 0.4040  716  ALA B C   
17803 O O   . ALA C 716  ? 2.7778 3.5275 3.3198 -0.2537 -0.9624 0.3989  716  ALA B O   
17804 C CB  . ALA C 716  ? 2.7028 3.4242 3.2356 -0.2387 -1.0889 0.4703  716  ALA B CB  
17805 N N   . ARG C 717  ? 2.0390 2.7891 2.6701 -0.2406 -0.9742 0.3548  717  ARG B N   
17806 C CA  . ARG C 717  ? 2.0806 2.8508 2.7707 -0.2440 -0.9498 0.2892  717  ARG B CA  
17807 C C   . ARG C 717  ? 2.1063 2.8738 2.7694 -0.2556 -0.8744 0.2828  717  ARG B C   
17808 O O   . ARG C 717  ? 2.1196 2.9012 2.8194 -0.2635 -0.8495 0.2325  717  ARG B O   
17809 C CB  . ARG C 717  ? 2.0902 2.8700 2.8478 -0.2358 -0.9446 0.2472  717  ARG B CB  
17810 C CG  . ARG C 717  ? 2.0400 2.8504 2.8730 -0.2359 -0.9508 0.1773  717  ARG B CG  
17811 C CD  . ARG C 717  ? 2.0226 2.8448 2.9183 -0.2232 -0.9615 0.1437  717  ARG B CD  
17812 N NE  . ARG C 717  ? 1.9838 2.7817 2.8571 -0.2102 -1.0058 0.1844  717  ARG B NE  
17813 C CZ  . ARG C 717  ? 2.0289 2.8061 2.8723 -0.2099 -0.9762 0.2174  717  ARG B CZ  
17814 N NH1 . ARG C 717  ? 2.0155 2.7933 2.8493 -0.2202 -0.9020 0.2147  717  ARG B NH1 
17815 N NH2 . ARG C 717  ? 2.0106 2.7645 2.8314 -0.2004 -1.0217 0.2539  717  ARG B NH2 
17816 N N   . ILE C 718  ? 2.6838 3.4327 3.2809 -0.2566 -0.8390 0.3344  718  ILE B N   
17817 C CA  . ILE C 718  ? 2.7558 3.4941 3.3167 -0.2641 -0.7668 0.3353  718  ILE B CA  
17818 C C   . ILE C 718  ? 2.8701 3.6091 3.3970 -0.2712 -0.7690 0.3345  718  ILE B C   
17819 O O   . ILE C 718  ? 2.8556 3.5939 3.3347 -0.2693 -0.8021 0.3764  718  ILE B O   
17820 C CB  . ILE C 718  ? 2.7125 3.4328 3.2160 -0.2595 -0.7255 0.3902  718  ILE B CB  
17821 C CG1 . ILE C 718  ? 2.7003 3.4166 3.2396 -0.2584 -0.6883 0.3723  718  ILE B CG1 
17822 C CG2 . ILE C 718  ? 2.7478 3.4544 3.1916 -0.2626 -0.6701 0.4080  718  ILE B CG2 
17823 C CD1 . ILE C 718  ? 2.7170 3.4158 3.2036 -0.2562 -0.6325 0.4158  718  ILE B CD1 
17824 N N   . SER C 719  ? 1.8344 2.5753 2.3857 -0.2813 -0.7328 0.2852  719  SER B N   
17825 C CA  . SER C 719  ? 1.8644 2.6038 2.3900 -0.2908 -0.7277 0.2721  719  SER B CA  
17826 C C   . SER C 719  ? 1.8822 2.5943 2.3427 -0.2931 -0.6595 0.2918  719  SER B C   
17827 O O   . SER C 719  ? 1.8944 2.5975 2.2905 -0.2868 -0.6592 0.3393  719  SER B O   
17828 C CB  . SER C 719  ? 1.8704 2.6276 2.4610 -0.3027 -0.7287 0.2040  719  SER B CB  
17829 O OG  . SER C 719  ? 1.9025 2.6561 2.4675 -0.3146 -0.7214 0.1885  719  SER B OG  
17830 N N   . LEU C 720  ? 3.1133 3.8131 3.5908 -0.3020 -0.6025 0.2543  720  LEU B N   
17831 C CA  . LEU C 720  ? 3.2068 3.8738 3.6272 -0.3053 -0.5344 0.2610  720  LEU B CA  
17832 C C   . LEU C 720  ? 3.2821 3.9329 3.6198 -0.2935 -0.5253 0.3174  720  LEU B C   
17833 O O   . LEU C 720  ? 3.2886 3.9188 3.5804 -0.2969 -0.4959 0.3132  720  LEU B O   
17834 C CB  . LEU C 720  ? 3.2312 3.8820 3.6621 -0.3060 -0.4777 0.2544  720  LEU B CB  
17835 C CG  . LEU C 720  ? 3.3164 3.9855 3.8258 -0.3173 -0.4754 0.2012  720  LEU B CG  
17836 C CD1 . LEU C 720  ? 3.3126 3.9626 3.8171 -0.3177 -0.4169 0.2064  720  LEU B CD1 
17837 C CD2 . LEU C 720  ? 3.3871 4.0631 3.9275 -0.3372 -0.4697 0.1423  720  LEU B CD2 
17838 N N   . GLY C 721  ? 3.0596 3.7199 3.3762 -0.2799 -0.5484 0.3698  721  GLY B N   
17839 C CA  . GLY C 721  ? 3.1399 3.7962 3.3820 -0.2688 -0.5460 0.4249  721  GLY B CA  
17840 C C   . GLY C 721  ? 3.1569 3.8228 3.3766 -0.2564 -0.5554 0.4823  721  GLY B C   
17841 O O   . GLY C 721  ? 3.1525 3.8118 3.3911 -0.2536 -0.5292 0.4847  721  GLY B O   
17842 N N   . PRO C 722  ? 3.5041 4.1871 3.6813 -0.2510 -0.5936 0.5295  722  PRO B N   
17843 C CA  . PRO C 722  ? 3.4546 4.1504 3.5980 -0.2417 -0.6044 0.5910  722  PRO B CA  
17844 C C   . PRO C 722  ? 3.3830 4.0635 3.4829 -0.2298 -0.5354 0.6181  722  PRO B C   
17845 O O   . PRO C 722  ? 3.3396 4.0295 3.4215 -0.2232 -0.5331 0.6627  722  PRO B O   
17846 C CB  . PRO C 722  ? 3.4877 4.2040 3.5829 -0.2415 -0.6459 0.6283  722  PRO B CB  
17847 C CG  . PRO C 722  ? 3.5177 4.2358 3.6466 -0.2528 -0.6832 0.5828  722  PRO B CG  
17848 C CD  . PRO C 722  ? 3.5264 4.2211 3.6881 -0.2568 -0.6342 0.5248  722  PRO B CD  
17849 N N   . ARG C 723  ? 3.1516 3.8069 3.2326 -0.2275 -0.4804 0.5916  723  ARG B N   
17850 C CA  . ARG C 723  ? 3.0929 3.7270 3.1340 -0.2151 -0.4132 0.6115  723  ARG B CA  
17851 C C   . ARG C 723  ? 3.0423 3.6733 3.1216 -0.2169 -0.3989 0.6116  723  ARG B C   
17852 O O   . ARG C 723  ? 3.0303 3.6609 3.0776 -0.2058 -0.3689 0.6527  723  ARG B O   
17853 C CB  . ARG C 723  ? 3.0677 3.6650 3.0963 -0.2171 -0.3606 0.5685  723  ARG B CB  
17854 C CG  . ARG C 723  ? 3.0501 3.6466 3.0688 -0.2244 -0.3831 0.5417  723  ARG B CG  
17855 C CD  . ARG C 723  ? 3.0279 3.5826 3.0379 -0.2306 -0.3313 0.4948  723  ARG B CD  
17856 N NE  . ARG C 723  ? 3.0323 3.5850 3.0337 -0.2402 -0.3525 0.4663  723  ARG B NE  
17857 C CZ  . ARG C 723  ? 3.0397 3.5966 3.0957 -0.2604 -0.3790 0.4146  723  ARG B CZ  
17858 N NH1 . ARG C 723  ? 3.0207 3.5858 3.1450 -0.2716 -0.3868 0.3844  723  ARG B NH1 
17859 N NH2 . ARG C 723  ? 3.0741 3.6298 3.1160 -0.2692 -0.3975 0.3929  723  ARG B NH2 
17860 N N   . CYS C 724  ? 3.2773 3.9087 3.4255 -0.2304 -0.4207 0.5650  724  CYS B N   
17861 C CA  . CYS C 724  ? 3.2237 3.8515 3.4118 -0.2333 -0.4046 0.5569  724  CYS B CA  
17862 C C   . CYS C 724  ? 3.2161 3.8685 3.4337 -0.2344 -0.4620 0.5791  724  CYS B C   
17863 O O   . CYS C 724  ? 3.1796 3.8311 3.4107 -0.2334 -0.4495 0.5922  724  CYS B O   
17864 C CB  . CYS C 724  ? 3.2129 3.8257 3.4570 -0.2470 -0.3818 0.4896  724  CYS B CB  
17865 S SG  . CYS C 724  ? 2.8318 3.4687 3.1506 -0.2600 -0.4478 0.4363  724  CYS B SG  
17866 N N   . ILE C 725  ? 3.2408 3.9120 3.4656 -0.2371 -0.5253 0.5834  725  ILE B N   
17867 C CA  . ILE C 725  ? 3.2446 3.9322 3.4918 -0.2386 -0.5850 0.6042  725  ILE B CA  
17868 C C   . ILE C 725  ? 3.2383 3.9287 3.4472 -0.2325 -0.5690 0.6618  725  ILE B C   
17869 O O   . ILE C 725  ? 3.2342 3.9254 3.4706 -0.2348 -0.5874 0.6665  725  ILE B O   
17870 C CB  . ILE C 725  ? 3.2547 3.9591 3.4901 -0.2414 -0.6533 0.6189  725  ILE B CB  
17871 C CG1 . ILE C 725  ? 3.2632 3.9679 3.5456 -0.2484 -0.6757 0.5593  725  ILE B CG1 
17872 C CG2 . ILE C 725  ? 3.2023 3.9162 3.4465 -0.2431 -0.7137 0.6493  725  ILE B CG2 
17873 C CD1 . ILE C 725  ? 3.2587 3.9787 3.5388 -0.2524 -0.7489 0.5681  725  ILE B CD1 
17874 N N   . LYS C 726  ? 3.2002 3.8929 3.3450 -0.2243 -0.5338 0.7046  726  LYS B N   
17875 C CA  . LYS C 726  ? 3.1871 3.8871 3.2927 -0.2181 -0.5127 0.7604  726  LYS B CA  
17876 C C   . LYS C 726  ? 3.0872 3.7690 3.2220 -0.2184 -0.4657 0.7410  726  LYS B C   
17877 O O   . LYS C 726  ? 3.0446 3.7313 3.1865 -0.2209 -0.4759 0.7647  726  LYS B O   
17878 C CB  . LYS C 726  ? 3.2782 3.9863 3.3128 -0.2057 -0.4761 0.8030  726  LYS B CB  
17879 C CG  . LYS C 726  ? 3.3916 4.1313 3.3810 -0.2057 -0.5231 0.8544  726  LYS B CG  
17880 C CD  . LYS C 726  ? 3.4503 4.2080 3.3711 -0.1914 -0.4831 0.9097  726  LYS B CD  
17881 C CE  . LYS C 726  ? 3.5064 4.3035 3.3825 -0.1947 -0.5307 0.9659  726  LYS B CE  
17882 N NZ  . LYS C 726  ? 3.5050 4.3290 3.3192 -0.1804 -0.4931 1.0237  726  LYS B NZ  
17883 N N   . ALA C 727  ? 3.8368 4.4964 3.9857 -0.2179 -0.4148 0.6978  727  ALA B N   
17884 C CA  . ALA C 727  ? 3.7869 4.4281 3.9620 -0.2208 -0.3664 0.6755  727  ALA B CA  
17885 C C   . ALA C 727  ? 3.7181 4.3639 3.9622 -0.2316 -0.4002 0.6392  727  ALA B C   
17886 O O   . ALA C 727  ? 3.6932 4.3307 3.9627 -0.2356 -0.3710 0.6258  727  ALA B O   
17887 C CB  . ALA C 727  ? 3.7980 4.4121 3.9715 -0.2217 -0.3110 0.6342  727  ALA B CB  
17888 N N   . PHE C 728  ? 2.5478 3.2072 2.8216 -0.2353 -0.4626 0.6227  728  PHE B N   
17889 C CA  . PHE C 728  ? 2.4803 3.1452 2.8173 -0.2413 -0.5015 0.5899  728  PHE B CA  
17890 C C   . PHE C 728  ? 2.4723 3.1440 2.7967 -0.2399 -0.5388 0.6361  728  PHE B C   
17891 O O   . PHE C 728  ? 2.4709 3.1372 2.8106 -0.2418 -0.5185 0.6373  728  PHE B O   
17892 C CB  . PHE C 728  ? 2.3625 3.0367 2.7390 -0.2444 -0.5528 0.5489  728  PHE B CB  
17893 C CG  . PHE C 728  ? 2.2342 2.9146 2.6821 -0.2472 -0.5849 0.5031  728  PHE B CG  
17894 C CD1 . PHE C 728  ? 2.2023 2.8807 2.6976 -0.2524 -0.5438 0.4541  728  PHE B CD1 
17895 C CD2 . PHE C 728  ? 2.1730 2.8614 2.6390 -0.2444 -0.6568 0.5087  728  PHE B CD2 
17896 C CE1 . PHE C 728  ? 2.1557 2.8456 2.7182 -0.2530 -0.5725 0.4102  728  PHE B CE1 
17897 C CE2 . PHE C 728  ? 2.1249 2.8185 2.6560 -0.2430 -0.6871 0.4651  728  PHE B CE2 
17898 C CZ  . PHE C 728  ? 2.1215 2.8187 2.7025 -0.2464 -0.6442 0.4151  728  PHE B CZ  
17899 N N   . THR C 729  ? 2.4330 3.1153 2.7260 -0.2388 -0.5928 0.6746  729  THR B N   
17900 C CA  . THR C 729  ? 2.3966 3.0830 2.6720 -0.2411 -0.6381 0.7197  729  THR B CA  
17901 C C   . THR C 729  ? 2.4134 3.1025 2.6396 -0.2405 -0.6013 0.7762  729  THR B C   
17902 O O   . THR C 729  ? 2.3815 3.0699 2.6008 -0.2451 -0.6269 0.8056  729  THR B O   
17903 C CB  . THR C 729  ? 2.7482 3.4453 2.9937 -0.2433 -0.7036 0.7501  729  THR B CB  
17904 O OG1 . THR C 729  ? 2.7835 3.4879 3.0117 -0.2407 -0.6905 0.7398  729  THR B OG1 
17905 C CG2 . THR C 729  ? 2.7252 3.4153 3.0184 -0.2458 -0.7725 0.7193  729  THR B CG2 
17906 N N   . GLU C 730  ? 3.2667 3.9579 3.4562 -0.2344 -0.5430 0.7916  730  GLU B N   
17907 C CA  . GLU C 730  ? 3.3029 3.9977 3.4508 -0.2313 -0.4982 0.8383  730  GLU B CA  
17908 C C   . GLU C 730  ? 3.2971 3.9763 3.4852 -0.2354 -0.4669 0.8106  730  GLU B C   
17909 O O   . GLU C 730  ? 3.2671 3.9486 3.4444 -0.2394 -0.4684 0.8427  730  GLU B O   
17910 C CB  . GLU C 730  ? 3.3157 4.0099 3.4230 -0.2204 -0.4392 0.8479  730  GLU B CB  
17911 C CG  . GLU C 730  ? 3.3130 4.0291 3.3643 -0.2140 -0.4576 0.8909  730  GLU B CG  
17912 C CD  . GLU C 730  ? 3.2830 4.0221 3.2764 -0.2090 -0.4430 0.9607  730  GLU B CD  
17913 O OE1 . GLU C 730  ? 3.2415 3.9737 3.2308 -0.2059 -0.3981 0.9722  730  GLU B OE1 
17914 O OE2 . GLU C 730  ? 3.2945 4.0610 3.2463 -0.2090 -0.4764 1.0042  730  GLU B OE2 
17915 N N   . CYS C 731  ? 4.5664 5.2313 4.7999 -0.2362 -0.4385 0.7501  731  CYS B N   
17916 C CA  . CYS C 731  ? 4.5839 5.2359 4.8520 -0.2409 -0.3957 0.7200  731  CYS B CA  
17917 C C   . CYS C 731  ? 4.5699 5.2221 4.8960 -0.2477 -0.4359 0.6867  731  CYS B C   
17918 O O   . CYS C 731  ? 4.5613 5.2079 4.9065 -0.2524 -0.4122 0.6792  731  CYS B O   
17919 C CB  . CYS C 731  ? 4.5709 5.2085 4.8547 -0.2411 -0.3440 0.6729  731  CYS B CB  
17920 S SG  . CYS C 731  ? 5.1607 5.7943 5.3732 -0.2291 -0.3110 0.7084  731  CYS B SG  
17921 N N   . CYS C 732  ? 3.5517 4.2097 3.9038 -0.2472 -0.4974 0.6673  732  CYS B N   
17922 C CA  . CYS C 732  ? 3.5350 4.1917 3.9369 -0.2494 -0.5427 0.6394  732  CYS B CA  
17923 C C   . CYS C 732  ? 3.5199 4.1732 3.8893 -0.2520 -0.5732 0.6924  732  CYS B C   
17924 O O   . CYS C 732  ? 3.5136 4.1598 3.9075 -0.2551 -0.5710 0.6812  732  CYS B O   
17925 C CB  . CYS C 732  ? 3.5263 4.1883 3.9635 -0.2462 -0.6021 0.6043  732  CYS B CB  
17926 S SG  . CYS C 732  ? 3.4029 4.0620 3.9080 -0.2436 -0.6547 0.5589  732  CYS B SG  
17927 N N   . VAL C 733  ? 3.2005 3.8599 3.5132 -0.2522 -0.6014 0.7496  733  VAL B N   
17928 C CA  . VAL C 733  ? 3.1672 3.8254 3.4397 -0.2583 -0.6299 0.8064  733  VAL B CA  
17929 C C   . VAL C 733  ? 3.1405 3.7969 3.3998 -0.2618 -0.5740 0.8258  733  VAL B C   
17930 O O   . VAL C 733  ? 3.1032 3.7508 3.3658 -0.2681 -0.5888 0.8367  733  VAL B O   
17931 C CB  . VAL C 733  ? 3.1734 3.8472 3.3797 -0.2601 -0.6534 0.8691  733  VAL B CB  
17932 C CG1 . VAL C 733  ? 3.1788 3.8555 3.3386 -0.2699 -0.6722 0.9315  733  VAL B CG1 
17933 C CG2 . VAL C 733  ? 3.1625 3.8366 3.3770 -0.2596 -0.7164 0.8556  733  VAL B CG2 
17934 N N   . VAL C 734  ? 3.6371 4.2994 3.8798 -0.2575 -0.5100 0.8291  734  VAL B N   
17935 C CA  . VAL C 734  ? 3.6483 4.3080 3.8782 -0.2600 -0.4523 0.8454  734  VAL B CA  
17936 C C   . VAL C 734  ? 3.6453 4.2917 3.9306 -0.2660 -0.4447 0.7987  734  VAL B C   
17937 O O   . VAL C 734  ? 3.6601 4.3032 3.9355 -0.2728 -0.4388 0.8222  734  VAL B O   
17938 C CB  . VAL C 734  ? 3.6729 4.3325 3.8856 -0.2526 -0.3857 0.8404  734  VAL B CB  
17939 C CG1 . VAL C 734  ? 3.6712 4.3235 3.8785 -0.2556 -0.3253 0.8479  734  VAL B CG1 
17940 C CG2 . VAL C 734  ? 3.6946 4.3708 3.8461 -0.2444 -0.3881 0.8925  734  VAL B CG2 
17941 N N   . ALA C 735  ? 4.0442 4.6860 4.3873 -0.2641 -0.4453 0.7326  735  ALA B N   
17942 C CA  . ALA C 735  ? 4.0233 4.6592 4.4234 -0.2687 -0.4326 0.6815  735  ALA B CA  
17943 C C   . ALA C 735  ? 4.0027 4.6336 4.4299 -0.2688 -0.4960 0.6704  735  ALA B C   
17944 O O   . ALA C 735  ? 3.9892 4.6160 4.4539 -0.2718 -0.4900 0.6394  735  ALA B O   
17945 C CB  . ALA C 735  ? 4.0252 4.6640 4.4758 -0.2679 -0.4068 0.6152  735  ALA B CB  
17946 N N   . SER C 736  ? 3.1244 3.7540 3.5300 -0.2652 -0.5572 0.6957  736  SER B N   
17947 C CA  . SER C 736  ? 3.1206 3.7380 3.5434 -0.2641 -0.6235 0.6889  736  SER B CA  
17948 C C   . SER C 736  ? 3.1212 3.7270 3.4982 -0.2730 -0.6369 0.7441  736  SER B C   
17949 O O   . SER C 736  ? 3.1179 3.7092 3.5168 -0.2746 -0.6553 0.7273  736  SER B O   
17950 C CB  . SER C 736  ? 3.1202 3.7373 3.5378 -0.2585 -0.6862 0.6913  736  SER B CB  
17951 O OG  . SER C 736  ? 3.1224 3.7513 3.5834 -0.2517 -0.6747 0.6389  736  SER B OG  
17952 N N   . GLN C 737  ? 2.6676 3.2817 2.9804 -0.2790 -0.6276 0.8094  737  GLN B N   
17953 C CA  . GLN C 737  ? 2.6551 3.2641 2.9202 -0.2904 -0.6332 0.8662  737  GLN B CA  
17954 C C   . GLN C 737  ? 2.6504 3.2552 2.9377 -0.2946 -0.5814 0.8474  737  GLN B C   
17955 O O   . GLN C 737  ? 2.6260 3.2192 2.8969 -0.3040 -0.5930 0.8699  737  GLN B O   
17956 C CB  . GLN C 737  ? 2.6593 3.2894 2.8571 -0.2946 -0.6143 0.9348  737  GLN B CB  
17957 C CG  . GLN C 737  ? 2.6662 3.3107 2.8481 -0.2875 -0.6320 0.9418  737  GLN B CG  
17958 C CD  . GLN C 737  ? 2.6680 3.3050 2.8329 -0.2923 -0.7117 0.9594  737  GLN B CD  
17959 O OE1 . GLN C 737  ? 2.6845 3.3216 2.8009 -0.3045 -0.7442 1.0141  737  GLN B OE1 
17960 N NE2 . GLN C 737  ? 2.6531 3.2835 2.8557 -0.2841 -0.7443 0.9143  737  GLN B NE2 
17961 N N   . LEU C 738  ? 3.3637 3.9765 3.6868 -0.2893 -0.5253 0.8051  738  LEU B N   
17962 C CA  . LEU C 738  ? 3.4103 4.0224 3.7521 -0.2948 -0.4661 0.7871  738  LEU B CA  
17963 C C   . LEU C 738  ? 3.4743 4.0752 3.8705 -0.2964 -0.4788 0.7346  738  LEU B C   
17964 O O   . LEU C 738  ? 3.4929 4.0897 3.8871 -0.3052 -0.4499 0.7400  738  LEU B O   
17965 C CB  . LEU C 738  ? 3.3969 4.0180 3.7546 -0.2906 -0.4045 0.7588  738  LEU B CB  
17966 C CG  . LEU C 738  ? 3.3720 3.9914 3.7451 -0.2981 -0.3389 0.7403  738  LEU B CG  
17967 C CD1 . LEU C 738  ? 3.3758 3.9979 3.6877 -0.3028 -0.3019 0.8061  738  LEU B CD1 
17968 C CD2 . LEU C 738  ? 3.3668 3.9886 3.7745 -0.2957 -0.2952 0.6886  738  LEU B CD2 
17969 N N   . ARG C 739  ? 3.5348 4.1331 3.9803 -0.2871 -0.5201 0.6827  739  ARG B N   
17970 C CA  . ARG C 739  ? 3.6109 4.2022 4.1102 -0.2845 -0.5361 0.6296  739  ARG B CA  
17971 C C   . ARG C 739  ? 3.6291 4.1972 4.1017 -0.2872 -0.5897 0.6596  739  ARG B C   
17972 O O   . ARG C 739  ? 3.6292 4.1866 4.1353 -0.2845 -0.6048 0.6241  739  ARG B O   
17973 C CB  . ARG C 739  ? 3.6845 4.2842 4.2450 -0.2713 -0.5654 0.5654  739  ARG B CB  
17974 C CG  . ARG C 739  ? 3.7696 4.3578 4.3167 -0.2622 -0.6398 0.5796  739  ARG B CG  
17975 C CD  . ARG C 739  ? 3.8498 4.4501 4.4599 -0.2487 -0.6648 0.5150  739  ARG B CD  
17976 N NE  . ARG C 739  ? 3.9296 4.5187 4.5255 -0.2404 -0.7350 0.5291  739  ARG B NE  
17977 C CZ  . ARG C 739  ? 3.9749 4.5738 4.6164 -0.2281 -0.7676 0.4829  739  ARG B CZ  
17978 N NH1 . ARG C 739  ? 3.9813 4.6049 4.6866 -0.2234 -0.7356 0.4193  739  ARG B NH1 
17979 N NH2 . ARG C 739  ? 3.9964 4.5824 4.6190 -0.2222 -0.8327 0.5010  739  ARG B NH2 
17980 N N   . ALA C 740  ? 2.9578 3.5180 3.3682 -0.2928 -0.6198 0.7242  740  ALA B N   
17981 C CA  . ALA C 740  ? 2.9777 3.5133 3.3487 -0.3009 -0.6668 0.7633  740  ALA B CA  
17982 C C   . ALA C 740  ? 2.9695 3.5068 3.3044 -0.3164 -0.6219 0.8036  740  ALA B C   
17983 O O   . ALA C 740  ? 3.0162 3.5341 3.3140 -0.3271 -0.6518 0.8391  740  ALA B O   
17984 C CB  . ALA C 740  ? 2.9913 3.5209 3.3095 -0.3039 -0.7209 0.8160  740  ALA B CB  
17985 N N   . ASN C 741  ? 3.8521 4.4106 4.1956 -0.3186 -0.5512 0.7984  741  ASN B N   
17986 C CA  . ASN C 741  ? 3.8073 4.3704 4.1148 -0.3328 -0.5048 0.8396  741  ASN B CA  
17987 C C   . ASN C 741  ? 3.9270 4.4958 4.2748 -0.3360 -0.4426 0.7970  741  ASN B C   
17988 O O   . ASN C 741  ? 3.9469 4.5120 4.2749 -0.3487 -0.4185 0.8191  741  ASN B O   
17989 C CB  . ASN C 741  ? 3.6569 4.2396 3.9071 -0.3361 -0.4792 0.9037  741  ASN B CB  
17990 C CG  . ASN C 741  ? 3.5489 4.1290 3.7408 -0.3432 -0.5346 0.9662  741  ASN B CG  
17991 O OD1 . ASN C 741  ? 3.5182 4.1094 3.6898 -0.3374 -0.5568 0.9865  741  ASN B OD1 
17992 N ND2 . ASN C 741  ? 3.4905 4.0557 3.6533 -0.3577 -0.5584 0.9967  741  ASN B ND2 
17993 N N   . ILE C 742  ? 4.0445 4.6237 4.4464 -0.3270 -0.4169 0.7375  742  ILE B N   
17994 C CA  . ILE C 742  ? 4.1557 4.7420 4.5995 -0.3324 -0.3623 0.6915  742  ILE B CA  
17995 C C   . ILE C 742  ? 4.2059 4.7809 4.6828 -0.3336 -0.3900 0.6555  742  ILE B C   
17996 O O   . ILE C 742  ? 4.2132 4.7927 4.7130 -0.3421 -0.3506 0.6294  742  ILE B O   
17997 C CB  . ILE C 742  ? 4.1835 4.7848 4.6800 -0.3249 -0.3349 0.6313  742  ILE B CB  
17998 C CG1 . ILE C 742  ? 4.1991 4.8064 4.6647 -0.3197 -0.3205 0.6594  742  ILE B CG1 
17999 C CG2 . ILE C 742  ? 4.1972 4.8077 4.7254 -0.3356 -0.2715 0.5937  742  ILE B CG2 
18000 C CD1 . ILE C 742  ? 4.1997 4.8181 4.7102 -0.3155 -0.2921 0.6029  742  ILE B CD1 
18001 N N   . SER C 743  ? 4.0212 4.5798 4.4980 -0.3246 -0.4589 0.6542  743  SER B N   
18002 C CA  . SER C 743  ? 4.0436 4.5864 4.5516 -0.3202 -0.4945 0.6158  743  SER B CA  
18003 C C   . SER C 743  ? 4.0535 4.5664 4.5254 -0.3161 -0.5709 0.6480  743  SER B C   
18004 O O   . SER C 743  ? 4.0402 4.5509 4.5031 -0.3074 -0.6105 0.6591  743  SER B O   
18005 C CB  . SER C 743  ? 4.0434 4.6029 4.6288 -0.3052 -0.4957 0.5349  743  SER B CB  
18006 O OG  . SER C 743  ? 4.0361 4.5981 4.6326 -0.2912 -0.5358 0.5261  743  SER B OG  
18007 N N   . GLY C 750  ? 2.7401 3.2892 3.6269 -0.1886 -0.7110 0.1812  750  GLY B N   
18008 C CA  . GLY C 750  ? 2.7574 3.3073 3.6432 -0.1800 -0.7460 0.1935  750  GLY B CA  
18009 C C   . GLY C 750  ? 2.7607 3.3631 3.6894 -0.1865 -0.6968 0.1674  750  GLY B C   
18010 O O   . GLY C 750  ? 2.7445 3.3602 3.6983 -0.1736 -0.7254 0.1503  750  GLY B O   
18011 N N   . ARG C 751  ? 3.7134 4.3436 4.6487 -0.2075 -0.6239 0.1640  751  ARG B N   
18012 C CA  . ARG C 751  ? 3.7159 4.3892 4.6827 -0.2182 -0.5724 0.1430  751  ARG B CA  
18013 C C   . ARG C 751  ? 3.8047 4.4642 4.7095 -0.2395 -0.5399 0.2091  751  ARG B C   
18014 O O   . ARG C 751  ? 3.8155 4.4641 4.6797 -0.2586 -0.4982 0.2469  751  ARG B O   
18015 C CB  . ARG C 751  ? 3.6312 4.3468 4.6486 -0.2284 -0.5109 0.0904  751  ARG B CB  
18016 C CG  . ARG C 751  ? 3.5373 4.2911 4.6347 -0.2066 -0.5304 0.0104  751  ARG B CG  
18017 C CD  . ARG C 751  ? 3.4081 4.2126 4.5541 -0.2222 -0.4637 -0.0394 751  ARG B CD  
18018 N NE  . ARG C 751  ? 3.3077 4.0962 4.4179 -0.2424 -0.4218 -0.0128 751  ARG B NE  
18019 C CZ  . ARG C 751  ? 3.2301 4.0133 4.3495 -0.2350 -0.4310 -0.0327 751  ARG B CZ  
18020 N NH1 . ARG C 751  ? 3.2188 4.0106 4.3826 -0.2053 -0.4806 -0.0808 751  ARG B NH1 
18021 N NH2 . ARG C 751  ? 3.1886 3.9574 4.2716 -0.2564 -0.3908 -0.0047 751  ARG B NH2 
18022 N N   . LEU C 752  ? 4.2424 4.9035 5.1395 -0.2351 -0.5594 0.2224  752  LEU B N   
18023 C CA  . LEU C 752  ? 4.2955 4.9499 5.1397 -0.2514 -0.5266 0.2772  752  LEU B CA  
18024 C C   . LEU C 752  ? 4.2825 4.9621 5.1567 -0.2479 -0.5210 0.2496  752  LEU B C   
18025 O O   . LEU C 752  ? 4.2883 4.9730 5.1923 -0.2307 -0.5725 0.2230  752  LEU B O   
18026 C CB  . LEU C 752  ? 4.3608 4.9765 5.1336 -0.2516 -0.5706 0.3491  752  LEU B CB  
18027 C CG  . LEU C 752  ? 4.4093 5.0217 5.1262 -0.2636 -0.5457 0.4075  752  LEU B CG  
18028 C CD1 . LEU C 752  ? 4.4324 5.0503 5.1225 -0.2827 -0.4728 0.4329  752  LEU B CD1 
18029 C CD2 . LEU C 752  ? 4.4324 5.0147 5.0874 -0.2622 -0.6007 0.4704  752  LEU B CD2 
18030 N N   . HIS C 753  ? 4.7307 5.4236 5.5945 -0.2642 -0.4597 0.2563  753  HIS B N   
18031 C CA  . HIS C 753  ? 4.6829 5.3997 5.5767 -0.2641 -0.4474 0.2234  753  HIS B CA  
18032 C C   . HIS C 753  ? 4.5637 5.2747 5.4136 -0.2813 -0.3889 0.2576  753  HIS B C   
18033 O O   . HIS C 753  ? 4.5493 5.2744 5.4149 -0.2960 -0.3307 0.2336  753  HIS B O   
18034 C CB  . HIS C 753  ? 4.7610 5.5180 5.7339 -0.2623 -0.4334 0.1448  753  HIS B CB  
18035 C CG  . HIS C 753  ? 4.8283 5.5921 5.8319 -0.2575 -0.4382 0.1170  753  HIS B CG  
18036 N ND1 . HIS C 753  ? 4.8674 5.6246 5.8515 -0.2730 -0.3924 0.1320  753  HIS B ND1 
18037 C CD2 . HIS C 753  ? 4.8487 5.6241 5.8997 -0.2372 -0.4856 0.0747  753  HIS B CD2 
18038 C CE1 . HIS C 753  ? 4.8780 5.6440 5.8970 -0.2638 -0.4096 0.0982  753  HIS B CE1 
18039 N NE2 . HIS C 753  ? 4.8683 5.6444 5.9278 -0.2404 -0.4669 0.0628  753  HIS B NE2 
18040 N N   . MET C 754  ? 3.7754 4.4650 4.5684 -0.2788 -0.4058 0.3134  754  MET B N   
18041 C CA  . MET C 754  ? 3.6917 4.3732 4.4381 -0.2902 -0.3545 0.3483  754  MET B CA  
18042 C C   . MET C 754  ? 3.6411 4.3423 4.4254 -0.2969 -0.3195 0.2966  754  MET B C   
18043 O O   . MET C 754  ? 3.6365 4.3611 4.4793 -0.2912 -0.3451 0.2412  754  MET B O   
18044 C CB  . MET C 754  ? 3.6543 4.3189 4.3435 -0.2827 -0.3875 0.4058  754  MET B CB  
18045 C CG  . MET C 754  ? 3.6169 4.2631 4.2647 -0.2782 -0.4319 0.4593  754  MET B CG  
18046 S SD  . MET C 754  ? 3.3140 3.9509 3.9101 -0.2700 -0.4826 0.5109  754  MET B SD  
18047 C CE  . MET C 754  ? 2.5497 3.1967 3.1392 -0.2730 -0.4298 0.4991  754  MET B CE  
18048 N N   . LYS C 755  ? 2.9395 3.6305 3.6883 -0.3091 -0.2619 0.3154  755  LYS B N   
18049 C CA  . LYS C 755  ? 2.9317 3.6323 3.7006 -0.3187 -0.2261 0.2752  755  LYS B CA  
18050 C C   . LYS C 755  ? 2.9963 3.6711 3.7038 -0.3277 -0.1695 0.3147  755  LYS B C   
18051 O O   . LYS C 755  ? 2.9744 3.6311 3.6337 -0.3280 -0.1498 0.3663  755  LYS B O   
18052 C CB  . LYS C 755  ? 2.8927 3.6208 3.7261 -0.3316 -0.1987 0.2089  755  LYS B CB  
18053 C CG  . LYS C 755  ? 2.8363 3.5983 3.7414 -0.3212 -0.2482 0.1522  755  LYS B CG  
18054 C CD  . LYS C 755  ? 2.8155 3.5824 3.7280 -0.3088 -0.2956 0.1449  755  LYS B CD  
18055 C CE  . LYS C 755  ? 2.8389 3.6046 3.7404 -0.3222 -0.2586 0.1311  755  LYS B CE  
18056 N NZ  . LYS C 755  ? 2.8292 3.6022 3.7399 -0.3116 -0.3052 0.1210  755  LYS B NZ  
18057 N N   . THR C 756  ? 2.6066 3.2792 3.3148 -0.3344 -0.1447 0.2899  756  THR B N   
18058 C CA  . THR C 756  ? 2.6994 3.3443 3.3549 -0.3432 -0.0861 0.3142  756  THR B CA  
18059 C C   . THR C 756  ? 2.7881 3.4378 3.4721 -0.3580 -0.0596 0.2583  756  THR B C   
18060 O O   . THR C 756  ? 2.8088 3.4571 3.4884 -0.3534 -0.0782 0.2488  756  THR B O   
18061 C CB  . THR C 756  ? 2.6567 3.2795 3.2444 -0.3281 -0.0973 0.3754  756  THR B CB  
18062 O OG1 . THR C 756  ? 2.6383 3.2576 3.1935 -0.3193 -0.1132 0.4310  756  THR B OG1 
18063 C CG2 . THR C 756  ? 2.6297 3.2224 3.1663 -0.3336 -0.0383 0.3908  756  THR B CG2 
18064 N N   . LEU C 757  ? 2.3045 2.9610 3.0164 -0.3780 -0.0166 0.2214  757  LEU B N   
18065 C CA  . LEU C 757  ? 2.4004 3.0722 3.1530 -0.3968 0.0031  0.1592  757  LEU B CA  
18066 C C   . LEU C 757  ? 2.4466 3.0871 3.1548 -0.4029 0.0299  0.1631  757  LEU B C   
18067 O O   . LEU C 757  ? 2.4083 3.0094 3.0492 -0.3966 0.0558  0.2118  757  LEU B O   
18068 C CB  . LEU C 757  ? 2.4545 3.1397 3.2381 -0.4204 0.0479  0.1246  757  LEU B CB  
18069 C CG  . LEU C 757  ? 2.5257 3.2427 3.3662 -0.4438 0.0641  0.0533  757  LEU B CG  
18070 C CD1 . LEU C 757  ? 2.5560 3.3282 3.4752 -0.4350 0.0133  0.0060  757  LEU B CD1 
18071 C CD2 . LEU C 757  ? 2.5461 3.2590 3.3855 -0.4714 0.1240  0.0376  757  LEU B CD2 
18072 N N   . LEU C 758  ? 3.1441 3.8042 3.8910 -0.4142 0.0214  0.1106  758  LEU B N   
18073 C CA  . LEU C 758  ? 3.2111 3.8434 3.9246 -0.4262 0.0490  0.0997  758  LEU B CA  
18074 C C   . LEU C 758  ? 3.4022 4.0738 4.1779 -0.4383 0.0244  0.0364  758  LEU B C   
18075 O O   . LEU C 758  ? 3.4178 4.1074 4.2111 -0.4230 -0.0265 0.0329  758  LEU B O   
18076 C CB  . LEU C 758  ? 3.0738 3.6729 3.7236 -0.4049 0.0334  0.1505  758  LEU B CB  
18077 C CG  . LEU C 758  ? 2.9481 3.4962 3.5304 -0.4117 0.0798  0.1650  758  LEU B CG  
18078 C CD1 . LEU C 758  ? 2.9007 3.4311 3.4352 -0.3896 0.0530  0.2020  758  LEU B CD1 
18079 C CD2 . LEU C 758  ? 2.9294 3.4767 3.5343 -0.4405 0.1060  0.1064  758  LEU B CD2 
18080 N N   . PRO C 759  ? 5.1370 5.8252 5.9465 -0.4669 0.0593  -0.0135 759  PRO B N   
18081 C CA  . PRO C 759  ? 5.2617 5.9944 6.1327 -0.4819 0.0404  -0.0763 759  PRO B CA  
18082 C C   . PRO C 759  ? 5.3694 6.0825 6.2121 -0.4824 0.0276  -0.0789 759  PRO B C   
18083 O O   . PRO C 759  ? 5.4347 6.1773 6.3163 -0.5004 0.0213  -0.1289 759  PRO B O   
18084 C CB  . PRO C 759  ? 5.2531 5.9920 6.1385 -0.5175 0.0952  -0.1149 759  PRO B CB  
18085 C CG  . PRO C 759  ? 5.2092 5.9288 6.0713 -0.5152 0.1254  -0.0811 759  PRO B CG  
18086 C CD  . PRO C 759  ? 5.1600 5.8313 5.9542 -0.4879 0.1166  -0.0131 759  PRO B CD  
18087 N N   . VAL C 760  ? 5.4439 3.7111 5.2054 -0.3274 0.0628  -0.1238 760  VAL B N   
18088 C CA  . VAL C 760  ? 5.5342 3.7913 5.2777 -0.3572 0.0924  -0.1249 760  VAL B CA  
18089 C C   . VAL C 760  ? 5.3874 3.6615 5.1272 -0.3564 0.1082  -0.1262 760  VAL B C   
18090 O O   . VAL C 760  ? 5.4207 3.6900 5.1387 -0.3783 0.1308  -0.1259 760  VAL B O   
18091 C CB  . VAL C 760  ? 5.8161 4.0539 5.5089 -0.3735 0.0879  -0.1157 760  VAL B CB  
18092 C CG1 . VAL C 760  ? 5.9355 4.1593 5.6175 -0.4072 0.1188  -0.1184 760  VAL B CG1 
18093 C CG2 . VAL C 760  ? 5.8964 4.1198 5.5890 -0.3664 0.0637  -0.1124 760  VAL B CG2 
18094 N N   . SER C 761  ? 4.6270 2.9211 4.3889 -0.3310 0.0957  -0.1278 761  SER B N   
18095 C CA  . SER C 761  ? 4.4284 2.7401 4.1903 -0.3265 0.1071  -0.1289 761  SER B CA  
18096 C C   . SER C 761  ? 4.2262 2.5426 3.9379 -0.3230 0.0978  -0.1194 761  SER B C   
18097 O O   . SER C 761  ? 4.1998 2.5264 3.9003 -0.3268 0.1117  -0.1193 761  SER B O   
18098 C CB  . SER C 761  ? 4.4812 2.7897 4.2592 -0.3507 0.1421  -0.1367 761  SER B CB  
18099 O OG  . SER C 761  ? 4.4464 2.7720 4.2317 -0.3447 0.1528  -0.1389 761  SER B OG  
18100 N N   . LYS C 762  ? 3.5667 1.8758 3.2492 -0.3155 0.0738  -0.1118 762  LYS B N   
18101 C CA  . LYS C 762  ? 3.3309 1.6429 2.9640 -0.3132 0.0637  -0.1029 762  LYS B CA  
18102 C C   . LYS C 762  ? 3.1704 1.5053 2.8022 -0.2861 0.0448  -0.1007 762  LYS B C   
18103 O O   . LYS C 762  ? 3.1514 1.4942 2.8031 -0.2634 0.0215  -0.1013 762  LYS B O   
18104 C CB  . LYS C 762  ? 3.2430 1.5376 2.8450 -0.3156 0.0445  -0.0959 762  LYS B CB  
18105 C CG  . LYS C 762  ? 3.1705 1.4419 2.7487 -0.3465 0.0627  -0.0939 762  LYS B CG  
18106 C CD  . LYS C 762  ? 3.0923 1.3473 2.6377 -0.3457 0.0396  -0.0857 762  LYS B CD  
18107 C CE  . LYS C 762  ? 3.0738 1.3035 2.6049 -0.3746 0.0539  -0.0843 762  LYS B CE  
18108 N NZ  . LYS C 762  ? 3.0654 1.2791 2.5752 -0.3695 0.0278  -0.0774 762  LYS B NZ  
18109 N N   . PRO C 763  ? 4.0170 2.3629 3.6243 -0.2891 0.0546  -0.0982 763  PRO B N   
18110 C CA  . PRO C 763  ? 3.8958 2.2636 3.4950 -0.2658 0.0377  -0.0953 763  PRO B CA  
18111 C C   . PRO C 763  ? 3.7950 2.1640 3.3642 -0.2496 0.0067  -0.0884 763  PRO B C   
18112 O O   . PRO C 763  ? 3.8190 2.1842 3.3447 -0.2570 0.0047  -0.0822 763  PRO B O   
18113 C CB  . PRO C 763  ? 3.8758 2.2493 3.4479 -0.2797 0.0586  -0.0936 763  PRO B CB  
18114 C CG  . PRO C 763  ? 3.9218 2.2816 3.5076 -0.3063 0.0898  -0.0990 763  PRO B CG  
18115 C CD  . PRO C 763  ? 4.0037 2.3430 3.5942 -0.3155 0.0850  -0.0991 763  PRO B CD  
18116 N N   . GLU C 764  ? 3.6401 2.0147 3.2329 -0.2279 -0.0172 -0.0898 764  GLU B N   
18117 C CA  . GLU C 764  ? 3.5231 1.9028 3.0925 -0.2090 -0.0482 -0.0845 764  GLU B CA  
18118 C C   . GLU C 764  ? 3.3668 1.7718 2.9523 -0.1821 -0.0656 -0.0861 764  GLU B C   
18119 O O   . GLU C 764  ? 3.3261 1.7415 2.9491 -0.1756 -0.0584 -0.0914 764  GLU B O   
18120 C CB  . GLU C 764  ? 3.5484 1.9112 3.1256 -0.2068 -0.0649 -0.0842 764  GLU B CB  
18121 C CG  . GLU C 764  ? 3.5391 1.9024 3.1667 -0.1985 -0.0667 -0.0910 764  GLU B CG  
18122 C CD  . GLU C 764  ? 3.5888 1.9287 3.2226 -0.2087 -0.0701 -0.0913 764  GLU B CD  
18123 O OE1 . GLU C 764  ? 3.6032 1.9335 3.2097 -0.2052 -0.0899 -0.0859 764  GLU B OE1 
18124 O OE2 . GLU C 764  ? 3.6069 1.9380 3.2728 -0.2206 -0.0531 -0.0969 764  GLU B OE2 
18125 N N   . ILE C 765  ? 2.9046 1.3195 2.4617 -0.1667 -0.0891 -0.0816 765  ILE B N   
18126 C CA  . ILE C 765  ? 2.8036 1.2444 2.3660 -0.1440 -0.1037 -0.0822 765  ILE B CA  
18127 C C   . ILE C 765  ? 2.8032 1.2497 2.3415 -0.1264 -0.1345 -0.0787 765  ILE B C   
18128 O O   . ILE C 765  ? 2.8538 1.2934 2.3521 -0.1334 -0.1383 -0.0738 765  ILE B O   
18129 C CB  . ILE C 765  ? 2.7255 1.1783 2.2655 -0.1513 -0.0870 -0.0804 765  ILE B CB  
18130 C CG1 . ILE C 765  ? 2.6801 1.1600 2.2207 -0.1277 -0.1044 -0.0804 765  ILE B CG1 
18131 C CG2 . ILE C 765  ? 2.7406 1.1829 2.2315 -0.1665 -0.0829 -0.0746 765  ILE B CG2 
18132 C CD1 . ILE C 765  ? 2.6456 1.1396 2.1902 -0.1318 -0.0850 -0.0815 765  ILE B CD1 
18133 N N   . ARG C 766  ? 3.0684 1.5280 2.6312 -0.1034 -0.1567 -0.0816 766  ARG B N   
18134 C CA  . ARG C 766  ? 3.0472 1.5106 2.5921 -0.0866 -0.1869 -0.0795 766  ARG B CA  
18135 C C   . ARG C 766  ? 3.0545 1.5424 2.5748 -0.0711 -0.2008 -0.0778 766  ARG B C   
18136 O O   . ARG C 766  ? 3.0432 1.5456 2.5672 -0.0493 -0.2267 -0.0792 766  ARG B O   
18137 C CB  . ARG C 766  ? 3.0000 1.4642 2.5825 -0.0702 -0.2050 -0.0839 766  ARG B CB  
18138 C CG  . ARG C 766  ? 2.9909 1.4332 2.6013 -0.0857 -0.1892 -0.0864 766  ARG B CG  
18139 C CD  . ARG C 766  ? 3.0374 1.4540 2.6184 -0.1054 -0.1838 -0.0821 766  ARG B CD  
18140 N NE  . ARG C 766  ? 3.0904 1.4857 2.6974 -0.1187 -0.1731 -0.0848 766  ARG B NE  
18141 C CZ  . ARG C 766  ? 3.1745 1.5501 2.7758 -0.1222 -0.1850 -0.0832 766  ARG B CZ  
18142 N NH1 . ARG C 766  ? 3.2320 1.6059 2.8032 -0.1126 -0.2085 -0.0789 766  ARG B NH1 
18143 N NH2 . ARG C 766  ? 3.1889 1.5464 2.8151 -0.1354 -0.1733 -0.0861 766  ARG B NH2 
18144 N N   . SER C 767  ? 2.7326 1.2255 2.2273 -0.0827 -0.1835 -0.0751 767  SER B N   
18145 C CA  . SER C 767  ? 2.7782 1.2949 2.2485 -0.0697 -0.1947 -0.0737 767  SER B CA  
18146 C C   . SER C 767  ? 2.8149 1.3297 2.2450 -0.0866 -0.1778 -0.0694 767  SER B C   
18147 O O   . SER C 767  ? 2.8173 1.3211 2.2487 -0.1070 -0.1505 -0.0689 767  SER B O   
18148 C CB  . SER C 767  ? 2.7835 1.3233 2.2837 -0.0551 -0.1953 -0.0774 767  SER B CB  
18149 O OG  . SER C 767  ? 2.7770 1.3079 2.3148 -0.0644 -0.1755 -0.0805 767  SER B OG  
18150 N N   . TYR C 768  ? 3.8269 2.3530 3.2217 -0.0779 -0.1944 -0.0668 768  TYR B N   
18151 C CA  . TYR C 768  ? 3.8805 2.4084 3.2350 -0.0911 -0.1818 -0.0629 768  TYR B CA  
18152 C C   . TYR C 768  ? 3.7765 2.3296 3.1323 -0.0842 -0.1754 -0.0643 768  TYR B C   
18153 O O   . TYR C 768  ? 3.7635 2.3362 3.1394 -0.0643 -0.1907 -0.0673 768  TYR B O   
18154 C CB  . TYR C 768  ? 4.0241 2.5525 3.3400 -0.0847 -0.2037 -0.0598 768  TYR B CB  
18155 C CG  . TYR C 768  ? 4.1244 2.6572 3.3967 -0.0961 -0.1938 -0.0558 768  TYR B CG  
18156 C CD1 . TYR C 768  ? 4.2100 2.7209 3.4579 -0.1197 -0.1763 -0.0516 768  TYR B CD1 
18157 C CD2 . TYR C 768  ? 4.1484 2.7076 3.4032 -0.0837 -0.2022 -0.0565 768  TYR B CD2 
18158 C CE1 . TYR C 768  ? 4.2624 2.7776 3.4702 -0.1303 -0.1674 -0.0481 768  TYR B CE1 
18159 C CE2 . TYR C 768  ? 4.2029 2.7665 3.4178 -0.0941 -0.1933 -0.0532 768  TYR B CE2 
18160 C CZ  . TYR C 768  ? 4.2643 2.8059 3.4560 -0.1172 -0.1759 -0.0490 768  TYR B CZ  
18161 O OH  . TYR C 768  ? 4.3010 2.8476 3.4531 -0.1278 -0.1671 -0.0458 768  TYR B OH  
18162 N N   . PHE C 769  ? 3.1812 1.7336 2.5150 -0.1012 -0.1529 -0.0619 769  PHE B N   
18163 C CA  . PHE C 769  ? 3.1054 1.6797 2.4378 -0.0973 -0.1447 -0.0628 769  PHE B CA  
18164 C C   . PHE C 769  ? 3.1128 1.6940 2.3985 -0.1048 -0.1410 -0.0592 769  PHE B C   
18165 O O   . PHE C 769  ? 3.1481 1.7181 2.4173 -0.1259 -0.1172 -0.0570 769  PHE B O   
18166 C CB  . PHE C 769  ? 3.0592 1.6263 2.4183 -0.1121 -0.1158 -0.0645 769  PHE B CB  
18167 C CG  . PHE C 769  ? 3.0051 1.5716 2.4132 -0.1025 -0.1184 -0.0688 769  PHE B CG  
18168 C CD1 . PHE C 769  ? 2.9675 1.5559 2.3974 -0.0835 -0.1299 -0.0712 769  PHE B CD1 
18169 C CD2 . PHE C 769  ? 2.9828 1.5272 2.4154 -0.1136 -0.1083 -0.0705 769  PHE B CD2 
18170 C CE1 . PHE C 769  ? 2.9566 1.5446 2.4319 -0.0751 -0.1319 -0.0750 769  PHE B CE1 
18171 C CE2 . PHE C 769  ? 2.9062 1.4505 2.3847 -0.1051 -0.1100 -0.0748 769  PHE B CE2 
18172 C CZ  . PHE C 769  ? 2.9486 1.5146 2.4484 -0.0858 -0.1219 -0.0769 769  PHE B CZ  
18173 N N   . PRO C 770  ? 2.7153 1.3160 1.9801 -0.0875 -0.1645 -0.0590 770  PRO B N   
18174 C CA  . PRO C 770  ? 2.7826 1.3913 2.0013 -0.0915 -0.1666 -0.0561 770  PRO B CA  
18175 C C   . PRO C 770  ? 2.8515 1.4613 2.0525 -0.1104 -0.1385 -0.0541 770  PRO B C   
18176 O O   . PRO C 770  ? 2.8519 1.4660 2.0761 -0.1143 -0.1214 -0.0558 770  PRO B O   
18177 C CB  . PRO C 770  ? 2.7581 1.3955 1.9731 -0.0673 -0.1919 -0.0586 770  PRO B CB  
18178 C CG  . PRO C 770  ? 2.7384 1.3751 1.9896 -0.0501 -0.2115 -0.0619 770  PRO B CG  
18179 C CD  . PRO C 770  ? 2.7067 1.3238 1.9930 -0.0623 -0.1915 -0.0624 770  PRO B CD  
18180 N N   . GLU C 771  ? 3.4668 2.0720 2.6272 -0.1224 -0.1339 -0.0507 771  GLU B N   
18181 C CA  . GLU C 771  ? 3.5213 2.1297 2.6615 -0.1392 -0.1091 -0.0490 771  GLU B CA  
18182 C C   . GLU C 771  ? 3.4619 2.0992 2.6026 -0.1249 -0.1149 -0.0511 771  GLU B C   
18183 O O   . GLU C 771  ? 3.4413 2.0968 2.5744 -0.1054 -0.1400 -0.0524 771  GLU B O   
18184 C CB  . GLU C 771  ? 3.6509 2.2525 2.7452 -0.1513 -0.1081 -0.0450 771  GLU B CB  
18185 C CG  . GLU C 771  ? 3.7419 2.3475 2.8113 -0.1690 -0.0835 -0.0434 771  GLU B CG  
18186 C CD  . GLU C 771  ? 3.8463 2.4480 2.8690 -0.1782 -0.0864 -0.0395 771  GLU B CD  
18187 O OE1 . GLU C 771  ? 3.8783 2.4652 2.8840 -0.2011 -0.0637 -0.0369 771  GLU B OE1 
18188 O OE2 . GLU C 771  ? 3.8871 2.5009 2.8906 -0.1626 -0.1116 -0.0393 771  GLU B OE2 
18189 N N   . SER C 772  ? 3.1677 1.8091 2.3179 -0.1346 -0.0920 -0.0517 772  SER B N   
18190 C CA  . SER C 772  ? 3.1166 1.7840 2.2700 -0.1225 -0.0956 -0.0533 772  SER B CA  
18191 C C   . SER C 772  ? 3.0893 1.7737 2.1986 -0.1229 -0.0993 -0.0516 772  SER B C   
18192 O O   . SER C 772  ? 3.1160 1.7947 2.1949 -0.1264 -0.1071 -0.0497 772  SER B O   
18193 C CB  . SER C 772  ? 3.0998 1.7641 2.2792 -0.1332 -0.0698 -0.0544 772  SER B CB  
18194 O OG  . SER C 772  ? 3.0886 1.7350 2.3069 -0.1356 -0.0642 -0.0562 772  SER B OG  
18195 N N   . TRP C 773  ? 2.8713 1.5761 1.9768 -0.1195 -0.0943 -0.0523 773  TRP B N   
18196 C CA  . TRP C 773  ? 2.9105 1.6329 1.9744 -0.1204 -0.0966 -0.0512 773  TRP B CA  
18197 C C   . TRP C 773  ? 2.9473 1.6896 2.0110 -0.1198 -0.0865 -0.0518 773  TRP B C   
18198 O O   . TRP C 773  ? 2.9644 1.7055 2.0604 -0.1196 -0.0764 -0.0528 773  TRP B O   
18199 C CB  . TRP C 773  ? 2.9137 1.6511 1.9601 -0.1015 -0.1277 -0.0524 773  TRP B CB  
18200 C CG  . TRP C 773  ? 2.8892 1.6414 1.9657 -0.0793 -0.1489 -0.0557 773  TRP B CG  
18201 C CD1 . TRP C 773  ? 2.8798 1.6209 1.9893 -0.0701 -0.1602 -0.0572 773  TRP B CD1 
18202 C CD2 . TRP C 773  ? 2.8942 1.6753 1.9706 -0.0639 -0.1614 -0.0580 773  TRP B CD2 
18203 N NE1 . TRP C 773  ? 2.8579 1.6197 1.9881 -0.0496 -0.1791 -0.0603 773  TRP B NE1 
18204 C CE2 . TRP C 773  ? 2.8667 1.6531 1.9768 -0.0457 -0.1802 -0.0608 773  TRP B CE2 
18205 C CE3 . TRP C 773  ? 2.8979 1.7012 1.9483 -0.0643 -0.1585 -0.0580 773  TRP B CE3 
18206 C CZ2 . TRP C 773  ? 2.8615 1.6749 1.9796 -0.0282 -0.1962 -0.0634 773  TRP B CZ2 
18207 C CZ3 . TRP C 773  ? 2.8875 1.7174 1.9459 -0.0469 -0.1744 -0.0607 773  TRP B CZ3 
18208 C CH2 . TRP C 773  ? 2.8715 1.7063 1.9633 -0.0293 -0.1930 -0.0633 773  TRP B CH2 
18209 N N   . LEU C 774  ? 3.6045 2.3648 2.6314 -0.1196 -0.0898 -0.0512 774  LEU B N   
18210 C CA  . LEU C 774  ? 3.6153 2.3927 2.6336 -0.1232 -0.0773 -0.0512 774  LEU B CA  
18211 C C   . LEU C 774  ? 3.5862 2.3472 2.6130 -0.1447 -0.0447 -0.0497 774  LEU B C   
18212 O O   . LEU C 774  ? 3.5355 2.3028 2.5806 -0.1453 -0.0337 -0.0502 774  LEU B O   
18213 C CB  . LEU C 774  ? 3.6241 2.4223 2.6670 -0.1042 -0.0920 -0.0533 774  LEU B CB  
18214 C CG  . LEU C 774  ? 3.6845 2.5126 2.7000 -0.0915 -0.1099 -0.0546 774  LEU B CG  
18215 C CD1 . LEU C 774  ? 3.6646 2.5119 2.7063 -0.0734 -0.1247 -0.0566 774  LEU B CD1 
18216 C CD2 . LEU C 774  ? 3.7242 2.5597 2.7064 -0.1063 -0.0914 -0.0530 774  LEU B CD2 
18217 N N   . TRP C 775  ? 2.8569 1.5970 1.8696 -0.1626 -0.0297 -0.0481 775  TRP B N   
18218 C CA  . TRP C 775  ? 2.8272 1.5487 1.8514 -0.1837 0.0009  -0.0476 775  TRP B CA  
18219 C C   . TRP C 775  ? 2.8634 1.5916 1.8561 -0.1991 0.0205  -0.0465 775  TRP B C   
18220 O O   . TRP C 775  ? 2.8573 1.5720 1.8554 -0.2179 0.0472  -0.0465 775  TRP B O   
18221 C CB  . TRP C 775  ? 2.8100 1.5057 1.8362 -0.1958 0.0069  -0.0467 775  TRP B CB  
18222 C CG  . TRP C 775  ? 2.8088 1.4850 1.8533 -0.2159 0.0361  -0.0474 775  TRP B CG  
18223 C CD1 . TRP C 775  ? 2.8633 1.5288 1.8851 -0.2384 0.0598  -0.0462 775  TRP B CD1 
18224 C CD2 . TRP C 775  ? 2.7813 1.4462 1.8714 -0.2161 0.0455  -0.0499 775  TRP B CD2 
18225 N NE1 . TRP C 775  ? 2.8521 1.5006 1.9024 -0.2531 0.0840  -0.0483 775  TRP B NE1 
18226 C CE2 . TRP C 775  ? 2.7946 1.4425 1.8875 -0.2395 0.0755  -0.0507 775  TRP B CE2 
18227 C CE3 . TRP C 775  ? 2.7470 1.4151 1.8761 -0.1989 0.0314  -0.0520 775  TRP B CE3 
18228 C CZ2 . TRP C 775  ? 2.7644 1.3987 1.8980 -0.2459 0.0917  -0.0538 775  TRP B CZ2 
18229 C CZ3 . TRP C 775  ? 2.7245 1.3787 1.8940 -0.2053 0.0475  -0.0547 775  TRP B CZ3 
18230 C CH2 . TRP C 775  ? 2.7357 1.3734 1.9073 -0.2284 0.0771  -0.0558 775  TRP B CH2 
18231 N N   . GLU C 776  ? 3.7898 2.5397 2.7504 -0.1911 0.0072  -0.0459 776  GLU B N   
18232 C CA  . GLU C 776  ? 3.8590 2.6188 2.7867 -0.2037 0.0229  -0.0450 776  GLU B CA  
18233 C C   . GLU C 776  ? 3.8441 2.6102 2.7901 -0.2076 0.0402  -0.0459 776  GLU B C   
18234 O O   . GLU C 776  ? 3.8038 2.5767 2.7810 -0.1940 0.0314  -0.0470 776  GLU B O   
18235 C CB  . GLU C 776  ? 3.9411 2.7253 2.8342 -0.1910 0.0011  -0.0451 776  GLU B CB  
18236 C CG  . GLU C 776  ? 3.9784 2.7833 2.8884 -0.1664 -0.0250 -0.0472 776  GLU B CG  
18237 C CD  . GLU C 776  ? 4.0746 2.9012 2.9522 -0.1534 -0.0492 -0.0483 776  GLU B CD  
18238 O OE1 . GLU C 776  ? 4.0824 2.9139 2.9694 -0.1360 -0.0742 -0.0500 776  GLU B OE1 
18239 O OE2 . GLU C 776  ? 4.1373 2.9763 2.9802 -0.1605 -0.0432 -0.0480 776  GLU B OE2 
18240 N N   . VAL C 777  ? 2.5790 1.3427 1.5059 -0.2263 0.0645  -0.0452 777  VAL B N   
18241 C CA  . VAL C 777  ? 2.5476 1.3190 1.4869 -0.2297 0.0797  -0.0459 777  VAL B CA  
18242 C C   . VAL C 777  ? 2.6663 1.4646 1.5745 -0.2229 0.0706  -0.0454 777  VAL B C   
18243 O O   . VAL C 777  ? 2.7222 1.5306 1.5956 -0.2205 0.0585  -0.0448 777  VAL B O   
18244 C CB  . VAL C 777  ? 2.5475 1.3003 1.4906 -0.2539 0.1129  -0.0463 777  VAL B CB  
18245 C CG1 . VAL C 777  ? 2.5407 1.3022 1.4919 -0.2576 0.1277  -0.0470 777  VAL B CG1 
18246 C CG2 . VAL C 777  ? 2.5010 1.2301 1.4809 -0.2587 0.1210  -0.0478 777  VAL B CG2 
18247 N N   . HIS C 778  ? 3.0302 1.8402 1.9509 -0.2194 0.0751  -0.0456 778  HIS B N   
18248 C CA  . HIS C 778  ? 3.1279 1.9635 2.0191 -0.2140 0.0672  -0.0452 778  HIS B CA  
18249 C C   . HIS C 778  ? 3.2777 2.1186 2.1701 -0.2232 0.0862  -0.0447 778  HIS B C   
18250 O O   . HIS C 778  ? 3.2519 2.0801 2.1767 -0.2283 0.1011  -0.0449 778  HIS B O   
18251 C CB  . HIS C 778  ? 3.0845 1.9411 1.9813 -0.1899 0.0363  -0.0460 778  HIS B CB  
18252 C CG  . HIS C 778  ? 3.0776 1.9409 1.9509 -0.1808 0.0147  -0.0468 778  HIS B CG  
18253 N ND1 . HIS C 778  ? 3.1003 1.9819 1.9318 -0.1808 0.0075  -0.0473 778  HIS B ND1 
18254 C CD2 . HIS C 778  ? 3.0547 1.9090 1.9408 -0.1711 -0.0017 -0.0474 778  HIS B CD2 
18255 C CE1 . HIS C 778  ? 3.1021 1.9854 1.9223 -0.1712 -0.0126 -0.0483 778  HIS B CE1 
18256 N NE2 . HIS C 778  ? 3.0742 1.9407 1.9267 -0.1653 -0.0186 -0.0482 778  HIS B NE2 
18257 N N   . LEU C 779  ? 3.1213 1.9816 1.9778 -0.2251 0.0851  -0.0444 779  LEU B N   
18258 C CA  . LEU C 779  ? 3.2568 2.1259 2.1093 -0.2319 0.0992  -0.0437 779  LEU B CA  
18259 C C   . LEU C 779  ? 3.3459 2.2392 2.2018 -0.2127 0.0763  -0.0435 779  LEU B C   
18260 O O   . LEU C 779  ? 3.3956 2.3087 2.2254 -0.2024 0.0566  -0.0443 779  LEU B O   
18261 C CB  . LEU C 779  ? 3.3176 2.1932 2.1258 -0.2473 0.1127  -0.0436 779  LEU B CB  
18262 C CG  . LEU C 779  ? 3.3329 2.2158 2.1325 -0.2576 0.1304  -0.0431 779  LEU B CG  
18263 C CD1 . LEU C 779  ? 3.3159 2.1775 2.1519 -0.2679 0.1527  -0.0431 779  LEU B CD1 
18264 C CD2 . LEU C 779  ? 3.3850 2.2733 2.1404 -0.2735 0.1439  -0.0433 779  LEU B CD2 
18265 N N   . VAL C 780  ? 3.6108 2.5030 2.4987 -0.2080 0.0784  -0.0426 780  VAL B N   
18266 C CA  . VAL C 780  ? 3.6818 2.5967 2.5745 -0.1905 0.0571  -0.0421 780  VAL B CA  
18267 C C   . VAL C 780  ? 3.6555 2.5766 2.5515 -0.1960 0.0690  -0.0401 780  VAL B C   
18268 O O   . VAL C 780  ? 3.6123 2.5187 2.5418 -0.1994 0.0810  -0.0391 780  VAL B O   
18269 C CB  . VAL C 780  ? 3.7298 2.6412 2.6616 -0.1730 0.0382  -0.0424 780  VAL B CB  
18270 C CG1 . VAL C 780  ? 3.7901 2.7250 2.7272 -0.1564 0.0177  -0.0417 780  VAL B CG1 
18271 C CG2 . VAL C 780  ? 3.7797 2.6875 2.7062 -0.1655 0.0228  -0.0443 780  VAL B CG2 
18272 N N   . PRO C 781  ? 3.6720 2.6150 2.5330 -0.1972 0.0658  -0.0398 781  PRO B N   
18273 C CA  . PRO C 781  ? 3.6722 2.6245 2.5311 -0.2013 0.0736  -0.0377 781  PRO B CA  
18274 C C   . PRO C 781  ? 3.6534 2.6223 2.5307 -0.1831 0.0512  -0.0364 781  PRO B C   
18275 O O   . PRO C 781  ? 3.6890 2.6824 2.5418 -0.1775 0.0388  -0.0363 781  PRO B O   
18276 C CB  . PRO C 781  ? 3.7403 2.7109 2.5504 -0.2092 0.0763  -0.0386 781  PRO B CB  
18277 C CG  . PRO C 781  ? 3.7681 2.7327 2.5577 -0.2132 0.0762  -0.0408 781  PRO B CG  
18278 C CD  . PRO C 781  ? 3.7295 2.6869 2.5478 -0.1983 0.0583  -0.0416 781  PRO B CD  
18279 N N   . ARG C 782  ? 3.9021 2.8581 2.8218 -0.1745 0.0463  -0.0357 782  ARG B N   
18280 C CA  . ARG C 782  ? 3.8959 2.8653 2.8373 -0.1575 0.0255  -0.0342 782  ARG B CA  
18281 C C   . ARG C 782  ? 3.8477 2.8337 2.7859 -0.1390 -0.0033 -0.0366 782  ARG B C   
18282 O O   . ARG C 782  ? 3.8393 2.8295 2.8054 -0.1242 -0.0203 -0.0361 782  ARG B O   
18283 C CB  . ARG C 782  ? 3.9880 2.9754 2.9122 -0.1598 0.0258  -0.0317 782  ARG B CB  
18284 C CG  . ARG C 782  ? 4.0717 3.0433 3.0018 -0.1768 0.0526  -0.0293 782  ARG B CG  
18285 C CD  . ARG C 782  ? 4.1723 3.1616 3.0867 -0.1778 0.0505  -0.0263 782  ARG B CD  
18286 N NE  . ARG C 782  ? 4.2724 3.2832 3.1393 -0.1821 0.0477  -0.0277 782  ARG B NE  
18287 C CZ  . ARG C 782  ? 4.3420 3.3720 3.1862 -0.1838 0.0447  -0.0259 782  ARG B CZ  
18288 N NH1 . ARG C 782  ? 4.3503 3.3800 3.2144 -0.1817 0.0436  -0.0219 782  ARG B NH1 
18289 N NH2 . ARG C 782  ? 4.3910 3.4406 3.1925 -0.1878 0.0425  -0.0280 782  ARG B NH2 
18290 N N   . ARG C 783  ? 3.8225 2.8181 2.7270 -0.1396 -0.0090 -0.0393 783  ARG B N   
18291 C CA  . ARG C 783  ? 3.7812 2.7917 2.6814 -0.1224 -0.0359 -0.0424 783  ARG B CA  
18292 C C   . ARG C 783  ? 3.7349 2.7402 2.6100 -0.1272 -0.0349 -0.0451 783  ARG B C   
18293 O O   . ARG C 783  ? 3.7550 2.7589 2.5997 -0.1418 -0.0191 -0.0451 783  ARG B O   
18294 C CB  . ARG C 783  ? 3.8245 2.8678 2.7033 -0.1115 -0.0557 -0.0434 783  ARG B CB  
18295 C CG  . ARG C 783  ? 3.8250 2.8770 2.7292 -0.1026 -0.0646 -0.0408 783  ARG B CG  
18296 C CD  . ARG C 783  ? 3.8729 2.9559 2.7479 -0.0990 -0.0760 -0.0412 783  ARG B CD  
18297 N NE  . ARG C 783  ? 3.8877 2.9724 2.7763 -0.1018 -0.0705 -0.0368 783  ARG B NE  
18298 C CZ  . ARG C 783  ? 3.9212 3.0196 2.7838 -0.1105 -0.0633 -0.0351 783  ARG B CZ  
18299 N NH1 . ARG C 783  ? 3.9557 3.0683 2.7773 -0.1172 -0.0605 -0.0379 783  ARG B NH1 
18300 N NH2 . ARG C 783  ? 3.9111 3.0088 2.7886 -0.1126 -0.0592 -0.0305 783  ARG B NH2 
18301 N N   . LYS C 784  ? 3.1306 2.1322 2.0190 -0.1150 -0.0520 -0.0473 784  LYS B N   
18302 C CA  . LYS C 784  ? 3.0969 2.0969 1.9612 -0.1156 -0.0578 -0.0499 784  LYS B CA  
18303 C C   . LYS C 784  ? 3.0544 2.0569 1.9375 -0.0969 -0.0833 -0.0525 784  LYS B C   
18304 O O   . LYS C 784  ? 3.0319 2.0170 1.9509 -0.0929 -0.0836 -0.0517 784  LYS B O   
18305 C CB  . LYS C 784  ? 3.0782 2.0504 1.9394 -0.1343 -0.0330 -0.0485 784  LYS B CB  
18306 C CG  . LYS C 784  ? 3.0879 2.0592 1.9160 -0.1385 -0.0362 -0.0503 784  LYS B CG  
18307 C CD  . LYS C 784  ? 3.0655 2.0120 1.8847 -0.1603 -0.0088 -0.0485 784  LYS B CD  
18308 C CE  . LYS C 784  ? 3.0708 2.0170 1.8547 -0.1648 -0.0128 -0.0497 784  LYS B CE  
18309 N NZ  . LYS C 784  ? 3.0573 1.9816 1.8286 -0.1868 0.0134  -0.0479 784  LYS B NZ  
18310 N N   . GLN C 785  ? 3.5241 2.5494 2.3834 -0.0853 -0.1049 -0.0561 785  GLN B N   
18311 C CA  . GLN C 785  ? 3.4827 2.5123 2.3558 -0.0675 -0.1301 -0.0593 785  GLN B CA  
18312 C C   . GLN C 785  ? 3.4635 2.4836 2.3151 -0.0709 -0.1324 -0.0610 785  GLN B C   
18313 O O   . GLN C 785  ? 3.4780 2.5040 2.2939 -0.0806 -0.1250 -0.0615 785  GLN B O   
18314 C CB  . GLN C 785  ? 3.5147 2.5780 2.3777 -0.0512 -0.1544 -0.0630 785  GLN B CB  
18315 C CG  . GLN C 785  ? 3.5450 2.6164 2.4222 -0.0315 -0.1822 -0.0672 785  GLN B CG  
18316 C CD  . GLN C 785  ? 3.5989 2.7042 2.4702 -0.0163 -0.2043 -0.0711 785  GLN B CD  
18317 O OE1 . GLN C 785  ? 3.6401 2.7664 2.4828 -0.0202 -0.2025 -0.0721 785  GLN B OE1 
18318 N NE2 . GLN C 785  ? 3.5970 2.7082 2.4950 0.0007  -0.2250 -0.0736 785  GLN B NE2 
18319 N N   . LEU C 786  ? 3.2282 2.2332 2.1013 -0.0632 -0.1427 -0.0618 786  LEU B N   
18320 C CA  . LEU C 786  ? 3.2499 2.2448 2.1041 -0.0653 -0.1476 -0.0631 786  LEU B CA  
18321 C C   . LEU C 786  ? 3.2705 2.2661 2.1429 -0.0470 -0.1735 -0.0663 786  LEU B C   
18322 O O   . LEU C 786  ? 3.2687 2.2446 2.1738 -0.0448 -0.1729 -0.0650 786  LEU B O   
18323 C CB  . LEU C 786  ? 3.2072 2.1705 2.0630 -0.0850 -0.1222 -0.0592 786  LEU B CB  
18324 C CG  . LEU C 786  ? 3.1289 2.0664 2.0248 -0.0905 -0.1078 -0.0565 786  LEU B CG  
18325 C CD1 . LEU C 786  ? 3.1083 2.0181 1.9980 -0.1107 -0.0844 -0.0538 786  LEU B CD1 
18326 C CD2 . LEU C 786  ? 3.0966 2.0408 2.0100 -0.0926 -0.0965 -0.0549 786  LEU B CD2 
18327 N N   . GLN C 787  ? 3.5525 2.5715 2.4041 -0.0338 -0.1963 -0.0709 787  GLN B N   
18328 C CA  . GLN C 787  ? 3.5480 2.5700 2.4149 -0.0156 -0.2225 -0.0748 787  GLN B CA  
18329 C C   . GLN C 787  ? 3.5038 2.5002 2.3680 -0.0203 -0.2224 -0.0737 787  GLN B C   
18330 O O   . GLN C 787  ? 3.5045 2.4868 2.3457 -0.0366 -0.2056 -0.0708 787  GLN B O   
18331 C CB  . GLN C 787  ? 3.6315 2.6876 2.4784 0.0002  -0.2473 -0.0811 787  GLN B CB  
18332 C CG  . GLN C 787  ? 3.7317 2.8028 2.5347 -0.0078 -0.2428 -0.0825 787  GLN B CG  
18333 C CD  . GLN C 787  ? 3.8205 2.9288 2.6070 0.0069  -0.2646 -0.0892 787  GLN B CD  
18334 O OE1 . GLN C 787  ? 3.8805 3.0036 2.6334 0.0061  -0.2698 -0.0926 787  GLN B OE1 
18335 N NE2 . GLN C 787  ? 3.8233 2.9474 2.6336 0.0201  -0.2773 -0.0913 787  GLN B NE2 
18336 N N   . PHE C 788  ? 3.5165 2.5067 2.4044 -0.0064 -0.2413 -0.0758 788  PHE B N   
18337 C CA  . PHE C 788  ? 3.4680 2.4338 2.3571 -0.0085 -0.2450 -0.0749 788  PHE B CA  
18338 C C   . PHE C 788  ? 3.4166 2.3813 2.3380 0.0096  -0.2671 -0.0779 788  PHE B C   
18339 O O   . PHE C 788  ? 3.4193 2.3922 2.3692 0.0181  -0.2707 -0.0787 788  PHE B O   
18340 C CB  . PHE C 788  ? 3.4153 2.3491 2.3133 -0.0289 -0.2173 -0.0690 788  PHE B CB  
18341 C CG  . PHE C 788  ? 3.3379 2.2617 2.2751 -0.0304 -0.2054 -0.0670 788  PHE B CG  
18342 C CD1 . PHE C 788  ? 3.3028 2.2073 2.2740 -0.0257 -0.2100 -0.0666 788  PHE B CD1 
18343 C CD2 . PHE C 788  ? 3.2945 2.2284 2.2348 -0.0365 -0.1900 -0.0655 788  PHE B CD2 
18344 C CE1 . PHE C 788  ? 3.2409 2.1369 2.2486 -0.0268 -0.1994 -0.0652 788  PHE B CE1 
18345 C CE2 . PHE C 788  ? 3.2369 2.1615 2.2138 -0.0375 -0.1798 -0.0637 788  PHE B CE2 
18346 C CZ  . PHE C 788  ? 3.2106 2.1166 2.2214 -0.0325 -0.1845 -0.0637 788  PHE B CZ  
18347 N N   . ALA C 789  ? 3.5857 2.5402 2.5029 0.0156  -0.2825 -0.0795 789  ALA B N   
18348 C CA  . ALA C 789  ? 3.5086 2.4606 2.4568 0.0322  -0.3031 -0.0825 789  ALA B CA  
18349 C C   . ALA C 789  ? 3.4481 2.3668 2.4253 0.0229  -0.2894 -0.0781 789  ALA B C   
18350 O O   . ALA C 789  ? 3.4442 2.3404 2.4110 0.0044  -0.2685 -0.0734 789  ALA B O   
18351 C CB  . ALA C 789  ? 3.5485 2.5077 2.4804 0.0452  -0.3290 -0.0872 789  ALA B CB  
18352 N N   . LEU C 790  ? 2.9796 1.8962 1.9932 0.0353  -0.3008 -0.0798 790  LEU B N   
18353 C CA  . LEU C 790  ? 2.9571 1.8442 2.0013 0.0277  -0.2890 -0.0765 790  LEU B CA  
18354 C C   . LEU C 790  ? 3.0013 1.8710 2.0461 0.0324  -0.3043 -0.0774 790  LEU B C   
18355 O O   . LEU C 790  ? 2.9910 1.8750 2.0295 0.0487  -0.3299 -0.0820 790  LEU B O   
18356 C CB  . LEU C 790  ? 2.8818 1.7748 1.9665 0.0375  -0.2916 -0.0777 790  LEU B CB  
18357 C CG  . LEU C 790  ? 2.8392 1.7591 1.9225 0.0415  -0.2893 -0.0785 790  LEU B CG  
18358 C CD1 . LEU C 790  ? 2.8431 1.7930 1.9278 0.0634  -0.3179 -0.0845 790  LEU B CD1 
18359 C CD2 . LEU C 790  ? 2.7734 1.6838 1.8911 0.0362  -0.2726 -0.0757 790  LEU B CD2 
18360 N N   . PRO C 791  ? 3.0077 1.8463 2.0609 0.0179  -0.2888 -0.0732 791  PRO B N   
18361 C CA  . PRO C 791  ? 3.1102 1.9287 2.1553 0.0170  -0.2992 -0.0725 791  PRO B CA  
18362 C C   . PRO C 791  ? 3.2083 2.0305 2.2797 0.0370  -0.3248 -0.0769 791  PRO B C   
18363 O O   . PRO C 791  ? 3.2273 2.0539 2.3326 0.0443  -0.3253 -0.0783 791  PRO B O   
18364 C CB  . PRO C 791  ? 3.0750 1.8610 2.1339 -0.0027 -0.2746 -0.0675 791  PRO B CB  
18365 C CG  . PRO C 791  ? 3.0241 1.8146 2.0964 -0.0123 -0.2509 -0.0659 791  PRO B CG  
18366 C CD  . PRO C 791  ? 2.9851 1.8064 2.0659 0.0051  -0.2647 -0.0699 791  PRO B CD  
18367 N N   . ASP C 792  ? 3.4267 2.2475 2.4835 0.0459  -0.3463 -0.0791 792  ASP B N   
18368 C CA  . ASP C 792  ? 3.5057 2.3245 2.5890 0.0628  -0.3692 -0.0829 792  ASP B CA  
18369 C C   . ASP C 792  ? 3.4278 2.2155 2.5393 0.0513  -0.3541 -0.0789 792  ASP B C   
18370 O O   . ASP C 792  ? 3.4265 2.1891 2.5250 0.0337  -0.3388 -0.0740 792  ASP B O   
18371 C CB  . ASP C 792  ? 3.7226 2.5408 2.7838 0.0720  -0.3931 -0.0855 792  ASP B CB  
18372 C CG  . ASP C 792  ? 3.9504 2.7781 3.0357 0.0945  -0.4217 -0.0918 792  ASP B CG  
18373 O OD1 . ASP C 792  ? 4.0265 2.8532 3.1479 0.1003  -0.4215 -0.0929 792  ASP B OD1 
18374 O OD2 . ASP C 792  ? 4.0959 2.9323 3.1644 0.1064  -0.4447 -0.0959 792  ASP B OD2 
18375 N N   . SER C 793  ? 3.4356 2.2263 2.5857 0.0608  -0.3577 -0.0812 793  SER B N   
18376 C CA  . SER C 793  ? 3.3462 2.1105 2.5283 0.0526  -0.3458 -0.0788 793  SER B CA  
18377 C C   . SER C 793  ? 3.2260 2.0016 2.4491 0.0642  -0.3487 -0.0818 793  SER B C   
18378 O O   . SER C 793  ? 3.2043 2.0027 2.4303 0.0692  -0.3461 -0.0831 793  SER B O   
18379 C CB  . SER C 793  ? 3.3304 2.0733 2.5040 0.0276  -0.3141 -0.0730 793  SER B CB  
18380 O OG  . SER C 793  ? 3.2867 2.0062 2.4930 0.0199  -0.3024 -0.0716 793  SER B OG  
18381 N N   . LEU C 794  ? 3.5007 2.2600 2.7551 0.0681  -0.3543 -0.0827 794  LEU B N   
18382 C CA  . LEU C 794  ? 3.3919 2.1596 2.6867 0.0780  -0.3563 -0.0853 794  LEU B CA  
18383 C C   . LEU C 794  ? 3.3565 2.1096 2.6711 0.0614  -0.3274 -0.0817 794  LEU B C   
18384 O O   . LEU C 794  ? 3.3929 2.1197 2.7220 0.0498  -0.3155 -0.0798 794  LEU B O   
18385 C CB  . LEU C 794  ? 3.3731 2.1313 2.6947 0.0903  -0.3756 -0.0885 794  LEU B CB  
18386 C CG  . LEU C 794  ? 3.3946 2.1773 2.7152 0.1136  -0.4068 -0.0944 794  LEU B CG  
18387 C CD1 . LEU C 794  ? 3.4364 2.2227 2.7167 0.1151  -0.4194 -0.0949 794  LEU B CD1 
18388 C CD2 . LEU C 794  ? 3.3989 2.1728 2.7536 0.1254  -0.4229 -0.0978 794  LEU B CD2 
18389 N N   . THR C 795  ? 3.2893 2.0596 2.6052 0.0603  -0.3164 -0.0812 795  THR B N   
18390 C CA  . THR C 795  ? 3.2123 1.9704 2.5479 0.0454  -0.2893 -0.0785 795  THR B CA  
18391 C C   . THR C 795  ? 3.1550 1.9363 2.5004 0.0513  -0.2857 -0.0790 795  THR B C   
18392 O O   . THR C 795  ? 3.1127 1.9203 2.4465 0.0656  -0.3032 -0.0812 795  THR B O   
18393 C CB  . THR C 795  ? 3.9433 2.6830 3.2518 0.0220  -0.2641 -0.0741 795  THR B CB  
18394 O OG1 . THR C 795  ? 3.9721 2.7238 3.2378 0.0220  -0.2710 -0.0733 795  THR B OG1 
18395 C CG2 . THR C 795  ? 3.9536 2.6624 3.2688 0.0100  -0.2570 -0.0727 795  THR B CG2 
18396 N N   . THR C 796  ? 3.2171 1.9884 2.5848 0.0400  -0.2632 -0.0771 796  THR B N   
18397 C CA  . THR C 796  ? 3.1911 1.9802 2.5640 0.0410  -0.2549 -0.0763 796  THR B CA  
18398 C C   . THR C 796  ? 3.2383 2.0161 2.5927 0.0195  -0.2262 -0.0727 796  THR B C   
18399 O O   . THR C 796  ? 3.2526 2.0088 2.6252 0.0053  -0.2052 -0.0716 796  THR B O   
18400 C CB  . THR C 796  ? 3.1298 1.9194 2.5489 0.0484  -0.2548 -0.0777 796  THR B CB  
18401 O OG1 . THR C 796  ? 3.1345 1.9355 2.5701 0.0684  -0.2820 -0.0813 796  THR B OG1 
18402 C CG2 . THR C 796  ? 3.0881 1.8950 2.5107 0.0489  -0.2467 -0.0762 796  THR B CG2 
18403 N N   . TRP C 797  ? 3.0013 1.7942 2.3190 0.0170  -0.2254 -0.0713 797  TRP B N   
18404 C CA  . TRP C 797  ? 2.9798 1.7649 2.2750 -0.0029 -0.1995 -0.0681 797  TRP B CA  
18405 C C   . TRP C 797  ? 2.8926 1.6830 2.2077 -0.0073 -0.1828 -0.0670 797  TRP B C   
18406 O O   . TRP C 797  ? 2.8750 1.6879 2.1938 0.0050  -0.1939 -0.0676 797  TRP B O   
18407 C CB  . TRP C 797  ? 3.0465 1.8477 2.2954 -0.0030 -0.2059 -0.0675 797  TRP B CB  
18408 C CG  . TRP C 797  ? 3.1405 1.9340 2.3655 -0.0020 -0.2190 -0.0680 797  TRP B CG  
18409 C CD1 . TRP C 797  ? 3.1961 2.0077 2.3971 0.0116  -0.2428 -0.0703 797  TRP B CD1 
18410 C CD2 . TRP C 797  ? 3.1925 1.9581 2.4157 -0.0152 -0.2092 -0.0664 797  TRP B CD2 
18411 N NE1 . TRP C 797  ? 3.2556 2.0511 2.4404 0.0080  -0.2488 -0.0698 797  TRP B NE1 
18412 C CE2 . TRP C 797  ? 3.2575 2.0244 2.4549 -0.0088 -0.2285 -0.0671 797  TRP B CE2 
18413 C CE3 . TRP C 797  ? 3.1983 1.9381 2.4394 -0.0323 -0.1861 -0.0646 797  TRP B CE3 
18414 C CZ2 . TRP C 797  ? 3.2914 2.0338 2.4796 -0.0190 -0.2257 -0.0653 797  TRP B CZ2 
18415 C CZ3 . TRP C 797  ? 3.2367 1.9533 2.4684 -0.0428 -0.1829 -0.0632 797  TRP B CZ3 
18416 C CH2 . TRP C 797  ? 3.2806 1.9981 2.4857 -0.0363 -0.2027 -0.0632 797  TRP B CH2 
18417 N N   . GLU C 798  ? 2.8576 1.6274 2.1855 -0.0248 -0.1567 -0.0656 798  GLU B N   
18418 C CA  . GLU C 798  ? 2.8210 1.5944 2.1644 -0.0308 -0.1390 -0.0645 798  GLU B CA  
18419 C C   . GLU C 798  ? 2.8227 1.5938 2.1335 -0.0488 -0.1172 -0.0621 798  GLU B C   
18420 O O   . GLU C 798  ? 2.8196 1.5701 2.1315 -0.0669 -0.0944 -0.0616 798  GLU B O   
18421 C CB  . GLU C 798  ? 2.8037 1.5577 2.1906 -0.0366 -0.1246 -0.0657 798  GLU B CB  
18422 C CG  . GLU C 798  ? 2.7994 1.5554 2.2025 -0.0434 -0.1059 -0.0648 798  GLU B CG  
18423 C CD  . GLU C 798  ? 2.8121 1.5514 2.2617 -0.0468 -0.0939 -0.0669 798  GLU B CD  
18424 O OE1 . GLU C 798  ? 2.8291 1.5558 2.2984 -0.0439 -0.1002 -0.0691 798  GLU B OE1 
18425 O OE2 . GLU C 798  ? 2.8125 1.5513 2.2793 -0.0525 -0.0782 -0.0665 798  GLU B OE2 
18426 N N   . ILE C 799  ? 2.3942 1.1873 1.6765 -0.0442 -0.1240 -0.0610 799  ILE B N   
18427 C CA  . ILE C 799  ? 2.4365 1.2300 1.6845 -0.0603 -0.1054 -0.0588 799  ILE B CA  
18428 C C   . ILE C 799  ? 2.4393 1.2324 1.7024 -0.0693 -0.0843 -0.0576 799  ILE B C   
18429 O O   . ILE C 799  ? 2.4448 1.2572 1.7064 -0.0614 -0.0905 -0.0567 799  ILE B O   
18430 C CB  . ILE C 799  ? 2.3791 1.1951 1.5854 -0.0526 -0.1224 -0.0587 799  ILE B CB  
18431 C CG1 . ILE C 799  ? 2.3694 1.2071 1.5599 -0.0520 -0.1192 -0.0575 799  ILE B CG1 
18432 C CG2 . ILE C 799  ? 2.3705 1.1992 1.5843 -0.0314 -0.1528 -0.0612 799  ILE B CG2 
18433 C CD1 . ILE C 799  ? 2.3648 1.2275 1.5200 -0.0409 -0.1403 -0.0586 799  ILE B CD1 
18434 N N   . GLN C 800  ? 2.7020 1.4724 1.9812 -0.0859 -0.0598 -0.0577 800  GLN B N   
18435 C CA  . GLN C 800  ? 2.7091 1.4755 2.0035 -0.0967 -0.0371 -0.0571 800  GLN B CA  
18436 C C   . GLN C 800  ? 2.7335 1.4992 1.9911 -0.1145 -0.0172 -0.0554 800  GLN B C   
18437 O O   . GLN C 800  ? 2.7575 1.5143 1.9883 -0.1252 -0.0114 -0.0552 800  GLN B O   
18438 C CB  . GLN C 800  ? 2.7180 1.4612 2.0528 -0.1053 -0.0204 -0.0593 800  GLN B CB  
18439 C CG  . GLN C 800  ? 2.7591 1.4798 2.0826 -0.1268 0.0025  -0.0601 800  GLN B CG  
18440 C CD  . GLN C 800  ? 2.7707 1.4748 2.1089 -0.1260 -0.0040 -0.0619 800  GLN B CD  
18441 O OE1 . GLN C 800  ? 2.7773 1.4879 2.1280 -0.1088 -0.0276 -0.0625 800  GLN B OE1 
18442 N NE2 . GLN C 800  ? 2.7711 1.4540 2.1077 -0.1451 0.0169  -0.0630 800  GLN B NE2 
18443 N N   . GLY C 801  ? 2.3893 1.1642 1.6456 -0.1179 -0.0068 -0.0542 801  GLY B N   
18444 C CA  . GLY C 801  ? 2.3969 1.1749 1.6164 -0.1328 0.0096  -0.0527 801  GLY B CA  
18445 C C   . GLY C 801  ? 2.3980 1.1684 1.6333 -0.1457 0.0346  -0.0526 801  GLY B C   
18446 O O   . GLY C 801  ? 2.3870 1.1670 1.6412 -0.1376 0.0309  -0.0517 801  GLY B O   
18447 N N   . ILE C 802  ? 2.8663 1.6189 2.0944 -0.1660 0.0597  -0.0536 802  ILE B N   
18448 C CA  . ILE C 802  ? 2.8710 1.6150 2.1093 -0.1814 0.0865  -0.0543 802  ILE B CA  
18449 C C   . ILE C 802  ? 2.8970 1.6507 2.0921 -0.1928 0.0974  -0.0524 802  ILE B C   
18450 O O   . ILE C 802  ? 2.9659 1.7226 2.1245 -0.1976 0.0946  -0.0516 802  ILE B O   
18451 C CB  . ILE C 802  ? 2.9025 1.6207 2.1653 -0.1974 0.1093  -0.0578 802  ILE B CB  
18452 C CG1 . ILE C 802  ? 2.9129 1.6224 2.1656 -0.2190 0.1394  -0.0590 802  ILE B CG1 
18453 C CG2 . ILE C 802  ? 2.9155 1.6231 2.1642 -0.2013 0.1045  -0.0584 802  ILE B CG2 
18454 C CD1 . ILE C 802  ? 2.9045 1.6159 2.1834 -0.2188 0.1498  -0.0596 802  ILE B CD1 
18455 N N   . GLY C 803  ? 3.0996 1.8586 2.2990 -0.1969 0.1090  -0.0517 803  GLY B N   
18456 C CA  . GLY C 803  ? 3.0952 1.8629 2.2562 -0.2085 0.1210  -0.0502 803  GLY B CA  
18457 C C   . GLY C 803  ? 3.1418 1.8973 2.3173 -0.2248 0.1493  -0.0516 803  GLY B C   
18458 O O   . GLY C 803  ? 3.0941 1.8420 2.3096 -0.2216 0.1537  -0.0529 803  GLY B O   
18459 N N   . ILE C 804  ? 2.6466 1.4004 1.7906 -0.2423 0.1684  -0.0517 804  ILE B N   
18460 C CA  . ILE C 804  ? 2.6526 1.3943 1.8095 -0.2591 0.1964  -0.0539 804  ILE B CA  
18461 C C   . ILE C 804  ? 2.6947 1.4459 1.8119 -0.2711 0.2088  -0.0524 804  ILE B C   
18462 O O   . ILE C 804  ? 2.6625 1.4225 1.7394 -0.2741 0.2038  -0.0510 804  ILE B O   
18463 C CB  . ILE C 804  ? 2.5810 1.2998 1.7540 -0.2746 0.2166  -0.0580 804  ILE B CB  
18464 C CG1 . ILE C 804  ? 2.5991 1.3161 1.7392 -0.2796 0.2118  -0.0574 804  ILE B CG1 
18465 C CG2 . ILE C 804  ? 2.5442 1.2519 1.7664 -0.2651 0.2109  -0.0604 804  ILE B CG2 
18466 C CD1 . ILE C 804  ? 2.5880 1.2837 1.7481 -0.2893 0.2226  -0.0608 804  ILE B CD1 
18467 N N   . SER C 805  ? 3.2565 2.0057 2.3867 -0.2778 0.2244  -0.0529 805  SER B N   
18468 C CA  . SER C 805  ? 3.3701 2.1274 2.4678 -0.2897 0.2380  -0.0518 805  SER B CA  
18469 C C   . SER C 805  ? 3.3905 2.1354 2.5142 -0.3013 0.2618  -0.0542 805  SER B C   
18470 O O   . SER C 805  ? 3.3997 2.1272 2.5607 -0.3056 0.2735  -0.0580 805  SER B O   
18471 C CB  . SER C 805  ? 3.3482 2.1294 2.4235 -0.2759 0.2172  -0.0475 805  SER B CB  
18472 O OG  . SER C 805  ? 3.3740 2.1689 2.4109 -0.2715 0.2021  -0.0460 805  SER B OG  
18473 N N   . ASN C 806  ? 3.6963 2.4510 2.8006 -0.3061 0.2683  -0.0523 806  ASN B N   
18474 C CA  . ASN C 806  ? 3.7991 2.5423 2.9212 -0.3194 0.2926  -0.0548 806  ASN B CA  
18475 C C   . ASN C 806  ? 3.8141 2.5507 2.9849 -0.3089 0.2885  -0.0550 806  ASN B C   
18476 O O   . ASN C 806  ? 3.8200 2.5448 3.0136 -0.3186 0.3079  -0.0578 806  ASN B O   
18477 C CB  . ASN C 806  ? 3.8949 2.6502 2.9792 -0.3284 0.3007  -0.0526 806  ASN B CB  
18478 C CG  . ASN C 806  ? 3.9944 2.7539 3.0332 -0.3413 0.3085  -0.0533 806  ASN B CG  
18479 O OD1 . ASN C 806  ? 4.0333 2.8106 3.0364 -0.3346 0.2923  -0.0500 806  ASN B OD1 
18480 N ND2 . ASN C 806  ? 4.0372 2.7805 3.0778 -0.3599 0.3331  -0.0577 806  ASN B ND2 
18481 N N   . THR C 807  ? 3.9385 2.6826 3.1261 -0.2890 0.2630  -0.0523 807  THR B N   
18482 C CA  . THR C 807  ? 3.9112 2.6481 3.1470 -0.2785 0.2578  -0.0527 807  THR B CA  
18483 C C   . THR C 807  ? 3.8327 2.5505 3.1067 -0.2811 0.2663  -0.0581 807  THR B C   
18484 O O   . THR C 807  ? 3.8609 2.5660 3.1756 -0.2822 0.2763  -0.0611 807  THR B O   
18485 C CB  . THR C 807  ? 3.9259 2.6802 3.1654 -0.2562 0.2271  -0.0474 807  THR B CB  
18486 O OG1 . THR C 807  ? 3.9347 2.6998 3.1525 -0.2466 0.2076  -0.0463 807  THR B OG1 
18487 C CG2 . THR C 807  ? 3.9450 2.7148 3.1592 -0.2555 0.2233  -0.0427 807  THR B CG2 
18488 N N   . GLY C 808  ? 3.2450 1.9605 2.5053 -0.2827 0.2628  -0.0595 808  GLY B N   
18489 C CA  . GLY C 808  ? 3.1495 1.8481 2.4428 -0.2850 0.2689  -0.0644 808  GLY B CA  
18490 C C   . GLY C 808  ? 3.1099 1.8128 2.3948 -0.2737 0.2476  -0.0630 808  GLY B C   
18491 O O   . GLY C 808  ? 3.0945 1.8080 2.3385 -0.2738 0.2390  -0.0602 808  GLY B O   
18492 N N   . ILE C 809  ? 2.6066 1.3016 1.9304 -0.2637 0.2388  -0.0650 809  ILE B N   
18493 C CA  . ILE C 809  ? 2.5593 1.2566 1.8801 -0.2526 0.2185  -0.0641 809  ILE B CA  
18494 C C   . ILE C 809  ? 2.5405 1.2481 1.8868 -0.2295 0.1921  -0.0615 809  ILE B C   
18495 O O   . ILE C 809  ? 2.5601 1.2610 1.9474 -0.2253 0.1952  -0.0633 809  ILE B O   
18496 C CB  . ILE C 809  ? 2.5203 1.1973 1.8644 -0.2629 0.2322  -0.0695 809  ILE B CB  
18497 C CG1 . ILE C 809  ? 2.5546 1.2323 1.8985 -0.2512 0.2108  -0.0686 809  ILE B CG1 
18498 C CG2 . ILE C 809  ? 2.5615 1.2257 1.9572 -0.2641 0.2446  -0.0743 809  ILE B CG2 
18499 C CD1 . ILE C 809  ? 2.5348 1.1944 1.9178 -0.2544 0.2179  -0.0737 809  ILE B CD1 
18500 N N   . CYS C 810  ? 3.5770 2.3013 2.9004 -0.2147 0.1665  -0.0576 810  CYS B N   
18501 C CA  . CYS C 810  ? 3.5298 2.2660 2.8754 -0.1925 0.1402  -0.0551 810  CYS B CA  
18502 C C   . CYS C 810  ? 3.5272 2.2717 2.8638 -0.1780 0.1147  -0.0542 810  CYS B C   
18503 O O   . CYS C 810  ? 3.5244 2.2812 2.8213 -0.1764 0.1046  -0.0522 810  CYS B O   
18504 C CB  . CYS C 810  ? 3.5041 2.2583 2.8362 -0.1854 0.1315  -0.0507 810  CYS B CB  
18505 S SG  . CYS C 810  ? 3.8788 2.6476 3.2402 -0.1602 0.1016  -0.0476 810  CYS B SG  
18506 N N   . VAL C 811  ? 3.0577 1.7958 2.4319 -0.1670 0.1040  -0.0560 811  VAL B N   
18507 C CA  . VAL C 811  ? 3.0472 1.7913 2.4182 -0.1529 0.0801  -0.0558 811  VAL B CA  
18508 C C   . VAL C 811  ? 3.0421 1.8086 2.4102 -0.1324 0.0525  -0.0525 811  VAL B C   
18509 O O   . VAL C 811  ? 3.0372 1.8070 2.4358 -0.1230 0.0465  -0.0516 811  VAL B O   
18510 C CB  . VAL C 811  ? 3.0406 1.7688 2.4546 -0.1494 0.0795  -0.0595 811  VAL B CB  
18511 C CG1 . VAL C 811  ? 3.0490 1.7829 2.4585 -0.1351 0.0546  -0.0592 811  VAL B CG1 
18512 C CG2 . VAL C 811  ? 3.0335 1.7397 2.4543 -0.1698 0.1068  -0.0635 811  VAL B CG2 
18513 N N   . ALA C 812  ? 3.6267 2.4086 2.9591 -0.1254 0.0352  -0.0508 812  ALA B N   
18514 C CA  . ALA C 812  ? 3.6031 2.4074 2.9329 -0.1057 0.0077  -0.0486 812  ALA B CA  
18515 C C   . ALA C 812  ? 3.5729 2.3747 2.9376 -0.0903 -0.0105 -0.0504 812  ALA B C   
18516 O O   . ALA C 812  ? 3.5658 2.3502 2.9467 -0.0945 -0.0048 -0.0532 812  ALA B O   
18517 C CB  . ALA C 812  ? 3.6483 2.4706 2.9310 -0.1026 -0.0055 -0.0475 812  ALA B CB  
18518 N N   . ASP C 813  ? 3.0618 1.8808 2.4380 -0.0729 -0.0321 -0.0488 813  ASP B N   
18519 C CA  . ASP C 813  ? 3.0252 1.8457 2.4291 -0.0567 -0.0528 -0.0505 813  ASP B CA  
18520 C C   . ASP C 813  ? 2.9804 1.8056 2.3567 -0.0526 -0.0665 -0.0520 813  ASP B C   
18521 O O   . ASP C 813  ? 2.9652 1.8068 2.3031 -0.0513 -0.0745 -0.0509 813  ASP B O   
18522 C CB  . ASP C 813  ? 3.0708 1.9118 2.4864 -0.0398 -0.0735 -0.0482 813  ASP B CB  
18523 C CG  . ASP C 813  ? 3.1020 1.9376 2.5467 -0.0430 -0.0617 -0.0462 813  ASP B CG  
18524 O OD1 . ASP C 813  ? 3.0961 1.9133 2.5787 -0.0460 -0.0512 -0.0483 813  ASP B OD1 
18525 O OD2 . ASP C 813  ? 3.1224 1.9718 2.5523 -0.0427 -0.0630 -0.0427 813  ASP B OD2 
18526 N N   . THR C 814  ? 2.5509 1.3613 1.9468 -0.0509 -0.0691 -0.0548 814  THR B N   
18527 C CA  . THR C 814  ? 2.5434 1.3555 1.9170 -0.0465 -0.0832 -0.0563 814  THR B CA  
18528 C C   . THR C 814  ? 2.5346 1.3731 1.8916 -0.0282 -0.1115 -0.0559 814  THR B C   
18529 O O   . THR C 814  ? 2.5316 1.3871 1.8927 -0.0204 -0.1188 -0.0542 814  THR B O   
18530 C CB  . THR C 814  ? 2.5087 1.3026 1.9132 -0.0440 -0.0860 -0.0592 814  THR B CB  
18531 O OG1 . THR C 814  ? 2.5153 1.3177 1.9070 -0.0310 -0.1102 -0.0605 814  THR B OG1 
18532 C CG2 . THR C 814  ? 2.4911 1.2822 1.9436 -0.0354 -0.0885 -0.0601 814  THR B CG2 
18533 N N   . VAL C 815  ? 3.3864 2.2286 2.7243 -0.0219 -0.1272 -0.0577 815  VAL B N   
18534 C CA  . VAL C 815  ? 3.4237 2.2905 2.7494 -0.0034 -0.1557 -0.0589 815  VAL B CA  
18535 C C   . VAL C 815  ? 3.4426 2.3031 2.7681 0.0040  -0.1712 -0.0618 815  VAL B C   
18536 O O   . VAL C 815  ? 3.5007 2.3622 2.7927 0.0006  -0.1743 -0.0624 815  VAL B O   
18537 C CB  . VAL C 815  ? 3.4678 2.3557 2.7489 -0.0051 -0.1587 -0.0578 815  VAL B CB  
18538 C CG1 . VAL C 815  ? 3.4780 2.3905 2.7453 0.0133  -0.1882 -0.0603 815  VAL B CG1 
18539 C CG2 . VAL C 815  ? 3.4652 2.3621 2.7468 -0.0101 -0.1472 -0.0547 815  VAL B CG2 
18540 N N   . LYS C 816  ? 3.3393 2.1925 2.7023 0.0138  -0.1807 -0.0636 816  LYS B N   
18541 C CA  . LYS C 816  ? 3.3792 2.2268 2.7459 0.0225  -0.1977 -0.0665 816  LYS B CA  
18542 C C   . LYS C 816  ? 3.4395 2.3109 2.7752 0.0353  -0.2212 -0.0682 816  LYS B C   
18543 O O   . LYS C 816  ? 3.4206 2.3138 2.7377 0.0387  -0.2254 -0.0674 816  LYS B O   
18544 C CB  . LYS C 816  ? 3.6705 2.5147 3.0823 0.0352  -0.2092 -0.0685 816  LYS B CB  
18545 C CG  . LYS C 816  ? 3.8800 2.6987 3.3262 0.0241  -0.1890 -0.0683 816  LYS B CG  
18546 C CD  . LYS C 816  ? 3.8510 2.6708 3.3141 0.0181  -0.1725 -0.0661 816  LYS B CD  
18547 C CE  . LYS C 816  ? 3.8054 2.6012 3.3062 0.0084  -0.1536 -0.0671 816  LYS B CE  
18548 N NZ  . LYS C 816  ? 3.7673 2.5634 3.2868 0.0029  -0.1379 -0.0654 816  LYS B NZ  
18549 N N   . ALA C 817  ? 2.8897 1.7571 2.2202 0.0423  -0.2368 -0.0708 817  ALA B N   
18550 C CA  . ALA C 817  ? 2.9918 1.8813 2.2935 0.0546  -0.2596 -0.0734 817  ALA B CA  
18551 C C   . ALA C 817  ? 3.0098 1.8892 2.3089 0.0605  -0.2747 -0.0762 817  ALA B C   
18552 O O   . ALA C 817  ? 3.0434 1.9182 2.3106 0.0543  -0.2742 -0.0761 817  ALA B O   
18553 C CB  . ALA C 817  ? 3.0546 1.9539 2.3136 0.0443  -0.2498 -0.0717 817  ALA B CB  
18554 N N   . LYS C 818  ? 3.5207 2.3964 2.8537 0.0726  -0.2884 -0.0786 818  LYS B N   
18555 C CA  . LYS C 818  ? 3.5397 2.4058 2.8747 0.0799  -0.3048 -0.0815 818  LYS B CA  
18556 C C   . LYS C 818  ? 3.5323 2.4192 2.8356 0.0915  -0.3273 -0.0848 818  LYS B C   
18557 O O   . LYS C 818  ? 3.5007 2.4154 2.7977 0.1035  -0.3412 -0.0872 818  LYS B O   
18558 C CB  . LYS C 818  ? 3.5689 2.4329 2.9467 0.0931  -0.3178 -0.0841 818  LYS B CB  
18559 C CG  . LYS C 818  ? 3.6321 2.5261 3.0210 0.1119  -0.3386 -0.0870 818  LYS B CG  
18560 C CD  . LYS C 818  ? 3.6844 2.5758 3.1175 0.1240  -0.3498 -0.0894 818  LYS B CD  
18561 C CE  . LYS C 818  ? 3.7360 2.6578 3.1796 0.1419  -0.3702 -0.0921 818  LYS B CE  
18562 N NZ  . LYS C 818  ? 3.7422 2.6631 3.2251 0.1555  -0.3855 -0.0953 818  LYS B NZ  
18563 N N   . VAL C 819  ? 3.3264 2.1996 2.6092 0.0875  -0.3307 -0.0851 819  VAL B N   
18564 C CA  . VAL C 819  ? 3.3491 2.2393 2.6063 0.0998  -0.3542 -0.0892 819  VAL B CA  
18565 C C   . VAL C 819  ? 3.3615 2.2411 2.6410 0.1111  -0.3725 -0.0923 819  VAL B C   
18566 O O   . VAL C 819  ? 3.3543 2.2077 2.6551 0.1033  -0.3623 -0.0902 819  VAL B O   
18567 C CB  . VAL C 819  ? 3.3552 2.2370 2.5717 0.0872  -0.3463 -0.0871 819  VAL B CB  
18568 C CG1 . VAL C 819  ? 3.3504 2.2396 2.5448 0.0736  -0.3251 -0.0837 819  VAL B CG1 
18569 C CG2 . VAL C 819  ? 3.3420 2.1896 2.5628 0.0742  -0.3350 -0.0840 819  VAL B CG2 
18570 N N   . PHE C 820  ? 3.2895 2.1895 2.5645 0.1293  -0.3994 -0.0979 820  PHE B N   
18571 C CA  . PHE C 820  ? 3.3566 2.2479 2.6520 0.1413  -0.4188 -0.1015 820  PHE B CA  
18572 C C   . PHE C 820  ? 3.3769 2.2959 2.6661 0.1622  -0.4488 -0.1087 820  PHE B C   
18573 O O   . PHE C 820  ? 3.3395 2.2872 2.6265 0.1711  -0.4561 -0.1114 820  PHE B O   
18574 C CB  . PHE C 820  ? 3.4426 2.3234 2.7822 0.1431  -0.4138 -0.1008 820  PHE B CB  
18575 C CG  . PHE C 820  ? 3.5970 2.4822 2.9610 0.1609  -0.4384 -0.1061 820  PHE B CG  
18576 C CD1 . PHE C 820  ? 3.6676 2.5813 3.0456 0.1783  -0.4565 -0.1109 820  PHE B CD1 
18577 C CD2 . PHE C 820  ? 3.6770 2.5383 3.0485 0.1602  -0.4441 -0.1066 820  PHE B CD2 
18578 C CE1 . PHE C 820  ? 3.7277 2.6463 3.1281 0.1949  -0.4794 -0.1163 820  PHE B CE1 
18579 C CE2 . PHE C 820  ? 3.7274 2.5927 3.1212 0.1767  -0.4671 -0.1118 820  PHE B CE2 
18580 C CZ  . PHE C 820  ? 3.7466 2.6409 3.1552 0.1943  -0.4848 -0.1169 820  PHE B CZ  
18581 N N   . LYS C 821  ? 3.7601 2.6699 3.0467 0.1696  -0.4663 -0.1118 821  LYS B N   
18582 C CA  . LYS C 821  ? 3.8101 2.7439 3.0912 0.1894  -0.4956 -0.1196 821  LYS B CA  
18583 C C   . LYS C 821  ? 3.8171 2.7527 3.1371 0.2046  -0.5124 -0.1239 821  LYS B C   
18584 O O   . LYS C 821  ? 3.8330 2.7425 3.1741 0.2010  -0.5093 -0.1219 821  LYS B O   
18585 C CB  . LYS C 821  ? 3.8237 2.7464 3.0765 0.1887  -0.5058 -0.1207 821  LYS B CB  
18586 C CG  . LYS C 821  ? 3.8069 2.7535 3.0506 0.2085  -0.5360 -0.1295 821  LYS B CG  
18587 C CD  . LYS C 821  ? 3.7995 2.7643 3.0018 0.2069  -0.5383 -0.1312 821  LYS B CD  
18588 C CE  . LYS C 821  ? 3.8183 2.7989 3.0095 0.2244  -0.5679 -0.1399 821  LYS B CE  
18589 N NZ  . LYS C 821  ? 3.8431 2.8445 2.9955 0.2242  -0.5716 -0.1428 821  LYS B NZ  
18590 N N   . ASP C 822  ? 3.1426 2.7564 3.3423 0.3451  -0.4144 -0.3765 822  ASP B N   
18591 C CA  . ASP C 822  ? 3.0868 2.7349 3.3658 0.3626  -0.4288 -0.3724 822  ASP B CA  
18592 C C   . ASP C 822  ? 3.0954 2.6678 3.3672 0.3662  -0.4694 -0.3611 822  ASP B C   
18593 O O   . ASP C 822  ? 3.0258 2.5502 3.3172 0.3484  -0.4398 -0.3290 822  ASP B O   
18594 C CB  . ASP C 822  ? 3.1305 2.8843 3.4631 0.3999  -0.4714 -0.4101 822  ASP B CB  
18595 C CG  . ASP C 822  ? 3.1922 3.0322 3.5534 0.3974  -0.4275 -0.4180 822  ASP B CG  
18596 O OD1 . ASP C 822  ? 3.2496 3.0681 3.5678 0.3710  -0.3776 -0.4047 822  ASP B OD1 
18597 O OD2 . ASP C 822  ? 3.1829 3.1098 3.6072 0.4211  -0.4430 -0.4374 822  ASP B OD2 
18598 N N   . VAL C 823  ? 2.3079 1.8716 2.5547 0.3900  -0.5380 -0.3878 823  VAL B N   
18599 C CA  . VAL C 823  ? 2.3436 1.8357 2.5794 0.3954  -0.5826 -0.3801 823  VAL B CA  
18600 C C   . VAL C 823  ? 2.4792 1.8975 2.6312 0.3902  -0.6184 -0.3876 823  VAL B C   
18601 O O   . VAL C 823  ? 2.5664 2.0157 2.6878 0.4011  -0.6414 -0.4143 823  VAL B O   
18602 C CB  . VAL C 823  ? 2.2624 1.8111 2.5577 0.4333  -0.6423 -0.4052 823  VAL B CB  
18603 C CG1 . VAL C 823  ? 2.2775 1.7514 2.5465 0.4421  -0.7000 -0.4049 823  VAL B CG1 
18604 C CG2 . VAL C 823  ? 2.1676 1.7648 2.5424 0.4341  -0.6118 -0.3901 823  VAL B CG2 
18605 N N   . PHE C 824  ? 2.5042 1.8243 2.6195 0.3734  -0.6251 -0.3641 824  PHE B N   
18606 C CA  . PHE C 824  ? 2.5755 1.8147 2.6043 0.3618  -0.6519 -0.3659 824  PHE B CA  
18607 C C   . PHE C 824  ? 2.5487 1.6910 2.5518 0.3539  -0.6795 -0.3469 824  PHE B C   
18608 O O   . PHE C 824  ? 2.4808 1.5889 2.5102 0.3385  -0.6471 -0.3178 824  PHE B O   
18609 C CB  . PHE C 824  ? 2.6413 1.8441 2.6086 0.3255  -0.5903 -0.3484 824  PHE B CB  
18610 C CG  . PHE C 824  ? 2.6424 1.8055 2.6198 0.2923  -0.5152 -0.3091 824  PHE B CG  
18611 C CD1 . PHE C 824  ? 2.7305 1.7820 2.6511 0.2610  -0.4947 -0.2790 824  PHE B CD1 
18612 C CD2 . PHE C 824  ? 2.5797 1.8157 2.6231 0.2915  -0.4643 -0.3020 824  PHE B CD2 
18613 C CE1 . PHE C 824  ? 2.7139 1.7282 2.6459 0.2303  -0.4234 -0.2430 824  PHE B CE1 
18614 C CE2 . PHE C 824  ? 2.5637 1.7629 2.6201 0.2611  -0.3947 -0.2653 824  PHE B CE2 
18615 C CZ  . PHE C 824  ? 2.6266 1.7153 2.6284 0.2310  -0.3738 -0.2361 824  PHE B CZ  
18616 N N   . LEU C 825  ? 2.6685 1.7675 2.6218 0.3646  -0.7407 -0.3635 825  LEU B N   
18617 C CA  . LEU C 825  ? 2.6416 1.6417 2.5591 0.3557  -0.7711 -0.3468 825  LEU B CA  
18618 C C   . LEU C 825  ? 2.7208 1.6141 2.5469 0.3149  -0.7391 -0.3211 825  LEU B C   
18619 O O   . LEU C 825  ? 2.7821 1.6686 2.5520 0.3024  -0.7284 -0.3285 825  LEU B O   
18620 C CB  . LEU C 825  ? 2.6065 1.6094 2.5180 0.3888  -0.8581 -0.3774 825  LEU B CB  
18621 C CG  . LEU C 825  ? 2.5827 1.4707 2.4298 0.3745  -0.8925 -0.3626 825  LEU B CG  
18622 C CD1 . LEU C 825  ? 2.4923 1.3449 2.3785 0.3739  -0.8938 -0.3409 825  LEU B CD1 
18623 C CD2 . LEU C 825  ? 2.6259 1.5076 2.4433 0.3998  -0.9723 -0.3932 825  LEU B CD2 
18624 N N   . GLU C 826  ? 3.3939 2.2020 3.2041 0.2935  -0.7245 -0.2909 826  GLU B N   
18625 C CA  . GLU C 826  ? 3.4769 2.1699 3.1941 0.2580  -0.7111 -0.2694 826  GLU B CA  
18626 C C   . GLU C 826  ? 3.5042 2.1245 3.2030 0.2648  -0.7697 -0.2659 826  GLU B C   
18627 O O   . GLU C 826  ? 3.4212 2.0697 3.1841 0.2878  -0.7976 -0.2685 826  GLU B O   
18628 C CB  . GLU C 826  ? 3.4727 2.1195 3.1785 0.2182  -0.6252 -0.2319 826  GLU B CB  
18629 C CG  . GLU C 826  ? 3.4745 2.0717 3.2132 0.2088  -0.6112 -0.2034 826  GLU B CG  
18630 C CD  . GLU C 826  ? 3.5468 2.0462 3.2301 0.1625  -0.5445 -0.1661 826  GLU B CD  
18631 O OE1 . GLU C 826  ? 3.5675 1.9885 3.2387 0.1491  -0.5480 -0.1439 826  GLU B OE1 
18632 O OE2 . GLU C 826  ? 3.5758 2.0751 3.2258 0.1392  -0.4882 -0.1594 826  GLU B OE2 
18633 N N   . MET C 827  ? 2.7259 1.2512 2.3357 0.2443  -0.7898 -0.2597 827  MET B N   
18634 C CA  . MET C 827  ? 2.7517 1.2062 2.3387 0.2506  -0.8491 -0.2578 827  MET B CA  
18635 C C   . MET C 827  ? 2.7859 1.1159 2.2921 0.2067  -0.8161 -0.2245 827  MET B C   
18636 O O   . MET C 827  ? 2.8820 1.1626 2.3099 0.1806  -0.7972 -0.2202 827  MET B O   
18637 C CB  . MET C 827  ? 2.8272 1.2929 2.3856 0.2768  -0.9286 -0.2911 827  MET B CB  
18638 C CG  . MET C 827  ? 2.7695 1.3553 2.4075 0.3231  -0.9686 -0.3272 827  MET B CG  
18639 S SD  . MET C 827  ? 2.5467 1.1662 2.2727 0.3561  -1.0077 -0.3314 827  MET B SD  
18640 C CE  . MET C 827  ? 2.4284 0.9511 2.0973 0.3616  -1.0886 -0.3352 827  MET B CE  
18641 N N   . ASN C 828  ? 3.1354 1.4131 2.6593 0.1976  -0.8081 -0.2006 828  ASN B N   
18642 C CA  . ASN C 828  ? 3.1868 1.3407 2.6333 0.1565  -0.7811 -0.1696 828  ASN B CA  
18643 C C   . ASN C 828  ? 3.2107 1.2842 2.5912 0.1593  -0.8559 -0.1775 828  ASN B C   
18644 O O   . ASN C 828  ? 3.1904 1.2393 2.5959 0.1727  -0.8968 -0.1744 828  ASN B O   
18645 C CB  . ASN C 828  ? 3.2219 1.3534 2.7175 0.1425  -0.7335 -0.1380 828  ASN B CB  
18646 C CG  . ASN C 828  ? 3.3785 1.4023 2.8049 0.0933  -0.6696 -0.1025 828  ASN B CG  
18647 O OD1 . ASN C 828  ? 3.4165 1.4463 2.8317 0.0691  -0.5988 -0.0898 828  ASN B OD1 
18648 N ND2 . ASN C 828  ? 3.4691 1.3932 2.8498 0.0778  -0.6929 -0.0862 828  ASN B ND2 
18649 N N   . ILE C 829  ? 2.8649 0.9000 2.1633 0.1470  -0.8749 -0.1878 829  ILE B N   
18650 C CA  . ILE C 829  ? 2.8578 0.8032 2.0786 0.1414  -0.9389 -0.1914 829  ILE B CA  
18651 C C   . ILE C 829  ? 2.9152 0.7303 2.0541 0.0933  -0.8992 -0.1559 829  ILE B C   
18652 O O   . ILE C 829  ? 2.8589 0.6501 1.9732 0.0603  -0.8228 -0.1345 829  ILE B O   
18653 C CB  . ILE C 829  ? 2.8865 0.8449 2.0530 0.1463  -0.9754 -0.2162 829  ILE B CB  
18654 C CG1 . ILE C 829  ? 2.7872 0.8795 2.0297 0.1838  -0.9844 -0.2472 829  ILE B CG1 
18655 C CG2 . ILE C 829  ? 2.9563 0.8522 2.0716 0.1555  -1.0609 -0.2283 829  ILE B CG2 
18656 C CD1 . ILE C 829  ? 2.7858 0.9503 2.1129 0.2313  -1.0458 -0.2712 829  ILE B CD1 
18657 N N   . PRO C 830  ? 3.0635 0.7926 2.1595 0.0888  -0.9502 -0.1497 830  PRO B N   
18658 C CA  . PRO C 830  ? 3.1830 0.7828 2.1977 0.0431  -0.9173 -0.1168 830  PRO B CA  
18659 C C   . PRO C 830  ? 3.3940 0.9221 2.2992 0.0087  -0.9052 -0.1134 830  PRO B C   
18660 O O   . PRO C 830  ? 3.5662 1.1438 2.4596 0.0225  -0.9308 -0.1371 830  PRO B O   
18661 C CB  . PRO C 830  ? 3.1724 0.7145 2.1749 0.0556  -0.9920 -0.1188 830  PRO B CB  
18662 C CG  . PRO C 830  ? 3.1478 0.7940 2.2374 0.1087  -1.0557 -0.1504 830  PRO B CG  
18663 C CD  . PRO C 830  ? 3.1296 0.8779 2.2514 0.1267  -1.0417 -0.1738 830  PRO B CD  
18664 N N   . TYR C 831  ? 4.0182 1.4287 2.8425 -0.0363 -0.8676 -0.0840 831  TYR B N   
18665 C CA  . TYR C 831  ? 4.1425 1.4683 2.8516 -0.0709 -0.8669 -0.0801 831  TYR B CA  
18666 C C   . TYR C 831  ? 4.1759 1.4678 2.8441 -0.0542 -0.9642 -0.0989 831  TYR B C   
18667 O O   . TYR C 831  ? 4.2238 1.5498 2.8717 -0.0407 -1.0052 -0.1220 831  TYR B O   
18668 C CB  . TYR C 831  ? 4.2497 1.4520 2.8794 -0.1244 -0.8025 -0.0440 831  TYR B CB  
18669 C CG  . TYR C 831  ? 4.4264 1.5336 2.9300 -0.1633 -0.8006 -0.0388 831  TYR B CG  
18670 C CD1 . TYR C 831  ? 4.5320 1.5029 2.9392 -0.2021 -0.8030 -0.0169 831  TYR B CD1 
18671 C CD2 . TYR C 831  ? 4.4590 1.6119 2.9386 -0.1618 -0.7983 -0.0559 831  TYR B CD2 
18672 C CE1 . TYR C 831  ? 4.6693 1.5502 2.9576 -0.2391 -0.8031 -0.0119 831  TYR B CE1 
18673 C CE2 . TYR C 831  ? 4.5970 1.6623 2.9603 -0.1981 -0.7989 -0.0507 831  TYR B CE2 
18674 C CZ  . TYR C 831  ? 4.7041 1.6324 2.9710 -0.2370 -0.8016 -0.0286 831  TYR B CZ  
18675 O OH  . TYR C 831  ? 4.8455 1.6827 2.9926 -0.2749 -0.8034 -0.0229 831  TYR B OH  
18676 N N   . SER C 832  ? 3.4838 0.7133 2.1469 -0.0532 -1.0025 -0.0894 832  SER B N   
18677 C CA  . SER C 832  ? 3.6070 0.7851 2.2212 -0.0437 -1.0916 -0.1025 832  SER B CA  
18678 C C   . SER C 832  ? 3.5356 0.7452 2.2237 -0.0061 -1.1497 -0.1121 832  SER B C   
18679 O O   . SER C 832  ? 3.4430 0.6874 2.2034 0.0028  -1.1160 -0.1015 832  SER B O   
18680 C CB  . SER C 832  ? 3.7665 0.7963 2.2651 -0.0928 -1.0821 -0.0760 832  SER B CB  
18681 O OG  . SER C 832  ? 3.7692 0.7488 2.2867 -0.1028 -1.0624 -0.0531 832  SER B OG  
18682 N N   . VAL C 833  ? 3.7556 0.9470 2.4224 0.0140  -1.2376 -0.1308 833  VAL B N   
18683 C CA  . VAL C 833  ? 3.6932 0.9030 2.4182 0.0492  -1.3029 -0.1416 833  VAL B CA  
18684 C C   . VAL C 833  ? 3.7718 0.8949 2.4207 0.0446  -1.3827 -0.1469 833  VAL B C   
18685 O O   . VAL C 833  ? 3.8350 0.9563 2.4376 0.0443  -1.4161 -0.1622 833  VAL B O   
18686 C CB  . VAL C 833  ? 3.6024 0.9491 2.4299 0.1034  -1.3389 -0.1757 833  VAL B CB  
18687 C CG1 . VAL C 833  ? 3.5566 0.9178 2.4430 0.1377  -1.4007 -0.1852 833  VAL B CG1 
18688 C CG2 . VAL C 833  ? 3.5186 0.9600 2.4177 0.1089  -1.2646 -0.1744 833  VAL B CG2 
18689 N N   . VAL C 834  ? 3.7660 0.8173 2.4028 0.0405  -1.4140 -0.1338 834  VAL B N   
18690 C CA  . VAL C 834  ? 3.8690 0.8392 2.4426 0.0397  -1.4963 -0.1388 834  VAL B CA  
18691 C C   . VAL C 834  ? 3.8936 0.9491 2.5335 0.0938  -1.5807 -0.1753 834  VAL B C   
18692 O O   . VAL C 834  ? 3.7982 0.9533 2.5384 0.1326  -1.5828 -0.1909 834  VAL B O   
18693 C CB  . VAL C 834  ? 3.8753 0.7480 2.4238 0.0210  -1.5032 -0.1138 834  VAL B CB  
18694 C CG1 . VAL C 834  ? 3.9768 0.7732 2.4702 0.0246  -1.5931 -0.1205 834  VAL B CG1 
18695 C CG2 . VAL C 834  ? 3.8938 0.6737 2.3710 -0.0342 -1.4216 -0.0781 834  VAL B CG2 
18696 N N   . ARG C 835  ? 3.8370 0.8536 2.4218 0.0962  -1.6494 -0.1889 835  ARG B N   
18697 C CA  . ARG C 835  ? 3.8965 0.9762 2.5387 0.1458  -1.7354 -0.2215 835  ARG B CA  
18698 C C   . ARG C 835  ? 3.8548 0.9314 2.5517 0.1681  -1.7645 -0.2194 835  ARG B C   
18699 O O   . ARG C 835  ? 3.8908 0.8692 2.5393 0.1396  -1.7577 -0.1935 835  ARG B O   
18700 C CB  . ARG C 835  ? 4.0581 1.0671 2.6220 0.1379  -1.8086 -0.2290 835  ARG B CB  
18701 C CG  . ARG C 835  ? 4.1197 1.1344 2.7191 0.1774  -1.9057 -0.2504 835  ARG B CG  
18702 C CD  . ARG C 835  ? 4.2658 1.2506 2.8139 0.1803  -1.9786 -0.2661 835  ARG B CD  
18703 N NE  . ARG C 835  ? 4.3758 1.2372 2.8028 0.1270  -1.9679 -0.2405 835  ARG B NE  
18704 C CZ  . ARG C 835  ? 4.3983 1.1511 2.7595 0.0875  -1.9413 -0.2095 835  ARG B CZ  
18705 N NH1 . ARG C 835  ? 4.3106 1.0635 2.7173 0.0958  -1.9243 -0.1997 835  ARG B NH1 
18706 N NH2 . ARG C 835  ? 4.5017 1.1437 2.7502 0.0389  -1.9320 -0.1881 835  ARG B NH2 
18707 N N   . GLY C 836  ? 4.1033 1.2858 2.8997 0.2179  -1.7956 -0.2464 836  GLY B N   
18708 C CA  . GLY C 836  ? 4.0863 1.2680 2.9340 0.2434  -1.8363 -0.2486 836  GLY B CA  
18709 C C   . GLY C 836  ? 4.0041 1.2025 2.9032 0.2378  -1.7759 -0.2285 836  GLY B C   
18710 O O   . GLY C 836  ? 3.9549 1.1527 2.8981 0.2575  -1.8063 -0.2285 836  GLY B O   
18711 N N   . GLU C 837  ? 3.8581 1.0689 2.7519 0.2103  -1.6908 -0.2102 837  GLU B N   
18712 C CA  . GLU C 837  ? 3.7652 1.0111 2.7235 0.2099  -1.6330 -0.1939 837  GLU B CA  
18713 C C   . GLU C 837  ? 3.7138 1.1005 2.7757 0.2536  -1.6295 -0.2215 837  GLU B C   
18714 O O   . GLU C 837  ? 3.7308 1.1795 2.7982 0.2683  -1.6378 -0.2447 837  GLU B O   
18715 C CB  . GLU C 837  ? 3.7460 0.9421 2.6570 0.1611  -1.5415 -0.1615 837  GLU B CB  
18716 C CG  . GLU C 837  ? 3.6722 0.7269 2.4900 0.1154  -1.5323 -0.1296 837  GLU B CG  
18717 C CD  . GLU C 837  ? 3.6178 0.6264 2.3917 0.0674  -1.4361 -0.0986 837  GLU B CD  
18718 O OE1 . GLU C 837  ? 3.6148 0.6607 2.3746 0.0578  -1.3942 -0.1037 837  GLU B OE1 
18719 O OE2 . GLU C 837  ? 3.5819 0.5155 2.3349 0.0387  -1.4012 -0.0691 837  GLU B OE2 
18720 N N   . GLN C 838  ? 3.5140 0.9499 2.6568 0.2743  -1.6204 -0.2195 838  GLN B N   
18721 C CA  . GLN C 838  ? 3.4221 0.9878 2.6618 0.3112  -1.6082 -0.2422 838  GLN B CA  
18722 C C   . GLN C 838  ? 3.3421 0.9380 2.5998 0.2858  -1.5137 -0.2212 838  GLN B C   
18723 O O   . GLN C 838  ? 3.2726 0.8252 2.5332 0.2612  -1.4670 -0.1911 838  GLN B O   
18724 C CB  . GLN C 838  ? 3.3866 0.9887 2.7032 0.3459  -1.6487 -0.2507 838  GLN B CB  
18725 C CG  . GLN C 838  ? 3.3514 1.0874 2.7690 0.3894  -1.6516 -0.2791 838  GLN B CG  
18726 C CD  . GLN C 838  ? 3.4179 1.1809 2.9068 0.4205  -1.6905 -0.2850 838  GLN B CD  
18727 O OE1 . GLN C 838  ? 3.4843 1.2596 2.9888 0.4540  -1.7642 -0.3106 838  GLN B OE1 
18728 N NE2 . GLN C 838  ? 3.3545 1.1271 2.8877 0.4093  -1.6403 -0.2612 838  GLN B NE2 
18729 N N   . ILE C 839  ? 3.7427 1.4107 3.0121 0.2905  -1.4841 -0.2362 839  ILE B N   
18730 C CA  . ILE C 839  ? 3.6875 1.3832 2.9727 0.2662  -1.3944 -0.2165 839  ILE B CA  
18731 C C   . ILE C 839  ? 3.6137 1.4282 3.0061 0.2975  -1.3734 -0.2288 839  ILE B C   
18732 O O   . ILE C 839  ? 3.6240 1.5082 3.0720 0.3392  -1.4282 -0.2580 839  ILE B O   
18733 C CB  . ILE C 839  ? 3.7338 1.4304 2.9614 0.2456  -1.3627 -0.2205 839  ILE B CB  
18734 C CG1 . ILE C 839  ? 3.6851 1.3736 2.9059 0.2092  -1.2658 -0.1920 839  ILE B CG1 
18735 C CG2 . ILE C 839  ? 3.7102 1.5174 2.9856 0.2839  -1.3924 -0.2579 839  ILE B CG2 
18736 C CD1 . ILE C 839  ? 3.7287 1.2971 2.8875 0.1653  -1.2303 -0.1545 839  ILE B CD1 
18737 N N   . GLN C 840  ? 3.4312 1.2669 2.8524 0.2769  -1.2945 -0.2065 840  GLN B N   
18738 C CA  . GLN C 840  ? 3.3243 1.2752 2.8412 0.3023  -1.2677 -0.2175 840  GLN B CA  
18739 C C   . GLN C 840  ? 3.2155 1.2150 2.7301 0.2860  -1.1987 -0.2155 840  GLN B C   
18740 O O   . GLN C 840  ? 3.1701 1.1378 2.6724 0.2521  -1.1269 -0.1862 840  GLN B O   
18741 C CB  . GLN C 840  ? 3.3299 1.2789 2.9075 0.3000  -1.2427 -0.1938 840  GLN B CB  
18742 C CG  . GLN C 840  ? 3.3670 1.4126 3.0406 0.3442  -1.2798 -0.2162 840  GLN B CG  
18743 C CD  . GLN C 840  ? 3.3473 1.4845 3.1002 0.3479  -1.2192 -0.2110 840  GLN B CD  
18744 O OE1 . GLN C 840  ? 3.3234 1.5360 3.1535 0.3791  -1.2409 -0.2254 840  GLN B OE1 
18745 N NE2 . GLN C 840  ? 3.3433 1.4719 3.0761 0.3156  -1.1437 -0.1903 840  GLN B NE2 
18746 N N   . LEU C 841  ? 3.4490 1.5267 2.9777 0.3112  -1.2219 -0.2476 841  LEU B N   
18747 C CA  . LEU C 841  ? 3.3816 1.5105 2.9044 0.2997  -1.1670 -0.2512 841  LEU B CA  
18748 C C   . LEU C 841  ? 3.2472 1.4729 2.8574 0.3098  -1.1140 -0.2494 841  LEU B C   
18749 O O   . LEU C 841  ? 3.1795 1.5041 2.8520 0.3456  -1.1390 -0.2779 841  LEU B O   
18750 C CB  . LEU C 841  ? 3.3981 1.5773 2.9069 0.3251  -1.2174 -0.2877 841  LEU B CB  
18751 C CG  . LEU C 841  ? 3.4511 1.5437 2.8654 0.3100  -1.2597 -0.2903 841  LEU B CG  
18752 C CD1 . LEU C 841  ? 3.4666 1.6250 2.8801 0.3348  -1.2985 -0.3253 841  LEU B CD1 
18753 C CD2 . LEU C 841  ? 3.4651 1.4675 2.7979 0.2586  -1.1973 -0.2578 841  LEU B CD2 
18754 N N   . LYS C 842  ? 3.4361 1.6355 3.0511 0.2783  -1.0400 -0.2167 842  LYS B N   
18755 C CA  . LYS C 842  ? 3.3437 1.6317 3.0448 0.2868  -0.9907 -0.2125 842  LYS B CA  
18756 C C   . LYS C 842  ? 3.3437 1.7033 3.0506 0.2834  -0.9435 -0.2230 842  LYS B C   
18757 O O   . LYS C 842  ? 3.4007 1.7515 3.0489 0.2788  -0.9541 -0.2377 842  LYS B O   
18758 C CB  . LYS C 842  ? 3.2939 1.5317 3.0138 0.2582  -0.9339 -0.1729 842  LYS B CB  
18759 C CG  . LYS C 842  ? 3.2999 1.4883 3.0369 0.2663  -0.9779 -0.1629 842  LYS B CG  
18760 C CD  . LYS C 842  ? 3.2524 1.4201 3.0341 0.2449  -0.9204 -0.1266 842  LYS B CD  
18761 C CE  . LYS C 842  ? 3.2755 1.3890 3.0700 0.2510  -0.9646 -0.1153 842  LYS B CE  
18762 N NZ  . LYS C 842  ? 3.2492 1.3397 3.0889 0.2292  -0.9096 -0.0784 842  LYS B NZ  
18763 N N   . GLY C 843  ? 2.4924 0.9231 2.2720 0.2859  -0.8930 -0.2151 843  GLY B N   
18764 C CA  . GLY C 843  ? 2.4966 1.0026 2.2927 0.2841  -0.8458 -0.2240 843  GLY B CA  
18765 C C   . GLY C 843  ? 2.4172 1.0171 2.3137 0.3015  -0.8198 -0.2236 843  GLY B C   
18766 O O   . GLY C 843  ? 2.3881 0.9899 2.3360 0.3144  -0.8415 -0.2167 843  GLY B O   
18767 N N   . THR C 844  ? 3.2388 1.9149 3.1627 0.3013  -0.7749 -0.2303 844  THR B N   
18768 C CA  . THR C 844  ? 3.1824 1.9513 3.2006 0.3168  -0.7498 -0.2306 844  THR B CA  
18769 C C   . THR C 844  ? 3.1298 1.9949 3.1670 0.3291  -0.7317 -0.2548 844  THR B C   
18770 O O   . THR C 844  ? 3.1425 1.9965 3.1384 0.3047  -0.6815 -0.2468 844  THR B O   
18771 C CB  . THR C 844  ? 2.9034 1.6415 2.9500 0.2855  -0.6761 -0.1896 844  THR B CB  
18772 O OG1 . THR C 844  ? 2.9150 1.6334 2.9177 0.2540  -0.6091 -0.1756 844  THR B OG1 
18773 C CG2 . THR C 844  ? 2.8491 1.4860 2.8723 0.2684  -0.6856 -0.1625 844  THR B CG2 
18774 N N   . VAL C 845  ? 2.3489 1.3067 2.4471 0.3660  -0.7711 -0.2843 845  VAL B N   
18775 C CA  . VAL C 845  ? 2.3395 1.3937 2.4595 0.3797  -0.7571 -0.3094 845  VAL B CA  
18776 C C   . VAL C 845  ? 2.2467 1.3620 2.4275 0.3689  -0.6898 -0.2931 845  VAL B C   
18777 O O   . VAL C 845  ? 2.1571 1.2953 2.4044 0.3745  -0.6830 -0.2801 845  VAL B O   
18778 C CB  . VAL C 845  ? 1.8853 1.0170 2.0430 0.4235  -0.8248 -0.3503 845  VAL B CB  
18779 C CG1 . VAL C 845  ? 1.8351 0.9755 2.0540 0.4433  -0.8592 -0.3481 845  VAL B CG1 
18780 C CG2 . VAL C 845  ? 1.8420 1.0809 2.0380 0.4361  -0.8006 -0.3719 845  VAL B CG2 
18781 N N   . TYR C 846  ? 2.9255 2.0692 3.0850 0.3540  -0.6422 -0.2942 846  TYR B N   
18782 C CA  . TYR C 846  ? 2.8622 2.0458 3.0692 0.3367  -0.5709 -0.2728 846  TYR B CA  
18783 C C   . TYR C 846  ? 2.8785 2.1806 3.1522 0.3606  -0.5687 -0.2959 846  TYR B C   
18784 O O   . TYR C 846  ? 2.8925 2.2467 3.1479 0.3716  -0.5769 -0.3228 846  TYR B O   
18785 C CB  . TYR C 846  ? 2.8171 1.9467 2.9632 0.2982  -0.5051 -0.2504 846  TYR B CB  
18786 C CG  . TYR C 846  ? 2.7700 1.7872 2.8762 0.2669  -0.4802 -0.2147 846  TYR B CG  
18787 C CD1 . TYR C 846  ? 2.8140 1.7482 2.8323 0.2359  -0.4526 -0.2020 846  TYR B CD1 
18788 C CD2 . TYR C 846  ? 2.6995 1.6920 2.8549 0.2677  -0.4847 -0.1936 846  TYR B CD2 
18789 C CE1 . TYR C 846  ? 2.8160 1.6451 2.7956 0.2061  -0.4282 -0.1698 846  TYR B CE1 
18790 C CE2 . TYR C 846  ? 2.6930 1.5828 2.8132 0.2388  -0.4612 -0.1610 846  TYR B CE2 
18791 C CZ  . TYR C 846  ? 2.7511 1.5592 2.7831 0.2080  -0.4322 -0.1495 846  TYR B CZ  
18792 O OH  . TYR C 846  ? 2.7645 1.4688 2.7601 0.1784  -0.4072 -0.1175 846  TYR B OH  
18793 N N   . ASN C 847  ? 2.5915 1.9333 2.9430 0.3674  -0.5579 -0.2841 847  ASN B N   
18794 C CA  . ASN C 847  ? 2.6210 2.0692 3.0402 0.3832  -0.5437 -0.2982 847  ASN B CA  
18795 C C   . ASN C 847  ? 2.6090 2.0669 3.0498 0.3537  -0.4623 -0.2688 847  ASN B C   
18796 O O   . ASN C 847  ? 2.5473 1.9535 3.0048 0.3308  -0.4245 -0.2332 847  ASN B O   
18797 C CB  . ASN C 847  ? 2.6143 2.1043 3.1075 0.4085  -0.5833 -0.3040 847  ASN B CB  
18798 C CG  . ASN C 847  ? 2.6170 2.2191 3.1727 0.4289  -0.5814 -0.3258 847  ASN B CG  
18799 O OD1 . ASN C 847  ? 2.6080 2.2529 3.1798 0.4147  -0.5270 -0.3181 847  ASN B OD1 
18800 N ND2 . ASN C 847  ? 2.6227 2.2710 3.2125 0.4618  -0.6405 -0.3532 847  ASN B ND2 
18801 N N   . TYR C 848  ? 2.9907 2.5162 3.4333 0.3547  -0.4353 -0.2841 848  TYR B N   
18802 C CA  . TYR C 848  ? 2.9922 2.5396 3.4615 0.3302  -0.3600 -0.2600 848  TYR B CA  
18803 C C   . TYR C 848  ? 2.9703 2.6310 3.4944 0.3487  -0.3559 -0.2823 848  TYR B C   
18804 O O   . TYR C 848  ? 2.9239 2.6189 3.4740 0.3323  -0.2977 -0.2680 848  TYR B O   
18805 C CB  . TYR C 848  ? 3.0624 2.5500 3.4555 0.2994  -0.3129 -0.2471 848  TYR B CB  
18806 C CG  . TYR C 848  ? 3.0882 2.4632 3.4405 0.2714  -0.2916 -0.2138 848  TYR B CG  
18807 C CD1 . TYR C 848  ? 3.0312 2.3752 3.4327 0.2675  -0.2890 -0.1878 848  TYR B CD1 
18808 C CD2 . TYR C 848  ? 3.1559 2.4547 3.4199 0.2475  -0.2728 -0.2075 848  TYR B CD2 
18809 C CE1 . TYR C 848  ? 3.0573 2.2987 3.4222 0.2414  -0.2679 -0.1574 848  TYR B CE1 
18810 C CE2 . TYR C 848  ? 3.1830 2.3771 3.4067 0.2205  -0.2515 -0.1775 848  TYR B CE2 
18811 C CZ  . TYR C 848  ? 3.1469 2.3134 3.4219 0.2178  -0.2485 -0.1528 848  TYR B CZ  
18812 O OH  . TYR C 848  ? 3.2092 2.2709 3.4437 0.1903  -0.2260 -0.1231 848  TYR B OH  
18813 N N   . ARG C 849  ? 2.6944 2.4116 3.2352 0.3827  -0.4180 -0.3179 849  ARG B N   
18814 C CA  . ARG C 849  ? 2.6796 2.5033 3.2801 0.4029  -0.4217 -0.3395 849  ARG B CA  
18815 C C   . ARG C 849  ? 2.5995 2.4419 3.2798 0.4021  -0.4102 -0.3167 849  ARG B C   
18816 O O   . ARG C 849  ? 2.5777 2.3599 3.2663 0.3990  -0.4274 -0.2974 849  ARG B O   
18817 C CB  . ARG C 849  ? 2.7685 2.6375 3.3608 0.4390  -0.4922 -0.3838 849  ARG B CB  
18818 C CG  . ARG C 849  ? 2.7891 2.7656 3.4390 0.4622  -0.5034 -0.4102 849  ARG B CG  
18819 C CD  . ARG C 849  ? 2.8456 2.8801 3.4905 0.4515  -0.4552 -0.4160 849  ARG B CD  
18820 N NE  . ARG C 849  ? 2.8462 2.9810 3.5517 0.4712  -0.4626 -0.4373 849  ARG B NE  
18821 C CZ  . ARG C 849  ? 2.8316 3.0263 3.5670 0.4600  -0.4137 -0.4318 849  ARG B CZ  
18822 N NH1 . ARG C 849  ? 2.8418 3.0073 3.5535 0.4297  -0.3521 -0.4057 849  ARG B NH1 
18823 N NH2 . ARG C 849  ? 2.7941 3.0766 3.5820 0.4786  -0.4260 -0.4525 849  ARG B NH2 
18824 N N   . THR C 850  ? 2.4490 2.3719 3.1865 0.4035  -0.3814 -0.3177 850  THR B N   
18825 C CA  . THR C 850  ? 2.3580 2.3012 3.1737 0.3973  -0.3602 -0.2914 850  THR B CA  
18826 C C   . THR C 850  ? 2.3479 2.2924 3.2023 0.4202  -0.4200 -0.2985 850  THR B C   
18827 O O   . THR C 850  ? 2.3437 2.2443 3.2308 0.4100  -0.4155 -0.2688 850  THR B O   
18828 C CB  . THR C 850  ? 2.2683 2.3074 3.1376 0.3981  -0.3274 -0.2970 850  THR B CB  
18829 O OG1 . THR C 850  ? 2.2752 2.3886 3.1423 0.4274  -0.3713 -0.3406 850  THR B OG1 
18830 C CG2 . THR C 850  ? 2.2555 2.2915 3.1027 0.3702  -0.2564 -0.2798 850  THR B CG2 
18831 N N   . SER C 851  ? 2.8759 2.8736 3.7283 0.4512  -0.4746 -0.3386 851  SER B N   
18832 C CA  . SER C 851  ? 2.8895 2.8893 3.7673 0.4766  -0.5379 -0.3531 851  SER B CA  
18833 C C   . SER C 851  ? 2.9769 2.8969 3.7952 0.4822  -0.5794 -0.3586 851  SER B C   
18834 O O   . SER C 851  ? 2.9992 2.8771 3.7554 0.4702  -0.5641 -0.3586 851  SER B O   
18835 C CB  . SER C 851  ? 2.9123 3.0016 3.8068 0.5069  -0.5752 -0.3964 851  SER B CB  
18836 O OG  . SER C 851  ? 2.9967 3.1013 3.8363 0.5127  -0.5770 -0.4234 851  SER B OG  
18837 N N   . GLY C 852  ? 1.8124 1.7104 2.6478 0.4999  -0.6329 -0.3634 852  GLY B N   
18838 C CA  . GLY C 852  ? 1.8707 1.6991 2.6526 0.5094  -0.6808 -0.3729 852  GLY B CA  
18839 C C   . GLY C 852  ? 1.8660 1.7262 2.6076 0.5357  -0.7257 -0.4176 852  GLY B C   
18840 O O   . GLY C 852  ? 1.8609 1.7951 2.6100 0.5437  -0.7129 -0.4403 852  GLY B O   
18841 N N   . MET C 853  ? 1.7875 1.5917 2.4874 0.5485  -0.7778 -0.4298 853  MET B N   
18842 C CA  . MET C 853  ? 1.7848 1.6192 2.4560 0.5779  -0.8304 -0.4735 853  MET B CA  
18843 C C   . MET C 853  ? 1.7948 1.5670 2.4303 0.5947  -0.8947 -0.4861 853  MET B C   
18844 O O   . MET C 853  ? 1.7841 1.4804 2.4093 0.5836  -0.9034 -0.4611 853  MET B O   
18845 C CB  . MET C 853  ? 1.8295 1.6872 2.4571 0.5700  -0.8023 -0.4866 853  MET B CB  
18846 C CG  . MET C 853  ? 1.8762 1.6567 2.4458 0.5364  -0.7602 -0.4571 853  MET B CG  
18847 S SD  . MET C 853  ? 2.2231 2.0560 2.7635 0.5248  -0.7132 -0.4689 853  MET B SD  
18848 C CE  . MET C 853  ? 2.2468 2.1437 2.8572 0.5102  -0.6495 -0.4473 853  MET B CE  
18849 N N   . GLN C 854  ? 3.0543 2.8619 3.6733 0.6223  -0.9401 -0.5260 854  GLN B N   
18850 C CA  . GLN C 854  ? 3.0953 2.8529 3.6838 0.6415  -1.0042 -0.5423 854  GLN B CA  
18851 C C   . GLN C 854  ? 3.1485 2.8599 3.6660 0.6329  -1.0092 -0.5474 854  GLN B C   
18852 O O   . GLN C 854  ? 3.1601 2.9139 3.6607 0.6295  -0.9851 -0.5603 854  GLN B O   
18853 C CB  . GLN C 854  ? 3.1101 2.9355 3.7335 0.6806  -1.0575 -0.5843 854  GLN B CB  
18854 C CG  . GLN C 854  ? 3.0415 2.9184 3.7326 0.6888  -1.0527 -0.5820 854  GLN B CG  
18855 C CD  . GLN C 854  ? 3.0572 2.9948 3.7775 0.7270  -1.1059 -0.6246 854  GLN B CD  
18856 O OE1 . GLN C 854  ? 3.1128 3.0621 3.8071 0.7479  -1.1421 -0.6570 854  GLN B OE1 
18857 N NE2 . GLN C 854  ? 3.0029 2.9783 3.7777 0.7358  -1.1110 -0.6248 854  GLN B NE2 
18858 N N   . PHE C 855  ? 2.4361 2.0595 2.9113 0.6286  -1.0417 -0.5369 855  PHE B N   
18859 C CA  . PHE C 855  ? 2.4757 2.0438 2.8789 0.6193  -1.0535 -0.5401 855  PHE B CA  
18860 C C   . PHE C 855  ? 2.5578 2.0914 2.9401 0.6448  -1.1281 -0.5631 855  PHE B C   
18861 O O   . PHE C 855  ? 2.5611 2.1274 2.9853 0.6740  -1.1717 -0.5839 855  PHE B O   
18862 C CB  . PHE C 855  ? 2.4321 1.9094 2.7874 0.5791  -1.0091 -0.4982 855  PHE B CB  
18863 C CG  . PHE C 855  ? 2.3619 1.7637 2.7218 0.5705  -1.0223 -0.4710 855  PHE B CG  
18864 C CD1 . PHE C 855  ? 2.3977 1.7442 2.7330 0.5860  -1.0860 -0.4807 855  PHE B CD1 
18865 C CD2 . PHE C 855  ? 2.2718 1.6554 2.6600 0.5454  -0.9692 -0.4342 855  PHE B CD2 
18866 C CE1 . PHE C 855  ? 2.3764 1.6526 2.7142 0.5766  -1.0966 -0.4549 855  PHE B CE1 
18867 C CE2 . PHE C 855  ? 2.2483 1.5628 2.6421 0.5361  -0.9791 -0.4079 855  PHE B CE2 
18868 C CZ  . PHE C 855  ? 2.2985 1.5588 2.6656 0.5512  -1.0422 -0.4181 855  PHE B CZ  
18869 N N   . CYS C 856  ? 3.1323 2.5959 3.4480 0.6326  -1.1429 -0.5585 856  CYS B N   
18870 C CA  . CYS C 856  ? 3.2118 2.6442 3.5056 0.6566  -1.2145 -0.5816 856  CYS B CA  
18871 C C   . CYS C 856  ? 3.3218 2.6692 3.5354 0.6333  -1.2176 -0.5682 856  CYS B C   
18872 O O   . CYS C 856  ? 3.3754 2.7417 3.5583 0.6365  -1.2259 -0.5869 856  CYS B O   
18873 C CB  . CYS C 856  ? 3.2227 2.7461 3.5477 0.6928  -1.2490 -0.6270 856  CYS B CB  
18874 S SG  . CYS C 856  ? 3.7510 3.2763 4.0980 0.7367  -1.3383 -0.6622 856  CYS B SG  
18875 N N   . VAL C 857  ? 2.6613 1.9140 2.8402 0.6083  -1.2099 -0.5350 857  VAL B N   
18876 C CA  . VAL C 857  ? 2.7325 1.8945 2.8299 0.5826  -1.2119 -0.5196 857  VAL B CA  
18877 C C   . VAL C 857  ? 2.8203 1.9334 2.8901 0.6028  -1.2893 -0.5370 857  VAL B C   
18878 O O   . VAL C 857  ? 2.8248 1.9152 2.9195 0.6176  -1.3262 -0.5365 857  VAL B O   
18879 C CB  . VAL C 857  ? 2.6900 1.7683 2.7567 0.5420  -1.1604 -0.4742 857  VAL B CB  
18880 C CG1 . VAL C 857  ? 2.6233 1.7409 2.7039 0.5176  -1.0804 -0.4563 857  VAL B CG1 
18881 C CG2 . VAL C 857  ? 2.6376 1.6864 2.7424 0.5481  -1.1779 -0.4593 857  VAL B CG2 
18882 N N   . LYS C 858  ? 3.4092 2.5069 3.4289 0.6032  -1.3146 -0.5522 858  LYS B N   
18883 C CA  . LYS C 858  ? 3.5045 2.5507 3.4931 0.6196  -1.3877 -0.5671 858  LYS B CA  
18884 C C   . LYS C 858  ? 3.5653 2.5282 3.4660 0.5907  -1.3896 -0.5534 858  LYS B C   
18885 O O   . LYS C 858  ? 3.5875 2.5709 3.4600 0.5757  -1.3575 -0.5545 858  LYS B O   
18886 C CB  . LYS C 858  ? 3.5773 2.7072 3.6123 0.6642  -1.4412 -0.6121 858  LYS B CB  
18887 C CG  . LYS C 858  ? 3.6300 2.8479 3.6798 0.6705  -1.4148 -0.6335 858  LYS B CG  
18888 C CD  . LYS C 858  ? 3.6984 2.9949 3.7946 0.7147  -1.4685 -0.6782 858  LYS B CD  
18889 C CE  . LYS C 858  ? 3.7385 3.1141 3.8415 0.7182  -1.4438 -0.6981 858  LYS B CE  
18890 N NZ  . LYS C 858  ? 3.7671 3.2244 3.9202 0.7610  -1.4905 -0.7421 858  LYS B NZ  
18891 N N   . MET C 859  ? 3.6900 2.5566 3.5456 0.5816  -1.4273 -0.5396 859  MET B N   
18892 C CA  . MET C 859  ? 3.7270 2.5029 3.4944 0.5519  -1.4327 -0.5241 859  MET B CA  
18893 C C   . MET C 859  ? 3.7958 2.5718 3.5434 0.5751  -1.5044 -0.5536 859  MET B C   
18894 O O   . MET C 859  ? 3.8084 2.5986 3.5909 0.6085  -1.5652 -0.5752 859  MET B O   
18895 C CB  . MET C 859  ? 3.7185 2.3829 3.4420 0.5246  -1.4303 -0.4901 859  MET B CB  
18896 C CG  . MET C 859  ? 3.8125 2.3807 3.4595 0.5131  -1.4808 -0.4865 859  MET B CG  
18897 S SD  . MET C 859  ? 3.3456 1.7932 2.9559 0.4905  -1.4913 -0.4527 859  MET B SD  
18898 C CE  . MET C 859  ? 4.2451 2.6398 3.8098 0.4371  -1.3954 -0.4101 859  MET B CE  
18899 N N   . SER C 860  ? 4.5902 3.3491 4.2820 0.5571  -1.4972 -0.5538 860  SER B N   
18900 C CA  . SER C 860  ? 4.6947 3.4512 4.3654 0.5756  -1.5630 -0.5792 860  SER B CA  
18901 C C   . SER C 860  ? 4.7881 3.4333 4.4006 0.5653  -1.6161 -0.5664 860  SER B C   
18902 O O   . SER C 860  ? 4.8376 3.3891 4.3768 0.5255  -1.5920 -0.5356 860  SER B O   
18903 C CB  . SER C 860  ? 4.7556 3.5266 4.3829 0.5566  -1.5371 -0.5810 860  SER B CB  
18904 O OG  . SER C 860  ? 4.8820 3.6064 4.4605 0.5581  -1.5963 -0.5909 860  SER B OG  
18905 N N   . ALA C 861  ? 3.5792 2.2334 3.2230 0.6006  -1.6879 -0.5904 861  ALA B N   
18906 C CA  . ALA C 861  ? 3.6362 2.1892 3.2281 0.5943  -1.7458 -0.5816 861  ALA B CA  
18907 C C   . ALA C 861  ? 3.7145 2.2155 3.2333 0.5756  -1.7713 -0.5807 861  ALA B C   
18908 O O   . ALA C 861  ? 3.7301 2.2790 3.2685 0.6016  -1.8163 -0.6097 861  ALA B O   
18909 C CB  . ALA C 861  ? 3.6366 2.2196 3.2859 0.6390  -1.8155 -0.6097 861  ALA B CB  
18910 N N   . VAL C 862  ? 4.3549 2.7565 3.7895 0.5302  -1.7433 -0.5473 862  VAL B N   
18911 C CA  . VAL C 862  ? 4.4667 2.8045 3.8221 0.5072  -1.7681 -0.5424 862  VAL B CA  
18912 C C   . VAL C 862  ? 4.5469 2.7886 3.8576 0.5067  -1.8411 -0.5383 862  VAL B C   
18913 O O   . VAL C 862  ? 4.5696 2.7264 3.8456 0.4863  -1.8374 -0.5134 862  VAL B O   
18914 C CB  . VAL C 862  ? 4.4957 2.7761 3.7754 0.4554  -1.6967 -0.5097 862  VAL B CB  
18915 C CG1 . VAL C 862  ? 4.6226 2.8249 3.8126 0.4287  -1.7260 -0.5025 862  VAL B CG1 
18916 C CG2 . VAL C 862  ? 4.4108 2.7884 3.7322 0.4567  -1.6299 -0.5161 862  VAL B CG2 
18917 N N   . GLU C 863  ? 4.2522 2.5095 3.5662 0.5293  -1.9071 -0.5630 863  GLU B N   
18918 C CA  . GLU C 863  ? 4.3137 2.4868 3.5879 0.5313  -1.9834 -0.5624 863  GLU B CA  
18919 C C   . GLU C 863  ? 4.2598 2.3390 3.5044 0.5157  -1.9903 -0.5376 863  GLU B C   
18920 O O   . GLU C 863  ? 4.1999 2.2989 3.5000 0.5459  -2.0213 -0.5490 863  GLU B O   
18921 C CB  . GLU C 863  ? 4.5035 2.6083 3.6906 0.4995  -2.0000 -0.5517 863  GLU B CB  
18922 C CG  . GLU C 863  ? 4.6969 2.8611 3.9101 0.5271  -2.0536 -0.5827 863  GLU B CG  
18923 C CD  . GLU C 863  ? 4.8144 2.9612 4.0528 0.5600  -2.1446 -0.6021 863  GLU B CD  
18924 O OE1 . GLU C 863  ? 4.7733 2.9295 4.0604 0.5853  -2.1639 -0.6092 863  GLU B OE1 
18925 O OE2 . GLU C 863  ? 4.9230 3.0465 4.1333 0.5605  -2.1976 -0.6102 863  GLU B OE2 
18926 N N   . GLY C 864  ? 3.7958 1.7707 2.9504 0.4673  -1.9611 -0.5037 864  GLY B N   
18927 C CA  . GLY C 864  ? 3.8245 1.6908 2.9319 0.4476  -1.9804 -0.4796 864  GLY B CA  
18928 C C   . GLY C 864  ? 3.6974 1.5566 2.8276 0.4374  -1.9244 -0.4589 864  GLY B C   
18929 O O   . GLY C 864  ? 3.7285 1.4994 2.8228 0.4198  -1.9340 -0.4372 864  GLY B O   
18930 N N   . ILE C 865  ? 3.8377 1.7883 3.0275 0.4469  -1.8653 -0.4643 865  ILE B N   
18931 C CA  . ILE C 865  ? 3.7022 1.6562 2.9266 0.4417  -1.8165 -0.4464 865  ILE B CA  
18932 C C   . ILE C 865  ? 3.6517 1.6698 2.9652 0.4891  -1.8597 -0.4699 865  ILE B C   
18933 O O   . ILE C 865  ? 3.6316 1.7292 2.9986 0.5284  -1.9018 -0.5038 865  ILE B O   
18934 C CB  . ILE C 865  ? 3.5789 1.5901 2.8210 0.4248  -1.7292 -0.4364 865  ILE B CB  
18935 C CG1 . ILE C 865  ? 3.6184 1.6024 2.7881 0.3933  -1.7041 -0.4295 865  ILE B CG1 
18936 C CG2 . ILE C 865  ? 3.5126 1.4752 2.7480 0.3969  -1.6703 -0.4030 865  ILE B CG2 
18937 C CD1 . ILE C 865  ? 3.5465 1.5627 2.7156 0.3677  -1.6137 -0.4134 865  ILE B CD1 
18938 N N   . CYS C 866  ? 3.8077 1.7870 3.1343 0.4842  -1.8499 -0.4514 866  CYS B N   
18939 C CA  . CYS C 866  ? 3.8280 1.8533 3.2310 0.5244  -1.8894 -0.4692 866  CYS B CA  
18940 C C   . CYS C 866  ? 3.8152 1.9345 3.2970 0.5385  -1.8353 -0.4725 866  CYS B C   
18941 O O   . CYS C 866  ? 3.7196 1.8423 3.1916 0.5100  -1.7625 -0.4506 866  CYS B O   
18942 C CB  . CYS C 866  ? 3.8359 1.7617 3.2077 0.5111  -1.9151 -0.4467 866  CYS B CB  
18943 S SG  . CYS C 866  ? 3.9722 1.8568 3.3357 0.5409  -2.0219 -0.4688 866  CYS B SG  
18944 N N   . THR C 867  ? 4.2784 2.4718 3.8381 0.5819  -1.8710 -0.4996 867  THR B N   
18945 C CA  . THR C 867  ? 4.3033 2.5859 3.9393 0.5965  -1.8254 -0.5038 867  THR B CA  
18946 C C   . THR C 867  ? 4.4235 2.7613 4.1339 0.6412  -1.8742 -0.5298 867  THR B C   
18947 O O   . THR C 867  ? 4.4897 2.7913 4.1936 0.6608  -1.9430 -0.5429 867  THR B O   
18948 C CB  . THR C 867  ? 4.1215 2.4956 3.7805 0.5990  -1.7801 -0.5182 867  THR B CB  
18949 O OG1 . THR C 867  ? 4.1994 2.5472 3.7993 0.5875  -1.7973 -0.5245 867  THR B OG1 
18950 C CG2 . THR C 867  ? 4.0364 2.4158 3.6949 0.5663  -1.6932 -0.4888 867  THR B CG2 
18951 N N   . SER C 868  ? 3.8446 2.2692 3.6249 0.6564  -1.8376 -0.5370 868  SER B N   
18952 C CA  . SER C 868  ? 3.9683 2.4401 3.8184 0.6930  -1.8719 -0.5559 868  SER B CA  
18953 C C   . SER C 868  ? 4.1263 2.7061 4.0366 0.7358  -1.8980 -0.5995 868  SER B C   
18954 O O   . SER C 868  ? 4.1133 2.7265 4.0737 0.7708  -1.9416 -0.6221 868  SER B O   
18955 C CB  . SER C 868  ? 3.8814 2.3646 3.7682 0.6790  -1.8175 -0.5307 868  SER B CB  
18956 O OG  . SER C 868  ? 3.9016 2.2872 3.7315 0.6372  -1.7864 -0.4903 868  SER B OG  
18957 N N   . GLU C 869  ? 4.5402 3.1725 4.4445 0.7324  -1.8706 -0.6111 869  GLU B N   
18958 C CA  . GLU C 869  ? 4.6995 3.4269 4.6516 0.7705  -1.8976 -0.6530 869  GLU B CA  
18959 C C   . GLU C 869  ? 4.8158 3.5694 4.7442 0.7567  -1.8968 -0.6425 869  GLU B C   
18960 O O   . GLU C 869  ? 4.8730 3.5522 4.7368 0.7253  -1.8950 -0.6172 869  GLU B O   
18961 C CB  . GLU C 869  ? 4.6988 3.4905 4.6505 0.7576  -1.8411 -0.6557 869  GLU B CB  
18962 C CG  . GLU C 869  ? 4.6941 3.5999 4.7069 0.7947  -1.8516 -0.6966 869  GLU B CG  
18963 C CD  . GLU C 869  ? 4.7526 3.6829 4.7430 0.7970  -1.8718 -0.7104 869  GLU B CD  
18964 O OE1 . GLU C 869  ? 4.8080 3.6679 4.7323 0.7675  -1.8738 -0.6879 869  GLU B OE1 
18965 O OE2 . GLU C 869  ? 4.7150 3.7550 4.7545 0.8150  -1.8590 -0.7309 869  GLU B OE2 
18966 N N   . SER C 870  ? 3.8523 2.6082 3.8283 0.8311  -2.0188 -0.7123 870  SER B N   
18967 C CA  . SER C 870  ? 4.0012 2.7247 3.9600 0.8513  -2.0925 -0.7328 870  SER B CA  
18968 C C   . SER C 870  ? 4.0910 2.7932 3.9953 0.8314  -2.0910 -0.7298 870  SER B C   
18969 O O   . SER C 870  ? 4.0840 2.8574 4.0037 0.8327  -2.0588 -0.7424 870  SER B O   
18970 C CB  . SER C 870  ? 4.0303 2.8370 4.0613 0.9020  -2.1372 -0.7771 870  SER B CB  
18971 O OG  . SER C 870  ? 4.0444 2.9356 4.1001 0.9156  -2.1244 -0.8029 870  SER B OG  
18972 N N   . LYS C 882  ? 3.8212 2.9044 3.8983 0.7497  -1.6425 -0.6688 882  LYS B N   
18973 C CA  . LYS C 882  ? 3.7702 2.9293 3.9233 0.7798  -1.6476 -0.6881 882  LYS B CA  
18974 C C   . LYS C 882  ? 3.6420 2.8589 3.8301 0.7645  -1.5758 -0.6735 882  LYS B C   
18975 O O   . LYS C 882  ? 3.6104 2.7881 3.7655 0.7280  -1.5222 -0.6404 882  LYS B O   
18976 C CB  . LYS C 882  ? 3.7976 2.9023 3.9623 0.7906  -1.6896 -0.6812 882  LYS B CB  
18977 C CG  . LYS C 882  ? 3.7825 2.8115 3.9233 0.7557  -1.6531 -0.6372 882  LYS B CG  
18978 C CD  . LYS C 882  ? 3.8086 2.7812 3.9575 0.7677  -1.7015 -0.6322 882  LYS B CD  
18979 C CE  . LYS C 882  ? 3.9188 2.8267 4.0228 0.7778  -1.7684 -0.6438 882  LYS B CE  
18980 N NZ  . LYS C 882  ? 3.9290 2.7863 4.0429 0.7928  -1.8204 -0.6426 882  LYS B NZ  
18981 N N   . CYS C 883  ? 3.7103 3.0186 3.9649 0.7920  -1.5750 -0.6982 883  CYS B N   
18982 C CA  . CYS C 883  ? 3.5954 2.9674 3.8889 0.7805  -1.5114 -0.6878 883  CYS B CA  
18983 C C   . CYS C 883  ? 3.4867 2.8511 3.8211 0.7790  -1.5005 -0.6692 883  CYS B C   
18984 O O   . CYS C 883  ? 3.4576 2.8780 3.8462 0.8073  -1.5231 -0.6913 883  CYS B O   
18985 C CB  . CYS C 883  ? 3.5803 3.0628 3.9191 0.8077  -1.5098 -0.7255 883  CYS B CB  
18986 S SG  . CYS C 883  ? 4.1600 3.7259 4.5423 0.7927  -1.4318 -0.7151 883  CYS B SG  
18987 N N   . VAL C 884  ? 3.6474 2.9420 3.9556 0.7449  -1.4649 -0.6282 884  VAL B N   
18988 C CA  . VAL C 884  ? 3.5595 2.8406 3.9048 0.7383  -1.4497 -0.6049 884  VAL B CA  
18989 C C   . VAL C 884  ? 3.4913 2.8265 3.8718 0.7193  -1.3789 -0.5869 884  VAL B C   
18990 O O   . VAL C 884  ? 3.4613 2.7490 3.8262 0.6859  -1.3313 -0.5492 884  VAL B O   
18991 C CB  . VAL C 884  ? 3.1320 2.3016 3.4319 0.7118  -1.4524 -0.5690 884  VAL B CB  
18992 C CG1 . VAL C 884  ? 3.1992 2.3173 3.4793 0.7337  -1.5273 -0.5849 884  VAL B CG1 
18993 C CG2 . VAL C 884  ? 3.1673 2.2851 3.4033 0.6763  -1.4110 -0.5462 884  VAL B CG2 
18994 N N   . ARG C 885  ? 3.4103 2.8435 3.8388 0.7401  -1.3716 -0.6137 885  ARG B N   
18995 C CA  . ARG C 885  ? 3.3293 2.8195 3.7876 0.7223  -1.3047 -0.5997 885  ARG B CA  
18996 C C   . ARG C 885  ? 3.2404 2.7097 3.7324 0.7033  -1.2715 -0.5644 885  ARG B C   
18997 O O   . ARG C 885  ? 3.2124 2.6762 3.7382 0.7180  -1.3036 -0.5653 885  ARG B O   
18998 C CB  . ARG C 885  ? 3.3061 2.9064 3.8081 0.7478  -1.3037 -0.6360 885  ARG B CB  
18999 C CG  . ARG C 885  ? 3.2802 2.9326 3.8381 0.7816  -1.3448 -0.6627 885  ARG B CG  
19000 C CD  . ARG C 885  ? 3.2526 3.0143 3.8522 0.7992  -1.3284 -0.6932 885  ARG B CD  
19001 N NE  . ARG C 885  ? 3.3126 3.1062 3.8838 0.8059  -1.3295 -0.7178 885  ARG B NE  
19002 C CZ  . ARG C 885  ? 3.3085 3.1914 3.9048 0.8178  -1.3123 -0.7438 885  ARG B CZ  
19003 N NH1 . ARG C 885  ? 3.2493 3.1993 3.8983 0.8243  -1.2925 -0.7495 885  ARG B NH1 
19004 N NH2 . ARG C 885  ? 3.3615 3.2657 3.9294 0.8225  -1.3156 -0.7638 885  ARG B NH2 
19005 N N   . GLN C 886  ? 2.8797 2.3367 3.3625 0.6698  -1.2064 -0.5329 886  GLN B N   
19006 C CA  . GLN C 886  ? 2.8327 2.2647 3.3460 0.6470  -1.1675 -0.4948 886  GLN B CA  
19007 C C   . GLN C 886  ? 2.7076 2.2116 3.2602 0.6340  -1.1042 -0.4863 886  GLN B C   
19008 O O   . GLN C 886  ? 2.7143 2.2863 3.2689 0.6441  -1.0943 -0.5114 886  GLN B O   
19009 C CB  . GLN C 886  ? 2.9419 2.2698 3.4013 0.6144  -1.1473 -0.4587 886  GLN B CB  
19010 C CG  . GLN C 886  ? 2.9803 2.2581 3.4649 0.5956  -1.1286 -0.4209 886  GLN B CG  
19011 C CD  . GLN C 886  ? 3.0808 2.2959 3.5535 0.6087  -1.1895 -0.4220 886  GLN B CD  
19012 O OE1 . GLN C 886  ? 3.0953 2.2558 3.5789 0.5932  -1.1822 -0.3913 886  GLN B OE1 
19013 N NE2 . GLN C 886  ? 3.1445 2.3665 3.5959 0.6374  -1.2505 -0.4574 886  GLN B NE2 
19014 N N   . LYS C 887  ? 2.9721 2.4617 3.5577 0.6117  -1.0618 -0.4508 887  LYS B N   
19015 C CA  . LYS C 887  ? 2.8797 2.4379 3.5106 0.6005  -1.0054 -0.4415 887  LYS B CA  
19016 C C   . LYS C 887  ? 2.8122 2.3191 3.4351 0.5612  -0.9402 -0.3963 887  LYS B C   
19017 O O   . LYS C 887  ? 2.7647 2.2017 3.3869 0.5462  -0.9392 -0.3666 887  LYS B O   
19018 C CB  . LYS C 887  ? 2.8291 2.4460 3.5316 0.6190  -1.0228 -0.4481 887  LYS B CB  
19019 C CG  . LYS C 887  ? 2.8749 2.5174 3.5865 0.6574  -1.0955 -0.4872 887  LYS B CG  
19020 C CD  . LYS C 887  ? 2.9094 2.4768 3.6150 0.6618  -1.1409 -0.4750 887  LYS B CD  
19021 C CE  . LYS C 887  ? 2.9451 2.5352 3.6611 0.7001  -1.2123 -0.5133 887  LYS B CE  
19022 N NZ  . LYS C 887  ? 2.8830 2.5258 3.6621 0.7142  -1.2243 -0.5186 887  LYS B NZ  
19023 N N   . VAL C 888  ? 2.4814 2.0229 3.0986 0.5443  -0.8848 -0.3914 888  VAL B N   
19024 C CA  . VAL C 888  ? 2.4543 1.9505 3.0629 0.5069  -0.8179 -0.3506 888  VAL B CA  
19025 C C   . VAL C 888  ? 2.4105 1.9687 3.0878 0.4980  -0.7699 -0.3340 888  VAL B C   
19026 O O   . VAL C 888  ? 2.4232 2.0625 3.1228 0.5074  -0.7557 -0.3538 888  VAL B O   
19027 C CB  . VAL C 888  ? 2.4509 1.9310 2.9969 0.4894  -0.7838 -0.3529 888  VAL B CB  
19028 C CG1 . VAL C 888  ? 2.5129 1.9023 2.9847 0.4841  -0.8157 -0.3527 888  VAL B CG1 
19029 C CG2 . VAL C 888  ? 2.4389 2.0093 2.9902 0.5110  -0.7936 -0.3911 888  VAL B CG2 
19030 N N   . GLU C 889  ? 2.4798 1.9995 3.1917 0.4792  -0.7448 -0.2970 889  GLU B N   
19031 C CA  . GLU C 889  ? 2.4670 2.0360 3.2428 0.4653  -0.6924 -0.2751 889  GLU B CA  
19032 C C   . GLU C 889  ? 2.4310 2.0113 3.1795 0.4427  -0.6287 -0.2676 889  GLU B C   
19033 O O   . GLU C 889  ? 2.4365 1.9521 3.1210 0.4247  -0.6104 -0.2590 889  GLU B O   
19034 C CB  . GLU C 889  ? 2.5681 2.0841 3.3827 0.4460  -0.6736 -0.2332 889  GLU B CB  
19035 C CG  . GLU C 889  ? 2.7559 2.1672 3.5179 0.4203  -0.6545 -0.2051 889  GLU B CG  
19036 C CD  . GLU C 889  ? 2.9366 2.2873 3.6528 0.4357  -0.7200 -0.2194 889  GLU B CD  
19037 O OE1 . GLU C 889  ? 2.9873 2.3770 3.7156 0.4673  -0.7806 -0.2509 889  GLU B OE1 
19038 O OE2 . GLU C 889  ? 3.0170 2.2792 3.6844 0.4156  -0.7103 -0.1990 889  GLU B OE2 
19039 N N   . GLY C 890  ? 2.9206 2.5818 3.7153 0.4432  -0.5961 -0.2715 890  GLY B N   
19040 C CA  . GLY C 890  ? 2.8844 2.5698 3.6559 0.4261  -0.5404 -0.2703 890  GLY B CA  
19041 C C   . GLY C 890  ? 2.7871 2.4007 3.5332 0.3889  -0.4770 -0.2312 890  GLY B C   
19042 O O   . GLY C 890  ? 2.7408 2.3154 3.5225 0.3722  -0.4535 -0.1966 890  GLY B O   
19043 N N   . SER C 891  ? 2.9552 2.5498 3.6391 0.3753  -0.4486 -0.2363 891  SER B N   
19044 C CA  . SER C 891  ? 2.8928 2.4259 3.5521 0.3388  -0.3810 -0.2009 891  SER B CA  
19045 C C   . SER C 891  ? 2.8937 2.3267 3.5333 0.3240  -0.3874 -0.1731 891  SER B C   
19046 O O   . SER C 891  ? 2.8671 2.2673 3.5411 0.3012  -0.3418 -0.1365 891  SER B O   
19047 C CB  . SER C 891  ? 2.7746 2.3574 3.5057 0.3247  -0.3221 -0.1770 891  SER B CB  
19048 O OG  . SER C 891  ? 2.7432 2.4270 3.5254 0.3487  -0.3428 -0.2023 891  SER B OG  
19049 N N   . SER C 892  ? 2.5233 1.9084 3.1099 0.3369  -0.4442 -0.1903 892  SER B N   
19050 C CA  . SER C 892  ? 2.5362 1.8213 3.0939 0.3222  -0.4534 -0.1661 892  SER B CA  
19051 C C   . SER C 892  ? 2.6171 1.8469 3.0928 0.3307  -0.5048 -0.1879 892  SER B C   
19052 O O   . SER C 892  ? 2.6397 1.8709 3.0578 0.3273  -0.4987 -0.2048 892  SER B O   
19053 C CB  . SER C 892  ? 2.4897 1.7784 3.1154 0.3341  -0.4831 -0.1535 892  SER B CB  
19054 O OG  . SER C 892  ? 2.4181 1.7307 3.1135 0.3174  -0.4284 -0.1224 892  SER B OG  
19055 N N   . SER C 893  ? 2.2797 1.4601 2.7506 0.3411  -0.5564 -0.1868 893  SER B N   
19056 C CA  . SER C 893  ? 2.3697 1.4936 2.7655 0.3489  -0.6086 -0.2059 893  SER B CA  
19057 C C   . SER C 893  ? 2.4089 1.4989 2.8141 0.3688  -0.6764 -0.2112 893  SER B C   
19058 O O   . SER C 893  ? 2.3879 1.4403 2.8262 0.3594  -0.6695 -0.1840 893  SER B O   
19059 C CB  . SER C 893  ? 2.4146 1.4443 2.7325 0.3132  -0.5672 -0.1830 893  SER B CB  
19060 O OG  . SER C 893  ? 2.4825 1.4758 2.7236 0.3202  -0.6121 -0.2065 893  SER B OG  
19061 N N   . HIS C 894  ? 2.1951 1.2988 2.5719 0.3966  -0.7424 -0.2465 894  HIS B N   
19062 C CA  . HIS C 894  ? 2.3420 1.4100 2.7183 0.4168  -0.8111 -0.2553 894  HIS B CA  
19063 C C   . HIS C 894  ? 2.2265 1.2013 2.5150 0.4060  -0.8373 -0.2557 894  HIS B C   
19064 O O   . HIS C 894  ? 2.2459 1.2286 2.4857 0.4152  -0.8619 -0.2819 894  HIS B O   
19065 C CB  . HIS C 894  ? 2.8080 1.9597 3.2230 0.4585  -0.8706 -0.2958 894  HIS B CB  
19066 C CG  . HIS C 894  ? 3.3894 2.5404 3.8528 0.4779  -0.9168 -0.2954 894  HIS B CG  
19067 N ND1 . HIS C 894  ? 3.7717 2.9132 4.2217 0.5067  -0.9911 -0.3225 894  HIS B ND1 
19068 C CD2 . HIS C 894  ? 3.5904 2.7471 4.1155 0.4721  -0.8996 -0.2705 894  HIS B CD2 
19069 C CE1 . HIS C 894  ? 4.0246 3.1655 4.5235 0.5177  -1.0171 -0.3148 894  HIS B CE1 
19070 N NE2 . HIS C 894  ? 3.8105 2.9606 4.3556 0.4968  -0.9634 -0.2830 894  HIS B NE2 
19071 N N   . LEU C 895  ? 3.1166 2.0021 3.3852 0.3848  -0.8308 -0.2252 895  LEU B N   
19072 C CA  . LEU C 895  ? 3.1262 1.9149 3.3122 0.3725  -0.8578 -0.2223 895  LEU B CA  
19073 C C   . LEU C 895  ? 3.0598 1.8677 3.2243 0.4063  -0.9367 -0.2616 895  LEU B C   
19074 O O   . LEU C 895  ? 3.0250 1.9055 3.2446 0.4394  -0.9757 -0.2861 895  LEU B O   
19075 C CB  . LEU C 895  ? 3.1633 1.8705 3.3519 0.3576  -0.8616 -0.1914 895  LEU B CB  
19076 C CG  . LEU C 895  ? 3.2191 1.8389 3.3613 0.3138  -0.7986 -0.1535 895  LEU B CG  
19077 C CD1 . LEU C 895  ? 3.1742 1.7681 3.3708 0.2997  -0.7697 -0.1184 895  LEU B CD1 
19078 C CD2 . LEU C 895  ? 3.3165 1.8391 3.3656 0.3021  -0.8319 -0.1552 895  LEU B CD2 
19079 N N   . VAL C 896  ? 2.6164 1.3582 2.7010 0.3977  -0.9605 -0.2676 896  VAL B N   
19080 C CA  . VAL C 896  ? 2.5622 1.3126 2.6251 0.4285  -1.0378 -0.3028 896  VAL B CA  
19081 C C   . VAL C 896  ? 2.6154 1.2552 2.6142 0.4158  -1.0740 -0.2901 896  VAL B C   
19082 O O   . VAL C 896  ? 2.6369 1.1981 2.6037 0.3818  -1.0342 -0.2559 896  VAL B O   
19083 C CB  . VAL C 896  ? 2.5355 1.3277 2.5621 0.4345  -1.0394 -0.3298 896  VAL B CB  
19084 C CG1 . VAL C 896  ? 2.5724 1.3975 2.6007 0.4732  -1.1194 -0.3697 896  VAL B CG1 
19085 C CG2 . VAL C 896  ? 2.4303 1.3153 2.5046 0.4340  -0.9833 -0.3333 896  VAL B CG2 
19086 N N   . THR C 897  ? 3.0080 1.6408 2.9899 0.4428  -1.1489 -0.3172 897  THR B N   
19087 C CA  . THR C 897  ? 3.0478 1.5754 2.9575 0.4302  -1.1871 -0.3089 897  THR B CA  
19088 C C   . THR C 897  ? 3.1225 1.6578 3.0123 0.4621  -1.2681 -0.3448 897  THR B C   
19089 O O   . THR C 897  ? 3.1046 1.7216 3.0491 0.4991  -1.3047 -0.3755 897  THR B O   
19090 C CB  . THR C 897  ? 2.9986 1.4551 2.9178 0.4191  -1.1932 -0.2804 897  THR B CB  
19091 O OG1 . THR C 897  ? 3.0310 1.4828 2.9629 0.4507  -1.2722 -0.3014 897  THR B OG1 
19092 C CG2 . THR C 897  ? 2.8924 1.3910 2.8859 0.4129  -1.1407 -0.2582 897  THR B CG2 
19093 N N   . PHE C 898  ? 3.0683 1.5151 2.8785 0.4459  -1.2942 -0.3399 898  PHE B N   
19094 C CA  . PHE C 898  ? 3.1269 1.5585 2.9082 0.4703  -1.3726 -0.3681 898  PHE B CA  
19095 C C   . PHE C 898  ? 3.1990 1.5058 2.9027 0.4437  -1.3929 -0.3457 898  PHE B C   
19096 O O   . PHE C 898  ? 3.2028 1.4432 2.8457 0.4044  -1.3461 -0.3195 898  PHE B O   
19097 C CB  . PHE C 898  ? 3.1641 1.6350 2.9150 0.4749  -1.3765 -0.3920 898  PHE B CB  
19098 C CG  . PHE C 898  ? 3.0851 1.6771 2.9026 0.4998  -1.3580 -0.4167 898  PHE B CG  
19099 C CD1 . PHE C 898  ? 3.0942 1.7531 2.9375 0.5377  -1.4123 -0.4563 898  PHE B CD1 
19100 C CD2 . PHE C 898  ? 3.0041 1.6421 2.8575 0.4844  -1.2856 -0.4004 898  PHE B CD2 
19101 C CE1 . PHE C 898  ? 3.0421 1.8106 2.9439 0.5594  -1.3946 -0.4794 898  PHE B CE1 
19102 C CE2 . PHE C 898  ? 2.9481 1.6955 2.8601 0.5060  -1.2692 -0.4227 898  PHE B CE2 
19103 C CZ  . PHE C 898  ? 2.9708 1.7836 2.9058 0.5432  -1.3232 -0.4625 898  PHE B CZ  
19104 N N   . THR C 899  ? 2.8410 1.1131 2.5432 0.4640  -1.4625 -0.3562 899  THR B N   
19105 C CA  . THR C 899  ? 2.8943 1.0478 2.5183 0.4399  -1.4885 -0.3378 899  THR B CA  
19106 C C   . THR C 899  ? 2.9433 1.0765 2.5183 0.4536  -1.5539 -0.3632 899  THR B C   
19107 O O   . THR C 899  ? 2.9227 1.1257 2.5402 0.4930  -1.6040 -0.3977 899  THR B O   
19108 C CB  . THR C 899  ? 2.9161 1.0208 2.5604 0.4443  -1.5168 -0.3233 899  THR B CB  
19109 O OG1 . THR C 899  ? 2.9329 1.0910 2.6291 0.4894  -1.5855 -0.3551 899  THR B OG1 
19110 C CG2 . THR C 899  ? 2.7762 0.8997 2.4709 0.4292  -1.4519 -0.2961 899  THR B CG2 
19111 N N   . VAL C 900  ? 3.3413 1.3773 2.8271 0.4196  -1.5515 -0.3453 900  VAL B N   
19112 C CA  . VAL C 900  ? 3.4238 1.4249 2.8512 0.4238  -1.6084 -0.3630 900  VAL B CA  
19113 C C   . VAL C 900  ? 3.4769 1.3452 2.8179 0.3913  -1.6280 -0.3379 900  VAL B C   
19114 O O   . VAL C 900  ? 3.4608 1.2646 2.7826 0.3623  -1.5893 -0.3062 900  VAL B O   
19115 C CB  . VAL C 900  ? 3.2348 1.2696 2.6308 0.4109  -1.5750 -0.3708 900  VAL B CB  
19116 C CG1 . VAL C 900  ? 3.2103 1.3657 2.6736 0.4528  -1.5977 -0.4092 900  VAL B CG1 
19117 C CG2 . VAL C 900  ? 3.1823 1.2107 2.5659 0.3743  -1.4835 -0.3421 900  VAL B CG2 
19118 N N   . LEU C 901  ? 3.2090 1.0370 2.4986 0.3957  -1.6885 -0.3523 901  LEU B N   
19119 C CA  . LEU C 901  ? 3.3634 1.0650 2.5668 0.3666  -1.7173 -0.3319 901  LEU B CA  
19120 C C   . LEU C 901  ? 3.5280 1.2015 2.6710 0.3660  -1.7681 -0.3480 901  LEU B C   
19121 O O   . LEU C 901  ? 3.5888 1.2988 2.7617 0.4025  -1.8378 -0.3771 901  LEU B O   
19122 C CB  . LEU C 901  ? 3.3398 1.0087 2.5704 0.3856  -1.7693 -0.3311 901  LEU B CB  
19123 C CG  . LEU C 901  ? 3.4523 1.0095 2.6118 0.3736  -1.8318 -0.3234 901  LEU B CG  
19124 C CD1 . LEU C 901  ? 3.4223 0.9051 2.5735 0.3552  -1.8203 -0.2945 901  LEU B CD1 
19125 C CD2 . LEU C 901  ? 3.5000 1.0931 2.6917 0.4182  -1.9211 -0.3583 901  LEU B CD2 
19126 N N   . PRO C 902  ? 3.3546 0.9636 2.4137 0.3240  -1.7323 -0.3291 902  PRO B N   
19127 C CA  . PRO C 902  ? 3.4648 1.0438 2.4600 0.3163  -1.7708 -0.3400 902  PRO B CA  
19128 C C   . PRO C 902  ? 3.6098 1.0731 2.5305 0.3013  -1.8339 -0.3305 902  PRO B C   
19129 O O   . PRO C 902  ? 3.6206 0.9973 2.5053 0.2769  -1.8236 -0.3044 902  PRO B O   
19130 C CB  . PRO C 902  ? 3.4862 1.0368 2.4203 0.2719  -1.6940 -0.3181 902  PRO B CB  
19131 C CG  . PRO C 902  ? 3.3013 0.8749 2.2758 0.2599  -1.6156 -0.2977 902  PRO B CG  
19132 C CD  . PRO C 902  ? 3.2758 0.8412 2.2995 0.2805  -1.6463 -0.2955 902  PRO B CD  
19133 N N   . LEU C 903  ? 3.9649 1.4279 2.8639 0.3155  -1.8985 -0.3513 903  LEU B N   
19134 C CA  . LEU C 903  ? 4.1077 1.4641 2.9329 0.3014  -1.9641 -0.3445 903  LEU B CA  
19135 C C   . LEU C 903  ? 4.2213 1.5330 2.9632 0.2705  -1.9625 -0.3397 903  LEU B C   
19136 O O   . LEU C 903  ? 4.3384 1.5455 2.9964 0.2448  -2.0020 -0.3271 903  LEU B O   
19137 C CB  . LEU C 903  ? 4.1183 1.5152 2.9991 0.3498  -2.0535 -0.3755 903  LEU B CB  
19138 C CG  . LEU C 903  ? 4.0151 1.4926 2.9975 0.3912  -2.0574 -0.3908 903  LEU B CG  
19139 C CD1 . LEU C 903  ? 3.9587 1.3809 2.9297 0.3654  -2.0078 -0.3595 903  LEU B CD1 
19140 C CD2 . LEU C 903  ? 3.9177 1.5294 2.9819 0.4203  -2.0217 -0.4146 903  LEU B CD2 
19141 N N   . GLU C 904  ? 4.1907 1.5829 2.9563 0.2734  -1.9181 -0.3500 904  GLU B N   
19142 C CA  . GLU C 904  ? 4.3271 1.6886 3.0191 0.2443  -1.9086 -0.3458 904  GLU B CA  
19143 C C   . GLU C 904  ? 4.2820 1.5920 2.9115 0.1943  -1.8187 -0.3145 904  GLU B C   
19144 O O   . GLU C 904  ? 4.1637 1.5462 2.8397 0.1966  -1.7505 -0.3139 904  GLU B O   
19145 C CB  . GLU C 904  ? 4.3809 1.8600 3.1338 0.2790  -1.9236 -0.3785 904  GLU B CB  
19146 C CG  . GLU C 904  ? 4.4656 1.9985 3.2865 0.3301  -2.0093 -0.4106 904  GLU B CG  
19147 C CD  . GLU C 904  ? 4.6056 2.1909 3.4351 0.3487  -2.0531 -0.4363 904  GLU B CD  
19148 O OE1 . GLU C 904  ? 4.6435 2.2440 3.4394 0.3267  -2.0122 -0.4322 904  GLU B OE1 
19149 O OE2 . GLU C 904  ? 4.6628 2.2736 3.5341 0.3856  -2.1288 -0.4605 904  GLU B OE2 
19150 N N   . ILE C 905  ? 4.1047 1.2861 2.6273 0.1491  -1.8214 -0.2888 905  ILE B N   
19151 C CA  . ILE C 905  ? 4.0136 1.1178 2.4585 0.0957  -1.7421 -0.2561 905  ILE B CA  
19152 C C   . ILE C 905  ? 3.9593 1.0930 2.3714 0.0770  -1.6996 -0.2581 905  ILE B C   
19153 O O   . ILE C 905  ? 3.9446 1.0590 2.3095 0.0722  -1.7442 -0.2672 905  ILE B O   
19154 C CB  . ILE C 905  ? 3.9367 0.8876 2.2690 0.0523  -1.7660 -0.2300 905  ILE B CB  
19155 C CG1 . ILE C 905  ? 3.9274 0.8465 2.2870 0.0743  -1.8287 -0.2322 905  ILE B CG1 
19156 C CG2 . ILE C 905  ? 3.9421 0.8135 2.2052 -0.0003 -1.6785 -0.1957 905  ILE B CG2 
19157 C CD1 . ILE C 905  ? 4.0411 0.8174 2.3076 0.0304  -1.8265 -0.2011 905  ILE B CD1 
19158 N N   . GLY C 906  ? 4.3113 1.4889 2.7476 0.0654  -1.6135 -0.2482 906  GLY B N   
19159 C CA  . GLY C 906  ? 4.3905 1.6101 2.8083 0.0513  -1.5666 -0.2514 906  GLY B CA  
19160 C C   . GLY C 906  ? 4.3429 1.7124 2.8679 0.0993  -1.5704 -0.2829 906  GLY B C   
19161 O O   . GLY C 906  ? 4.2848 1.7119 2.8220 0.0926  -1.5123 -0.2843 906  GLY B O   
19162 N N   . LEU C 907  ? 4.0368 1.4683 2.6390 0.1470  -1.6368 -0.3081 907  LEU B N   
19163 C CA  . LEU C 907  ? 4.0047 1.5765 2.7061 0.1942  -1.6487 -0.3412 907  LEU B CA  
19164 C C   . LEU C 907  ? 3.9126 1.5657 2.6772 0.1982  -1.5672 -0.3379 907  LEU B C   
19165 O O   . LEU C 907  ? 3.8355 1.4768 2.6283 0.1950  -1.5327 -0.3225 907  LEU B O   
19166 C CB  . LEU C 907  ? 4.0166 1.6365 2.7928 0.2443  -1.7272 -0.3674 907  LEU B CB  
19167 C CG  . LEU C 907  ? 4.0097 1.7762 2.8913 0.2926  -1.7325 -0.4017 907  LEU B CG  
19168 C CD1 . LEU C 907  ? 4.0716 1.8840 2.9361 0.2906  -1.7313 -0.4162 907  LEU B CD1 
19169 C CD2 . LEU C 907  ? 4.0474 1.8575 2.9994 0.3414  -1.8097 -0.4286 907  LEU B CD2 
19170 N N   . HIS C 908  ? 3.9250 1.6617 2.7135 0.2055  -1.5389 -0.3525 908  HIS B N   
19171 C CA  . HIS C 908  ? 3.8682 1.6731 2.7003 0.2009  -1.4555 -0.3466 908  HIS B CA  
19172 C C   . HIS C 908  ? 3.7862 1.7351 2.7265 0.2497  -1.4645 -0.3792 908  HIS B C   
19173 O O   . HIS C 908  ? 3.8136 1.8077 2.8061 0.2898  -1.5324 -0.4050 908  HIS B O   
19174 C CB  . HIS C 908  ? 3.9341 1.7096 2.6920 0.1605  -1.4004 -0.3326 908  HIS B CB  
19175 C CG  . HIS C 908  ? 4.0118 1.6570 2.6511 0.1186  -1.4201 -0.3131 908  HIS B CG  
19176 N ND1 . HIS C 908  ? 4.0745 1.6867 2.6778 0.1268  -1.5012 -0.3265 908  HIS B ND1 
19177 C CD2 . HIS C 908  ? 4.0243 1.5649 2.5712 0.0666  -1.3671 -0.2814 908  HIS B CD2 
19178 C CE1 . HIS C 908  ? 4.1586 1.6497 2.6513 0.0813  -1.4995 -0.3031 908  HIS B CE1 
19179 N NE2 . HIS C 908  ? 4.1279 1.5723 2.5826 0.0438  -1.4179 -0.2759 908  HIS B NE2 
19180 N N   . ASN C 909  ? 3.8307 1.8485 2.8023 0.2447  -1.3945 -0.3776 909  ASN B N   
19181 C CA  . ASN C 909  ? 3.7437 1.8980 2.8066 0.2842  -1.3926 -0.4074 909  ASN B CA  
19182 C C   . ASN C 909  ? 3.6002 1.8291 2.7634 0.3285  -1.4195 -0.4257 909  ASN B C   
19183 O O   . ASN C 909  ? 3.6017 1.8171 2.7808 0.3536  -1.4897 -0.4396 909  ASN B O   
19184 C CB  . ASN C 909  ? 3.8750 2.0692 2.9279 0.3004  -1.4428 -0.4340 909  ASN B CB  
19185 C CG  . ASN C 909  ? 3.8735 2.2061 3.0271 0.3482  -1.4581 -0.4693 909  ASN B CG  
19186 O OD1 . ASN C 909  ? 3.9304 2.3012 3.1148 0.3818  -1.5266 -0.4970 909  ASN B OD1 
19187 N ND2 . ASN C 909  ? 3.7994 2.2066 3.0054 0.3512  -1.3939 -0.4682 909  ASN B ND2 
19188 N N   . ILE C 910  ? 3.1702 1.4782 2.4003 0.3376  -1.3637 -0.4259 910  ILE B N   
19189 C CA  . ILE C 910  ? 3.0066 1.4021 2.3365 0.3801  -1.3825 -0.4458 910  ILE B CA  
19190 C C   . ILE C 910  ? 2.9435 1.4463 2.3309 0.3883  -1.3248 -0.4551 910  ILE B C   
19191 O O   . ILE C 910  ? 2.9646 1.4567 2.3398 0.3592  -1.2517 -0.4313 910  ILE B O   
19192 C CB  . ILE C 910  ? 2.8615 1.2047 2.2072 0.3741  -1.3729 -0.4234 910  ILE B CB  
19193 C CG1 . ILE C 910  ? 2.8732 1.1340 2.1831 0.3794  -1.4461 -0.4237 910  ILE B CG1 
19194 C CG2 . ILE C 910  ? 2.7313 1.1707 2.1796 0.4085  -1.3656 -0.4372 910  ILE B CG2 
19195 C CD1 . ILE C 910  ? 2.8133 1.0052 2.1218 0.3663  -1.4358 -0.3978 910  ILE B CD1 
19196 N N   . ASN C 911  ? 3.4188 2.0236 2.8671 0.4271  -1.3571 -0.4900 911  ASN B N   
19197 C CA  . ASN C 911  ? 3.2887 2.0020 2.7953 0.4382  -1.3086 -0.5024 911  ASN B CA  
19198 C C   . ASN C 911  ? 3.1969 1.9788 2.7942 0.4647  -1.2967 -0.5082 911  ASN B C   
19199 O O   . ASN C 911  ? 3.1623 1.9842 2.8124 0.5024  -1.3521 -0.5323 911  ASN B O   
19200 C CB  . ASN C 911  ? 3.2833 2.0742 2.8070 0.4639  -1.3439 -0.5369 911  ASN B CB  
19201 C CG  . ASN C 911  ? 3.3412 2.0666 2.7779 0.4394  -1.3629 -0.5323 911  ASN B CG  
19202 O OD1 . ASN C 911  ? 3.4328 2.0674 2.8147 0.4290  -1.4074 -0.5233 911  ASN B OD1 
19203 N ND2 . ASN C 911  ? 3.3443 2.1166 2.7684 0.4300  -1.3309 -0.5385 911  ASN B ND2 
19204 N N   . PHE C 912  ? 3.0482 1.8416 2.6631 0.4443  -1.2249 -0.4856 912  PHE B N   
19205 C CA  . PHE C 912  ? 2.9383 1.7943 2.6370 0.4647  -1.2082 -0.4873 912  PHE B CA  
19206 C C   . PHE C 912  ? 2.9210 1.9011 2.6855 0.4864  -1.1831 -0.5107 912  PHE B C   
19207 O O   . PHE C 912  ? 2.9519 1.9577 2.6930 0.4706  -1.1438 -0.5105 912  PHE B O   
19208 C CB  . PHE C 912  ? 2.8359 1.6319 2.5249 0.4315  -1.1483 -0.4478 912  PHE B CB  
19209 C CG  . PHE C 912  ? 2.8028 1.4931 2.4532 0.4196  -1.1789 -0.4280 912  PHE B CG  
19210 C CD1 . PHE C 912  ? 2.7465 1.4436 2.4477 0.4456  -1.2208 -0.4342 912  PHE B CD1 
19211 C CD2 . PHE C 912  ? 2.8460 1.4284 2.4070 0.3813  -1.1656 -0.4032 912  PHE B CD2 
19212 C CE1 . PHE C 912  ? 2.7538 1.3539 2.4191 0.4344  -1.2494 -0.4160 912  PHE B CE1 
19213 C CE2 . PHE C 912  ? 2.8549 1.3390 2.3786 0.3694  -1.1937 -0.3851 912  PHE B CE2 
19214 C CZ  . PHE C 912  ? 2.8026 1.2966 2.3794 0.3962  -1.2356 -0.3914 912  PHE B CZ  
19215 N N   . SER C 913  ? 3.0296 2.0828 2.8737 0.5212  -1.2051 -0.5301 913  SER B N   
19216 C CA  . SER C 913  ? 3.0147 2.1881 2.9256 0.5466  -1.1915 -0.5566 913  SER B CA  
19217 C C   . SER C 913  ? 2.9885 2.2149 2.9776 0.5617  -1.1737 -0.5543 913  SER B C   
19218 O O   . SER C 913  ? 2.9619 2.1627 2.9742 0.5768  -1.2114 -0.5540 913  SER B O   
19219 C CB  . SER C 913  ? 3.0517 2.2764 2.9782 0.5836  -1.2582 -0.5975 913  SER B CB  
19220 O OG  . SER C 913  ? 2.9906 2.3300 2.9803 0.6090  -1.2478 -0.6251 913  SER B OG  
19221 N N   . LEU C 914  ? 2.7394 2.0372 2.7675 0.5565  -1.1171 -0.5518 914  LEU B N   
19222 C CA  . LEU C 914  ? 2.7037 2.0620 2.8090 0.5714  -1.1010 -0.5518 914  LEU B CA  
19223 C C   . LEU C 914  ? 2.7829 2.2594 2.9437 0.5984  -1.0997 -0.5847 914  LEU B C   
19224 O O   . LEU C 914  ? 2.8386 2.3508 2.9780 0.5975  -1.0910 -0.5999 914  LEU B O   
19225 C CB  . LEU C 914  ? 2.5536 1.8800 2.6630 0.5373  -1.0309 -0.5116 914  LEU B CB  
19226 C CG  . LEU C 914  ? 2.4546 1.7852 2.5370 0.5043  -0.9574 -0.4922 914  LEU B CG  
19227 C CD1 . LEU C 914  ? 2.3941 1.8367 2.5213 0.5198  -0.9361 -0.5160 914  LEU B CD1 
19228 C CD2 . LEU C 914  ? 2.3710 1.6539 2.4599 0.4725  -0.8967 -0.4506 914  LEU B CD2 
19229 N N   . GLU C 915  ? 3.1074 2.6427 3.3378 0.6218  -1.1091 -0.5957 915  GLU B N   
19230 C CA  . GLU C 915  ? 3.1767 2.8216 3.4598 0.6501  -1.1151 -0.6300 915  GLU B CA  
19231 C C   . GLU C 915  ? 3.1374 2.8423 3.4848 0.6499  -1.0744 -0.6213 915  GLU B C   
19232 O O   . GLU C 915  ? 3.0745 2.7539 3.4505 0.6498  -1.0786 -0.6050 915  GLU B O   
19233 C CB  . GLU C 915  ? 3.2452 2.9142 3.5488 0.6903  -1.1900 -0.6674 915  GLU B CB  
19234 C CG  . GLU C 915  ? 3.3792 3.0397 3.6384 0.6989  -1.2270 -0.6899 915  GLU B CG  
19235 C CD  . GLU C 915  ? 3.4807 3.0610 3.7055 0.7078  -1.2899 -0.6918 915  GLU B CD  
19236 O OE1 . GLU C 915  ? 3.4620 3.0241 3.7152 0.7237  -1.3224 -0.6926 915  GLU B OE1 
19237 O OE2 . GLU C 915  ? 3.5782 3.1126 3.7466 0.6982  -1.3080 -0.6921 915  GLU B OE2 
19238 N N   . THR C 916  ? 3.1738 2.9582 3.5432 0.6491  -1.0363 -0.6320 916  THR B N   
19239 C CA  . THR C 916  ? 3.1787 3.0266 3.6080 0.6474  -0.9952 -0.6248 916  THR B CA  
19240 C C   . THR C 916  ? 3.2861 3.2407 3.7513 0.6707  -0.9975 -0.6608 916  THR B C   
19241 O O   . THR C 916  ? 3.3465 3.3230 3.7841 0.6791  -1.0127 -0.6840 916  THR B O   
19242 C CB  . THR C 916  ? 3.1122 2.9341 3.5264 0.6081  -0.9212 -0.5863 916  THR B CB  
19243 O OG1 . THR C 916  ? 3.1087 2.8290 3.4883 0.5849  -0.9158 -0.5523 916  THR B OG1 
19244 C CG2 . THR C 916  ? 3.0111 2.8995 3.4916 0.6065  -0.8811 -0.5780 916  THR B CG2 
19245 N N   . TRP C 917  ? 3.7798 3.7990 4.3063 0.6799  -0.9824 -0.6646 917  TRP B N   
19246 C CA  . TRP C 917  ? 3.8660 3.9879 4.4312 0.7019  -0.9837 -0.6985 917  TRP B CA  
19247 C C   . TRP C 917  ? 3.9576 4.1094 4.4884 0.6931  -0.9588 -0.7090 917  TRP B C   
19248 O O   . TRP C 917  ? 3.9880 4.1821 4.5152 0.7163  -0.9925 -0.7439 917  TRP B O   
19249 C CB  . TRP C 917  ? 3.8401 4.0156 4.4621 0.6955  -0.9439 -0.6864 917  TRP B CB  
19250 C CG  . TRP C 917  ? 3.8519 4.1156 4.5248 0.7265  -0.9694 -0.7226 917  TRP B CG  
19251 C CD1 . TRP C 917  ? 3.7704 4.1229 4.4689 0.7315  -0.9440 -0.7419 917  TRP B CD1 
19252 C CD2 . TRP C 917  ? 3.8637 4.1340 4.5660 0.7565  -1.0254 -0.7447 917  TRP B CD2 
19253 N NE1 . TRP C 917  ? 3.7117 4.1250 4.4532 0.7622  -0.9798 -0.7748 917  TRP B NE1 
19254 C CE2 . TRP C 917  ? 3.7660 4.1299 4.5103 0.7782  -1.0298 -0.7773 917  TRP B CE2 
19255 C CE3 . TRP C 917  ? 3.9509 4.1553 4.6467 0.7666  -1.0718 -0.7402 917  TRP B CE3 
19256 C CZ2 . TRP C 917  ? 3.7516 4.1438 4.5303 0.8091  -1.0778 -0.8057 917  TRP B CZ2 
19257 C CZ3 . TRP C 917  ? 3.9128 4.1463 4.6438 0.7979  -1.1203 -0.7681 917  TRP B CZ3 
19258 C CH2 . TRP C 917  ? 3.8259 4.1518 4.5973 0.8187  -1.1223 -0.8006 917  TRP B CH2 
19259 N N   . PHE C 918  ? 3.1154 3.2436 3.6214 0.6592  -0.8997 -0.6783 918  PHE B N   
19260 C CA  . PHE C 918  ? 3.1930 3.3502 3.6662 0.6478  -0.8705 -0.6856 918  PHE B CA  
19261 C C   . PHE C 918  ? 3.1831 3.2583 3.5812 0.6274  -0.8721 -0.6716 918  PHE B C   
19262 O O   . PHE C 918  ? 3.2109 3.2918 3.5745 0.6081  -0.8358 -0.6663 918  PHE B O   
19263 C CB  . PHE C 918  ? 3.2233 3.4298 3.7212 0.6266  -0.8019 -0.6687 918  PHE B CB  
19264 C CG  . PHE C 918  ? 3.2380 3.3834 3.7327 0.5939  -0.7529 -0.6234 918  PHE B CG  
19265 C CD1 . PHE C 918  ? 3.2964 3.3829 3.7369 0.5606  -0.7091 -0.5961 918  PHE B CD1 
19266 C CD2 . PHE C 918  ? 3.1900 3.3390 3.7374 0.5957  -0.7483 -0.6083 918  PHE B CD2 
19267 C CE1 . PHE C 918  ? 3.2662 3.2977 3.7065 0.5307  -0.6609 -0.5551 918  PHE B CE1 
19268 C CE2 . PHE C 918  ? 3.1574 3.2531 3.7073 0.5659  -0.7019 -0.5663 918  PHE B CE2 
19269 C CZ  . PHE C 918  ? 3.1945 3.2319 3.6919 0.5337  -0.6573 -0.5401 918  PHE B CZ  
19270 N N   . GLY C 919  ? 3.5045 3.5029 3.8752 0.6313  -0.9155 -0.6662 919  GLY B N   
19271 C CA  . GLY C 919  ? 3.4825 3.3971 3.7789 0.6101  -0.9187 -0.6515 919  GLY B CA  
19272 C C   . GLY C 919  ? 3.4652 3.3057 3.7322 0.6211  -0.9801 -0.6547 919  GLY B C   
19273 O O   . GLY C 919  ? 3.4212 3.2586 3.7242 0.6418  -1.0171 -0.6612 919  GLY B O   
19274 N N   . LYS C 920  ? 3.4301 3.2088 3.6292 0.6060  -0.9908 -0.6495 920  LYS B N   
19275 C CA  . LYS C 920  ? 3.4143 3.1106 3.5731 0.6103  -1.0460 -0.6486 920  LYS B CA  
19276 C C   . LYS C 920  ? 3.4028 3.0184 3.4786 0.5756  -1.0258 -0.6262 920  LYS B C   
19277 O O   . LYS C 920  ? 3.4660 3.1078 3.5141 0.5704  -1.0168 -0.6374 920  LYS B O   
19278 C CB  . LYS C 920  ? 3.4377 3.1799 3.6180 0.6499  -1.1149 -0.6902 920  LYS B CB  
19279 C CG  . LYS C 920  ? 3.4791 3.1433 3.6267 0.6593  -1.1789 -0.6926 920  LYS B CG  
19280 C CD  . LYS C 920  ? 3.4765 3.1969 3.6663 0.7035  -1.2445 -0.7345 920  LYS B CD  
19281 C CE  . LYS C 920  ? 3.5234 3.1675 3.6791 0.7129  -1.3101 -0.7381 920  LYS B CE  
19282 N NZ  . LYS C 920  ? 3.5233 3.2124 3.7315 0.7564  -1.3706 -0.7735 920  LYS B NZ  
19283 N N   . GLU C 921  ? 3.7905 3.3068 3.8257 0.5509  -1.0182 -0.5944 921  GLU B N   
19284 C CA  . GLU C 921  ? 3.7559 3.1876 3.7108 0.5113  -0.9854 -0.5667 921  GLU B CA  
19285 C C   . GLU C 921  ? 3.7220 3.0483 3.6176 0.5041  -1.0335 -0.5574 921  GLU B C   
19286 O O   . GLU C 921  ? 3.6917 2.9924 3.6106 0.5202  -1.0726 -0.5581 921  GLU B O   
19287 C CB  . GLU C 921  ? 3.7344 3.1421 3.6924 0.4788  -0.9099 -0.5303 921  GLU B CB  
19288 C CG  . GLU C 921  ? 3.8221 3.1724 3.7080 0.4375  -0.8565 -0.5055 921  GLU B CG  
19289 C CD  . GLU C 921  ? 3.8390 3.2666 3.7441 0.4302  -0.8008 -0.5094 921  GLU B CD  
19290 O OE1 . GLU C 921  ? 3.8347 3.3626 3.7978 0.4593  -0.8147 -0.5379 921  GLU B OE1 
19291 O OE2 . GLU C 921  ? 3.8583 3.2444 3.7187 0.3946  -0.7425 -0.4841 921  GLU B OE2 
19292 N N   . ILE C 922  ? 3.0975 2.3614 2.9151 0.4792  -1.0313 -0.5484 922  ILE B N   
19293 C CA  . ILE C 922  ? 3.0625 2.2230 2.8161 0.4692  -1.0770 -0.5392 922  ILE B CA  
19294 C C   . ILE C 922  ? 3.0123 2.0699 2.6834 0.4215  -1.0316 -0.5026 922  ILE B C   
19295 O O   . ILE C 922  ? 3.0404 2.0853 2.6580 0.4000  -1.0088 -0.4996 922  ILE B O   
19296 C CB  . ILE C 922  ? 3.1089 2.2811 2.8394 0.4892  -1.1417 -0.5688 922  ILE B CB  
19297 C CG1 . ILE C 922  ? 3.0682 2.3012 2.8667 0.5361  -1.2054 -0.6018 922  ILE B CG1 
19298 C CG2 . ILE C 922  ? 3.2055 2.2611 2.8503 0.4655  -1.1720 -0.5522 922  ILE B CG2 
19299 C CD1 . ILE C 922  ? 3.1352 2.3535 2.9097 0.5552  -1.2784 -0.6257 922  ILE B CD1 
19300 N N   . LEU C 923  ? 3.3763 2.3585 3.0357 0.4044  -1.0186 -0.4750 923  LEU B N   
19301 C CA  . LEU C 923  ? 3.3995 2.2724 2.9769 0.3593  -0.9806 -0.4405 923  LEU B CA  
19302 C C   . LEU C 923  ? 3.4825 2.2595 2.9963 0.3547  -1.0415 -0.4385 923  LEU B C   
19303 O O   . LEU C 923  ? 3.4975 2.2537 3.0367 0.3733  -1.0866 -0.4414 923  LEU B O   
19304 C CB  . LEU C 923  ? 3.3058 2.1499 2.9075 0.3398  -0.9237 -0.4089 923  LEU B CB  
19305 C CG  . LEU C 923  ? 3.3342 2.0507 2.8690 0.3052  -0.9125 -0.3756 923  LEU B CG  
19306 C CD1 . LEU C 923  ? 3.4164 2.0595 2.8558 0.2648  -0.8782 -0.3591 923  LEU B CD1 
19307 C CD2 . LEU C 923  ? 3.2435 1.9515 2.8228 0.2932  -0.8596 -0.3483 923  LEU B CD2 
19308 N N   . VAL C 924  ? 2.9681 1.6851 2.3982 0.3294  -1.0439 -0.4332 924  VAL B N   
19309 C CA  . VAL C 924  ? 3.0216 1.6429 2.3857 0.3220  -1.1021 -0.4299 924  VAL B CA  
19310 C C   . VAL C 924  ? 2.9836 1.4801 2.2729 0.2780  -1.0685 -0.3920 924  VAL B C   
19311 O O   . VAL C 924  ? 2.9453 1.4105 2.1955 0.2424  -0.9999 -0.3689 924  VAL B O   
19312 C CB  . VAL C 924  ? 3.1066 1.7278 2.4218 0.3235  -1.1433 -0.4488 924  VAL B CB  
19313 C CG1 . VAL C 924  ? 3.1812 1.7531 2.4778 0.3406  -1.2274 -0.4603 924  VAL B CG1 
19314 C CG2 . VAL C 924  ? 3.0788 1.8257 2.4572 0.3543  -1.1454 -0.4802 924  VAL B CG2 
19315 N N   . LYS C 925  ? 2.9571 1.3817 2.2262 0.2810  -1.1190 -0.3868 925  LYS B N   
19316 C CA  . LYS C 925  ? 2.9368 1.2415 2.1411 0.2430  -1.0950 -0.3523 925  LYS B CA  
19317 C C   . LYS C 925  ? 3.0185 1.2245 2.1431 0.2325  -1.1585 -0.3512 925  LYS B C   
19318 O O   . LYS C 925  ? 3.1214 1.3548 2.2495 0.2581  -1.2254 -0.3774 925  LYS B O   
19319 C CB  . LYS C 925  ? 2.8243 1.1318 2.0907 0.2542  -1.0861 -0.3406 925  LYS B CB  
19320 C CG  . LYS C 925  ? 2.7508 1.0110 2.0043 0.2175  -1.0046 -0.3049 925  LYS B CG  
19321 C CD  . LYS C 925  ? 2.6685 1.0199 1.9771 0.2191  -0.9385 -0.3060 925  LYS B CD  
19322 C CE  . LYS C 925  ? 2.6234 0.9367 1.9404 0.1894  -0.8623 -0.2713 925  LYS B CE  
19323 N NZ  . LYS C 925  ? 2.5886 0.9496 1.9147 0.1724  -0.7863 -0.2643 925  LYS B NZ  
19324 N N   . THR C 926  ? 3.2134 1.3036 2.2681 0.1948  -1.1378 -0.3203 926  THR B N   
19325 C CA  . THR C 926  ? 3.2483 1.2331 2.2151 0.1769  -1.1900 -0.3147 926  THR B CA  
19326 C C   . THR C 926  ? 3.2348 1.1097 2.1616 0.1509  -1.1817 -0.2851 926  THR B C   
19327 O O   . THR C 926  ? 3.2062 1.0361 2.1098 0.1175  -1.1104 -0.2569 926  THR B O   
19328 C CB  . THR C 926  ? 3.6794 1.6210 2.5587 0.1418  -1.1641 -0.3073 926  THR B CB  
19329 O OG1 . THR C 926  ? 3.6266 1.5949 2.5134 0.1198  -1.0749 -0.2919 926  THR B OG1 
19330 C CG2 . THR C 926  ? 3.6773 1.6923 2.5723 0.1696  -1.2158 -0.3398 926  THR B CG2 
19331 N N   . LEU C 927  ? 2.9669 0.7982 1.8859 0.1662  -1.2547 -0.2917 927  LEU B N   
19332 C CA  . LEU C 927  ? 3.0247 0.7664 1.9231 0.1503  -1.2567 -0.2678 927  LEU B CA  
19333 C C   . LEU C 927  ? 3.1512 0.7610 1.9366 0.1144  -1.2842 -0.2514 927  LEU B C   
19334 O O   . LEU C 927  ? 3.1909 0.7869 1.9453 0.1257  -1.3527 -0.2687 927  LEU B O   
19335 C CB  . LEU C 927  ? 2.9856 0.7731 1.9615 0.1951  -1.3214 -0.2868 927  LEU B CB  
19336 C CG  . LEU C 927  ? 3.0252 0.7458 2.0065 0.1935  -1.3413 -0.2699 927  LEU B CG  
19337 C CD1 . LEU C 927  ? 3.0044 0.7661 2.0408 0.2400  -1.4277 -0.2975 927  LEU B CD1 
19338 C CD2 . LEU C 927  ? 3.1470 0.7253 2.0215 0.1487  -1.3404 -0.2420 927  LEU B CD2 
19339 N N   . ARG C 928  ? 3.8432 1.3546 2.5684 0.0713  -1.2323 -0.2181 928  ARG B N   
19340 C CA  . ARG C 928  ? 3.9548 1.3305 2.5654 0.0320  -1.2523 -0.1995 928  ARG B CA  
19341 C C   . ARG C 928  ? 3.9999 1.3068 2.6038 0.0388  -1.3110 -0.1938 928  ARG B C   
19342 O O   . ARG C 928  ? 3.9579 1.2394 2.5874 0.0324  -1.2810 -0.1751 928  ARG B O   
19343 C CB  . ARG C 928  ? 3.9809 1.2774 2.5187 -0.0219 -1.1640 -0.1668 928  ARG B CB  
19344 C CG  . ARG C 928  ? 4.0645 1.3808 2.5579 -0.0424 -1.1211 -0.1696 928  ARG B CG  
19345 C CD  . ARG C 928  ? 4.1100 1.4116 2.5915 -0.0775 -1.0158 -0.1441 928  ARG B CD  
19346 N NE  . ARG C 928  ? 4.0860 1.4989 2.6810 -0.0491 -0.9741 -0.1496 928  ARG B NE  
19347 C CZ  . ARG C 928  ? 4.0718 1.5817 2.7138 -0.0375 -0.9340 -0.1613 928  ARG B CZ  
19348 N NH1 . ARG C 928  ? 4.1441 1.6551 2.7300 -0.0520 -0.9275 -0.1689 928  ARG B NH1 
19349 N NH2 . ARG C 928  ? 3.9339 1.5385 2.6782 -0.0125 -0.9005 -0.1649 928  ARG B NH2 
19350 N N   . VAL C 929  ? 3.4751 0.7508 2.0450 0.0511  -1.3946 -0.2091 929  VAL B N   
19351 C CA  . VAL C 929  ? 3.5087 0.7215 2.0717 0.0600  -1.4582 -0.2063 929  VAL B CA  
19352 C C   . VAL C 929  ? 3.6468 0.7091 2.0857 0.0129  -1.4718 -0.1822 929  VAL B C   
19353 O O   . VAL C 929  ? 3.7057 0.7267 2.0692 -0.0073 -1.4890 -0.1842 929  VAL B O   
19354 C CB  . VAL C 929  ? 3.5421 0.8293 2.1684 0.1127  -1.5488 -0.2416 929  VAL B CB  
19355 C CG1 . VAL C 929  ? 3.5404 0.7916 2.1912 0.1313  -1.6048 -0.2410 929  VAL B CG1 
19356 C CG2 . VAL C 929  ? 3.4198 0.8521 2.1521 0.1532  -1.5302 -0.2665 929  VAL B CG2 
19357 N N   . VAL C 930  ? 3.9290 0.9103 2.3477 -0.0047 -1.4654 -0.1597 930  VAL B N   
19358 C CA  . VAL C 930  ? 4.0720 0.9055 2.3737 -0.0548 -1.4615 -0.1321 930  VAL B CA  
19359 C C   . VAL C 930  ? 4.1811 0.9485 2.4699 -0.0457 -1.5359 -0.1309 930  VAL B C   
19360 O O   . VAL C 930  ? 4.1683 1.0030 2.5425 -0.0022 -1.5801 -0.1484 930  VAL B O   
19361 C CB  . VAL C 930  ? 4.0578 0.8394 2.3396 -0.0935 -1.3680 -0.0995 930  VAL B CB  
19362 C CG1 . VAL C 930  ? 4.1731 0.8093 2.3204 -0.1530 -1.3432 -0.0723 930  VAL B CG1 
19363 C CG2 . VAL C 930  ? 3.9729 0.8526 2.3168 -0.0872 -1.2911 -0.1023 930  VAL B CG2 
19364 N N   . PRO C 931  ? 3.2587 1.2705 2.3755 -0.0168 -1.5447 0.3025  931  PRO B N   
19365 C CA  . PRO C 931  ? 3.2958 1.2956 2.4152 -0.0268 -1.5742 0.2997  931  PRO B CA  
19366 C C   . PRO C 931  ? 3.2105 1.2309 2.4008 -0.0440 -1.5810 0.3158  931  PRO B C   
19367 O O   . PRO C 931  ? 3.2124 1.2489 2.4439 -0.0463 -1.5750 0.3321  931  PRO B O   
19368 C CB  . PRO C 931  ? 3.2635 1.2681 2.3629 -0.0270 -1.5515 0.2812  931  PRO B CB  
19369 C CG  . PRO C 931  ? 3.2227 1.2410 2.3061 -0.0167 -1.5116 0.2743  931  PRO B CG  
19370 C CD  . PRO C 931  ? 3.1945 1.2283 2.3159 -0.0171 -1.5015 0.2914  931  PRO B CD  
19371 N N   . GLU C 932  ? 3.2978 1.3178 2.5022 -0.0557 -1.5921 0.3111  932  GLU B N   
19372 C CA  . GLU C 932  ? 3.2930 1.3216 2.5521 -0.0715 -1.6125 0.3250  932  GLU B CA  
19373 C C   . GLU C 932  ? 3.1912 1.2425 2.4963 -0.0869 -1.5929 0.3223  932  GLU B C   
19374 O O   . GLU C 932  ? 3.1496 1.1893 2.4353 -0.0910 -1.6031 0.3105  932  GLU B O   
19375 C CB  . GLU C 932  ? 3.3811 1.3778 2.6066 -0.0722 -1.6591 0.3230  932  GLU B CB  
19376 C CG  . GLU C 932  ? 3.4677 1.4328 2.6235 -0.0559 -1.6778 0.3163  932  GLU B CG  
19377 C CD  . GLU C 932  ? 3.4814 1.4316 2.5780 -0.0449 -1.6633 0.2951  932  GLU B CD  
19378 O OE1 . GLU C 932  ? 3.4291 1.3998 2.5368 -0.0451 -1.6277 0.2871  932  GLU B OE1 
19379 O OE2 . GLU C 932  ? 3.5464 1.4643 2.5845 -0.0360 -1.6874 0.2866  932  GLU B OE2 
19380 N N   . GLY C 933  ? 3.1657 1.2477 2.5313 -0.0959 -1.5655 0.3336  933  GLY B N   
19381 C CA  . GLY C 933  ? 3.1271 1.2309 2.5382 -0.1117 -1.5451 0.3317  933  GLY B CA  
19382 C C   . GLY C 933  ? 3.0579 1.1856 2.4780 -0.1123 -1.4969 0.3239  933  GLY B C   
19383 O O   . GLY C 933  ? 3.0098 1.1403 2.4188 -0.1166 -1.4840 0.3105  933  GLY B O   
19384 N N   . VAL C 934  ? 3.2409 1.3862 2.6813 -0.1082 -1.4699 0.3328  934  VAL B N   
19385 C CA  . VAL C 934  ? 3.2684 1.4368 2.7166 -0.1088 -1.4225 0.3266  934  VAL B CA  
19386 C C   . VAL C 934  ? 3.1824 1.3761 2.6874 -0.1279 -1.3989 0.3290  934  VAL B C   
19387 O O   . VAL C 934  ? 3.1315 1.3407 2.6950 -0.1389 -1.3953 0.3447  934  VAL B O   
19388 C CB  . VAL C 934  ? 3.3523 1.5323 2.8114 -0.1006 -1.3998 0.3374  934  VAL B CB  
19389 C CG1 . VAL C 934  ? 2.8614 1.0675 2.3357 -0.1041 -1.3487 0.3325  934  VAL B CG1 
19390 C CG2 . VAL C 934  ? 3.4620 1.6174 2.8603 -0.0813 -1.4173 0.3329  934  VAL B CG2 
19391 N N   . LYS C 935  ? 3.0724 1.2700 2.5599 -0.1317 -1.3828 0.3135  935  LYS B N   
19392 C CA  . LYS C 935  ? 3.0343 1.2571 2.5688 -0.1493 -1.3532 0.3134  935  LYS B CA  
19393 C C   . LYS C 935  ? 3.0511 1.2889 2.5618 -0.1456 -1.3114 0.3005  935  LYS B C   
19394 O O   . LYS C 935  ? 3.0617 1.2861 2.5146 -0.1327 -1.3145 0.2861  935  LYS B O   
19395 C CB  . LYS C 935  ? 3.0505 1.2643 2.5913 -0.1608 -1.3768 0.3077  935  LYS B CB  
19396 C CG  . LYS C 935  ? 2.6365 0.8636 2.2465 -0.1805 -1.3806 0.3209  935  LYS B CG  
19397 C CD  . LYS C 935  ? 2.7282 0.9628 2.3805 -0.1812 -1.3843 0.3407  935  LYS B CD  
19398 C CE  . LYS C 935  ? 2.7176 0.9763 2.4447 -0.2010 -1.3648 0.3530  935  LYS B CE  
19399 N NZ  . LYS C 935  ? 2.7658 1.0182 2.5278 -0.2142 -1.3963 0.3599  935  LYS B NZ  
19400 N N   . ARG C 936  ? 2.8121 1.0773 2.3656 -0.1568 -1.2719 0.3056  936  ARG B N   
19401 C CA  . ARG C 936  ? 2.8124 1.0927 2.3431 -0.1551 -1.2326 0.2929  936  ARG B CA  
19402 C C   . ARG C 936  ? 2.7910 1.0938 2.3594 -0.1747 -1.2053 0.2900  936  ARG B C   
19403 O O   . ARG C 936  ? 2.7951 1.1144 2.4219 -0.1899 -1.1909 0.3023  936  ARG B O   
19404 C CB  . ARG C 936  ? 2.8038 1.0946 2.3307 -0.1462 -1.2031 0.2977  936  ARG B CB  
19405 C CG  . ARG C 936  ? 2.7795 1.0942 2.3690 -0.1595 -1.1730 0.3126  936  ARG B CG  
19406 C CD  . ARG C 936  ? 2.8483 1.1633 2.4325 -0.1471 -1.1610 0.3216  936  ARG B CD  
19407 N NE  . ARG C 936  ? 2.8645 1.2027 2.4608 -0.1514 -1.1108 0.3208  936  ARG B NE  
19408 C CZ  . ARG C 936  ? 2.9115 1.2524 2.5008 -0.1413 -1.0916 0.3265  936  ARG B CZ  
19409 N NH1 . ARG C 936  ? 2.9571 1.2794 2.5279 -0.1262 -1.1192 0.3337  936  ARG B NH1 
19410 N NH2 . ARG C 936  ? 2.8883 1.2501 2.4881 -0.1467 -1.0446 0.3250  936  ARG B NH2 
19411 N N   . GLU C 937  ? 3.4553 1.7580 2.9884 -0.1739 -1.1984 0.2737  937  GLU B N   
19412 C CA  . GLU C 937  ? 3.5216 1.8430 3.0795 -0.1915 -1.1756 0.2680  937  GLU B CA  
19413 C C   . GLU C 937  ? 3.5562 1.8960 3.0886 -0.1897 -1.1349 0.2562  937  GLU B C   
19414 O O   . GLU C 937  ? 3.5072 1.8386 2.9863 -0.1777 -1.1392 0.2419  937  GLU B O   
19415 C CB  . GLU C 937  ? 3.6955 2.0003 3.2369 -0.1940 -1.2075 0.2596  937  GLU B CB  
19416 C CG  . GLU C 937  ? 4.3628 2.6488 3.8344 -0.1761 -1.2231 0.2439  937  GLU B CG  
19417 C CD  . GLU C 937  ? 4.5394 2.8018 3.9933 -0.1757 -1.2629 0.2387  937  GLU B CD  
19418 O OE1 . GLU C 937  ? 4.5677 2.8111 4.0285 -0.1735 -1.2971 0.2471  937  GLU B OE1 
19419 O OE2 . GLU C 937  ? 4.5356 2.7984 3.9677 -0.1775 -1.2597 0.2264  937  GLU B OE2 
19420 N N   . SER C 938  ? 2.5487 0.9139 2.1205 -0.2024 -1.0952 0.2624  938  SER B N   
19421 C CA  . SER C 938  ? 2.5816 0.9656 2.1329 -0.2003 -1.0531 0.2544  938  SER B CA  
19422 C C   . SER C 938  ? 2.6779 1.0860 2.2462 -0.2185 -1.0200 0.2473  938  SER B C   
19423 O O   . SER C 938  ? 2.7588 1.1844 2.3108 -0.2186 -0.9838 0.2404  938  SER B O   
19424 C CB  . SER C 938  ? 2.2875 0.6816 1.8632 -0.1991 -1.0285 0.2665  938  SER B CB  
19425 O OG  . SER C 938  ? 2.2518 0.6505 1.8889 -0.2131 -1.0318 0.2828  938  SER B OG  
19426 N N   . TYR C 939  ? 3.7782 2.1866 3.3771 -0.2338 -1.0329 0.2488  939  TYR B N   
19427 C CA  . TYR C 939  ? 3.8572 2.2889 3.4881 -0.2558 -1.0017 0.2465  939  TYR B CA  
19428 C C   . TYR C 939  ? 3.6946 2.1420 3.2895 -0.2560 -0.9741 0.2314  939  TYR B C   
19429 O O   . TYR C 939  ? 3.5629 2.0322 3.1830 -0.2746 -0.9430 0.2300  939  TYR B O   
19430 C CB  . TYR C 939  ? 4.2340 2.6589 3.8975 -0.2704 -1.0257 0.2493  939  TYR B CB  
19431 C CG  . TYR C 939  ? 4.4795 2.8843 4.1017 -0.2608 -1.0615 0.2381  939  TYR B CG  
19432 C CD1 . TYR C 939  ? 4.5456 2.9584 4.1439 -0.2648 -1.0514 0.2249  939  TYR B CD1 
19433 C CD2 . TYR C 939  ? 4.6012 2.9791 4.2086 -0.2482 -1.1051 0.2412  939  TYR B CD2 
19434 C CE1 . TYR C 939  ? 4.6083 3.0019 4.1691 -0.2555 -1.0831 0.2152  939  TYR B CE1 
19435 C CE2 . TYR C 939  ? 4.6654 3.0234 4.2344 -0.2398 -1.1366 0.2311  939  TYR B CE2 
19436 C CZ  . TYR C 939  ? 4.6662 3.0318 4.2122 -0.2431 -1.1253 0.2182  939  TYR B CZ  
19437 O OH  . TYR C 939  ? 4.7154 3.0602 4.2229 -0.2340 -1.1562 0.2086  939  TYR B OH  
19438 N N   . SER C 940  ? 3.2532 1.6894 2.7896 -0.2358 -0.9859 0.2203  940  SER B N   
19439 C CA  . SER C 940  ? 3.1763 1.6288 2.6762 -0.2329 -0.9573 0.2069  940  SER B CA  
19440 C C   . SER C 940  ? 3.0201 1.4948 2.5355 -0.2387 -0.9126 0.2111  940  SER B C   
19441 O O   . SER C 940  ? 3.0252 1.4934 2.5402 -0.2287 -0.9110 0.2182  940  SER B O   
19442 C CB  . SER C 940  ? 3.2593 1.6928 2.6952 -0.2082 -0.9795 0.1960  940  SER B CB  
19443 O OG  . SER C 940  ? 3.2877 1.7072 2.7130 -0.1934 -0.9886 0.2024  940  SER B OG  
19444 N N   . GLY C 941  ? 3.1787 1.6791 2.7075 -0.2556 -0.8760 0.2068  941  GLY B N   
19445 C CA  . GLY C 941  ? 3.0444 1.5672 2.5877 -0.2639 -0.8301 0.2097  941  GLY B CA  
19446 C C   . GLY C 941  ? 2.9383 1.4872 2.4831 -0.2812 -0.7970 0.2012  941  GLY B C   
19447 O O   . GLY C 941  ? 2.9113 1.4626 2.4733 -0.2943 -0.8067 0.1997  941  GLY B O   
19448 N N   . VAL C 942  ? 2.9044 1.4724 2.4301 -0.2815 -0.7585 0.1956  942  VAL B N   
19449 C CA  . VAL C 942  ? 2.7787 1.3740 2.3042 -0.2987 -0.7236 0.1877  942  VAL B CA  
19450 C C   . VAL C 942  ? 2.6910 1.3079 2.2408 -0.3132 -0.6746 0.1930  942  VAL B C   
19451 O O   . VAL C 942  ? 2.7210 1.3314 2.2772 -0.3055 -0.6672 0.2006  942  VAL B O   
19452 C CB  . VAL C 942  ? 2.7816 1.3818 2.2470 -0.2839 -0.7227 0.1716  942  VAL B CB  
19453 C CG1 . VAL C 942  ? 2.7686 1.3912 2.2350 -0.3008 -0.7056 0.1638  942  VAL B CG1 
19454 C CG2 . VAL C 942  ? 2.8342 1.4064 2.2625 -0.2602 -0.7696 0.1669  942  VAL B CG2 
19455 N N   . THR C 943  ? 1.9404 0.5825 1.5040 -0.3348 -0.6409 0.1895  943  THR B N   
19456 C CA  . THR C 943  ? 1.8717 0.5358 1.4365 -0.3447 -0.5917 0.1890  943  THR B CA  
19457 C C   . THR C 943  ? 1.8825 0.5642 1.3997 -0.3414 -0.5767 0.1732  943  THR B C   
19458 O O   . THR C 943  ? 1.8932 0.5831 1.4058 -0.3496 -0.5838 0.1668  943  THR B O   
19459 C CB  . THR C 943  ? 1.9043 0.5854 1.5249 -0.3746 -0.5575 0.1985  943  THR B CB  
19460 O OG1 . THR C 943  ? 1.8923 0.5569 1.5605 -0.3795 -0.5798 0.2123  943  THR B OG1 
19461 C CG2 . THR C 943  ? 1.8514 0.5475 1.4749 -0.3805 -0.5101 0.2013  943  THR B CG2 
19462 N N   . LEU C 944  ? 2.6999 1.3861 2.1797 -0.3281 -0.5581 0.1668  944  LEU B N   
19463 C CA  . LEU C 944  ? 2.6833 1.3914 2.1239 -0.3290 -0.5353 0.1529  944  LEU B CA  
19464 C C   . LEU C 944  ? 2.6961 1.4331 2.1654 -0.3575 -0.4863 0.1550  944  LEU B C   
19465 O O   . LEU C 944  ? 2.6971 1.4382 2.1882 -0.3655 -0.4563 0.1626  944  LEU B O   
19466 C CB  . LEU C 944  ? 2.6906 1.3939 2.0799 -0.3056 -0.5315 0.1443  944  LEU B CB  
19467 C CG  . LEU C 944  ? 2.7083 1.3872 2.0588 -0.2795 -0.5782 0.1379  944  LEU B CG  
19468 C CD1 . LEU C 944  ? 2.7433 1.4229 2.0355 -0.2589 -0.5721 0.1251  944  LEU B CD1 
19469 C CD2 . LEU C 944  ? 2.6824 1.3650 2.0346 -0.2862 -0.5990 0.1334  944  LEU B CD2 
19470 N N   . ASP C 945  ? 2.4344 1.1903 1.9041 -0.3732 -0.4789 0.1488  945  ASP B N   
19471 C CA  . ASP C 945  ? 2.3895 1.1741 1.8826 -0.4023 -0.4335 0.1495  945  ASP B CA  
19472 C C   . ASP C 945  ? 2.3710 1.1787 1.8269 -0.4047 -0.4225 0.1358  945  ASP B C   
19473 O O   . ASP C 945  ? 2.3792 1.1914 1.8383 -0.4118 -0.4389 0.1329  945  ASP B O   
19474 C CB  . ASP C 945  ? 2.3643 1.1483 1.9114 -0.4261 -0.4371 0.1593  945  ASP B CB  
19475 C CG  . ASP C 945  ? 2.3192 1.1246 1.9006 -0.4553 -0.3880 0.1648  945  ASP B CG  
19476 O OD1 . ASP C 945  ? 2.3260 1.1474 1.8870 -0.4571 -0.3509 0.1605  945  ASP B OD1 
19477 O OD2 . ASP C 945  ? 2.2648 1.0696 1.8926 -0.4763 -0.3866 0.1733  945  ASP B OD2 
19478 N N   . PRO C 946  ? 1.9415 0.7649 1.3624 -0.3997 -0.3930 0.1276  946  PRO B N   
19479 C CA  . PRO C 946  ? 1.9765 0.8211 1.3579 -0.3982 -0.3876 0.1142  946  PRO B CA  
19480 C C   . PRO C 946  ? 1.9532 0.8276 1.3588 -0.4303 -0.3544 0.1146  946  PRO B C   
19481 O O   . PRO C 946  ? 1.9535 0.8425 1.3456 -0.4352 -0.3612 0.1078  946  PRO B O   
19482 C CB  . PRO C 946  ? 1.9990 0.8515 1.3393 -0.3849 -0.3628 0.1061  946  PRO B CB  
19483 C CG  . PRO C 946  ? 1.9788 0.8173 1.3424 -0.3847 -0.3481 0.1162  946  PRO B CG  
19484 C CD  . PRO C 946  ? 1.9941 0.8230 1.4155 -0.4021 -0.3557 0.1303  946  PRO B CD  
19485 N N   . ARG C 947  ? 2.3350 1.2174 1.7758 -0.4521 -0.3182 0.1228  947  ARG B N   
19486 C CA  . ARG C 947  ? 2.3075 1.2172 1.7717 -0.4848 -0.2805 0.1238  947  ARG B CA  
19487 C C   . ARG C 947  ? 2.2604 1.1628 1.7743 -0.5043 -0.2937 0.1335  947  ARG B C   
19488 O O   . ARG C 947  ? 2.2619 1.1779 1.8095 -0.5328 -0.2611 0.1391  947  ARG B O   
19489 C CB  . ARG C 947  ? 2.3105 1.2315 1.7859 -0.4994 -0.2316 0.1275  947  ARG B CB  
19490 C CG  . ARG C 947  ? 2.3551 1.2788 1.7862 -0.4802 -0.2173 0.1195  947  ARG B CG  
19491 C CD  . ARG C 947  ? 2.3656 1.3230 1.7644 -0.4920 -0.1817 0.1079  947  ARG B CD  
19492 N NE  . ARG C 947  ? 2.3574 1.3300 1.7673 -0.5125 -0.1293 0.1105  947  ARG B NE  
19493 C CZ  . ARG C 947  ? 2.4219 1.4069 1.7957 -0.5070 -0.0995 0.1024  947  ARG B CZ  
19494 N NH1 . ARG C 947  ? 2.4685 1.4529 1.7933 -0.4814 -0.1172 0.0909  947  ARG B NH1 
19495 N NH2 . ARG C 947  ? 2.4297 1.4271 1.8157 -0.5273 -0.0511 0.1054  947  ARG B NH2 
19496 N N   . GLY C 948  ? 1.8978 0.7775 1.4162 -0.4895 -0.3406 0.1355  948  GLY B N   
19497 C CA  . GLY C 948  ? 1.8485 0.7195 1.4125 -0.5069 -0.3559 0.1440  948  GLY B CA  
19498 C C   . GLY C 948  ? 1.7808 0.6478 1.3982 -0.5285 -0.3317 0.1570  948  GLY B C   
19499 O O   . GLY C 948  ? 1.7583 0.6139 1.4164 -0.5408 -0.3471 0.1650  948  GLY B O   
19500 N N   . ILE C 949  ? 1.8961 0.7720 1.5130 -0.5331 -0.2934 0.1590  949  ILE B N   
19501 C CA  . ILE C 949  ? 1.7876 0.6617 1.4519 -0.5533 -0.2635 0.1711  949  ILE B CA  
19502 C C   . ILE C 949  ? 1.7595 0.6126 1.4767 -0.5609 -0.2867 0.1838  949  ILE B C   
19503 O O   . ILE C 949  ? 1.7606 0.6190 1.5206 -0.5871 -0.2592 0.1921  949  ILE B O   
19504 C CB  . ILE C 949  ? 1.8189 0.6873 1.4709 -0.5389 -0.2439 0.1738  949  ILE B CB  
19505 C CG1 . ILE C 949  ? 1.9457 0.8338 1.5433 -0.5303 -0.2218 0.1604  949  ILE B CG1 
19506 C CG2 . ILE C 949  ? 1.7830 0.6527 1.4808 -0.5609 -0.2058 0.1859  949  ILE B CG2 
19507 C CD1 . ILE C 949  ? 1.9384 0.8309 1.5265 -0.5288 -0.1818 0.1618  949  ILE B CD1 
19508 N N   . TYR C 950  ? 2.4388 1.2682 2.1534 -0.5393 -0.3359 0.1853  950  TYR B N   
19509 C CA  . TYR C 950  ? 2.4574 1.2655 2.2215 -0.5442 -0.3592 0.1977  950  TYR B CA  
19510 C C   . TYR C 950  ? 2.4566 1.2585 2.2410 -0.5548 -0.3887 0.1976  950  TYR B C   
19511 O O   . TYR C 950  ? 2.4770 1.2657 2.3084 -0.5660 -0.3984 0.2080  950  TYR B O   
19512 C CB  . TYR C 950  ? 2.3727 1.1558 2.1349 -0.5172 -0.3876 0.2042  950  TYR B CB  
19513 C CG  . TYR C 950  ? 2.3538 1.1382 2.1378 -0.5216 -0.3525 0.2138  950  TYR B CG  
19514 C CD1 . TYR C 950  ? 2.2979 1.0712 2.1368 -0.5329 -0.3499 0.2286  950  TYR B CD1 
19515 C CD2 . TYR C 950  ? 2.3666 1.1644 2.1170 -0.5159 -0.3197 0.2079  950  TYR B CD2 
19516 C CE1 . TYR C 950  ? 2.3031 1.0778 2.1626 -0.5371 -0.3163 0.2379  950  TYR B CE1 
19517 C CE2 . TYR C 950  ? 2.3843 1.1829 2.1538 -0.5204 -0.2858 0.2166  950  TYR B CE2 
19518 C CZ  . TYR C 950  ? 2.3818 1.1686 2.2059 -0.5307 -0.2842 0.2319  950  TYR B CZ  
19519 O OH  . TYR C 950  ? 2.3813 1.1686 2.2247 -0.5347 -0.2498 0.2411  950  TYR B OH  
19520 N N   . GLY C 951  ? 1.8985 0.7101 1.6487 -0.5519 -0.4011 0.1861  951  GLY B N   
19521 C CA  . GLY C 951  ? 1.9361 0.7409 1.6991 -0.5593 -0.4304 0.1849  951  GLY B CA  
19522 C C   . GLY C 951  ? 2.0075 0.8113 1.7212 -0.5389 -0.4616 0.1730  951  GLY B C   
19523 O O   . GLY C 951  ? 2.0256 0.8195 1.7433 -0.5393 -0.4922 0.1714  951  GLY B O   
19524 N N   . THR C 952  ? 1.9205 0.7327 1.5879 -0.5201 -0.4544 0.1649  952  THR B N   
19525 C CA  . THR C 952  ? 1.9326 0.7495 1.5474 -0.5012 -0.4740 0.1524  952  THR B CA  
19526 C C   . THR C 952  ? 1.9463 0.7649 1.5161 -0.4770 -0.4688 0.1459  952  THR B C   
19527 O O   . THR C 952  ? 1.9986 0.8080 1.5749 -0.4692 -0.4601 0.1514  952  THR B O   
19528 C CB  . THR C 952  ? 1.9404 0.7337 1.5439 -0.4839 -0.5266 0.1501  952  THR B CB  
19529 O OG1 . THR C 952  ? 2.0112 0.8048 1.5593 -0.4583 -0.5427 0.1391  952  THR B OG1 
19530 C CG2 . THR C 952  ? 1.9713 0.7334 1.6009 -0.4731 -0.5581 0.1597  952  THR B CG2 
19531 N N   . ILE C 953  ? 2.3855 1.2156 1.9092 -0.4649 -0.4740 0.1342  953  ILE B N   
19532 C CA  . ILE C 953  ? 2.4616 1.2908 1.9390 -0.4399 -0.4738 0.1268  953  ILE B CA  
19533 C C   . ILE C 953  ? 2.6161 1.4129 2.0732 -0.4098 -0.5213 0.1264  953  ILE B C   
19534 O O   . ILE C 953  ? 2.6615 1.4462 2.1102 -0.4019 -0.5561 0.1238  953  ILE B O   
19535 C CB  . ILE C 953  ? 2.5188 1.3754 1.9551 -0.4394 -0.4565 0.1145  953  ILE B CB  
19536 C CG1 . ILE C 953  ? 2.5500 1.3970 1.9540 -0.4201 -0.4959 0.1070  953  ILE B CG1 
19537 C CG2 . ILE C 953  ? 2.5315 1.4173 1.9920 -0.4721 -0.4206 0.1155  953  ILE B CG2 
19538 C CD1 . ILE C 953  ? 2.5706 1.4412 1.9281 -0.4120 -0.4821 0.0949  953  ILE B CD1 
19539 N N   . SER C 954  ? 2.7935 1.5758 2.2425 -0.3937 -0.5220 0.1293  954  SER B N   
19540 C CA  . SER C 954  ? 2.7533 1.5041 2.1817 -0.3655 -0.5647 0.1296  954  SER B CA  
19541 C C   . SER C 954  ? 2.7714 1.5217 2.1496 -0.3423 -0.5596 0.1208  954  SER B C   
19542 O O   . SER C 954  ? 2.7842 1.5395 2.1625 -0.3423 -0.5326 0.1230  954  SER B O   
19543 C CB  . SER C 954  ? 2.6704 1.3990 2.1395 -0.3666 -0.5776 0.1431  954  SER B CB  
19544 O OG  . SER C 954  ? 2.6708 1.3694 2.1298 -0.3468 -0.6258 0.1443  954  SER B OG  
19545 N N   . ARG C 955  ? 2.5775 1.3209 1.9123 -0.3226 -0.5852 0.1108  955  ARG B N   
19546 C CA  . ARG C 955  ? 2.6186 1.3610 1.9027 -0.3002 -0.5820 0.1012  955  ARG B CA  
19547 C C   . ARG C 955  ? 2.7034 1.4163 1.9532 -0.2726 -0.6281 0.0968  955  ARG B C   
19548 O O   . ARG C 955  ? 2.7736 1.4840 1.9764 -0.2527 -0.6304 0.0871  955  ARG B O   
19549 C CB  . ARG C 955  ? 2.6222 1.3970 1.8779 -0.3062 -0.5518 0.0899  955  ARG B CB  
19550 C CG  . ARG C 955  ? 2.5985 1.4050 1.8777 -0.3328 -0.5021 0.0919  955  ARG B CG  
19551 C CD  . ARG C 955  ? 2.5980 1.4343 1.8439 -0.3357 -0.4825 0.0800  955  ARG B CD  
19552 N NE  . ARG C 955  ? 2.5211 1.3913 1.7868 -0.3644 -0.4388 0.0804  955  ARG B NE  
19553 C CZ  . ARG C 955  ? 2.5131 1.4120 1.7601 -0.3728 -0.4234 0.0723  955  ARG B CZ  
19554 N NH1 . ARG C 955  ? 2.5533 1.4507 1.7630 -0.3540 -0.4483 0.0635  955  ARG B NH1 
19555 N NH2 . ARG C 955  ? 2.5426 1.4718 1.8079 -0.4003 -0.3830 0.0732  955  ARG B NH2 
19556 N N   . ARG C 956  ? 2.2642 0.9546 1.5366 -0.2724 -0.6637 0.1036  956  ARG B N   
19557 C CA  . ARG C 956  ? 2.3014 0.9597 1.5450 -0.2477 -0.7092 0.1010  956  ARG B CA  
19558 C C   . ARG C 956  ? 2.3619 0.9961 1.6410 -0.2523 -0.7439 0.1111  956  ARG B C   
19559 O O   . ARG C 956  ? 2.3288 0.9680 1.6299 -0.2666 -0.7511 0.1125  956  ARG B O   
19560 C CB  . ARG C 956  ? 2.3061 0.9690 1.5048 -0.2351 -0.7206 0.0884  956  ARG B CB  
19561 C CG  . ARG C 956  ? 2.3713 1.0104 1.5186 -0.2053 -0.7452 0.0808  956  ARG B CG  
19562 C CD  . ARG C 956  ? 2.4461 1.0905 1.5516 -0.1934 -0.7544 0.0690  956  ARG B CD  
19563 N NE  . ARG C 956  ? 2.4884 1.1084 1.5920 -0.1863 -0.7953 0.0701  956  ARG B NE  
19564 C CZ  . ARG C 956  ? 2.5591 1.1667 1.6205 -0.1673 -0.8176 0.0614  956  ARG B CZ  
19565 N NH1 . ARG C 956  ? 2.5981 1.2161 1.6167 -0.1531 -0.8035 0.0510  956  ARG B NH1 
19566 N NH2 . ARG C 956  ? 2.5750 1.1594 1.6369 -0.1625 -0.8534 0.0631  956  ARG B NH2 
19567 N N   . LYS C 957  ? 2.5222 1.1309 1.8070 -0.2409 -0.7642 0.1182  957  LYS B N   
19568 C CA  . LYS C 957  ? 2.5368 1.1188 1.8462 -0.2403 -0.8026 0.1267  957  LYS B CA  
19569 C C   . LYS C 957  ? 2.5558 1.1066 1.8231 -0.2133 -0.8402 0.1227  957  LYS B C   
19570 O O   . LYS C 957  ? 2.5427 1.0904 1.7740 -0.1968 -0.8334 0.1174  957  LYS B O   
19571 C CB  . LYS C 957  ? 2.5192 1.0991 1.8813 -0.2544 -0.7946 0.1411  957  LYS B CB  
19572 C CG  . LYS C 957  ? 2.5796 1.1329 1.9672 -0.2539 -0.8352 0.1499  957  LYS B CG  
19573 C CD  . LYS C 957  ? 2.5886 1.1498 2.0391 -0.2786 -0.8244 0.1621  957  LYS B CD  
19574 C CE  . LYS C 957  ? 2.6373 1.1858 2.1076 -0.2869 -0.8555 0.1638  957  LYS B CE  
19575 N NZ  . LYS C 957  ? 2.7091 1.2253 2.1549 -0.2677 -0.9035 0.1627  957  LYS B NZ  
19576 N N   . GLU C 958  ? 2.6377 1.1649 1.9090 -0.2095 -0.8791 0.1251  958  GLU B N   
19577 C CA  . GLU C 958  ? 2.7528 1.2496 1.9810 -0.1855 -0.9165 0.1201  958  GLU B CA  
19578 C C   . GLU C 958  ? 2.7709 1.2388 2.0209 -0.1829 -0.9514 0.1306  958  GLU B C   
19579 O O   . GLU C 958  ? 2.7635 1.2239 2.0429 -0.1940 -0.9705 0.1359  958  GLU B O   
19580 C CB  . GLU C 958  ? 2.8510 1.3454 2.0515 -0.1809 -0.9322 0.1103  958  GLU B CB  
19581 C CG  . GLU C 958  ? 2.9899 1.4539 2.1405 -0.1560 -0.9672 0.1035  958  GLU B CG  
19582 C CD  . GLU C 958  ? 3.0906 1.5535 2.2154 -0.1517 -0.9800 0.0944  958  GLU B CD  
19583 O OE1 . GLU C 958  ? 3.1134 1.6038 2.2298 -0.1571 -0.9531 0.0876  958  GLU B OE1 
19584 O OE2 . GLU C 958  ? 3.1354 1.5699 2.2478 -0.1432 -1.0167 0.0943  958  GLU B OE2 
19585 N N   . PHE C 959  ? 2.9190 1.3713 2.1545 -0.1686 -0.9586 0.1339  959  PHE B N   
19586 C CA  . PHE C 959  ? 2.9494 1.3722 2.1946 -0.1619 -0.9950 0.1428  959  PHE B CA  
19587 C C   . PHE C 959  ? 3.0681 1.4619 2.2597 -0.1397 -1.0298 0.1343  959  PHE B C   
19588 O O   . PHE C 959  ? 3.1206 1.5085 2.2689 -0.1225 -1.0256 0.1271  959  PHE B O   
19589 C CB  . PHE C 959  ? 2.8670 1.2888 2.1238 -0.1581 -0.9833 0.1513  959  PHE B CB  
19590 C CG  . PHE C 959  ? 2.7720 1.2245 2.0631 -0.1746 -0.9389 0.1557  959  PHE B CG  
19591 C CD1 . PHE C 959  ? 2.7242 1.1850 2.0735 -0.1935 -0.9311 0.1687  959  PHE B CD1 
19592 C CD2 . PHE C 959  ? 2.7425 1.2155 2.0076 -0.1719 -0.9039 0.1466  959  PHE B CD2 
19593 C CE1 . PHE C 959  ? 2.6703 1.1577 2.0510 -0.2094 -0.8892 0.1730  959  PHE B CE1 
19594 C CE2 . PHE C 959  ? 2.6926 1.1931 1.9884 -0.1883 -0.8619 0.1506  959  PHE B CE2 
19595 C CZ  . PHE C 959  ? 2.6564 1.1635 2.0099 -0.2071 -0.8543 0.1639  959  PHE B CZ  
19596 N N   . PRO C 960  ? 2.9990 1.3732 2.1920 -0.1404 -1.0636 0.1347  960  PRO B N   
19597 C CA  . PRO C 960  ? 3.1212 1.4665 2.2628 -0.1208 -1.0964 0.1263  960  PRO B CA  
19598 C C   . PRO C 960  ? 3.2540 1.5666 2.3872 -0.1096 -1.1317 0.1329  960  PRO B C   
19599 O O   . PRO C 960  ? 3.2399 1.5533 2.4014 -0.1135 -1.1285 0.1436  960  PRO B O   
19600 C CB  . PRO C 960  ? 3.1092 1.4520 2.2600 -0.1299 -1.1120 0.1237  960  PRO B CB  
19601 C CG  . PRO C 960  ? 2.8871 1.2586 2.0949 -0.1551 -1.0861 0.1307  960  PRO B CG  
19602 C CD  . PRO C 960  ? 2.8970 1.2778 2.1364 -0.1607 -1.0684 0.1410  960  PRO B CD  
19603 N N   . TYR C 961  ? 3.7520 2.0357 2.8458 -0.0960 -1.1649 0.1268  961  TYR B N   
19604 C CA  . TYR C 961  ? 3.8770 2.1273 2.9617 -0.0875 -1.2032 0.1327  961  TYR B CA  
19605 C C   . TYR C 961  ? 3.9060 2.1467 3.0266 -0.1015 -1.2283 0.1401  961  TYR B C   
19606 O O   . TYR C 961  ? 3.9258 2.1664 3.0436 -0.1064 -1.2342 0.1344  961  TYR B O   
19607 C CB  . TYR C 961  ? 3.9928 2.2148 3.0140 -0.0663 -1.2257 0.1217  961  TYR B CB  
19608 C CG  . TYR C 961  ? 4.0730 2.2778 3.0654 -0.0509 -1.2327 0.1228  961  TYR B CG  
19609 C CD1 . TYR C 961  ? 4.1333 2.3047 3.1122 -0.0437 -1.2701 0.1278  961  TYR B CD1 
19610 C CD2 . TYR C 961  ? 4.0834 2.3054 3.0628 -0.0447 -1.2016 0.1192  961  TYR B CD2 
19611 C CE1 . TYR C 961  ? 4.1805 2.3358 3.1328 -0.0301 -1.2767 0.1292  961  TYR B CE1 
19612 C CE2 . TYR C 961  ? 4.1397 2.3453 3.0925 -0.0308 -1.2074 0.1201  961  TYR B CE2 
19613 C CZ  . TYR C 961  ? 4.1925 2.3647 3.1319 -0.0235 -1.2452 0.1252  961  TYR B CZ  
19614 O OH  . TYR C 961  ? 4.2515 2.4069 3.1639 -0.0102 -1.2512 0.1264  961  TYR B OH  
19615 N N   . ARG C 962  ? 3.7599 1.9926 2.9138 -0.1077 -1.2432 0.1527  962  ARG B N   
19616 C CA  . ARG C 962  ? 3.8141 2.0343 2.9992 -0.1197 -1.2710 0.1598  962  ARG B CA  
19617 C C   . ARG C 962  ? 3.8073 2.0000 2.9889 -0.1130 -1.3053 0.1683  962  ARG B C   
19618 O O   . ARG C 962  ? 3.7509 1.9502 2.9749 -0.1219 -1.3052 0.1812  962  ARG B O   
19619 C CB  . ARG C 962  ? 3.8704 2.1179 3.1202 -0.1429 -1.2496 0.1687  962  ARG B CB  
19620 C CG  . ARG C 962  ? 3.9939 2.2284 3.2826 -0.1557 -1.2783 0.1786  962  ARG B CG  
19621 C CD  . ARG C 962  ? 4.0659 2.3104 3.3820 -0.1729 -1.2743 0.1762  962  ARG B CD  
19622 N NE  . ARG C 962  ? 4.0850 2.3510 3.4656 -0.1938 -1.2566 0.1875  962  ARG B NE  
19623 C CZ  . ARG C 962  ? 4.1047 2.3780 3.5213 -0.2122 -1.2556 0.1889  962  ARG B CZ  
19624 N NH1 . ARG C 962  ? 4.1438 2.4047 3.5380 -0.2120 -1.2719 0.1799  962  ARG B NH1 
19625 N NH2 . ARG C 962  ? 4.0673 2.3595 3.5421 -0.2307 -1.2379 0.1994  962  ARG B NH2 
19626 N N   . ILE C 963  ? 3.5358 1.6977 2.6664 -0.0975 -1.3345 0.1614  963  ILE B N   
19627 C CA  . ILE C 963  ? 3.4874 1.6208 2.6080 -0.0909 -1.3695 0.1685  963  ILE B CA  
19628 C C   . ILE C 963  ? 3.4841 1.6093 2.6433 -0.1059 -1.3954 0.1771  963  ILE B C   
19629 O O   . ILE C 963  ? 3.4984 1.6105 2.6461 -0.1089 -1.4121 0.1710  963  ILE B O   
19630 C CB  . ILE C 963  ? 3.4296 1.5304 2.4829 -0.0715 -1.3933 0.1579  963  ILE B CB  
19631 C CG1 . ILE C 963  ? 3.3683 1.4791 2.3811 -0.0589 -1.3663 0.1447  963  ILE B CG1 
19632 C CG2 . ILE C 963  ? 3.4633 1.5410 2.4997 -0.0618 -1.4170 0.1647  963  ILE B CG2 
19633 C CD1 . ILE C 963  ? 3.4068 1.4859 2.3537 -0.0407 -1.3874 0.1330  963  ILE B CD1 
19634 N N   . PRO C 964  ? 3.1884 1.3209 2.3936 -0.1154 -1.3986 0.1915  964  PRO B N   
19635 C CA  . PRO C 964  ? 3.2139 1.3391 2.4581 -0.1300 -1.4237 0.2005  964  PRO B CA  
19636 C C   . PRO C 964  ? 3.3337 1.4214 2.5359 -0.1210 -1.4662 0.1968  964  PRO B C   
19637 O O   . PRO C 964  ? 3.3814 1.4503 2.5433 -0.1057 -1.4794 0.1956  964  PRO B O   
19638 C CB  . PRO C 964  ? 3.1876 1.3241 2.4762 -0.1356 -1.4209 0.2166  964  PRO B CB  
19639 C CG  . PRO C 964  ? 3.1142 1.2699 2.3958 -0.1276 -1.3862 0.2157  964  PRO B CG  
19640 C CD  . PRO C 964  ? 3.1454 1.2893 2.3632 -0.1109 -1.3828 0.2001  964  PRO B CD  
19641 N N   . LEU C 965  ? 3.7048 1.7804 2.9140 -0.1303 -1.4870 0.1948  965  LEU B N   
19642 C CA  . LEU C 965  ? 3.8517 1.8903 3.0192 -0.1225 -1.5267 0.1911  965  LEU B CA  
19643 C C   . LEU C 965  ? 3.9192 1.9422 3.0980 -0.1233 -1.5565 0.2037  965  LEU B C   
19644 O O   . LEU C 965  ? 3.9936 1.9867 3.1457 -0.1207 -1.5913 0.2026  965  LEU B O   
19645 C CB  . LEU C 965  ? 3.8965 1.9247 3.0640 -0.1316 -1.5401 0.1845  965  LEU B CB  
19646 C CG  . LEU C 965  ? 4.0635 2.1013 3.2101 -0.1287 -1.5169 0.1714  965  LEU B CG  
19647 C CD1 . LEU C 965  ? 4.0977 2.1177 3.2366 -0.1354 -1.5370 0.1653  965  LEU B CD1 
19648 C CD2 . LEU C 965  ? 4.1038 2.1325 3.1905 -0.1078 -1.5087 0.1608  965  LEU B CD2 
19649 N N   . ASP C 966  ? 3.7381 1.7819 2.9561 -0.1270 -1.5422 0.2157  966  ASP B N   
19650 C CA  . ASP C 966  ? 3.7364 1.7699 2.9667 -0.1266 -1.5667 0.2289  966  ASP B CA  
19651 C C   . ASP C 966  ? 3.6531 1.6835 2.8523 -0.1102 -1.5593 0.2299  966  ASP B C   
19652 O O   . ASP C 966  ? 3.6675 1.6961 2.8821 -0.1094 -1.5717 0.2423  966  ASP B O   
19653 C CB  . ASP C 966  ? 3.7330 1.7921 3.0362 -0.1436 -1.5575 0.2441  966  ASP B CB  
19654 C CG  . ASP C 966  ? 3.7716 1.8218 3.1044 -0.1587 -1.5851 0.2492  966  ASP B CG  
19655 O OD1 . ASP C 966  ? 3.8302 1.8530 3.1258 -0.1561 -1.6129 0.2413  966  ASP B OD1 
19656 O OD2 . ASP C 966  ? 3.7333 1.8036 3.1267 -0.1735 -1.5784 0.2610  966  ASP B OD2 
19657 N N   . LEU C 967  ? 3.3064 1.3372 2.4635 -0.0973 -1.5384 0.2174  967  LEU B N   
19658 C CA  . LEU C 967  ? 3.2477 1.2776 2.3769 -0.0824 -1.5271 0.2176  967  LEU B CA  
19659 C C   . LEU C 967  ? 3.2578 1.2559 2.3533 -0.0730 -1.5641 0.2219  967  LEU B C   
19660 O O   . LEU C 967  ? 3.3165 1.2868 2.3829 -0.0722 -1.5952 0.2174  967  LEU B O   
19661 C CB  . LEU C 967  ? 3.2437 1.2749 2.3261 -0.0694 -1.5032 0.2017  967  LEU B CB  
19662 C CG  . LEU C 967  ? 3.2855 1.3088 2.3276 -0.0522 -1.4958 0.1993  967  LEU B CG  
19663 C CD1 . LEU C 967  ? 3.2615 1.3092 2.3440 -0.0553 -1.4733 0.2116  967  LEU B CD1 
19664 C CD2 . LEU C 967  ? 3.2852 1.3089 2.2804 -0.0399 -1.4741 0.1828  967  LEU B CD2 
19665 N N   . VAL C 968  ? 3.3096 1.3110 2.4084 -0.0666 -1.5605 0.2309  968  VAL B N   
19666 C CA  . VAL C 968  ? 3.3074 1.2795 2.3712 -0.0571 -1.5932 0.2350  968  VAL B CA  
19667 C C   . VAL C 968  ? 3.3437 1.2931 2.3362 -0.0385 -1.5917 0.2206  968  VAL B C   
19668 O O   . VAL C 968  ? 3.3128 1.2711 2.2916 -0.0284 -1.5682 0.2186  968  VAL B O   
19669 C CB  . VAL C 968  ? 3.2482 1.2336 2.3467 -0.0581 -1.5902 0.2514  968  VAL B CB  
19670 C CG1 . VAL C 968  ? 3.1882 1.1921 2.3545 -0.0759 -1.5960 0.2659  968  VAL B CG1 
19671 C CG2 . VAL C 968  ? 3.2058 1.2157 2.3108 -0.0518 -1.5484 0.2496  968  VAL B CG2 
19672 N N   . PRO C 969  ? 3.7558 1.6747 2.7022 -0.0340 -1.6170 0.2106  969  PRO B N   
19673 C CA  . PRO C 969  ? 3.8191 1.7209 2.7030 -0.0187 -1.6089 0.1938  969  PRO B CA  
19674 C C   . PRO C 969  ? 3.8970 1.7955 2.7470 -0.0032 -1.5945 0.1912  969  PRO B C   
19675 O O   . PRO C 969  ? 3.9109 1.8084 2.7715 -0.0020 -1.6021 0.2023  969  PRO B O   
19676 C CB  . PRO C 969  ? 3.8795 1.7425 2.7214 -0.0168 -1.6474 0.1890  969  PRO B CB  
19677 C CG  . PRO C 969  ? 3.8514 1.7192 2.7410 -0.0343 -1.6673 0.1994  969  PRO B CG  
19678 C CD  . PRO C 969  ? 3.7948 1.6906 2.7421 -0.0424 -1.6565 0.2154  969  PRO B CD  
19679 N N   . LYS C 970  ? 3.9279 1.8257 2.7382 0.0084  -1.5732 0.1764  970  LYS B N   
19680 C CA  . LYS C 970  ? 4.0443 1.9377 2.8170 0.0237  -1.5574 0.1711  970  LYS B CA  
19681 C C   . LYS C 970  ? 4.0360 1.9589 2.8471 0.0218  -1.5300 0.1808  970  LYS B C   
19682 O O   . LYS C 970  ? 4.0511 1.9669 2.8351 0.0333  -1.5235 0.1800  970  LYS B O   
19683 C CB  . LYS C 970  ? 4.1988 2.0521 2.9203 0.0340  -1.5902 0.1706  970  LYS B CB  
19684 C CG  . LYS C 970  ? 4.3486 2.1705 3.0045 0.0459  -1.6006 0.1544  970  LYS B CG  
19685 C CD  . LYS C 970  ? 4.5012 2.2846 3.1055 0.0564  -1.6277 0.1542  970  LYS B CD  
19686 C CE  . LYS C 970  ? 4.6075 2.3571 3.1452 0.0684  -1.6377 0.1383  970  LYS B CE  
19687 N NZ  . LYS C 970  ? 4.6933 2.4068 3.1775 0.0794  -1.6576 0.1365  970  LYS B NZ  
19688 N N   . THR C 971  ? 3.7304 1.6850 2.6034 0.0073  -1.5136 0.1899  971  THR B N   
19689 C CA  . THR C 971  ? 3.7222 1.7069 2.6323 0.0050  -1.4816 0.1979  971  THR B CA  
19690 C C   . THR C 971  ? 3.6578 1.6738 2.5861 0.0003  -1.4418 0.1900  971  THR B C   
19691 O O   . THR C 971  ? 3.6504 1.6804 2.6105 -0.0123 -1.4386 0.1901  971  THR B O   
19692 C CB  . THR C 971  ? 3.7253 1.7249 2.6983 -0.0092 -1.4897 0.2166  971  THR B CB  
19693 O OG1 . THR C 971  ? 3.6561 1.6789 2.6766 -0.0250 -1.4780 0.2182  971  THR B OG1 
19694 C CG2 . THR C 971  ? 3.8112 1.7820 2.7741 -0.0095 -1.5342 0.2247  971  THR B CG2 
19695 N N   . GLU C 972  ? 4.3921 2.4195 3.3010 0.0097  -1.4111 0.1837  972  GLU B N   
19696 C CA  . GLU C 972  ? 4.3129 2.3699 3.2325 0.0061  -1.3718 0.1752  972  GLU B CA  
19697 C C   . GLU C 972  ? 4.1275 2.2194 3.1163 -0.0117 -1.3479 0.1864  972  GLU B C   
19698 O O   . GLU C 972  ? 4.0652 2.1632 3.0911 -0.0171 -1.3501 0.2011  972  GLU B O   
19699 C CB  . GLU C 972  ? 4.4335 2.4927 3.3138 0.0205  -1.3459 0.1660  972  GLU B CB  
19700 C CG  . GLU C 972  ? 4.5773 2.6149 3.4350 0.0316  -1.3612 0.1721  972  GLU B CG  
19701 C CD  . GLU C 972  ? 4.6811 2.7128 3.4874 0.0477  -1.3415 0.1598  972  GLU B CD  
19702 O OE1 . GLU C 972  ? 4.6731 2.7259 3.4734 0.0482  -1.3089 0.1492  972  GLU B OE1 
19703 O OE2 . GLU C 972  ? 4.7607 2.7668 3.5321 0.0594  -1.3586 0.1605  972  GLU B OE2 
19704 N N   . ILE C 973  ? 3.0381 1.1521 2.0429 -0.0207 -1.3253 0.1795  973  ILE B N   
19705 C CA  . ILE C 973  ? 2.8842 1.0323 1.9504 -0.0384 -1.2974 0.1876  973  ILE B CA  
19706 C C   . ILE C 973  ? 2.9044 1.0781 1.9747 -0.0366 -1.2535 0.1858  973  ILE B C   
19707 O O   . ILE C 973  ? 2.9298 1.1153 1.9744 -0.0327 -1.2283 0.1729  973  ILE B O   
19708 C CB  . ILE C 973  ? 2.7031 0.8633 1.7871 -0.0510 -1.2935 0.1817  973  ILE B CB  
19709 C CG1 . ILE C 973  ? 2.7093 0.8401 1.7570 -0.0453 -1.3298 0.1741  973  ILE B CG1 
19710 C CG2 . ILE C 973  ? 2.6028 0.7815 1.7537 -0.0707 -1.2899 0.1951  973  ILE B CG2 
19711 C CD1 . ILE C 973  ? 2.6707 0.8094 1.7477 -0.0603 -1.3348 0.1734  973  ILE B CD1 
19712 N N   . LYS C 974  ? 3.4329 1.6151 2.5357 -0.0396 -1.2444 0.1991  974  LYS B N   
19713 C CA  . LYS C 974  ? 3.3902 1.5920 2.4942 -0.0367 -1.2053 0.1987  974  LYS B CA  
19714 C C   . LYS C 974  ? 3.2485 1.4850 2.4074 -0.0549 -1.1696 0.2042  974  LYS B C   
19715 O O   . LYS C 974  ? 3.2149 1.4586 2.4260 -0.0687 -1.1767 0.2173  974  LYS B O   
19716 C CB  . LYS C 974  ? 3.4644 1.6542 2.5706 -0.0287 -1.2150 0.2106  974  LYS B CB  
19717 C CG  . LYS C 974  ? 3.5089 1.7231 2.6459 -0.0329 -1.1763 0.2183  974  LYS B CG  
19718 C CD  . LYS C 974  ? 3.6279 1.8265 2.7619 -0.0230 -1.1907 0.2300  974  LYS B CD  
19719 C CE  . LYS C 974  ? 3.6457 1.8661 2.8081 -0.0258 -1.1523 0.2382  974  LYS B CE  
19720 N NZ  . LYS C 974  ? 3.6875 1.8922 2.8497 -0.0163 -1.1692 0.2511  974  LYS B NZ  
19721 N N   . ARG C 975  ? 2.7310 0.9890 1.8785 -0.0557 -1.1308 0.1944  975  ARG B N   
19722 C CA  . ARG C 975  ? 2.6064 0.8974 1.8025 -0.0743 -1.0944 0.1983  975  ARG B CA  
19723 C C   . ARG C 975  ? 2.5253 0.8391 1.7175 -0.0742 -1.0480 0.1947  975  ARG B C   
19724 O O   . ARG C 975  ? 2.5610 0.8711 1.7042 -0.0608 -1.0372 0.1824  975  ARG B O   
19725 C CB  . ARG C 975  ? 2.5619 0.8615 1.7607 -0.0842 -1.0955 0.1895  975  ARG B CB  
19726 C CG  . ARG C 975  ? 2.5787 0.8639 1.7168 -0.0697 -1.1069 0.1730  975  ARG B CG  
19727 C CD  . ARG C 975  ? 2.5606 0.8398 1.7030 -0.0767 -1.1298 0.1693  975  ARG B CD  
19728 N NE  . ARG C 975  ? 2.5726 0.8573 1.6758 -0.0713 -1.1191 0.1533  975  ARG B NE  
19729 C CZ  . ARG C 975  ? 2.5377 0.8312 1.6503 -0.0812 -1.1198 0.1484  975  ARG B CZ  
19730 N NH1 . ARG C 975  ? 2.4839 0.7814 1.6439 -0.0979 -1.1302 0.1575  975  ARG B NH1 
19731 N NH2 . ARG C 975  ? 2.5576 0.8566 1.6323 -0.0745 -1.1097 0.1344  975  ARG B NH2 
19732 N N   . ILE C 976  ? 2.5432 0.8800 1.7880 -0.0898 -1.0202 0.2056  976  ILE B N   
19733 C CA  . ILE C 976  ? 2.4720 0.8311 1.7195 -0.0925 -0.9741 0.2040  976  ILE B CA  
19734 C C   . ILE C 976  ? 2.3952 0.7834 1.6645 -0.1103 -0.9413 0.1984  976  ILE B C   
19735 O O   . ILE C 976  ? 2.3970 0.7887 1.6916 -0.1226 -0.9539 0.1997  976  ILE B O   
19736 C CB  . ILE C 976  ? 2.4524 0.8174 1.7437 -0.0977 -0.9607 0.2211  976  ILE B CB  
19737 C CG1 . ILE C 976  ? 2.5299 0.8702 1.8328 -0.0911 -1.0043 0.2336  976  ILE B CG1 
19738 C CG2 . ILE C 976  ? 2.4417 0.8134 1.7081 -0.0887 -0.9265 0.2174  976  ILE B CG2 
19739 C CD1 . ILE C 976  ? 2.5539 0.9005 1.9098 -0.0982 -0.9973 0.2531  976  ILE B CD1 
19740 N N   . LEU C 977  ? 2.5805 0.9893 1.8417 -0.1127 -0.8982 0.1931  977  LEU B N   
19741 C CA  . LEU C 977  ? 2.4668 0.9031 1.7303 -0.1261 -0.8639 0.1835  977  LEU B CA  
19742 C C   . LEU C 977  ? 2.4329 0.8917 1.7128 -0.1343 -0.8157 0.1865  977  LEU B C   
19743 O O   . LEU C 977  ? 2.4757 0.9378 1.7164 -0.1240 -0.7946 0.1771  977  LEU B O   
19744 C CB  . LEU C 977  ? 2.4795 0.9101 1.6816 -0.1114 -0.8689 0.1656  977  LEU B CB  
19745 C CG  . LEU C 977  ? 2.4783 0.9328 1.6644 -0.1189 -0.8420 0.1523  977  LEU B CG  
19746 C CD1 . LEU C 977  ? 2.4671 0.9154 1.6526 -0.1220 -0.8710 0.1483  977  LEU B CD1 
19747 C CD2 . LEU C 977  ? 2.5585 1.0082 1.6845 -0.1003 -0.8334 0.1384  977  LEU B CD2 
19748 N N   . SER C 978  ? 2.6047 1.0779 1.9419 -0.1529 -0.7980 0.1997  978  SER B N   
19749 C CA  . SER C 978  ? 2.6524 1.1438 2.0101 -0.1611 -0.7533 0.2053  978  SER B CA  
19750 C C   . SER C 978  ? 2.7310 1.2530 2.0993 -0.1802 -0.7103 0.1983  978  SER B C   
19751 O O   . SER C 978  ? 2.7557 1.2905 2.1658 -0.1999 -0.7048 0.2033  978  SER B O   
19752 C CB  . SER C 978  ? 2.6189 1.1080 2.0340 -0.1699 -0.7556 0.2249  978  SER B CB  
19753 O OG  . SER C 978  ? 2.5086 1.0119 1.9390 -0.1753 -0.7130 0.2305  978  SER B OG  
19754 N N   . VAL C 979  ? 2.2769 0.8104 1.6074 -0.1752 -0.6792 0.1868  979  VAL B N   
19755 C CA  . VAL C 979  ? 2.2081 0.7710 1.5412 -0.1926 -0.6392 0.1786  979  VAL B CA  
19756 C C   . VAL C 979  ? 2.1876 0.7672 1.5333 -0.2012 -0.5905 0.1825  979  VAL B C   
19757 O O   . VAL C 979  ? 2.2485 0.8236 1.5579 -0.1871 -0.5773 0.1770  979  VAL B O   
19758 C CB  . VAL C 979  ? 2.2065 0.7739 1.4820 -0.1819 -0.6397 0.1596  979  VAL B CB  
19759 C CG1 . VAL C 979  ? 2.1532 0.7476 1.4401 -0.2017 -0.6171 0.1533  979  VAL B CG1 
19760 C CG2 . VAL C 979  ? 2.2432 0.7848 1.4880 -0.1634 -0.6891 0.1548  979  VAL B CG2 
19761 N N   . LYS C 980  ? 2.9612 1.5591 2.3569 -0.2246 -0.5626 0.1915  980  LYS B N   
19762 C CA  . LYS C 980  ? 2.9725 1.5859 2.3820 -0.2346 -0.5139 0.1956  980  LYS B CA  
19763 C C   . LYS C 980  ? 2.9183 1.5605 2.3577 -0.2627 -0.4732 0.1950  980  LYS B C   
19764 O O   . LYS C 980  ? 2.9014 1.5486 2.3784 -0.2787 -0.4827 0.2004  980  LYS B O   
19765 C CB  . LYS C 980  ? 2.9856 1.5850 2.4320 -0.2316 -0.5176 0.2135  980  LYS B CB  
19766 C CG  . LYS C 980  ? 2.9922 1.5728 2.4702 -0.2285 -0.5642 0.2250  980  LYS B CG  
19767 C CD  . LYS C 980  ? 3.0243 1.5779 2.4624 -0.2019 -0.6067 0.2222  980  LYS B CD  
19768 C CE  . LYS C 980  ? 3.0121 1.5572 2.4338 -0.1878 -0.5913 0.2264  980  LYS B CE  
19769 N NZ  . LYS C 980  ? 3.0495 1.5682 2.4261 -0.1618 -0.6285 0.2223  980  LYS B NZ  
19770 N N   . GLY C 981  ? 2.3315 0.9922 1.7528 -0.2691 -0.4276 0.1882  981  GLY B N   
19771 C CA  . GLY C 981  ? 2.2645 0.9521 1.7129 -0.2967 -0.3843 0.1884  981  GLY B CA  
19772 C C   . GLY C 981  ? 2.2045 0.8926 1.7148 -0.3139 -0.3684 0.2062  981  GLY B C   
19773 O O   . GLY C 981  ? 2.2217 0.8961 1.7458 -0.3049 -0.3677 0.2172  981  GLY B O   
19774 N N   . LEU C 982  ? 1.9420 0.6455 1.4899 -0.3388 -0.3556 0.2093  982  LEU B N   
19775 C CA  . LEU C 982  ? 1.8953 0.6007 1.5044 -0.3580 -0.3376 0.2257  982  LEU B CA  
19776 C C   . LEU C 982  ? 1.9286 0.6170 1.5786 -0.3571 -0.3801 0.2377  982  LEU B C   
19777 O O   . LEU C 982  ? 1.9500 0.6178 1.5833 -0.3355 -0.4237 0.2383  982  LEU B O   
19778 C CB  . LEU C 982  ? 1.8654 0.5656 1.4808 -0.3521 -0.3104 0.2347  982  LEU B CB  
19779 C CG  . LEU C 982  ? 2.0064 0.7251 1.5972 -0.3605 -0.2567 0.2268  982  LEU B CG  
19780 C CD1 . LEU C 982  ? 1.8219 0.5540 1.4634 -0.3881 -0.2129 0.2380  982  LEU B CD1 
19781 C CD2 . LEU C 982  ? 2.0102 0.7461 1.5545 -0.3627 -0.2496 0.2078  982  LEU B CD2 
19782 N N   . LEU C 983  ? 2.4723 1.1691 2.1752 -0.3816 -0.3665 0.2471  983  LEU B N   
19783 C CA  . LEU C 983  ? 2.4833 1.1662 2.2315 -0.3847 -0.4017 0.2592  983  LEU B CA  
19784 C C   . LEU C 983  ? 2.5775 1.2473 2.3566 -0.3769 -0.4017 0.2757  983  LEU B C   
19785 O O   . LEU C 983  ? 2.5579 1.2178 2.3828 -0.3811 -0.4224 0.2890  983  LEU B O   
19786 C CB  . LEU C 983  ? 2.3973 1.0943 2.1920 -0.4149 -0.3825 0.2633  983  LEU B CB  
19787 C CG  . LEU C 983  ? 2.3753 1.0869 2.1563 -0.4297 -0.3824 0.2506  983  LEU B CG  
19788 C CD1 . LEU C 983  ? 2.3880 1.1001 2.1059 -0.4110 -0.4015 0.2337  983  LEU B CD1 
19789 C CD2 . LEU C 983  ? 2.3705 1.1057 2.1674 -0.4568 -0.3282 0.2496  983  LEU B CD2 
19790 N N   . VAL C 984  ? 2.0596 0.8926 1.9995 -0.5130 -0.2551 0.3138  984  VAL B N   
19791 C CA  . VAL C 984  ? 2.1215 0.8972 1.9922 -0.4943 -0.2521 0.3037  984  VAL B CA  
19792 C C   . VAL C 984  ? 2.3389 1.0133 2.1218 -0.4578 -0.2243 0.2932  984  VAL B C   
19793 O O   . VAL C 984  ? 2.3702 0.9965 2.0815 -0.4380 -0.2043 0.2893  984  VAL B O   
19794 C CB  . VAL C 984  ? 2.0936 0.9358 1.9644 -0.5115 -0.2230 0.3160  984  VAL B CB  
19795 C CG1 . VAL C 984  ? 2.0953 0.9563 1.9367 -0.5108 -0.1643 0.3271  984  VAL B CG1 
19796 C CG2 . VAL C 984  ? 2.1062 0.9019 1.9245 -0.4971 -0.2309 0.3072  984  VAL B CG2 
19797 N N   . GLY C 985  ? 2.9858 1.6293 2.7766 -0.4480 -0.2249 0.2888  985  GLY B N   
19798 C CA  . GLY C 985  ? 3.0441 1.6150 2.7565 -0.4059 -0.2044 0.2729  985  GLY B CA  
19799 C C   . GLY C 985  ? 3.0919 1.6124 2.7628 -0.3643 -0.2442 0.2400  985  GLY B C   
19800 O O   . GLY C 985  ? 3.1967 1.6700 2.7885 -0.3251 -0.2283 0.2223  985  GLY B O   
19801 N N   . GLU C 986  ? 2.3067 0.8379 2.0296 -0.3744 -0.2966 0.2323  986  GLU B N   
19802 C CA  . GLU C 986  ? 2.3398 0.8254 2.0250 -0.3397 -0.3376 0.2033  986  GLU B CA  
19803 C C   . GLU C 986  ? 2.3343 0.8105 1.9698 -0.3286 -0.3449 0.1988  986  GLU B C   
19804 O O   . GLU C 986  ? 2.4251 0.8548 1.9915 -0.2925 -0.3530 0.1779  986  GLU B O   
19805 C CB  . GLU C 986  ? 2.3298 0.8328 2.0896 -0.3577 -0.3929 0.1997  986  GLU B CB  
19806 C CG  . GLU C 986  ? 2.4226 0.8730 2.1514 -0.3222 -0.4290 0.1698  986  GLU B CG  
19807 C CD  . GLU C 986  ? 2.5130 0.9221 2.2007 -0.2910 -0.3985 0.1549  986  GLU B CD  
19808 O OE1 . GLU C 986  ? 2.5367 0.9247 2.2467 -0.2803 -0.4232 0.1395  986  GLU B OE1 
19809 O OE2 . GLU C 986  ? 2.5583 0.9568 2.1911 -0.2775 -0.3504 0.1585  986  GLU B OE2 
19810 N N   . ILE C 987  ? 2.2212 0.7443 1.8952 -0.3618 -0.3414 0.2194  987  ILE B N   
19811 C CA  . ILE C 987  ? 2.2094 0.7305 1.8422 -0.3549 -0.3398 0.2198  987  ILE B CA  
19812 C C   . ILE C 987  ? 2.2868 0.7801 1.8411 -0.3320 -0.2876 0.2206  987  ILE B C   
19813 O O   . ILE C 987  ? 2.3255 0.7966 1.8239 -0.3113 -0.2869 0.2136  987  ILE B O   
19814 C CB  . ILE C 987  ? 2.1091 0.6921 1.8110 -0.3989 -0.3503 0.2408  987  ILE B CB  
19815 C CG1 . ILE C 987  ? 2.1502 0.7583 1.9218 -0.4187 -0.4079 0.2383  987  ILE B CG1 
19816 C CG2 . ILE C 987  ? 2.0488 0.6322 1.7127 -0.3920 -0.3467 0.2419  987  ILE B CG2 
19817 C CD1 . ILE C 987  ? 2.1318 0.8094 1.9831 -0.4684 -0.4178 0.2599  987  ILE B CD1 
19818 N N   . LEU C 988  ? 2.0638 0.5586 1.6131 -0.3357 -0.2456 0.2301  988  LEU B N   
19819 C CA  . LEU C 988  ? 2.1190 0.5857 1.5893 -0.3127 -0.1984 0.2305  988  LEU B CA  
19820 C C   . LEU C 988  ? 2.2214 0.6303 1.6186 -0.2670 -0.2035 0.2038  988  LEU B C   
19821 O O   . LEU C 988  ? 2.2951 0.6744 1.6214 -0.2418 -0.1934 0.1951  988  LEU B O   
19822 C CB  . LEU C 988  ? 2.1045 0.5960 1.5903 -0.3351 -0.1496 0.2535  988  LEU B CB  
19823 C CG  . LEU C 988  ? 2.0609 0.5879 1.5537 -0.3652 -0.1126 0.2796  988  LEU B CG  
19824 C CD1 . LEU C 988  ? 2.0693 0.6072 1.5543 -0.3785 -0.0620 0.3000  988  LEU B CD1 
19825 C CD2 . LEU C 988  ? 2.0565 0.5592 1.4817 -0.3431 -0.1051 0.2727  988  LEU B CD2 
19826 N N   . SER C 989  ? 2.4575 0.8518 1.8744 -0.2577 -0.2201 0.1906  989  SER B N   
19827 C CA  . SER C 989  ? 2.5209 0.8624 1.8738 -0.2165 -0.2245 0.1631  989  SER B CA  
19828 C C   . SER C 989  ? 2.5276 0.8348 1.8363 -0.1918 -0.2615 0.1416  989  SER B C   
19829 O O   . SER C 989  ? 2.5711 0.8387 1.8035 -0.1604 -0.2519 0.1250  989  SER B O   
19830 C CB  . SER C 989  ? 2.5666 0.9028 1.9610 -0.2147 -0.2369 0.1536  989  SER B CB  
19831 O OG  . SER C 989  ? 2.6722 0.9605 2.0032 -0.1763 -0.2316 0.1278  989  SER B OG  
19832 N N   . ALA C 990  ? 3.0121 1.3370 2.3693 -0.2081 -0.3043 0.1432  990  ALA B N   
19833 C CA  . ALA C 990  ? 3.0583 1.3577 2.3789 -0.1905 -0.3397 0.1288  990  ALA B CA  
19834 C C   . ALA C 990  ? 3.0805 1.3636 2.3291 -0.1739 -0.3114 0.1311  990  ALA B C   
19835 O O   . ALA C 990  ? 3.1826 1.4236 2.3607 -0.1432 -0.3088 0.1132  990  ALA B O   
19836 C CB  . ALA C 990  ? 3.0135 1.3490 2.3985 -0.2181 -0.3799 0.1400  990  ALA B CB  
19837 N N   . VAL C 991  ? 2.3490 0.6669 1.6171 -0.1957 -0.2900 0.1532  991  VAL B N   
19838 C CA  . VAL C 991  ? 2.3813 0.6877 1.5909 -0.1834 -0.2679 0.1577  991  VAL B CA  
19839 C C   . VAL C 991  ? 2.4510 0.7334 1.5939 -0.1641 -0.2221 0.1557  991  VAL B C   
19840 O O   . VAL C 991  ? 2.4929 0.7613 1.5815 -0.1514 -0.2051 0.1579  991  VAL B O   
19841 C CB  . VAL C 991  ? 2.0153 0.3674 1.2715 -0.2141 -0.2621 0.1808  991  VAL B CB  
19842 C CG1 . VAL C 991  ? 2.0210 0.3664 1.2255 -0.2059 -0.2298 0.1896  991  VAL B CG1 
19843 C CG2 . VAL C 991  ? 2.0038 0.3711 1.3027 -0.2240 -0.3126 0.1786  991  VAL B CG2 
19844 N N   . LEU C 992  ? 2.6589 0.9362 1.8040 -0.1609 -0.2036 0.1515  992  LEU B N   
19845 C CA  . LEU C 992  ? 2.7680 1.0289 1.8511 -0.1455 -0.1591 0.1526  992  LEU B CA  
19846 C C   . LEU C 992  ? 3.0269 1.2568 2.0769 -0.1208 -0.1559 0.1315  992  LEU B C   
19847 O O   . LEU C 992  ? 3.0967 1.3336 2.1436 -0.1227 -0.1229 0.1382  992  LEU B O   
19848 C CB  . LEU C 992  ? 2.6227 0.9202 1.7332 -0.1728 -0.1173 0.1800  992  LEU B CB  
19849 C CG  . LEU C 992  ? 2.5026 0.8318 1.6362 -0.1983 -0.1062 0.2025  992  LEU B CG  
19850 C CD1 . LEU C 992  ? 2.4272 0.7918 1.5932 -0.2282 -0.0666 0.2282  992  LEU B CD1 
19851 C CD2 . LEU C 992  ? 2.5363 0.8427 1.6002 -0.1792 -0.0950 0.2009  992  LEU B CD2 
19852 N N   . SER C 993  ? 3.4885 1.6846 2.5116 -0.0979 -0.1891 0.1065  993  SER B N   
19853 C CA  . SER C 993  ? 3.6547 1.8204 2.6488 -0.0743 -0.1895 0.0828  993  SER B CA  
19854 C C   . SER C 993  ? 3.8331 1.9598 2.7769 -0.0499 -0.2207 0.0580  993  SER B C   
19855 O O   . SER C 993  ? 3.9216 2.0172 2.8070 -0.0253 -0.2128 0.0375  993  SER B O   
19856 C CB  . SER C 993  ? 3.6190 1.7980 2.6858 -0.0868 -0.2065 0.0805  993  SER B CB  
19857 O OG  . SER C 993  ? 3.5563 1.7741 2.6724 -0.1128 -0.1769 0.1059  993  SER B OG  
19858 N N   . GLN C 994  ? 3.2377 1.3680 2.2055 -0.0586 -0.2571 0.0606  994  GLN B N   
19859 C CA  . GLN C 994  ? 3.3908 1.4901 2.3044 -0.0406 -0.2813 0.0466  994  GLN B CA  
19860 C C   . GLN C 994  ? 3.3876 1.5009 2.2776 -0.0464 -0.2625 0.0662  994  GLN B C   
19861 O O   . GLN C 994  ? 3.2939 1.4409 2.2197 -0.0668 -0.2397 0.0886  994  GLN B O   
19862 C CB  . GLN C 994  ? 3.4491 1.5437 2.3986 -0.0463 -0.3330 0.0400  994  GLN B CB  
19863 C CG  . GLN C 994  ? 3.4221 1.5569 2.4363 -0.0742 -0.3491 0.0636  994  GLN B CG  
19864 C CD  . GLN C 994  ? 3.4698 1.5967 2.4793 -0.0737 -0.3919 0.0625  994  GLN B CD  
19865 O OE1 . GLN C 994  ? 3.5539 1.6442 2.5197 -0.0552 -0.4155 0.0440  994  GLN B OE1 
19866 N NE2 . GLN C 994  ? 3.4038 1.5665 2.4581 -0.0954 -0.4015 0.0832  994  GLN B NE2 
19867 N N   . GLU C 995  ? 3.4698 1.5571 2.2993 -0.0296 -0.2706 0.0582  995  GLU B N   
19868 C CA  . GLU C 995  ? 3.5166 1.6157 2.3321 -0.0353 -0.2622 0.0765  995  GLU B CA  
19869 C C   . GLU C 995  ? 3.5153 1.6146 2.3546 -0.0404 -0.3057 0.0778  995  GLU B C   
19870 O O   . GLU C 995  ? 3.5068 1.5994 2.3737 -0.0417 -0.3393 0.0664  995  GLU B O   
19871 C CB  . GLU C 995  ? 3.6351 1.7092 2.3698 -0.0154 -0.2416 0.0707  995  GLU B CB  
19872 C CG  . GLU C 995  ? 3.6681 1.7568 2.3827 -0.0187 -0.1946 0.0850  995  GLU B CG  
19873 C CD  . GLU C 995  ? 3.7584 1.8265 2.4152 -0.0003 -0.1719 0.0690  995  GLU B CD  
19874 O OE1 . GLU C 995  ? 3.8185 1.8615 2.4555 0.0146  -0.1911 0.0449  995  GLU B OE1 
19875 O OE2 . GLU C 995  ? 3.7658 1.8434 2.3957 -0.0014 -0.1349 0.0806  995  GLU B OE2 
19876 N N   . GLY C 996  ? 3.8394 1.9469 2.6687 -0.0435 -0.3055 0.0926  996  GLY B N   
19877 C CA  . GLY C 996  ? 3.8692 1.9781 2.7156 -0.0474 -0.3452 0.0964  996  GLY B CA  
19878 C C   . GLY C 996  ? 3.8303 1.9713 2.7546 -0.0698 -0.3703 0.1043  996  GLY B C   
19879 O O   . GLY C 996  ? 3.8275 1.9697 2.7830 -0.0746 -0.3813 0.0946  996  GLY B O   
19880 N N   . ILE C 997  ? 3.8853 2.0539 2.8425 -0.0840 -0.3803 0.1220  997  ILE B N   
19881 C CA  . ILE C 997  ? 3.8333 2.0380 2.8644 -0.1078 -0.4077 0.1311  997  ILE B CA  
19882 C C   . ILE C 997  ? 3.9092 2.0954 2.9466 -0.1033 -0.4540 0.1159  997  ILE B C   
19883 O O   . ILE C 997  ? 3.9871 2.1338 2.9692 -0.0826 -0.4687 0.1018  997  ILE B O   
19884 C CB  . ILE C 997  ? 3.7506 1.9814 2.8017 -0.1181 -0.4161 0.1491  997  ILE B CB  
19885 C CG1 . ILE C 997  ? 3.7940 1.9985 2.8059 -0.1020 -0.4508 0.1450  997  ILE B CG1 
19886 C CG2 . ILE C 997  ? 3.7339 1.9716 2.7638 -0.1172 -0.3705 0.1612  997  ILE B CG2 
19887 C CD1 . ILE C 997  ? 3.7662 1.9892 2.7836 -0.1056 -0.4519 0.1624  997  ILE B CD1 
19888 N N   . ASN C 998  ? 3.7221 1.9366 2.8258 -0.1241 -0.4777 0.1191  998  ASN B N   
19889 C CA  . ASN C 998  ? 3.7670 1.9617 2.8778 -0.1204 -0.5193 0.1037  998  ASN B CA  
19890 C C   . ASN C 998  ? 3.6348 1.8691 2.8246 -0.1478 -0.5545 0.1128  998  ASN B C   
19891 O O   . ASN C 998  ? 3.6063 1.8805 2.8533 -0.1706 -0.5372 0.1247  998  ASN B O   
19892 C CB  . ASN C 998  ? 3.9004 2.0644 2.9861 -0.1053 -0.4995 0.0843  998  ASN B CB  
19893 C CG  . ASN C 998  ? 3.9795 2.1410 3.1072 -0.1122 -0.5322 0.0730  998  ASN B CG  
19894 O OD1 . ASN C 998  ? 4.0406 2.1865 3.1648 -0.1097 -0.5763 0.0657  998  ASN B OD1 
19895 N ND2 . ASN C 998  ? 3.9804 2.1567 3.1471 -0.1212 -0.5108 0.0726  998  ASN B ND2 
19896 N N   . ILE C 999  ? 3.5462 1.7706 2.7380 -0.1475 -0.6045 0.1081  999  ILE B N   
19897 C CA  . ILE C 999  ? 3.3792 1.6403 2.6425 -0.1736 -0.6455 0.1160  999  ILE B CA  
19898 C C   . ILE C 999  ? 3.2562 1.5170 2.5593 -0.1811 -0.6474 0.1059  999  ILE B C   
19899 O O   . ILE C 999  ? 3.2663 1.4842 2.5311 -0.1600 -0.6400 0.0864  999  ILE B O   
19900 C CB  . ILE C 999  ? 4.8198 3.0665 4.0675 -0.1702 -0.7011 0.1140  999  ILE B CB  
19901 C CG1 . ILE C 999  ? 4.8402 3.0827 4.0443 -0.1602 -0.7002 0.1244  999  ILE B CG1 
19902 C CG2 . ILE C 999  ? 4.7611 3.0529 4.0841 -0.2001 -0.7440 0.1250  999  ILE B CG2 
19903 C CD1 . ILE C 999  ? 4.7700 3.0651 4.0185 -0.1802 -0.6855 0.1457  999  ILE B CD1 
19904 N N   . LEU C 1000 ? 3.2993 1.6097 2.6813 -0.2121 -0.6578 0.1192  1000 LEU B N   
19905 C CA  . LEU C 1000 ? 3.1843 1.5004 2.6118 -0.2221 -0.6531 0.1137  1000 LEU B CA  
19906 C C   . LEU C 1000 ? 3.1613 1.4741 2.6245 -0.2304 -0.7080 0.1063  1000 LEU B C   
19907 O O   . LEU C 1000 ? 3.1346 1.4649 2.6555 -0.2468 -0.7140 0.1067  1000 LEU B O   
19908 C CB  . LEU C 1000 ? 3.0191 1.3902 2.5117 -0.2529 -0.6229 0.1333  1000 LEU B CB  
19909 C CG  . LEU C 1000 ? 2.9030 1.2631 2.3568 -0.2404 -0.5609 0.1349  1000 LEU B CG  
19910 C CD1 . LEU C 1000 ? 2.8021 1.2159 2.3192 -0.2736 -0.5319 0.1557  1000 LEU B CD1 
19911 C CD2 . LEU C 1000 ? 2.9227 1.2354 2.3347 -0.2136 -0.5422 0.1150  1000 LEU B CD2 
19912 N N   . THR C 1001 ? 3.3072 1.5963 2.7346 -0.2193 -0.7487 0.1004  1001 THR B N   
19913 C CA  . THR C 1001 ? 3.3167 1.5953 2.7668 -0.2245 -0.8025 0.0923  1001 THR B CA  
19914 C C   . THR C 1001 ? 3.4564 1.6720 2.8257 -0.1930 -0.8177 0.0726  1001 THR B C   
19915 O O   . THR C 1001 ? 3.5222 1.7083 2.8264 -0.1701 -0.7851 0.0663  1001 THR B O   
19916 C CB  . THR C 1001 ? 3.1776 1.5042 2.6764 -0.2529 -0.8480 0.1110  1001 THR B CB  
19917 O OG1 . THR C 1001 ? 3.0479 1.4252 2.5771 -0.2718 -0.8187 0.1307  1001 THR B OG1 
19918 C CG2 . THR C 1001 ? 3.1470 1.4986 2.7192 -0.2778 -0.8874 0.1126  1001 THR B CG2 
19919 N N   . HIS C 1002 ? 3.1339 1.3289 2.5065 -0.1932 -0.8673 0.0632  1002 HIS B N   
19920 C CA  . HIS C 1002 ? 3.2670 1.4054 2.5629 -0.1683 -0.8874 0.0472  1002 HIS B CA  
19921 C C   . HIS C 1002 ? 2.9487 1.1007 2.2257 -0.1756 -0.9229 0.0637  1002 HIS B C   
19922 O O   . HIS C 1002 ? 3.0293 1.1403 2.2429 -0.1595 -0.9432 0.0562  1002 HIS B O   
19923 C CB  . HIS C 1002 ? 3.4205 1.5231 2.7210 -0.1629 -0.9213 0.0275  1002 HIS B CB  
19924 C CG  . HIS C 1002 ? 3.5395 1.6153 2.8388 -0.1470 -0.8841 0.0069  1002 HIS B CG  
19925 N ND1 . HIS C 1002 ? 3.5247 1.6316 2.8973 -0.1629 -0.8718 0.0110  1002 HIS B ND1 
19926 C CD2 . HIS C 1002 ? 3.6509 1.6738 2.8853 -0.1176 -0.8572 -0.0172 1002 HIS B CD2 
19927 C CE1 . HIS C 1002 ? 3.5775 1.6512 2.9302 -0.1423 -0.8383 -0.0092 1002 HIS B CE1 
19928 N NE2 . HIS C 1002 ? 3.6529 1.6761 2.9218 -0.1145 -0.8289 -0.0276 1002 HIS B NE2 
19929 N N   . LEU C 1003 ? 2.7328 0.9440 2.0644 -0.2008 -0.9284 0.0868  1003 LEU B N   
19930 C CA  . LEU C 1003 ? 2.6650 0.8982 1.9872 -0.2097 -0.9609 0.1050  1003 LEU B CA  
19931 C C   . LEU C 1003 ? 2.7403 0.9432 1.9843 -0.1869 -0.9439 0.1067  1003 LEU B C   
19932 O O   . LEU C 1003 ? 2.7785 0.9762 1.9982 -0.1745 -0.8946 0.1058  1003 LEU B O   
19933 C CB  . LEU C 1003 ? 2.4663 0.7729 1.8651 -0.2415 -0.9627 0.1276  1003 LEU B CB  
19934 C CG  . LEU C 1003 ? 2.3461 0.6833 1.8146 -0.2684 -1.0088 0.1307  1003 LEU B CG  
19935 C CD1 . LEU C 1003 ? 2.2482 0.6378 1.7522 -0.2938 -1.0525 0.1519  1003 LEU B CD1 
19936 C CD2 . LEU C 1003 ? 2.4030 0.6849 1.8384 -0.2532 -1.0426 0.1114  1003 LEU B CD2 
19937 N N   . PRO C 1004 ? 3.1479 1.3331 2.3544 -0.1838 -0.9874 0.1113  1004 PRO B N   
19938 C CA  . PRO C 1004 ? 3.1682 1.3244 2.3029 -0.1667 -0.9882 0.1161  1004 PRO B CA  
19939 C C   . PRO C 1004 ? 3.1068 1.2961 2.2443 -0.1678 -0.9578 0.1347  1004 PRO B C   
19940 O O   . PRO C 1004 ? 3.0331 1.2778 2.2282 -0.1891 -0.9669 0.1523  1004 PRO B O   
19941 C CB  . PRO C 1004 ? 3.2251 1.3854 2.3578 -0.1785 -1.0519 0.1271  1004 PRO B CB  
19942 C CG  . PRO C 1004 ? 3.1410 1.3485 2.3556 -0.2056 -1.0809 0.1327  1004 PRO B CG  
19943 C CD  . PRO C 1004 ? 3.1236 1.3189 2.3629 -0.2012 -1.0469 0.1138  1004 PRO B CD  
19944 N N   . LYS C 1005 ? 2.8377 0.9933 1.9128 -0.1461 -0.9252 0.1308  1005 LYS B N   
19945 C CA  . LYS C 1005 ? 2.8546 1.0342 1.9285 -0.1437 -0.8896 0.1457  1005 LYS B CA  
19946 C C   . LYS C 1005 ? 2.8355 1.0448 1.9148 -0.1525 -0.9189 0.1699  1005 LYS B C   
19947 O O   . LYS C 1005 ? 2.7781 1.0088 1.8598 -0.1508 -0.8931 0.1836  1005 LYS B O   
19948 C CB  . LYS C 1005 ? 2.9834 1.1175 1.9886 -0.1186 -0.8492 0.1344  1005 LYS B CB  
19949 C CG  . LYS C 1005 ? 3.0909 1.2037 2.0921 -0.1092 -0.8115 0.1126  1005 LYS B CG  
19950 C CD  . LYS C 1005 ? 3.1030 1.2540 2.1488 -0.1174 -0.7667 0.1198  1005 LYS B CD  
19951 C CE  . LYS C 1005 ? 3.1454 1.3090 2.1719 -0.1124 -0.7406 0.1359  1005 LYS B CE  
19952 N NZ  . LYS C 1005 ? 3.0975 1.2967 2.1648 -0.1217 -0.6968 0.1432  1005 LYS B NZ  
19953 N N   . GLY C 1006 ? 3.0200 1.2316 2.1029 -0.1625 -0.9731 0.1756  1006 GLY B N   
19954 C CA  . GLY C 1006 ? 3.0558 1.2858 2.1284 -0.1676 -1.0061 0.1980  1006 GLY B CA  
19955 C C   . GLY C 1006 ? 2.9373 1.2234 2.0543 -0.1784 -0.9913 0.2183  1006 GLY B C   
19956 O O   . GLY C 1006 ? 2.9181 1.2008 2.0052 -0.1674 -0.9762 0.2307  1006 GLY B O   
19957 N N   . SER C 1007 ? 3.0849 1.4233 2.2753 -0.2012 -0.9959 0.2217  1007 SER B N   
19958 C CA  . SER C 1007 ? 2.9830 1.3822 2.2252 -0.2169 -0.9877 0.2398  1007 SER B CA  
19959 C C   . SER C 1007 ? 2.9028 1.2997 2.1338 -0.2038 -0.9299 0.2409  1007 SER B C   
19960 O O   . SER C 1007 ? 2.9009 1.2493 2.0797 -0.1821 -0.8982 0.2292  1007 SER B O   
19961 C CB  . SER C 1007 ? 2.9367 1.3905 2.2607 -0.2464 -0.9970 0.2396  1007 SER B CB  
19962 O OG  . SER C 1007 ? 2.8901 1.4042 2.2654 -0.2633 -0.9844 0.2546  1007 SER B OG  
19963 N N   . ALA C 1008 ? 2.6076 1.0582 1.8874 -0.2181 -0.9182 0.2549  1008 ALA B N   
19964 C CA  . ALA C 1008 ? 2.5832 1.0420 1.8709 -0.2129 -0.8617 0.2549  1008 ALA B CA  
19965 C C   . ALA C 1008 ? 2.5116 0.9896 1.8466 -0.2293 -0.8357 0.2439  1008 ALA B C   
19966 O O   . ALA C 1008 ? 2.5260 0.9755 1.8391 -0.2177 -0.7927 0.2327  1008 ALA B O   
19967 C CB  . ALA C 1008 ? 2.5639 1.0726 1.8862 -0.2225 -0.8606 0.2736  1008 ALA B CB  
19968 N N   . GLU C 1009 ? 2.5838 1.1126 1.9840 -0.2581 -0.8640 0.2487  1009 GLU B N   
19969 C CA  . GLU C 1009 ? 2.5250 1.0766 1.9770 -0.2788 -0.8493 0.2411  1009 GLU B CA  
19970 C C   . GLU C 1009 ? 2.5372 1.0342 1.9472 -0.2589 -0.8158 0.2239  1009 GLU B C   
19971 O O   . GLU C 1009 ? 2.5205 1.0203 1.9393 -0.2599 -0.7675 0.2209  1009 GLU B O   
19972 C CB  . GLU C 1009 ? 2.4923 1.0700 1.9870 -0.3017 -0.9052 0.2419  1009 GLU B CB  
19973 C CG  . GLU C 1009 ? 2.3719 0.9977 1.9433 -0.3342 -0.8977 0.2416  1009 GLU B CG  
19974 C CD  . GLU C 1009 ? 2.3245 0.9803 1.9425 -0.3592 -0.9557 0.2441  1009 GLU B CD  
19975 O OE1 . GLU C 1009 ? 2.3460 0.9851 1.9349 -0.3513 -1.0037 0.2461  1009 GLU B OE1 
19976 O OE2 . GLU C 1009 ? 2.2701 0.9669 1.9538 -0.3882 -0.9533 0.2452  1009 GLU B OE2 
19977 N N   . ALA C 1010 ? 2.8386 1.2863 2.2009 -0.2413 -0.8419 0.2128  1010 ALA B N   
19978 C CA  . ALA C 1010 ? 2.9111 1.3084 2.2351 -0.2230 -0.8160 0.1942  1010 ALA B CA  
19979 C C   . ALA C 1010 ? 2.8968 1.2684 2.1754 -0.2023 -0.7610 0.1917  1010 ALA B C   
19980 O O   . ALA C 1010 ? 2.8453 1.2035 2.1201 -0.1979 -0.7225 0.1819  1010 ALA B O   
19981 C CB  . ALA C 1010 ? 3.0347 1.3824 2.3081 -0.2065 -0.8533 0.1830  1010 ALA B CB  
19982 N N   . GLU C 1011 ? 3.4779 1.8434 2.7223 -0.1899 -0.7586 0.2018  1011 GLU B N   
19983 C CA  . GLU C 1011 ? 3.5290 1.8725 2.7319 -0.1716 -0.7099 0.2015  1011 GLU B CA  
19984 C C   . GLU C 1011 ? 3.4557 1.8404 2.7058 -0.1876 -0.6681 0.2091  1011 GLU B C   
19985 O O   . GLU C 1011 ? 3.4728 1.8409 2.6944 -0.1757 -0.6230 0.2075  1011 GLU B O   
19986 C CB  . GLU C 1011 ? 3.6010 1.9297 2.7608 -0.1561 -0.7203 0.2126  1011 GLU B CB  
19987 C CG  . GLU C 1011 ? 3.6805 1.9554 2.7650 -0.1290 -0.6940 0.2046  1011 GLU B CG  
19988 C CD  . GLU C 1011 ? 3.7741 2.0003 2.8072 -0.1156 -0.7197 0.1895  1011 GLU B CD  
19989 O OE1 . GLU C 1011 ? 3.8120 2.0373 2.8452 -0.1205 -0.7664 0.1932  1011 GLU B OE1 
19990 O OE2 . GLU C 1011 ? 3.8167 2.0058 2.8074 -0.1008 -0.6933 0.1739  1011 GLU B OE2 
19991 N N   . LEU C 1012 ? 2.1996 0.6391 1.5206 -0.2163 -0.6839 0.2180  1012 LEU B N   
19992 C CA  . LEU C 1012 ? 2.0777 0.5600 1.4501 -0.2377 -0.6457 0.2246  1012 LEU B CA  
19993 C C   . LEU C 1012 ? 2.0970 0.5787 1.4931 -0.2491 -0.6300 0.2152  1012 LEU B C   
19994 O O   . LEU C 1012 ? 2.0947 0.5835 1.4987 -0.2547 -0.5846 0.2165  1012 LEU B O   
19995 C CB  . LEU C 1012 ? 1.9369 0.4830 1.3760 -0.2662 -0.6686 0.2389  1012 LEU B CB  
19996 C CG  . LEU C 1012 ? 1.9013 0.4617 1.3318 -0.2594 -0.6625 0.2512  1012 LEU B CG  
19997 C CD1 . LEU C 1012 ? 1.8520 0.4625 1.3292 -0.2788 -0.7077 0.2628  1012 LEU B CD1 
19998 C CD2 . LEU C 1012 ? 1.8633 0.4390 1.3057 -0.2648 -0.6066 0.2554  1012 LEU B CD2 
19999 N N   . MET C 1013 ? 2.8790 1.3504 2.2844 -0.2519 -0.6679 0.2065  1013 MET B N   
20000 C CA  . MET C 1013 ? 2.8647 1.3375 2.2993 -0.2633 -0.6569 0.1985  1013 MET B CA  
20001 C C   . MET C 1013 ? 2.9473 1.3718 2.3263 -0.2387 -0.6138 0.1862  1013 MET B C   
20002 O O   . MET C 1013 ? 2.9657 1.3836 2.3591 -0.2426 -0.6014 0.1784  1013 MET B O   
20003 C CB  . MET C 1013 ? 2.8652 1.3331 2.3203 -0.2695 -0.7087 0.1910  1013 MET B CB  
20004 C CG  . MET C 1013 ? 2.8186 1.3266 2.3471 -0.3002 -0.7106 0.1941  1013 MET B CG  
20005 S SD  . MET C 1013 ? 3.0040 1.5882 2.5997 -0.3362 -0.6978 0.2154  1013 MET B SD  
20006 C CE  . MET C 1013 ? 2.7305 1.3426 2.3436 -0.3455 -0.7633 0.2233  1013 MET B CE  
20007 N N   . SER C 1014 ? 2.6190 1.0120 1.9359 -0.2141 -0.5925 0.1853  1014 SER B N   
20008 C CA  . SER C 1014 ? 2.6574 1.0079 1.9162 -0.1908 -0.5513 0.1749  1014 SER B CA  
20009 C C   . SER C 1014 ? 2.5449 0.9198 1.8191 -0.2018 -0.4996 0.1856  1014 SER B C   
20010 O O   . SER C 1014 ? 2.5147 0.8751 1.7725 -0.1971 -0.4643 0.1803  1014 SER B O   
20011 C CB  . SER C 1014 ? 2.8038 1.1097 1.9874 -0.1614 -0.5555 0.1699  1014 SER B CB  
20012 O OG  . SER C 1014 ? 2.8258 1.1475 2.0042 -0.1609 -0.5423 0.1846  1014 SER B OG  
20013 N N   . VAL C 1015 ? 2.5394 0.9516 1.8439 -0.2168 -0.4953 0.2009  1015 VAL B N   
20014 C CA  . VAL C 1015 ? 2.5213 0.9543 1.8352 -0.2271 -0.4462 0.2116  1015 VAL B CA  
20015 C C   . VAL C 1015 ? 2.4766 0.9497 1.8525 -0.2586 -0.4291 0.2179  1015 VAL B C   
20016 O O   . VAL C 1015 ? 2.5026 0.9808 1.8748 -0.2652 -0.3833 0.2238  1015 VAL B O   
20017 C CB  . VAL C 1015 ? 2.5841 1.0440 1.9119 -0.2330 -0.4450 0.2250  1015 VAL B CB  
20018 C CG1 . VAL C 1015 ? 2.5661 1.0468 1.9236 -0.2397 -0.4979 0.2277  1015 VAL B CG1 
20019 C CG2 . VAL C 1015 ? 2.5367 1.0422 1.9136 -0.2618 -0.4085 0.2377  1015 VAL B CG2 
20020 N N   . VAL C 1016 ? 2.1183 0.6202 1.5507 -0.2794 -0.4673 0.2180  1016 VAL B N   
20021 C CA  . VAL C 1016 ? 1.9667 0.5131 1.4676 -0.3142 -0.4580 0.2260  1016 VAL B CA  
20022 C C   . VAL C 1016 ? 1.9040 0.4294 1.3906 -0.3104 -0.4239 0.2216  1016 VAL B C   
20023 O O   . VAL C 1016 ? 1.8407 0.3763 1.3243 -0.3191 -0.3781 0.2309  1016 VAL B O   
20024 C CB  . VAL C 1016 ? 1.9077 0.4893 1.4717 -0.3375 -0.5112 0.2272  1016 VAL B CB  
20025 C CG1 . VAL C 1016 ? 1.8572 0.4661 1.4799 -0.3656 -0.5078 0.2305  1016 VAL B CG1 
20026 C CG2 . VAL C 1016 ? 1.8682 0.4995 1.4737 -0.3591 -0.5276 0.2396  1016 VAL B CG2 
20027 N N   . PRO C 1017 ? 2.0493 0.5445 1.5244 -0.2968 -0.4448 0.2076  1017 PRO B N   
20028 C CA  . PRO C 1017 ? 2.0740 0.5571 1.5442 -0.2962 -0.4101 0.2055  1017 PRO B CA  
20029 C C   . PRO C 1017 ? 2.1088 0.5781 1.5319 -0.2866 -0.3525 0.2114  1017 PRO B C   
20030 O O   . PRO C 1017 ? 2.0725 0.5535 1.5135 -0.3001 -0.3215 0.2183  1017 PRO B O   
20031 C CB  . PRO C 1017 ? 2.1191 0.5525 1.5501 -0.2671 -0.4346 0.1845  1017 PRO B CB  
20032 C CG  . PRO C 1017 ? 2.1117 0.5539 1.5697 -0.2724 -0.4913 0.1810  1017 PRO B CG  
20033 C CD  . PRO C 1017 ? 2.0894 0.5595 1.5542 -0.2818 -0.4966 0.1937  1017 PRO B CD  
20034 N N   . VAL C 1018 ? 2.1135 0.5598 1.4797 -0.2654 -0.3385 0.2104  1018 VAL B N   
20035 C CA  . VAL C 1018 ? 2.2131 0.6548 1.5440 -0.2630 -0.2851 0.2197  1018 VAL B CA  
20036 C C   . VAL C 1018 ? 2.1877 0.6809 1.5721 -0.2978 -0.2663 0.2393  1018 VAL B C   
20037 O O   . VAL C 1018 ? 2.1532 0.6703 1.5646 -0.3211 -0.2343 0.2513  1018 VAL B O   
20038 C CB  . VAL C 1018 ? 2.3284 0.7302 1.5835 -0.2312 -0.2750 0.2136  1018 VAL B CB  
20039 C CG1 . VAL C 1018 ? 2.3685 0.7594 1.5805 -0.2267 -0.2214 0.2212  1018 VAL B CG1 
20040 C CG2 . VAL C 1018 ? 2.4090 0.7649 1.6169 -0.2007 -0.3030 0.1933  1018 VAL B CG2 
20041 N N   . PHE C 1019 ? 2.5618 1.0742 1.9636 -0.3031 -0.2860 0.2433  1019 PHE B N   
20042 C CA  . PHE C 1019 ? 2.4964 1.0571 1.9448 -0.3350 -0.2652 0.2601  1019 PHE B CA  
20043 C C   . PHE C 1019 ? 2.3975 1.0010 1.9068 -0.3740 -0.2463 0.2726  1019 PHE B C   
20044 O O   . PHE C 1019 ? 2.3842 0.9996 1.8901 -0.3890 -0.2010 0.2852  1019 PHE B O   
20045 C CB  . PHE C 1019 ? 2.4870 1.0793 1.9761 -0.3458 -0.3029 0.2619  1019 PHE B CB  
20046 C CG  . PHE C 1019 ? 2.3989 1.0516 1.9544 -0.3867 -0.2889 0.2770  1019 PHE B CG  
20047 C CD1 . PHE C 1019 ? 2.3671 1.0268 1.9096 -0.3949 -0.2409 0.2872  1019 PHE B CD1 
20048 C CD2 . PHE C 1019 ? 2.3282 1.0312 1.9580 -0.4186 -0.3239 0.2808  1019 PHE B CD2 
20049 C CE1 . PHE C 1019 ? 2.3004 1.0148 1.9021 -0.4337 -0.2266 0.2998  1019 PHE B CE1 
20050 C CE2 . PHE C 1019 ? 2.2632 1.0243 1.9538 -0.4584 -0.3109 0.2937  1019 PHE B CE2 
20051 C CZ  . PHE C 1019 ? 2.2590 1.0255 1.9355 -0.4661 -0.2614 0.3027  1019 PHE B CZ  
20052 N N   . TYR C 1020 ? 1.9388 0.5662 1.5042 -0.3921 -0.2818 0.2707  1020 TYR B N   
20053 C CA  . TYR C 1020 ? 1.8625 0.5313 1.4900 -0.4306 -0.2676 0.2837  1020 TYR B CA  
20054 C C   . TYR C 1020 ? 1.8568 0.4995 1.4454 -0.4222 -0.2217 0.2875  1020 TYR B C   
20055 O O   . TYR C 1020 ? 1.8289 0.5106 1.4390 -0.4476 -0.1838 0.3020  1020 TYR B O   
20056 C CB  . TYR C 1020 ? 1.8608 0.5493 1.5461 -0.4450 -0.3156 0.2792  1020 TYR B CB  
20057 C CG  . TYR C 1020 ? 1.8742 0.6032 1.6084 -0.4641 -0.3570 0.2810  1020 TYR B CG  
20058 C CD1 . TYR C 1020 ? 1.8945 0.6456 1.6281 -0.4716 -0.3438 0.2877  1020 TYR B CD1 
20059 C CD2 . TYR C 1020 ? 1.8997 0.6454 1.6800 -0.4743 -0.4102 0.2761  1020 TYR B CD2 
20060 C CE1 . TYR C 1020 ? 1.9079 0.6991 1.6858 -0.4886 -0.3813 0.2895  1020 TYR B CE1 
20061 C CE2 . TYR C 1020 ? 1.9070 0.6927 1.7297 -0.4923 -0.4503 0.2788  1020 TYR B CE2 
20062 C CZ  . TYR C 1020 ? 1.9263 0.7361 1.7479 -0.4994 -0.4352 0.2855  1020 TYR B CZ  
20063 O OH  . TYR C 1020 ? 1.9432 0.7964 1.8075 -0.5173 -0.4752 0.2883  1020 TYR B OH  
20064 N N   . VAL C 1021 ? 1.7550 0.3449 1.2842 -0.3843 -0.2250 0.2721  1021 VAL B N   
20065 C CA  . VAL C 1021 ? 1.7739 0.3378 1.2599 -0.3727 -0.1832 0.2744  1021 VAL B CA  
20066 C C   . VAL C 1021 ? 1.7688 0.3248 1.2046 -0.3695 -0.1334 0.2855  1021 VAL B C   
20067 O O   . VAL C 1021 ? 1.7522 0.3040 1.1666 -0.3739 -0.0931 0.2957  1021 VAL B O   
20068 C CB  . VAL C 1021 ? 1.7133 0.2258 1.1511 -0.3342 -0.2014 0.2530  1021 VAL B CB  
20069 C CG1 . VAL C 1021 ? 1.7342 0.2166 1.1138 -0.3162 -0.1582 0.2532  1021 VAL B CG1 
20070 C CG2 . VAL C 1021 ? 1.7000 0.2277 1.1989 -0.3475 -0.2382 0.2480  1021 VAL B CG2 
20071 N N   . PHE C 1022 ? 2.0572 0.6132 1.4769 -0.3637 -0.1362 0.2854  1022 PHE B N   
20072 C CA  . PHE C 1022 ? 2.1232 0.6728 1.5007 -0.3629 -0.0912 0.2964  1022 PHE B CA  
20073 C C   . PHE C 1022 ? 2.0932 0.7036 1.5321 -0.4063 -0.0708 0.3139  1022 PHE B C   
20074 O O   . PHE C 1022 ? 2.1130 0.7554 1.5378 -0.4140 -0.0283 0.3202  1022 PHE B O   
20075 C CB  . PHE C 1022 ? 2.1750 0.7001 1.5103 -0.3365 -0.1027 0.2880  1022 PHE B CB  
20076 C CG  . PHE C 1022 ? 2.1862 0.6974 1.4720 -0.3306 -0.0597 0.2973  1022 PHE B CG  
20077 C CD1 . PHE C 1022 ? 2.2287 0.6999 1.4421 -0.3064 -0.0323 0.2954  1022 PHE B CD1 
20078 C CD2 . PHE C 1022 ? 2.1596 0.6977 1.4701 -0.3491 -0.0478 0.3074  1022 PHE B CD2 
20079 C CE1 . PHE C 1022 ? 2.2630 0.7206 1.4287 -0.3015 0.0047  0.3048  1022 PHE B CE1 
20080 C CE2 . PHE C 1022 ? 2.1985 0.7213 1.4635 -0.3435 -0.0094 0.3157  1022 PHE B CE2 
20081 C CZ  . PHE C 1022 ? 2.2475 0.7295 1.4391 -0.3198 0.0163  0.3152  1022 PHE B CZ  
20082 N N   . HIS C 1023 ? 2.0700 0.7273 1.5774 -0.4277 -0.1053 0.3121  1023 HIS B N   
20083 C CA  . HIS C 1023 ? 2.0068 0.7601 1.5807 -0.4620 -0.0954 0.3174  1023 HIS B CA  
20084 C C   . HIS C 1023 ? 1.9339 0.7433 1.5408 -0.4805 -0.0757 0.3216  1023 HIS B C   
20085 O O   . HIS C 1023 ? 1.9256 0.7915 1.5432 -0.4959 -0.0407 0.3266  1023 HIS B O   
20086 C CB  . HIS C 1023 ? 1.9872 0.7743 1.6251 -0.4786 -0.1441 0.3145  1023 HIS B CB  
20087 C CG  . HIS C 1023 ? 1.9493 0.8379 1.6587 -0.5129 -0.1411 0.3192  1023 HIS B CG  
20088 N ND1 . HIS C 1023 ? 1.9265 0.8844 1.7050 -0.5374 -0.1618 0.3217  1023 HIS B ND1 
20089 C CD2 . HIS C 1023 ? 1.9406 0.8731 1.6629 -0.5251 -0.1215 0.3216  1023 HIS B CD2 
20090 C CE1 . HIS C 1023 ? 1.9055 0.9465 1.7337 -0.5621 -0.1562 0.3258  1023 HIS B CE1 
20091 N NE2 . HIS C 1023 ? 1.9213 0.9478 1.7168 -0.5555 -0.1310 0.3247  1023 HIS B NE2 
20092 N N   . TYR C 1024 ? 1.6381 0.4290 1.2601 -0.4773 -0.0994 0.3190  1024 TYR B N   
20093 C CA  . TYR C 1024 ? 1.6183 0.4398 1.2558 -0.4860 -0.0784 0.3238  1024 TYR B CA  
20094 C C   . TYR C 1024 ? 1.6694 0.4600 1.2363 -0.4696 -0.0275 0.3273  1024 TYR B C   
20095 O O   . TYR C 1024 ? 1.6481 0.4944 1.2236 -0.4841 0.0068  0.3330  1024 TYR B O   
20096 C CB  . TYR C 1024 ? 1.6534 0.4381 1.3047 -0.4779 -0.1103 0.3187  1024 TYR B CB  
20097 C CG  . TYR C 1024 ? 1.6945 0.5093 1.3624 -0.4857 -0.0864 0.3252  1024 TYR B CG  
20098 C CD1 . TYR C 1024 ? 1.7082 0.5781 1.4524 -0.5066 -0.1119 0.3284  1024 TYR B CD1 
20099 C CD2 . TYR C 1024 ? 1.7455 0.5380 1.3539 -0.4724 -0.0386 0.3296  1024 TYR B CD2 
20100 C CE1 . TYR C 1024 ? 1.7412 0.6408 1.5035 -0.5132 -0.0893 0.3360  1024 TYR B CE1 
20101 C CE2 . TYR C 1024 ? 1.7781 0.6007 1.4018 -0.4795 -0.0161 0.3364  1024 TYR B CE2 
20102 C CZ  . TYR C 1024 ? 1.8046 0.6799 1.5063 -0.4996 -0.0409 0.3398  1024 TYR B CZ  
20103 O OH  . TYR C 1024 ? 1.8656 0.7708 1.5843 -0.5055 -0.0182 0.3479  1024 TYR B OH  
20104 N N   . LEU C 1025 ? 2.1664 0.8692 1.6612 -0.4384 -0.0237 0.3233  1025 LEU B N   
20105 C CA  . LEU C 1025 ? 2.2275 0.9063 1.6553 -0.4238 0.0222  0.3280  1025 LEU B CA  
20106 C C   . LEU C 1025 ? 2.2179 0.9384 1.6326 -0.4338 0.0576  0.3323  1025 LEU B C   
20107 O O   . LEU C 1025 ? 2.1994 0.9468 1.5953 -0.4381 0.0954  0.3367  1025 LEU B O   
20108 C CB  . LEU C 1025 ? 2.2991 0.8771 1.6451 -0.3865 0.0177  0.3229  1025 LEU B CB  
20109 C CG  . LEU C 1025 ? 2.3307 0.8584 1.6717 -0.3709 -0.0045 0.3163  1025 LEU B CG  
20110 C CD1 . LEU C 1025 ? 2.4044 0.8783 1.6647 -0.3233 -0.0140 0.2947  1025 LEU B CD1 
20111 C CD2 . LEU C 1025 ? 2.3234 0.8814 1.6720 -0.3796 0.0255  0.3234  1025 LEU B CD2 
20112 N N   . GLU C 1026 ? 2.2130 0.9381 1.6382 -0.4369 0.0444  0.3301  1026 GLU B N   
20113 C CA  . GLU C 1026 ? 2.2928 1.0384 1.6948 -0.4402 0.0767  0.3320  1026 GLU B CA  
20114 C C   . GLU C 1026 ? 2.2927 1.1336 1.7612 -0.4726 0.0878  0.3328  1026 GLU B C   
20115 O O   . GLU C 1026 ? 2.3370 1.2136 1.7953 -0.4803 0.1238  0.3341  1026 GLU B O   
20116 C CB  . GLU C 1026 ? 2.3450 1.0487 1.7279 -0.4267 0.0581  0.3296  1026 GLU B CB  
20117 C CG  . GLU C 1026 ? 2.3934 1.1237 1.7691 -0.4334 0.0853  0.3308  1026 GLU B CG  
20118 C CD  . GLU C 1026 ? 2.4810 1.1734 1.7776 -0.4143 0.1257  0.3334  1026 GLU B CD  
20119 O OE1 . GLU C 1026 ? 2.5125 1.1762 1.7668 -0.4015 0.1381  0.3350  1026 GLU B OE1 
20120 O OE2 . GLU C 1026 ? 2.5042 1.1954 1.7806 -0.4119 0.1445  0.3337  1026 GLU B OE2 
20121 N N   . THR C 1027 ? 2.1410 1.0220 1.6758 -0.4905 0.0540  0.3311  1027 THR B N   
20122 C CA  . THR C 1027 ? 2.0943 1.0648 1.6921 -0.5196 0.0584  0.3313  1027 THR B CA  
20123 C C   . THR C 1027 ? 2.0914 1.1138 1.7135 -0.5334 0.0750  0.3347  1027 THR B C   
20124 O O   . THR C 1027 ? 2.1150 1.1812 1.7365 -0.5437 0.1059  0.3342  1027 THR B O   
20125 C CB  . THR C 1027 ? 2.0372 1.0425 1.7025 -0.5356 0.0132  0.3303  1027 THR B CB  
20126 O OG1 . THR C 1027 ? 2.0499 1.0695 1.7205 -0.5404 0.0168  0.3278  1027 THR B OG1 
20127 C CG2 . THR C 1027 ? 1.9846 1.0752 1.7225 -0.5623 0.0008  0.3336  1027 THR B CG2 
20128 N N   . GLY C 1028 ? 1.6121 0.6240 1.2525 -0.5316 0.0542  0.3374  1028 GLY B N   
20129 C CA  . GLY C 1028 ? 1.6420 0.6871 1.2950 -0.5385 0.0718  0.3422  1028 GLY B CA  
20130 C C   . GLY C 1028 ? 1.7115 0.7073 1.2894 -0.5180 0.1113  0.3430  1028 GLY B C   
20131 O O   . GLY C 1028 ? 1.7010 0.6922 1.2789 -0.5147 0.1161  0.3470  1028 GLY B O   
20132 N N   . ASN C 1029 ? 2.1309 1.0934 1.6470 -0.5047 0.1394  0.3399  1029 ASN B N   
20133 C CA  . ASN C 1029 ? 2.2577 1.1606 1.6941 -0.4807 0.1686  0.3410  1029 ASN B CA  
20134 C C   . ASN C 1029 ? 2.2365 1.1271 1.6730 -0.4751 0.1678  0.3455  1029 ASN B C   
20135 O O   . ASN C 1029 ? 2.1907 1.1367 1.6657 -0.4905 0.1774  0.3491  1029 ASN B O   
20136 C CB  . ASN C 1029 ? 2.3913 1.3105 1.7880 -0.4808 0.2095  0.3386  1029 ASN B CB  
20137 C CG  . ASN C 1029 ? 2.5130 1.4641 1.9072 -0.4860 0.2348  0.3410  1029 ASN B CG  
20138 O OD1 . ASN C 1029 ? 2.6028 1.5220 1.9326 -0.4705 0.2638  0.3406  1029 ASN B OD1 
20139 N ND2 . ASN C 1029 ? 2.5022 1.5175 1.9674 -0.5075 0.2218  0.3440  1029 ASN B ND2 
20140 N N   . HIS C 1030 ? 2.4768 1.2907 1.8695 -0.4513 0.1543  0.3452  1030 HIS B N   
20141 C CA  . HIS C 1030 ? 2.4766 1.2629 1.8638 -0.4417 0.1506  0.3482  1030 HIS B CA  
20142 C C   . HIS C 1030 ? 2.5140 1.2069 1.8115 -0.4077 0.1572  0.3469  1030 HIS B C   
20143 O O   . HIS C 1030 ? 2.5209 1.1688 1.8016 -0.3927 0.1488  0.3470  1030 HIS B O   
20144 C CB  . HIS C 1030 ? 2.4138 1.2080 1.8697 -0.4517 0.1066  0.3465  1030 HIS B CB  
20145 C CG  . HIS C 1030 ? 2.3295 1.2175 1.8744 -0.4837 0.0969  0.3502  1030 HIS B CG  
20146 N ND1 . HIS C 1030 ? 2.3007 1.2461 1.8679 -0.4969 0.1224  0.3568  1030 HIS B ND1 
20147 C CD2 . HIS C 1030 ? 2.2751 1.2102 1.8905 -0.5039 0.0624  0.3489  1030 HIS B CD2 
20148 C CE1 . HIS C 1030 ? 2.2454 1.2681 1.8924 -0.5230 0.1033  0.3597  1030 HIS B CE1 
20149 N NE2 . HIS C 1030 ? 2.2223 1.2419 1.8997 -0.5281 0.0671  0.3553  1030 HIS B NE2 
20150 N N   . TRP C 1031 ? 2.8464 1.5107 2.0864 -0.3948 0.1716  0.3454  1031 TRP B N   
20151 C CA  . TRP C 1031 ? 2.8608 1.4444 2.0112 -0.3626 0.1794  0.3455  1031 TRP B CA  
20152 C C   . TRP C 1031 ? 2.8986 1.4696 2.0111 -0.3523 0.2039  0.3501  1031 TRP B C   
20153 O O   . TRP C 1031 ? 2.9891 1.4907 2.0423 -0.3257 0.1994  0.3499  1031 TRP B O   
20154 C CB  . TRP C 1031 ? 2.8531 1.4278 1.9526 -0.3553 0.1996  0.3455  1031 TRP B CB  
20155 C CG  . TRP C 1031 ? 2.8008 1.3677 1.9250 -0.3574 0.1728  0.3419  1031 TRP B CG  
20156 C CD1 . TRP C 1031 ? 2.7781 1.3834 1.9225 -0.3714 0.1819  0.3410  1031 TRP B CD1 
20157 C CD2 . TRP C 1031 ? 2.8017 1.3184 1.9345 -0.3444 0.1310  0.3374  1031 TRP B CD2 
20158 N NE1 . TRP C 1031 ? 2.7691 1.3529 1.9341 -0.3681 0.1496  0.3382  1031 TRP B NE1 
20159 C CE2 . TRP C 1031 ? 2.7956 1.3254 1.9535 -0.3514 0.1169  0.3355  1031 TRP B CE2 
20160 C CE3 . TRP C 1031 ? 2.8349 1.2944 1.9560 -0.3259 0.1032  0.3328  1031 TRP B CE3 
20161 C CZ2 . TRP C 1031 ? 2.8287 1.3194 2.0002 -0.3409 0.0752  0.3301  1031 TRP B CZ2 
20162 C CZ3 . TRP C 1031 ? 2.8664 1.3122 2.0031 -0.3096 0.0591  0.3144  1031 TRP B CZ3 
20163 C CH2 . TRP C 1031 ? 2.8611 1.3208 2.0221 -0.3179 0.0454  0.3151  1031 TRP B CH2 
20164 N N   . ASN C 1032 ? 3.0103 1.6478 2.1576 -0.3722 0.2279  0.3538  1032 ASN B N   
20165 C CA  . ASN C 1032 ? 3.0574 1.6870 2.1670 -0.3622 0.2539  0.3587  1032 ASN B CA  
20166 C C   . ASN C 1032 ? 3.0343 1.6337 2.1630 -0.3548 0.2357  0.3608  1032 ASN B C   
20167 O O   . ASN C 1032 ? 3.0488 1.6447 2.1547 -0.3476 0.2563  0.3660  1032 ASN B O   
20168 C CB  . ASN C 1032 ? 3.0602 1.7681 2.2054 -0.3843 0.2814  0.3608  1032 ASN B CB  
20169 C CG  . ASN C 1032 ? 2.9965 1.7720 2.2415 -0.4124 0.2631  0.3623  1032 ASN B CG  
20170 O OD1 . ASN C 1032 ? 2.9402 1.7351 2.2344 -0.4259 0.2372  0.3591  1032 ASN B OD1 
20171 N ND2 . ASN C 1032 ? 2.9950 1.8089 2.2712 -0.4213 0.2748  0.3680  1032 ASN B ND2 
20172 N N   . ILE C 1033 ? 2.3504 0.9276 1.5223 -0.3561 0.1963  0.3555  1033 ILE B N   
20173 C CA  . ILE C 1033 ? 2.3541 0.8867 1.5405 -0.3446 0.1733  0.3528  1033 ILE B CA  
20174 C C   . ILE C 1033 ? 2.4507 0.8986 1.5459 -0.3093 0.1830  0.3518  1033 ILE B C   
20175 O O   . ILE C 1033 ? 2.4824 0.9183 1.5803 -0.2946 0.1790  0.3435  1033 ILE B O   
20176 C CB  . ILE C 1033 ? 2.3129 0.8096 1.5368 -0.3413 0.1239  0.3411  1033 ILE B CB  
20177 C CG1 . ILE C 1033 ? 2.2457 0.8077 1.5414 -0.3695 0.1049  0.3402  1033 ILE B CG1 
20178 C CG2 . ILE C 1033 ? 2.3163 0.7966 1.5802 -0.3358 0.1004  0.3331  1033 ILE B CG2 
20179 C CD1 . ILE C 1033 ? 2.2296 0.7661 1.5727 -0.3690 0.0540  0.3289  1033 ILE B CD1 
20180 N N   . PHE C 1034 ? 3.0101 1.4291 2.0322 -0.2888 0.1900  0.3460  1034 PHE B N   
20181 C CA  . PHE C 1034 ? 3.0963 1.4733 2.0356 -0.2457 0.1873  0.3238  1034 PHE B CA  
20182 C C   . PHE C 1034 ? 3.2177 1.5891 2.0901 -0.2395 0.2293  0.3389  1034 PHE B C   
20183 O O   . PHE C 1034 ? 3.2107 1.6005 2.0675 -0.2615 0.2626  0.3647  1034 PHE B O   
20184 C CB  . PHE C 1034 ? 3.0475 1.4014 1.9439 -0.2279 0.1712  0.3104  1034 PHE B CB  
20185 C CG  . PHE C 1034 ? 2.9528 1.3124 1.9066 -0.2329 0.1302  0.2973  1034 PHE B CG  
20186 C CD1 . PHE C 1034 ? 2.9315 1.2831 1.9212 -0.2207 0.0933  0.2755  1034 PHE B CD1 
20187 C CD2 . PHE C 1034 ? 2.8912 1.2642 1.8620 -0.2496 0.1282  0.3069  1034 PHE B CD2 
20188 C CE1 . PHE C 1034 ? 2.8793 1.2371 1.9186 -0.2261 0.0538  0.2652  1034 PHE B CE1 
20189 C CE2 . PHE C 1034 ? 2.8272 1.2083 1.8498 -0.2543 0.0898  0.2960  1034 PHE B CE2 
20190 C CZ  . PHE C 1034 ? 2.8227 1.1967 1.8783 -0.2430 0.0520  0.2760  1034 PHE B CZ  
20191 N N   . HIS C 1035 ? 3.0071 1.3554 1.8380 -0.2090 0.2268  0.3207  1035 HIS B N   
20192 C CA  . HIS C 1035 ? 3.1815 1.5237 1.9421 -0.1988 0.2628  0.3321  1035 HIS B CA  
20193 C C   . HIS C 1035 ? 3.2807 1.5951 1.9554 -0.1755 0.2642  0.3226  1035 HIS B C   
20194 O O   . HIS C 1035 ? 3.3448 1.6556 1.9526 -0.1712 0.2940  0.3362  1035 HIS B O   
20195 C CB  . HIS C 1035 ? 3.3271 1.6588 2.0825 -0.1755 0.2581  0.3144  1035 HIS B CB  
20196 C CG  . HIS C 1035 ? 3.3828 1.7333 2.2295 -0.1908 0.2411  0.3132  1035 HIS B CG  
20197 N ND1 . HIS C 1035 ? 3.4076 1.7827 2.2895 -0.2084 0.2649  0.3343  1035 HIS B ND1 
20198 C CD2 . HIS C 1035 ? 3.3876 1.7371 2.2984 -0.1924 0.2014  0.2952  1035 HIS B CD2 
20199 C CE1 . HIS C 1035 ? 3.3834 1.7717 2.3499 -0.2202 0.2400  0.3286  1035 HIS B CE1 
20200 N NE2 . HIS C 1035 ? 3.3753 1.7483 2.3594 -0.2108 0.2007  0.3047  1035 HIS B NE2 
20201 N N   . SER C 1036 ? 3.5789 1.8750 2.2569 -0.1618 0.2304  0.3008  1036 SER B N   
20202 C CA  . SER C 1036 ? 3.6292 1.8983 2.2338 -0.1394 0.2249  0.2898  1036 SER B CA  
20203 C C   . SER C 1036 ? 3.5883 1.8668 2.1791 -0.1596 0.2455  0.3144  1036 SER B C   
20204 O O   . SER C 1036 ? 3.5324 1.8376 2.1553 -0.1904 0.2717  0.3416  1036 SER B O   
20205 C CB  . SER C 1036 ? 3.6588 1.9070 2.2789 -0.1206 0.1806  0.2605  1036 SER B CB  
20206 O OG  . SER C 1036 ? 3.6101 1.8727 2.2876 -0.1411 0.1657  0.2683  1036 SER B OG  
20207 N N   . ASP C 1037 ? 3.9708 2.2273 2.5144 -0.1434 0.2343  0.3054  1037 ASP B N   
20208 C CA  . ASP C 1037 ? 3.9078 2.1725 2.4603 -0.1625 0.2438  0.3233  1037 ASP B CA  
20209 C C   . ASP C 1037 ? 3.7558 2.0325 2.3878 -0.1742 0.2144  0.3155  1037 ASP B C   
20210 O O   . ASP C 1037 ? 3.7620 2.0237 2.4067 -0.1552 0.1784  0.2911  1037 ASP B O   
20211 C CB  . ASP C 1037 ? 3.9908 2.2300 2.4744 -0.1434 0.2405  0.3187  1037 ASP B CB  
20212 C CG  . ASP C 1037 ? 3.9486 2.1960 2.4471 -0.1633 0.2515  0.3371  1037 ASP B CG  
20213 O OD1 . ASP C 1037 ? 3.8392 2.1118 2.4073 -0.1901 0.2543  0.3479  1037 ASP B OD1 
20214 O OD2 . ASP C 1037 ? 4.0039 2.2335 2.4454 -0.1529 0.2572  0.3406  1037 ASP B OD2 
20215 N N   . PRO C 1038 ? 3.1331 1.4387 1.8181 -0.2075 0.2297  0.3369  1038 PRO B N   
20216 C CA  . PRO C 1038 ? 3.0370 1.3624 1.8037 -0.2241 0.2031  0.3322  1038 PRO B CA  
20217 C C   . PRO C 1038 ? 3.0143 1.3320 1.7802 -0.2202 0.1875  0.3281  1038 PRO B C   
20218 O O   . PRO C 1038 ? 2.9977 1.3158 1.8043 -0.2151 0.1517  0.3128  1038 PRO B O   
20219 C CB  . PRO C 1038 ? 2.9842 1.3586 1.8078 -0.2631 0.2301  0.3534  1038 PRO B CB  
20220 C CG  . PRO C 1038 ? 3.0425 1.4312 1.8193 -0.2591 0.2654  0.3578  1038 PRO B CG  
20221 C CD  . PRO C 1038 ? 3.1189 1.4560 1.8016 -0.2325 0.2713  0.3599  1038 PRO B CD  
20222 N N   . LEU C 1039 ? 3.4633 1.7734 2.1819 -0.2222 0.2137  0.3422  1039 LEU B N   
20223 C CA  . LEU C 1039 ? 3.4375 1.7445 2.1637 -0.2227 0.2040  0.3421  1039 LEU B CA  
20224 C C   . LEU C 1039 ? 3.4222 1.7016 2.1290 -0.1904 0.1648  0.3176  1039 LEU B C   
20225 O O   . LEU C 1039 ? 3.3764 1.6597 2.1188 -0.1908 0.1412  0.3118  1039 LEU B O   
20226 C CB  . LEU C 1039 ? 3.4774 1.7816 2.1517 -0.2270 0.2387  0.3575  1039 LEU B CB  
20227 C CG  . LEU C 1039 ? 3.4839 1.8043 2.1837 -0.2355 0.2385  0.3571  1039 LEU B CG  
20228 C CD1 . LEU C 1039 ? 3.4035 1.7602 2.1935 -0.2572 0.2197  0.3532  1039 LEU B CD1 
20229 C CD2 . LEU C 1039 ? 3.5131 1.8727 2.1970 -0.2468 0.2759  0.3558  1039 LEU B CD2 
20230 N N   . ILE C 1040 ? 3.1768 1.4301 1.8272 -0.1637 0.1583  0.3039  1040 ILE B N   
20231 C CA  . ILE C 1040 ? 3.1928 1.4194 1.8200 -0.1349 0.1221  0.2809  1040 ILE B CA  
20232 C C   . ILE C 1040 ? 3.1767 1.4116 1.8631 -0.1355 0.0885  0.2649  1040 ILE B C   
20233 O O   . ILE C 1040 ? 3.1879 1.4121 1.8865 -0.1232 0.0539  0.2507  1040 ILE B O   
20234 C CB  . ILE C 1040 ? 3.2338 1.4329 1.7808 -0.1091 0.1270  0.2704  1040 ILE B CB  
20235 C CG1 . ILE C 1040 ? 3.3153 1.4870 1.8140 -0.0860 0.1066  0.2598  1040 ILE B CG1 
20236 C CG2 . ILE C 1040 ? 3.2033 1.3989 1.7584 -0.0987 0.1129  0.2522  1040 ILE B CG2 
20237 C CD1 . ILE C 1040 ? 3.5359 1.7088 2.0802 -0.0867 0.0763  0.2552  1040 ILE B CD1 
20238 N N   . GLU C 1041 ? 2.9760 1.2304 1.6988 -0.1507 0.0985  0.2688  1041 GLU B N   
20239 C CA  . GLU C 1041 ? 2.9799 1.2441 1.7630 -0.1543 0.0672  0.2558  1041 GLU B CA  
20240 C C   . GLU C 1041 ? 2.9443 1.2309 1.7894 -0.1729 0.0483  0.2617  1041 GLU B C   
20241 O O   . GLU C 1041 ? 2.9006 1.1875 1.7825 -0.1690 0.0104  0.2481  1041 GLU B O   
20242 C CB  . GLU C 1041 ? 2.9945 1.2807 1.8130 -0.1725 0.0853  0.2645  1041 GLU B CB  
20243 C CG  . GLU C 1041 ? 3.0547 1.3334 1.8980 -0.1609 0.0569  0.2441  1041 GLU B CG  
20244 C CD  . GLU C 1041 ? 3.2073 1.4560 1.9832 -0.1319 0.0639  0.2284  1041 GLU B CD  
20245 O OE1 . GLU C 1041 ? 3.2498 1.4968 1.9760 -0.1305 0.0989  0.2405  1041 GLU B OE1 
20246 O OE2 . GLU C 1041 ? 3.2882 1.5163 2.0597 -0.1116 0.0345  0.2042  1041 GLU B OE2 
20247 N N   . LYS C 1042 ? 2.8723 1.1774 1.7260 -0.1933 0.0751  0.2819  1042 LYS B N   
20248 C CA  . LYS C 1042 ? 2.8899 1.2205 1.8018 -0.2132 0.0626  0.2887  1042 LYS B CA  
20249 C C   . LYS C 1042 ? 2.9880 1.2968 1.8812 -0.1900 0.0314  0.2755  1042 LYS B C   
20250 O O   . LYS C 1042 ? 2.9828 1.3030 1.9231 -0.1930 -0.0029 0.2682  1042 LYS B O   
20251 C CB  . LYS C 1042 ? 2.8869 1.2371 1.8016 -0.2379 0.1018  0.3116  1042 LYS B CB  
20252 C CG  . LYS C 1042 ? 2.8995 1.2726 1.8639 -0.2540 0.0911  0.3163  1042 LYS B CG  
20253 C CD  . LYS C 1042 ? 2.9247 1.3152 1.8900 -0.2788 0.1318  0.3373  1042 LYS B CD  
20254 C CE  . LYS C 1042 ? 2.8514 1.3114 1.8967 -0.3168 0.1401  0.3407  1042 LYS B CE  
20255 N NZ  . LYS C 1042 ? 2.8467 1.3565 1.9030 -0.3339 0.1725  0.3420  1042 LYS B NZ  
20256 N N   . GLN C 1043 ? 3.1226 1.4013 1.9462 -0.1682 0.0432  0.2744  1043 GLN B N   
20257 C CA  . GLN C 1043 ? 3.1908 1.4469 1.9897 -0.1459 0.0170  0.2648  1043 GLN B CA  
20258 C C   . GLN C 1043 ? 3.1326 1.3791 1.9480 -0.1324 -0.0265 0.2456  1043 GLN B C   
20259 O O   . GLN C 1043 ? 3.1190 1.3714 1.9664 -0.1321 -0.0561 0.2427  1043 GLN B O   
20260 C CB  . GLN C 1043 ? 3.3317 1.5548 2.0476 -0.1233 0.0327  0.2637  1043 GLN B CB  
20261 C CG  . GLN C 1043 ? 3.4104 1.6390 2.1059 -0.1350 0.0708  0.2832  1043 GLN B CG  
20262 C CD  . GLN C 1043 ? 3.4128 1.6670 2.1673 -0.1554 0.0715  0.2940  1043 GLN B CD  
20263 O OE1 . GLN C 1043 ? 3.4147 1.6702 2.1981 -0.1491 0.0410  0.2870  1043 GLN B OE1 
20264 N NE2 . GLN C 1043 ? 3.3889 1.6656 2.1623 -0.1813 0.1063  0.3114  1043 GLN B NE2 
20265 N N   . LYS C 1044 ? 2.8944 1.1262 1.6863 -0.1214 -0.0294 0.2331  1044 LYS B N   
20266 C CA  . LYS C 1044 ? 2.8795 1.0954 1.6752 -0.1062 -0.0686 0.2127  1044 LYS B CA  
20267 C C   . LYS C 1044 ? 2.8089 1.0515 1.6814 -0.1241 -0.0984 0.2130  1044 LYS B C   
20268 O O   . LYS C 1044 ? 2.8301 1.0627 1.7104 -0.1142 -0.1365 0.2021  1044 LYS B O   
20269 C CB  . LYS C 1044 ? 2.8967 1.0978 1.6645 -0.0956 -0.0613 0.1996  1044 LYS B CB  
20270 C CG  . LYS C 1044 ? 3.4041 1.5749 2.0876 -0.0724 -0.0446 0.1928  1044 LYS B CG  
20271 C CD  . LYS C 1044 ? 3.3904 1.5507 2.0489 -0.0624 -0.0353 0.1795  1044 LYS B CD  
20272 C CE  . LYS C 1044 ? 3.4018 1.5426 2.0638 -0.0471 -0.0724 0.1546  1044 LYS B CE  
20273 N NZ  . LYS C 1044 ? 3.4099 1.5422 2.0539 -0.0377 -0.0617 0.1410  1044 LYS B NZ  
20274 N N   . LEU C 1045 ? 3.0784 1.3567 2.0068 -0.1523 -0.0817 0.2271  1045 LEU B N   
20275 C CA  . LEU C 1045 ? 2.9725 1.2820 1.9765 -0.1730 -0.1102 0.2286  1045 LEU B CA  
20276 C C   . LEU C 1045 ? 2.9450 1.2679 1.9671 -0.1782 -0.1202 0.2367  1045 LEU B C   
20277 O O   . LEU C 1045 ? 2.9146 1.2495 1.9751 -0.1817 -0.1569 0.2327  1045 LEU B O   
20278 C CB  . LEU C 1045 ? 2.8745 1.2209 1.9333 -0.2045 -0.0888 0.2418  1045 LEU B CB  
20279 C CG  . LEU C 1045 ? 2.8465 1.1788 1.8780 -0.1979 -0.0674 0.2380  1045 LEU B CG  
20280 C CD1 . LEU C 1045 ? 2.7992 1.1688 1.9003 -0.2292 -0.0625 0.2484  1045 LEU B CD1 
20281 C CD2 . LEU C 1045 ? 2.8524 1.1476 1.8456 -0.1676 -0.0940 0.2146  1045 LEU B CD2 
20282 N N   . LYS C 1046 ? 2.7608 1.0810 1.7535 -0.1780 -0.0877 0.2484  1046 LYS B N   
20283 C CA  . LYS C 1046 ? 2.8029 1.1328 1.8090 -0.1803 -0.0929 0.2559  1046 LYS B CA  
20284 C C   . LYS C 1046 ? 2.8898 1.1934 1.8707 -0.1547 -0.1314 0.2439  1046 LYS B C   
20285 O O   . LYS C 1046 ? 2.8900 1.2096 1.9114 -0.1594 -0.1640 0.2430  1046 LYS B O   
20286 C CB  . LYS C 1046 ? 2.8425 1.1634 1.8078 -0.1786 -0.0519 0.2682  1046 LYS B CB  
20287 C CG  . LYS C 1046 ? 2.8229 1.1743 1.8172 -0.2092 -0.0123 0.2844  1046 LYS B CG  
20288 C CD  . LYS C 1046 ? 2.8968 1.2416 1.8616 -0.2086 0.0188  0.2966  1046 LYS B CD  
20289 C CE  . LYS C 1046 ? 2.9134 1.2745 1.8775 -0.2335 0.0654  0.3135  1046 LYS B CE  
20290 N NZ  . LYS C 1046 ? 2.9632 1.3117 1.8918 -0.2302 0.0934  0.3240  1046 LYS B NZ  
20291 N N   . LYS C 1047 ? 2.6434 0.9080 1.5557 -0.1291 -0.1279 0.2355  1047 LYS B N   
20292 C CA  . LYS C 1047 ? 2.6982 0.9357 1.5812 -0.1064 -0.1635 0.2242  1047 LYS B CA  
20293 C C   . LYS C 1047 ? 2.5880 0.8378 1.5171 -0.1132 -0.2031 0.2153  1047 LYS B C   
20294 O O   . LYS C 1047 ? 2.5452 0.8092 1.5076 -0.1174 -0.2316 0.2187  1047 LYS B O   
20295 C CB  . LYS C 1047 ? 2.8576 1.0560 1.6664 -0.0829 -0.1570 0.2123  1047 LYS B CB  
20296 C CG  . LYS C 1047 ? 3.0202 1.1885 1.7867 -0.0607 -0.1863 0.2043  1047 LYS B CG  
20297 C CD  . LYS C 1047 ? 3.1924 1.3287 1.8825 -0.0419 -0.1696 0.1981  1047 LYS B CD  
20298 C CE  . LYS C 1047 ? 3.3267 1.4387 1.9803 -0.0253 -0.1959 0.1948  1047 LYS B CE  
20299 N NZ  . LYS C 1047 ? 3.3628 1.4682 2.0327 -0.0222 -0.2368 0.1829  1047 LYS B NZ  
20300 N N   . LYS C 1048 ? 2.5185 0.7642 1.4506 -0.1147 -0.2050 0.2046  1048 LYS B N   
20301 C CA  . LYS C 1048 ? 2.4381 0.6860 1.4021 -0.1167 -0.2458 0.1935  1048 LYS B CA  
20302 C C   . LYS C 1048 ? 2.3393 0.6226 1.3667 -0.1358 -0.2702 0.2032  1048 LYS B C   
20303 O O   . LYS C 1048 ? 2.3203 0.6035 1.3663 -0.1347 -0.3116 0.1969  1048 LYS B O   
20304 C CB  . LYS C 1048 ? 2.3808 0.6364 1.3687 -0.1267 -0.2386 0.1871  1048 LYS B CB  
20305 C CG  . LYS C 1048 ? 2.4236 0.6430 1.3532 -0.1050 -0.2288 0.1719  1048 LYS B CG  
20306 C CD  . LYS C 1048 ? 2.4227 0.6401 1.3790 -0.1070 -0.2504 0.1585  1048 LYS B CD  
20307 C CE  . LYS C 1048 ? 2.4399 0.6463 1.3695 -0.1009 -0.2182 0.1529  1048 LYS B CE  
20308 N NZ  . LYS C 1048 ? 2.4388 0.6417 1.3978 -0.1017 -0.2397 0.1389  1048 LYS B NZ  
20309 N N   . LEU C 1049 ? 2.7244 1.0392 1.7842 -0.1548 -0.2438 0.2187  1049 LEU B N   
20310 C CA  . LEU C 1049 ? 2.6647 1.0202 1.7876 -0.1762 -0.2607 0.2291  1049 LEU B CA  
20311 C C   . LEU C 1049 ? 2.7290 1.0753 1.8331 -0.1615 -0.2765 0.2331  1049 LEU B C   
20312 O O   . LEU C 1049 ? 2.7623 1.1099 1.8791 -0.1574 -0.3175 0.2302  1049 LEU B O   
20313 C CB  . LEU C 1049 ? 2.5510 0.9459 1.7181 -0.2054 -0.2244 0.2431  1049 LEU B CB  
20314 C CG  . LEU C 1049 ? 2.4283 0.8745 1.6781 -0.2400 -0.2399 0.2489  1049 LEU B CG  
20315 C CD1 . LEU C 1049 ? 2.3612 0.8064 1.6304 -0.2454 -0.2592 0.2400  1049 LEU B CD1 
20316 C CD2 . LEU C 1049 ? 2.3817 0.8656 1.6682 -0.2699 -0.2004 0.2640  1049 LEU B CD2 
20317 N N   . LYS C 1050 ? 2.8922 1.2276 1.9643 -0.1529 -0.2461 0.2408  1050 LYS B N   
20318 C CA  . LYS C 1050 ? 2.9339 1.2605 1.9922 -0.1387 -0.2633 0.2454  1050 LYS B CA  
20319 C C   . LYS C 1050 ? 3.0299 1.3271 2.0565 -0.1189 -0.3045 0.2353  1050 LYS B C   
20320 O O   . LYS C 1050 ? 3.0140 1.3232 2.0645 -0.1200 -0.3388 0.2387  1050 LYS B O   
20321 C CB  . LYS C 1050 ? 2.9530 1.2593 1.9668 -0.1256 -0.2293 0.2525  1050 LYS B CB  
20322 C CG  . LYS C 1050 ? 2.9684 1.2658 1.9718 -0.1109 -0.2480 0.2588  1050 LYS B CG  
20323 C CD  . LYS C 1050 ? 2.9895 1.2809 1.9740 -0.1061 -0.2136 0.2692  1050 LYS B CD  
20324 C CE  . LYS C 1050 ? 3.0286 1.3274 2.0311 -0.0994 -0.2319 0.2783  1050 LYS B CE  
20325 N NZ  . LYS C 1050 ? 3.0617 1.3658 2.0675 -0.1014 -0.1973 0.2890  1050 LYS B NZ  
20326 N N   . GLU C 1051 ? 3.5738 1.8341 2.5467 -0.1023 -0.3020 0.2232  1051 GLU B N   
20327 C CA  . GLU C 1051 ? 3.7269 1.9572 2.6646 -0.0847 -0.3391 0.2138  1051 GLU B CA  
20328 C C   . GLU C 1051 ? 3.6946 1.9407 2.6744 -0.0951 -0.3819 0.2093  1051 GLU B C   
20329 O O   . GLU C 1051 ? 3.7251 1.9639 2.6986 -0.0885 -0.4177 0.2109  1051 GLU B O   
20330 C CB  . GLU C 1051 ? 3.8971 2.0879 2.7715 -0.0673 -0.3279 0.1993  1051 GLU B CB  
20331 C CG  . GLU C 1051 ? 3.9942 2.1833 2.8809 -0.0724 -0.3344 0.1848  1051 GLU B CG  
20332 C CD  . GLU C 1051 ? 4.1315 2.2861 2.9572 -0.0557 -0.3165 0.1703  1051 GLU B CD  
20333 O OE1 . GLU C 1051 ? 4.1872 2.3261 2.9658 -0.0445 -0.2923 0.1740  1051 GLU B OE1 
20334 O OE2 . GLU C 1051 ? 4.1744 2.3186 3.0000 -0.0539 -0.3272 0.1552  1051 GLU B OE2 
20335 N N   . GLY C 1052 ? 2.6210 0.8889 1.6428 -0.1124 -0.3793 0.2050  1052 GLY B N   
20336 C CA  . GLY C 1052 ? 2.6149 0.9024 1.6825 -0.1255 -0.4202 0.2023  1052 GLY B CA  
20337 C C   . GLY C 1052 ? 2.5666 0.8893 1.6766 -0.1376 -0.4384 0.2172  1052 GLY B C   
20338 O O   . GLY C 1052 ? 2.5726 0.9047 1.7019 -0.1413 -0.4808 0.2184  1052 GLY B O   
20339 N N   . MET C 1053 ? 3.2743 1.6161 2.3966 -0.1434 -0.4056 0.2286  1053 MET B N   
20340 C CA  . MET C 1053 ? 3.2517 1.6314 2.4189 -0.1559 -0.4157 0.2422  1053 MET B CA  
20341 C C   . MET C 1053 ? 3.2880 1.6493 2.4258 -0.1374 -0.4443 0.2470  1053 MET B C   
20342 O O   . MET C 1053 ? 3.2707 1.6588 2.4428 -0.1456 -0.4767 0.2546  1053 MET B O   
20343 C CB  . MET C 1053 ? 3.2740 1.6714 2.4532 -0.1639 -0.3697 0.2516  1053 MET B CB  
20344 C CG  . MET C 1053 ? 3.2311 1.6776 2.4712 -0.1836 -0.3759 0.2631  1053 MET B CG  
20345 S SD  . MET C 1053 ? 4.5777 3.0608 3.8740 -0.2031 -0.4317 0.2618  1053 MET B SD  
20346 C CE  . MET C 1053 ? 2.3415 0.8912 1.7206 -0.2439 -0.4132 0.2687  1053 MET B CE  
20347 N N   . LEU C 1054 ? 3.2227 1.5405 2.2968 -0.1139 -0.4326 0.2440  1054 LEU B N   
20348 C CA  . LEU C 1054 ? 3.2754 1.5758 2.3211 -0.0981 -0.4583 0.2511  1054 LEU B CA  
20349 C C   . LEU C 1054 ? 3.2554 1.5480 2.2984 -0.0984 -0.5057 0.2450  1054 LEU B C   
20350 O O   . LEU C 1054 ? 3.2520 1.5519 2.3011 -0.0972 -0.5396 0.2545  1054 LEU B O   
20351 C CB  . LEU C 1054 ? 3.3960 1.6529 2.3743 -0.0758 -0.4372 0.2496  1054 LEU B CB  
20352 C CG  . LEU C 1054 ? 3.4435 1.7010 2.4140 -0.0741 -0.3891 0.2545  1054 LEU B CG  
20353 C CD1 . LEU C 1054 ? 3.5259 1.7410 2.4275 -0.0531 -0.3755 0.2528  1054 LEU B CD1 
20354 C CD2 . LEU C 1054 ? 3.4344 1.7265 2.4514 -0.0831 -0.3789 0.2697  1054 LEU B CD2 
20355 N N   . SER C 1055 ? 3.0363 1.3159 2.0730 -0.1012 -0.5080 0.2299  1055 SER B N   
20356 C CA  . SER C 1055 ? 3.0468 1.3060 2.0660 -0.0975 -0.5495 0.2207  1055 SER B CA  
20357 C C   . SER C 1055 ? 2.9515 1.2389 2.0077 -0.1089 -0.5950 0.2318  1055 SER B C   
20358 O O   . SER C 1055 ? 3.0067 1.2746 2.0403 -0.1043 -0.6336 0.2288  1055 SER B O   
20359 C CB  . SER C 1055 ? 3.1027 1.3565 2.1323 -0.1042 -0.5466 0.2042  1055 SER B CB  
20360 O OG  . SER C 1055 ? 3.1737 1.4025 2.1818 -0.0989 -0.5862 0.1938  1055 SER B OG  
20361 N N   . ILE C 1056 ? 3.0068 1.3406 2.1178 -0.1245 -0.5902 0.2447  1056 ILE B N   
20362 C CA  . ILE C 1056 ? 2.9731 1.3438 2.1274 -0.1391 -0.6317 0.2554  1056 ILE B CA  
20363 C C   . ILE C 1056 ? 2.9626 1.3408 2.1096 -0.1306 -0.6407 0.2726  1056 ILE B C   
20364 O O   . ILE C 1056 ? 2.9640 1.3542 2.1179 -0.1337 -0.6824 0.2821  1056 ILE B O   
20365 C CB  . ILE C 1056 ? 2.7560 1.1812 1.9840 -0.1666 -0.6243 0.2573  1056 ILE B CB  
20366 C CG1 . ILE C 1056 ? 2.6764 1.1508 1.9511 -0.1797 -0.6405 0.2736  1056 ILE B CG1 
20367 C CG2 . ILE C 1056 ? 2.7027 1.1272 1.9340 -0.1689 -0.5698 0.2523  1056 ILE B CG2 
20368 C CD1 . ILE C 1056 ? 2.6133 1.1296 1.9372 -0.1964 -0.6010 0.2783  1056 ILE B CD1 
20369 N N   . MET C 1057 ? 3.3146 1.6847 2.4463 -0.1198 -0.6021 0.2776  1057 MET B N   
20370 C CA  . MET C 1057 ? 3.4057 1.7864 2.5391 -0.1123 -0.6053 0.2948  1057 MET B CA  
20371 C C   . MET C 1057 ? 3.4849 1.8599 2.6020 -0.1081 -0.6545 0.3044  1057 MET B C   
20372 O O   . MET C 1057 ? 3.4658 1.8739 2.6138 -0.1139 -0.6758 0.3195  1057 MET B O   
20373 C CB  . MET C 1057 ? 3.5236 1.8680 2.6091 -0.0920 -0.5703 0.2965  1057 MET B CB  
20374 C CG  . MET C 1057 ? 3.5479 1.9172 2.6620 -0.0914 -0.5464 0.3101  1057 MET B CG  
20375 S SD  . MET C 1057 ? 3.8939 2.3167 3.0803 -0.1168 -0.5179 0.3067  1057 MET B SD  
20376 C CE  . MET C 1057 ? 4.2898 2.6826 3.4430 -0.1102 -0.4612 0.2970  1057 MET B CE  
20377 N N   . SER C 1058 ? 3.2757 1.6087 2.3423 -0.0986 -0.6721 0.2955  1058 SER B N   
20378 C CA  . SER C 1058 ? 3.2833 1.6013 2.3210 -0.0941 -0.7170 0.3046  1058 SER B CA  
20379 C C   . SER C 1058 ? 3.2119 1.5741 2.2971 -0.1116 -0.7591 0.3150  1058 SER B C   
20380 O O   . SER C 1058 ? 3.2269 1.5927 2.3009 -0.1093 -0.7921 0.3315  1058 SER B O   
20381 C CB  . SER C 1058 ? 3.3041 1.5745 2.2888 -0.0869 -0.7285 0.2882  1058 SER B CB  
20382 O OG  . SER C 1058 ? 3.3084 1.5426 2.2498 -0.0721 -0.6896 0.2780  1058 SER B OG  
20383 N N   . TYR C 1059 ? 3.0089 1.4069 2.1472 -0.1305 -0.7585 0.3067  1059 TYR B N   
20384 C CA  . TYR C 1059 ? 2.9744 1.4180 2.1598 -0.1504 -0.8012 0.3150  1059 TYR B CA  
20385 C C   . TYR C 1059 ? 3.0024 1.4999 2.2410 -0.1602 -0.7918 0.3291  1059 TYR B C   
20386 O O   . TYR C 1059 ? 2.9991 1.5419 2.2783 -0.1765 -0.8260 0.3391  1059 TYR B O   
20387 C CB  . TYR C 1059 ? 2.8701 1.3288 2.0902 -0.1691 -0.8097 0.2999  1059 TYR B CB  
20388 C CG  . TYR C 1059 ? 2.8823 1.2888 2.0543 -0.1593 -0.8185 0.2836  1059 TYR B CG  
20389 C CD1 . TYR C 1059 ? 2.9327 1.2940 2.0598 -0.1416 -0.7792 0.2706  1059 TYR B CD1 
20390 C CD2 . TYR C 1059 ? 2.9213 1.3243 2.0923 -0.1680 -0.8665 0.2808  1059 TYR B CD2 
20391 C CE1 . TYR C 1059 ? 3.0246 1.3392 2.1077 -0.1323 -0.7862 0.2538  1059 TYR B CE1 
20392 C CE2 . TYR C 1059 ? 3.0279 1.3816 2.1555 -0.1586 -0.8740 0.2641  1059 TYR B CE2 
20393 C CZ  . TYR C 1059 ? 3.0761 1.3864 2.1606 -0.1406 -0.8332 0.2500  1059 TYR B CZ  
20394 O OH  . TYR C 1059 ? 3.1334 1.3974 2.1766 -0.1317 -0.8411 0.2319  1059 TYR B OH  
20395 N N   . ARG C 1060 ? 2.9500 1.4429 2.1877 -0.1506 -0.7452 0.3295  1060 ARG B N   
20396 C CA  . ARG C 1060 ? 2.9615 1.5016 2.2482 -0.1582 -0.7302 0.3407  1060 ARG B CA  
20397 C C   . ARG C 1060 ? 3.0210 1.5658 2.2960 -0.1466 -0.7527 0.3608  1060 ARG B C   
20398 O O   . ARG C 1060 ? 3.0725 1.5784 2.3018 -0.1254 -0.7393 0.3670  1060 ARG B O   
20399 C CB  . ARG C 1060 ? 2.9903 1.5190 2.2751 -0.1505 -0.6733 0.3352  1060 ARG B CB  
20400 C CG  . ARG C 1060 ? 2.8947 1.4643 2.2224 -0.1543 -0.6571 0.3468  1060 ARG B CG  
20401 C CD  . ARG C 1060 ? 2.9072 1.4700 2.2391 -0.1516 -0.6017 0.3406  1060 ARG B CD  
20402 N NE  . ARG C 1060 ? 2.9903 1.5490 2.3165 -0.1352 -0.5848 0.3530  1060 ARG B NE  
20403 C CZ  . ARG C 1060 ? 3.0262 1.5786 2.3549 -0.1303 -0.5384 0.3511  1060 ARG B CZ  
20404 N NH1 . ARG C 1060 ? 3.0385 1.5891 2.3727 -0.1414 -0.5041 0.3384  1060 ARG B NH1 
20405 N NH2 . ARG C 1060 ? 3.0387 1.5865 2.3643 -0.1148 -0.5267 0.3630  1060 ARG B NH2 
20406 N N   . ASN C 1061 ? 2.5614 1.1567 1.8793 -0.1614 -0.7859 0.3723  1061 ASN B N   
20407 C CA  . ASN C 1061 ? 2.6641 1.2684 1.9741 -0.1509 -0.8075 0.3938  1061 ASN B CA  
20408 C C   . ASN C 1061 ? 2.6972 1.3118 2.0239 -0.1394 -0.7695 0.4021  1061 ASN B C   
20409 O O   . ASN C 1061 ? 2.6832 1.2823 2.0100 -0.1340 -0.7228 0.3916  1061 ASN B O   
20410 C CB  . ASN C 1061 ? 2.6972 1.3536 2.0436 -0.1693 -0.8582 0.4055  1061 ASN B CB  
20411 C CG  . ASN C 1061 ? 2.8053 1.4344 2.1069 -0.1683 -0.9085 0.4108  1061 ASN B CG  
20412 O OD1 . ASN C 1061 ? 2.8325 1.4277 2.1079 -0.1697 -0.9122 0.3956  1061 ASN B OD1 
20413 N ND2 . ASN C 1061 ? 2.8647 1.5090 2.1574 -0.1663 -0.9471 0.4328  1061 ASN B ND2 
20414 N N   . ALA C 1062 ? 2.9901 1.6309 2.3301 -0.1357 -0.7917 0.4220  1062 ALA B N   
20415 C CA  . ALA C 1062 ? 3.0242 1.6669 2.3720 -0.1201 -0.7638 0.4338  1062 ALA B CA  
20416 C C   . ALA C 1062 ? 2.9686 1.6611 2.3809 -0.1326 -0.7331 0.4272  1062 ALA B C   
20417 O O   . ALA C 1062 ? 2.9903 1.6679 2.4052 -0.1249 -0.6865 0.4201  1062 ALA B O   
20418 C CB  . ALA C 1062 ? 3.0789 1.7327 2.4181 -0.1120 -0.8009 0.4592  1062 ALA B CB  
20419 N N   . ASP C 1063 ? 3.3756 2.1282 2.8382 -0.1535 -0.7611 0.4302  1063 ASP B N   
20420 C CA  . ASP C 1063 ? 3.3075 2.1194 2.8375 -0.1702 -0.7404 0.4256  1063 ASP B CA  
20421 C C   . ASP C 1063 ? 3.2007 2.0180 2.7530 -0.1888 -0.7075 0.4044  1063 ASP B C   
20422 O O   . ASP C 1063 ? 3.1375 2.0072 2.7472 -0.2106 -0.6932 0.3980  1063 ASP B O   
20423 C CB  . ASP C 1063 ? 3.3125 2.1876 2.8840 -0.1901 -0.7876 0.4349  1063 ASP B CB  
20424 C CG  . ASP C 1063 ? 3.3283 2.2047 2.8898 -0.2077 -0.8283 0.4293  1063 ASP B CG  
20425 O OD1 . ASP C 1063 ? 3.3263 2.1699 2.8698 -0.2112 -0.8112 0.4134  1063 ASP B OD1 
20426 O OD2 . ASP C 1063 ? 3.3488 2.2586 2.9199 -0.2179 -0.8778 0.4414  1063 ASP B OD2 
20427 N N   . TYR C 1064 ? 2.8756 1.6395 2.3815 -0.1812 -0.6962 0.3943  1064 TYR B N   
20428 C CA  . TYR C 1064 ? 2.8089 1.5686 2.3260 -0.1953 -0.6621 0.3764  1064 TYR B CA  
20429 C C   . TYR C 1064 ? 2.7773 1.5674 2.3215 -0.2223 -0.6941 0.3690  1064 TYR B C   
20430 O O   . TYR C 1064 ? 2.7919 1.5821 2.3487 -0.2375 -0.6729 0.3557  1064 TYR B O   
20431 C CB  . TYR C 1064 ? 2.7468 1.5358 2.3067 -0.2035 -0.6149 0.3722  1064 TYR B CB  
20432 C CG  . TYR C 1064 ? 2.7860 1.5340 2.3133 -0.1757 -0.5787 0.3773  1064 TYR B CG  
20433 C CD1 . TYR C 1064 ? 2.7998 1.4931 2.2803 -0.1620 -0.5441 0.3694  1064 TYR B CD1 
20434 C CD2 . TYR C 1064 ? 2.8151 1.5798 2.3584 -0.1630 -0.5808 0.3908  1064 TYR B CD2 
20435 C CE1 . TYR C 1064 ? 2.8609 1.5173 2.3114 -0.1378 -0.5136 0.3750  1064 TYR B CE1 
20436 C CE2 . TYR C 1064 ? 2.8791 1.6054 2.3950 -0.1378 -0.5492 0.3965  1064 TYR B CE2 
20437 C CZ  . TYR C 1064 ? 2.8912 1.5637 2.3608 -0.1261 -0.5166 0.3887  1064 TYR B CZ  
20438 O OH  . TYR C 1064 ? 2.9381 1.5746 2.3817 -0.1031 -0.4882 0.3950  1064 TYR B OH  
20439 N N   . SER C 1065 ? 2.8768 1.6918 2.4286 -0.2283 -0.7466 0.3792  1065 SER B N   
20440 C CA  . SER C 1065 ? 2.8145 1.6495 2.3829 -0.2509 -0.7851 0.3738  1065 SER B CA  
20441 C C   . SER C 1065 ? 2.8211 1.5912 2.3293 -0.2362 -0.7921 0.3660  1065 SER B C   
20442 O O   . SER C 1065 ? 2.8782 1.5996 2.3295 -0.2107 -0.7974 0.3724  1065 SER B O   
20443 C CB  . SER C 1065 ? 2.8274 1.7041 2.4136 -0.2601 -0.8417 0.3886  1065 SER B CB  
20444 O OG  . SER C 1065 ? 2.9098 1.7400 2.4351 -0.2366 -0.8704 0.3997  1065 SER B OG  
20445 N N   . TYR C 1066 ? 2.4674 1.2382 1.9897 -0.2534 -0.7915 0.3523  1066 TYR B N   
20446 C CA  . TYR C 1066 ? 2.5030 1.2163 1.9739 -0.2413 -0.7989 0.3425  1066 TYR B CA  
20447 C C   . TYR C 1066 ? 2.5334 1.2485 1.9924 -0.2458 -0.8609 0.3488  1066 TYR B C   
20448 O O   . TYR C 1066 ? 2.5314 1.2935 2.0216 -0.2584 -0.8952 0.3617  1066 TYR B O   
20449 C CB  . TYR C 1066 ? 2.4349 1.1487 1.9283 -0.2569 -0.7693 0.3264  1066 TYR B CB  
20450 C CG  . TYR C 1066 ? 2.4343 1.1329 1.9207 -0.2476 -0.7081 0.3220  1066 TYR B CG  
20451 C CD1 . TYR C 1066 ? 2.4290 1.1537 1.9363 -0.2454 -0.6856 0.3310  1066 TYR B CD1 
20452 C CD2 . TYR C 1066 ? 2.4524 1.1098 1.9092 -0.2399 -0.6733 0.3094  1066 TYR B CD2 
20453 C CE1 . TYR C 1066 ? 2.4647 1.1731 1.9631 -0.2367 -0.6306 0.3276  1066 TYR B CE1 
20454 C CE2 . TYR C 1066 ? 2.4826 1.1255 1.9283 -0.2317 -0.6184 0.3071  1066 TYR B CE2 
20455 C CZ  . TYR C 1066 ? 2.4983 1.1659 1.9645 -0.2304 -0.5976 0.3163  1066 TYR B CZ  
20456 O OH  . TYR C 1066 ? 2.5343 1.1862 1.9884 -0.2227 -0.5450 0.3146  1066 TYR B OH  
20457 N N   . SER C 1067 ? 2.6858 1.3503 2.0980 -0.2357 -0.8764 0.3403  1067 SER B N   
20458 C CA  . SER C 1067 ? 2.7082 1.3722 2.1078 -0.2419 -0.9361 0.3458  1067 SER B CA  
20459 C C   . SER C 1067 ? 2.7416 1.3615 2.1116 -0.2402 -0.9498 0.3300  1067 SER B C   
20460 O O   . SER C 1067 ? 2.7708 1.3404 2.1014 -0.2231 -0.9162 0.3169  1067 SER B O   
20461 C CB  . SER C 1067 ? 2.7607 1.4061 2.1146 -0.2236 -0.9611 0.3638  1067 SER B CB  
20462 O OG  . SER C 1067 ? 2.7881 1.4373 2.1305 -0.2324 -1.0202 0.3713  1067 SER B OG  
20463 N N   . VAL C 1068 ? 2.7513 1.3919 2.1410 -0.2584 -1.0006 0.3316  1068 VAL B N   
20464 C CA  . VAL C 1068 ? 2.7837 1.3899 2.1566 -0.2605 -1.0200 0.3168  1068 VAL B CA  
20465 C C   . VAL C 1068 ? 2.9125 1.4412 2.2076 -0.2324 -1.0084 0.3062  1068 VAL B C   
20466 O O   . VAL C 1068 ? 2.9303 1.4282 2.2130 -0.2229 -0.9682 0.2899  1068 VAL B O   
20467 C CB  . VAL C 1068 ? 2.7761 1.4066 2.1639 -0.2786 -1.0854 0.3250  1068 VAL B CB  
20468 C CG1 . VAL C 1068 ? 2.8631 1.4844 2.2058 -0.2666 -1.1191 0.3446  1068 VAL B CG1 
20469 C CG2 . VAL C 1068 ? 2.7840 1.3738 2.1533 -0.2787 -1.1044 0.3086  1068 VAL B CG2 
20470 N N   . TRP C 1069 ? 2.8068 1.3062 2.0503 -0.2215 -1.0454 0.3156  1069 TRP B N   
20471 C CA  . TRP C 1069 ? 2.8954 1.3253 2.0615 -0.1960 -1.0332 0.3088  1069 TRP B CA  
20472 C C   . TRP C 1069 ? 2.9406 1.3629 2.0718 -0.1803 -1.0231 0.3273  1069 TRP B C   
20473 O O   . TRP C 1069 ? 2.9201 1.3820 2.0722 -0.1882 -1.0478 0.3481  1069 TRP B O   
20474 C CB  . TRP C 1069 ? 2.9394 1.3321 2.0638 -0.1956 -1.0803 0.3048  1069 TRP B CB  
20475 C CG  . TRP C 1069 ? 2.8700 1.2841 2.0375 -0.2161 -1.1119 0.2959  1069 TRP B CG  
20476 C CD1 . TRP C 1069 ? 2.8449 1.2385 2.0237 -0.2175 -1.0987 0.2736  1069 TRP B CD1 
20477 C CD2 . TRP C 1069 ? 2.7957 1.2574 2.0025 -0.2391 -1.1648 0.3100  1069 TRP B CD2 
20478 N NE1 . TRP C 1069 ? 2.7961 1.2207 2.0213 -0.2405 -1.1405 0.2732  1069 TRP B NE1 
20479 C CE2 . TRP C 1069 ? 2.7855 1.2530 2.0280 -0.2547 -1.1825 0.2952  1069 TRP B CE2 
20480 C CE3 . TRP C 1069 ? 2.7576 1.2596 1.9734 -0.2484 -1.1998 0.3344  1069 TRP B CE3 
20481 C CZ2 . TRP C 1069 ? 2.7754 1.2876 2.0623 -0.2806 -1.2353 0.3040  1069 TRP B CZ2 
20482 C CZ3 . TRP C 1069 ? 2.7603 1.3076 2.0174 -0.2735 -1.2517 0.3428  1069 TRP B CZ3 
20483 C CH2 . TRP C 1069 ? 2.7750 1.3273 2.0673 -0.2900 -1.2699 0.3276  1069 TRP B CH2 
20484 N N   . LYS C 1070 ? 2.6506 1.0224 1.7284 -0.1589 -0.9891 0.3201  1070 LYS B N   
20485 C CA  . LYS C 1070 ? 2.6511 1.0169 1.7058 -0.1439 -0.9643 0.3350  1070 LYS B CA  
20486 C C   . LYS C 1070 ? 2.6803 1.0750 1.7393 -0.1480 -0.9998 0.3622  1070 LYS B C   
20487 O O   . LYS C 1070 ? 2.7217 1.1051 1.7523 -0.1520 -1.0451 0.3714  1070 LYS B O   
20488 C CB  . LYS C 1070 ? 2.6830 0.9855 1.6660 -0.1234 -0.9440 0.3270  1070 LYS B CB  
20489 C CG  . LYS C 1070 ? 2.6478 0.9352 1.6305 -0.1133 -0.8879 0.3104  1070 LYS B CG  
20490 C CD  . LYS C 1070 ? 2.7099 0.9580 1.6369 -0.0942 -0.8623 0.3143  1070 LYS B CD  
20491 C CE  . LYS C 1070 ? 2.7694 0.9616 1.6322 -0.0854 -0.8682 0.2988  1070 LYS B CE  
20492 N NZ  . LYS C 1070 ? 2.8267 0.9869 1.6423 -0.0696 -0.8365 0.3005  1070 LYS B NZ  
20493 N N   . GLY C 1071 ? 2.6466 1.0786 1.7410 -0.1472 -0.9782 0.3753  1071 GLY B N   
20494 C CA  . GLY C 1071 ? 2.7058 1.1689 1.8083 -0.1489 -1.0054 0.4022  1071 GLY B CA  
20495 C C   . GLY C 1071 ? 2.7070 1.2235 1.8536 -0.1708 -1.0522 0.4114  1071 GLY B C   
20496 O O   . GLY C 1071 ? 2.7559 1.3153 1.9284 -0.1751 -1.0675 0.4321  1071 GLY B O   
20497 N N   . GLY C 1072 ? 4.5119 3.0271 3.6680 -0.1848 -1.0755 0.3964  1072 GLY B N   
20498 C CA  . GLY C 1072 ? 4.4889 3.0534 3.6857 -0.2082 -1.1242 0.4036  1072 GLY B CA  
20499 C C   . GLY C 1072 ? 4.4384 3.0742 3.7018 -0.2213 -1.1182 0.4148  1072 GLY B C   
20500 O O   . GLY C 1072 ? 4.4066 3.0537 3.6963 -0.2158 -1.0701 0.4091  1072 GLY B O   
20501 N N   . SER C 1073 ? 3.1655 1.8501 2.4547 -0.2390 -1.1671 0.4307  1073 SER B N   
20502 C CA  . SER C 1073 ? 3.1057 1.8622 2.4575 -0.2523 -1.1644 0.4415  1073 SER B CA  
20503 C C   . SER C 1073 ? 2.9976 1.7802 2.4070 -0.2655 -1.1242 0.4208  1073 SER B C   
20504 O O   . SER C 1073 ? 2.9499 1.7332 2.3779 -0.2812 -1.1342 0.4058  1073 SER B O   
20505 C CB  . SER C 1073 ? 3.1112 1.9209 2.4867 -0.2748 -1.2269 0.4575  1073 SER B CB  
20506 O OG  . SER C 1073 ? 3.1267 1.9281 2.5024 -0.2911 -1.2617 0.4463  1073 SER B OG  
20507 N N   . ALA C 1074 ? 2.7338 1.5357 2.1701 -0.2592 -1.0782 0.4209  1074 ALA B N   
20508 C CA  . ALA C 1074 ? 2.6521 1.4732 2.1360 -0.2706 -1.0329 0.4028  1074 ALA B CA  
20509 C C   . ALA C 1074 ? 2.5649 1.4427 2.1115 -0.3057 -1.0587 0.3957  1074 ALA B C   
20510 O O   . ALA C 1074 ? 2.5560 1.4961 2.1442 -0.3261 -1.0935 0.4072  1074 ALA B O   
20511 C CB  . ALA C 1074 ? 2.6611 1.5088 2.1724 -0.2638 -0.9908 0.4081  1074 ALA B CB  
20512 N N   . SER C 1075 ? 3.1499 2.0075 2.7035 -0.3138 -1.0433 0.3777  1075 SER B N   
20513 C CA  . SER C 1075 ? 3.0730 1.9820 2.6883 -0.3486 -1.0657 0.3716  1075 SER B CA  
20514 C C   . SER C 1075 ? 3.0044 1.9637 2.6827 -0.3679 -1.0222 0.3660  1075 SER B C   
20515 O O   . SER C 1075 ? 2.9764 1.9057 2.6434 -0.3553 -0.9675 0.3563  1075 SER B O   
20516 C CB  . SER C 1075 ? 3.0911 1.9555 2.6879 -0.3490 -1.0700 0.3560  1075 SER B CB  
20517 O OG  . SER C 1075 ? 3.1027 1.9207 2.6763 -0.3317 -1.0125 0.3419  1075 SER B OG  
20518 N N   . THR C 1076 ? 2.5275 1.5638 2.2707 -0.3998 -1.0461 0.3722  1076 THR B N   
20519 C CA  . THR C 1076 ? 2.4278 1.5161 2.2341 -0.4236 -1.0060 0.3664  1076 THR B CA  
20520 C C   . THR C 1076 ? 2.3727 1.4519 2.2026 -0.4414 -0.9832 0.3519  1076 THR B C   
20521 O O   . THR C 1076 ? 2.3505 1.4305 2.1981 -0.4456 -0.9291 0.3443  1076 THR B O   
20522 C CB  . THR C 1076 ? 2.3570 1.5358 2.2287 -0.4565 -1.0398 0.3765  1076 THR B CB  
20523 O OG1 . THR C 1076 ? 2.3471 1.5684 2.2639 -0.4685 -0.9933 0.3734  1076 THR B OG1 
20524 C CG2 . THR C 1076 ? 2.2839 1.5060 2.2032 -0.4941 -1.0832 0.3745  1076 THR B CG2 
20525 N N   . TRP C 1077 ? 2.4817 1.5500 2.3092 -0.4510 -1.0253 0.3493  1077 TRP B N   
20526 C CA  . TRP C 1077 ? 2.4507 1.5055 2.2974 -0.4658 -1.0137 0.3372  1077 TRP B CA  
20527 C C   . TRP C 1077 ? 2.4154 1.4035 2.2170 -0.4385 -0.9544 0.3255  1077 TRP B C   
20528 O O   . TRP C 1077 ? 2.3327 1.3347 2.1647 -0.4520 -0.9084 0.3199  1077 TRP B O   
20529 C CB  . TRP C 1077 ? 2.5030 1.5376 2.3336 -0.4677 -1.0725 0.3370  1077 TRP B CB  
20530 C CG  . TRP C 1077 ? 2.5276 1.5537 2.3845 -0.4849 -1.0739 0.3263  1077 TRP B CG  
20531 C CD1 . TRP C 1077 ? 2.5087 1.5940 2.4360 -0.5257 -1.1037 0.3286  1077 TRP B CD1 
20532 C CD2 . TRP C 1077 ? 2.5878 1.5431 2.4019 -0.4621 -1.0472 0.3126  1077 TRP B CD2 
20533 N NE1 . TRP C 1077 ? 2.5266 1.5816 2.4599 -0.5293 -1.0959 0.3180  1077 TRP B NE1 
20534 C CE2 . TRP C 1077 ? 2.5723 1.5477 2.4361 -0.4898 -1.0609 0.3075  1077 TRP B CE2 
20535 C CE3 . TRP C 1077 ? 2.6535 1.5334 2.3940 -0.4222 -1.0130 0.3043  1077 TRP B CE3 
20536 C CZ2 . TRP C 1077 ? 2.5800 1.5013 2.4219 -0.4767 -1.0404 0.2941  1077 TRP B CZ2 
20537 C CZ3 . TRP C 1077 ? 2.6800 1.5084 2.3975 -0.4105 -0.9933 0.2901  1077 TRP B CZ3 
20538 C CH2 . TRP C 1077 ? 2.6297 1.4783 2.3972 -0.4365 -1.0064 0.2850  1077 TRP B CH2 
20539 N N   . LEU C 1078 ? 2.4656 1.3831 2.1931 -0.4019 -0.9564 0.3227  1078 LEU B N   
20540 C CA  . LEU C 1078 ? 2.4712 1.3249 2.1489 -0.3742 -0.9044 0.3120  1078 LEU B CA  
20541 C C   . LEU C 1078 ? 2.4843 1.3473 2.1640 -0.3664 -0.8516 0.3151  1078 LEU B C   
20542 O O   . LEU C 1078 ? 2.4926 1.3349 2.1659 -0.3621 -0.8008 0.3072  1078 LEU B O   
20543 C CB  . LEU C 1078 ? 2.4878 1.2701 2.0864 -0.3393 -0.9218 0.3095  1078 LEU B CB  
20544 C CG  . LEU C 1078 ? 2.4503 1.1663 1.9982 -0.3149 -0.8789 0.2953  1078 LEU B CG  
20545 C CD1 . LEU C 1078 ? 2.4676 1.1241 1.9570 -0.2947 -0.9082 0.2878  1078 LEU B CD1 
20546 C CD2 . LEU C 1078 ? 2.4668 1.1613 1.9812 -0.2922 -0.8320 0.2982  1078 LEU B CD2 
20547 N N   . THR C 1079 ? 2.5573 1.4530 2.2472 -0.3654 -0.8641 0.3270  1079 THR B N   
20548 C CA  . THR C 1079 ? 2.5588 1.4637 2.2526 -0.3571 -0.8174 0.3302  1079 THR B CA  
20549 C C   . THR C 1079 ? 2.4903 1.4282 2.2340 -0.3830 -0.7739 0.3235  1079 THR B C   
20550 O O   . THR C 1079 ? 2.5033 1.4233 2.2339 -0.3723 -0.7219 0.3207  1079 THR B O   
20551 C CB  . THR C 1079 ? 2.6889 1.6437 2.4088 -0.3620 -0.8415 0.3439  1079 THR B CB  
20552 O OG1 . THR C 1079 ? 2.7514 1.6686 2.4159 -0.3338 -0.8720 0.3532  1079 THR B OG1 
20553 C CG2 . THR C 1079 ? 2.6601 1.6342 2.3998 -0.3600 -0.7910 0.3449  1079 THR B CG2 
20554 N N   . ALA C 1080 ? 1.8628 0.8497 1.6638 -0.4189 -0.7960 0.3222  1080 ALA B N   
20555 C CA  . ALA C 1080 ? 1.7771 0.7928 1.6238 -0.4468 -0.7557 0.3173  1080 ALA B CA  
20556 C C   . ALA C 1080 ? 1.7598 0.7251 1.5787 -0.4393 -0.7341 0.3077  1080 ALA B C   
20557 O O   . ALA C 1080 ? 1.7363 0.6860 1.5486 -0.4383 -0.6813 0.3039  1080 ALA B O   
20558 C CB  . ALA C 1080 ? 1.7233 0.8195 1.6492 -0.4927 -0.7852 0.3216  1080 ALA B CB  
20559 N N   . PHE C 1081 ? 2.2737 1.2143 2.0767 -0.4347 -0.7744 0.3040  1081 PHE B N   
20560 C CA  . PHE C 1081 ? 2.2544 1.1517 2.0370 -0.4288 -0.7538 0.2941  1081 PHE B CA  
20561 C C   . PHE C 1081 ? 2.2485 1.0867 1.9691 -0.3960 -0.7012 0.2886  1081 PHE B C   
20562 O O   . PHE C 1081 ? 2.1978 1.0171 1.9132 -0.3977 -0.6630 0.2829  1081 PHE B O   
20563 C CB  . PHE C 1081 ? 2.3180 1.1815 2.0765 -0.4186 -0.8010 0.2886  1081 PHE B CB  
20564 C CG  . PHE C 1081 ? 2.3620 1.1838 2.1042 -0.4126 -0.7792 0.2773  1081 PHE B CG  
20565 C CD1 . PHE C 1081 ? 2.3365 1.1844 2.1299 -0.4408 -0.8005 0.2758  1081 PHE B CD1 
20566 C CD2 . PHE C 1081 ? 2.4525 1.2115 2.1302 -0.3798 -0.7381 0.2689  1081 PHE B CD2 
20567 C CE1 . PHE C 1081 ? 2.3572 1.1682 2.1386 -0.4347 -0.7801 0.2661  1081 PHE B CE1 
20568 C CE2 . PHE C 1081 ? 2.4761 1.2000 2.1394 -0.3742 -0.7183 0.2586  1081 PHE B CE2 
20569 C CZ  . PHE C 1081 ? 2.4262 1.1757 2.1418 -0.4009 -0.7386 0.2571  1081 PHE B CZ  
20570 N N   . ALA C 1082 ? 2.9247 1.7336 2.5970 -0.3664 -0.7001 0.2914  1082 ALA B N   
20571 C CA  . ALA C 1082 ? 2.9686 1.7313 2.5900 -0.3400 -0.6486 0.2881  1082 ALA B CA  
20572 C C   . ALA C 1082 ? 2.9187 1.7229 2.5820 -0.3610 -0.6039 0.2926  1082 ALA B C   
20573 O O   . ALA C 1082 ? 2.9161 1.7020 2.5673 -0.3608 -0.5572 0.2889  1082 ALA B O   
20574 C CB  . ALA C 1082 ? 3.0480 1.7725 2.6125 -0.3061 -0.6579 0.2919  1082 ALA B CB  
20575 N N   . LEU C 1083 ? 1.6497 0.5110 1.3618 -0.3805 -0.6181 0.3007  1083 LEU B N   
20576 C CA  . LEU C 1083 ? 1.5854 0.4846 1.3341 -0.3993 -0.5750 0.3041  1083 LEU B CA  
20577 C C   . LEU C 1083 ? 1.5702 0.4735 1.3384 -0.4215 -0.5443 0.3003  1083 LEU B C   
20578 O O   . LEU C 1083 ? 1.6106 0.4830 1.3491 -0.4117 -0.4957 0.2982  1083 LEU B O   
20579 C CB  . LEU C 1083 ? 1.5022 0.4761 1.3176 -0.4292 -0.6014 0.3109  1083 LEU B CB  
20580 C CG  . LEU C 1083 ? 1.5063 0.4768 1.3013 -0.4049 -0.6077 0.3167  1083 LEU B CG  
20581 C CD1 . LEU C 1083 ? 1.4914 0.5276 1.3376 -0.4251 -0.6513 0.3239  1083 LEU B CD1 
20582 C CD2 . LEU C 1083 ? 1.5463 0.5055 1.3308 -0.3958 -0.5497 0.3163  1083 LEU B CD2 
20583 N N   . ARG C 1084 ? 1.8464 0.7858 1.6621 -0.4507 -0.5763 0.3004  1084 ARG B N   
20584 C CA  . ARG C 1084 ? 1.8415 0.7851 1.6792 -0.4731 -0.5545 0.2985  1084 ARG B CA  
20585 C C   . ARG C 1084 ? 1.9120 0.7865 1.6838 -0.4433 -0.5127 0.2923  1084 ARG B C   
20586 O O   . ARG C 1084 ? 1.9154 0.7865 1.6806 -0.4479 -0.4610 0.2946  1084 ARG B O   
20587 C CB  . ARG C 1084 ? 1.8357 0.8073 1.7168 -0.4967 -0.6053 0.2983  1084 ARG B CB  
20588 C CG  . ARG C 1084 ? 1.7798 0.7384 1.6706 -0.5093 -0.5881 0.2956  1084 ARG B CG  
20589 C CD  . ARG C 1084 ? 1.7534 0.7712 1.7206 -0.5535 -0.6193 0.3007  1084 ARG B CD  
20590 N NE  . ARG C 1084 ? 1.8054 0.8051 1.7781 -0.5618 -0.5981 0.2993  1084 ARG B NE  
20591 C CZ  . ARG C 1084 ? 1.8771 0.8833 1.8805 -0.5756 -0.6337 0.2982  1084 ARG B CZ  
20592 N NH1 . ARG C 1084 ? 1.9229 0.9544 1.9536 -0.5847 -0.6940 0.2984  1084 ARG B NH1 
20593 N NH2 . ARG C 1084 ? 1.8736 0.8623 1.8807 -0.5805 -0.6095 0.2976  1084 ARG B NH2 
20594 N N   . VAL C 1085 ? 2.0284 0.8486 1.7493 -0.4136 -0.5336 0.2846  1085 VAL B N   
20595 C CA  . VAL C 1085 ? 2.0979 0.8612 1.7630 -0.3907 -0.4952 0.2781  1085 VAL B CA  
20596 C C   . VAL C 1085 ? 2.1349 0.8612 1.7430 -0.3613 -0.4587 0.2786  1085 VAL B C   
20597 O O   . VAL C 1085 ? 2.1534 0.8315 1.7074 -0.3392 -0.4281 0.2738  1085 VAL B O   
20598 C CB  . VAL C 1085 ? 2.0105 0.7264 1.6384 -0.3693 -0.5238 0.2675  1085 VAL B CB  
20599 C CG1 . VAL C 1085 ? 2.0103 0.6901 1.6077 -0.3611 -0.4832 0.2618  1085 VAL B CG1 
20600 C CG2 . VAL C 1085 ? 1.9516 0.7030 1.6342 -0.3939 -0.5756 0.2677  1085 VAL B CG2 
20601 N N   . LEU C 1086 ? 2.9753 1.7258 2.5969 -0.3614 -0.4637 0.2847  1086 LEU B N   
20602 C CA  . LEU C 1086 ? 3.0612 1.7850 2.6412 -0.3386 -0.4282 0.2871  1086 LEU B CA  
20603 C C   . LEU C 1086 ? 3.0304 1.7810 2.6373 -0.3618 -0.3776 0.2921  1086 LEU B C   
20604 O O   . LEU C 1086 ? 3.0718 1.7873 2.6354 -0.3474 -0.3346 0.2920  1086 LEU B O   
20605 C CB  . LEU C 1086 ? 3.1170 1.8567 2.7041 -0.3289 -0.4550 0.2923  1086 LEU B CB  
20606 C CG  . LEU C 1086 ? 3.2671 1.9529 2.7897 -0.2901 -0.4756 0.2906  1086 LEU B CG  
20607 C CD1 . LEU C 1086 ? 3.2905 1.9287 2.7560 -0.2640 -0.4315 0.2901  1086 LEU B CD1 
20608 C CD2 . LEU C 1086 ? 3.2960 1.9527 2.7948 -0.2827 -0.5086 0.2826  1086 LEU B CD2 
20609 N N   . GLY C 1087 ? 2.3318 1.1465 2.0097 -0.3996 -0.3841 0.2971  1087 GLY B N   
20610 C CA  . GLY C 1087 ? 2.2748 1.1240 1.9869 -0.4290 -0.3388 0.3026  1087 GLY B CA  
20611 C C   . GLY C 1087 ? 2.2231 1.0660 1.9358 -0.4466 -0.3105 0.3038  1087 GLY B C   
20612 O O   . GLY C 1087 ? 2.2338 1.0847 1.9498 -0.4628 -0.2635 0.3092  1087 GLY B O   
20613 N N   . GLN C 1088 ? 1.9023 0.7309 1.6120 -0.4437 -0.3393 0.2994  1088 GLN B N   
20614 C CA  . GLN C 1088 ? 1.9084 0.7280 1.6177 -0.4569 -0.3154 0.3007  1088 GLN B CA  
20615 C C   . GLN C 1088 ? 2.0184 0.7755 1.6505 -0.4242 -0.2754 0.2979  1088 GLN B C   
20616 O O   . GLN C 1088 ? 2.0177 0.7730 1.6423 -0.4368 -0.2309 0.3042  1088 GLN B O   
20617 C CB  . GLN C 1088 ? 1.8893 0.7075 1.6162 -0.4593 -0.3594 0.2954  1088 GLN B CB  
20618 C CG  . GLN C 1088 ? 1.8618 0.7433 1.6661 -0.4949 -0.4027 0.2992  1088 GLN B CG  
20619 C CD  . GLN C 1088 ? 1.8600 0.7423 1.6888 -0.5047 -0.4368 0.2961  1088 GLN B CD  
20620 O OE1 . GLN C 1088 ? 1.8246 0.7372 1.6939 -0.5182 -0.4877 0.2955  1088 GLN B OE1 
20621 N NE2 . GLN C 1088 ? 1.8720 0.7218 1.6766 -0.4982 -0.4092 0.2946  1088 GLN B NE2 
20622 N N   . VAL C 1089 ? 2.5912 1.2984 2.1646 -0.3837 -0.2924 0.2896  1089 VAL B N   
20623 C CA  . VAL C 1089 ? 2.6483 1.2984 2.1471 -0.3525 -0.2593 0.2865  1089 VAL B CA  
20624 C C   . VAL C 1089 ? 2.6898 1.3382 2.1707 -0.3483 -0.2221 0.2931  1089 VAL B C   
20625 O O   . VAL C 1089 ? 2.7098 1.3176 2.1325 -0.3272 -0.1902 0.2932  1089 VAL B O   
20626 C CB  . VAL C 1089 ? 2.6049 1.2050 2.0492 -0.3144 -0.2913 0.2753  1089 VAL B CB  
20627 C CG1 . VAL C 1089 ? 2.6301 1.1765 2.0015 -0.2870 -0.2597 0.2711  1089 VAL B CG1 
20628 C CG2 . VAL C 1089 ? 2.5949 1.2025 2.0669 -0.3222 -0.3329 0.2685  1089 VAL B CG2 
20629 N N   . ASN C 1090 ? 2.2274 0.9216 1.7594 -0.3694 -0.2263 0.2985  1090 ASN B N   
20630 C CA  . ASN C 1090 ? 2.3033 0.9964 1.8228 -0.3663 -0.1905 0.3039  1090 ASN B CA  
20631 C C   . ASN C 1090 ? 2.3191 1.0150 1.8332 -0.3866 -0.1380 0.3112  1090 ASN B C   
20632 O O   . ASN C 1090 ? 2.3451 1.0262 1.8319 -0.3805 -0.1012 0.3156  1090 ASN B O   
20633 C CB  . ASN C 1090 ? 2.3059 1.0504 1.8841 -0.3855 -0.2050 0.3068  1090 ASN B CB  
20634 C CG  . ASN C 1090 ? 2.3615 1.0991 1.9244 -0.3769 -0.1705 0.3105  1090 ASN B CG  
20635 O OD1 . ASN C 1090 ? 2.3577 1.0843 1.9013 -0.3840 -0.1242 0.3150  1090 ASN B OD1 
20636 N ND2 . ASN C 1090 ? 2.4162 1.1589 1.9861 -0.3609 -0.1934 0.3095  1090 ASN B ND2 
20637 N N   . LYS C 1091 ? 2.3994 1.1144 1.9400 -0.4119 -0.1353 0.3139  1091 LYS B N   
20638 C CA  . LYS C 1091 ? 2.4148 1.1375 1.9543 -0.4361 -0.0869 0.3239  1091 LYS B CA  
20639 C C   . LYS C 1091 ? 2.4172 1.0822 1.8759 -0.4055 -0.0540 0.3242  1091 LYS B C   
20640 O O   . LYS C 1091 ? 2.4396 1.1050 1.8791 -0.4122 -0.0112 0.3311  1091 LYS B O   
20641 C CB  . LYS C 1091 ? 2.4784 1.2428 2.0572 -0.4597 -0.0953 0.3228  1091 LYS B CB  
20642 C CG  . LYS C 1091 ? 2.5173 1.3789 2.1824 -0.4973 -0.1104 0.3215  1091 LYS B CG  
20643 C CD  . LYS C 1091 ? 2.5646 1.4842 2.2557 -0.5170 -0.0919 0.3215  1091 LYS B CD  
20644 C CE  . LYS C 1091 ? 2.6536 1.5622 2.2948 -0.5090 -0.0368 0.3231  1091 LYS B CE  
20645 N NZ  . LYS C 1091 ? 2.6550 1.6282 2.3222 -0.5291 -0.0138 0.3236  1091 LYS B NZ  
20646 N N   . TYR C 1092 ? 2.4955 1.1163 1.9057 -0.3713 -0.0754 0.3148  1092 TYR B N   
20647 C CA  . TYR C 1092 ? 2.5303 1.1000 1.8642 -0.3451 -0.0470 0.3147  1092 TYR B CA  
20648 C C   . TYR C 1092 ? 2.6619 1.1854 1.9376 -0.3030 -0.0629 0.3062  1092 TYR B C   
20649 O O   . TYR C 1092 ? 2.7401 1.2221 1.9500 -0.2802 -0.0421 0.3058  1092 TYR B O   
20650 C CB  . TYR C 1092 ? 2.4697 1.0273 1.7914 -0.3452 -0.0487 0.3121  1092 TYR B CB  
20651 C CG  . TYR C 1092 ? 2.3884 0.9938 1.7768 -0.3867 -0.0449 0.3205  1092 TYR B CG  
20652 C CD1 . TYR C 1092 ? 2.3689 1.0226 1.7718 -0.4107 -0.0033 0.3269  1092 TYR B CD1 
20653 C CD2 . TYR C 1092 ? 2.3694 0.9967 1.8068 -0.3964 -0.0860 0.3143  1092 TYR B CD2 
20654 C CE1 . TYR C 1092 ? 2.3339 1.0634 1.7999 -0.4412 -0.0032 0.3257  1092 TYR B CE1 
20655 C CE2 . TYR C 1092 ? 2.3241 1.0107 1.8261 -0.4325 -0.0856 0.3191  1092 TYR B CE2 
20656 C CZ  . TYR C 1092 ? 2.3067 1.0536 1.8233 -0.4520 -0.0445 0.3227  1092 TYR B CZ  
20657 O OH  . TYR C 1092 ? 2.2574 1.0824 1.8381 -0.4813 -0.0467 0.3231  1092 TYR B OH  
20658 N N   . VAL C 1093 ? 3.0427 1.5754 2.3428 -0.2944 -0.1013 0.3005  1093 VAL B N   
20659 C CA  . VAL C 1093 ? 3.0911 1.5848 2.3429 -0.2582 -0.1190 0.2949  1093 VAL B CA  
20660 C C   . VAL C 1093 ? 3.0477 1.5688 2.3397 -0.2628 -0.1333 0.2985  1093 VAL B C   
20661 O O   . VAL C 1093 ? 3.0132 1.5591 2.3461 -0.2682 -0.1725 0.2954  1093 VAL B O   
20662 C CB  . VAL C 1093 ? 3.1250 1.5934 2.3547 -0.2376 -0.1599 0.2832  1093 VAL B CB  
20663 C CG1 . VAL C 1093 ? 3.2062 1.6446 2.3999 -0.2069 -0.1861 0.2795  1093 VAL B CG1 
20664 C CG2 . VAL C 1093 ? 3.1301 1.5675 2.3129 -0.2287 -0.1415 0.2783  1093 VAL B CG2 
20665 N N   . GLU C 1094 ? 2.4961 1.0140 1.7773 -0.2617 -0.1008 0.3053  1094 GLU B N   
20666 C CA  . GLU C 1094 ? 2.4710 1.0188 1.7954 -0.2683 -0.1077 0.3088  1094 GLU B CA  
20667 C C   . GLU C 1094 ? 2.4680 1.0092 1.7933 -0.2471 -0.1559 0.3042  1094 GLU B C   
20668 O O   . GLU C 1094 ? 2.5550 1.0529 1.8268 -0.2181 -0.1693 0.3008  1094 GLU B O   
20669 C CB  . GLU C 1094 ? 2.5522 1.0805 1.8489 -0.2565 -0.0734 0.3146  1094 GLU B CB  
20670 C CG  . GLU C 1094 ? 2.6142 1.1681 1.9526 -0.2553 -0.0879 0.3164  1094 GLU B CG  
20671 C CD  . GLU C 1094 ? 2.7204 1.2614 2.0448 -0.2480 -0.0525 0.3219  1094 GLU B CD  
20672 O OE1 . GLU C 1094 ? 2.7801 1.2825 2.0496 -0.2365 -0.0224 0.3250  1094 GLU B OE1 
20673 O OE2 . GLU C 1094 ? 2.7394 1.3100 2.1084 -0.2537 -0.0565 0.3231  1094 GLU B OE2 
20674 N N   . GLN C 1095 ? 2.2072 0.7926 1.5917 -0.2630 -0.1826 0.3049  1095 GLN B N   
20675 C CA  . GLN C 1095 ? 2.2360 0.8165 1.6195 -0.2438 -0.2281 0.3034  1095 GLN B CA  
20676 C C   . GLN C 1095 ? 2.3268 0.9166 1.7236 -0.2341 -0.2255 0.3095  1095 GLN B C   
20677 O O   . GLN C 1095 ? 2.3315 0.9438 1.7550 -0.2487 -0.1931 0.3129  1095 GLN B O   
20678 C CB  . GLN C 1095 ? 2.1708 0.7905 1.6042 -0.2643 -0.2688 0.3005  1095 GLN B CB  
20679 C CG  . GLN C 1095 ? 2.2155 0.8200 1.6338 -0.2693 -0.2749 0.2940  1095 GLN B CG  
20680 C CD  . GLN C 1095 ? 2.6375 1.1829 1.9855 -0.2351 -0.2871 0.2880  1095 GLN B CD  
20681 O OE1 . GLN C 1095 ? 2.6679 1.1961 1.9959 -0.2143 -0.3187 0.2880  1095 GLN B OE1 
20682 N NE2 . GLN C 1095 ? 2.6471 1.1632 1.9574 -0.2308 -0.2620 0.2835  1095 GLN B NE2 
20683 N N   . ASN C 1096 ? 3.0532 1.6239 2.4297 -0.2093 -0.2592 0.3113  1096 ASN B N   
20684 C CA  . ASN C 1096 ? 3.1398 1.7114 2.5216 -0.1940 -0.2595 0.3185  1096 ASN B CA  
20685 C C   . ASN C 1096 ? 3.1117 1.7437 2.5650 -0.2183 -0.2633 0.3208  1096 ASN B C   
20686 O O   . ASN C 1096 ? 3.0756 1.7430 2.5660 -0.2310 -0.3010 0.3205  1096 ASN B O   
20687 C CB  . ASN C 1096 ? 3.2353 1.7795 2.5848 -0.1672 -0.3003 0.3221  1096 ASN B CB  
20688 C CG  . ASN C 1096 ? 3.3308 1.8739 2.6850 -0.1496 -0.3017 0.3321  1096 ASN B CG  
20689 O OD1 . ASN C 1096 ? 3.4290 1.9298 2.7359 -0.1239 -0.3013 0.3372  1096 ASN B OD1 
20690 N ND2 . ASN C 1096 ? 3.3009 1.8927 2.7143 -0.1646 -0.3037 0.3353  1096 ASN B ND2 
20691 N N   . GLN C 1097 ? 2.6980 1.3427 2.1701 -0.2256 -0.2249 0.3228  1097 GLN B N   
20692 C CA  . GLN C 1097 ? 2.6847 1.3896 2.2257 -0.2509 -0.2250 0.3230  1097 GLN B CA  
20693 C C   . GLN C 1097 ? 2.7219 1.4497 2.2874 -0.2410 -0.2704 0.3275  1097 GLN B C   
20694 O O   . GLN C 1097 ? 2.6814 1.4342 2.2673 -0.2523 -0.3098 0.3266  1097 GLN B O   
20695 C CB  . GLN C 1097 ? 2.6767 1.3886 2.2322 -0.2570 -0.1779 0.3239  1097 GLN B CB  
20696 C CG  . GLN C 1097 ? 2.6143 1.3954 2.2456 -0.2885 -0.1783 0.3218  1097 GLN B CG  
20697 C CD  . GLN C 1097 ? 2.6230 1.4219 2.2769 -0.3116 -0.1266 0.3194  1097 GLN B CD  
20698 O OE1 . GLN C 1097 ? 2.6560 1.4131 2.2689 -0.2985 -0.0890 0.3209  1097 GLN B OE1 
20699 N NE2 . GLN C 1097 ? 2.5801 1.4429 2.2991 -0.3478 -0.1257 0.3160  1097 GLN B NE2 
20700 N N   . ASN C 1098 ? 2.7512 1.4699 2.3140 -0.2197 -0.2663 0.3336  1098 ASN B N   
20701 C CA  . ASN C 1098 ? 2.7895 1.5399 2.3843 -0.2143 -0.3053 0.3398  1098 ASN B CA  
20702 C C   . ASN C 1098 ? 2.5967 1.3471 2.1797 -0.2115 -0.3581 0.3423  1098 ASN B C   
20703 O O   . ASN C 1098 ? 2.5588 1.3486 2.1764 -0.2174 -0.3946 0.3472  1098 ASN B O   
20704 C CB  . ASN C 1098 ? 2.8889 1.6141 2.4674 -0.1840 -0.2981 0.3486  1098 ASN B CB  
20705 C CG  . ASN C 1098 ? 2.9501 1.7068 2.5580 -0.1768 -0.3391 0.3578  1098 ASN B CG  
20706 O OD1 . ASN C 1098 ? 3.0060 1.7352 2.5800 -0.1548 -0.3709 0.3671  1098 ASN B OD1 
20707 N ND2 . ASN C 1098 ? 2.9496 1.7665 2.6203 -0.1970 -0.3391 0.3558  1098 ASN B ND2 
20708 N N   . SER C 1099 ? 2.8880 1.5949 2.4215 -0.2032 -0.3625 0.3388  1099 SER B N   
20709 C CA  . SER C 1099 ? 2.8390 1.5441 2.3610 -0.2037 -0.4100 0.3388  1099 SER B CA  
20710 C C   . SER C 1099 ? 2.7285 1.4927 2.3095 -0.2393 -0.4275 0.3341  1099 SER B C   
20711 O O   . SER C 1099 ? 2.7294 1.5351 2.3462 -0.2486 -0.4658 0.3390  1099 SER B O   
20712 C CB  . SER C 1099 ? 2.8364 1.4857 2.2976 -0.1908 -0.4047 0.3327  1099 SER B CB  
20713 O OG  . SER C 1099 ? 2.7968 1.4484 2.2548 -0.1983 -0.4446 0.3289  1099 SER B OG  
20714 N N   . ILE C 1100 ? 2.6229 1.3925 2.2141 -0.2605 -0.3995 0.3259  1100 ILE B N   
20715 C CA  . ILE C 1100 ? 2.4918 1.3164 2.1395 -0.2979 -0.4128 0.3220  1100 ILE B CA  
20716 C C   . ILE C 1100 ? 2.4882 1.3774 2.1986 -0.3170 -0.4240 0.3259  1100 ILE B C   
20717 O O   . ILE C 1100 ? 2.4544 1.3890 2.2039 -0.3362 -0.4650 0.3274  1100 ILE B O   
20718 C CB  . ILE C 1100 ? 2.3642 1.1899 2.0195 -0.3197 -0.3678 0.3161  1100 ILE B CB  
20719 C CG1 . ILE C 1100 ? 2.3064 1.0901 1.9199 -0.3132 -0.3714 0.3111  1100 ILE B CG1 
20720 C CG2 . ILE C 1100 ? 2.2872 1.1837 2.0160 -0.3629 -0.3683 0.3152  1100 ILE B CG2 
20721 C CD1 . ILE C 1100 ? 2.2495 1.0606 1.8930 -0.3326 -0.4165 0.3089  1100 ILE B CD1 
20722 N N   . CYS C 1101 ? 2.4075 1.3010 2.1267 -0.3112 -0.3883 0.3273  1101 CYS B N   
20723 C CA  . CYS C 1101 ? 2.3942 1.3481 2.1718 -0.3264 -0.3942 0.3296  1101 CYS B CA  
20724 C C   . CYS C 1101 ? 2.3833 1.3615 2.1728 -0.3205 -0.4522 0.3369  1101 CYS B C   
20725 O O   . CYS C 1101 ? 2.3317 1.3657 2.1681 -0.3491 -0.4834 0.3364  1101 CYS B O   
20726 C CB  . CYS C 1101 ? 2.4519 1.3892 2.2218 -0.3065 -0.3558 0.3314  1101 CYS B CB  
20727 S SG  . CYS C 1101 ? 2.7493 1.7026 2.5456 -0.3321 -0.2897 0.3235  1101 CYS B SG  
20728 N N   . ASN C 1102 ? 2.4433 1.3806 2.1894 -0.2850 -0.4679 0.3451  1102 ASN B N   
20729 C CA  . ASN C 1102 ? 2.4412 1.3998 2.1938 -0.2786 -0.5213 0.3549  1102 ASN B CA  
20730 C C   . ASN C 1102 ? 2.4008 1.3719 2.1560 -0.2966 -0.5643 0.3531  1102 ASN B C   
20731 O O   . ASN C 1102 ? 2.3741 1.3948 2.1643 -0.3124 -0.6068 0.3583  1102 ASN B O   
20732 C CB  . ASN C 1102 ? 2.4984 1.4020 2.1955 -0.2391 -0.5289 0.3654  1102 ASN B CB  
20733 C CG  . ASN C 1102 ? 2.5274 1.4283 2.2330 -0.2226 -0.4951 0.3695  1102 ASN B CG  
20734 O OD1 . ASN C 1102 ? 2.5272 1.4813 2.2843 -0.2337 -0.4965 0.3715  1102 ASN B OD1 
20735 N ND2 . ASN C 1102 ? 2.5483 1.3893 2.2056 -0.1970 -0.4641 0.3703  1102 ASN B ND2 
20736 N N   . SER C 1103 ? 2.9508 1.8790 2.6710 -0.2952 -0.5528 0.3457  1103 SER B N   
20737 C CA  . SER C 1103 ? 2.9187 1.8496 2.6378 -0.3100 -0.5905 0.3425  1103 SER B CA  
20738 C C   . SER C 1103 ? 2.8708 1.8752 2.6613 -0.3532 -0.6061 0.3394  1103 SER B C   
20739 O O   . SER C 1103 ? 2.8480 1.8758 2.6536 -0.3674 -0.6543 0.3416  1103 SER B O   
20740 C CB  . SER C 1103 ? 2.9214 1.7928 2.5919 -0.2992 -0.5671 0.3339  1103 SER B CB  
20741 O OG  . SER C 1103 ? 2.9802 1.7877 2.5832 -0.2623 -0.5683 0.3373  1103 SER B OG  
20742 N N   . LEU C 1104 ? 2.2252 1.2657 2.0587 -0.3756 -0.5658 0.3348  1104 LEU B N   
20743 C CA  . LEU C 1104 ? 2.1773 1.2966 2.0846 -0.4195 -0.5778 0.3332  1104 LEU B CA  
20744 C C   . LEU C 1104 ? 2.2406 1.4112 2.1804 -0.4209 -0.6105 0.3408  1104 LEU B C   
20745 O O   . LEU C 1104 ? 2.2254 1.4364 2.1901 -0.4370 -0.6624 0.3456  1104 LEU B O   
20746 C CB  . LEU C 1104 ? 2.1136 1.2556 2.0544 -0.4447 -0.5215 0.3265  1104 LEU B CB  
20747 C CG  . LEU C 1104 ? 2.0623 1.1779 1.9915 -0.4581 -0.4851 0.3207  1104 LEU B CG  
20748 C CD1 . LEU C 1104 ? 2.0374 1.1674 1.9869 -0.4747 -0.4260 0.3175  1104 LEU B CD1 
20749 C CD2 . LEU C 1104 ? 1.9840 1.1359 1.9519 -0.4934 -0.5148 0.3199  1104 LEU B CD2 
20750 N N   . LEU C 1105 ? 2.0752 1.2417 2.0120 -0.4027 -0.5805 0.3426  1105 LEU B N   
20751 C CA  . LEU C 1105 ? 2.1131 1.3272 2.0812 -0.4008 -0.6018 0.3497  1105 LEU B CA  
20752 C C   . LEU C 1105 ? 2.1460 1.3563 2.0909 -0.3839 -0.6615 0.3621  1105 LEU B C   
20753 O O   . LEU C 1105 ? 2.1748 1.4253 2.1423 -0.3816 -0.6851 0.3705  1105 LEU B O   
20754 C CB  . LEU C 1105 ? 2.1579 1.3489 2.1140 -0.3749 -0.5573 0.3501  1105 LEU B CB  
20755 C CG  . LEU C 1105 ? 2.1534 1.3734 2.1504 -0.3965 -0.5032 0.3398  1105 LEU B CG  
20756 C CD1 . LEU C 1105 ? 2.2200 1.3747 2.1721 -0.3654 -0.4522 0.3382  1105 LEU B CD1 
20757 C CD2 . LEU C 1105 ? 2.1533 1.4476 2.2117 -0.4136 -0.5104 0.3399  1105 LEU B CD2 
20758 N N   . TRP C 1106 ? 2.3141 1.4758 2.2121 -0.3719 -0.6854 0.3636  1106 TRP B N   
20759 C CA  . TRP C 1106 ? 2.3479 1.5087 2.2244 -0.3617 -0.7443 0.3755  1106 TRP B CA  
20760 C C   . TRP C 1106 ? 2.2881 1.5159 2.2154 -0.4006 -0.7898 0.3755  1106 TRP B C   
20761 O O   . TRP C 1106 ? 2.2908 1.5741 2.2488 -0.4108 -0.8255 0.3846  1106 TRP B O   
20762 C CB  . TRP C 1106 ? 2.3938 1.4754 2.1976 -0.3333 -0.7541 0.3770  1106 TRP B CB  
20763 C CG  . TRP C 1106 ? 2.4033 1.4827 2.1825 -0.3257 -0.8140 0.3898  1106 TRP B CG  
20764 C CD1 . TRP C 1106 ? 2.4169 1.5091 2.1879 -0.3105 -0.8404 0.4060  1106 TRP B CD1 
20765 C CD2 . TRP C 1106 ? 2.4096 1.4738 2.1693 -0.3340 -0.8560 0.3886  1106 TRP B CD2 
20766 N NE1 . TRP C 1106 ? 2.4315 1.5172 2.1758 -0.3101 -0.8966 0.4161  1106 TRP B NE1 
20767 C CE2 . TRP C 1106 ? 2.4359 1.5035 2.1729 -0.3242 -0.9074 0.4047  1106 TRP B CE2 
20768 C CE3 . TRP C 1106 ? 2.4139 1.4617 2.1736 -0.3490 -0.8551 0.3761  1106 TRP B CE3 
20769 C CZ2 . TRP C 1106 ? 2.4820 1.5349 2.1939 -0.3292 -0.9578 0.4077  1106 TRP B CZ2 
20770 C CZ3 . TRP C 1106 ? 2.4339 1.4677 2.1726 -0.3526 -0.9048 0.3781  1106 TRP B CZ3 
20771 C CH2 . TRP C 1106 ? 2.4686 1.5041 2.1827 -0.3430 -0.9556 0.3933  1106 TRP B CH2 
20772 N N   . LEU C 1107 ? 2.3727 1.5985 2.3113 -0.4233 -0.7884 0.3659  1107 LEU B N   
20773 C CA  . LEU C 1107 ? 2.3397 1.6236 2.3243 -0.4607 -0.8361 0.3668  1107 LEU B CA  
20774 C C   . LEU C 1107 ? 2.3833 1.7558 2.4376 -0.4918 -0.8410 0.3685  1107 LEU B C   
20775 O O   . LEU C 1107 ? 2.3983 1.8193 2.4728 -0.5020 -0.8909 0.3781  1107 LEU B O   
20776 C CB  . LEU C 1107 ? 2.2429 1.5193 2.2430 -0.4846 -0.8213 0.3560  1107 LEU B CB  
20777 C CG  . LEU C 1107 ? 2.2209 1.4129 2.1586 -0.4577 -0.8036 0.3501  1107 LEU B CG  
20778 C CD1 . LEU C 1107 ? 2.2141 1.3767 2.1421 -0.4502 -0.7350 0.3418  1107 LEU B CD1 
20779 C CD2 . LEU C 1107 ? 2.1706 1.3640 2.1209 -0.4794 -0.8342 0.3460  1107 LEU B CD2 
20780 N N   . VAL C 1108 ? 2.1929 1.5853 2.2810 -0.5067 -0.7878 0.3593  1108 VAL B N   
20781 C CA  . VAL C 1108 ? 2.1822 1.6578 2.3386 -0.5386 -0.7807 0.3574  1108 VAL B CA  
20782 C C   . VAL C 1108 ? 2.2557 1.7639 2.4171 -0.5239 -0.8081 0.3674  1108 VAL B C   
20783 O O   . VAL C 1108 ? 2.2547 1.8352 2.4604 -0.5510 -0.8507 0.3722  1108 VAL B O   
20784 C CB  . VAL C 1108 ? 2.1654 1.6333 2.3343 -0.5409 -0.7108 0.3473  1108 VAL B CB  
20785 C CG1 . VAL C 1108 ? 2.2203 1.6024 2.3212 -0.4924 -0.6758 0.3480  1108 VAL B CG1 
20786 C CG2 . VAL C 1108 ? 2.1642 1.7051 2.3895 -0.5600 -0.7003 0.3455  1108 VAL B CG2 
20787 N N   . GLU C 1109 ? 2.6062 2.0637 2.7234 -0.4821 -0.7847 0.3717  1109 GLU B N   
20788 C CA  . GLU C 1109 ? 2.6709 2.1614 2.7979 -0.4682 -0.8031 0.3819  1109 GLU B CA  
20789 C C   . GLU C 1109 ? 2.7006 2.2058 2.8107 -0.4644 -0.8729 0.3977  1109 GLU B C   
20790 O O   . GLU C 1109 ? 2.7221 2.2842 2.8596 -0.4696 -0.9013 0.4068  1109 GLU B O   
20791 C CB  . GLU C 1109 ? 2.7338 2.1653 2.8203 -0.4251 -0.7607 0.3843  1109 GLU B CB  
20792 C CG  . GLU C 1109 ? 2.7267 2.1399 2.8246 -0.4289 -0.6930 0.3696  1109 GLU B CG  
20793 C CD  . GLU C 1109 ? 2.7695 2.1463 2.8463 -0.3930 -0.6534 0.3719  1109 GLU B CD  
20794 O OE1 . GLU C 1109 ? 2.7655 2.1028 2.8290 -0.3855 -0.5996 0.3626  1109 GLU B OE1 
20795 O OE2 . GLU C 1109 ? 2.8058 2.1943 2.8799 -0.3729 -0.6772 0.3842  1109 GLU B OE2 
20796 N N   . ASN C 1110 ? 2.6839 2.1402 2.7496 -0.4570 -0.9010 0.4008  1110 ASN B N   
20797 C CA  . ASN C 1110 ? 2.7092 2.1637 2.7447 -0.4481 -0.9644 0.4171  1110 ASN B CA  
20798 C C   . ASN C 1110 ? 2.6547 2.1444 2.7117 -0.4824 -1.0166 0.4169  1110 ASN B C   
20799 O O   . ASN C 1110 ? 2.6658 2.2003 2.7328 -0.4941 -1.0727 0.4295  1110 ASN B O   
20800 C CB  . ASN C 1110 ? 2.7776 2.1390 2.7322 -0.4051 -0.9611 0.4243  1110 ASN B CB  
20801 C CG  . ASN C 1110 ? 2.8373 2.1643 2.7684 -0.3696 -0.9188 0.4290  1110 ASN B CG  
20802 O OD1 . ASN C 1110 ? 2.8594 2.1254 2.7589 -0.3491 -0.8724 0.4208  1110 ASN B OD1 
20803 N ND2 . ASN C 1110 ? 2.8722 2.2388 2.8186 -0.3623 -0.9363 0.4430  1110 ASN B ND2 
20804 N N   . TYR C 1111 ? 2.8894 2.3591 2.9534 -0.4988 -0.9994 0.4038  1111 TYR B N   
20805 C CA  . TYR C 1111 ? 2.8562 2.3431 2.9321 -0.5256 -1.0494 0.4043  1111 TYR B CA  
20806 C C   . TYR C 1111 ? 2.8033 2.3625 2.9552 -0.5761 -1.0492 0.3951  1111 TYR B C   
20807 O O   . TYR C 1111 ? 2.7586 2.3119 2.9191 -0.5958 -1.0684 0.3909  1111 TYR B O   
20808 C CB  . TYR C 1111 ? 2.8639 2.2637 2.8793 -0.5024 -1.0455 0.3998  1111 TYR B CB  
20809 C CG  . TYR C 1111 ? 2.9316 2.2703 2.8745 -0.4608 -1.0616 0.4116  1111 TYR B CG  
20810 C CD1 . TYR C 1111 ? 2.9656 2.2970 2.8785 -0.4588 -1.1237 0.4237  1111 TYR B CD1 
20811 C CD2 . TYR C 1111 ? 2.9649 2.2552 2.8700 -0.4256 -1.0162 0.4123  1111 TYR B CD2 
20812 C CE1 . TYR C 1111 ? 3.0372 2.3137 2.8823 -0.4236 -1.1384 0.4365  1111 TYR B CE1 
20813 C CE2 . TYR C 1111 ? 3.0349 2.2721 2.8758 -0.3905 -1.0314 0.4251  1111 TYR B CE2 
20814 C CZ  . TYR C 1111 ? 3.0742 2.3046 2.8845 -0.3901 -1.0918 0.4375  1111 TYR B CZ  
20815 O OH  . TYR C 1111 ? 3.1497 2.3278 2.8948 -0.3580 -1.1062 0.4520  1111 TYR B OH  
20816 N N   . GLN C 1112 ? 2.4733 2.1016 2.6815 -0.5983 -1.0284 0.3923  1112 GLN B N   
20817 C CA  . GLN C 1112 ? 2.4303 2.1337 2.7128 -0.6486 -1.0247 0.3864  1112 GLN B CA  
20818 C C   . GLN C 1112 ? 2.5224 2.2898 2.8316 -0.6563 -1.0407 0.4090  1112 GLN B C   
20819 O O   . GLN C 1112 ? 2.5412 2.3543 2.8779 -0.6593 -1.0244 0.4056  1112 GLN B O   
20820 C CB  . GLN C 1112 ? 2.3699 2.0769 2.6804 -0.6586 -0.9548 0.3718  1112 GLN B CB  
20821 C CG  . GLN C 1112 ? 2.3128 2.0857 2.6742 -0.6865 -0.9279 0.3801  1112 GLN B CG  
20822 C CD  . GLN C 1112 ? 2.2544 2.0322 2.6404 -0.6985 -0.8623 0.3640  1112 GLN B CD  
20823 O OE1 . GLN C 1112 ? 2.2617 2.0207 2.6446 -0.6892 -0.8363 0.3514  1112 GLN B OE1 
20824 N NE2 . GLN C 1112 ? 2.2105 2.0064 2.6107 -0.7113 -0.8296 0.3692  1112 GLN B NE2 
20825 N N   . LEU C 1113 ? 2.7005 2.4675 3.0030 -0.6623 -1.0698 0.4309  1113 LEU B N   
20826 C CA  . LEU C 1113 ? 2.7737 2.5877 3.0927 -0.6726 -1.0886 0.4535  1113 LEU B CA  
20827 C C   . LEU C 1113 ? 2.7951 2.6809 3.1629 -0.6918 -1.0505 0.4530  1113 LEU B C   
20828 O O   . LEU C 1113 ? 2.7460 2.6448 3.1372 -0.6997 -1.0061 0.4374  1113 LEU B O   
20829 C CB  . LEU C 1113 ? 2.7789 2.5757 3.0891 -0.6839 -1.1158 0.4751  1113 LEU B CB  
20830 C CG  . LEU C 1113 ? 2.7630 2.4905 3.0230 -0.6657 -1.1582 0.4770  1113 LEU B CG  
20831 C CD1 . LEU C 1113 ? 2.7680 2.4691 3.0249 -0.6777 -1.1768 0.4915  1113 LEU B CD1 
20832 C CD2 . LEU C 1113 ? 2.8142 2.5406 3.0479 -0.6534 -1.1932 0.4883  1113 LEU B CD2 
20833 N N   . ASP C 1114 ? 3.9553 3.8856 4.3354 -0.6999 -1.0667 0.4698  1114 ASP B N   
20834 C CA  . ASP C 1114 ? 3.9981 3.9999 4.4201 -0.7183 -1.0354 0.4702  1114 ASP B CA  
20835 C C   . ASP C 1114 ? 3.9741 4.0008 4.4143 -0.7423 -1.0161 0.4815  1114 ASP B C   
20836 O O   . ASP C 1114 ? 4.0215 4.1006 4.4804 -0.7606 -1.0141 0.4952  1114 ASP B O   
20837 C CB  . ASP C 1114 ? 4.1156 4.1563 4.5408 -0.7191 -1.0611 0.4844  1114 ASP B CB  
20838 C CG  . ASP C 1114 ? 4.1699 4.2291 4.6040 -0.7020 -1.0546 0.4688  1114 ASP B CG  
20839 O OD1 . ASP C 1114 ? 4.1368 4.2066 4.5943 -0.7014 -1.0161 0.4466  1114 ASP B OD1 
20840 O OD2 . ASP C 1114 ? 4.2383 4.3008 4.6563 -0.6895 -1.0873 0.4796  1114 ASP B OD2 
20841 N N   . ASN C 1115 ? 1.8775 1.8671 2.3098 -0.7418 -1.0028 0.4762  1115 ASN B N   
20842 C CA  . ASN C 1115 ? 1.8365 1.8470 2.2832 -0.7614 -0.9849 0.4875  1115 ASN B CA  
20843 C C   . ASN C 1115 ? 1.6991 1.6717 2.1402 -0.7552 -0.9582 0.4728  1115 ASN B C   
20844 O O   . ASN C 1115 ? 1.6650 1.6364 2.1095 -0.7651 -0.9505 0.4821  1115 ASN B O   
20845 C CB  . ASN C 1115 ? 1.9068 1.9128 2.3437 -0.7728 -1.0249 0.5160  1115 ASN B CB  
20846 C CG  . ASN C 1115 ? 1.9060 1.8418 2.3135 -0.7605 -1.0583 0.5205  1115 ASN B CG  
20847 O OD1 . ASN C 1115 ? 1.9430 1.8655 2.3417 -0.7689 -1.0919 0.5419  1115 ASN B OD1 
20848 N ND2 . ASN C 1115 ? 1.8643 1.7545 2.2563 -0.7421 -1.0489 0.4999  1115 ASN B ND2 
20849 N N   . GLY C 1116 ? 2.0282 1.9701 2.4603 -0.7391 -0.9441 0.4499  1116 GLY B N   
20850 C CA  . GLY C 1116 ? 1.9346 1.8371 2.3588 -0.7337 -0.9139 0.4330  1116 GLY B CA  
20851 C C   . GLY C 1116 ? 1.8627 1.6980 2.2540 -0.7203 -0.9442 0.4332  1116 GLY B C   
20852 O O   . GLY C 1116 ? 1.8241 1.6169 2.2021 -0.7132 -0.9223 0.4162  1116 GLY B O   
20853 N N   . SER C 1117 ? 2.5130 2.3345 2.8892 -0.7180 -0.9923 0.4518  1117 SER B N   
20854 C CA  . SER C 1117 ? 2.4958 2.2525 2.8397 -0.7056 -1.0231 0.4512  1117 SER B CA  
20855 C C   . SER C 1117 ? 2.5117 2.2165 2.8173 -0.6831 -1.0436 0.4334  1117 SER B C   
20856 O O   . SER C 1117 ? 2.5452 2.2672 2.8502 -0.6766 -1.0431 0.4270  1117 SER B O   
20857 C CB  . SER C 1117 ? 2.5322 2.2858 2.8723 -0.7128 -1.0652 0.4770  1117 SER B CB  
20858 O OG  . SER C 1117 ? 2.5767 2.3188 2.8949 -0.7045 -1.1045 0.4843  1117 SER B OG  
20859 N N   . PHE C 1118 ? 2.1914 1.8341 2.4633 -0.6707 -1.0626 0.4253  1118 PHE B N   
20860 C CA  . PHE C 1118 ? 2.1679 1.7560 2.3951 -0.6491 -1.0762 0.4045  1118 PHE B CA  
20861 C C   . PHE C 1118 ? 2.1981 1.7397 2.3765 -0.6307 -1.1328 0.4121  1118 PHE B C   
20862 O O   . PHE C 1118 ? 2.2123 1.7163 2.3765 -0.6299 -1.1490 0.4137  1118 PHE B O   
20863 C CB  . PHE C 1118 ? 2.1289 1.6732 2.3483 -0.6497 -1.0380 0.3807  1118 PHE B CB  
20864 C CG  . PHE C 1118 ? 2.1117 1.6708 2.3540 -0.6588 -0.9821 0.3655  1118 PHE B CG  
20865 C CD1 . PHE C 1118 ? 2.0992 1.7289 2.3853 -0.6725 -0.9585 0.3759  1118 PHE B CD1 
20866 C CD2 . PHE C 1118 ? 2.1519 1.6342 2.3425 -0.6252 -0.9306 0.3571  1118 PHE B CD2 
20867 C CE1 . PHE C 1118 ? 2.0759 1.7154 2.3818 -0.6803 -0.9051 0.3622  1118 PHE B CE1 
20868 C CE2 . PHE C 1118 ? 2.1415 1.6251 2.3395 -0.6212 -0.8690 0.3516  1118 PHE B CE2 
20869 C CZ  . PHE C 1118 ? 2.0948 1.6577 2.3555 -0.6541 -0.8592 0.3513  1118 PHE B CZ  
20870 N N   . LYS C 1119 ? 2.4343 1.9779 2.5857 -0.6148 -1.1612 0.4178  1119 LYS B N   
20871 C CA  . LYS C 1119 ? 2.4808 1.9791 2.5798 -0.5963 -1.2110 0.4286  1119 LYS B CA  
20872 C C   . LYS C 1119 ? 2.4656 1.9003 2.5018 -0.5679 -1.2230 0.4101  1119 LYS B C   
20873 O O   . LYS C 1119 ? 2.4749 1.8742 2.4822 -0.5398 -1.1754 0.4056  1119 LYS B O   
20874 C CB  . LYS C 1119 ? 2.6485 2.1717 2.7375 -0.5890 -1.2345 0.4468  1119 LYS B CB  
20875 C CG  . LYS C 1119 ? 2.7439 2.2849 2.8187 -0.5675 -1.2239 0.4391  1119 LYS B CG  
20876 C CD  . LYS C 1119 ? 3.1731 2.7012 3.2027 -0.5447 -1.2595 0.4584  1119 LYS B CD  
20877 C CE  . LYS C 1119 ? 3.1923 2.7779 3.2620 -0.5643 -1.2637 0.4768  1119 LYS B CE  
20878 N NZ  . LYS C 1119 ? 3.1679 2.8025 3.2572 -0.5542 -1.2456 0.4749  1119 LYS B NZ  
20879 N N   . GLU C 1120 ? 2.8689 2.2517 2.8713 -0.5614 -1.2505 0.4113  1120 GLU B N   
20880 C CA  . GLU C 1120 ? 2.9404 2.2368 2.8679 -0.5239 -1.2424 0.4032  1120 GLU B CA  
20881 C C   . GLU C 1120 ? 3.0474 2.3163 2.9138 -0.4953 -1.2736 0.4191  1120 GLU B C   
20882 O O   . GLU C 1120 ? 3.0846 2.3772 2.9525 -0.5077 -1.3253 0.4336  1120 GLU B O   
20883 C CB  . GLU C 1120 ? 2.9542 2.2104 2.8706 -0.5296 -1.2632 0.3939  1120 GLU B CB  
20884 C CG  . GLU C 1120 ? 3.0368 2.1962 2.8681 -0.4887 -1.2574 0.3901  1120 GLU B CG  
20885 C CD  . GLU C 1120 ? 3.0350 2.1389 2.8324 -0.4585 -1.1867 0.3795  1120 GLU B CD  
20886 O OE1 . GLU C 1120 ? 3.0191 2.0767 2.8033 -0.4518 -1.1596 0.3650  1120 GLU B OE1 
20887 O OE2 . GLU C 1120 ? 3.0466 2.1533 2.8305 -0.4414 -1.1595 0.3861  1120 GLU B OE2 
20888 N N   . ASN C 1121 ? 2.9363 2.1457 2.7490 -0.4576 -1.2321 0.4188  1121 ASN B N   
20889 C CA  . ASN C 1121 ? 3.0127 2.1960 2.7689 -0.4298 -1.2522 0.4361  1121 ASN B CA  
20890 C C   . ASN C 1121 ? 3.1127 2.2401 2.8051 -0.4168 -1.2977 0.4421  1121 ASN B C   
20891 O O   . ASN C 1121 ? 3.1350 2.2870 2.8174 -0.4255 -1.3557 0.4587  1121 ASN B O   
20892 C CB  . ASN C 1121 ? 3.0089 2.1432 2.7293 -0.3955 -1.1926 0.4337  1121 ASN B CB  
20893 C CG  . ASN C 1121 ? 3.0238 2.1381 2.6941 -0.3696 -1.2101 0.4540  1121 ASN B CG  
20894 O OD1 . ASN C 1121 ? 3.0200 2.1884 2.7095 -0.3802 -1.2472 0.4709  1121 ASN B OD1 
20895 N ND2 . ASN C 1121 ? 3.0334 2.0722 2.6396 -0.3368 -1.1846 0.4537  1121 ASN B ND2 
20896 N N   . SER C 1122 ? 3.1317 2.1835 2.7789 -0.3959 -1.2698 0.4285  1122 SER B N   
20897 C CA  . SER C 1122 ? 3.2194 2.2086 2.8026 -0.3819 -1.3034 0.4295  1122 SER B CA  
20898 C C   . SER C 1122 ? 3.2437 2.2620 2.8511 -0.4106 -1.3644 0.4305  1122 SER B C   
20899 O O   . SER C 1122 ? 3.2007 2.2883 2.8772 -0.4428 -1.3790 0.4295  1122 SER B O   
20900 C CB  . SER C 1122 ? 3.1989 2.1146 2.7468 -0.3613 -1.2574 0.4092  1122 SER B CB  
20901 O OG  . SER C 1122 ? 3.1182 2.0565 2.7216 -0.3824 -1.2357 0.3919  1122 SER B OG  
20902 N N   . GLN C 1123 ? 3.6342 2.5992 3.1844 -0.4003 -1.4005 0.4324  1123 GLN B N   
20903 C CA  . GLN C 1123 ? 3.6645 2.6439 3.2347 -0.4260 -1.4538 0.4315  1123 GLN B CA  
20904 C C   . GLN C 1123 ? 3.5486 2.5084 3.1435 -0.4332 -1.4366 0.4083  1123 GLN B C   
20905 O O   . GLN C 1123 ? 3.5550 2.5141 3.1737 -0.4539 -1.4674 0.4045  1123 GLN B O   
20906 C CB  . GLN C 1123 ? 3.8709 2.7909 3.3739 -0.4154 -1.4886 0.4410  1123 GLN B CB  
20907 C CG  . GLN C 1123 ? 4.0309 2.9578 3.5061 -0.4077 -1.4935 0.4631  1123 GLN B CG  
20908 C CD  . GLN C 1123 ? 4.2300 3.1150 3.6613 -0.4137 -1.5314 0.4738  1123 GLN B CD  
20909 O OE1 . GLN C 1123 ? 4.2875 3.1639 3.7394 -0.4369 -1.5571 0.4706  1123 GLN B OE1 
20910 N NE2 . GLN C 1123 ? 4.3372 3.1949 3.7077 -0.3935 -1.5343 0.4889  1123 GLN B NE2 
20911 N N   . TYR C 1124 ? 2.7180 1.6494 2.3137 -0.4175 -1.3713 0.3931  1124 TYR B N   
20912 C CA  . TYR C 1124 ? 2.6057 1.5047 2.2148 -0.4194 -1.3467 0.3715  1124 TYR B CA  
20913 C C   . TYR C 1124 ? 2.5148 1.4733 2.2036 -0.4588 -1.3715 0.3675  1124 TYR B C   
20914 O O   . TYR C 1124 ? 2.4302 1.4592 2.1848 -0.4843 -1.3610 0.3718  1124 TYR B O   
20915 C CB  . TYR C 1124 ? 2.5243 1.3944 2.1259 -0.3995 -1.2720 0.3590  1124 TYR B CB  
20916 C CG  . TYR C 1124 ? 2.4602 1.2787 2.0518 -0.3912 -1.2425 0.3377  1124 TYR B CG  
20917 C CD1 . TYR C 1124 ? 2.4992 1.2449 2.0263 -0.3690 -1.2554 0.3287  1124 TYR B CD1 
20918 C CD2 . TYR C 1124 ? 2.3734 1.2163 2.0188 -0.4061 -1.2002 0.3269  1124 TYR B CD2 
20919 C CE1 . TYR C 1124 ? 2.4715 1.1714 1.9901 -0.3603 -1.2272 0.3082  1124 TYR B CE1 
20920 C CE2 . TYR C 1124 ? 2.3414 1.1390 1.9780 -0.3981 -1.1721 0.3089  1124 TYR B CE2 
20921 C CZ  . TYR C 1124 ? 2.3645 1.0911 1.9383 -0.3743 -1.1855 0.2989  1124 TYR B CZ  
20922 O OH  . TYR C 1124 ? 2.3015 0.9855 1.8680 -0.3656 -1.1567 0.2803  1124 TYR B OH  
20923 N N   . GLN C 1125 ? 2.9083 1.8377 2.5903 -0.4644 -1.4062 0.3595  1125 GLN B N   
20924 C CA  . GLN C 1125 ? 2.8418 1.8130 2.5953 -0.4990 -1.4268 0.3536  1125 GLN B CA  
20925 C C   . GLN C 1125 ? 2.7501 1.6717 2.5021 -0.4864 -1.3762 0.3328  1125 GLN B C   
20926 O O   . GLN C 1125 ? 2.7481 1.5998 2.4479 -0.4635 -1.3790 0.3215  1125 GLN B O   
20927 C CB  . GLN C 1125 ? 3.0056 1.9460 2.7521 -0.5054 -1.4732 0.3650  1125 GLN B CB  
20928 C CG  . GLN C 1125 ? 3.1650 2.1001 2.8851 -0.5059 -1.5035 0.3894  1125 GLN B CG  
20929 C CD  . GLN C 1125 ? 3.2196 2.2172 3.0055 -0.5340 -1.4950 0.4141  1125 GLN B CD  
20930 O OE1 . GLN C 1125 ? 3.1714 2.2217 3.0039 -0.5438 -1.4598 0.4146  1125 GLN B OE1 
20931 N NE2 . GLN C 1125 ? 3.3040 2.2951 3.0899 -0.5476 -1.5269 0.4347  1125 GLN B NE2 
20932 N N   . PRO C 1126 ? 2.2956 1.2531 2.1027 -0.5014 -1.3289 0.3278  1126 PRO B N   
20933 C CA  . PRO C 1126 ? 2.2944 1.2062 2.0977 -0.4892 -1.2791 0.3101  1126 PRO B CA  
20934 C C   . PRO C 1126 ? 2.3145 1.2380 2.1682 -0.5146 -1.3082 0.3040  1126 PRO B C   
20935 O O   . PRO C 1126 ? 2.3794 1.2423 2.2022 -0.4966 -1.3054 0.2901  1126 PRO B O   
20936 C CB  . PRO C 1126 ? 2.2030 1.1556 2.0473 -0.4998 -1.2204 0.3112  1126 PRO B CB  
20937 C CG  . PRO C 1126 ? 2.1961 1.2099 2.0600 -0.5131 -1.2385 0.3276  1126 PRO B CG  
20938 C CD  . PRO C 1126 ? 2.2349 1.2721 2.1035 -0.5282 -1.3142 0.3381  1126 PRO B CD  
20939 N N   . ILE C 1127 ? 2.3265 1.3294 2.2590 -0.5571 -1.3375 0.3144  1127 ILE B N   
20940 C CA  . ILE C 1127 ? 2.3455 1.3566 2.3288 -0.5692 -1.3464 0.3259  1127 ILE B CA  
20941 C C   . ILE C 1127 ? 2.4030 1.4299 2.4036 -0.5755 -1.3905 0.3572  1127 ILE B C   
20942 O O   . ILE C 1127 ? 2.3928 1.4532 2.3993 -0.5821 -1.3959 0.3790  1127 ILE B O   
20943 C CB  . ILE C 1127 ? 2.3527 1.4213 2.4071 -0.5889 -1.2993 0.3382  1127 ILE B CB  
20944 C CG1 . ILE C 1127 ? 2.3113 1.4313 2.3786 -0.5965 -1.2687 0.3486  1127 ILE B CG1 
20945 C CG2 . ILE C 1127 ? 2.3313 1.3645 2.3869 -0.5878 -1.2598 0.3116  1127 ILE B CG2 
20946 C CD1 . ILE C 1127 ? 2.3504 1.5022 2.4181 -0.5996 -1.2993 0.3752  1127 ILE B CD1 
20947 N N   . LYS C 1128 ? 2.4644 1.4640 2.4756 -0.5762 -1.4191 0.3590  1128 LYS B N   
20948 C CA  . LYS C 1128 ? 2.5456 1.5518 2.5759 -0.5870 -1.4581 0.3883  1128 LYS B CA  
20949 C C   . LYS C 1128 ? 2.5725 1.6405 2.6796 -0.6109 -1.4397 0.4167  1128 LYS B C   
20950 O O   . LYS C 1128 ? 2.5655 1.6396 2.7117 -0.6157 -1.4309 0.4159  1128 LYS B O   
20951 C CB  . LYS C 1128 ? 2.5873 1.5333 2.5925 -0.5774 -1.5011 0.3783  1128 LYS B CB  
20952 C CG  . LYS C 1128 ? 2.6317 1.5795 2.6619 -0.5927 -1.5406 0.4083  1128 LYS B CG  
20953 C CD  . LYS C 1128 ? 2.6752 1.6143 2.6661 -0.5947 -1.5666 0.4242  1128 LYS B CD  
20954 C CE  . LYS C 1128 ? 2.6404 1.6426 2.6786 -0.6193 -1.5533 0.4571  1128 LYS B CE  
20955 N NZ  . LYS C 1128 ? 2.7071 1.6987 2.7285 -0.6314 -1.5901 0.4801  1128 LYS B NZ  
20956 N N   . LEU C 1129 ? 2.9314 2.0459 3.0584 -0.6258 -1.4340 0.4423  1129 LEU B N   
20957 C CA  . LEU C 1129 ? 2.9615 2.1346 3.1531 -0.6494 -1.4197 0.4717  1129 LEU B CA  
20958 C C   . LEU C 1129 ? 3.0981 2.2607 3.3060 -0.6635 -1.4629 0.4976  1129 LEU B C   
20959 O O   . LEU C 1129 ? 3.1936 2.3242 3.3657 -0.6621 -1.4984 0.5021  1129 LEU B O   
20960 C CB  . LEU C 1129 ? 2.8845 2.1173 3.0916 -0.6608 -1.3877 0.4850  1129 LEU B CB  
20961 C CG  . LEU C 1129 ? 2.7844 2.0424 2.9935 -0.6540 -1.3375 0.4657  1129 LEU B CG  
20962 C CD1 . LEU C 1129 ? 2.7434 2.0718 2.9867 -0.6710 -1.3052 0.4847  1129 LEU B CD1 
20963 C CD2 . LEU C 1129 ? 2.7380 1.9906 2.9699 -0.6512 -1.3142 0.4520  1129 LEU B CD2 
20964 N N   . GLN C 1130 ? 2.6136 1.8026 2.8738 -0.6780 -1.4599 0.5154  1130 GLN B N   
20965 C CA  . GLN C 1130 ? 2.6800 1.8625 2.9596 -0.6946 -1.4992 0.5425  1130 GLN B CA  
20966 C C   . GLN C 1130 ? 2.6238 1.8531 2.9164 -0.7168 -1.4969 0.5722  1130 GLN B C   
20967 O O   . GLN C 1130 ? 2.5437 1.8206 2.8433 -0.7208 -1.4606 0.5739  1130 GLN B O   
20968 C CB  . GLN C 1130 ? 2.7579 1.9555 3.0898 -0.7031 -1.4972 0.5535  1130 GLN B CB  
20969 C CG  . GLN C 1130 ? 2.7900 1.9552 3.1204 -0.6839 -1.4901 0.5246  1130 GLN B CG  
20970 C CD  . GLN C 1130 ? 2.8501 2.0231 3.2323 -0.6926 -1.4999 0.5380  1130 GLN B CD  
20971 O OE1 . GLN C 1130 ? 2.9315 2.0896 3.3274 -0.7038 -1.5391 0.5584  1130 GLN B OE1 
20972 N NE2 . GLN C 1130 ? 2.8004 1.9966 3.2119 -0.6884 -1.4641 0.5272  1130 GLN B NE2 
20973 N N   . GLY C 1131 ? 3.0306 2.2467 3.3261 -0.7323 -1.5359 0.5952  1131 GLY B N   
20974 C CA  . GLY C 1131 ? 3.0681 2.3308 3.3781 -0.7564 -1.5345 0.6246  1131 GLY B CA  
20975 C C   . GLY C 1131 ? 3.1734 2.4108 3.4424 -0.7597 -1.5657 0.6298  1131 GLY B C   
20976 O O   . GLY C 1131 ? 3.2231 2.4112 3.4450 -0.7406 -1.5817 0.6081  1131 GLY B O   
20977 N N   . THR C 1132 ? 3.5419 2.8154 3.8272 -0.7851 -1.5740 0.6596  1132 THR B N   
20978 C CA  . THR C 1132 ? 3.5949 2.8538 3.8470 -0.7937 -1.6027 0.6699  1132 THR B CA  
20979 C C   . THR C 1132 ? 3.5402 2.8001 3.7553 -0.7762 -1.5839 0.6490  1132 THR B C   
20980 O O   . THR C 1132 ? 3.4462 2.7319 3.6691 -0.7635 -1.5447 0.6323  1132 THR B O   
20981 C CB  . THR C 1132 ? 3.6558 2.9706 3.9355 -0.8248 -1.6021 0.7040  1132 THR B CB  
20982 O OG1 . THR C 1132 ? 3.6402 2.9879 3.9673 -0.8386 -1.5896 0.7204  1132 THR B OG1 
20983 C CG2 . THR C 1132 ? 3.7710 3.0548 4.0291 -0.8409 -1.6497 0.7231  1132 THR B CG2 
20984 N N   . LEU C 1133 ? 3.1561 2.3877 3.3302 -0.7761 -1.6125 0.6510  1133 LEU B N   
20985 C CA  . LEU C 1133 ? 3.1721 2.4086 3.3112 -0.7618 -1.5984 0.6363  1133 LEU B CA  
20986 C C   . LEU C 1133 ? 3.1719 2.4825 3.3402 -0.7704 -1.5570 0.6430  1133 LEU B C   
20987 O O   . LEU C 1133 ? 3.1544 2.4758 3.3101 -0.7527 -1.5296 0.6234  1133 LEU B O   
20988 C CB  . LEU C 1133 ? 3.2367 2.4395 3.3313 -0.7657 -1.6371 0.6444  1133 LEU B CB  
20989 C CG  . LEU C 1133 ? 3.2393 2.3630 3.2904 -0.7487 -1.6722 0.6280  1133 LEU B CG  
20990 C CD1 . LEU C 1133 ? 3.2697 2.3698 3.3471 -0.7607 -1.6975 0.6389  1133 LEU B CD1 
20991 C CD2 . LEU C 1133 ? 3.3005 2.3892 3.2963 -0.7473 -1.7042 0.6311  1133 LEU B CD2 
20992 N N   . PRO C 1134 ? 3.2726 2.6341 3.4779 -0.7975 -1.5532 0.6706  1134 PRO B N   
20993 C CA  . PRO C 1134 ? 3.2418 2.6759 3.4770 -0.8061 -1.5120 0.6758  1134 PRO B CA  
20994 C C   . PRO C 1134 ? 3.1924 2.6429 3.4549 -0.7961 -1.4750 0.6614  1134 PRO B C   
20995 O O   . PRO C 1134 ? 3.1192 2.5955 3.3833 -0.7837 -1.4392 0.6442  1134 PRO B O   
20996 C CB  . PRO C 1134 ? 3.2901 2.7647 3.5551 -0.8381 -1.5226 0.7092  1134 PRO B CB  
20997 C CG  . PRO C 1134 ? 3.3787 2.8035 3.6225 -0.8468 -1.5716 0.7223  1134 PRO B CG  
20998 C CD  . PRO C 1134 ? 3.3582 2.7125 3.5757 -0.8220 -1.5879 0.6983  1134 PRO B CD  
20999 N N   . VAL C 1135 ? 2.6821 2.1180 2.9670 -0.8025 -1.4846 0.6694  1135 VAL B N   
21000 C CA  . VAL C 1135 ? 2.5909 2.0459 2.9053 -0.7964 -1.4508 0.6600  1135 VAL B CA  
21001 C C   . VAL C 1135 ? 2.5142 1.9446 2.8065 -0.7685 -1.4289 0.6266  1135 VAL B C   
21002 O O   . VAL C 1135 ? 2.4434 1.9124 2.7503 -0.7642 -1.3873 0.6164  1135 VAL B O   
21003 C CB  . VAL C 1135 ? 2.6047 2.0293 2.9377 -0.8000 -1.4726 0.6677  1135 VAL B CB  
21004 C CG1 . VAL C 1135 ? 2.5223 1.9445 2.8701 -0.7833 -1.4423 0.6470  1135 VAL B CG1 
21005 C CG2 . VAL C 1135 ? 2.6474 2.1136 3.0155 -0.8294 -1.4792 0.7017  1135 VAL B CG2 
21006 N N   . GLU C 1136 ? 3.2164 2.5814 3.4708 -0.7502 -1.4574 0.6095  1136 GLU B N   
21007 C CA  . GLU C 1136 ? 3.1523 2.4849 3.3795 -0.7232 -1.4418 0.5770  1136 GLU B CA  
21008 C C   . GLU C 1136 ? 3.1197 2.4819 3.3330 -0.7145 -1.4113 0.5646  1136 GLU B C   
21009 O O   . GLU C 1136 ? 3.0704 2.4335 3.2800 -0.6995 -1.3808 0.5424  1136 GLU B O   
21010 C CB  . GLU C 1136 ? 3.1784 2.4355 3.3576 -0.7065 -1.4829 0.5627  1136 GLU B CB  
21011 C CG  . GLU C 1136 ? 3.1334 2.3516 3.2731 -0.6782 -1.4716 0.5288  1136 GLU B CG  
21012 C CD  . GLU C 1136 ? 3.1756 2.3193 3.2618 -0.6618 -1.5134 0.5150  1136 GLU B CD  
21013 O OE1 . GLU C 1136 ? 3.2183 2.3405 3.2939 -0.6722 -1.5512 0.5315  1136 GLU B OE1 
21014 O OE2 . GLU C 1136 ? 3.1622 2.2686 3.2139 -0.6390 -1.5081 0.4873  1136 GLU B OE2 
21015 N N   . ALA C 1137 ? 2.7960 2.1826 3.0025 -0.7248 -1.4202 0.5791  1137 ALA B N   
21016 C CA  . ALA C 1137 ? 2.7765 2.1919 2.9713 -0.7165 -1.3963 0.5691  1137 ALA B CA  
21017 C C   . ALA C 1137 ? 2.7140 2.1907 2.9503 -0.7242 -1.3486 0.5683  1137 ALA B C   
21018 O O   . ALA C 1137 ? 2.6558 2.1392 2.8876 -0.7101 -1.3180 0.5473  1137 ALA B O   
21019 C CB  . ALA C 1137 ? 2.8481 2.2827 3.0333 -0.7289 -1.4171 0.5880  1137 ALA B CB  
21020 N N   . ARG C 1138 ? 2.9967 2.5171 3.2708 -0.7479 -1.3433 0.5920  1138 ARG B N   
21021 C CA  . ARG C 1138 ? 2.9503 2.5309 3.2625 -0.7586 -1.3000 0.5950  1138 ARG B CA  
21022 C C   . ARG C 1138 ? 2.8395 2.4038 3.1604 -0.7467 -1.2755 0.5771  1138 ARG B C   
21023 O O   . ARG C 1138 ? 2.7680 2.3649 3.1026 -0.7440 -1.2337 0.5648  1138 ARG B O   
21024 C CB  . ARG C 1138 ? 3.0578 2.6784 3.4004 -0.7863 -1.3079 0.6260  1138 ARG B CB  
21025 C CG  . ARG C 1138 ? 3.0717 2.7625 3.4477 -0.8010 -1.2660 0.6327  1138 ARG B CG  
21026 C CD  . ARG C 1138 ? 3.1809 2.9117 3.5779 -0.8298 -1.2789 0.6648  1138 ARG B CD  
21027 N NE  . ARG C 1138 ? 3.2106 3.0041 3.6367 -0.8444 -1.2404 0.6715  1138 ARG B NE  
21028 C CZ  . ARG C 1138 ? 3.2989 3.1402 3.7418 -0.8704 -1.2420 0.6967  1138 ARG B CZ  
21029 N NH1 . ARG C 1138 ? 3.3827 3.2168 3.8187 -0.8854 -1.2797 0.7183  1138 ARG B NH1 
21030 N NH2 . ARG C 1138 ? 3.2882 3.1846 3.7520 -0.8825 -1.2060 0.7000  1138 ARG B NH2 
21031 N N   . GLU C 1139 ? 3.0752 2.5886 3.3875 -0.7401 -1.3017 0.5748  1139 GLU B N   
21032 C CA  . GLU C 1139 ? 2.9681 2.4573 3.2831 -0.7266 -1.2839 0.5553  1139 GLU B CA  
21033 C C   . GLU C 1139 ? 2.9313 2.3911 3.2118 -0.7037 -1.2691 0.5242  1139 GLU B C   
21034 O O   . GLU C 1139 ? 2.8680 2.3484 3.1584 -0.6998 -1.2281 0.5093  1139 GLU B O   
21035 C CB  . GLU C 1139 ? 2.9693 2.4054 3.2783 -0.7228 -1.3220 0.5576  1139 GLU B CB  
21036 C CG  . GLU C 1139 ? 2.9534 2.4144 3.3037 -0.7422 -1.3275 0.5830  1139 GLU B CG  
21037 C CD  . GLU C 1139 ? 2.8841 2.3722 3.2650 -0.7420 -1.2888 0.5772  1139 GLU B CD  
21038 O OE1 . GLU C 1139 ? 2.8968 2.3548 3.2867 -0.7360 -1.2997 0.5723  1139 GLU B OE1 
21039 O OE2 . GLU C 1139 ? 2.8374 2.3773 3.2330 -0.7482 -1.2474 0.5771  1139 GLU B OE2 
21040 N N   . ASN C 1140 ? 3.2393 2.6492 3.4762 -0.6897 -1.3031 0.5150  1140 ASN B N   
21041 C CA  . ASN C 1140 ? 3.2152 2.5910 3.4101 -0.6672 -1.2961 0.4868  1140 ASN B CA  
21042 C C   . ASN C 1140 ? 3.1059 2.5285 3.3116 -0.6681 -1.2558 0.4800  1140 ASN B C   
21043 O O   . ASN C 1140 ? 3.0459 2.4574 3.2397 -0.6565 -1.2282 0.4565  1140 ASN B O   
21044 C CB  . ASN C 1140 ? 3.3533 2.6791 3.4967 -0.6542 -1.3403 0.4845  1140 ASN B CB  
21045 C CG  . ASN C 1140 ? 3.4289 2.7023 3.5181 -0.6277 -1.3427 0.4549  1140 ASN B CG  
21046 O OD1 . ASN C 1140 ? 3.5202 2.7619 3.5608 -0.6137 -1.3692 0.4518  1140 ASN B OD1 
21047 N ND2 . ASN C 1140 ? 3.4023 2.6662 3.4961 -0.6213 -1.3145 0.4340  1140 ASN B ND2 
21048 N N   . SER C 1141 ? 3.0739 2.5479 3.3024 -0.6833 -1.2517 0.4996  1141 SER B N   
21049 C CA  . SER C 1141 ? 3.0087 2.5325 3.2528 -0.6859 -1.2140 0.4939  1141 SER B CA  
21050 C C   . SER C 1141 ? 2.8899 2.4422 3.1643 -0.6916 -1.1659 0.4846  1141 SER B C   
21051 O O   . SER C 1141 ? 2.8267 2.3809 3.0954 -0.6835 -1.1339 0.4639  1141 SER B O   
21052 C CB  . SER C 1141 ? 3.0601 2.6393 3.3286 -0.7046 -1.2170 0.5179  1141 SER B CB  
21053 O OG  . SER C 1141 ? 3.0377 2.6749 3.3350 -0.7125 -1.1733 0.5140  1141 SER B OG  
21054 N N   . LEU C 1142 ? 2.4318 2.0061 2.7377 -0.7066 -1.1604 0.5010  1142 LEU B N   
21055 C CA  . LEU C 1142 ? 2.3244 1.9279 2.6575 -0.7129 -1.1153 0.4956  1142 LEU B CA  
21056 C C   . LEU C 1142 ? 2.2798 1.8339 2.5895 -0.6957 -1.1001 0.4673  1142 LEU B C   
21057 O O   . LEU C 1142 ? 2.2332 1.7969 2.5429 -0.6933 -1.0588 0.4500  1142 LEU B O   
21058 C CB  . LEU C 1142 ? 2.2941 1.9173 2.6573 -0.7284 -1.1215 0.5183  1142 LEU B CB  
21059 C CG  . LEU C 1142 ? 2.2078 1.8901 2.6051 -0.7436 -1.0768 0.5257  1142 LEU B CG  
21060 C CD1 . LEU C 1142 ? 2.2215 1.9182 2.6438 -0.7584 -1.0926 0.5509  1142 LEU B CD1 
21061 C CD2 . LEU C 1142 ? 2.1171 1.7892 2.5110 -0.7339 -1.0341 0.5014  1142 LEU B CD2 
21062 N N   . TYR C 1143 ? 2.3124 1.8100 2.5994 -0.6847 -1.1331 0.4616  1143 TYR B N   
21063 C CA  . TYR C 1143 ? 2.2643 1.7126 2.5290 -0.6711 -1.1188 0.4351  1143 TYR B CA  
21064 C C   . TYR C 1143 ? 2.2163 1.6486 2.4534 -0.6615 -1.0922 0.4109  1143 TYR B C   
21065 O O   . TYR C 1143 ? 2.1563 1.5875 2.3985 -0.6632 -1.0459 0.3964  1143 TYR B O   
21066 C CB  . TYR C 1143 ? 2.2835 1.6675 2.5162 -0.6579 -1.1648 0.4282  1143 TYR B CB  
21067 C CG  . TYR C 1143 ? 2.2555 1.5841 2.4616 -0.6451 -1.1498 0.3989  1143 TYR B CG  
21068 C CD1 . TYR C 1143 ? 2.2227 1.5470 2.4530 -0.6490 -1.1360 0.3983  1143 TYR B CD1 
21069 C CD2 . TYR C 1143 ? 2.2673 1.5445 2.4216 -0.6298 -1.1485 0.3718  1143 TYR B CD2 
21070 C CE1 . TYR C 1143 ? 2.2246 1.4923 2.4283 -0.6385 -1.1180 0.3708  1143 TYR B CE1 
21071 C CE2 . TYR C 1143 ? 2.2558 1.4696 2.3792 -0.6207 -1.1298 0.3437  1143 TYR B CE2 
21072 C CZ  . TYR C 1143 ? 2.2370 1.4447 2.3853 -0.6250 -1.1129 0.3433  1143 TYR B CZ  
21073 O OH  . TYR C 1143 ? 2.2376 1.3729 2.3524 -0.6157 -1.0882 0.3168  1143 TYR B OH  
21074 N N   . LEU C 1144 ? 3.2505 2.6689 3.4576 -0.6521 -1.1204 0.4084  1144 LEU B N   
21075 C CA  . LEU C 1144 ? 3.2453 2.6481 3.4257 -0.6432 -1.1001 0.3870  1144 LEU B CA  
21076 C C   . LEU C 1144 ? 3.2197 2.6761 3.4393 -0.6577 -1.0453 0.3886  1144 LEU B C   
21077 O O   . LEU C 1144 ? 3.1951 2.6292 3.4103 -0.6581 -1.0004 0.3707  1144 LEU B O   
21078 C CB  . LEU C 1144 ? 3.2584 2.6591 3.4087 -0.6317 -1.1397 0.3919  1144 LEU B CB  
21079 C CG  . LEU C 1144 ? 3.2297 2.5853 3.3254 -0.6116 -1.1473 0.3681  1144 LEU B CG  
21080 C CD1 . LEU C 1144 ? 3.2621 2.5337 3.2947 -0.5833 -1.1611 0.3588  1144 LEU B CD1 
21081 C CD2 . LEU C 1144 ? 3.2521 2.6303 3.3293 -0.6002 -1.1785 0.3816  1144 LEU B CD2 
21082 N N   . THR C 1145 ? 2.3042 1.8258 2.5591 -0.6705 -1.0455 0.4106  1145 THR B N   
21083 C CA  . THR C 1145 ? 2.2650 1.8409 2.5523 -0.6832 -0.9964 0.4109  1145 THR B CA  
21084 C C   . THR C 1145 ? 2.2296 1.8129 2.5356 -0.6912 -0.9502 0.4072  1145 THR B C   
21085 O O   . THR C 1145 ? 2.1996 1.8124 2.5216 -0.6987 -0.9018 0.4015  1145 THR B O   
21086 C CB  . THR C 1145 ? 2.3409 1.9845 2.6598 -0.6975 -1.0051 0.4350  1145 THR B CB  
21087 O OG1 . THR C 1145 ? 2.3714 2.0026 2.6712 -0.6908 -1.0546 0.4451  1145 THR B OG1 
21088 C CG2 . THR C 1145 ? 2.3296 2.0194 2.6690 -0.7048 -0.9621 0.4274  1145 THR B CG2 
21089 N N   . ALA C 1146 ? 1.7985 1.3552 2.1016 -0.6891 -0.9649 0.4107  1146 ALA B N   
21090 C CA  . ALA C 1146 ? 1.8198 1.3785 2.1360 -0.6938 -0.9242 0.4070  1146 ALA B CA  
21091 C C   . ALA C 1146 ? 1.8225 1.3158 2.1036 -0.6822 -0.8927 0.3802  1146 ALA B C   
21092 O O   . ALA C 1146 ? 1.7791 1.2782 2.0634 -0.6859 -0.8382 0.3731  1146 ALA B O   
21093 C CB  . ALA C 1146 ? 1.8400 1.3915 2.1674 -0.6951 -0.9531 0.4204  1146 ALA B CB  
21094 N N   . PHE C 1147 ? 2.5710 1.9963 2.8127 -0.6680 -0.9268 0.3665  1147 PHE B N   
21095 C CA  . PHE C 1147 ? 2.5677 1.9051 2.7613 -0.6549 -0.9034 0.3418  1147 PHE B CA  
21096 C C   . PHE C 1147 ? 2.5481 1.8608 2.7213 -0.6521 -0.8634 0.3310  1147 PHE B C   
21097 O O   . PHE C 1147 ? 2.5578 1.8254 2.7012 -0.6373 -0.8075 0.3249  1147 PHE B O   
21098 C CB  . PHE C 1147 ? 2.6015 1.8745 2.7527 -0.6409 -0.9568 0.3309  1147 PHE B CB  
21099 C CG  . PHE C 1147 ? 2.6175 1.8030 2.7096 -0.6087 -0.9308 0.3190  1147 PHE B CG  
21100 C CD1 . PHE C 1147 ? 2.6077 1.7584 2.6870 -0.6025 -0.9667 0.3145  1147 PHE B CD1 
21101 C CD2 . PHE C 1147 ? 2.6372 1.7780 2.6848 -0.5816 -0.8689 0.3139  1147 PHE B CD2 
21102 C CE1 . PHE C 1147 ? 2.6324 1.7068 2.6559 -0.5694 -0.9401 0.3039  1147 PHE B CE1 
21103 C CE2 . PHE C 1147 ? 2.6674 1.7335 2.6582 -0.5496 -0.8439 0.3046  1147 PHE B CE2 
21104 C CZ  . PHE C 1147 ? 2.6640 1.6976 2.6430 -0.5434 -0.8788 0.2991  1147 PHE B CZ  
21105 N N   . THR C 1148 ? 1.8459 1.1891 2.0232 -0.6516 -0.8896 0.3348  1148 THR B N   
21106 C CA  . THR C 1148 ? 1.8853 1.2194 2.0363 -0.6292 -0.8491 0.3344  1148 THR B CA  
21107 C C   . THR C 1148 ? 1.7650 1.1334 1.9562 -0.6555 -0.7906 0.3325  1148 THR B C   
21108 O O   . THR C 1148 ? 1.7798 1.1102 1.9343 -0.6310 -0.7387 0.3290  1148 THR B O   
21109 C CB  . THR C 1148 ? 1.8027 1.1795 1.9623 -0.6273 -0.8884 0.3417  1148 THR B CB  
21110 O OG1 . THR C 1148 ? 1.8090 1.2285 1.9986 -0.6388 -0.8498 0.3417  1148 THR B OG1 
21111 C CG2 . THR C 1148 ? 1.7587 1.2003 1.9667 -0.6582 -0.9505 0.3510  1148 THR B CG2 
21112 N N   . VAL C 1149 ? 1.9964 1.4468 2.2389 -0.6766 -0.7920 0.3448  1149 VAL B N   
21113 C CA  . VAL C 1149 ? 1.9681 1.4642 2.2350 -0.6871 -0.7353 0.3481  1149 VAL B CA  
21114 C C   . VAL C 1149 ? 1.9404 1.3764 2.1765 -0.6787 -0.6898 0.3395  1149 VAL B C   
21115 O O   . VAL C 1149 ? 1.9382 1.3491 2.1568 -0.6748 -0.6366 0.3333  1149 VAL B O   
21116 C CB  . VAL C 1149 ? 1.7519 1.3319 2.0622 -0.7018 -0.7445 0.3668  1149 VAL B CB  
21117 C CG1 . VAL C 1149 ? 1.7385 1.3547 2.0631 -0.7113 -0.6847 0.3672  1149 VAL B CG1 
21118 C CG2 . VAL C 1149 ? 1.7339 1.3738 2.0708 -0.7096 -0.7809 0.3804  1149 VAL B CG2 
21119 N N   . ILE C 1150 ? 1.6744 1.0857 1.9019 -0.6742 -0.7106 0.3406  1150 ILE B N   
21120 C CA  . ILE C 1150 ? 1.6185 0.9817 1.8198 -0.6661 -0.6693 0.3350  1150 ILE B CA  
21121 C C   . ILE C 1150 ? 1.6328 0.9044 1.7775 -0.6473 -0.6322 0.3239  1150 ILE B C   
21122 O O   . ILE C 1150 ? 1.6400 0.8989 1.7679 -0.6431 -0.5747 0.3228  1150 ILE B O   
21123 C CB  . ILE C 1150 ? 1.5818 0.9066 1.7716 -0.6590 -0.7055 0.3333  1150 ILE B CB  
21124 C CG1 . ILE C 1150 ? 1.5938 0.9892 1.8295 -0.6715 -0.7597 0.3481  1150 ILE B CG1 
21125 C CG2 . ILE C 1150 ? 1.5138 0.8167 1.6919 -0.6548 -0.6637 0.3315  1150 ILE B CG2 
21126 C CD1 . ILE C 1150 ? 1.6193 0.9894 1.8545 -0.6671 -0.7907 0.3490  1150 ILE B CD1 
21127 N N   . GLY C 1151 ? 3.2509 2.4693 3.3537 -0.6207 -0.6661 0.3195  1151 GLY B N   
21128 C CA  . GLY C 1151 ? 3.3177 2.4758 3.3500 -0.5744 -0.6382 0.3157  1151 GLY B CA  
21129 C C   . GLY C 1151 ? 3.3248 2.5105 3.3727 -0.5832 -0.5923 0.3176  1151 GLY B C   
21130 O O   . GLY C 1151 ? 3.3352 2.4927 3.3606 -0.5777 -0.5375 0.3161  1151 GLY B O   
21131 N N   . ILE C 1152 ? 1.5571 0.7996 1.6441 -0.5983 -0.6145 0.3211  1152 ILE B N   
21132 C CA  . ILE C 1152 ? 1.5902 0.8505 1.6836 -0.5976 -0.5741 0.3211  1152 ILE B CA  
21133 C C   . ILE C 1152 ? 1.6178 0.8831 1.7277 -0.6222 -0.5187 0.3204  1152 ILE B C   
21134 O O   . ILE C 1152 ? 1.6570 0.8825 1.7284 -0.6025 -0.4685 0.3185  1152 ILE B O   
21135 C CB  . ILE C 1152 ? 1.5179 0.8613 1.6756 -0.6286 -0.6002 0.3242  1152 ILE B CB  
21136 C CG1 . ILE C 1152 ? 1.4703 0.8250 1.6248 -0.6172 -0.6683 0.3282  1152 ILE B CG1 
21137 C CG2 . ILE C 1152 ? 1.3336 0.6826 1.4877 -0.6181 -0.5566 0.3224  1152 ILE B CG2 
21138 C CD1 . ILE C 1152 ? 1.3848 0.8271 1.6134 -0.6637 -0.7138 0.3323  1152 ILE B CD1 
21139 N N   . ARG C 1153 ? 2.4916 1.8172 2.6524 -0.6566 -0.5299 0.3236  1153 ARG B N   
21140 C CA  . ARG C 1153 ? 2.5058 1.8626 2.6713 -0.6626 -0.4807 0.3246  1153 ARG B CA  
21141 C C   . ARG C 1153 ? 2.5024 1.7631 2.6037 -0.6388 -0.4420 0.3212  1153 ARG B C   
21142 O O   . ARG C 1153 ? 2.5432 1.7703 2.6149 -0.6282 -0.3956 0.3200  1153 ARG B O   
21143 C CB  . ARG C 1153 ? 2.5491 1.9790 2.7552 -0.6786 -0.5034 0.3318  1153 ARG B CB  
21144 C CG  . ARG C 1153 ? 2.6103 2.1376 2.8717 -0.6983 -0.5319 0.3404  1153 ARG B CG  
21145 C CD  . ARG C 1153 ? 2.6606 2.2459 2.9408 -0.7104 -0.4840 0.3402  1153 ARG B CD  
21146 N NE  . ARG C 1153 ? 2.6711 2.3423 2.9958 -0.7271 -0.5077 0.3494  1153 ARG B NE  
21147 C CZ  . ARG C 1153 ? 2.6802 2.4061 3.0231 -0.7391 -0.4751 0.3483  1153 ARG B CZ  
21148 N NH1 . ARG C 1153 ? 2.6692 2.3762 2.9924 -0.7369 -0.4183 0.3381  1153 ARG B NH1 
21149 N NH2 . ARG C 1153 ? 2.7142 2.5099 3.0904 -0.7529 -0.4988 0.3578  1153 ARG B NH2 
21150 N N   . LYS C 1154 ? 1.7706 0.9834 1.8463 -0.6277 -0.4611 0.3204  1154 LYS B N   
21151 C CA  . LYS C 1154 ? 1.7906 0.9287 1.8079 -0.6058 -0.4199 0.3186  1154 LYS B CA  
21152 C C   . LYS C 1154 ? 1.8727 0.9549 1.8341 -0.5773 -0.3763 0.3174  1154 LYS B C   
21153 O O   . LYS C 1154 ? 1.8677 0.9285 1.8044 -0.5768 -0.3244 0.3194  1154 LYS B O   
21154 C CB  . LYS C 1154 ? 1.7924 0.8697 1.7733 -0.5827 -0.4545 0.3147  1154 LYS B CB  
21155 C CG  . LYS C 1154 ? 1.7452 0.8631 1.7686 -0.6046 -0.4814 0.3161  1154 LYS B CG  
21156 C CD  . LYS C 1154 ? 1.7494 0.8636 1.7561 -0.6013 -0.4351 0.3167  1154 LYS B CD  
21157 C CE  . LYS C 1154 ? 1.7510 0.8675 1.7723 -0.6039 -0.4609 0.3161  1154 LYS B CE  
21158 N NZ  . LYS C 1154 ? 1.7611 0.8638 1.7586 -0.5976 -0.4132 0.3167  1154 LYS B NZ  
21159 N N   . ALA C 1155 ? 2.6443 1.7152 2.5845 -0.5488 -0.4000 0.3142  1155 ALA B N   
21160 C CA  . ALA C 1155 ? 2.7333 1.7567 2.6168 -0.5114 -0.3689 0.3123  1155 ALA B CA  
21161 C C   . ALA C 1155 ? 2.8059 1.8688 2.7216 -0.5293 -0.3370 0.3144  1155 ALA B C   
21162 O O   . ALA C 1155 ? 2.8670 1.8951 2.7435 -0.5060 -0.3002 0.3138  1155 ALA B O   
21163 C CB  . ALA C 1155 ? 2.7374 1.7295 2.5835 -0.4729 -0.4098 0.3099  1155 ALA B CB  
21164 N N   . PHE C 1156 ? 2.3807 1.5177 2.3689 -0.5715 -0.3522 0.3166  1156 PHE B N   
21165 C CA  . PHE C 1156 ? 2.4171 1.6000 2.4424 -0.5876 -0.3339 0.3164  1156 PHE B CA  
21166 C C   . PHE C 1156 ? 2.4302 1.5793 2.4211 -0.5757 -0.2717 0.3159  1156 PHE B C   
21167 O O   . PHE C 1156 ? 2.4584 1.6070 2.4446 -0.5598 -0.2583 0.3137  1156 PHE B O   
21168 C CB  . PHE C 1156 ? 2.3894 1.6672 2.4955 -0.6395 -0.3442 0.3176  1156 PHE B CB  
21169 C CG  . PHE C 1156 ? 2.4097 1.7424 2.5508 -0.6532 -0.3198 0.3145  1156 PHE B CG  
21170 C CD1 . PHE C 1156 ? 2.4234 1.7830 2.5992 -0.6608 -0.3521 0.3142  1156 PHE B CD1 
21171 C CD2 . PHE C 1156 ? 2.4228 1.7771 2.5593 -0.6577 -0.2640 0.3110  1156 PHE B CD2 
21172 C CE1 . PHE C 1156 ? 2.4321 1.8403 2.6405 -0.6725 -0.3278 0.3100  1156 PHE B CE1 
21173 C CE2 . PHE C 1156 ? 2.4372 1.8367 2.6034 -0.6693 -0.2403 0.3063  1156 PHE B CE2 
21174 C CZ  . PHE C 1156 ? 2.4482 1.8745 2.6517 -0.6766 -0.2713 0.3056  1156 PHE B CZ  
21175 N N   . ASP C 1157 ? 2.5661 1.6852 2.5312 -0.5820 -0.2345 0.3186  1157 ASP B N   
21176 C CA  . ASP C 1157 ? 2.5976 1.7029 2.5408 -0.5818 -0.1755 0.3190  1157 ASP B CA  
21177 C C   . ASP C 1157 ? 2.6498 1.6882 2.5288 -0.5356 -0.1555 0.3175  1157 ASP B C   
21178 O O   . ASP C 1157 ? 2.6616 1.6920 2.5303 -0.5370 -0.1111 0.3181  1157 ASP B O   
21179 C CB  . ASP C 1157 ? 2.6324 1.7582 2.5605 -0.5874 -0.1461 0.3168  1157 ASP B CB  
21180 C CG  . ASP C 1157 ? 2.6747 1.8970 2.6641 -0.6177 -0.1667 0.3139  1157 ASP B CG  
21181 O OD1 . ASP C 1157 ? 2.6904 1.9671 2.7327 -0.6346 -0.2018 0.3132  1157 ASP B OD1 
21182 O OD2 . ASP C 1157 ? 2.6759 1.9201 2.6593 -0.6232 -0.1492 0.3137  1157 ASP B OD2 
21183 N N   . ILE C 1158 ? 2.3211 1.3158 2.1573 -0.4946 -0.1889 0.3154  1158 ILE B N   
21184 C CA  . ILE C 1158 ? 2.3191 1.2555 2.0954 -0.4495 -0.1748 0.3145  1158 ILE B CA  
21185 C C   . ILE C 1158 ? 2.3791 1.3392 2.1804 -0.4380 -0.1925 0.3132  1158 ILE B C   
21186 O O   . ILE C 1158 ? 2.4565 1.3830 2.2261 -0.4093 -0.1734 0.3136  1158 ILE B O   
21187 C CB  . ILE C 1158 ? 2.2652 1.1388 1.9768 -0.4100 -0.1980 0.3136  1158 ILE B CB  
21188 C CG1 . ILE C 1158 ? 2.1486 1.0352 1.8760 -0.4244 -0.2345 0.3122  1158 ILE B CG1 
21189 C CG2 . ILE C 1158 ? 2.2852 1.0986 1.9309 -0.3891 -0.1541 0.3149  1158 ILE B CG2 
21190 C CD1 . ILE C 1158 ? 2.1481 0.9877 1.8272 -0.3885 -0.2735 0.3094  1158 ILE B CD1 
21191 N N   . CYS C 1159 ? 3.1001 2.1196 2.9593 -0.4606 -0.2305 0.3125  1159 CYS B N   
21192 C CA  . CYS C 1159 ? 3.1331 2.1862 3.0244 -0.4557 -0.2433 0.3118  1159 CYS B CA  
21193 C C   . CYS C 1159 ? 3.1339 2.2689 3.1028 -0.5037 -0.2437 0.3095  1159 CYS B C   
21194 O O   . CYS C 1159 ? 3.1486 2.3331 3.1597 -0.5141 -0.2857 0.3096  1159 CYS B O   
21195 C CB  . CYS C 1159 ? 3.1060 2.1478 2.9819 -0.4263 -0.2972 0.3146  1159 CYS B CB  
21196 S SG  . CYS C 1159 ? 3.9287 2.9694 3.8046 -0.3955 -0.2982 0.3172  1159 CYS B SG  
21197 N N   . PRO C 1160 ? 2.4316 1.5826 2.4183 -0.5348 -0.1968 0.3083  1160 PRO B N   
21198 C CA  . PRO C 1160 ? 2.3734 1.6023 2.4328 -0.5824 -0.1881 0.3055  1160 PRO B CA  
21199 C C   . PRO C 1160 ? 2.3956 1.6524 2.4803 -0.5696 -0.1977 0.3014  1160 PRO B C   
21200 O O   . PRO C 1160 ? 2.4213 1.6424 2.4778 -0.5419 -0.1667 0.2994  1160 PRO B O   
21201 C CB  . PRO C 1160 ? 2.4170 1.6322 2.4656 -0.6017 -0.1252 0.3058  1160 PRO B CB  
21202 C CG  . PRO C 1160 ? 2.4764 1.6060 2.4454 -0.5554 -0.1016 0.3079  1160 PRO B CG  
21203 C CD  . PRO C 1160 ? 2.4610 1.5584 2.3981 -0.5277 -0.1477 0.3101  1160 PRO B CD  
21204 N N   . LEU C 1161 ? 2.1744 1.4961 2.3132 -0.5900 -0.2415 0.3006  1161 LEU B N   
21205 C CA  . LEU C 1161 ? 2.2079 1.5546 2.3665 -0.5726 -0.2593 0.2983  1161 LEU B CA  
21206 C C   . LEU C 1161 ? 2.1997 1.6408 2.4365 -0.6176 -0.2815 0.2948  1161 LEU B C   
21207 O O   . LEU C 1161 ? 2.1699 1.6535 2.4385 -0.6473 -0.3197 0.2976  1161 LEU B O   
21208 C CB  . LEU C 1161 ? 2.1852 1.4921 2.3023 -0.5286 -0.3064 0.3047  1161 LEU B CB  
21209 C CG  . LEU C 1161 ? 2.1855 1.4861 2.2944 -0.4916 -0.3254 0.3075  1161 LEU B CG  
21210 C CD1 . LEU C 1161 ? 2.1043 1.4471 2.2568 -0.5009 -0.2954 0.3011  1161 LEU B CD1 
21211 C CD2 . LEU C 1161 ? 2.1961 1.4085 2.2291 -0.4394 -0.3202 0.3133  1161 LEU B CD2 
21212 N N   . VAL C 1162 ? 2.2294 1.7030 2.4973 -0.6229 -0.2562 0.2882  1162 VAL B N   
21213 C CA  . VAL C 1162 ? 2.2295 1.7946 2.5700 -0.6601 -0.2771 0.2834  1162 VAL B CA  
21214 C C   . VAL C 1162 ? 2.2126 1.8014 2.5606 -0.6545 -0.3463 0.2906  1162 VAL B C   
21215 O O   . VAL C 1162 ? 2.1467 1.7706 2.5202 -0.6877 -0.3770 0.2938  1162 VAL B O   
21216 C CB  . VAL C 1162 ? 2.3342 1.9151 2.6924 -0.6436 -0.2539 0.2760  1162 VAL B CB  
21217 C CG1 . VAL C 1162 ? 2.3501 1.9308 2.7195 -0.6654 -0.1875 0.2668  1162 VAL B CG1 
21218 C CG2 . VAL C 1162 ? 2.4220 1.9332 2.7238 -0.5814 -0.2611 0.2816  1162 VAL B CG2 
21219 N N   . LYS C 1163 ? 1.9363 1.4996 2.2572 -0.6108 -0.3706 0.2948  1163 LYS B N   
21220 C CA  . LYS C 1163 ? 1.9447 1.5401 2.2766 -0.6063 -0.4359 0.3023  1163 LYS B CA  
21221 C C   . LYS C 1163 ? 1.9070 1.4931 2.2263 -0.6201 -0.4752 0.3085  1163 LYS B C   
21222 O O   . LYS C 1163 ? 1.8853 1.5192 2.2313 -0.6360 -0.5306 0.3135  1163 LYS B O   
21223 C CB  . LYS C 1163 ? 1.9927 1.5413 2.2808 -0.5516 -0.4498 0.3095  1163 LYS B CB  
21224 C CG  . LYS C 1163 ? 1.9867 1.5935 2.3055 -0.5505 -0.5029 0.3159  1163 LYS B CG  
21225 C CD  . LYS C 1163 ? 2.0336 1.5867 2.3013 -0.4965 -0.5227 0.3278  1163 LYS B CD  
21226 C CE  . LYS C 1163 ? 2.0329 1.6396 2.3210 -0.4982 -0.5865 0.3386  1163 LYS B CE  
21227 N NZ  . LYS C 1163 ? 2.0753 1.6322 2.3120 -0.4503 -0.6122 0.3541  1163 LYS B NZ  
21228 N N   . ILE C 1164 ? 2.7377 2.2648 3.0178 -0.6149 -0.4477 0.3082  1164 ILE B N   
21229 C CA  . ILE C 1164 ? 2.7310 2.2462 2.9999 -0.6256 -0.4830 0.3131  1164 ILE B CA  
21230 C C   . ILE C 1164 ? 2.6924 2.2579 3.0124 -0.6807 -0.4715 0.3104  1164 ILE B C   
21231 O O   . ILE C 1164 ? 2.6597 2.2398 2.9931 -0.7011 -0.5077 0.3144  1164 ILE B O   
21232 C CB  . ILE C 1164 ? 2.4602 1.8801 2.6525 -0.5849 -0.4712 0.3157  1164 ILE B CB  
21233 C CG1 . ILE C 1164 ? 2.4282 1.8247 2.6132 -0.6045 -0.4252 0.3125  1164 ILE B CG1 
21234 C CG2 . ILE C 1164 ? 2.5151 1.8759 2.6541 -0.5328 -0.4551 0.3175  1164 ILE B CG2 
21235 C CD1 . ILE C 1164 ? 2.4503 1.7714 2.5727 -0.5765 -0.4296 0.3150  1164 ILE B CD1 
21236 N N   . ASP C 1165 ? 2.4939 2.0848 2.8426 -0.7060 -0.4205 0.3043  1165 ASP B N   
21237 C CA  . ASP C 1165 ? 2.4851 2.1536 2.8610 -0.7272 -0.4106 0.3046  1165 ASP B CA  
21238 C C   . ASP C 1165 ? 2.4708 2.2286 2.8910 -0.7412 -0.4601 0.3096  1165 ASP B C   
21239 O O   . ASP C 1165 ? 2.4458 2.2423 2.8716 -0.7472 -0.4887 0.3192  1165 ASP B O   
21240 C CB  . ASP C 1165 ? 2.5273 2.2172 2.9086 -0.7340 -0.3472 0.2964  1165 ASP B CB  
21241 C CG  . ASP C 1165 ? 2.5253 2.2920 2.9237 -0.7506 -0.3371 0.2975  1165 ASP B CG  
21242 O OD1 . ASP C 1165 ? 2.4916 2.2646 2.8809 -0.7512 -0.3607 0.3062  1165 ASP B OD1 
21243 O OD2 . ASP C 1165 ? 2.5581 2.3744 2.9771 -0.7628 -0.3054 0.2901  1165 ASP B OD2 
21244 N N   . THR C 1166 ? 2.4326 2.2190 2.8813 -0.7446 -0.4685 0.3052  1166 THR B N   
21245 C CA  . THR C 1166 ? 2.4343 2.2991 2.9181 -0.7539 -0.5158 0.3117  1166 THR B CA  
21246 C C   . THR C 1166 ? 2.4067 2.2602 2.8749 -0.7477 -0.5750 0.3245  1166 THR B C   
21247 O O   . THR C 1166 ? 2.4167 2.3091 2.8884 -0.7550 -0.5914 0.3365  1166 THR B O   
21248 C CB  . THR C 1166 ? 2.4603 2.3336 2.9676 -0.7515 -0.5295 0.3055  1166 THR B CB  
21249 O OG1 . THR C 1166 ? 2.4929 2.3827 3.0204 -0.7585 -0.4744 0.2937  1166 THR B OG1 
21250 C CG2 . THR C 1166 ? 2.4679 2.4158 3.0017 -0.7566 -0.5851 0.3155  1166 THR B CG2 
21251 N N   . ALA C 1167 ? 3.3314 3.1247 3.7788 -0.7342 -0.6059 0.3226  1167 ALA B N   
21252 C CA  . ALA C 1167 ? 3.2761 3.0543 3.7051 -0.7268 -0.6656 0.3326  1167 ALA B CA  
21253 C C   . ALA C 1167 ? 3.1922 2.9655 3.6077 -0.7295 -0.6589 0.3403  1167 ALA B C   
21254 O O   . ALA C 1167 ? 3.1751 2.9723 3.5920 -0.7308 -0.7017 0.3544  1167 ALA B O   
21255 C CB  . ALA C 1167 ? 3.2949 2.9862 3.6726 -0.6945 -0.6798 0.3297  1167 ALA B CB  
21256 N N   . LEU C 1168 ? 1.6979 1.4399 2.0994 -0.7299 -0.6041 0.3331  1168 LEU B N   
21257 C CA  . LEU C 1168 ? 1.6615 1.3985 2.0503 -0.7313 -0.5968 0.3394  1168 LEU B CA  
21258 C C   . LEU C 1168 ? 1.7292 1.5478 2.1470 -0.7461 -0.6115 0.3543  1168 LEU B C   
21259 O O   . LEU C 1168 ? 1.7461 1.5654 2.1595 -0.7464 -0.6389 0.3665  1168 LEU B O   
21260 C CB  . LEU C 1168 ? 1.5962 1.2932 1.9628 -0.7283 -0.5327 0.3304  1168 LEU B CB  
21261 C CG  . LEU C 1168 ? 1.5643 1.1904 1.8923 -0.7157 -0.5365 0.3309  1168 LEU B CG  
21262 C CD1 . LEU C 1168 ? 1.5738 1.1329 1.8630 -0.7048 -0.4757 0.3230  1168 LEU B CD1 
21263 C CD2 . LEU C 1168 ? 1.5167 1.1866 1.8586 -0.7237 -0.5571 0.3423  1168 LEU B CD2 
21264 N N   . ILE C 1169 ? 1.8214 1.7022 2.2662 -0.7585 -0.5924 0.3538  1169 ILE B N   
21265 C CA  . ILE C 1169 ? 1.8068 1.7586 2.2726 -0.7743 -0.6015 0.3685  1169 ILE B CA  
21266 C C   . ILE C 1169 ? 1.8312 1.8057 2.3058 -0.7750 -0.6615 0.3856  1169 ILE B C   
21267 O O   . ILE C 1169 ? 1.8308 1.8177 2.3045 -0.7802 -0.6881 0.4037  1169 ILE B O   
21268 C CB  . ILE C 1169 ? 1.8067 1.8124 2.2932 -0.7878 -0.5612 0.3600  1169 ILE B CB  
21269 C CG1 . ILE C 1169 ? 1.7663 1.7558 2.2399 -0.7898 -0.5003 0.3472  1169 ILE B CG1 
21270 C CG2 . ILE C 1169 ? 1.8397 1.9142 2.3433 -0.8050 -0.5788 0.3758  1169 ILE B CG2 
21271 C CD1 . ILE C 1169 ? 1.7668 1.7353 2.2417 -0.7859 -0.4575 0.3280  1169 ILE B CD1 
21272 N N   . LYS C 1170 ? 2.0720 2.0498 2.5542 -0.7698 -0.6816 0.3810  1170 LYS B N   
21273 C CA  . LYS C 1170 ? 2.1320 2.1246 2.6160 -0.7679 -0.7386 0.3973  1170 LYS B CA  
21274 C C   . LYS C 1170 ? 2.0761 2.0267 2.5383 -0.7607 -0.7760 0.4105  1170 LYS B C   
21275 O O   . LYS C 1170 ? 2.0789 2.0447 2.5414 -0.7650 -0.8161 0.4309  1170 LYS B O   
21276 C CB  . LYS C 1170 ? 2.2204 2.1949 2.7028 -0.7553 -0.7594 0.3874  1170 LYS B CB  
21277 C CG  . LYS C 1170 ? 2.3254 2.3427 2.8351 -0.7615 -0.7291 0.3748  1170 LYS B CG  
21278 C CD  . LYS C 1170 ? 2.4493 2.5411 2.9817 -0.7775 -0.7364 0.3880  1170 LYS B CD  
21279 C CE  . LYS C 1170 ? 2.5466 2.6471 3.0718 -0.7737 -0.7955 0.4080  1170 LYS B CE  
21280 N NZ  . LYS C 1170 ? 2.6090 2.7772 3.1525 -0.7916 -0.7999 0.4216  1170 LYS B NZ  
21281 N N   . ALA C 1171 ? 2.2512 2.1451 2.6933 -0.7505 -0.7606 0.3986  1171 ALA B N   
21282 C CA  . ALA C 1171 ? 2.2597 2.1088 2.6812 -0.7427 -0.7912 0.4064  1171 ALA B CA  
21283 C C   . ALA C 1171 ? 2.2621 2.1401 2.6951 -0.7552 -0.7801 0.4213  1171 ALA B C   
21284 O O   . ALA C 1171 ? 2.2825 2.1719 2.7194 -0.7602 -0.8166 0.4417  1171 ALA B O   
21285 C CB  . ALA C 1171 ? 2.2504 2.0271 2.6437 -0.7288 -0.7745 0.3869  1171 ALA B CB  
21286 N N   . ASP C 1172 ? 2.3202 2.2077 2.7568 -0.7606 -0.7290 0.4121  1172 ASP B N   
21287 C CA  . ASP C 1172 ? 2.3277 2.2458 2.7739 -0.7727 -0.7165 0.4256  1172 ASP B CA  
21288 C C   . ASP C 1172 ? 2.3676 2.3407 2.8323 -0.7881 -0.7445 0.4482  1172 ASP B C   
21289 O O   . ASP C 1172 ? 2.3624 2.3390 2.8303 -0.7939 -0.7710 0.4678  1172 ASP B O   
21290 C CB  . ASP C 1172 ? 2.3437 2.2806 2.7914 -0.7794 -0.6549 0.4129  1172 ASP B CB  
21291 C CG  . ASP C 1172 ? 2.3462 2.2259 2.7713 -0.7673 -0.6261 0.3990  1172 ASP B CG  
21292 O OD1 . ASP C 1172 ? 2.3376 2.1585 2.7442 -0.7529 -0.6490 0.3932  1172 ASP B OD1 
21293 O OD2 . ASP C 1172 ? 2.3641 2.2552 2.7857 -0.7727 -0.5798 0.3937  1172 ASP B OD2 
21294 N N   . ASN C 1173 ? 2.3984 2.4109 2.8745 -0.7953 -0.7390 0.4456  1173 ASN B N   
21295 C CA  . ASN C 1173 ? 2.4653 2.5284 2.9550 -0.8115 -0.7627 0.4660  1173 ASN B CA  
21296 C C   . ASN C 1173 ? 2.4572 2.4962 2.9405 -0.8088 -0.8181 0.4874  1173 ASN B C   
21297 O O   . ASN C 1173 ? 2.4796 2.5319 2.9675 -0.8205 -0.8321 0.5079  1173 ASN B O   
21298 C CB  . ASN C 1173 ? 2.5589 2.6564 3.0594 -0.8148 -0.7578 0.4577  1173 ASN B CB  
21299 C CG  . ASN C 1173 ? 2.6412 2.7815 3.1535 -0.8263 -0.7049 0.4425  1173 ASN B CG  
21300 O OD1 . ASN C 1173 ? 2.7169 2.9108 3.2423 -0.8415 -0.7001 0.4458  1173 ASN B OD1 
21301 N ND2 . ASN C 1173 ? 2.6205 2.7356 3.1255 -0.8201 -0.6640 0.4253  1173 ASN B ND2 
21302 N N   . PHE C 1174 ? 2.3050 2.3067 2.7764 -0.7938 -0.8497 0.4829  1174 PHE B N   
21303 C CA  . PHE C 1174 ? 2.3114 2.2830 2.7721 -0.7903 -0.9029 0.5014  1174 PHE B CA  
21304 C C   . PHE C 1174 ? 2.2659 2.2186 2.7268 -0.7933 -0.9071 0.5125  1174 PHE B C   
21305 O O   . PHE C 1174 ? 2.3102 2.2695 2.7760 -0.8042 -0.9368 0.5361  1174 PHE B O   
21306 C CB  . PHE C 1174 ? 2.2941 2.2088 2.7317 -0.7687 -0.9300 0.4884  1174 PHE B CB  
21307 C CG  . PHE C 1174 ? 2.2970 2.1698 2.7172 -0.7634 -0.9839 0.5043  1174 PHE B CG  
21308 C CD1 . PHE C 1174 ? 2.3440 2.2218 2.7575 -0.7651 -1.0208 0.5174  1174 PHE B CD1 
21309 C CD2 . PHE C 1174 ? 2.2695 2.0961 2.6791 -0.7564 -0.9963 0.5047  1174 PHE B CD2 
21310 C CE1 . PHE C 1174 ? 2.3773 2.2127 2.7721 -0.7613 -1.0680 0.5312  1174 PHE B CE1 
21311 C CE2 . PHE C 1174 ? 2.2952 2.0804 2.6887 -0.7518 -1.0446 0.5170  1174 PHE B CE2 
21312 C CZ  . PHE C 1174 ? 2.3511 2.1392 2.7360 -0.7546 -1.0799 0.5303  1174 PHE B CZ  
21313 N N   . LEU C 1175 ? 2.2385 2.1693 2.6954 -0.7852 -0.8753 0.4961  1175 LEU B N   
21314 C CA  . LEU C 1175 ? 2.2181 2.1264 2.6755 -0.7848 -0.8799 0.5039  1175 LEU B CA  
21315 C C   . LEU C 1175 ? 2.2345 2.1914 2.7112 -0.8057 -0.8748 0.5266  1175 LEU B C   
21316 O O   . LEU C 1175 ? 2.2440 2.1927 2.7257 -0.8116 -0.9097 0.5479  1175 LEU B O   
21317 C CB  . LEU C 1175 ? 2.1769 2.0543 2.6246 -0.7731 -0.8430 0.4814  1175 LEU B CB  
21318 C CG  . LEU C 1175 ? 2.1620 1.9697 2.5849 -0.7529 -0.8661 0.4663  1175 LEU B CG  
21319 C CD1 . LEU C 1175 ? 2.1179 1.8926 2.5305 -0.7450 -0.8314 0.4492  1175 LEU B CD1 
21320 C CD2 . LEU C 1175 ? 2.1836 1.9635 2.6024 -0.7501 -0.9210 0.4827  1175 LEU B CD2 
21321 N N   . LEU C 1176 ? 2.2443 2.2496 2.7301 -0.8178 -0.8325 0.5221  1176 LEU B N   
21322 C CA  . LEU C 1176 ? 2.2814 2.3356 2.7809 -0.8397 -0.8292 0.5435  1176 LEU B CA  
21323 C C   . LEU C 1176 ? 2.4017 2.4708 2.9057 -0.8518 -0.8726 0.5673  1176 LEU B C   
21324 O O   . LEU C 1176 ? 2.4492 2.5078 2.9581 -0.8586 -0.9046 0.5899  1176 LEU B O   
21325 C CB  . LEU C 1176 ? 2.2299 2.3351 2.7328 -0.8516 -0.7816 0.5319  1176 LEU B CB  
21326 C CG  . LEU C 1176 ? 2.1329 2.2088 2.6262 -0.8358 -0.7421 0.5046  1176 LEU B CG  
21327 C CD1 . LEU C 1176 ? 2.1284 2.2392 2.6222 -0.8420 -0.6970 0.4860  1176 LEU B CD1 
21328 C CD2 . LEU C 1176 ? 2.1044 2.1662 2.5966 -0.8348 -0.7280 0.5081  1176 LEU B CD2 
21329 N N   . GLU C 1177 ? 2.7075 2.7982 3.2099 -0.8539 -0.8734 0.5616  1177 GLU B N   
21330 C CA  . GLU C 1177 ? 2.8038 2.9190 3.3092 -0.8684 -0.9066 0.5826  1177 GLU B CA  
21331 C C   . GLU C 1177 ? 2.8251 2.8933 3.3230 -0.8621 -0.9588 0.5988  1177 GLU B C   
21332 O O   . GLU C 1177 ? 2.9044 2.9841 3.4009 -0.8718 -0.9878 0.6143  1177 GLU B O   
21333 C CB  . GLU C 1177 ? 2.8759 3.0198 3.3816 -0.8681 -0.8958 0.5690  1177 GLU B CB  
21334 C CG  . GLU C 1177 ? 2.9589 3.1696 3.4750 -0.8873 -0.8586 0.5645  1177 GLU B CG  
21335 C CD  . GLU C 1177 ? 3.0619 3.3070 3.5825 -0.8913 -0.8600 0.5581  1177 GLU B CD  
21336 O OE1 . GLU C 1177 ? 3.1353 3.4364 3.6629 -0.9131 -0.8519 0.5660  1177 GLU B OE1 
21337 O OE2 . GLU C 1177 ? 3.0676 3.2849 3.5845 -0.8732 -0.8701 0.5450  1177 GLU B OE2 
21338 N N   . ASN C 1178 ? 2.2602 2.2757 2.7525 -0.8469 -0.9705 0.5948  1178 ASN B N   
21339 C CA  . ASN C 1178 ? 2.2462 2.2110 2.7287 -0.8397 -1.0200 0.6064  1178 ASN B CA  
21340 C C   . ASN C 1178 ? 2.1947 2.1137 2.6783 -0.8310 -1.0337 0.6086  1178 ASN B C   
21341 O O   . ASN C 1178 ? 2.2179 2.0916 2.6931 -0.8253 -1.0750 0.6164  1178 ASN B O   
21342 C CB  . ASN C 1178 ? 2.2160 2.1460 2.6787 -0.8213 -1.0360 0.5897  1178 ASN B CB  
21343 C CG  . ASN C 1178 ? 2.2492 2.2005 2.7083 -0.8320 -1.0626 0.6041  1178 ASN B CG  
21344 O OD1 . ASN C 1178 ? 2.2848 2.2144 2.7378 -0.8381 -1.1038 0.6234  1178 ASN B OD1 
21345 N ND2 . ASN C 1178 ? 2.2473 2.2396 2.7103 -0.8340 -1.0389 0.5933  1178 ASN B ND2 
21346 N N   . THR C 1179 ? 2.4217 2.3511 2.9151 -0.8302 -1.0002 0.6013  1179 THR B N   
21347 C CA  . THR C 1179 ? 2.3751 2.2634 2.8722 -0.8215 -1.0132 0.6025  1179 THR B CA  
21348 C C   . THR C 1179 ? 2.3875 2.2872 2.9031 -0.8390 -1.0391 0.6325  1179 THR B C   
21349 O O   . THR C 1179 ? 2.3836 2.2403 2.9002 -0.8342 -1.0768 0.6410  1179 THR B O   
21350 C CB  . THR C 1179 ? 2.1478 2.0421 2.6497 -0.8151 -0.9683 0.5856  1179 THR B CB  
21351 O OG1 . THR C 1179 ? 2.1227 2.0220 2.6117 -0.8057 -0.9326 0.5602  1179 THR B OG1 
21352 C CG2 . THR C 1179 ? 2.0239 1.8644 2.5246 -0.7998 -0.9829 0.5782  1179 THR B CG2 
21353 N N   . LEU C 1180 ? 3.1975 3.1546 3.7266 -0.8599 -1.0186 0.6479  1180 LEU B N   
21354 C CA  . LEU C 1180 ? 3.2217 3.1946 3.7705 -0.8746 -1.0245 0.6705  1180 LEU B CA  
21355 C C   . LEU C 1180 ? 3.3473 3.3034 3.9061 -0.8867 -1.0739 0.6995  1180 LEU B C   
21356 O O   . LEU C 1180 ? 3.3639 3.3073 3.9396 -0.8892 -1.0864 0.7120  1180 LEU B O   
21357 C CB  . LEU C 1180 ? 3.1790 3.2162 3.7347 -0.8934 -0.9860 0.6761  1180 LEU B CB  
21358 C CG  . LEU C 1180 ? 3.0675 3.1032 3.6234 -0.8811 -0.9433 0.6546  1180 LEU B CG  
21359 C CD1 . LEU C 1180 ? 3.0558 3.1498 3.6155 -0.8995 -0.9056 0.6594  1180 LEU B CD1 
21360 C CD2 . LEU C 1180 ? 3.0331 3.0261 3.6008 -0.8697 -0.9608 0.6575  1180 LEU B CD2 
21361 N N   . PRO C 1181 ? 2.4156 2.3727 2.9654 -0.8957 -1.1018 0.7110  1181 PRO B N   
21362 C CA  . PRO C 1181 ? 2.4489 2.3709 3.0054 -0.9020 -1.1514 0.7334  1181 PRO B CA  
21363 C C   . PRO C 1181 ? 2.4090 2.2626 2.9586 -0.8764 -1.1704 0.7148  1181 PRO B C   
21364 O O   . PRO C 1181 ? 2.4117 2.2248 2.9429 -0.8668 -1.1993 0.7085  1181 PRO B O   
21365 C CB  . PRO C 1181 ? 2.4802 2.4117 3.0232 -0.9141 -1.1750 0.7448  1181 PRO B CB  
21366 C CG  . PRO C 1181 ? 2.4772 2.4735 3.0185 -0.9262 -1.1362 0.7409  1181 PRO B CG  
21367 C CD  . PRO C 1181 ? 2.4177 2.4166 2.9575 -0.9077 -1.0919 0.7120  1181 PRO B CD  
21368 N N   . ALA C 1182 ? 2.5678 2.4102 3.1305 -0.8662 -1.1540 0.7056  1182 ALA B N   
21369 C CA  . ALA C 1182 ? 2.5033 2.2878 3.0581 -0.8408 -1.1609 0.6816  1182 ALA B CA  
21370 C C   . ALA C 1182 ? 2.5732 2.2991 3.1215 -0.8351 -1.2141 0.6867  1182 ALA B C   
21371 O O   . ALA C 1182 ? 2.6375 2.3584 3.2050 -0.8481 -1.2438 0.7105  1182 ALA B O   
21372 C CB  . ALA C 1182 ? 2.4095 2.1998 2.9853 -0.8365 -1.1367 0.6770  1182 ALA B CB  
21373 N N   . GLN C 1183 ? 2.4219 2.1024 2.9414 -0.8160 -1.2262 0.6640  1183 GLN B N   
21374 C CA  . GLN C 1183 ? 2.4243 2.0428 2.9287 -0.8078 -1.2755 0.6630  1183 GLN B CA  
21375 C C   . GLN C 1183 ? 2.3412 1.9113 2.8497 -0.7898 -1.2848 0.6455  1183 GLN B C   
21376 O O   . GLN C 1183 ? 2.3833 1.9134 2.8965 -0.7896 -1.3257 0.6531  1183 GLN B O   
21377 C CB  . GLN C 1183 ? 2.4635 2.0561 2.9301 -0.7962 -1.2855 0.6467  1183 GLN B CB  
21378 C CG  . GLN C 1183 ? 2.5630 2.0982 3.0088 -0.7929 -1.3386 0.6504  1183 GLN B CG  
21379 C CD  . GLN C 1183 ? 2.6572 2.2110 3.1169 -0.8185 -1.3678 0.6845  1183 GLN B CD  
21380 O OE1 . GLN C 1183 ? 2.6675 2.2795 3.1474 -0.8384 -1.3479 0.7042  1183 GLN B OE1 
21381 N NE2 . GLN C 1183 ? 2.7200 2.2240 3.1661 -0.8193 -1.4155 0.6912  1183 GLN B NE2 
21382 N N   . SER C 1184 ? 2.2456 1.8198 2.7520 -0.7756 -1.2463 0.6214  1184 SER B N   
21383 C CA  . SER C 1184 ? 2.1975 1.7330 2.7089 -0.7595 -1.2473 0.6024  1184 SER B CA  
21384 C C   . SER C 1184 ? 2.1167 1.6773 2.6370 -0.7532 -1.1946 0.5848  1184 SER B C   
21385 O O   . SER C 1184 ? 2.0752 1.6617 2.5813 -0.7520 -1.1583 0.5740  1184 SER B O   
21386 C CB  . SER C 1184 ? 2.2284 1.6954 2.7013 -0.7388 -1.2768 0.5770  1184 SER B CB  
21387 O OG  . SER C 1184 ? 2.1982 1.6332 2.6717 -0.7231 -1.2679 0.5531  1184 SER B OG  
21388 N N   . THR C 1185 ? 2.1110 1.6611 2.6546 -0.7494 -1.1915 0.5816  1185 THR B N   
21389 C CA  . THR C 1185 ? 2.0407 1.6105 2.5942 -0.7449 -1.1427 0.5665  1185 THR B CA  
21390 C C   . THR C 1185 ? 2.0009 1.5442 2.5158 -0.7286 -1.1165 0.5333  1185 THR B C   
21391 O O   . THR C 1185 ? 1.9308 1.5058 2.4416 -0.7307 -1.0688 0.5253  1185 THR B O   
21392 C CB  . THR C 1185 ? 2.0299 1.5732 2.6076 -0.7384 -1.1519 0.5610  1185 THR B CB  
21393 O OG1 . THR C 1185 ? 2.0564 1.6196 2.6720 -0.7534 -1.1795 0.5923  1185 THR B OG1 
21394 C CG2 . THR C 1185 ? 1.9685 1.5316 2.5549 -0.7352 -1.0982 0.5463  1185 THR B CG2 
21395 N N   . PHE C 1186 ? 2.6066 2.0884 3.0905 -0.7129 -1.1486 0.5137  1186 PHE B N   
21396 C CA  . PHE C 1186 ? 2.5782 2.0250 3.0185 -0.6977 -1.1315 0.4826  1186 PHE B CA  
21397 C C   . PHE C 1186 ? 2.5909 2.0799 3.0229 -0.7056 -1.1095 0.4900  1186 PHE B C   
21398 O O   . PHE C 1186 ? 2.5704 2.0809 2.9984 -0.7058 -1.0622 0.4785  1186 PHE B O   
21399 C CB  . PHE C 1186 ? 2.5718 1.9487 2.9740 -0.6821 -1.1791 0.4657  1186 PHE B CB  
21400 C CG  . PHE C 1186 ? 2.5326 1.8650 2.8824 -0.6663 -1.1664 0.4333  1186 PHE B CG  
21401 C CD1 . PHE C 1186 ? 2.5038 1.7982 2.8351 -0.6561 -1.1365 0.4047  1186 PHE B CD1 
21402 C CD2 . PHE C 1186 ? 2.5451 1.8680 2.8612 -0.6622 -1.1853 0.4322  1186 PHE B CD2 
21403 C CE1 . PHE C 1186 ? 2.4928 1.7371 2.7705 -0.6432 -1.1243 0.3761  1186 PHE B CE1 
21404 C CE2 . PHE C 1186 ? 2.5375 1.8175 2.8036 -0.6480 -1.1764 0.4039  1186 PHE B CE2 
21405 C CZ  . PHE C 1186 ? 2.5131 1.7513 2.7586 -0.6390 -1.1459 0.3757  1186 PHE B CZ  
21406 N N   . THR C 1187 ? 1.7329 1.2356 2.1649 -0.7138 -1.1410 0.5103  1187 THR B N   
21407 C CA  . THR C 1187 ? 1.7012 1.2396 2.1234 -0.7200 -1.1239 0.5144  1187 THR B CA  
21408 C C   . THR C 1187 ? 1.6498 1.2468 2.0938 -0.7308 -1.0700 0.5176  1187 THR B C   
21409 O O   . THR C 1187 ? 1.6169 1.2245 2.0459 -0.7271 -1.0350 0.5013  1187 THR B O   
21410 C CB  . THR C 1187 ? 1.7325 1.2928 2.1633 -0.7344 -1.1573 0.5427  1187 THR B CB  
21411 O OG1 . THR C 1187 ? 1.7610 1.2679 2.1752 -0.7277 -1.2092 0.5445  1187 THR B OG1 
21412 C CG2 . THR C 1187 ? 1.7344 1.3217 2.1496 -0.7372 -1.1436 0.5410  1187 THR B CG2 
21413 N N   . LEU C 1188 ? 2.1540 1.7871 2.6322 -0.7449 -1.0652 0.5393  1188 LEU B N   
21414 C CA  . LEU C 1188 ? 2.1256 1.8157 2.6238 -0.7571 -1.0182 0.5458  1188 LEU B CA  
21415 C C   . LEU C 1188 ? 2.0745 1.7503 2.5589 -0.7455 -0.9734 0.5182  1188 LEU B C   
21416 O O   . LEU C 1188 ? 2.0559 1.7570 2.5310 -0.7475 -0.9338 0.5083  1188 LEU B O   
21417 C CB  . LEU C 1188 ? 2.1406 1.8522 2.6729 -0.7692 -1.0264 0.5690  1188 LEU B CB  
21418 C CG  . LEU C 1188 ? 2.1003 1.8769 2.6524 -0.7917 -1.0125 0.5951  1188 LEU B CG  
21419 C CD1 . LEU C 1188 ? 2.1097 1.9039 2.6482 -0.7995 -1.0255 0.6027  1188 LEU B CD1 
21420 C CD2 . LEU C 1188 ? 2.1067 1.8893 2.6886 -0.8035 -1.0415 0.6223  1188 LEU B CD2 
21421 N N   . ALA C 1189 ? 2.0148 1.6457 2.4967 -0.7339 -0.9805 0.5051  1189 ALA B N   
21422 C CA  . ALA C 1189 ? 2.0166 1.6301 2.4881 -0.7257 -0.9366 0.4825  1189 ALA B CA  
21423 C C   . ALA C 1189 ? 1.9769 1.5776 2.4152 -0.7188 -0.9021 0.4599  1189 ALA B C   
21424 O O   . ALA C 1189 ? 1.9287 1.5494 2.3650 -0.7218 -0.8509 0.4527  1189 ALA B O   
21425 C CB  . ALA C 1189 ? 2.0261 1.5794 2.4907 -0.7124 -0.9579 0.4678  1189 ALA B CB  
21426 N N   . ILE C 1190 ? 2.3419 1.9065 2.7523 -0.7095 -0.9297 0.4490  1190 ILE B N   
21427 C CA  . ILE C 1190 ? 2.3450 1.8927 2.7245 -0.7031 -0.9001 0.4285  1190 ILE B CA  
21428 C C   . ILE C 1190 ? 2.3372 1.9500 2.7333 -0.7164 -0.8776 0.4413  1190 ILE B C   
21429 O O   . ILE C 1190 ? 2.3072 1.9319 2.6955 -0.7177 -0.8299 0.4300  1190 ILE B O   
21430 C CB  . ILE C 1190 ? 2.3529 1.8388 2.6932 -0.6885 -0.9374 0.4119  1190 ILE B CB  
21431 C CG1 . ILE C 1190 ? 2.3653 1.7805 2.6817 -0.6751 -0.9530 0.3940  1190 ILE B CG1 
21432 C CG2 . ILE C 1190 ? 2.3372 1.8051 2.6477 -0.6833 -0.9062 0.3933  1190 ILE B CG2 
21433 C CD1 . ILE C 1190 ? 2.3976 1.7467 2.6675 -0.6605 -0.9911 0.3762  1190 ILE B CD1 
21434 N N   . SER C 1191 ? 1.8072 1.4593 2.2245 -0.7270 -0.9092 0.4649  1191 SER B N   
21435 C CA  . SER C 1191 ? 1.7822 1.4941 2.2127 -0.7406 -0.8888 0.4758  1191 SER B CA  
21436 C C   . SER C 1191 ? 1.7412 1.4933 2.1861 -0.7501 -0.8365 0.4762  1191 SER B C   
21437 O O   . SER C 1191 ? 1.7092 1.4962 2.1537 -0.7568 -0.7997 0.4713  1191 SER B O   
21438 C CB  . SER C 1191 ? 1.8145 1.5594 2.2640 -0.7536 -0.9268 0.5038  1191 SER B CB  
21439 O OG  . SER C 1191 ? 1.8245 1.6205 2.2802 -0.7654 -0.9083 0.5096  1191 SER B OG  
21440 N N   . ALA C 1192 ? 1.3882 1.1329 1.8448 -0.7504 -0.8345 0.4815  1192 ALA B N   
21441 C CA  . ALA C 1192 ? 1.3515 1.1281 1.8188 -0.7581 -0.7884 0.4828  1192 ALA B CA  
21442 C C   . ALA C 1192 ? 1.3753 1.1265 1.8172 -0.7490 -0.7393 0.4573  1192 ALA B C   
21443 O O   . ALA C 1192 ? 1.3935 1.1735 1.8295 -0.7548 -0.7008 0.4514  1192 ALA B O   
21444 C CB  . ALA C 1192 ? 1.3174 1.0813 1.8023 -0.7574 -0.8023 0.4924  1192 ALA B CB  
21445 N N   . TYR C 1193 ? 1.7602 1.4527 2.1848 -0.7351 -0.7405 0.4422  1193 TYR B N   
21446 C CA  . TYR C 1193 ? 1.7375 1.3929 2.1325 -0.7262 -0.6926 0.4205  1193 TYR B CA  
21447 C C   . TYR C 1193 ? 1.7382 1.3912 2.1126 -0.7246 -0.6703 0.4082  1193 TYR B C   
21448 O O   . TYR C 1193 ? 1.7555 1.3988 2.1103 -0.7227 -0.6198 0.3964  1193 TYR B O   
21449 C CB  . TYR C 1193 ? 1.7393 1.3191 2.1107 -0.7106 -0.7073 0.4054  1193 TYR B CB  
21450 C CG  . TYR C 1193 ? 1.7275 1.2533 2.0576 -0.6996 -0.6581 0.3848  1193 TYR B CG  
21451 C CD1 . TYR C 1193 ? 1.7411 1.2731 2.0678 -0.7009 -0.6100 0.3843  1193 TYR B CD1 
21452 C CD2 . TYR C 1193 ? 1.7129 1.1778 2.0030 -0.6873 -0.6585 0.3679  1193 TYR B CD2 
21453 C CE1 . TYR C 1193 ? 1.7460 1.2232 2.0281 -0.6894 -0.5625 0.3687  1193 TYR B CE1 
21454 C CE2 . TYR C 1193 ? 1.7220 1.1274 1.9668 -0.6753 -0.6107 0.3530  1193 TYR B CE2 
21455 C CZ  . TYR C 1193 ? 1.7262 1.1380 1.9663 -0.6761 -0.5624 0.3541  1193 TYR B CZ  
21456 O OH  . TYR C 1193 ? 1.7089 1.0590 1.8981 -0.6621 -0.5139 0.3428  1193 TYR B OH  
21457 N N   . ALA C 1194 ? 2.3915 2.0547 2.7711 -0.7259 -0.7073 0.4126  1194 ALA B N   
21458 C CA  . ALA C 1194 ? 2.3759 2.0348 2.7402 -0.7238 -0.6932 0.4011  1194 ALA B CA  
21459 C C   . ALA C 1194 ? 2.3425 2.0646 2.7228 -0.7374 -0.6551 0.4055  1194 ALA B C   
21460 O O   . ALA C 1194 ? 2.3321 2.0429 2.6959 -0.7350 -0.6123 0.3913  1194 ALA B O   
21461 C CB  . ALA C 1194 ? 2.4003 2.0510 2.7648 -0.7204 -0.7476 0.4052  1194 ALA B CB  
21462 N N   . LEU C 1195 ? 1.7064 1.4898 2.1154 -0.7517 -0.6706 0.4253  1195 LEU B N   
21463 C CA  . LEU C 1195 ? 1.6957 1.5379 2.1162 -0.7662 -0.6339 0.4287  1195 LEU B CA  
21464 C C   . LEU C 1195 ? 1.7036 1.5388 2.1122 -0.7657 -0.5835 0.4204  1195 LEU B C   
21465 O O   . LEU C 1195 ? 1.7262 1.5739 2.1245 -0.7689 -0.5377 0.4093  1195 LEU B O   
21466 C CB  . LEU C 1195 ? 1.6828 1.5798 2.1289 -0.7820 -0.6615 0.4533  1195 LEU B CB  
21467 C CG  . LEU C 1195 ? 1.7184 1.5991 2.1686 -0.7775 -0.7178 0.4625  1195 LEU B CG  
21468 C CD1 . LEU C 1195 ? 1.7469 1.6601 2.2175 -0.7905 -0.7548 0.4903  1195 LEU B CD1 
21469 C CD2 . LEU C 1195 ? 1.7273 1.6164 2.1728 -0.7765 -0.7170 0.4529  1195 LEU B CD2 
21470 N N   . SER C 1196 ? 1.0021 0.8140 1.4108 -0.7609 -0.5929 0.4254  1196 SER B N   
21471 C CA  . SER C 1196 ? 1.0218 0.8170 1.4159 -0.7575 -0.5495 0.4180  1196 SER B CA  
21472 C C   . SER C 1196 ? 1.0599 0.8179 1.4208 -0.7486 -0.5013 0.3971  1196 SER B C   
21473 O O   . SER C 1196 ? 1.0319 0.7968 1.3787 -0.7509 -0.4532 0.3920  1196 SER B O   
21474 C CB  . SER C 1196 ? 1.0144 0.7654 1.4073 -0.7473 -0.5723 0.4196  1196 SER B CB  
21475 O OG  . SER C 1196 ? 1.0167 0.7637 1.4020 -0.7467 -0.5345 0.4178  1196 SER B OG  
21476 N N   . LEU C 1197 ? 2.2226 1.9382 2.5681 -0.7385 -0.5145 0.3861  1197 LEU B N   
21477 C CA  . LEU C 1197 ? 2.3426 2.0133 2.6535 -0.7290 -0.4699 0.3689  1197 LEU B CA  
21478 C C   . LEU C 1197 ? 2.4185 2.1261 2.7381 -0.7371 -0.4519 0.3650  1197 LEU B C   
21479 O O   . LEU C 1197 ? 2.4261 2.0964 2.7290 -0.7290 -0.4448 0.3544  1197 LEU B O   
21480 C CB  . LEU C 1197 ? 2.3900 1.9752 2.6678 -0.7108 -0.4862 0.3581  1197 LEU B CB  
21481 C CG  . LEU C 1197 ? 2.4316 1.9653 2.6909 -0.7001 -0.4941 0.3569  1197 LEU B CG  
21482 C CD1 . LEU C 1197 ? 2.4760 1.9285 2.7037 -0.6837 -0.5256 0.3474  1197 LEU B CD1 
21483 C CD2 . LEU C 1197 ? 2.4418 1.9523 2.6721 -0.6948 -0.4371 0.3524  1197 LEU B CD2 
21484 N N   . GLY C 1198 ? 2.5932 2.3709 2.9371 -0.7533 -0.4431 0.3736  1198 GLY B N   
21485 C CA  . GLY C 1198 ? 2.6747 2.4916 3.0274 -0.7629 -0.4220 0.3685  1198 GLY B CA  
21486 C C   . GLY C 1198 ? 2.7215 2.6033 3.0871 -0.7804 -0.4002 0.3752  1198 GLY B C   
21487 O O   . GLY C 1198 ? 2.7552 2.6352 3.1054 -0.7817 -0.3658 0.3734  1198 GLY B O   
21488 N N   . ASP C 1199 ? 2.3658 2.3026 2.7557 -0.7942 -0.4200 0.3828  1199 ASP B N   
21489 C CA  . ASP C 1199 ? 2.3405 2.3385 2.7407 -0.8133 -0.4095 0.3919  1199 ASP B CA  
21490 C C   . ASP C 1199 ? 2.2300 2.2447 2.6429 -0.8188 -0.4436 0.4134  1199 ASP B C   
21491 O O   . ASP C 1199 ? 2.2262 2.2596 2.6584 -0.8236 -0.4891 0.4298  1199 ASP B O   
21492 C CB  . ASP C 1199 ? 2.4297 2.4772 2.8476 -0.8271 -0.4187 0.3930  1199 ASP B CB  
21493 C CG  . ASP C 1199 ? 2.5222 2.6284 2.9474 -0.8484 -0.4172 0.4054  1199 ASP B CG  
21494 O OD1 . ASP C 1199 ? 2.5187 2.6267 2.9334 -0.8522 -0.3997 0.4096  1199 ASP B OD1 
21495 O OD2 . ASP C 1199 ? 2.5947 2.7441 3.0344 -0.8620 -0.4337 0.4115  1199 ASP B OD2 
21496 N N   . LYS C 1200 ? 2.2879 2.2947 2.6890 -0.8184 -0.4195 0.4141  1200 LYS B N   
21497 C CA  . LYS C 1200 ? 2.2294 2.2429 2.6425 -0.8211 -0.4460 0.4329  1200 LYS B CA  
21498 C C   . LYS C 1200 ? 2.3024 2.3768 2.7285 -0.8429 -0.4525 0.4499  1200 LYS B C   
21499 O O   . LYS C 1200 ? 2.3652 2.4512 2.7997 -0.8486 -0.4645 0.4662  1200 LYS B O   
21500 C CB  . LYS C 1200 ? 2.1555 2.1359 2.5491 -0.8118 -0.4127 0.4252  1200 LYS B CB  
21501 C CG  . LYS C 1200 ? 2.1774 2.1268 2.5407 -0.8033 -0.3622 0.4021  1200 LYS B CG  
21502 C CD  . LYS C 1200 ? 2.2029 2.0908 2.5441 -0.7853 -0.3474 0.3940  1200 LYS B CD  
21503 C CE  . LYS C 1200 ? 2.2290 2.1263 2.5730 -0.7882 -0.3441 0.4049  1200 LYS B CE  
21504 N NZ  . LYS C 1200 ? 2.2240 2.0615 2.5496 -0.7711 -0.3369 0.3988  1200 LYS B NZ  
21505 N N   . THR C 1201 ? 2.3849 2.4970 2.8123 -0.8561 -0.4447 0.4463  1201 THR B N   
21506 C CA  . THR C 1201 ? 2.3825 2.5515 2.8136 -0.8797 -0.4419 0.4588  1201 THR B CA  
21507 C C   . THR C 1201 ? 2.4302 2.6404 2.8767 -0.8952 -0.4730 0.4718  1201 THR B C   
21508 O O   . THR C 1201 ? 2.4700 2.7266 2.9163 -0.9169 -0.4707 0.4821  1201 THR B O   
21509 C CB  . THR C 1201 ? 2.3705 2.5561 2.7800 -0.8888 -0.3891 0.4403  1201 THR B CB  
21510 O OG1 . THR C 1201 ? 2.3571 2.5256 2.7598 -0.8805 -0.3667 0.4180  1201 THR B OG1 
21511 C CG2 . THR C 1201 ? 2.3280 2.4887 2.7193 -0.8818 -0.3586 0.4353  1201 THR B CG2 
21512 N N   . HIS C 1202 ? 1.8169 2.0100 2.2740 -0.8852 -0.5018 0.4714  1202 HIS B N   
21513 C CA  . HIS C 1202 ? 1.8950 2.1227 2.3660 -0.8985 -0.5366 0.4870  1202 HIS B CA  
21514 C C   . HIS C 1202 ? 1.9567 2.2020 2.4385 -0.9109 -0.5722 0.5171  1202 HIS B C   
21515 O O   . HIS C 1202 ? 1.9362 2.1488 2.4271 -0.8996 -0.6043 0.5296  1202 HIS B O   
21516 C CB  . HIS C 1202 ? 1.8641 2.0618 2.3432 -0.8832 -0.5680 0.4845  1202 HIS B CB  
21517 C CG  . HIS C 1202 ? 1.9270 2.1604 2.4170 -0.8964 -0.5975 0.4971  1202 HIS B CG  
21518 N ND1 . HIS C 1202 ? 1.9547 2.1945 2.4476 -0.8933 -0.5946 0.4831  1202 HIS B ND1 
21519 C CD2 . HIS C 1202 ? 1.9667 2.2329 2.4647 -0.9145 -0.6281 0.5229  1202 HIS B CD2 
21520 C CE1 . HIS C 1202 ? 1.9858 2.2615 2.4875 -0.9081 -0.6229 0.4992  1202 HIS B CE1 
21521 N NE2 . HIS C 1202 ? 2.0094 2.3004 2.5129 -0.9217 -0.6433 0.5238  1202 HIS B NE2 
21522 N N   . PRO C 1203 ? 2.0111 2.3067 2.4920 -0.9353 -0.5683 0.5289  1203 PRO B N   
21523 C CA  . PRO C 1203 ? 2.0414 2.3543 2.5326 -0.9497 -0.6014 0.5599  1203 PRO B CA  
21524 C C   . PRO C 1203 ? 2.0002 2.2758 2.5067 -0.9359 -0.6491 0.5755  1203 PRO B C   
21525 O O   . PRO C 1203 ? 2.0003 2.2558 2.5164 -0.9318 -0.6682 0.5909  1203 PRO B O   
21526 C CB  . PRO C 1203 ? 2.1335 2.5004 2.6236 -0.9757 -0.6076 0.5697  1203 PRO B CB  
21527 C CG  . PRO C 1203 ? 2.1347 2.5208 2.6100 -0.9791 -0.5605 0.5404  1203 PRO B CG  
21528 C CD  . PRO C 1203 ? 2.0544 2.3927 2.5276 -0.9517 -0.5423 0.5159  1203 PRO B CD  
21529 N N   . GLN C 1204 ? 1.6707 1.9351 2.1795 -0.9284 -0.6675 0.5700  1204 GLN B N   
21530 C CA  . GLN C 1204 ? 1.5979 1.8258 2.1171 -0.9169 -0.7149 0.5836  1204 GLN B CA  
21531 C C   . GLN C 1204 ? 1.4760 1.6490 1.9967 -0.8945 -0.7193 0.5768  1204 GLN B C   
21532 O O   . GLN C 1204 ? 1.4422 1.5946 1.9746 -0.8929 -0.7534 0.5957  1204 GLN B O   
21533 C CB  . GLN C 1204 ? 1.5947 1.8181 2.1119 -0.9108 -0.7281 0.5741  1204 GLN B CB  
21534 C CG  . GLN C 1204 ? 1.5720 1.7552 2.0945 -0.8995 -0.7774 0.5863  1204 GLN B CG  
21535 C CD  . GLN C 1204 ? 1.5844 1.7786 2.1175 -0.9158 -0.8165 0.6192  1204 GLN B CD  
21536 O OE1 . GLN C 1204 ? 1.5911 1.8267 2.1276 -0.9370 -0.8082 0.6343  1204 GLN B OE1 
21537 N NE2 . GLN C 1204 ? 1.5920 1.7469 2.1286 -0.9071 -0.8603 0.6306  1204 GLN B NE2 
21538 N N   . PHE C 1205 ? 1.8018 1.9503 2.3108 -0.8784 -0.6847 0.5497  1205 PHE B N   
21539 C CA  . PHE C 1205 ? 1.7458 1.8450 2.2527 -0.8593 -0.6820 0.5408  1205 PHE B CA  
21540 C C   . PHE C 1205 ? 1.7540 1.8629 2.2735 -0.8679 -0.6912 0.5615  1205 PHE B C   
21541 O O   . PHE C 1205 ? 1.7499 1.8237 2.2797 -0.8578 -0.7192 0.5693  1205 PHE B O   
21542 C CB  . PHE C 1205 ? 1.5802 1.6649 2.0692 -0.8488 -0.6304 0.5120  1205 PHE B CB  
21543 C CG  . PHE C 1205 ? 1.5071 1.5497 1.9897 -0.8339 -0.6151 0.5028  1205 PHE B CG  
21544 C CD1 . PHE C 1205 ? 1.4927 1.4797 1.9712 -0.8148 -0.6349 0.4939  1205 PHE B CD1 
21545 C CD2 . PHE C 1205 ? 1.4644 1.5227 1.9416 -0.8397 -0.5787 0.5014  1205 PHE B CD2 
21546 C CE1 . PHE C 1205 ? 1.4596 1.4090 1.9302 -0.8029 -0.6181 0.4844  1205 PHE B CE1 
21547 C CE2 . PHE C 1205 ? 1.4251 1.4468 1.8956 -0.8269 -0.5622 0.4932  1205 PHE B CE2 
21548 C CZ  . PHE C 1205 ? 1.4236 1.3917 1.8913 -0.8089 -0.5809 0.4847  1205 PHE B CZ  
21549 N N   . ARG C 1206 ? 1.4131 1.5701 1.9324 -0.8877 -0.6703 0.5708  1206 ARG B N   
21550 C CA  . ARG C 1206 ? 1.4381 1.6100 1.9695 -0.8984 -0.6768 0.5918  1206 ARG B CA  
21551 C C   . ARG C 1206 ? 1.4511 1.6138 2.0033 -0.9027 -0.7308 0.6195  1206 ARG B C   
21552 O O   . ARG C 1206 ? 1.4278 1.5740 1.9962 -0.9000 -0.7481 0.6331  1206 ARG B O   
21553 C CB  . ARG C 1206 ? 1.5230 1.7516 2.0475 -0.9233 -0.6538 0.6000  1206 ARG B CB  
21554 C CG  . ARG C 1206 ? 1.5745 1.8175 2.0769 -0.9240 -0.6015 0.5740  1206 ARG B CG  
21555 C CD  . ARG C 1206 ? 1.6419 1.8700 2.1370 -0.9166 -0.5698 0.5653  1206 ARG B CD  
21556 N NE  . ARG C 1206 ? 1.6971 1.9255 2.1676 -0.9135 -0.5187 0.5375  1206 ARG B NE  
21557 C CZ  . ARG C 1206 ? 1.7683 2.0257 2.2258 -0.9252 -0.4974 0.5253  1206 ARG B CZ  
21558 N NH1 . ARG C 1206 ? 1.8152 2.1077 2.2808 -0.9416 -0.5218 0.5382  1206 ARG B NH1 
21559 N NH2 . ARG C 1206 ? 1.7590 2.0095 2.1949 -0.9212 -0.4504 0.4999  1206 ARG B NH2 
21560 N N   . SER C 1207 ? 1.7832 1.9570 2.3353 -0.9104 -0.7568 0.6280  1207 SER B N   
21561 C CA  . SER C 1207 ? 1.7907 1.9560 2.3588 -0.9174 -0.8081 0.6553  1207 SER B CA  
21562 C C   . SER C 1207 ? 1.7303 1.8349 2.3043 -0.8940 -0.8343 0.6479  1207 SER B C   
21563 O O   . SER C 1207 ? 1.7498 1.8324 2.3413 -0.8925 -0.8637 0.6640  1207 SER B O   
21564 C CB  . SER C 1207 ? 1.8308 2.0215 2.3930 -0.9310 -0.8254 0.6634  1207 SER B CB  
21565 O OG  . SER C 1207 ? 1.8668 2.0643 2.4421 -0.9473 -0.8686 0.6956  1207 SER B OG  
21566 N N   . ILE C 1208 ? 1.7747 1.8508 2.3337 -0.8760 -0.8236 0.6223  1208 ILE B N   
21567 C CA  . ILE C 1208 ? 1.6641 1.6806 2.2228 -0.8546 -0.8488 0.6123  1208 ILE B CA  
21568 C C   . ILE C 1208 ? 1.5656 1.5589 2.1336 -0.8450 -0.8378 0.6078  1208 ILE B C   
21569 O O   . ILE C 1208 ? 1.5344 1.4985 2.1181 -0.8406 -0.8721 0.6193  1208 ILE B O   
21570 C CB  . ILE C 1208 ? 1.6088 1.6003 2.1465 -0.8382 -0.8343 0.5844  1208 ILE B CB  
21571 C CG1 . ILE C 1208 ? 1.5880 1.6263 2.1175 -0.8506 -0.8090 0.5801  1208 ILE B CG1 
21572 C CG2 . ILE C 1208 ? 1.6284 1.5704 2.1615 -0.8253 -0.8811 0.5842  1208 ILE B CG2 
21573 C CD1 . ILE C 1208 ? 1.5544 1.5747 2.0688 -0.8385 -0.8078 0.5599  1208 ILE B CD1 
21574 N N   . VAL C 1209 ? 1.0147 1.0219 1.5735 -0.8428 -0.7892 0.5913  1209 VAL B N   
21575 C CA  . VAL C 1209 ? 1.0386 1.0290 1.6040 -0.8350 -0.7707 0.5858  1209 VAL B CA  
21576 C C   . VAL C 1209 ? 1.1545 1.1612 1.7473 -0.8474 -0.7975 0.6146  1209 VAL B C   
21577 O O   . VAL C 1209 ? 1.1493 1.1297 1.7578 -0.8391 -0.8075 0.6162  1209 VAL B O   
21578 C CB  . VAL C 1209 ? 1.0190 1.0346 1.5686 -0.8378 -0.7122 0.5703  1209 VAL B CB  
21579 C CG1 . VAL C 1209 ? 0.9964 0.9978 1.5524 -0.8316 -0.6923 0.5673  1209 VAL B CG1 
21580 C CG2 . VAL C 1209 ? 1.0040 1.0003 1.5277 -0.8261 -0.6841 0.5422  1209 VAL B CG2 
21581 N N   . SER C 1210 ? 1.6475 1.6980 2.2461 -0.8685 -0.8087 0.6373  1210 SER B N   
21582 C CA  . SER C 1210 ? 1.7527 1.8197 2.3765 -0.8835 -0.8377 0.6683  1210 SER B CA  
21583 C C   . SER C 1210 ? 1.8106 1.8324 2.4507 -0.8744 -0.8885 0.6773  1210 SER B C   
21584 O O   . SER C 1210 ? 1.8254 1.8230 2.4865 -0.8677 -0.9034 0.6824  1210 SER B O   
21585 C CB  . SER C 1210 ? 1.8284 1.9464 2.4495 -0.9094 -0.8436 0.6902  1210 SER B CB  
21586 O OG  . SER C 1210 ? 1.8995 2.0064 2.5272 -0.9155 -0.8901 0.7082  1210 SER B OG  
21587 N N   . ALA C 1211 ? 2.0840 2.0938 2.7137 -0.8744 -0.9152 0.6786  1211 ALA B N   
21588 C CA  . ALA C 1211 ? 2.1007 2.0678 2.7411 -0.8687 -0.9667 0.6887  1211 ALA B CA  
21589 C C   . ALA C 1211 ? 2.0420 1.9554 2.6877 -0.8458 -0.9724 0.6692  1211 ALA B C   
21590 O O   . ALA C 1211 ? 2.0376 1.9305 2.7078 -0.8449 -0.9997 0.6814  1211 ALA B O   
21591 C CB  . ALA C 1211 ? 2.1149 2.0716 2.7351 -0.8675 -0.9852 0.6843  1211 ALA B CB  
21592 N N   . LEU C 1212 ? 1.9593 1.8497 2.5819 -0.8282 -0.9467 0.6385  1212 LEU B N   
21593 C CA  . LEU C 1212 ? 1.9365 1.7780 2.5585 -0.8081 -0.9453 0.6167  1212 LEU B CA  
21594 C C   . LEU C 1212 ? 1.9230 1.7792 2.5732 -0.8127 -0.9332 0.6273  1212 LEU B C   
21595 O O   . LEU C 1212 ? 1.9405 1.7681 2.6132 -0.8082 -0.9638 0.6337  1212 LEU B O   
21596 C CB  . LEU C 1212 ? 1.8699 1.6976 2.4619 -0.7942 -0.9040 0.5845  1212 LEU B CB  
21597 C CG  . LEU C 1212 ? 1.8140 1.5959 2.3990 -0.7761 -0.8878 0.5592  1212 LEU B CG  
21598 C CD1 . LEU C 1212 ? 1.8300 1.5599 2.4228 -0.7656 -0.9364 0.5578  1212 LEU B CD1 
21599 C CD2 . LEU C 1212 ? 1.7781 1.5376 2.3276 -0.7639 -0.8534 0.5294  1212 LEU B CD2 
21600 N N   . LYS C 1213 ? 1.1358 1.0376 1.7849 -0.8227 -0.8899 0.6299  1213 LYS B N   
21601 C CA  . LYS C 1213 ? 1.0974 1.0135 1.7682 -0.8257 -0.8706 0.6365  1213 LYS B CA  
21602 C C   . LYS C 1213 ? 1.1878 1.1129 1.8943 -0.8381 -0.9111 0.6680  1213 LYS B C   
21603 O O   . LYS C 1213 ? 1.1810 1.0991 1.9143 -0.8357 -0.9133 0.6735  1213 LYS B O   
21604 C CB  . LYS C 1213 ? 1.0088 0.9735 1.6660 -0.8367 -0.8206 0.6354  1213 LYS B CB  
21605 C CG  . LYS C 1213 ? 0.9668 0.9207 1.6199 -0.8263 -0.7801 0.6173  1213 LYS B CG  
21606 C CD  . LYS C 1213 ? 0.9593 0.9334 1.5801 -0.8273 -0.7287 0.5991  1213 LYS B CD  
21607 C CE  . LYS C 1213 ? 0.9681 0.9581 1.5911 -0.8293 -0.6895 0.5982  1213 LYS B CE  
21608 N NZ  . LYS C 1213 ? 0.9411 0.9328 1.5295 -0.8249 -0.6346 0.5746  1213 LYS B NZ  
21609 N N   . ARG C 1214 ? 2.2766 2.2160 2.9832 -0.8518 -0.9427 0.6887  1214 ARG B N   
21610 C CA  . ARG C 1214 ? 2.4396 2.3795 3.1758 -0.8646 -0.9879 0.7198  1214 ARG B CA  
21611 C C   . ARG C 1214 ? 2.4559 2.3373 3.2089 -0.8479 -1.0247 0.7117  1214 ARG B C   
21612 O O   . ARG C 1214 ? 2.5039 2.3781 3.2911 -0.8510 -1.0474 0.7277  1214 ARG B O   
21613 C CB  . ARG C 1214 ? 2.6180 2.5760 3.3424 -0.8814 -1.0132 0.7390  1214 ARG B CB  
21614 C CG  . ARG C 1214 ? 2.8223 2.7583 3.5694 -0.8901 -1.0697 0.7655  1214 ARG B CG  
21615 C CD  . ARG C 1214 ? 2.9962 2.9600 3.7324 -0.9125 -1.0893 0.7894  1214 ARG B CD  
21616 N NE  . ARG C 1214 ? 3.0604 3.0364 3.7624 -0.9096 -1.0665 0.7711  1214 ARG B NE  
21617 C CZ  . ARG C 1214 ? 3.1449 3.1686 3.8330 -0.9296 -1.0536 0.7827  1214 ARG B CZ  
21618 N NH1 . ARG C 1214 ? 3.2211 3.2838 3.9229 -0.9547 -1.0616 0.8130  1214 ARG B NH1 
21619 N NH2 . ARG C 1214 ? 3.1371 3.1701 3.7981 -0.9252 -1.0331 0.7638  1214 ARG B NH2 
21620 N N   . GLU C 1215 ? 1.6853 1.5242 2.4139 -0.8300 -1.0303 0.6854  1215 GLU B N   
21621 C CA  . GLU C 1215 ? 1.6740 1.4545 2.4099 -0.8167 -1.0751 0.6784  1215 GLU B CA  
21622 C C   . GLU C 1215 ? 1.6043 1.3479 2.3565 -0.7997 -1.0718 0.6584  1215 GLU B C   
21623 O O   . GLU C 1215 ? 1.6416 1.3417 2.4082 -0.7923 -1.1133 0.6570  1215 GLU B O   
21624 C CB  . GLU C 1215 ? 1.6551 1.4028 2.3546 -0.8066 -1.0905 0.6611  1215 GLU B CB  
21625 C CG  . GLU C 1215 ? 1.7109 1.4703 2.4050 -0.8222 -1.1235 0.6854  1215 GLU B CG  
21626 C CD  . GLU C 1215 ? 1.7957 1.5152 2.5068 -0.8235 -1.1801 0.7001  1215 GLU B CD  
21627 O OE1 . GLU C 1215 ? 1.8064 1.4983 2.5415 -0.8148 -1.1935 0.6955  1215 GLU B OE1 
21628 O OE2 . GLU C 1215 ? 1.8559 1.5712 2.5562 -0.8338 -1.2106 0.7157  1215 GLU B OE2 
21629 N N   . ALA C 1216 ? 1.8059 1.5649 2.5544 -0.7944 -1.0230 0.6424  1216 ALA B N   
21630 C CA  . ALA C 1216 ? 1.7201 1.4471 2.4826 -0.7802 -1.0132 0.6229  1216 ALA B CA  
21631 C C   . ALA C 1216 ? 1.7300 1.4480 2.5392 -0.7844 -1.0512 0.6423  1216 ALA B C   
21632 O O   . ALA C 1216 ? 1.7947 1.5332 2.6237 -0.7995 -1.0822 0.6727  1216 ALA B O   
21633 C CB  . ALA C 1216 ? 1.6485 1.4070 2.4073 -0.7814 -0.9545 0.6151  1216 ALA B CB  
21634 N N   . LEU C 1217 ? 1.4792 1.1647 2.3055 -0.7717 -1.0482 0.6243  1217 LEU B N   
21635 C CA  . LEU C 1217 ? 1.4762 1.1533 2.3530 -0.7740 -1.0783 0.6391  1217 LEU B CA  
21636 C C   . LEU C 1217 ? 1.4407 1.1081 2.3293 -0.7641 -1.0416 0.6187  1217 LEU B C   
21637 O O   . LEU C 1217 ? 1.3466 1.0205 2.2038 -0.7593 -0.9933 0.6003  1217 LEU B O   
21638 C CB  . LEU C 1217 ? 1.4893 1.1106 2.3702 -0.7652 -1.1362 0.6320  1217 LEU B CB  
21639 C CG  . LEU C 1217 ? 1.4952 1.0994 2.3333 -0.7642 -1.1590 0.6289  1217 LEU B CG  
21640 C CD1 . LEU C 1217 ? 1.4793 1.0157 2.2901 -0.7444 -1.1828 0.5950  1217 LEU B CD1 
21641 C CD2 . LEU C 1217 ? 1.5684 1.1888 2.4222 -0.7816 -1.2011 0.6650  1217 LEU B CD2 
21642 N N   . VAL C 1218 ? 1.2942 0.9439 2.2268 -0.7613 -1.0621 0.6215  1218 VAL B N   
21643 C CA  . VAL C 1218 ? 1.2995 0.9537 2.2481 -0.7566 -1.0192 0.6100  1218 VAL B CA  
21644 C C   . VAL C 1218 ? 1.3023 0.9391 2.3053 -0.7537 -1.0381 0.6125  1218 VAL B C   
21645 O O   . VAL C 1218 ? 1.2940 0.9252 2.3349 -0.7587 -1.0877 0.6312  1218 VAL B O   
21646 C CB  . VAL C 1218 ? 1.3641 1.0821 2.3195 -0.7713 -0.9803 0.6342  1218 VAL B CB  
21647 C CG1 . VAL C 1218 ? 1.3294 1.0579 2.2330 -0.7680 -0.9278 0.6155  1218 VAL B CG1 
21648 C CG2 . VAL C 1218 ? 1.4686 1.2238 2.4383 -0.7893 -1.0140 0.6709  1218 VAL B CG2 
21649 N N   . LYS C 1219 ? 1.6563 1.2881 2.6637 -0.7474 -0.9941 0.5964  1219 LYS B N   
21650 C CA  . LYS C 1219 ? 1.8125 1.4129 2.8622 -0.7400 -1.0030 0.5862  1219 LYS B CA  
21651 C C   . LYS C 1219 ? 1.8910 1.5330 2.9783 -0.7475 -0.9645 0.6042  1219 LYS B C   
21652 O O   . LYS C 1219 ? 1.8760 1.5305 2.9344 -0.7458 -0.9088 0.5951  1219 LYS B O   
21653 C CB  . LYS C 1219 ? 1.8600 1.3914 2.8695 -0.7218 -0.9875 0.5414  1219 LYS B CB  
21654 C CG  . LYS C 1219 ? 2.6944 2.1637 3.6827 -0.7109 -1.0427 0.5188  1219 LYS B CG  
21655 C CD  . LYS C 1219 ? 2.5246 1.9202 3.4509 -0.6934 -1.0226 0.4731  1219 LYS B CD  
21656 C CE  . LYS C 1219 ? 2.3495 1.6831 3.2470 -0.6824 -1.0784 0.4507  1219 LYS B CE  
21657 N NZ  . LYS C 1219 ? 2.3391 1.6032 3.1633 -0.6668 -1.0550 0.4106  1219 LYS B NZ  
21658 N N   . GLY C 1220 ? 3.0457 2.7053 4.1962 -0.7553 -0.9954 0.6299  1220 GLY B N   
21659 C CA  . GLY C 1220 ? 3.0544 2.7543 4.2463 -0.7631 -0.9657 0.6512  1220 GLY B CA  
21660 C C   . GLY C 1220 ? 3.0625 2.8276 4.2384 -0.7788 -0.9384 0.6804  1220 GLY B C   
21661 O O   . GLY C 1220 ? 3.0462 2.8211 4.1666 -0.7792 -0.9142 0.6714  1220 GLY B O   
21662 N N   . ASN C 1221 ? 2.0999 1.9072 3.3236 -0.7921 -0.9438 0.7149  1221 ASN B N   
21663 C CA  . ASN C 1221 ? 2.1049 1.9731 3.3144 -0.8087 -0.9192 0.7435  1221 ASN B CA  
21664 C C   . ASN C 1221 ? 2.0392 1.9313 3.2581 -0.8085 -0.8683 0.7455  1221 ASN B C   
21665 O O   . ASN C 1221 ? 2.0526 1.9293 3.3176 -0.8026 -0.8684 0.7444  1221 ASN B O   
21666 C CB  . ASN C 1221 ? 2.1946 2.0923 3.4425 -0.8272 -0.9666 0.7849  1221 ASN B CB  
21667 C CG  . ASN C 1221 ? 2.2120 2.1703 3.4406 -0.8470 -0.9452 0.8144  1221 ASN B CG  
21668 O OD1 . ASN C 1221 ? 2.2325 2.2243 3.4971 -0.8587 -0.9425 0.8423  1221 ASN B OD1 
21669 N ND2 . ASN C 1221 ? 2.1972 2.1688 3.3692 -0.8514 -0.9316 0.8079  1221 ASN B ND2 
21670 N N   . PRO C 1222 ? 1.7291 1.6554 2.9013 -0.8141 -0.8233 0.7463  1222 PRO B N   
21671 C CA  . PRO C 1222 ? 1.6784 1.6152 2.7929 -0.8183 -0.8176 0.7395  1222 PRO B CA  
21672 C C   . PRO C 1222 ? 1.6462 1.5287 2.7253 -0.8007 -0.8179 0.7015  1222 PRO B C   
21673 O O   . PRO C 1222 ? 1.6666 1.5052 2.7622 -0.7868 -0.8184 0.6807  1222 PRO B O   
21674 C CB  . PRO C 1222 ? 1.6563 1.6292 2.7319 -0.8231 -0.7603 0.7387  1222 PRO B CB  
21675 C CG  . PRO C 1222 ? 1.6747 1.6718 2.7949 -0.8287 -0.7498 0.7605  1222 PRO B CG  
21676 C CD  . PRO C 1222 ? 1.6915 1.6470 2.8630 -0.8166 -0.7746 0.7527  1222 PRO B CD  
21677 N N   . PRO C 1223 ? 2.2021 2.0851 3.2335 -0.8019 -0.8190 0.6925  1223 PRO B N   
21678 C CA  . PRO C 1223 ? 2.0968 1.9283 3.0889 -0.7853 -0.8126 0.6558  1223 PRO B CA  
21679 C C   . PRO C 1223 ? 2.0025 1.8003 2.9749 -0.7708 -0.7648 0.6268  1223 PRO B C   
21680 O O   . PRO C 1223 ? 1.9461 1.7673 2.8907 -0.7728 -0.7142 0.6253  1223 PRO B O   
21681 C CB  . PRO C 1223 ? 2.0676 1.9220 3.0082 -0.7914 -0.7984 0.6541  1223 PRO B CB  
21682 C CG  . PRO C 1223 ? 2.1368 2.0354 3.1003 -0.8102 -0.8312 0.6900  1223 PRO B CG  
21683 C CD  . PRO C 1223 ? 2.2178 2.1398 3.2347 -0.8184 -0.8373 0.7159  1223 PRO B CD  
21684 N N   . ILE C 1224 ? 1.8638 1.6043 2.8476 -0.7571 -0.7817 0.6045  1224 ILE B N   
21685 C CA  . ILE C 1224 ? 1.8124 1.5029 2.7618 -0.7422 -0.7404 0.5721  1224 ILE B CA  
21686 C C   . ILE C 1224 ? 1.8001 1.4341 2.6966 -0.7303 -0.7496 0.5404  1224 ILE B C   
21687 O O   . ILE C 1224 ? 1.7842 1.3839 2.6285 -0.7207 -0.7067 0.5167  1224 ILE B O   
21688 C CB  . ILE C 1224 ? 1.8050 1.4619 2.7967 -0.7349 -0.7428 0.5658  1224 ILE B CB  
21689 C CG1 . ILE C 1224 ? 1.8520 1.5612 2.9024 -0.7463 -0.7414 0.5985  1224 ILE B CG1 
21690 C CG2 . ILE C 1224 ? 1.7465 1.3594 2.6951 -0.7225 -0.6874 0.5397  1224 ILE B CG2 
21691 C CD1 . ILE C 1224 ? 1.8898 1.5684 2.9696 -0.7381 -0.7220 0.5896  1224 ILE B CD1 
21692 N N   . TYR C 1225 ? 1.6067 1.2285 2.5134 -0.7307 -0.8055 0.5418  1225 TYR B N   
21693 C CA  . TYR C 1225 ? 1.5833 1.1604 2.4394 -0.7214 -0.8193 0.5170  1225 TYR B CA  
21694 C C   . TYR C 1225 ? 1.5633 1.1761 2.4178 -0.7310 -0.8540 0.5359  1225 TYR B C   
21695 O O   . TYR C 1225 ? 1.5875 1.2199 2.4832 -0.7388 -0.8991 0.5589  1225 TYR B O   
21696 C CB  . TYR C 1225 ? 1.6372 1.1422 2.4950 -0.7081 -0.8568 0.4921  1225 TYR B CB  
21697 C CG  . TYR C 1225 ? 1.6686 1.1274 2.5288 -0.6981 -0.8276 0.4727  1225 TYR B CG  
21698 C CD1 . TYR C 1225 ? 1.6751 1.0817 2.4742 -0.6859 -0.7801 0.4454  1225 TYR B CD1 
21699 C CD2 . TYR C 1225 ? 1.7107 1.1729 2.6321 -0.7001 -0.8466 0.4829  1225 TYR B CD2 
21700 C CE1 . TYR C 1225 ? 1.7061 1.0625 2.5004 -0.6755 -0.7503 0.4295  1225 TYR B CE1 
21701 C CE2 . TYR C 1225 ? 1.7402 1.1570 2.6637 -0.6905 -0.8179 0.4652  1225 TYR B CE2 
21702 C CZ  . TYR C 1225 ? 1.7285 1.0913 2.5859 -0.6780 -0.7687 0.4389  1225 TYR B CZ  
21703 O OH  . TYR C 1225 ? 1.7464 1.0575 2.5991 -0.6671 -0.7375 0.4237  1225 TYR B OH  
21704 N N   . ARG C 1226 ? 1.5611 1.1781 2.3659 -0.7303 -0.8316 0.5265  1226 ARG B N   
21705 C CA  . ARG C 1226 ? 1.6235 1.2657 2.4182 -0.7379 -0.8606 0.5402  1226 ARG B CA  
21706 C C   . ARG C 1226 ? 1.6405 1.2279 2.3903 -0.7253 -0.8762 0.5127  1226 ARG B C   
21707 O O   . ARG C 1226 ? 1.6256 1.1769 2.3348 -0.7152 -0.8403 0.4869  1226 ARG B O   
21708 C CB  . ARG C 1226 ? 1.6533 1.3484 2.4251 -0.7481 -0.8183 0.5508  1226 ARG B CB  
21709 C CG  . ARG C 1226 ? 1.6884 1.4051 2.4442 -0.7556 -0.8429 0.5618  1226 ARG B CG  
21710 C CD  . ARG C 1226 ? 1.6622 1.4444 2.4127 -0.7717 -0.8125 0.5821  1226 ARG B CD  
21711 N NE  . ARG C 1226 ? 1.6223 1.4344 2.3804 -0.7764 -0.7668 0.5871  1226 ARG B NE  
21712 C CZ  . ARG C 1226 ? 1.5690 1.4230 2.3629 -0.7896 -0.7709 0.6148  1226 ARG B CZ  
21713 N NH1 . ARG C 1226 ? 1.5552 1.4257 2.3821 -0.8005 -0.8181 0.6417  1226 ARG B NH1 
21714 N NH2 . ARG C 1226 ? 1.5313 1.4084 2.3252 -0.7925 -0.7277 0.6166  1226 ARG B NH2 
21715 N N   . PHE C 1227 ? 1.7446 1.3219 2.4963 -0.7258 -0.9284 0.5191  1227 PHE B N   
21716 C CA  . PHE C 1227 ? 1.7153 1.2459 2.4185 -0.7149 -0.9435 0.4954  1227 PHE B CA  
21717 C C   . PHE C 1227 ? 1.7221 1.2678 2.4294 -0.7214 -0.9917 0.5147  1227 PHE B C   
21718 O O   . PHE C 1227 ? 1.7417 1.3250 2.4877 -0.7340 -1.0147 0.5450  1227 PHE B O   
21719 C CB  . PHE C 1227 ? 1.7544 1.2073 2.4388 -0.6982 -0.9598 0.4637  1227 PHE B CB  
21720 C CG  . PHE C 1227 ? 1.8238 1.2591 2.5513 -0.6972 -1.0067 0.4699  1227 PHE B CG  
21721 C CD1 . PHE C 1227 ? 1.8530 1.2748 2.5863 -0.6972 -1.0669 0.4784  1227 PHE B CD1 
21722 C CD2 . PHE C 1227 ? 1.8285 1.2567 2.5896 -0.6958 -0.9902 0.4668  1227 PHE B CD2 
21723 C CE1 . PHE C 1227 ? 1.8722 1.2737 2.6444 -0.6959 -1.1114 0.4835  1227 PHE B CE1 
21724 C CE2 . PHE C 1227 ? 1.8373 1.2469 2.6414 -0.6944 -1.0344 0.4709  1227 PHE B CE2 
21725 C CZ  . PHE C 1227 ? 1.8680 1.2639 2.6778 -0.6945 -1.0960 0.4790  1227 PHE B CZ  
21726 N N   . TRP C 1228 ? 1.3006 0.8161 1.9656 -0.7140 -1.0058 0.4993  1228 TRP B N   
21727 C CA  . TRP C 1228 ? 1.3527 0.8816 2.0199 -0.7211 -1.0498 0.5199  1228 TRP B CA  
21728 C C   . TRP C 1228 ? 1.6193 1.0824 2.2667 -0.7075 -1.0980 0.5015  1228 TRP B C   
21729 O O   . TRP C 1228 ? 1.6038 1.0170 2.2332 -0.6940 -1.0905 0.4722  1228 TRP B O   
21730 C CB  . TRP C 1228 ? 1.3117 0.8696 1.9483 -0.7262 -1.0284 0.5227  1228 TRP B CB  
21731 C CG  . TRP C 1228 ? 1.2998 0.9226 1.9457 -0.7396 -0.9775 0.5371  1228 TRP B CG  
21732 C CD1 . TRP C 1228 ? 1.3222 0.9963 1.9706 -0.7545 -0.9741 0.5598  1228 TRP B CD1 
21733 C CD2 . TRP C 1228 ? 1.2642 0.9027 1.9107 -0.7391 -0.9228 0.5274  1228 TRP B CD2 
21734 N NE1 . TRP C 1228 ? 1.2888 1.0087 1.9383 -0.7627 -0.9232 0.5630  1228 TRP B NE1 
21735 C CE2 . TRP C 1228 ? 1.2567 0.9557 1.9048 -0.7532 -0.8913 0.5442  1228 TRP B CE2 
21736 C CE3 . TRP C 1228 ? 1.2219 0.8263 1.8643 -0.7285 -0.8965 0.5062  1228 TRP B CE3 
21737 C CZ2 . TRP C 1228 ? 1.2102 0.9362 1.8552 -0.7564 -0.8374 0.5405  1228 TRP B CZ2 
21738 C CZ3 . TRP C 1228 ? 1.1786 0.8110 1.8188 -0.7323 -0.8400 0.5049  1228 TRP B CZ3 
21739 C CH2 . TRP C 1228 ? 1.1690 0.8612 1.8101 -0.7457 -0.8125 0.5217  1228 TRP B CH2 
21740 N N   . LYS C 1229 ? 1.7870 1.2462 2.4336 -0.7117 -1.1461 0.5184  1229 LYS B N   
21741 C CA  . LYS C 1229 ? 1.8609 1.2572 2.4889 -0.6999 -1.1996 0.5048  1229 LYS B CA  
21742 C C   . LYS C 1229 ? 1.9758 1.3562 2.5579 -0.6968 -1.2189 0.5019  1229 LYS B C   
21743 O O   . LYS C 1229 ? 1.9708 1.3950 2.5477 -0.7069 -1.1975 0.5168  1229 LYS B O   
21744 C CB  . LYS C 1229 ? 1.8952 1.2940 2.5671 -0.7086 -1.2458 0.5311  1229 LYS B CB  
21745 C CG  . LYS C 1229 ? 1.9583 1.2956 2.6337 -0.6953 -1.2844 0.5108  1229 LYS B CG  
21746 C CD  . LYS C 1229 ? 2.4254 1.7762 3.1590 -0.7059 -1.3157 0.5379  1229 LYS B CD  
21747 C CE  . LYS C 1229 ? 2.4141 1.7749 3.1540 -0.7201 -1.3584 0.5720  1229 LYS B CE  
21748 N NZ  . LYS C 1229 ? 2.3993 1.6970 3.1161 -0.7109 -1.4153 0.5617  1229 LYS B NZ  
21749 N N   . ASP C 1230 ? 2.8328 2.1511 3.3805 -0.6832 -1.2589 0.4825  1230 ASP B N   
21750 C CA  . ASP C 1230 ? 2.9391 2.2399 3.4410 -0.6796 -1.2784 0.4800  1230 ASP B CA  
21751 C C   . ASP C 1230 ? 3.0497 2.3948 3.5725 -0.6981 -1.2949 0.5181  1230 ASP B C   
21752 O O   . ASP C 1230 ? 3.0169 2.3928 3.5242 -0.7044 -1.2762 0.5257  1230 ASP B O   
21753 C CB  . ASP C 1230 ? 3.0285 2.2553 3.4907 -0.6636 -1.3266 0.4580  1230 ASP B CB  
21754 C CG  . ASP C 1230 ? 3.1079 2.3133 3.5165 -0.6580 -1.3443 0.4532  1230 ASP B CG  
21755 O OD1 . ASP C 1230 ? 3.1032 2.3533 3.5141 -0.6686 -1.3254 0.4710  1230 ASP B OD1 
21756 O OD2 . ASP C 1230 ? 3.1683 2.3120 3.5309 -0.6429 -1.3768 0.4310  1230 ASP B OD2 
21757 N N   . ASN C 1231 ? 3.6388 2.9859 4.1975 -0.7080 -1.3284 0.5415  1231 ASN B N   
21758 C CA  . ASN C 1231 ? 3.7860 3.1637 4.3606 -0.7278 -1.3501 0.5781  1231 ASN B CA  
21759 C C   . ASN C 1231 ? 3.8358 3.2852 4.4284 -0.7453 -1.3090 0.6001  1231 ASN B C   
21760 O O   . ASN C 1231 ? 3.7798 3.2531 4.3589 -0.7408 -1.2645 0.5853  1231 ASN B O   
21761 C CB  . ASN C 1231 ? 3.8936 3.2609 4.5083 -0.7369 -1.3890 0.5995  1231 ASN B CB  
21762 C CG  . ASN C 1231 ? 3.9180 3.3319 4.5846 -0.7469 -1.3615 0.6148  1231 ASN B CG  
21763 O OD1 . ASN C 1231 ? 3.9064 3.3169 4.5843 -0.7358 -1.3357 0.5941  1231 ASN B OD1 
21764 N ND2 . ASN C 1231 ? 3.9548 3.4120 4.6508 -0.7693 -1.3663 0.6516  1231 ASN B ND2 
21765 N N   . LEU C 1232 ? 2.5280 2.0088 3.1485 -0.7664 -1.3258 0.6352  1232 LEU B N   
21766 C CA  . LEU C 1232 ? 2.5533 2.1016 3.1890 -0.7860 -1.2940 0.6590  1232 LEU B CA  
21767 C C   . LEU C 1232 ? 2.7178 2.2848 3.3865 -0.8083 -1.3240 0.6965  1232 LEU B C   
21768 O O   . LEU C 1232 ? 2.8274 2.3937 3.4850 -0.8218 -1.3514 0.7154  1232 LEU B O   
21769 C CB  . LEU C 1232 ? 2.4346 1.9975 3.0353 -0.7891 -1.2841 0.6571  1232 LEU B CB  
21770 C CG  . LEU C 1232 ? 2.3194 1.9462 2.9321 -0.8136 -1.2674 0.6859  1232 LEU B CG  
21771 C CD1 . LEU C 1232 ? 2.2133 1.8866 2.8201 -0.8125 -1.2112 0.6736  1232 LEU B CD1 
21772 C CD2 . LEU C 1232 ? 2.3263 1.9480 2.9172 -0.8240 -1.2959 0.6991  1232 LEU B CD2 
21773 N N   . GLN C 1233 ? 3.9190 3.5009 4.6275 -0.8129 -1.3198 0.7074  1233 GLN B N   
21774 C CA  . GLN C 1233 ? 4.0557 3.6611 4.7995 -0.8359 -1.3440 0.7452  1233 GLN B CA  
21775 C C   . GLN C 1233 ? 4.2806 3.8417 5.0277 -0.8422 -1.4038 0.7607  1233 GLN B C   
21776 O O   . GLN C 1233 ? 4.3085 3.8884 5.0796 -0.8643 -1.4261 0.7943  1233 GLN B O   
21777 C CB  . GLN C 1233 ? 4.1740 3.8444 4.9160 -0.8592 -1.3186 0.7702  1233 GLN B CB  
21778 C CG  . GLN C 1233 ? 4.3211 3.9927 5.0340 -0.8711 -1.3372 0.7812  1233 GLN B CG  
21779 C CD  . GLN C 1233 ? 4.4173 4.1556 5.1280 -0.8942 -1.3099 0.8024  1233 GLN B CD  
21780 O OE1 . GLN C 1233 ? 4.4963 4.2675 5.2313 -0.9160 -1.3167 0.8326  1233 GLN B OE1 
21781 N NE2 . GLN C 1233 ? 4.4028 4.1616 5.0838 -0.8898 -1.2794 0.7861  1233 GLN B NE2 
21782 N N   . HIS C 1234 ? 3.0333 2.5351 3.7532 -0.8242 -1.4301 0.7366  1234 HIS B N   
21783 C CA  . HIS C 1234 ? 3.1264 2.5781 3.8487 -0.8273 -1.4874 0.7463  1234 HIS B CA  
21784 C C   . HIS C 1234 ? 3.1836 2.6103 3.9446 -0.8176 -1.5029 0.7398  1234 HIS B C   
21785 O O   . HIS C 1234 ? 3.2373 2.6307 4.0168 -0.8229 -1.5489 0.7524  1234 HIS B O   
21786 C CB  . HIS C 1234 ? 3.0890 2.4869 3.7617 -0.8120 -1.5098 0.7223  1234 HIS B CB  
21787 C CG  . HIS C 1234 ? 3.0492 2.4716 3.6871 -0.8210 -1.4955 0.7281  1234 HIS B CG  
21788 N ND1 . HIS C 1234 ? 3.0932 2.5506 3.7372 -0.8477 -1.5047 0.7620  1234 HIS B ND1 
21789 C CD2 . HIS C 1234 ? 2.9942 2.4113 3.5917 -0.8072 -1.4738 0.7039  1234 HIS B CD2 
21790 C CE1 . HIS C 1234 ? 3.0715 2.5461 3.6823 -0.8495 -1.4882 0.7575  1234 HIS B CE1 
21791 N NE2 . HIS C 1234 ? 3.0115 2.4618 3.5949 -0.8249 -1.4698 0.7230  1234 HIS B NE2 
21792 N N   . LYS C 1235 ? 3.1540 2.5972 3.9269 -0.8039 -1.4631 0.7190  1235 LYS B N   
21793 C CA  . LYS C 1235 ? 3.2372 2.6748 4.0550 -0.7976 -1.4647 0.7150  1235 LYS B CA  
21794 C C   . LYS C 1235 ? 3.4239 2.8003 4.2546 -0.7896 -1.5194 0.7087  1235 LYS B C   
21795 O O   . LYS C 1235 ? 3.4894 2.8692 4.3659 -0.8006 -1.5440 0.7312  1235 LYS B O   
21796 C CB  . LYS C 1235 ? 3.2151 2.7120 4.0779 -0.8196 -1.4486 0.7505  1235 LYS B CB  
21797 C CG  . LYS C 1235 ? 3.1179 2.6767 3.9709 -0.8261 -1.3909 0.7533  1235 LYS B CG  
21798 C CD  . LYS C 1235 ? 3.0081 2.5775 3.8743 -0.8106 -1.3482 0.7286  1235 LYS B CD  
21799 C CE  . LYS C 1235 ? 2.9275 2.5614 3.7895 -0.8208 -1.2935 0.7367  1235 LYS B CE  
21800 N NZ  . LYS C 1235 ? 2.8830 2.5281 3.6969 -0.8189 -1.2693 0.7241  1235 LYS B NZ  
21801 N N   . ASP C 1236 ? 3.8340 3.1539 4.6232 -0.7708 -1.5397 0.6781  1236 ASP B N   
21802 C CA  . ASP C 1236 ? 3.9944 3.2536 4.7917 -0.7589 -1.5864 0.6631  1236 ASP B CA  
21803 C C   . ASP C 1236 ? 4.0187 3.2824 4.8544 -0.7464 -1.5645 0.6434  1236 ASP B C   
21804 O O   . ASP C 1236 ? 4.0567 3.2850 4.9200 -0.7391 -1.5962 0.6344  1236 ASP B O   
21805 C CB  . ASP C 1236 ? 4.0518 3.2510 4.7879 -0.7405 -1.6082 0.6315  1236 ASP B CB  
21806 C CG  . ASP C 1236 ? 4.1711 3.3062 4.9077 -0.7324 -1.6650 0.6215  1236 ASP B CG  
21807 O OD1 . ASP C 1236 ? 4.2017 3.3354 4.9899 -0.7336 -1.6793 0.6265  1236 ASP B OD1 
21808 O OD2 . ASP C 1236 ? 4.2360 3.3225 4.9216 -0.7250 -1.6957 0.6091  1236 ASP B OD2 
21809 N N   . SER C 1237 ? 3.9009 3.2089 4.7373 -0.7448 -1.5084 0.6363  1237 SER B N   
21810 C CA  . SER C 1237 ? 3.8911 3.2161 4.7645 -0.7376 -1.4756 0.6222  1237 SER B CA  
21811 C C   . SER C 1237 ? 3.9010 3.1674 4.7600 -0.7142 -1.4856 0.5784  1237 SER B C   
21812 O O   . SER C 1237 ? 3.9245 3.1947 4.8167 -0.7083 -1.4644 0.5641  1237 SER B O   
21813 C CB  . SER C 1237 ? 3.9190 3.2758 4.8595 -0.7537 -1.4868 0.6558  1237 SER B CB  
21814 O OG  . SER C 1237 ? 3.8575 3.2501 4.8310 -0.7520 -1.4414 0.6505  1237 SER B OG  
21815 N N   . SER C 1238 ? 5.4241 4.9361 6.0132 -0.5241 -1.0373 0.3342  1238 SER B N   
21816 C CA  . SER C 1238 ? 5.3993 4.8423 5.9833 -0.5240 -1.0805 0.3185  1238 SER B CA  
21817 C C   . SER C 1238 ? 5.3376 4.7195 5.9379 -0.5499 -1.1273 0.3334  1238 SER B C   
21818 O O   . SER C 1238 ? 5.2983 4.6214 5.8738 -0.5627 -1.1812 0.3429  1238 SER B O   
21819 C CB  . SER C 1238 ? 5.4731 4.9151 5.9939 -0.4957 -1.0616 0.2871  1238 SER B CB  
21820 O OG  . SER C 1238 ? 5.5040 4.9594 5.9888 -0.4930 -1.0487 0.2893  1238 SER B OG  
21821 N N   . VAL C 1239 ? 3.2172 2.4009 4.0055 -0.6711 -1.4307 0.4775  1239 VAL B N   
21822 C CA  . VAL C 1239 ? 3.1042 2.2809 3.8662 -0.6617 -1.3762 0.4460  1239 VAL B CA  
21823 C C   . VAL C 1239 ? 3.0796 2.1946 3.8416 -0.6471 -1.3842 0.4086  1239 VAL B C   
21824 O O   . VAL C 1239 ? 3.0267 2.1454 3.8079 -0.6458 -1.3405 0.3956  1239 VAL B O   
21825 C CB  . VAL C 1239 ? 3.0640 2.3096 3.8679 -0.6747 -1.3201 0.4673  1239 VAL B CB  
21826 C CG1 . VAL C 1239 ? 3.0774 2.3838 3.8865 -0.6912 -1.3142 0.5057  1239 VAL B CG1 
21827 C CG2 . VAL C 1239 ? 3.1131 2.3740 3.9870 -0.6802 -1.3244 0.4794  1239 VAL B CG2 
21828 N N   . PRO C 1240 ? 4.1422 3.1960 4.8775 -0.6361 -1.4378 0.3904  1240 PRO B N   
21829 C CA  . PRO C 1240 ? 4.1796 3.1800 4.9332 -0.6260 -1.4602 0.3638  1240 PRO B CA  
21830 C C   . PRO C 1240 ? 4.0810 3.0460 4.8189 -0.6161 -1.4072 0.3272  1240 PRO B C   
21831 O O   . PRO C 1240 ? 4.1575 3.0427 4.8364 -0.5993 -1.4098 0.2861  1240 PRO B O   
21832 C CB  . PRO C 1240 ? 4.2934 3.2258 4.9876 -0.6129 -1.5151 0.3423  1240 PRO B CB  
21833 C CG  . PRO C 1240 ? 4.2671 3.2047 4.8972 -0.6115 -1.5024 0.3434  1240 PRO B CG  
21834 C CD  . PRO C 1240 ? 4.1938 3.2152 4.8646 -0.6297 -1.4715 0.3849  1240 PRO B CD  
21835 N N   . ASN C 1241 ? 4.0431 3.0605 4.8281 -0.6261 -1.3573 0.3435  1241 ASN B N   
21836 C CA  . ASN C 1241 ? 3.8814 2.8648 4.6533 -0.6179 -1.3004 0.3155  1241 ASN B CA  
21837 C C   . ASN C 1241 ? 3.6253 2.5448 4.3041 -0.6029 -1.2688 0.2813  1241 ASN B C   
21838 O O   . ASN C 1241 ? 3.5955 2.4447 4.2378 -0.5878 -1.2331 0.2494  1241 ASN B O   
21839 C CB  . ASN C 1241 ? 4.0722 3.0002 4.8730 -0.6088 -1.3191 0.2930  1241 ASN B CB  
21840 C CG  . ASN C 1241 ? 4.1841 3.1673 5.0771 -0.6225 -1.3553 0.3267  1241 ASN B CG  
21841 O OD1 . ASN C 1241 ? 4.1597 3.2231 5.1036 -0.6386 -1.3379 0.3658  1241 ASN B OD1 
21842 N ND2 . ASN C 1241 ? 4.2865 3.2224 5.1981 -0.6153 -1.4056 0.3118  1241 ASN B ND2 
21843 N N   . THR C 1242 ? 3.0349 1.9727 3.6723 -0.6054 -1.2797 0.2898  1242 THR B N   
21844 C CA  . THR C 1242 ? 2.8226 1.6941 3.3694 -0.5903 -1.2596 0.2586  1242 THR B CA  
21845 C C   . THR C 1242 ? 2.5060 1.4263 3.0275 -0.5983 -1.2405 0.2763  1242 THR B C   
21846 O O   . THR C 1242 ? 2.4141 1.3894 2.9564 -0.6093 -1.2752 0.3046  1242 THR B O   
21847 C CB  . THR C 1242 ? 2.9418 1.7441 3.4376 -0.5770 -1.3171 0.2354  1242 THR B CB  
21848 O OG1 . THR C 1242 ? 2.9677 1.8266 3.4942 -0.5891 -1.3724 0.2672  1242 THR B OG1 
21849 C CG2 . THR C 1242 ? 3.0158 1.7465 3.5170 -0.5639 -1.3348 0.2078  1242 THR B CG2 
21850 N N   . GLY C 1243 ? 2.5245 1.4136 2.9947 -0.5903 -1.1840 0.2591  1243 GLY B N   
21851 C CA  . GLY C 1243 ? 2.3680 1.2910 2.8073 -0.5956 -1.1602 0.2696  1243 GLY B CA  
21852 C C   . GLY C 1243 ? 2.3040 1.1856 2.6800 -0.5867 -1.1982 0.2562  1243 GLY B C   
21853 O O   . GLY C 1243 ? 2.3702 1.1997 2.7240 -0.5770 -1.2471 0.2402  1243 GLY B O   
21854 N N   . THR C 1244 ? 2.1325 1.0375 2.4782 -0.5899 -1.1744 0.2629  1244 THR B N   
21855 C CA  . THR C 1244 ? 2.1366 1.0220 2.4306 -0.5850 -1.2084 0.2579  1244 THR B CA  
21856 C C   . THR C 1244 ? 2.2150 1.0829 2.4569 -0.5801 -1.1598 0.2487  1244 THR B C   
21857 O O   . THR C 1244 ? 2.2089 1.1038 2.4652 -0.5850 -1.1035 0.2557  1244 THR B O   
21858 C CB  . THR C 1244 ? 2.0676 1.0361 2.4066 -0.6007 -1.2495 0.2954  1244 THR B CB  
21859 O OG1 . THR C 1244 ? 2.0898 1.0671 2.4741 -0.6041 -1.2975 0.3086  1244 THR B OG1 
21860 C CG2 . THR C 1244 ? 2.0664 1.0195 2.3512 -0.5955 -1.2794 0.2934  1244 THR B CG2 
21861 N N   . ALA C 1245 ? 2.4932 1.3135 2.6717 -0.5699 -1.1822 0.2341  1245 ALA B N   
21862 C CA  . ALA C 1245 ? 2.4963 1.3077 2.6315 -0.5669 -1.1441 0.2311  1245 ALA B CA  
21863 C C   . ALA C 1245 ? 2.4471 1.3675 2.6391 -0.5879 -1.1383 0.2645  1245 ALA B C   
21864 O O   . ALA C 1245 ? 2.3787 1.3290 2.5802 -0.5935 -1.0848 0.2716  1245 ALA B O   
21865 C CB  . ALA C 1245 ? 2.5652 1.3351 2.6225 -0.5365 -1.1734 0.2236  1245 ALA B CB  
21866 N N   . ARG C 1246 ? 2.2888 1.2615 2.5134 -0.5970 -1.1917 0.2869  1246 ARG B N   
21867 C CA  . ARG C 1246 ? 2.2628 1.3240 2.5302 -0.6130 -1.1891 0.3208  1246 ARG B CA  
21868 C C   . ARG C 1246 ? 2.1910 1.3182 2.5260 -0.6275 -1.1583 0.3438  1246 ARG B C   
21869 O O   . ARG C 1246 ? 2.1396 1.3253 2.4951 -0.6385 -1.1221 0.3606  1246 ARG B O   
21870 C CB  . ARG C 1246 ? 2.3016 1.3807 2.5755 -0.6156 -1.2502 0.3420  1246 ARG B CB  
21871 C CG  . ARG C 1246 ? 2.2863 1.4373 2.5872 -0.6298 -1.2434 0.3743  1246 ARG B CG  
21872 C CD  . ARG C 1246 ? 2.3810 1.5329 2.6770 -0.6320 -1.2980 0.3954  1246 ARG B CD  
21873 N NE  . ARG C 1246 ? 2.5025 1.6002 2.7327 -0.6170 -1.3260 0.3757  1246 ARG B NE  
21874 C CZ  . ARG C 1246 ? 2.5849 1.6966 2.7894 -0.6175 -1.3302 0.3838  1246 ARG B CZ  
21875 N NH1 . ARG C 1246 ? 2.5771 1.7532 2.8166 -0.6329 -1.3075 0.4093  1246 ARG B NH1 
21876 N NH2 . ARG C 1246 ? 2.6499 1.7110 2.7914 -0.6023 -1.3571 0.3662  1246 ARG B NH2 
21877 N N   . MET C 1247 ? 2.8027 1.9208 3.1714 -0.6275 -1.1733 0.3446  1247 MET B N   
21878 C CA  . MET C 1247 ? 2.7348 1.9103 3.1657 -0.6402 -1.1435 0.3651  1247 MET B CA  
21879 C C   . MET C 1247 ? 2.6797 1.8643 3.0987 -0.6412 -1.0736 0.3558  1247 MET B C   
21880 O O   . MET C 1247 ? 2.6333 1.8804 3.0702 -0.6528 -1.0431 0.3751  1247 MET B O   
21881 C CB  . MET C 1247 ? 2.7308 1.8766 3.1906 -0.6361 -1.1650 0.3582  1247 MET B CB  
21882 C CG  . MET C 1247 ? 2.6967 1.9041 3.2280 -0.6499 -1.1499 0.3851  1247 MET B CG  
21883 S SD  . MET C 1247 ? 2.9346 2.1116 3.5058 -0.6466 -1.2040 0.3852  1247 MET B SD  
21884 C CE  . MET C 1247 ? 2.7108 1.8629 3.2510 -0.6428 -1.2732 0.3915  1247 MET B CE  
21885 N N   . VAL C 1248 ? 1.8836 0.9991 2.2663 -0.6280 -1.0464 0.3267  1248 VAL B N   
21886 C CA  . VAL C 1248 ? 1.8239 0.9366 2.1876 -0.6268 -0.9786 0.3204  1248 VAL B CA  
21887 C C   . VAL C 1248 ? 1.7540 0.8747 2.0797 -0.6271 -0.9572 0.3197  1248 VAL B C   
21888 O O   . VAL C 1248 ? 1.6962 0.8376 2.0164 -0.6305 -0.9029 0.3231  1248 VAL B O   
21889 C CB  . VAL C 1248 ? 1.5509 0.5729 1.8719 -0.6085 -0.9498 0.2922  1248 VAL B CB  
21890 C CG1 . VAL C 1248 ? 1.5511 0.5635 1.8425 -0.6043 -0.8759 0.2896  1248 VAL B CG1 
21891 C CG2 . VAL C 1248 ? 1.5722 0.5977 1.9421 -0.6105 -0.9667 0.2949  1248 VAL B CG2 
21892 N N   . GLU C 1249 ? 2.5724 1.6779 2.8714 -0.6237 -0.9984 0.3160  1249 GLU B N   
21893 C CA  . GLU C 1249 ? 2.5874 1.7114 2.8612 -0.6262 -0.9768 0.3186  1249 GLU B CA  
21894 C C   . GLU C 1249 ? 2.5657 1.7916 2.8951 -0.6455 -0.9645 0.3496  1249 GLU B C   
21895 O O   . GLU C 1249 ? 2.5506 1.8057 2.8763 -0.6506 -0.9168 0.3529  1249 GLU B O   
21896 C CB  . GLU C 1249 ? 2.6704 1.7554 2.8996 -0.6178 -1.0206 0.3080  1249 GLU B CB  
21897 C CG  . GLU C 1249 ? 2.7114 1.8210 2.9219 -0.6214 -0.9985 0.3122  1249 GLU B CG  
21898 C CD  . GLU C 1249 ? 2.8226 1.8681 2.9710 -0.6083 -1.0248 0.2941  1249 GLU B CD  
21899 O OE1 . GLU C 1249 ? 2.9239 1.8935 3.0312 -0.5941 -1.0520 0.2746  1249 GLU B OE1 
21900 O OE2 . GLU C 1249 ? 2.8121 1.8818 2.9513 -0.6119 -1.0173 0.2992  1249 GLU B OE2 
21901 N N   . THR C 1250 ? 1.9908 1.2644 2.3679 -0.6551 -1.0046 0.3730  1250 THR B N   
21902 C CA  . THR C 1250 ? 1.9231 1.2824 2.3446 -0.6721 -0.9953 0.4045  1250 THR B CA  
21903 C C   . THR C 1250 ? 1.8088 1.2110 2.2589 -0.6809 -0.9415 0.4127  1250 THR B C   
21904 O O   . THR C 1250 ? 1.7329 1.1790 2.1830 -0.6888 -0.9021 0.4198  1250 THR B O   
21905 C CB  . THR C 1250 ? 1.9945 1.3789 2.4536 -0.6795 -1.0488 0.4303  1250 THR B CB  
21906 O OG1 . THR C 1250 ? 2.0411 1.4178 2.5332 -0.6795 -1.0552 0.4326  1250 THR B OG1 
21907 C CG2 . THR C 1250 ? 2.0201 1.3580 2.4467 -0.6700 -1.1036 0.4231  1250 THR B CG2 
21908 N N   . THR C 1251 ? 1.7972 1.1862 2.2705 -0.6793 -0.9406 0.4115  1251 THR B N   
21909 C CA  . THR C 1251 ? 1.7828 1.2092 2.2819 -0.6867 -0.8918 0.4199  1251 THR B CA  
21910 C C   . THR C 1251 ? 1.7693 1.1796 2.2284 -0.6821 -0.8305 0.4029  1251 THR B C   
21911 O O   . THR C 1251 ? 1.7687 1.2227 2.2406 -0.6902 -0.7850 0.4128  1251 THR B O   
21912 C CB  . THR C 1251 ? 1.8014 1.2017 2.3259 -0.6826 -0.8990 0.4159  1251 THR B CB  
21913 O OG1 . THR C 1251 ? 1.8372 1.1790 2.3231 -0.6705 -0.8568 0.3897  1251 THR B OG1 
21914 C CG2 . THR C 1251 ? 1.8110 1.1765 2.3460 -0.6772 -0.9646 0.4143  1251 THR B CG2 
21915 N N   . ALA C 1252 ? 1.7335 1.0759 2.1396 -0.6684 -0.8289 0.3782  1252 ALA B N   
21916 C CA  . ALA C 1252 ? 1.7499 1.0740 2.1144 -0.6639 -0.7731 0.3664  1252 ALA B CA  
21917 C C   . ALA C 1252 ? 1.7436 1.1326 2.1192 -0.6758 -0.7667 0.3809  1252 ALA B C   
21918 O O   . ALA C 1252 ? 1.7023 1.1240 2.0746 -0.6815 -0.7180 0.3848  1252 ALA B O   
21919 C CB  . ALA C 1252 ? 1.7971 1.0248 2.0969 -0.6447 -0.7741 0.3395  1252 ALA B CB  
21920 N N   . TYR C 1253 ? 2.0642 1.4710 2.4509 -0.6794 -0.8152 0.3892  1253 TYR B N   
21921 C CA  . TYR C 1253 ? 2.0840 1.5436 2.4754 -0.6890 -0.8074 0.4006  1253 TYR B CA  
21922 C C   . TYR C 1253 ? 2.0678 1.6084 2.4998 -0.7055 -0.7846 0.4246  1253 TYR B C   
21923 O O   . TYR C 1253 ? 2.0848 1.6643 2.5127 -0.7128 -0.7541 0.4281  1253 TYR B O   
21924 C CB  . TYR C 1253 ? 2.1374 1.5943 2.5268 -0.6881 -0.8631 0.4057  1253 TYR B CB  
21925 C CG  . TYR C 1253 ? 2.1895 1.5766 2.5267 -0.6736 -0.8714 0.3810  1253 TYR B CG  
21926 C CD1 . TYR C 1253 ? 2.1811 1.5588 2.4885 -0.6712 -0.8318 0.3700  1253 TYR B CD1 
21927 C CD2 . TYR C 1253 ? 2.2284 1.5545 2.5426 -0.6618 -0.9191 0.3688  1253 TYR B CD2 
21928 C CE1 . TYR C 1253 ? 2.1925 1.4993 2.4487 -0.6574 -0.8389 0.3495  1253 TYR B CE1 
21929 C CE2 . TYR C 1253 ? 2.2488 1.5060 2.5081 -0.6481 -0.9270 0.3465  1253 TYR B CE2 
21930 C CZ  . TYR C 1253 ? 2.2341 1.4807 2.4649 -0.6459 -0.8864 0.3380  1253 TYR B CZ  
21931 O OH  . TYR C 1253 ? 2.2959 1.4672 2.4697 -0.6315 -0.8925 0.3186  1253 TYR B OH  
21932 N N   . ALA C 1254 ? 2.1664 1.7287 2.6351 -0.7111 -0.7993 0.4402  1254 ALA B N   
21933 C CA  . ALA C 1254 ? 2.0782 1.7091 2.5802 -0.7263 -0.7765 0.4627  1254 ALA B CA  
21934 C C   . ALA C 1254 ? 2.0438 1.6729 2.5346 -0.7245 -0.7187 0.4529  1254 ALA B C   
21935 O O   . ALA C 1254 ? 1.9992 1.6719 2.4873 -0.7333 -0.6791 0.4583  1254 ALA B O   
21936 C CB  . ALA C 1254 ? 2.0511 1.7016 2.5959 -0.7333 -0.8165 0.4856  1254 ALA B CB  
21937 N N   . LEU C 1255 ? 1.3739 0.9497 1.8549 -0.7132 -0.7136 0.4383  1255 LEU B N   
21938 C CA  . LEU C 1255 ? 1.4182 0.9844 1.8829 -0.7101 -0.6575 0.4300  1255 LEU B CA  
21939 C C   . LEU C 1255 ? 1.3932 0.9517 1.8143 -0.7073 -0.6101 0.4170  1255 LEU B C   
21940 O O   . LEU C 1255 ? 1.3462 0.9269 1.7575 -0.7108 -0.5609 0.4184  1255 LEU B O   
21941 C CB  . LEU C 1255 ? 1.4823 0.9790 1.9334 -0.6963 -0.6585 0.4137  1255 LEU B CB  
21942 C CG  . LEU C 1255 ? 1.4866 0.9559 1.9047 -0.6893 -0.5967 0.4030  1255 LEU B CG  
21943 C CD1 . LEU C 1255 ? 1.4670 1.0073 1.9102 -0.7026 -0.5630 0.4212  1255 LEU B CD1 
21944 C CD2 . LEU C 1255 ? 1.4899 0.8964 1.9000 -0.6770 -0.5972 0.3912  1255 LEU B CD2 
21945 N N   . LEU C 1256 ? 2.0912 1.6170 2.4852 -0.7008 -0.6260 0.4049  1256 LEU B N   
21946 C CA  . LEU C 1256 ? 2.1504 1.6709 2.5083 -0.6989 -0.5849 0.3950  1256 LEU B CA  
21947 C C   . LEU C 1256 ? 2.1780 1.7787 2.5604 -0.7151 -0.5755 0.4104  1256 LEU B C   
21948 O O   . LEU C 1256 ? 2.1897 1.8099 2.5560 -0.7185 -0.5264 0.4077  1256 LEU B O   
21949 C CB  . LEU C 1256 ? 2.1916 1.6473 2.5109 -0.6860 -0.6037 0.3776  1256 LEU B CB  
21950 C CG  . LEU C 1256 ? 2.2184 1.5771 2.4849 -0.6662 -0.5883 0.3576  1256 LEU B CG  
21951 C CD1 . LEU C 1256 ? 2.2687 1.5723 2.4924 -0.6549 -0.5981 0.3442  1256 LEU B CD1 
21952 C CD2 . LEU C 1256 ? 2.1737 1.5181 2.4124 -0.6614 -0.5250 0.3547  1256 LEU B CD2 
21953 N N   . THR C 1257 ? 1.2639 0.9074 1.6804 -0.7249 -0.6202 0.4267  1257 THR B N   
21954 C CA  . THR C 1257 ? 1.2303 0.9403 1.6608 -0.7395 -0.6085 0.4395  1257 THR B CA  
21955 C C   . THR C 1257 ? 1.1700 0.9173 1.6083 -0.7479 -0.5679 0.4474  1257 THR B C   
21956 O O   . THR C 1257 ? 1.1293 0.8888 1.5457 -0.7501 -0.5209 0.4392  1257 THR B O   
21957 C CB  . THR C 1257 ? 1.1038 0.8535 1.5656 -0.7499 -0.6601 0.4605  1257 THR B CB  
21958 O OG1 . THR C 1257 ? 1.1261 0.8328 1.5914 -0.7407 -0.7107 0.4593  1257 THR B OG1 
21959 C CG2 . THR C 1257 ? 1.0971 0.8761 1.5507 -0.7564 -0.6550 0.4597  1257 THR B CG2 
21960 N N   . SER C 1258 ? 1.4393 1.1986 1.9065 -0.7514 -0.5860 0.4620  1258 SER B N   
21961 C CA  . SER C 1258 ? 1.4823 1.2749 1.9595 -0.7592 -0.5537 0.4717  1258 SER B CA  
21962 C C   . SER C 1258 ? 1.4773 1.2511 1.9171 -0.7530 -0.4938 0.4545  1258 SER B C   
21963 O O   . SER C 1258 ? 1.4603 1.2742 1.8938 -0.7628 -0.4598 0.4586  1258 SER B O   
21964 C CB  . SER C 1258 ? 1.4983 1.2769 2.0039 -0.7562 -0.5762 0.4811  1258 SER B CB  
21965 O OG  . SER C 1258 ? 1.5207 1.3352 2.0657 -0.7673 -0.6204 0.5055  1258 SER B OG  
21966 N N   . LEU C 1259 ? 1.4258 1.1337 1.8364 -0.7370 -0.4819 0.4359  1259 LEU B N   
21967 C CA  . LEU C 1259 ? 1.3937 1.0685 1.7610 -0.7283 -0.4255 0.4208  1259 LEU B CA  
21968 C C   . LEU C 1259 ? 1.3972 1.0758 1.7323 -0.7290 -0.3924 0.4101  1259 LEU B C   
21969 O O   . LEU C 1259 ? 1.3912 1.0571 1.6921 -0.7252 -0.3429 0.4018  1259 LEU B O   
21970 C CB  . LEU C 1259 ? 1.3403 0.9353 1.6799 -0.7105 -0.4248 0.4062  1259 LEU B CB  
21971 C CG  . LEU C 1259 ? 1.2936 0.8780 1.6564 -0.7081 -0.4365 0.4126  1259 LEU B CG  
21972 C CD1 . LEU C 1259 ? 1.3226 0.8203 1.6534 -0.6900 -0.4417 0.3960  1259 LEU B CD1 
21973 C CD2 . LEU C 1259 ? 1.2551 0.8676 1.6151 -0.7123 -0.3915 0.4193  1259 LEU B CD2 
21974 N N   . ASN C 1260 ? 1.6050 1.2993 1.9509 -0.7334 -0.4207 0.4107  1260 ASN B N   
21975 C CA  . ASN C 1260 ? 1.6321 1.3524 1.9642 -0.7397 -0.3956 0.4055  1260 ASN B CA  
21976 C C   . ASN C 1260 ? 1.6777 1.4678 2.0273 -0.7569 -0.3793 0.4177  1260 ASN B C   
21977 O O   . ASN C 1260 ? 1.7229 1.5238 2.0486 -0.7600 -0.3345 0.4102  1260 ASN B O   
21978 C CB  . ASN C 1260 ? 1.6075 1.3332 1.9533 -0.7415 -0.4353 0.4059  1260 ASN B CB  
21979 C CG  . ASN C 1260 ? 1.6272 1.2941 1.9378 -0.7280 -0.4240 0.3881  1260 ASN B CG  
21980 O OD1 . ASN C 1260 ? 1.6532 1.3146 1.9383 -0.7268 -0.3825 0.3785  1260 ASN B OD1 
21981 N ND2 . ASN C 1260 ? 1.6219 1.2411 1.9286 -0.7178 -0.4621 0.3840  1260 ASN B ND2 
21982 N N   . LEU C 1261 ? 1.5219 1.3550 1.9097 -0.7682 -0.4169 0.4371  1261 LEU B N   
21983 C CA  . LEU C 1261 ? 1.4724 1.3688 1.8746 -0.7863 -0.4090 0.4514  1261 LEU B CA  
21984 C C   . LEU C 1261 ? 1.4669 1.3722 1.8672 -0.7886 -0.3829 0.4571  1261 LEU B C   
21985 O O   . LEU C 1261 ? 1.4708 1.4246 1.8838 -0.8040 -0.3816 0.4716  1261 LEU B O   
21986 C CB  . LEU C 1261 ? 1.4347 1.3686 1.8735 -0.7979 -0.4608 0.4727  1261 LEU B CB  
21987 C CG  . LEU C 1261 ? 1.4055 1.3349 1.8460 -0.7966 -0.4881 0.4688  1261 LEU B CG  
21988 C CD1 . LEU C 1261 ? 1.4373 1.3991 1.9093 -0.8078 -0.5390 0.4924  1261 LEU B CD1 
21989 C CD2 . LEU C 1261 ? 1.3598 1.3073 1.7785 -0.8019 -0.4527 0.4552  1261 LEU B CD2 
21990 N N   . LYS C 1262 ? 1.2930 1.1494 1.6746 -0.7738 -0.3622 0.4463  1262 LYS B N   
21991 C CA  . LYS C 1262 ? 1.2805 1.1392 1.6511 -0.7737 -0.3281 0.4479  1262 LYS B CA  
21992 C C   . LYS C 1262 ? 1.2431 1.1422 1.6521 -0.7850 -0.3524 0.4708  1262 LYS B C   
21993 O O   . LYS C 1262 ? 1.2426 1.1637 1.6470 -0.7913 -0.3277 0.4765  1262 LYS B O   
21994 C CB  . LYS C 1262 ? 1.3452 1.2200 1.6809 -0.7794 -0.2803 0.4376  1262 LYS B CB  
21995 C CG  . LYS C 1262 ? 1.4542 1.2906 1.7564 -0.7693 -0.2597 0.4175  1262 LYS B CG  
21996 C CD  . LYS C 1262 ? 1.5680 1.3650 1.8209 -0.7586 -0.2053 0.4023  1262 LYS B CD  
21997 C CE  . LYS C 1262 ? 1.6274 1.3664 1.8464 -0.7434 -0.1905 0.3857  1262 LYS B CE  
21998 N NZ  . LYS C 1262 ? 1.6390 1.3349 1.8691 -0.7318 -0.2269 0.3862  1262 LYS B NZ  
21999 N N   . ASP C 1263 ? 1.2847 1.1884 1.7304 -0.7866 -0.4023 0.4840  1263 ASP B N   
22000 C CA  . ASP C 1263 ? 1.3131 1.2499 1.7999 -0.7969 -0.4340 0.5086  1263 ASP B CA  
22001 C C   . ASP C 1263 ? 1.2767 1.1914 1.7773 -0.7889 -0.4282 0.5119  1263 ASP B C   
22002 O O   . ASP C 1263 ? 1.3352 1.2523 1.8749 -0.7901 -0.4646 0.5276  1263 ASP B O   
22003 C CB  . ASP C 1263 ? 1.3412 1.2761 1.8567 -0.7978 -0.4887 0.5187  1263 ASP B CB  
22004 C CG  . ASP C 1263 ? 1.7069 1.6876 2.2583 -0.8141 -0.5223 0.5473  1263 ASP B CG  
22005 O OD1 . ASP C 1263 ? 1.7040 1.6919 2.2787 -0.8163 -0.5254 0.5608  1263 ASP B OD1 
22006 O OD2 . ASP C 1263 ? 1.6960 1.7044 2.2514 -0.8253 -0.5448 0.5571  1263 ASP B OD2 
22007 N N   . ILE C 1264 ? 1.0406 0.9326 1.5080 -0.7808 -0.3812 0.4973  1264 ILE B N   
22008 C CA  . ILE C 1264 ? 1.0633 0.9260 1.5342 -0.7707 -0.3667 0.4962  1264 ILE B CA  
22009 C C   . ILE C 1264 ? 1.0310 0.9069 1.5535 -0.7743 -0.4011 0.5167  1264 ILE B C   
22010 O O   . ILE C 1264 ? 1.0373 0.8763 1.5665 -0.7631 -0.3976 0.5120  1264 ILE B O   
22011 C CB  . ILE C 1264 ? 1.2039 1.0711 1.6377 -0.7706 -0.3120 0.4895  1264 ILE B CB  
22012 C CG1 . ILE C 1264 ? 1.1803 1.0238 1.5640 -0.7649 -0.2803 0.4681  1264 ILE B CG1 
22013 C CG2 . ILE C 1264 ? 1.0669 0.9024 1.4995 -0.7595 -0.2920 0.4886  1264 ILE B CG2 
22014 C CD1 . ILE C 1264 ? 1.1788 1.0309 1.5226 -0.7673 -0.2309 0.4608  1264 ILE B CD1 
22015 N N   . ASN C 1265 ? 1.2045 1.1288 1.7627 -0.7896 -0.4336 0.5398  1265 ASN B N   
22016 C CA  . ASN C 1265 ? 1.2901 1.2227 1.8953 -0.7920 -0.4594 0.5594  1265 ASN B CA  
22017 C C   . ASN C 1265 ? 1.2984 1.2158 1.9397 -0.7900 -0.5147 0.5666  1265 ASN B C   
22018 O O   . ASN C 1265 ? 1.3095 1.2068 1.9854 -0.7845 -0.5366 0.5721  1265 ASN B O   
22019 C CB  . ASN C 1265 ? 1.3602 1.3502 1.9834 -0.8100 -0.4569 0.5845  1265 ASN B CB  
22020 C CG  . ASN C 1265 ? 1.4253 1.4146 2.0487 -0.8069 -0.4228 0.5868  1265 ASN B CG  
22021 O OD1 . ASN C 1265 ? 1.4566 1.4081 2.0908 -0.7933 -0.4180 0.5793  1265 ASN B OD1 
22022 N ND2 . ASN C 1265 ? 1.4442 1.4744 2.0543 -0.8202 -0.4001 0.5970  1265 ASN B ND2 
22023 N N   . TYR C 1266 ? 1.2941 1.2187 1.9257 -0.7941 -0.5366 0.5653  1266 TYR B N   
22024 C CA  . TYR C 1266 ? 1.2897 1.1959 1.9471 -0.7916 -0.5906 0.5706  1266 TYR B CA  
22025 C C   . TYR C 1266 ? 1.3128 1.1549 1.9629 -0.7730 -0.5947 0.5478  1266 TYR B C   
22026 O O   . TYR C 1266 ? 1.3667 1.1843 2.0460 -0.7687 -0.6387 0.5514  1266 TYR B O   
22027 C CB  . TYR C 1266 ? 1.2294 1.1452 1.8660 -0.7961 -0.6046 0.5674  1266 TYR B CB  
22028 C CG  . TYR C 1266 ? 1.1911 1.0992 1.8543 -0.7978 -0.6631 0.5802  1266 TYR B CG  
22029 C CD1 . TYR C 1266 ? 1.2107 1.1237 1.9175 -0.8024 -0.6997 0.6018  1266 TYR B CD1 
22030 C CD2 . TYR C 1266 ? 1.1590 1.0545 1.8034 -0.7953 -0.6821 0.5718  1266 TYR B CD2 
22031 C CE1 . TYR C 1266 ? 1.2585 1.1617 1.9868 -0.8046 -0.7539 0.6150  1266 TYR B CE1 
22032 C CE2 . TYR C 1266 ? 1.1798 1.0671 1.8452 -0.7974 -0.7369 0.5854  1266 TYR B CE2 
22033 C CZ  . TYR C 1266 ? 1.2356 1.1255 1.9416 -0.8021 -0.7725 0.6069  1266 TYR B CZ  
22034 O OH  . TYR C 1266 ? 1.2617 1.1399 1.9871 -0.8049 -0.8270 0.6219  1266 TYR B OH  
22035 N N   . VAL C 1267 ? 1.3119 1.1237 1.9189 -0.7627 -0.5488 0.5243  1267 VAL B N   
22036 C CA  . VAL C 1267 ? 1.3452 1.0886 1.9240 -0.7456 -0.5460 0.4983  1267 VAL B CA  
22037 C C   . VAL C 1267 ? 1.2338 0.9331 1.8227 -0.7348 -0.5402 0.4910  1267 VAL B C   
22038 O O   . VAL C 1267 ? 1.2333 0.8807 1.8236 -0.7246 -0.5687 0.4784  1267 VAL B O   
22039 C CB  . VAL C 1267 ? 1.3079 1.0339 1.8299 -0.7401 -0.5000 0.4785  1267 VAL B CB  
22040 C CG1 . VAL C 1267 ? 1.3013 0.9564 1.7863 -0.7232 -0.4746 0.4561  1267 VAL B CG1 
22041 C CG2 . VAL C 1267 ? 1.2858 1.0190 1.7962 -0.7430 -0.5221 0.4750  1267 VAL B CG2 
22042 N N   . ASN C 1268 ? 1.3873 1.1090 1.9849 -0.7381 -0.5070 0.5000  1268 ASN B N   
22043 C CA  . ASN C 1268 ? 1.4945 1.1814 2.1023 -0.7291 -0.4930 0.4955  1268 ASN B CA  
22044 C C   . ASN C 1268 ? 1.5277 1.1794 2.1758 -0.7235 -0.5372 0.4946  1268 ASN B C   
22045 O O   . ASN C 1268 ? 1.5820 1.1919 2.2282 -0.7138 -0.5208 0.4850  1268 ASN B O   
22046 C CB  . ASN C 1268 ? 1.5701 1.3071 2.1975 -0.7384 -0.4651 0.5148  1268 ASN B CB  
22047 C CG  . ASN C 1268 ? 1.6412 1.4058 2.2243 -0.7429 -0.4181 0.5125  1268 ASN B CG  
22048 O OD1 . ASN C 1268 ? 1.6568 1.3828 2.1875 -0.7326 -0.3813 0.4925  1268 ASN B OD1 
22049 N ND2 . ASN C 1268 ? 1.6714 1.4988 2.2724 -0.7585 -0.4196 0.5328  1268 ASN B ND2 
22050 N N   . PRO C 1269 ? 1.4475 1.1176 2.1332 -0.7301 -0.5924 0.5065  1269 PRO B N   
22051 C CA  . PRO C 1269 ? 1.4335 1.0697 2.1568 -0.7251 -0.6408 0.5046  1269 PRO B CA  
22052 C C   . PRO C 1269 ? 1.3837 0.9893 2.0905 -0.7206 -0.6837 0.4927  1269 PRO B C   
22053 O O   . PRO C 1269 ? 1.3612 0.9497 2.0990 -0.7193 -0.7357 0.4952  1269 PRO B O   
22054 C CB  . PRO C 1269 ? 1.4908 1.1866 2.2751 -0.7395 -0.6704 0.5375  1269 PRO B CB  
22055 C CG  . PRO C 1269 ? 1.5021 1.2619 2.2726 -0.7527 -0.6369 0.5552  1269 PRO B CG  
22056 C CD  . PRO C 1269 ? 1.4702 1.2105 2.1799 -0.7466 -0.6063 0.5331  1269 PRO B CD  
22057 N N   . VAL C 1270 ? 1.4142 1.0165 2.0727 -0.7189 -0.6624 0.4816  1270 VAL B N   
22058 C CA  . VAL C 1270 ? 1.3765 0.9315 2.0029 -0.7101 -0.6900 0.4626  1270 VAL B CA  
22059 C C   . VAL C 1270 ? 1.3314 0.8081 1.9102 -0.6934 -0.6600 0.4335  1270 VAL B C   
22060 O O   . VAL C 1270 ? 1.3738 0.7873 1.9441 -0.6822 -0.6893 0.4162  1270 VAL B O   
22061 C CB  . VAL C 1270 ? 1.3472 0.9335 1.9462 -0.7160 -0.6831 0.4656  1270 VAL B CB  
22062 C CG1 . VAL C 1270 ? 1.3177 0.8415 1.8644 -0.7030 -0.6836 0.4391  1270 VAL B CG1 
22063 C CG2 . VAL C 1270 ? 1.3704 1.0032 2.0053 -0.7279 -0.7321 0.4895  1270 VAL B CG2 
22064 N N   . ILE C 1271 ? 1.2867 0.7620 1.8296 -0.6910 -0.6009 0.4286  1271 ILE B N   
22065 C CA  . ILE C 1271 ? 1.2798 0.6739 1.7676 -0.6736 -0.5664 0.4047  1271 ILE B CA  
22066 C C   . ILE C 1271 ? 1.2874 0.6468 1.7902 -0.6663 -0.5562 0.4016  1271 ILE B C   
22067 O O   . ILE C 1271 ? 1.3349 0.6267 1.7871 -0.6508 -0.5216 0.3851  1271 ILE B O   
22068 C CB  . ILE C 1271 ? 1.2992 0.6882 1.7292 -0.6697 -0.5044 0.3993  1271 ILE B CB  
22069 C CG1 . ILE C 1271 ? 1.2795 0.7159 1.7229 -0.6768 -0.4585 0.4142  1271 ILE B CG1 
22070 C CG2 . ILE C 1271 ? 1.2924 0.7127 1.7080 -0.6764 -0.5096 0.4007  1271 ILE B CG2 
22071 C CD1 . ILE C 1271 ? 1.3028 0.6915 1.7341 -0.6653 -0.4303 0.4086  1271 ILE B CD1 
22072 N N   . LYS C 1272 ? 1.6116 1.0136 2.1803 -0.6761 -0.5832 0.4186  1272 LYS B N   
22073 C CA  . LYS C 1272 ? 1.7182 1.0797 2.3029 -0.6679 -0.5775 0.4129  1272 LYS B CA  
22074 C C   . LYS C 1272 ? 1.7936 1.0879 2.3741 -0.6571 -0.6275 0.3928  1272 LYS B C   
22075 O O   . LYS C 1272 ? 1.8495 1.0779 2.4205 -0.6438 -0.6268 0.3768  1272 LYS B O   
22076 C CB  . LYS C 1272 ? 1.7491 1.1795 2.4083 -0.6819 -0.5875 0.4396  1272 LYS B CB  
22077 C CG  . LYS C 1272 ? 1.7618 1.1564 2.4640 -0.6765 -0.6148 0.4354  1272 LYS B CG  
22078 C CD  . LYS C 1272 ? 1.7674 1.1398 2.4652 -0.6696 -0.5655 0.4342  1272 LYS B CD  
22079 C CE  . LYS C 1272 ? 1.8272 1.1904 2.5893 -0.6695 -0.5928 0.4387  1272 LYS B CE  
22080 N NZ  . LYS C 1272 ? 1.8610 1.2123 2.6222 -0.6640 -0.5418 0.4421  1272 LYS B NZ  
22081 N N   . TRP C 1273 ? 1.8815 1.1904 2.4640 -0.6617 -0.6706 0.3932  1273 TRP B N   
22082 C CA  . TRP C 1273 ? 1.8645 1.1258 2.4515 -0.6546 -0.7296 0.3787  1273 TRP B CA  
22083 C C   . TRP C 1273 ? 1.8348 1.0197 2.3472 -0.6388 -0.7337 0.3517  1273 TRP B C   
22084 O O   . TRP C 1273 ? 1.8970 1.0061 2.3854 -0.6241 -0.7647 0.3292  1273 TRP B O   
22085 C CB  . TRP C 1273 ? 1.8481 1.1803 2.4908 -0.6702 -0.7807 0.4030  1273 TRP B CB  
22086 C CG  . TRP C 1273 ? 1.8742 1.1731 2.5146 -0.6654 -0.8441 0.3932  1273 TRP B CG  
22087 C CD1 . TRP C 1273 ? 1.9328 1.2055 2.6076 -0.6621 -0.8937 0.3895  1273 TRP B CD1 
22088 C CD2 . TRP C 1273 ? 1.8708 1.1625 2.4736 -0.6639 -0.8675 0.3878  1273 TRP B CD2 
22089 N NE1 . TRP C 1273 ? 1.9506 1.1993 2.6067 -0.6583 -0.9462 0.3821  1273 TRP B NE1 
22090 C CE2 . TRP C 1273 ? 1.9090 1.1697 2.5218 -0.6593 -0.9313 0.3817  1273 TRP B CE2 
22091 C CE3 . TRP C 1273 ? 1.8591 1.1673 2.4215 -0.6657 -0.8406 0.3877  1273 TRP B CE3 
22092 C CZ2 . TRP C 1273 ? 1.9375 1.1835 2.5179 -0.6564 -0.9688 0.3767  1273 TRP B CZ2 
22093 C CZ3 . TRP C 1273 ? 1.8819 1.1768 2.4181 -0.6632 -0.8772 0.3826  1273 TRP B CZ3 
22094 C CH2 . TRP C 1273 ? 1.9188 1.1834 2.4629 -0.6586 -0.9408 0.3778  1273 TRP B CH2 
22095 N N   . LEU C 1274 ? 1.4555 0.6571 1.9291 -0.6407 -0.7037 0.3536  1274 LEU B N   
22096 C CA  . LEU C 1274 ? 1.5449 0.6647 1.9405 -0.6224 -0.6931 0.3291  1274 LEU B CA  
22097 C C   . LEU C 1274 ? 1.5294 0.5681 1.8858 -0.6025 -0.6584 0.3122  1274 LEU B C   
22098 O O   . LEU C 1274 ? 1.5908 0.5612 1.9354 -0.5880 -0.6866 0.2941  1274 LEU B O   
22099 C CB  . LEU C 1274 ? 1.4600 0.6086 1.8219 -0.6267 -0.6571 0.3348  1274 LEU B CB  
22100 C CG  . LEU C 1274 ? 1.4947 0.6916 1.8779 -0.6385 -0.7027 0.3435  1274 LEU B CG  
22101 C CD1 . LEU C 1274 ? 1.5058 0.6825 1.8348 -0.6330 -0.6837 0.3353  1274 LEU B CD1 
22102 C CD2 . LEU C 1274 ? 1.5305 0.6898 1.9234 -0.6330 -0.7661 0.3335  1274 LEU B CD2 
22103 N N   . SER C 1275 ? 1.4286 0.4771 1.7668 -0.6014 -0.5984 0.3193  1275 SER B N   
22104 C CA  . SER C 1275 ? 1.5215 0.5014 1.8264 -0.5824 -0.5623 0.3084  1275 SER B CA  
22105 C C   . SER C 1275 ? 1.5498 0.4910 1.8871 -0.5750 -0.5902 0.2992  1275 SER B C   
22106 O O   . SER C 1275 ? 1.5533 0.4552 1.8748 -0.5622 -0.5550 0.2954  1275 SER B O   
22107 C CB  . SER C 1275 ? 1.6002 0.6311 1.9099 -0.5909 -0.5019 0.3267  1275 SER B CB  
22108 O OG  . SER C 1275 ? 1.4498 0.4259 1.7362 -0.5747 -0.4682 0.3208  1275 SER B OG  
22109 N N   . GLU C 1276 ? 1.9072 0.8567 2.2871 -0.5814 -0.6523 0.2955  1276 GLU B N   
22110 C CA  . GLU C 1276 ? 2.0171 0.9097 2.4133 -0.5692 -0.6809 0.2800  1276 GLU B CA  
22111 C C   . GLU C 1276 ? 2.0603 0.9012 2.4367 -0.5597 -0.7416 0.2595  1276 GLU B C   
22112 O O   . GLU C 1276 ? 2.1391 0.9123 2.5092 -0.5436 -0.7688 0.2392  1276 GLU B O   
22113 C CB  . GLU C 1276 ? 2.0500 1.0197 2.5407 -0.5900 -0.6948 0.3022  1276 GLU B CB  
22114 C CG  . GLU C 1276 ? 2.0507 1.0668 2.5560 -0.5976 -0.6340 0.3218  1276 GLU B CG  
22115 C CD  . GLU C 1276 ? 2.0172 1.1020 2.6133 -0.6147 -0.6463 0.3443  1276 GLU B CD  
22116 O OE1 . GLU C 1276 ? 1.9938 1.1158 2.6486 -0.6262 -0.7025 0.3524  1276 GLU B OE1 
22117 O OE2 . GLU C 1276 ? 2.0130 1.1135 2.6199 -0.6155 -0.6006 0.3553  1276 GLU B OE2 
22118 N N   . GLU C 1277 ? 2.4496 1.3251 2.8157 -0.5695 -0.7619 0.2655  1277 GLU B N   
22119 C CA  . GLU C 1277 ? 2.4990 1.3234 2.8259 -0.5590 -0.8102 0.2472  1277 GLU B CA  
22120 C C   . GLU C 1277 ? 2.5435 1.2571 2.7699 -0.5263 -0.7806 0.2211  1277 GLU B C   
22121 O O   . GLU C 1277 ? 2.6025 1.2436 2.7873 -0.4967 -0.8028 0.1972  1277 GLU B O   
22122 C CB  . GLU C 1277 ? 2.4598 1.3593 2.8037 -0.5786 -0.8312 0.2650  1277 GLU B CB  
22123 C CG  . GLU C 1277 ? 2.4744 1.3795 2.8360 -0.5835 -0.9032 0.2626  1277 GLU B CG  
22124 C CD  . GLU C 1277 ? 2.4902 1.4317 2.9270 -0.5942 -0.9445 0.2732  1277 GLU B CD  
22125 O OE1 . GLU C 1277 ? 2.5216 1.4707 2.9764 -0.5980 -1.0063 0.2749  1277 GLU B OE1 
22126 O OE2 . GLU C 1277 ? 2.4855 1.4478 2.9629 -0.5983 -0.9156 0.2817  1277 GLU B OE2 
22127 N N   . GLN C 1278 ? 1.9100 0.6279 2.0942 -0.5230 -0.7295 0.2278  1278 GLN B N   
22128 C CA  . GLN C 1278 ? 2.0147 0.6605 2.0967 -0.4804 -0.6973 0.2092  1278 GLN B CA  
22129 C C   . GLN C 1278 ? 2.1345 0.7110 2.1693 -0.4376 -0.6969 0.1839  1278 GLN B C   
22130 O O   . GLN C 1278 ? 2.1354 0.7092 2.2064 -0.4409 -0.6834 0.1849  1278 GLN B O   
22131 C CB  . GLN C 1278 ? 2.0787 0.7375 2.1317 -0.4827 -0.6309 0.2222  1278 GLN B CB  
22132 C CG  . GLN C 1278 ? 2.4296 1.1473 2.5024 -0.5126 -0.6263 0.2408  1278 GLN B CG  
22133 C CD  . GLN C 1278 ? 1.8479 0.5766 1.9276 -0.5199 -0.6834 0.2370  1278 GLN B CD  
22134 O OE1 . GLN C 1278 ? 1.8207 0.5572 1.8669 -0.5162 -0.6760 0.2394  1278 GLN B OE1 
22135 N NE2 . GLN C 1278 ? 1.8436 0.5841 1.9685 -0.5290 -0.7403 0.2333  1278 GLN B NE2 
22136 N N   . ARG C 1279 ? 2.9213 1.4440 2.8784 -0.3993 -0.7129 0.1617  1279 ARG B N   
22137 C CA  . ARG C 1279 ? 2.9759 1.4329 2.8863 -0.3601 -0.7178 0.1350  1279 ARG B CA  
22138 C C   . ARG C 1279 ? 2.9531 1.3638 2.7777 -0.3218 -0.6640 0.1213  1279 ARG B C   
22139 O O   . ARG C 1279 ? 2.9417 1.3441 2.7069 -0.3092 -0.6452 0.1216  1279 ARG B O   
22140 C CB  . ARG C 1279 ? 3.0823 1.5082 2.9698 -0.3463 -0.7780 0.1182  1279 ARG B CB  
22141 C CG  . ARG C 1279 ? 3.1062 1.5682 3.0820 -0.3802 -0.8350 0.1274  1279 ARG B CG  
22142 C CD  . ARG C 1279 ? 3.2406 1.6564 3.1930 -0.3606 -0.8894 0.1063  1279 ARG B CD  
22143 N NE  . ARG C 1279 ? 3.3592 1.7033 3.2194 -0.3134 -0.8672 0.0794  1279 ARG B NE  
22144 C CZ  . ARG C 1279 ? 3.4640 1.7552 3.2863 -0.2896 -0.9029 0.0567  1279 ARG B CZ  
22145 N NH1 . ARG C 1279 ? 3.4599 1.7607 3.3289 -0.3078 -0.9633 0.0584  1279 ARG B NH1 
22146 N NH2 . ARG C 1279 ? 3.5592 1.7894 3.2977 -0.2496 -0.8784 0.0325  1279 ARG B NH2 
22147 N N   . TYR C 1280 ? 2.6201 1.0024 2.4410 -0.3043 -0.6407 0.1098  1280 TYR B N   
22148 C CA  . TYR C 1280 ? 2.6643 1.0111 2.4137 -0.2725 -0.5864 0.0992  1280 TYR B CA  
22149 C C   . TYR C 1280 ? 2.4452 0.7734 2.1158 -0.2540 -0.5760 0.0946  1280 TYR B C   
22150 O O   . TYR C 1280 ? 2.4677 0.7644 2.0974 -0.2366 -0.6104 0.0789  1280 TYR B O   
22151 C CB  . TYR C 1280 ? 2.7365 1.0269 2.4538 -0.2378 -0.5905 0.0704  1280 TYR B CB  
22152 C CG  . TYR C 1280 ? 2.7667 1.0161 2.3974 -0.2014 -0.5424 0.0547  1280 TYR B CG  
22153 C CD1 . TYR C 1280 ? 2.9044 1.0962 2.4816 -0.1648 -0.5479 0.0232  1280 TYR B CD1 
22154 C CD2 . TYR C 1280 ? 2.6905 0.9593 2.2917 -0.2046 -0.4926 0.0708  1280 TYR B CD2 
22155 C CE1 . TYR C 1280 ? 2.9631 1.1205 2.4607 -0.1329 -0.5060 0.0079  1280 TYR B CE1 
22156 C CE2 . TYR C 1280 ? 2.7802 1.0129 2.3002 -0.1721 -0.4514 0.0567  1280 TYR B CE2 
22157 C CZ  . TYR C 1280 ? 2.9110 1.0894 2.3802 -0.1365 -0.4590 0.0249  1280 TYR B CZ  
22158 O OH  . TYR C 1280 ? 2.9898 1.1351 2.3793 -0.1057 -0.4214 0.0094  1280 TYR B OH  
22159 N N   . GLY C 1281 ? 1.9067 0.2554 1.5576 -0.2597 -0.5292 0.1102  1281 GLY B N   
22160 C CA  . GLY C 1281 ? 1.9337 0.2667 1.5129 -0.2430 -0.5151 0.1080  1281 GLY B CA  
22161 C C   . GLY C 1281 ? 1.8877 0.2594 1.4874 -0.2669 -0.5333 0.1257  1281 GLY B C   
22162 O O   . GLY C 1281 ? 1.9072 0.2748 1.4572 -0.2577 -0.5092 0.1298  1281 GLY B O   
22163 N N   . GLY C 1282 ? 1.9260 0.3358 1.5973 -0.2972 -0.5760 0.1360  1282 GLY B N   
22164 C CA  . GLY C 1282 ? 1.9704 0.4170 1.6584 -0.3180 -0.5962 0.1505  1282 GLY B CA  
22165 C C   . GLY C 1282 ? 2.1114 0.5955 1.8736 -0.3484 -0.6531 0.1578  1282 GLY B C   
22166 O O   . GLY C 1282 ? 2.1276 0.6018 1.9235 -0.3503 -0.6829 0.1495  1282 GLY B O   
22167 N N   . GLY C 1283 ? 2.3585 0.8860 2.1458 -0.3720 -0.6698 0.1730  1283 GLY B N   
22168 C CA  . GLY C 1283 ? 2.4379 1.0203 2.3086 -0.4117 -0.7158 0.1864  1283 GLY B CA  
22169 C C   . GLY C 1283 ? 2.4853 1.0538 2.3696 -0.4096 -0.7816 0.1760  1283 GLY B C   
22170 O O   . GLY C 1283 ? 2.4162 1.0261 2.3419 -0.4353 -0.8246 0.1866  1283 GLY B O   
22171 N N   . PHE C 1284 ? 2.6991 1.2119 2.5508 -0.3808 -0.7898 0.1557  1284 PHE B N   
22172 C CA  . PHE C 1284 ? 2.8919 1.3728 2.7277 -0.3681 -0.8479 0.1413  1284 PHE B CA  
22173 C C   . PHE C 1284 ? 2.7676 1.2755 2.6089 -0.3829 -0.8980 0.1506  1284 PHE B C   
22174 O O   . PHE C 1284 ? 2.8487 1.3269 2.6221 -0.3594 -0.9029 0.1444  1284 PHE B O   
22175 C CB  . PHE C 1284 ? 3.1844 1.6632 3.0777 -0.3790 -0.8771 0.1360  1284 PHE B CB  
22176 C CG  . PHE C 1284 ? 3.6218 2.0426 3.4730 -0.3521 -0.9197 0.1135  1284 PHE B CG  
22177 C CD1 . PHE C 1284 ? 3.8766 2.2306 3.6382 -0.3092 -0.8978 0.0911  1284 PHE B CD1 
22178 C CD2 . PHE C 1284 ? 3.8045 2.2380 3.7044 -0.3711 -0.9819 0.1150  1284 PHE B CD2 
22179 C CE1 . PHE C 1284 ? 4.1298 2.4299 3.8504 -0.2864 -0.9351 0.0700  1284 PHE B CE1 
22180 C CE2 . PHE C 1284 ? 4.0350 2.4129 3.8932 -0.3472 -1.0206 0.0945  1284 PHE B CE2 
22181 C CZ  . PHE C 1284 ? 4.2303 2.5407 3.9981 -0.3049 -0.9961 0.0717  1284 PHE B CZ  
22182 N N   . TYR C 1285 ? 2.7649 1.3305 2.6870 -0.4227 -0.9367 0.1662  1285 TYR B N   
22183 C CA  . TYR C 1285 ? 2.6366 1.2259 2.5652 -0.4363 -0.9943 0.1734  1285 TYR B CA  
22184 C C   . TYR C 1285 ? 2.5759 1.1736 2.4564 -0.4275 -0.9794 0.1804  1285 TYR B C   
22185 O O   . TYR C 1285 ? 2.5713 1.2087 2.4726 -0.4429 -0.9406 0.1933  1285 TYR B O   
22186 C CB  . TYR C 1285 ? 2.5156 1.1784 2.5450 -0.4862 -1.0326 0.1920  1285 TYR B CB  
22187 C CG  . TYR C 1285 ? 2.4941 1.1528 2.5791 -0.4975 -1.0469 0.1879  1285 TYR B CG  
22188 C CD1 . TYR C 1285 ? 2.5607 1.1496 2.6024 -0.4628 -1.0492 0.1658  1285 TYR B CD1 
22189 C CD2 . TYR C 1285 ? 2.4063 1.1316 2.5884 -0.5437 -1.0576 0.2060  1285 TYR B CD2 
22190 C CE1 . TYR C 1285 ? 2.5522 1.1360 2.6467 -0.4714 -1.0613 0.1616  1285 TYR B CE1 
22191 C CE2 . TYR C 1285 ? 2.3876 1.1173 2.6218 -0.5493 -1.0698 0.2059  1285 TYR B CE2 
22192 C CZ  . TYR C 1285 ? 2.4654 1.1157 2.6583 -0.5170 -1.0725 0.1815  1285 TYR B CZ  
22193 O OH  . TYR C 1285 ? 2.4842 1.1307 2.7340 -0.5264 -1.0855 0.1791  1285 TYR B OH  
22194 N N   . SER C 1286 ? 2.5152 1.0741 2.3313 -0.4028 -1.0088 0.1723  1286 SER B N   
22195 C CA  . SER C 1286 ? 2.4299 1.0027 2.2100 -0.3983 -1.0083 0.1819  1286 SER B CA  
22196 C C   . SER C 1286 ? 2.3456 0.9318 2.1107 -0.3937 -0.9449 0.1884  1286 SER B C   
22197 O O   . SER C 1286 ? 2.3398 0.9050 2.0932 -0.3823 -0.8948 0.1818  1286 SER B O   
22198 C CB  . SER C 1286 ? 2.3812 1.0168 2.2167 -0.4332 -1.0633 0.1993  1286 SER B CB  
22199 O OG  . SER C 1286 ? 2.3522 1.0021 2.1546 -0.4281 -1.0670 0.2090  1286 SER B OG  
22200 N N   . THR C 1287 ? 2.7363 1.3577 2.5010 -0.4026 -0.9485 0.2019  1287 THR B N   
22201 C CA  . THR C 1287 ? 2.7643 1.3947 2.5091 -0.3963 -0.8932 0.2079  1287 THR B CA  
22202 C C   . THR C 1287 ? 2.7844 1.4917 2.6055 -0.4371 -0.8810 0.2256  1287 THR B C   
22203 O O   . THR C 1287 ? 2.7749 1.4983 2.6247 -0.4501 -0.8368 0.2288  1287 THR B O   
22204 C CB  . THR C 1287 ? 2.7618 1.3679 2.4403 -0.3708 -0.8977 0.2089  1287 THR B CB  
22205 O OG1 . THR C 1287 ? 2.7310 1.3767 2.4358 -0.3891 -0.9510 0.2207  1287 THR B OG1 
22206 C CG2 . THR C 1287 ? 2.8484 1.3782 2.4467 -0.3320 -0.9015 0.1917  1287 THR B CG2 
22207 N N   . GLN C 1288 ? 3.1602 1.9158 3.0130 -0.4584 -0.9208 0.2375  1288 GLN B N   
22208 C CA  . GLN C 1288 ? 3.1142 1.9456 3.0332 -0.4966 -0.9101 0.2535  1288 GLN B CA  
22209 C C   . GLN C 1288 ? 3.0997 1.9681 3.0864 -0.5297 -0.8840 0.2588  1288 GLN B C   
22210 O O   . GLN C 1288 ? 3.0959 2.0057 3.1142 -0.5515 -0.8453 0.2686  1288 GLN B O   
22211 C CB  . GLN C 1288 ? 3.0795 1.9638 3.0390 -0.5221 -0.9717 0.2640  1288 GLN B CB  
22212 C CG  . GLN C 1288 ? 3.1126 1.9912 3.0251 -0.5024 -0.9822 0.2678  1288 GLN B CG  
22213 C CD  . GLN C 1288 ? 3.0806 1.9798 2.9910 -0.5024 -0.9286 0.2735  1288 GLN B CD  
22214 O OE1 . GLN C 1288 ? 3.0469 2.0063 3.0201 -0.5372 -0.9109 0.2822  1288 GLN B OE1 
22215 N NE2 . GLN C 1288 ? 3.0958 1.9450 2.9343 -0.4647 -0.9024 0.2689  1288 GLN B NE2 
22216 N N   . ASP C 1289 ? 2.3565 1.2101 2.3660 -0.5345 -0.9058 0.2531  1289 ASP B N   
22217 C CA  . ASP C 1289 ? 2.3143 1.1984 2.3874 -0.5647 -0.8825 0.2593  1289 ASP B CA  
22218 C C   . ASP C 1289 ? 2.3178 1.1613 2.3488 -0.5420 -0.8139 0.2540  1289 ASP B C   
22219 O O   . ASP C 1289 ? 2.3128 1.1925 2.3743 -0.5650 -0.7707 0.2654  1289 ASP B O   
22220 C CB  . ASP C 1289 ? 2.3358 1.2105 2.4432 -0.5725 -0.9274 0.2542  1289 ASP B CB  
22221 C CG  . ASP C 1289 ? 2.4234 1.2150 2.4580 -0.5259 -0.9296 0.2343  1289 ASP B CG  
22222 O OD1 . ASP C 1289 ? 2.4570 1.2187 2.4458 -0.5045 -0.9683 0.2268  1289 ASP B OD1 
22223 O OD2 . ASP C 1289 ? 2.4648 1.2220 2.4862 -0.5114 -0.8908 0.2266  1289 ASP B OD2 
22224 N N   . THR C 1290 ? 1.8668 0.6365 1.8252 -0.4979 -0.8047 0.2371  1290 THR B N   
22225 C CA  . THR C 1290 ? 1.7988 0.5254 1.7138 -0.4741 -0.7456 0.2301  1290 THR B CA  
22226 C C   . THR C 1290 ? 1.6877 0.4158 1.5652 -0.4659 -0.6901 0.2362  1290 THR B C   
22227 O O   . THR C 1290 ? 1.6694 0.3684 1.5124 -0.4500 -0.6401 0.2332  1290 THR B O   
22228 C CB  . THR C 1290 ? 1.8707 0.5207 1.7194 -0.4309 -0.7530 0.2086  1290 THR B CB  
22229 O OG1 . THR C 1290 ? 1.8840 0.5358 1.7775 -0.4427 -0.7958 0.2041  1290 THR B OG1 
22230 C CG2 . THR C 1290 ? 1.8448 0.4568 1.6522 -0.4087 -0.6941 0.2018  1290 THR B CG2 
22231 N N   . ILE C 1291 ? 2.3565 1.1200 2.2424 -0.4776 -0.6988 0.2452  1291 ILE B N   
22232 C CA  . ILE C 1291 ? 2.3164 1.0919 2.1835 -0.4779 -0.6477 0.2532  1291 ILE B CA  
22233 C C   . ILE C 1291 ? 2.2272 1.0738 2.1723 -0.5267 -0.6288 0.2705  1291 ILE B C   
22234 O O   . ILE C 1291 ? 2.2328 1.0839 2.1754 -0.5343 -0.5756 0.2773  1291 ILE B O   
22235 C CB  . ILE C 1291 ? 2.2026 0.9741 2.0320 -0.4606 -0.6619 0.2529  1291 ILE B CB  
22236 C CG1 . ILE C 1291 ? 2.1106 0.9109 1.9438 -0.4716 -0.6160 0.2635  1291 ILE B CG1 
22237 C CG2 . ILE C 1291 ? 2.1909 1.0015 2.0627 -0.4798 -0.7250 0.2571  1291 ILE B CG2 
22238 C CD1 . ILE C 1291 ? 2.0934 0.8873 1.8901 -0.4521 -0.6267 0.2636  1291 ILE B CD1 
22239 N N   . ASN C 1292 ? 1.7251 0.6282 1.7380 -0.5615 -0.6742 0.2782  1292 ASN B N   
22240 C CA  . ASN C 1292 ? 1.6509 0.6608 1.7368 -0.5915 -0.6663 0.2948  1292 ASN B CA  
22241 C C   . ASN C 1292 ? 1.6645 0.6806 1.7696 -0.5924 -0.6454 0.2969  1292 ASN B C   
22242 O O   . ASN C 1292 ? 1.6761 0.7346 1.7952 -0.6004 -0.5990 0.3065  1292 ASN B O   
22243 C CB  . ASN C 1292 ? 1.6146 0.6904 1.7558 -0.6101 -0.7279 0.3031  1292 ASN B CB  
22244 C CG  . ASN C 1292 ? 1.6291 0.6954 1.7498 -0.6085 -0.7538 0.3003  1292 ASN B CG  
22245 O OD1 . ASN C 1292 ? 1.6236 0.6898 1.7234 -0.6068 -0.7196 0.3014  1292 ASN B OD1 
22246 N ND2 . ASN C 1292 ? 1.6363 0.6944 1.7622 -0.6088 -0.8151 0.2971  1292 ASN B ND2 
22247 N N   . ALA C 1293 ? 1.5126 0.4834 1.6159 -0.5834 -0.6793 0.2872  1293 ALA B N   
22248 C CA  . ALA C 1293 ? 1.5440 0.5189 1.6705 -0.5842 -0.6637 0.2889  1293 ALA B CA  
22249 C C   . ALA C 1293 ? 1.5833 0.5207 1.6631 -0.5700 -0.5962 0.2872  1293 ALA B C   
22250 O O   . ALA C 1293 ? 1.5595 0.5439 1.6693 -0.5806 -0.5636 0.2980  1293 ALA B O   
22251 C CB  . ALA C 1293 ? 1.6077 0.5153 1.7230 -0.5699 -0.7057 0.2733  1293 ALA B CB  
22252 N N   . ILE C 1294 ? 2.1882 1.0426 2.1917 -0.5448 -0.5757 0.2757  1294 ILE B N   
22253 C CA  . ILE C 1294 ? 2.2212 1.0333 2.1702 -0.5270 -0.5141 0.2753  1294 ILE B CA  
22254 C C   . ILE C 1294 ? 2.2006 1.0793 2.1606 -0.5428 -0.4712 0.2894  1294 ILE B C   
22255 O O   . ILE C 1294 ? 2.2208 1.1106 2.1680 -0.5421 -0.4214 0.2955  1294 ILE B O   
22256 C CB  . ILE C 1294 ? 2.2711 0.9984 2.1247 -0.4771 -0.5077 0.2572  1294 ILE B CB  
22257 C CG1 . ILE C 1294 ? 2.2934 0.9771 2.1294 -0.4516 -0.5468 0.2394  1294 ILE B CG1 
22258 C CG2 . ILE C 1294 ? 2.2796 0.9743 2.0767 -0.4576 -0.4461 0.2579  1294 ILE B CG2 
22259 C CD1 . ILE C 1294 ? 2.2874 0.9409 2.1135 -0.4398 -0.5216 0.2338  1294 ILE B CD1 
22260 N N   . GLU C 1295 ? 2.2989 1.2222 2.2814 -0.5567 -0.4903 0.2940  1295 GLU B N   
22261 C CA  . GLU C 1295 ? 2.2564 1.2454 2.2531 -0.5719 -0.4519 0.3053  1295 GLU B CA  
22262 C C   . GLU C 1295 ? 2.1484 1.2289 2.2081 -0.5959 -0.4396 0.3184  1295 GLU B C   
22263 O O   . GLU C 1295 ? 2.1318 1.2361 2.1817 -0.5986 -0.3898 0.3245  1295 GLU B O   
22264 C CB  . GLU C 1295 ? 2.3196 1.3439 2.3357 -0.5829 -0.4782 0.3075  1295 GLU B CB  
22265 C CG  . GLU C 1295 ? 2.3484 1.4576 2.3959 -0.6029 -0.4460 0.3187  1295 GLU B CG  
22266 C CD  . GLU C 1295 ? 2.4012 1.5232 2.4491 -0.6066 -0.4592 0.3183  1295 GLU B CD  
22267 O OE1 . GLU C 1295 ? 2.4102 1.4731 2.4304 -0.5930 -0.4919 0.3106  1295 GLU B OE1 
22268 O OE2 . GLU C 1295 ? 2.4181 1.6086 2.4926 -0.6223 -0.4360 0.3256  1295 GLU B OE2 
22269 N N   . GLY C 1296 ? 1.8275 0.9574 1.9485 -0.6114 -0.4865 0.3238  1296 GLY B N   
22270 C CA  . GLY C 1296 ? 1.8138 1.0173 1.9910 -0.6287 -0.4804 0.3377  1296 GLY B CA  
22271 C C   . GLY C 1296 ? 1.8178 0.9831 1.9632 -0.6171 -0.4334 0.3355  1296 GLY B C   
22272 O O   . GLY C 1296 ? 1.8163 0.9966 1.9380 -0.6173 -0.3821 0.3397  1296 GLY B O   
22273 N N   . LEU C 1297 ? 1.3300 0.4413 1.4700 -0.6053 -0.4509 0.3279  1297 LEU B N   
22274 C CA  . LEU C 1297 ? 1.3517 0.4380 1.4750 -0.5966 -0.4125 0.3287  1297 LEU B CA  
22275 C C   . LEU C 1297 ? 1.4205 0.4821 1.4835 -0.5853 -0.3489 0.3290  1297 LEU B C   
22276 O O   . LEU C 1297 ? 1.4189 0.4803 1.4744 -0.5824 -0.3136 0.3339  1297 LEU B O   
22277 C CB  . LEU C 1297 ? 1.3533 0.3559 1.4558 -0.5771 -0.4375 0.3142  1297 LEU B CB  
22278 C CG  . LEU C 1297 ? 1.3374 0.3983 1.5202 -0.5952 -0.4751 0.3233  1297 LEU B CG  
22279 C CD1 . LEU C 1297 ? 1.3326 0.3884 1.5422 -0.5983 -0.5415 0.3168  1297 LEU B CD1 
22280 C CD2 . LEU C 1297 ? 1.3735 0.3978 1.5551 -0.5850 -0.4568 0.3208  1297 LEU B CD2 
22281 N N   . THR C 1298 ? 2.3622 1.4032 2.3827 -0.5785 -0.3359 0.3247  1298 THR B N   
22282 C CA  . THR C 1298 ? 2.3834 1.4094 2.3488 -0.5695 -0.2790 0.3265  1298 THR B CA  
22283 C C   . THR C 1298 ? 2.3361 1.4587 2.3414 -0.5936 -0.2596 0.3380  1298 THR B C   
22284 O O   . THR C 1298 ? 2.3004 1.4596 2.3057 -0.5996 -0.2199 0.3455  1298 THR B O   
22285 C CB  . THR C 1298 ? 2.3878 1.3336 2.2816 -0.5458 -0.2744 0.3162  1298 THR B CB  
22286 O OG1 . THR C 1298 ? 2.4315 1.2937 2.2965 -0.5239 -0.3101 0.3035  1298 THR B OG1 
22287 C CG2 . THR C 1298 ? 2.4042 1.3137 2.2288 -0.5292 -0.2163 0.3178  1298 THR B CG2 
22288 N N   . GLU C 1299 ? 2.0988 1.2612 2.1359 -0.6062 -0.2891 0.3388  1299 GLU B N   
22289 C CA  . GLU C 1299 ? 2.0982 1.3428 2.1644 -0.6254 -0.2719 0.3470  1299 GLU B CA  
22290 C C   . GLU C 1299 ? 2.0756 1.3893 2.1847 -0.6406 -0.2594 0.3589  1299 GLU B C   
22291 O O   . GLU C 1299 ? 2.1146 1.4661 2.2151 -0.6468 -0.2194 0.3632  1299 GLU B O   
22292 C CB  . GLU C 1299 ? 2.1000 1.3881 2.2105 -0.6390 -0.3175 0.3488  1299 GLU B CB  
22293 C CG  . GLU C 1299 ? 2.1632 1.4950 2.2726 -0.6482 -0.2954 0.3503  1299 GLU B CG  
22294 C CD  . GLU C 1299 ? 2.2536 1.5143 2.2964 -0.6296 -0.2649 0.3402  1299 GLU B CD  
22295 O OE1 . GLU C 1299 ? 2.3085 1.5068 2.3266 -0.6157 -0.2909 0.3329  1299 GLU B OE1 
22296 O OE2 . GLU C 1299 ? 2.2655 1.5300 2.2775 -0.6275 -0.2159 0.3401  1299 GLU B OE2 
22297 N N   . TYR C 1300 ? 1.3396 0.6641 1.4927 -0.6452 -0.2959 0.3638  1300 TYR B N   
22298 C CA  . TYR C 1300 ? 1.2860 0.6704 1.4852 -0.6579 -0.2924 0.3773  1300 TYR B CA  
22299 C C   . TYR C 1300 ? 1.3677 0.7273 1.5329 -0.6486 -0.2439 0.3777  1300 TYR B C   
22300 O O   . TYR C 1300 ? 1.2911 0.7082 1.4765 -0.6595 -0.2214 0.3884  1300 TYR B O   
22301 C CB  . TYR C 1300 ? 1.3208 0.7184 1.5771 -0.6638 -0.3469 0.3834  1300 TYR B CB  
22302 C CG  . TYR C 1300 ? 1.3069 0.7466 1.6046 -0.6718 -0.3409 0.3975  1300 TYR B CG  
22303 C CD1 . TYR C 1300 ? 1.3041 0.8248 1.6614 -0.6900 -0.3641 0.4159  1300 TYR B CD1 
22304 C CD2 . TYR C 1300 ? 1.2962 0.6920 1.5693 -0.6601 -0.3101 0.3941  1300 TYR B CD2 
22305 C CE1 . TYR C 1300 ? 1.3044 0.8603 1.6981 -0.6963 -0.3584 0.4305  1300 TYR B CE1 
22306 C CE2 . TYR C 1300 ? 1.2987 0.7333 1.6108 -0.6672 -0.3031 0.4078  1300 TYR B CE2 
22307 C CZ  . TYR C 1300 ? 1.3218 0.8358 1.6951 -0.6853 -0.3279 0.4258  1300 TYR B CZ  
22308 O OH  . TYR C 1300 ? 1.3614 0.9086 1.7719 -0.6910 -0.3222 0.4405  1300 TYR B OH  
22309 N N   . SER C 1301 ? 1.4702 0.7438 1.5815 -0.6276 -0.2291 0.3670  1301 SER B N   
22310 C CA  . SER C 1301 ? 1.5272 0.7777 1.6015 -0.6177 -0.1821 0.3688  1301 SER B CA  
22311 C C   . SER C 1301 ? 1.4841 0.7428 1.5091 -0.6156 -0.1336 0.3675  1301 SER B C   
22312 O O   . SER C 1301 ? 1.4470 0.7040 1.4410 -0.6107 -0.0915 0.3705  1301 SER B O   
22313 C CB  . SER C 1301 ? 1.6327 0.7877 1.6615 -0.5941 -0.1815 0.3592  1301 SER B CB  
22314 O OG  . SER C 1301 ? 1.6668 0.8290 1.7247 -0.5952 -0.1795 0.3658  1301 SER B OG  
22315 N N   . LEU C 1302 ? 2.1641 1.4338 2.1845 -0.6199 -0.1419 0.3631  1302 LEU B N   
22316 C CA  . LEU C 1302 ? 2.2270 1.5107 2.2105 -0.6205 -0.1024 0.3607  1302 LEU B CA  
22317 C C   . LEU C 1302 ? 2.2361 1.6114 2.2639 -0.6425 -0.0959 0.3688  1302 LEU B C   
22318 O O   . LEU C 1302 ? 2.3212 1.7125 2.3206 -0.6434 -0.0554 0.3683  1302 LEU B O   
22319 C CB  . LEU C 1302 ? 2.2851 1.5394 2.2492 -0.6154 -0.1165 0.3526  1302 LEU B CB  
22320 C CG  . LEU C 1302 ? 2.3568 1.5285 2.2394 -0.5914 -0.0847 0.3449  1302 LEU B CG  
22321 C CD1 . LEU C 1302 ? 2.3574 1.5020 2.2316 -0.5868 -0.1075 0.3388  1302 LEU B CD1 
22322 C CD2 . LEU C 1302 ? 2.3807 1.5671 2.2241 -0.5904 -0.0310 0.3457  1302 LEU B CD2 
22323 N N   . LEU C 1303 ? 2.0636 1.4941 2.1564 -0.6588 -0.1387 0.3760  1303 LEU B N   
22324 C CA  . LEU C 1303 ? 1.9762 1.4930 2.1141 -0.6798 -0.1450 0.3855  1303 LEU B CA  
22325 C C   . LEU C 1303 ? 1.9053 1.4681 2.0697 -0.6887 -0.1350 0.3981  1303 LEU B C   
22326 O O   . LEU C 1303 ? 1.9042 1.5045 2.0580 -0.6967 -0.1065 0.4000  1303 LEU B O   
22327 C CB  . LEU C 1303 ? 1.9573 1.5062 2.1466 -0.6906 -0.1983 0.3904  1303 LEU B CB  
22328 C CG  . LEU C 1303 ? 1.9138 1.5423 2.1469 -0.7106 -0.2177 0.4010  1303 LEU B CG  
22329 C CD1 . LEU C 1303 ? 1.8696 1.5442 2.1450 -0.7209 -0.2310 0.4175  1303 LEU B CD1 
22330 C CD2 . LEU C 1303 ? 1.9509 1.6002 2.1532 -0.7156 -0.1784 0.3946  1303 LEU B CD2 
22331 N N   . VAL C 1304 ? 1.3478 0.9054 1.5465 -0.6874 -0.1601 0.4061  1304 VAL B N   
22332 C CA  . VAL C 1304 ? 1.3991 0.9760 1.6128 -0.6894 -0.1453 0.4168  1304 VAL B CA  
22333 C C   . VAL C 1304 ? 1.4201 0.9530 1.5706 -0.6751 -0.0925 0.4088  1304 VAL B C   
22334 O O   . VAL C 1304 ? 1.4784 0.9728 1.5754 -0.6655 -0.0680 0.3966  1304 VAL B O   
22335 C CB  . VAL C 1304 ? 1.4414 0.9943 1.6911 -0.6846 -0.1777 0.4217  1304 VAL B CB  
22336 C CG1 . VAL C 1304 ? 1.4834 1.0607 1.7581 -0.6876 -0.1658 0.4348  1304 VAL B CG1 
22337 C CG2 . VAL C 1304 ? 1.4101 0.9935 1.7140 -0.6953 -0.2327 0.4281  1304 VAL B CG2 
22338 N N   . LYS C 1305 ? 1.8462 0.6949 1.7179 -0.6144 0.0289  0.2551  1305 LYS B N   
22339 C CA  . LYS C 1305 ? 1.8788 0.7319 1.7012 -0.5977 0.0480  0.2469  1305 LYS B CA  
22340 C C   . LYS C 1305 ? 1.9140 0.7635 1.6858 -0.5688 0.0058  0.2344  1305 LYS B C   
22341 O O   . LYS C 1305 ? 1.9167 0.7706 1.6782 -0.5687 -0.0244 0.2269  1305 LYS B O   
22342 C CB  . LYS C 1305 ? 1.9102 0.7870 1.7126 -0.6213 0.1050  0.2387  1305 LYS B CB  
22343 C CG  . LYS C 1305 ? 2.0173 0.8927 1.7952 -0.6116 0.1408  0.2386  1305 LYS B CG  
22344 C CD  . LYS C 1305 ? 2.1842 1.0733 1.9798 -0.6434 0.2050  0.2422  1305 LYS B CD  
22345 C CE  . LYS C 1305 ? 2.3353 1.2175 2.1974 -0.6671 0.2137  0.2580  1305 LYS B CE  
22346 N NZ  . LYS C 1305 ? 2.3445 1.2408 2.2284 -0.7039 0.2719  0.2608  1305 LYS B NZ  
22347 N N   . GLN C 1306 ? 2.3370 1.1773 2.0773 -0.5444 0.0048  0.2327  1306 GLN B N   
22348 C CA  . GLN C 1306 ? 2.3437 1.1760 2.0362 -0.5142 -0.0356 0.2222  1306 GLN B CA  
22349 C C   . GLN C 1306 ? 2.3779 1.2316 2.0211 -0.5173 -0.0274 0.2039  1306 GLN B C   
22350 O O   . GLN C 1306 ? 2.3989 1.2744 2.0334 -0.5389 0.0178  0.1982  1306 GLN B O   
22351 C CB  . GLN C 1306 ? 2.8652 1.6821 2.5359 -0.4891 -0.0337 0.2250  1306 GLN B CB  
22352 C CG  . GLN C 1306 ? 3.5103 2.3001 3.2084 -0.4684 -0.0733 0.2392  1306 GLN B CG  
22353 C CD  . GLN C 1306 ? 2.6561 1.4313 2.3264 -0.4428 -0.0715 0.2407  1306 GLN B CD  
22354 O OE1 . GLN C 1306 ? 2.6833 1.4555 2.3016 -0.4220 -0.0871 0.2284  1306 GLN B OE1 
22355 N NE2 . GLN C 1306 ? 2.6599 1.4257 2.3653 -0.4447 -0.0522 0.2560  1306 GLN B NE2 
22356 N N   . LEU C 1307 ? 2.3281 1.1753 1.9386 -0.4955 -0.0716 0.1950  1307 LEU B N   
22357 C CA  . LEU C 1307 ? 2.3410 1.2074 1.9101 -0.4970 -0.0737 0.1788  1307 LEU B CA  
22358 C C   . LEU C 1307 ? 2.3676 1.2286 1.8800 -0.4681 -0.0876 0.1674  1307 LEU B C   
22359 O O   . LEU C 1307 ? 2.3816 1.2286 1.8736 -0.4457 -0.1334 0.1632  1307 LEU B O   
22360 C CB  . LEU C 1307 ? 2.3288 1.1924 1.9124 -0.4989 -0.1155 0.1783  1307 LEU B CB  
22361 C CG  . LEU C 1307 ? 2.2920 1.1415 1.9368 -0.5112 -0.1284 0.1943  1307 LEU B CG  
22362 C CD1 . LEU C 1307 ? 2.3417 1.1617 1.9931 -0.4836 -0.1733 0.2023  1307 LEU B CD1 
22363 C CD2 . LEU C 1307 ? 2.2644 1.1237 1.9331 -0.5324 -0.1401 0.1934  1307 LEU B CD2 
22364 N N   . ARG C 1308 ? 2.4073 1.2789 1.8937 -0.4698 -0.0463 0.1620  1308 ARG B N   
22365 C CA  . ARG C 1308 ? 2.4051 1.2713 1.8372 -0.4438 -0.0518 0.1511  1308 ARG B CA  
22366 C C   . ARG C 1308 ? 2.3662 1.2222 1.7678 -0.4200 -0.1034 0.1427  1308 ARG B C   
22367 O O   . ARG C 1308 ? 2.3265 1.1974 1.7159 -0.4261 -0.1142 0.1342  1308 ARG B O   
22368 C CB  . ARG C 1308 ? 2.4144 1.3071 1.8098 -0.4555 -0.0058 0.1381  1308 ARG B CB  
22369 C CG  . ARG C 1308 ? 2.4671 1.3600 1.8018 -0.4307 -0.0204 0.1225  1308 ARG B CG  
22370 C CD  . ARG C 1308 ? 2.5192 1.4361 1.8185 -0.4409 0.0278  0.1108  1308 ARG B CD  
22371 N NE  . ARG C 1308 ? 2.5919 1.5117 1.8340 -0.4190 0.0122  0.0949  1308 ARG B NE  
22372 C CZ  . ARG C 1308 ? 2.6348 1.5663 1.8570 -0.4154 -0.0126 0.0854  1308 ARG B CZ  
22373 N NH1 . ARG C 1308 ? 2.5794 1.5202 1.8334 -0.4323 -0.0253 0.0901  1308 ARG B NH1 
22374 N NH2 . ARG C 1308 ? 2.7090 1.6420 1.8792 -0.3946 -0.0244 0.0714  1308 ARG B NH2 
22375 N N   . LEU C 1309 ? 2.0883 0.9183 1.4774 -0.3929 -0.1349 0.1456  1309 LEU B N   
22376 C CA  . LEU C 1309 ? 2.1127 0.9284 1.4731 -0.3690 -0.1851 0.1388  1309 LEU B CA  
22377 C C   . LEU C 1309 ? 2.0935 0.9215 1.3944 -0.3571 -0.1802 0.1208  1309 LEU B C   
22378 O O   . LEU C 1309 ? 2.1722 1.0099 1.4466 -0.3570 -0.1445 0.1144  1309 LEU B O   
22379 C CB  . LEU C 1309 ? 2.1054 0.8897 1.4671 -0.3445 -0.2157 0.1471  1309 LEU B CB  
22380 C CG  . LEU C 1309 ? 2.1466 0.9120 1.5571 -0.3454 -0.2500 0.1625  1309 LEU B CG  
22381 C CD1 . LEU C 1309 ? 2.0749 0.8153 1.4951 -0.3280 -0.2620 0.1738  1309 LEU B CD1 
22382 C CD2 . LEU C 1309 ? 2.1102 0.8671 1.5073 -0.3343 -0.2988 0.1568  1309 LEU B CD2 
22383 N N   . SER C 1310 ? 2.1578 0.9844 1.4370 -0.3463 -0.2161 0.1128  1310 SER B N   
22384 C CA  . SER C 1310 ? 2.1502 0.9855 1.3718 -0.3311 -0.2168 0.0960  1310 SER B CA  
22385 C C   . SER C 1310 ? 2.2130 1.0431 1.4129 -0.3172 -0.2605 0.0886  1310 SER B C   
22386 O O   . SER C 1310 ? 2.1775 1.0266 1.3425 -0.3161 -0.2535 0.0755  1310 SER B O   
22387 C CB  . SER C 1310 ? 2.1865 1.0555 1.3934 -0.3512 -0.1670 0.0870  1310 SER B CB  
22388 O OG  . SER C 1310 ? 2.2476 1.1250 1.3989 -0.3355 -0.1669 0.0711  1310 SER B OG  
22389 N N   . MET C 1311 ? 2.0380 0.8425 1.2581 -0.3065 -0.3045 0.0970  1311 MET B N   
22390 C CA  . MET C 1311 ? 2.0906 0.8835 1.2899 -0.2904 -0.3501 0.0913  1311 MET B CA  
22391 C C   . MET C 1311 ? 2.1959 0.9828 1.3353 -0.2652 -0.3611 0.0771  1311 MET B C   
22392 O O   . MET C 1311 ? 2.2010 1.0013 1.3112 -0.2638 -0.3289 0.0687  1311 MET B O   
22393 C CB  . MET C 1311 ? 2.2443 1.0063 1.4712 -0.2806 -0.3935 0.1031  1311 MET B CB  
22394 C CG  . MET C 1311 ? 2.2026 0.9665 1.4675 -0.2957 -0.4137 0.1095  1311 MET B CG  
22395 S SD  . MET C 1311 ? 2.0969 0.8461 1.4276 -0.3093 -0.4184 0.1293  1311 MET B SD  
22396 C CE  . MET C 1311 ? 2.1098 0.8845 1.4627 -0.3337 -0.3555 0.1330  1311 MET B CE  
22397 N N   . ASP C 1312 ? 2.3060 1.0719 1.4265 -0.2455 -0.4063 0.0743  1312 ASP B N   
22398 C CA  . ASP C 1312 ? 2.3155 1.0738 1.3793 -0.2214 -0.4189 0.0608  1312 ASP B CA  
22399 C C   . ASP C 1312 ? 2.3668 1.0958 1.4210 -0.2020 -0.4718 0.0618  1312 ASP B C   
22400 O O   . ASP C 1312 ? 2.3836 1.1141 1.4087 -0.1923 -0.4908 0.0523  1312 ASP B O   
22401 C CB  . ASP C 1312 ? 2.3946 1.1845 1.4318 -0.2285 -0.3969 0.0477  1312 ASP B CB  
22402 C CG  . ASP C 1312 ? 2.5266 1.3147 1.5064 -0.2073 -0.3940 0.0334  1312 ASP B CG  
22403 O OD1 . ASP C 1312 ? 2.5765 1.3344 1.5325 -0.1835 -0.4254 0.0320  1312 ASP B OD1 
22404 O OD2 . ASP C 1312 ? 2.5743 1.3909 1.5326 -0.2149 -0.3601 0.0235  1312 ASP B OD2 
22405 N N   . ILE C 1313 ? 2.2277 0.9299 1.3065 -0.1965 -0.4952 0.0736  1313 ILE B N   
22406 C CA  . ILE C 1313 ? 2.2143 0.8900 1.2992 -0.1855 -0.5448 0.0783  1313 ILE B CA  
22407 C C   . ILE C 1313 ? 2.3162 0.9709 1.3495 -0.1591 -0.5772 0.0677  1313 ILE B C   
22408 O O   . ILE C 1313 ? 2.4315 1.0858 1.4215 -0.1448 -0.5658 0.0573  1313 ILE B O   
22409 C CB  . ILE C 1313 ? 2.1396 0.7919 1.2605 -0.1850 -0.5616 0.0934  1313 ILE B CB  
22410 C CG1 . ILE C 1313 ? 2.1039 0.7755 1.2668 -0.2072 -0.5194 0.1028  1313 ILE B CG1 
22411 C CG2 . ILE C 1313 ? 2.1135 0.7490 1.2579 -0.1856 -0.6038 0.1002  1313 ILE B CG2 
22412 C CD1 . ILE C 1313 ? 2.0828 0.7418 1.3003 -0.2170 -0.5315 0.1202  1313 ILE B CD1 
22413 N N   . ASP C 1314 ? 2.7799 1.4165 1.8179 -0.1533 -0.6177 0.0702  1314 ASP B N   
22414 C CA  . ASP C 1314 ? 2.8157 1.4263 1.8089 -0.1284 -0.6532 0.0624  1314 ASP B CA  
22415 C C   . ASP C 1314 ? 2.7821 1.3658 1.7946 -0.1248 -0.6985 0.0709  1314 ASP B C   
22416 O O   . ASP C 1314 ? 2.7651 1.3555 1.7957 -0.1348 -0.7103 0.0720  1314 ASP B O   
22417 C CB  . ASP C 1314 ? 2.8581 1.4857 1.8119 -0.1229 -0.6463 0.0476  1314 ASP B CB  
22418 C CG  . ASP C 1314 ? 2.9459 1.5456 1.8562 -0.0983 -0.6852 0.0400  1314 ASP B CG  
22419 O OD1 . ASP C 1314 ? 2.9276 1.5114 1.8488 -0.0970 -0.7191 0.0441  1314 ASP B OD1 
22420 O OD2 . ASP C 1314 ? 3.0408 1.6336 1.9055 -0.0809 -0.6812 0.0298  1314 ASP B OD2 
22421 N N   . VAL C 1315 ? 2.5055 1.0591 1.5148 -0.1115 -0.7227 0.0772  1315 VAL B N   
22422 C CA  . VAL C 1315 ? 2.5045 1.0280 1.5197 -0.1035 -0.7693 0.0832  1315 VAL B CA  
22423 C C   . VAL C 1315 ? 2.5641 1.0683 1.5231 -0.0811 -0.7949 0.0708  1315 VAL B C   
22424 O O   . VAL C 1315 ? 2.6163 1.1231 1.5337 -0.0685 -0.7794 0.0602  1315 VAL B O   
22425 C CB  . VAL C 1315 ? 2.5021 1.0029 1.5365 -0.0990 -0.7835 0.0956  1315 VAL B CB  
22426 C CG1 . VAL C 1315 ? 2.4386 0.9242 1.4283 -0.0789 -0.7805 0.0894  1315 VAL B CG1 
22427 C CG2 . VAL C 1315 ? 2.3926 0.8664 1.4415 -0.0957 -0.8294 0.1033  1315 VAL B CG2 
22428 N N   . SER C 1316 ? 2.8842 1.3692 1.8416 -0.0766 -0.8325 0.0717  1316 SER B N   
22429 C CA  . SER C 1316 ? 3.0110 1.4782 1.9176 -0.0573 -0.8567 0.0601  1316 SER B CA  
22430 C C   . SER C 1316 ? 3.0790 1.5206 1.9903 -0.0541 -0.9001 0.0639  1316 SER B C   
22431 O O   . SER C 1316 ? 3.0547 1.5032 2.0079 -0.0704 -0.9059 0.0721  1316 SER B O   
22432 C CB  . SER C 1316 ? 3.0222 1.5184 1.9084 -0.0598 -0.8311 0.0481  1316 SER B CB  
22433 O OG  . SER C 1316 ? 3.0959 1.5834 1.9268 -0.0394 -0.8307 0.0355  1316 SER B OG  
22434 N N   . TYR C 1317 ? 3.3977 1.8091 2.2644 -0.0334 -0.9297 0.0575  1317 TYR B N   
22435 C CA  . TYR C 1317 ? 3.4673 1.8511 2.3296 -0.0282 -0.9714 0.0596  1317 TYR B CA  
22436 C C   . TYR C 1317 ? 3.4872 1.8835 2.3403 -0.0306 -0.9718 0.0520  1317 TYR B C   
22437 O O   . TYR C 1317 ? 3.5080 1.9255 2.3374 -0.0272 -0.9475 0.0419  1317 TYR B O   
22438 C CB  . TYR C 1317 ? 3.5862 1.9323 2.4012 -0.0056 -1.0006 0.0551  1317 TYR B CB  
22439 C CG  . TYR C 1317 ? 3.6462 1.9784 2.4702 -0.0030 -1.0033 0.0635  1317 TYR B CG  
22440 C CD1 . TYR C 1317 ? 3.6974 2.0358 2.4994 0.0048  -0.9784 0.0588  1317 TYR B CD1 
22441 C CD2 . TYR C 1317 ? 3.6636 1.9779 2.5199 -0.0092 -1.0296 0.0766  1317 TYR B CD2 
22442 C CE1 . TYR C 1317 ? 3.7318 2.0576 2.5427 0.0072  -0.9802 0.0672  1317 TYR B CE1 
22443 C CE2 . TYR C 1317 ? 3.7002 2.0033 2.5669 -0.0069 -1.0321 0.0854  1317 TYR B CE2 
22444 C CZ  . TYR C 1317 ? 3.7399 2.0483 2.5837 0.0015  -1.0073 0.0809  1317 TYR B CZ  
22445 O OH  . TYR C 1317 ? 3.7612 2.0580 2.6148 0.0043  -1.0097 0.0902  1317 TYR B OH  
22446 N N   . LYS C 1318 ? 3.3777 1.7607 2.2486 -0.0360 -0.9998 0.0569  1318 LYS B N   
22447 C CA  . LYS C 1318 ? 3.4045 1.7991 2.2723 -0.0401 -1.0013 0.0514  1318 LYS B CA  
22448 C C   . LYS C 1318 ? 3.5230 1.9077 2.3337 -0.0194 -1.0078 0.0383  1318 LYS B C   
22449 O O   . LYS C 1318 ? 3.5141 1.9229 2.3138 -0.0205 -0.9889 0.0308  1318 LYS B O   
22450 C CB  . LYS C 1318 ? 3.3837 1.7601 2.2777 -0.0481 -1.0334 0.0590  1318 LYS B CB  
22451 C CG  . LYS C 1318 ? 3.4311 1.8130 2.3158 -0.0492 -1.0402 0.0531  1318 LYS B CG  
22452 C CD  . LYS C 1318 ? 3.3990 1.8057 2.3347 -0.0734 -1.0278 0.0597  1318 LYS B CD  
22453 C CE  . LYS C 1318 ? 3.3970 1.7796 2.3606 -0.0811 -1.0607 0.0685  1318 LYS B CE  
22454 N NZ  . LYS C 1318 ? 3.3661 1.7670 2.3650 -0.1004 -1.0550 0.0713  1318 LYS B NZ  
22455 N N   . HIS C 1319 ? 3.4823 1.8315 2.2566 -0.0008 -1.0344 0.0357  1319 HIS B N   
22456 C CA  . HIS C 1319 ? 3.6100 1.9445 2.3294 0.0195  -1.0438 0.0237  1319 HIS B CA  
22457 C C   . HIS C 1319 ? 3.7810 2.1066 2.4624 0.0353  -1.0339 0.0172  1319 HIS B C   
22458 O O   . HIS C 1319 ? 3.8181 2.1521 2.4623 0.0471  -1.0191 0.0059  1319 HIS B O   
22459 C CB  . HIS C 1319 ? 3.5817 1.8775 2.2848 0.0284  -1.0861 0.0250  1319 HIS B CB  
22460 C CG  . HIS C 1319 ? 3.5256 1.8255 2.2677 0.0124  -1.0989 0.0323  1319 HIS B CG  
22461 N ND1 . HIS C 1319 ? 3.4848 1.7785 2.2704 -0.0020 -1.1111 0.0443  1319 HIS B ND1 
22462 C CD2 . HIS C 1319 ? 3.5373 1.8462 2.2810 0.0087  -1.1013 0.0293  1319 HIS B CD2 
22463 C CE1 . HIS C 1319 ? 3.4672 1.7652 2.2790 -0.0142 -1.1206 0.0478  1319 HIS B CE1 
22464 N NE2 . HIS C 1319 ? 3.5018 1.8087 2.2886 -0.0080 -1.1149 0.0389  1319 HIS B NE2 
22465 N N   . LYS C 1320 ? 3.9424 2.2513 2.6336 0.0354  -1.0419 0.0244  1320 LYS B N   
22466 C CA  . LYS C 1320 ? 4.1223 2.4235 2.7825 0.0482  -1.0306 0.0194  1320 LYS B CA  
22467 C C   . LYS C 1320 ? 4.1911 2.5313 2.8557 0.0420  -0.9857 0.0141  1320 LYS B C   
22468 O O   . LYS C 1320 ? 4.1646 2.5366 2.8706 0.0233  -0.9629 0.0192  1320 LYS B O   
22469 C CB  . LYS C 1320 ? 4.1629 2.4450 2.8434 0.0455  -1.0441 0.0306  1320 LYS B CB  
22470 C CG  . LYS C 1320 ? 4.2380 2.5202 2.8991 0.0535  -1.0243 0.0279  1320 LYS B CG  
22471 C CD  . LYS C 1320 ? 4.3577 2.6174 2.9564 0.0756  -1.0322 0.0147  1320 LYS B CD  
22472 C CE  . LYS C 1320 ? 4.3994 2.6578 2.9779 0.0834  -1.0125 0.0116  1320 LYS B CE  
22473 N NZ  . LYS C 1320 ? 4.4716 2.7102 2.9891 0.1041  -1.0163 -0.0023 1320 LYS B NZ  
22474 N N   . GLY C 1321 ? 3.8519 2.1890 2.4731 0.0571  -0.9728 0.0036  1321 GLY B N   
22475 C CA  . GLY C 1321 ? 3.8401 2.2113 2.4604 0.0525  -0.9304 -0.0022 1321 GLY B CA  
22476 C C   . GLY C 1321 ? 3.7685 2.1591 2.4348 0.0348  -0.9075 0.0083  1321 GLY B C   
22477 O O   . GLY C 1321 ? 3.7781 2.1544 2.4763 0.0278  -0.9254 0.0204  1321 GLY B O   
22478 N N   . ALA C 1322 ? 4.2721 2.6959 2.9419 0.0274  -0.8671 0.0038  1322 ALA B N   
22479 C CA  . ALA C 1322 ? 4.1454 2.5915 2.8605 0.0086  -0.8404 0.0134  1322 ALA B CA  
22480 C C   . ALA C 1322 ? 4.0697 2.4954 2.7875 0.0134  -0.8432 0.0202  1322 ALA B C   
22481 O O   . ALA C 1322 ? 4.0650 2.4732 2.7419 0.0301  -0.8442 0.0131  1322 ALA B O   
22482 C CB  . ALA C 1322 ? 4.0949 2.5823 2.8113 -0.0018 -0.7950 0.0064  1322 ALA B CB  
22483 N N   . LEU C 1323 ? 3.9786 2.4065 2.7458 -0.0015 -0.8449 0.0344  1323 LEU B N   
22484 C CA  . LEU C 1323 ? 3.9011 2.3208 2.6842 -0.0025 -0.8374 0.0433  1323 LEU B CA  
22485 C C   . LEU C 1323 ? 3.9281 2.3831 2.7278 -0.0159 -0.7883 0.0422  1323 LEU B C   
22486 O O   . LEU C 1323 ? 4.0053 2.4884 2.7990 -0.0228 -0.7638 0.0337  1323 LEU B O   
22487 C CB  . LEU C 1323 ? 3.5853 1.9934 2.4165 -0.0131 -0.8613 0.0595  1323 LEU B CB  
22488 C CG  . LEU C 1323 ? 3.3364 1.7427 2.2017 -0.0197 -0.8521 0.0728  1323 LEU B CG  
22489 C CD1 . LEU C 1323 ? 3.2536 1.6388 2.0803 -0.0017 -0.8533 0.0693  1323 LEU B CD1 
22490 C CD2 . LEU C 1323 ? 3.1682 1.5582 2.0734 -0.0267 -0.8849 0.0873  1323 LEU B CD2 
22491 N N   . HIS C 1324 ? 3.4810 1.9350 2.3017 -0.0202 -0.7736 0.0511  1324 HIS B N   
22492 C CA  . HIS C 1324 ? 3.4412 1.9246 2.2724 -0.0314 -0.7258 0.0497  1324 HIS B CA  
22493 C C   . HIS C 1324 ? 3.3615 1.8823 2.2294 -0.0548 -0.6963 0.0512  1324 HIS B C   
22494 O O   . HIS C 1324 ? 3.3132 1.8384 2.2081 -0.0649 -0.7126 0.0558  1324 HIS B O   
22495 C CB  . HIS C 1324 ? 3.4496 1.9235 2.3007 -0.0322 -0.7162 0.0608  1324 HIS B CB  
22496 C CG  . HIS C 1324 ? 3.4812 1.9572 2.3923 -0.0484 -0.7227 0.0782  1324 HIS B CG  
22497 N ND1 . HIS C 1324 ? 3.4684 1.9711 2.4220 -0.0685 -0.6863 0.0858  1324 HIS B ND1 
22498 C CD2 . HIS C 1324 ? 3.5071 1.9613 2.4424 -0.0476 -0.7609 0.0895  1324 HIS B CD2 
22499 C CE1 . HIS C 1324 ? 3.4548 1.9520 2.4571 -0.0789 -0.7017 0.1011  1324 HIS B CE1 
22500 N NE2 . HIS C 1324 ? 3.4831 1.9517 2.4756 -0.0666 -0.7472 0.1036  1324 HIS B NE2 
22501 N N   . ASN C 1325 ? 3.0810 1.6279 1.9473 -0.0634 -0.6522 0.0468  1325 ASN B N   
22502 C CA  . ASN C 1325 ? 3.0693 1.6533 1.9655 -0.0863 -0.6182 0.0472  1325 ASN B CA  
22503 C C   . ASN C 1325 ? 2.9968 1.6005 1.8942 -0.0947 -0.5717 0.0459  1325 ASN B C   
22504 O O   . ASN C 1325 ? 3.0184 1.6219 1.8735 -0.0824 -0.5567 0.0349  1325 ASN B O   
22505 C CB  . ASN C 1325 ? 3.1779 1.7794 2.0484 -0.0856 -0.6178 0.0345  1325 ASN B CB  
22506 C CG  . ASN C 1325 ? 3.2843 1.8858 2.0971 -0.0680 -0.6079 0.0188  1325 ASN B CG  
22507 O OD1 . ASN C 1325 ? 3.3302 1.9103 2.1062 -0.0488 -0.6376 0.0115  1325 ASN B OD1 
22508 N ND2 . ASN C 1325 ? 3.3017 1.9267 2.1057 -0.0749 -0.5653 0.0131  1325 ASN B ND2 
22509 N N   . TYR C 1326 ? 3.1409 1.7612 2.0866 -0.1158 -0.5480 0.0571  1326 TYR B N   
22510 C CA  . TYR C 1326 ? 3.1442 1.7779 2.0928 -0.1231 -0.5054 0.0578  1326 TYR B CA  
22511 C C   . TYR C 1326 ? 2.9775 1.6448 1.9636 -0.1504 -0.4655 0.0617  1326 TYR B C   
22512 O O   . TYR C 1326 ? 2.9224 1.5940 1.9556 -0.1665 -0.4710 0.0731  1326 TYR B O   
22513 C CB  . TYR C 1326 ? 3.2512 1.8597 2.2165 -0.1159 -0.5151 0.0701  1326 TYR B CB  
22514 C CG  . TYR C 1326 ? 3.3084 1.9063 2.3267 -0.1252 -0.5389 0.0870  1326 TYR B CG  
22515 C CD1 . TYR C 1326 ? 3.3122 1.9185 2.3776 -0.1415 -0.5146 0.1006  1326 TYR B CD1 
22516 C CD2 . TYR C 1326 ? 3.3626 1.9405 2.3831 -0.1172 -0.5853 0.0896  1326 TYR B CD2 
22517 C CE1 . TYR C 1326 ? 3.3099 1.9065 2.4243 -0.1496 -0.5362 0.1162  1326 TYR B CE1 
22518 C CE2 . TYR C 1326 ? 3.3618 1.9298 2.4301 -0.1257 -0.6073 0.1047  1326 TYR B CE2 
22519 C CZ  . TYR C 1326 ? 3.3366 1.9145 2.4522 -0.1418 -0.5828 0.1180  1326 TYR B CZ  
22520 O OH  . TYR C 1326 ? 3.3132 1.8818 2.4774 -0.1503 -0.6044 0.1331  1326 TYR B OH  
22521 N N   . LYS C 1327 ? 2.9694 1.6598 1.9336 -0.1561 -0.4240 0.0521  1327 LYS B N   
22522 C CA  . LYS C 1327 ? 2.8402 1.5614 1.8369 -0.1827 -0.3811 0.0559  1327 LYS B CA  
22523 C C   . LYS C 1327 ? 2.6914 1.4035 1.7291 -0.1914 -0.3673 0.0712  1327 LYS B C   
22524 O O   . LYS C 1327 ? 2.6943 1.3934 1.7164 -0.1805 -0.3563 0.0718  1327 LYS B O   
22525 C CB  . LYS C 1327 ? 2.9073 1.6542 1.8678 -0.1862 -0.3398 0.0417  1327 LYS B CB  
22526 C CG  . LYS C 1327 ? 2.9245 1.7066 1.9150 -0.2161 -0.2959 0.0439  1327 LYS B CG  
22527 C CD  . LYS C 1327 ? 2.9873 1.8009 1.9445 -0.2222 -0.2716 0.0286  1327 LYS B CD  
22528 C CE  . LYS C 1327 ? 2.9239 1.7720 1.9142 -0.2541 -0.2346 0.0318  1327 LYS B CE  
22529 N NZ  . LYS C 1327 ? 2.8612 1.7158 1.8823 -0.2656 -0.2579 0.0373  1327 LYS B NZ  
22530 N N   . MET C 1328 ? 2.3668 1.0850 1.4568 -0.2105 -0.3689 0.0836  1328 MET B N   
22531 C CA  . MET C 1328 ? 2.2118 0.9265 1.3485 -0.2230 -0.3518 0.0993  1328 MET B CA  
22532 C C   . MET C 1328 ? 2.2018 0.9457 1.3488 -0.2456 -0.2941 0.0978  1328 MET B C   
22533 O O   . MET C 1328 ? 2.1947 0.9638 1.3228 -0.2556 -0.2727 0.0867  1328 MET B O   
22534 C CB  . MET C 1328 ? 2.1121 0.8211 1.2988 -0.2343 -0.3790 0.1120  1328 MET B CB  
22535 C CG  . MET C 1328 ? 2.1963 0.9037 1.4375 -0.2497 -0.3631 0.1289  1328 MET B CG  
22536 S SD  . MET C 1328 ? 2.1333 0.8236 1.4247 -0.2538 -0.4082 0.1434  1328 MET B SD  
22537 C CE  . MET C 1328 ? 2.2031 0.8558 1.4742 -0.2233 -0.4541 0.1478  1328 MET B CE  
22538 N N   . THR C 1329 ? 2.2855 1.0263 1.4606 -0.2534 -0.2684 0.1089  1329 THR B N   
22539 C CA  . THR C 1329 ? 2.2653 1.0318 1.4582 -0.2780 -0.2142 0.1100  1329 THR B CA  
22540 C C   . THR C 1329 ? 2.2276 0.9802 1.4626 -0.2822 -0.2048 0.1271  1329 THR B C   
22541 O O   . THR C 1329 ? 2.2258 0.9557 1.4832 -0.2717 -0.2416 0.1379  1329 THR B O   
22542 C CB  . THR C 1329 ? 2.3200 1.1005 1.4650 -0.2747 -0.1766 0.0958  1329 THR B CB  
22543 O OG1 . THR C 1329 ? 2.3541 1.1099 1.4665 -0.2490 -0.1898 0.0935  1329 THR B OG1 
22544 C CG2 . THR C 1329 ? 2.3574 1.1584 1.4649 -0.2750 -0.1778 0.0792  1329 THR B CG2 
22545 N N   . ASP C 1330 ? 2.5306 1.2961 1.7763 -0.2972 -0.1559 0.1300  1330 ASP B N   
22546 C CA  . ASP C 1330 ? 2.5485 1.2996 1.8319 -0.2990 -0.1450 0.1466  1330 ASP B CA  
22547 C C   . ASP C 1330 ? 2.6199 1.3507 1.8691 -0.2748 -0.1454 0.1450  1330 ASP B C   
22548 O O   . ASP C 1330 ? 2.6419 1.3601 1.9145 -0.2728 -0.1339 0.1579  1330 ASP B O   
22549 C CB  . ASP C 1330 ? 2.5418 1.3140 1.8595 -0.3282 -0.0920 0.1528  1330 ASP B CB  
22550 C CG  . ASP C 1330 ? 2.5050 1.2963 1.8583 -0.3538 -0.0901 0.1550  1330 ASP B CG  
22551 O OD1 . ASP C 1330 ? 2.4320 1.2128 1.8195 -0.3540 -0.1261 0.1642  1330 ASP B OD1 
22552 O OD2 . ASP C 1330 ? 2.5370 1.3540 1.8837 -0.3747 -0.0510 0.1475  1330 ASP B OD2 
22553 N N   . LYS C 1331 ? 2.8683 1.5964 2.0615 -0.2567 -0.1579 0.1291  1331 LYS B N   
22554 C CA  . LYS C 1331 ? 2.9260 1.6314 2.0789 -0.2305 -0.1689 0.1251  1331 LYS B CA  
22555 C C   . LYS C 1331 ? 2.9285 1.6032 2.0939 -0.2106 -0.2215 0.1358  1331 LYS B C   
22556 O O   . LYS C 1331 ? 2.9263 1.5841 2.1126 -0.2044 -0.2225 0.1492  1331 LYS B O   
22557 C CB  . LYS C 1331 ? 2.9735 1.6850 2.0648 -0.2181 -0.1716 0.1043  1331 LYS B CB  
22558 C CG  . LYS C 1331 ? 2.9531 1.6964 2.0271 -0.2368 -0.1225 0.0922  1331 LYS B CG  
22559 C CD  . LYS C 1331 ? 2.9364 1.6869 2.0342 -0.2527 -0.0736 0.1007  1331 LYS B CD  
22560 C CE  . LYS C 1331 ? 2.9839 1.7544 2.0421 -0.2597 -0.0258 0.0861  1331 LYS B CE  
22561 N NZ  . LYS C 1331 ? 3.0027 1.7691 2.0732 -0.2660 0.0157  0.0941  1331 LYS B NZ  
22562 N N   . ASN C 1332 ? 2.4353 1.1027 1.5855 -0.2004 -0.2648 0.1298  1332 ASN B N   
22563 C CA  . ASN C 1332 ? 2.4627 1.1056 1.6336 -0.1884 -0.3159 0.1407  1332 ASN B CA  
22564 C C   . ASN C 1332 ? 2.4478 1.1015 1.6650 -0.2067 -0.3297 0.1481  1332 ASN B C   
22565 O O   . ASN C 1332 ? 2.4531 1.1264 1.6634 -0.2183 -0.3232 0.1385  1332 ASN B O   
22566 C CB  . ASN C 1332 ? 2.5360 1.1615 1.6583 -0.1652 -0.3572 0.1287  1332 ASN B CB  
22567 C CG  . ASN C 1332 ? 2.5377 1.1708 1.6646 -0.1709 -0.3846 0.1237  1332 ASN B CG  
22568 O OD1 . ASN C 1332 ? 2.5180 1.1721 1.6231 -0.1782 -0.3684 0.1106  1332 ASN B OD1 
22569 N ND2 . ASN C 1332 ? 2.5221 1.1385 1.6780 -0.1681 -0.4258 0.1345  1332 ASN B ND2 
22570 N N   . PHE C 1333 ? 2.6955 1.3359 1.9589 -0.2089 -0.3508 0.1651  1333 PHE B N   
22571 C CA  . PHE C 1333 ? 2.6245 1.2688 1.9236 -0.2211 -0.3761 0.1702  1333 PHE B CA  
22572 C C   . PHE C 1333 ? 2.6902 1.3096 2.0169 -0.2108 -0.4203 0.1843  1333 PHE B C   
22573 O O   . PHE C 1333 ? 2.7020 1.3162 2.0426 -0.2125 -0.4550 0.1858  1333 PHE B O   
22574 C CB  . PHE C 1333 ? 2.4663 1.1373 1.8080 -0.2513 -0.3390 0.1746  1333 PHE B CB  
22575 C CG  . PHE C 1333 ? 2.3531 1.0260 1.7419 -0.2643 -0.3089 0.1907  1333 PHE B CG  
22576 C CD1 . PHE C 1333 ? 2.2781 0.9413 1.7210 -0.2707 -0.3288 0.2077  1333 PHE B CD1 
22577 C CD2 . PHE C 1333 ? 2.3580 1.0436 1.7381 -0.2718 -0.2583 0.1887  1333 PHE B CD2 
22578 C CE1 . PHE C 1333 ? 2.2654 0.9310 1.7535 -0.2830 -0.2997 0.2231  1333 PHE B CE1 
22579 C CE2 . PHE C 1333 ? 2.2557 0.9427 1.6793 -0.2842 -0.2284 0.2038  1333 PHE B CE2 
22580 C CZ  . PHE C 1333 ? 2.2232 0.9002 1.7016 -0.2894 -0.2492 0.2213  1333 PHE B CZ  
22581 N N   . LEU C 1334 ? 2.5900 1.1933 1.9217 -0.1993 -0.4202 0.1944  1334 LEU B N   
22582 C CA  . LEU C 1334 ? 2.5316 1.1108 1.8858 -0.1879 -0.4638 0.2079  1334 LEU B CA  
22583 C C   . LEU C 1334 ? 2.6614 1.2162 1.9642 -0.1615 -0.5053 0.1993  1334 LEU B C   
22584 O O   . LEU C 1334 ? 2.7019 1.2337 2.0076 -0.1467 -0.5350 0.2091  1334 LEU B O   
22585 C CB  . LEU C 1334 ? 2.4038 0.9773 1.7919 -0.1881 -0.4465 0.2249  1334 LEU B CB  
22586 C CG  . LEU C 1334 ? 2.2909 0.8847 1.7172 -0.2093 -0.3938 0.2328  1334 LEU B CG  
22587 C CD1 . LEU C 1334 ? 2.1996 0.8050 1.6834 -0.2317 -0.3941 0.2429  1334 LEU B CD1 
22588 C CD2 . LEU C 1334 ? 2.2796 0.8930 1.6701 -0.2165 -0.3485 0.2172  1334 LEU B CD2 
22589 N N   . GLY C 1335 ? 2.7404 1.3004 1.9963 -0.1562 -0.5065 0.1813  1335 GLY B N   
22590 C CA  . GLY C 1335 ? 2.8716 1.4099 2.0734 -0.1323 -0.5398 0.1706  1335 GLY B CA  
22591 C C   . GLY C 1335 ? 2.9477 1.4560 2.1522 -0.1166 -0.5910 0.1797  1335 GLY B C   
22592 O O   . GLY C 1335 ? 2.9329 1.4361 2.1847 -0.1234 -0.6081 0.1955  1335 GLY B O   
22593 N N   . ARG C 1336 ? 3.2967 1.7850 2.4480 -0.0954 -0.6151 0.1692  1336 ARG B N   
22594 C CA  . ARG C 1336 ? 3.4085 1.8667 2.5508 -0.0794 -0.6653 0.1748  1336 ARG B CA  
22595 C C   . ARG C 1336 ? 3.2885 1.7460 2.4562 -0.0880 -0.6976 0.1777  1336 ARG B C   
22596 O O   . ARG C 1336 ? 3.2682 1.7428 2.4328 -0.0981 -0.6880 0.1680  1336 ARG B O   
22597 C CB  . ARG C 1336 ? 3.6367 2.0772 2.7120 -0.0583 -0.6806 0.1588  1336 ARG B CB  
22598 C CG  . ARG C 1336 ? 3.7832 2.2438 2.8283 -0.0628 -0.6575 0.1408  1336 ARG B CG  
22599 C CD  . ARG C 1336 ? 3.9531 2.3978 2.9541 -0.0489 -0.6924 0.1280  1336 ARG B CD  
22600 N NE  . ARG C 1336 ? 4.0529 2.5207 3.0331 -0.0553 -0.6696 0.1128  1336 ARG B NE  
22601 C CZ  . ARG C 1336 ? 4.1723 2.6338 3.0986 -0.0412 -0.6765 0.0966  1336 ARG B CZ  
22602 N NH1 . ARG C 1336 ? 4.2501 2.6810 3.1366 -0.0202 -0.7054 0.0929  1336 ARG B NH1 
22603 N NH2 . ARG C 1336 ? 4.1866 2.6724 3.0989 -0.0484 -0.6544 0.0842  1336 ARG B NH2 
22604 N N   . PRO C 1337 ? 2.5160 0.9545 1.7099 -0.0847 -0.7350 0.1914  1337 PRO B N   
22605 C CA  . PRO C 1337 ? 2.4150 0.8431 1.6157 -0.0860 -0.7764 0.1914  1337 PRO B CA  
22606 C C   . PRO C 1337 ? 2.4139 0.8230 1.5529 -0.0680 -0.8036 0.1756  1337 PRO B C   
22607 O O   . PRO C 1337 ? 2.5224 0.9283 1.6151 -0.0554 -0.7887 0.1643  1337 PRO B O   
22608 C CB  . PRO C 1337 ? 2.4300 0.8404 1.6660 -0.0839 -0.8073 0.2097  1337 PRO B CB  
22609 C CG  . PRO C 1337 ? 2.4511 0.8760 1.7248 -0.0924 -0.7705 0.2222  1337 PRO B CG  
22610 C CD  . PRO C 1337 ? 2.4940 0.9273 1.7268 -0.0858 -0.7327 0.2099  1337 PRO B CD  
22611 N N   . VAL C 1338 ? 2.5460 0.9429 1.6838 -0.0672 -0.8411 0.1742  1338 VAL B N   
22612 C CA  . VAL C 1338 ? 2.6534 1.0279 1.7343 -0.0493 -0.8706 0.1611  1338 VAL B CA  
22613 C C   . VAL C 1338 ? 2.7375 1.0939 1.8282 -0.0496 -0.9161 0.1651  1338 VAL B C   
22614 O O   . VAL C 1338 ? 2.7250 1.0944 1.8501 -0.0649 -0.9178 0.1680  1338 VAL B O   
22615 C CB  . VAL C 1338 ? 3.1673 1.5563 2.2062 -0.0466 -0.8471 0.1420  1338 VAL B CB  
22616 C CG1 . VAL C 1338 ? 3.1839 1.5577 2.1903 -0.0384 -0.8811 0.1317  1338 VAL B CG1 
22617 C CG2 . VAL C 1338 ? 3.2109 1.5952 2.2047 -0.0318 -0.8267 0.1333  1338 VAL B CG2 
22618 N N   . GLU C 1339 ? 3.2010 1.5264 2.2608 -0.0331 -0.9527 0.1655  1339 GLU B N   
22619 C CA  . GLU C 1339 ? 3.2723 1.5768 2.3365 -0.0321 -0.9976 0.1694  1339 GLU B CA  
22620 C C   . GLU C 1339 ? 3.2807 1.5775 2.2988 -0.0244 -1.0098 0.1527  1339 GLU B C   
22621 O O   . GLU C 1339 ? 3.2941 1.5841 2.2611 -0.0102 -1.0022 0.1397  1339 GLU B O   
22622 C CB  . GLU C 1339 ? 3.3912 1.6665 2.4481 -0.0201 -1.0310 0.1797  1339 GLU B CB  
22623 C CG  . GLU C 1339 ? 3.4357 1.7197 2.5505 -0.0301 -1.0248 0.1998  1339 GLU B CG  
22624 C CD  . GLU C 1339 ? 3.5364 1.7974 2.6389 -0.0165 -1.0444 0.2094  1339 GLU B CD  
22625 O OE1 . GLU C 1339 ? 3.6016 1.8339 2.6697 -0.0044 -1.0826 0.2070  1339 GLU B OE1 
22626 O OE2 . GLU C 1339 ? 3.5371 1.8085 2.6649 -0.0185 -1.0214 0.2200  1339 GLU B OE2 
22627 N N   . VAL C 1340 ? 2.9847 1.2843 2.0228 -0.0346 -1.0260 0.1531  1340 VAL B N   
22628 C CA  . VAL C 1340 ? 3.0409 1.3334 2.0401 -0.0281 -1.0386 0.1388  1340 VAL B CA  
22629 C C   . VAL C 1340 ? 3.1185 1.3735 2.0791 -0.0123 -1.0827 0.1365  1340 VAL B C   
22630 O O   . VAL C 1340 ? 3.1504 1.3896 2.1307 -0.0164 -1.1156 0.1450  1340 VAL B O   
22631 C CB  . VAL C 1340 ? 3.0259 1.3350 2.0589 -0.0449 -1.0382 0.1394  1340 VAL B CB  
22632 C CG1 . VAL C 1340 ? 3.0732 1.3656 2.0678 -0.0364 -1.0644 0.1280  1340 VAL B CG1 
22633 C CG2 . VAL C 1340 ? 2.9792 1.3247 2.0314 -0.0580 -0.9918 0.1358  1340 VAL B CG2 
22634 N N   . LEU C 1341 ? 3.9909 2.2320 2.8952 0.0052  -1.0819 0.1245  1341 LEU B N   
22635 C CA  . LEU C 1341 ? 4.0639 2.2679 2.9220 0.0217  -1.1198 0.1200  1341 LEU B CA  
22636 C C   . LEU C 1341 ? 4.1335 2.3263 2.9779 0.0215  -1.1447 0.1133  1341 LEU B C   
22637 O O   . LEU C 1341 ? 4.1277 2.3097 2.9972 0.0139  -1.1727 0.1217  1341 LEU B O   
22638 C CB  . LEU C 1341 ? 4.0942 2.2888 2.8951 0.0394  -1.1069 0.1070  1341 LEU B CB  
22639 C CG  . LEU C 1341 ? 4.3349 2.5271 3.1280 0.0464  -1.0911 0.1107  1341 LEU B CG  
22640 C CD1 . LEU C 1341 ? 4.3394 2.5061 3.1450 0.0488  -1.1241 0.1248  1341 LEU B CD1 
22641 C CD2 . LEU C 1341 ? 4.2850 2.5139 3.1165 0.0337  -1.0464 0.1147  1341 LEU B CD2 
22642 N N   . LEU C 1342 ? 3.2864 1.4833 2.0912 0.0297  -1.1321 0.0982  1342 LEU B N   
22643 C CA  . LEU C 1342 ? 3.3276 1.5071 2.0999 0.0366  -1.1555 0.0887  1342 LEU B CA  
22644 C C   . LEU C 1342 ? 3.2856 1.4681 2.0936 0.0226  -1.1733 0.0946  1342 LEU B C   
22645 O O   . LEU C 1342 ? 3.2256 1.4205 2.0857 0.0072  -1.1724 0.1070  1342 LEU B O   
22646 C CB  . LEU C 1342 ? 3.3213 1.5162 2.0573 0.0445  -1.1287 0.0730  1342 LEU B CB  
22647 C CG  . LEU C 1342 ? 3.2731 1.4845 1.9977 0.0490  -1.0934 0.0691  1342 LEU B CG  
22648 C CD1 . LEU C 1342 ? 3.2835 1.5106 1.9712 0.0568  -1.0673 0.0533  1342 LEU B CD1 
22649 C CD2 . LEU C 1342 ? 3.3046 1.4869 2.0016 0.0625  -1.1087 0.0713  1342 LEU B CD2 
22650 N N   . ASN C 1343 ? 3.5776 1.7469 2.3566 0.0285  -1.1903 0.0856  1343 ASN B N   
22651 C CA  . ASN C 1343 ? 3.6209 1.7900 2.4282 0.0165  -1.2083 0.0897  1343 ASN B CA  
22652 C C   . ASN C 1343 ? 3.5890 1.7843 2.4022 0.0096  -1.1870 0.0820  1343 ASN B C   
22653 O O   . ASN C 1343 ? 3.6164 1.8001 2.3947 0.0185  -1.1978 0.0723  1343 ASN B O   
22654 C CB  . ASN C 1343 ? 3.7668 1.8956 2.5431 0.0259  -1.2514 0.0887  1343 ASN B CB  
22655 C CG  . ASN C 1343 ? 3.8818 1.9908 2.6777 0.0227  -1.2777 0.1016  1343 ASN B CG  
22656 O OD1 . ASN C 1343 ? 3.9369 2.0231 2.7354 0.0200  -1.3109 0.1059  1343 ASN B OD1 
22657 N ND2 . ASN C 1343 ? 3.9031 2.0215 2.7139 0.0224  -1.2625 0.1083  1343 ASN B ND2 
22658 N N   . ASP C 1344 ? 3.6003 1.8305 2.4588 -0.0069 -1.1569 0.0870  1344 ASP B N   
22659 C CA  . ASP C 1344 ? 3.5300 1.7897 2.3962 -0.0151 -1.1315 0.0802  1344 ASP B CA  
22660 C C   . ASP C 1344 ? 3.4581 1.7433 2.3868 -0.0385 -1.1175 0.0906  1344 ASP B C   
22661 O O   . ASP C 1344 ? 3.4527 1.7325 2.4176 -0.0472 -1.1272 0.1027  1344 ASP B O   
22662 C CB  . ASP C 1344 ? 3.4691 1.7508 2.3102 -0.0081 -1.0953 0.0709  1344 ASP B CB  
22663 C CG  . ASP C 1344 ? 3.4031 1.6903 2.2052 0.0013  -1.0894 0.0573  1344 ASP B CG  
22664 O OD1 . ASP C 1344 ? 3.3808 1.6626 2.1846 -0.0015 -1.1064 0.0560  1344 ASP B OD1 
22665 O OD2 . ASP C 1344 ? 3.3777 1.6747 2.1475 0.0116  -1.0674 0.0480  1344 ASP B OD2 
22666 N N   . ASP C 1345 ? 3.6783 1.9909 2.6196 -0.0489 -1.0952 0.0861  1345 ASP B N   
22667 C CA  . ASP C 1345 ? 3.5905 1.9311 2.5888 -0.0720 -1.0740 0.0946  1345 ASP B CA  
22668 C C   . ASP C 1345 ? 3.1933 1.5654 2.1974 -0.0767 -1.0301 0.0926  1345 ASP B C   
22669 O O   . ASP C 1345 ? 3.2265 1.6075 2.1921 -0.0658 -1.0132 0.0816  1345 ASP B O   
22670 C CB  . ASP C 1345 ? 3.5817 1.9325 2.5927 -0.0828 -1.0769 0.0917  1345 ASP B CB  
22671 C CG  . ASP C 1345 ? 3.6668 1.9846 2.6661 -0.0770 -1.1196 0.0923  1345 ASP B CG  
22672 O OD1 . ASP C 1345 ? 3.6635 1.9846 2.6926 -0.0910 -1.1277 0.0958  1345 ASP B OD1 
22673 O OD2 . ASP C 1345 ? 3.7283 2.0159 2.6878 -0.0589 -1.1448 0.0889  1345 ASP B OD2 
22674 N N   . LEU C 1346 ? 3.0564 1.4450 2.1080 -0.0928 -1.0111 0.1031  1346 LEU B N   
22675 C CA  . LEU C 1346 ? 3.0021 1.4163 2.0575 -0.0965 -0.9705 0.1020  1346 LEU B CA  
22676 C C   . LEU C 1346 ? 2.9847 1.4359 2.0665 -0.1159 -0.9345 0.1003  1346 LEU B C   
22677 O O   . LEU C 1346 ? 2.9993 1.4572 2.1101 -0.1303 -0.9405 0.1034  1346 LEU B O   
22678 C CB  . LEU C 1346 ? 2.9166 1.3261 2.0025 -0.1002 -0.9668 0.1144  1346 LEU B CB  
22679 C CG  . LEU C 1346 ? 2.8806 1.3105 1.9594 -0.0996 -0.9267 0.1120  1346 LEU B CG  
22680 C CD1 . LEU C 1346 ? 2.9295 1.3500 1.9462 -0.0779 -0.9263 0.0985  1346 LEU B CD1 
22681 C CD2 . LEU C 1346 ? 2.8592 1.2841 1.9693 -0.1029 -0.9229 0.1251  1346 LEU B CD2 
22682 N N   . ILE C 1347 ? 2.7243 1.1991 1.7949 -0.1166 -0.8969 0.0951  1347 ILE B N   
22683 C CA  . ILE C 1347 ? 2.6028 1.1146 1.6951 -0.1356 -0.8583 0.0931  1347 ILE B CA  
22684 C C   . ILE C 1347 ? 2.5096 1.0448 1.6045 -0.1407 -0.8150 0.0925  1347 ILE B C   
22685 O O   . ILE C 1347 ? 2.5247 1.0696 1.5799 -0.1304 -0.7970 0.0817  1347 ILE B O   
22686 C CB  . ILE C 1347 ? 2.6172 1.1408 1.6796 -0.1324 -0.8580 0.0811  1347 ILE B CB  
22687 C CG1 . ILE C 1347 ? 2.6811 1.1751 1.6928 -0.1077 -0.8926 0.0730  1347 ILE B CG1 
22688 C CG2 . ILE C 1347 ? 2.5794 1.1128 1.6787 -0.1513 -0.8635 0.0856  1347 ILE B CG2 
22689 C CD1 . ILE C 1347 ? 2.7375 1.2427 1.7179 -0.1025 -0.8920 0.0615  1347 ILE B CD1 
22690 N N   . VAL C 1348 ? 2.5697 1.1128 1.7115 -0.1568 -0.7987 0.1044  1348 VAL B N   
22691 C CA  . VAL C 1348 ? 2.5373 1.1083 1.6950 -0.1700 -0.7519 0.1055  1348 VAL B CA  
22692 C C   . VAL C 1348 ? 2.6435 1.2464 1.8059 -0.1865 -0.7259 0.0989  1348 VAL B C   
22693 O O   . VAL C 1348 ? 2.6605 1.2649 1.8432 -0.1969 -0.7408 0.1008  1348 VAL B O   
22694 C CB  . VAL C 1348 ? 2.4269 0.9998 1.6422 -0.1871 -0.7417 0.1212  1348 VAL B CB  
22695 C CG1 . VAL C 1348 ? 2.4205 1.0167 1.6467 -0.1974 -0.6940 0.1227  1348 VAL B CG1 
22696 C CG2 . VAL C 1348 ? 2.4355 0.9762 1.6568 -0.1742 -0.7768 0.1305  1348 VAL B CG2 
22697 N N   . SER C 1349 ? 3.4003 2.0286 2.5446 -0.1899 -0.6871 0.0913  1349 SER B N   
22698 C CA  . SER C 1349 ? 3.4001 2.0597 2.5400 -0.2033 -0.6629 0.0835  1349 SER B CA  
22699 C C   . SER C 1349 ? 3.4559 2.1448 2.5816 -0.2100 -0.6159 0.0770  1349 SER B C   
22700 O O   . SER C 1349 ? 3.4844 2.1810 2.5652 -0.1971 -0.6089 0.0649  1349 SER B O   
22701 C CB  . SER C 1349 ? 3.4107 2.0627 2.5084 -0.1866 -0.6894 0.0726  1349 SER B CB  
22702 O OG  . SER C 1349 ? 3.4503 2.0859 2.4995 -0.1618 -0.6985 0.0645  1349 SER B OG  
22703 N N   . THR C 1350 ? 2.9487 1.6542 2.1123 -0.2308 -0.5829 0.0848  1350 THR B N   
22704 C CA  . THR C 1350 ? 2.9672 1.7009 2.1195 -0.2399 -0.5361 0.0791  1350 THR B CA  
22705 C C   . THR C 1350 ? 2.9513 1.7150 2.0847 -0.2485 -0.5197 0.0685  1350 THR B C   
22706 O O   . THR C 1350 ? 2.9196 1.6836 2.0585 -0.2514 -0.5416 0.0679  1350 THR B O   
22707 C CB  . THR C 1350 ? 3.0439 1.7894 2.2446 -0.2634 -0.5034 0.0905  1350 THR B CB  
22708 O OG1 . THR C 1350 ? 3.0817 1.8488 2.2665 -0.2690 -0.4587 0.0851  1350 THR B OG1 
22709 C CG2 . THR C 1350 ? 2.9839 1.7460 2.2268 -0.2894 -0.4972 0.0961  1350 THR B CG2 
22710 N N   . GLY C 1351 ? 2.5739 1.3619 1.6833 -0.2517 -0.4821 0.0601  1351 GLY B N   
22711 C CA  . GLY C 1351 ? 2.5592 1.3809 1.6555 -0.2637 -0.4595 0.0514  1351 GLY B CA  
22712 C C   . GLY C 1351 ? 2.4674 1.3144 1.6077 -0.2958 -0.4245 0.0587  1351 GLY B C   
22713 O O   . GLY C 1351 ? 2.4097 1.2470 1.5934 -0.3086 -0.4359 0.0698  1351 GLY B O   
22714 N N   . PHE C 1352 ? 2.7735 1.6521 1.9038 -0.3100 -0.3814 0.0528  1352 PHE B N   
22715 C CA  . PHE C 1352 ? 2.7061 1.6072 1.8784 -0.3421 -0.3480 0.0600  1352 PHE B CA  
22716 C C   . PHE C 1352 ? 2.6643 1.5549 1.8695 -0.3515 -0.3280 0.0706  1352 PHE B C   
22717 O O   . PHE C 1352 ? 2.6549 1.5219 1.8934 -0.3507 -0.3508 0.0816  1352 PHE B O   
22718 C CB  . PHE C 1352 ? 2.6884 1.6291 1.8447 -0.3594 -0.3069 0.0515  1352 PHE B CB  
22719 C CG  . PHE C 1352 ? 2.6125 1.5738 1.8125 -0.3936 -0.2746 0.0594  1352 PHE B CG  
22720 C CD1 . PHE C 1352 ? 2.5453 1.5018 1.7837 -0.4074 -0.2939 0.0677  1352 PHE B CD1 
22721 C CD2 . PHE C 1352 ? 2.6073 1.5900 1.8112 -0.4124 -0.2255 0.0590  1352 PHE B CD2 
22722 C CE1 . PHE C 1352 ? 2.4724 1.4451 1.7520 -0.4394 -0.2655 0.0751  1352 PHE B CE1 
22723 C CE2 . PHE C 1352 ? 2.5360 1.5353 1.7812 -0.4450 -0.1960 0.0667  1352 PHE B CE2 
22724 C CZ  . PHE C 1352 ? 2.4757 1.4697 1.7590 -0.4584 -0.2165 0.0748  1352 PHE B CZ  
22725 N N   . GLY C 1353 ? 2.6837 1.5933 1.8801 -0.3615 -0.2837 0.0675  1353 GLY B N   
22726 C CA  . GLY C 1353 ? 2.6620 1.5610 1.8785 -0.3653 -0.2614 0.0757  1353 GLY B CA  
22727 C C   . GLY C 1353 ? 2.6099 1.5157 1.8805 -0.3942 -0.2366 0.0881  1353 GLY B C   
22728 O O   . GLY C 1353 ? 2.5693 1.4992 1.8566 -0.4186 -0.2168 0.0879  1353 GLY B O   
22729 N N   . SER C 1354 ? 2.3162 1.2007 1.6136 -0.3913 -0.2371 0.0993  1354 SER B N   
22730 C CA  . SER C 1354 ? 2.2536 1.1405 1.6047 -0.4167 -0.2137 0.1125  1354 SER B CA  
22731 C C   . SER C 1354 ? 2.2140 1.0716 1.5944 -0.4065 -0.2289 0.1258  1354 SER B C   
22732 O O   . SER C 1354 ? 2.2463 1.0829 1.6017 -0.3803 -0.2505 0.1245  1354 SER B O   
22733 C CB  . SER C 1354 ? 2.2758 1.1895 1.6261 -0.4392 -0.1560 0.1099  1354 SER B CB  
22734 O OG  . SER C 1354 ? 2.3012 1.2083 1.6283 -0.4263 -0.1355 0.1080  1354 SER B OG  
22735 N N   . GLY C 1355 ? 2.3505 1.2074 1.7841 -0.4280 -0.2162 0.1388  1355 GLY B N   
22736 C CA  . GLY C 1355 ? 2.3271 1.1593 1.7959 -0.4217 -0.2289 0.1532  1355 GLY B CA  
22737 C C   . GLY C 1355 ? 2.3335 1.1429 1.8226 -0.4110 -0.2815 0.1596  1355 GLY B C   
22738 O O   . GLY C 1355 ? 2.3587 1.1734 1.8534 -0.4186 -0.3009 0.1565  1355 GLY B O   
22739 N N   . LEU C 1356 ? 2.4307 1.2145 1.9285 -0.3928 -0.3052 0.1684  1356 LEU B N   
22740 C CA  . LEU C 1356 ? 2.4397 1.2008 1.9650 -0.3855 -0.3514 0.1773  1356 LEU B CA  
22741 C C   . LEU C 1356 ? 2.5791 1.3126 2.0800 -0.3547 -0.3895 0.1785  1356 LEU B C   
22742 O O   . LEU C 1356 ? 2.6468 1.3719 2.1452 -0.3450 -0.3770 0.1836  1356 LEU B O   
22743 C CB  . LEU C 1356 ? 2.3746 1.1335 1.9616 -0.4051 -0.3365 0.1936  1356 LEU B CB  
22744 C CG  . LEU C 1356 ? 2.2864 1.0588 1.9092 -0.4323 -0.3295 0.1956  1356 LEU B CG  
22745 C CD1 . LEU C 1356 ? 2.2107 0.9855 1.8892 -0.4541 -0.2999 0.2101  1356 LEU B CD1 
22746 C CD2 . LEU C 1356 ? 2.2706 1.0257 1.8991 -0.4228 -0.3816 0.1963  1356 LEU B CD2 
22747 N N   . ALA C 1357 ? 2.8754 1.5938 2.3591 -0.3397 -0.4357 0.1742  1357 ALA B N   
22748 C CA  . ALA C 1357 ? 2.8323 1.5230 2.2915 -0.3114 -0.4740 0.1752  1357 ALA B CA  
22749 C C   . ALA C 1357 ? 2.7846 1.4531 2.2708 -0.3070 -0.5211 0.1841  1357 ALA B C   
22750 O O   . ALA C 1357 ? 2.7580 1.4263 2.2420 -0.3102 -0.5444 0.1792  1357 ALA B O   
22751 C CB  . ALA C 1357 ? 2.8371 1.5265 2.2335 -0.2913 -0.4857 0.1590  1357 ALA B CB  
22752 N N   . THR C 1358 ? 2.3931 1.0431 1.9039 -0.2995 -0.5351 0.1971  1358 THR B N   
22753 C CA  . THR C 1358 ? 2.3752 1.0036 1.9110 -0.2947 -0.5804 0.2061  1358 THR B CA  
22754 C C   . THR C 1358 ? 2.4459 1.0493 1.9372 -0.2668 -0.6243 0.2004  1358 THR B C   
22755 O O   . THR C 1358 ? 2.4706 1.0586 1.9503 -0.2504 -0.6326 0.2052  1358 THR B O   
22756 C CB  . THR C 1358 ? 2.6066 1.2286 2.1968 -0.3024 -0.5757 0.2245  1358 THR B CB  
22757 O OG1 . THR C 1358 ? 2.6022 1.2362 2.1961 -0.3066 -0.5314 0.2278  1358 THR B OG1 
22758 C CG2 . THR C 1358 ? 2.5510 1.1814 2.1954 -0.3272 -0.5729 0.2323  1358 THR B CG2 
22759 N N   . VAL C 1359 ? 2.1531 0.7520 1.6184 -0.2617 -0.6513 0.1902  1359 VAL B N   
22760 C CA  . VAL C 1359 ? 2.2567 0.8300 1.6823 -0.2375 -0.6953 0.1851  1359 VAL B CA  
22761 C C   . VAL C 1359 ? 2.3180 0.8694 1.7785 -0.2365 -0.7341 0.1982  1359 VAL B C   
22762 O O   . VAL C 1359 ? 2.2697 0.8208 1.7571 -0.2488 -0.7504 0.2007  1359 VAL B O   
22763 C CB  . VAL C 1359 ? 2.2181 0.7947 1.6055 -0.2334 -0.7090 0.1700  1359 VAL B CB  
22764 C CG1 . VAL C 1359 ? 2.2656 0.8132 1.6200 -0.2119 -0.7573 0.1664  1359 VAL B CG1 
22765 C CG2 . VAL C 1359 ? 2.2354 0.8308 1.5816 -0.2298 -0.6762 0.1568  1359 VAL B CG2 
22766 N N   . HIS C 1360 ? 2.4218 0.9556 1.8837 -0.2230 -0.7480 0.2071  1360 HIS B N   
22767 C CA  . HIS C 1360 ? 2.4657 0.9770 1.9513 -0.2187 -0.7901 0.2181  1360 HIS B CA  
22768 C C   . HIS C 1360 ? 2.5287 1.0137 1.9644 -0.1947 -0.8305 0.2112  1360 HIS B C   
22769 O O   . HIS C 1360 ? 2.5986 1.0784 1.9888 -0.1781 -0.8247 0.2033  1360 HIS B O   
22770 C CB  . HIS C 1360 ? 2.4998 1.0077 2.0252 -0.2204 -0.7836 0.2349  1360 HIS B CB  
22771 C CG  . HIS C 1360 ? 2.4587 0.9852 2.0453 -0.2450 -0.7556 0.2460  1360 HIS B CG  
22772 N ND1 . HIS C 1360 ? 2.4254 0.9708 2.0298 -0.2551 -0.7087 0.2499  1360 HIS B ND1 
22773 C CD2 . HIS C 1360 ? 2.4300 0.9575 2.0644 -0.2615 -0.7680 0.2542  1360 HIS B CD2 
22774 C CE1 . HIS C 1360 ? 2.3860 0.9432 2.0468 -0.2770 -0.6928 0.2603  1360 HIS B CE1 
22775 N NE2 . HIS C 1360 ? 2.3931 0.9399 2.0733 -0.2813 -0.7283 0.2629  1360 HIS B NE2 
22776 N N   . VAL C 1361 ? 2.4433 0.9100 1.8884 -0.1932 -0.8718 0.2149  1361 VAL B N   
22777 C CA  . VAL C 1361 ? 2.5001 0.9397 1.8990 -0.1720 -0.9122 0.2088  1361 VAL B CA  
22778 C C   . VAL C 1361 ? 2.5267 0.9449 1.9524 -0.1717 -0.9544 0.2206  1361 VAL B C   
22779 O O   . VAL C 1361 ? 2.5087 0.9257 1.9590 -0.1835 -0.9716 0.2220  1361 VAL B O   
22780 C CB  . VAL C 1361 ? 2.4890 0.9289 1.8419 -0.1664 -0.9177 0.1915  1361 VAL B CB  
22781 C CG1 . VAL C 1361 ? 2.4338 0.8503 1.7756 -0.1608 -0.9638 0.1897  1361 VAL B CG1 
22782 C CG2 . VAL C 1361 ? 2.4468 0.8832 1.7429 -0.1475 -0.9070 0.1801  1361 VAL B CG2 
22783 N N   . THR C 1362 ? 2.1773 0.5795 1.5984 -0.1587 -0.9692 0.2291  1362 THR B N   
22784 C CA  . THR C 1362 ? 2.1968 0.5798 1.6428 -0.1571 -1.0069 0.2422  1362 THR B CA  
22785 C C   . THR C 1362 ? 2.2389 0.5920 1.6314 -0.1365 -1.0478 0.2353  1362 THR B C   
22786 O O   . THR C 1362 ? 2.2607 0.6030 1.6150 -0.1198 -1.0481 0.2322  1362 THR B O   
22787 C CB  . THR C 1362 ? 2.1899 0.5795 1.6776 -0.1603 -0.9916 0.2592  1362 THR B CB  
22788 O OG1 . THR C 1362 ? 2.2011 0.5783 1.7259 -0.1638 -1.0248 0.2735  1362 THR B OG1 
22789 C CG2 . THR C 1362 ? 2.2100 0.5919 1.6594 -0.1419 -0.9834 0.2574  1362 THR B CG2 
22790 N N   . THR C 1363 ? 2.3530 0.6930 1.7414 -0.1390 -1.0799 0.2316  1363 THR B N   
22791 C CA  . THR C 1363 ? 2.3871 0.6978 1.7264 -0.1228 -1.1199 0.2241  1363 THR B CA  
22792 C C   . THR C 1363 ? 2.4922 0.7827 1.8533 -0.1223 -1.1592 0.2374  1363 THR B C   
22793 O O   . THR C 1363 ? 2.4833 0.7791 1.8923 -0.1376 -1.1677 0.2466  1363 THR B O   
22794 C CB  . THR C 1363 ? 3.1108 1.4186 2.4284 -0.1258 -1.1305 0.2108  1363 THR B CB  
22795 O OG1 . THR C 1363 ? 3.0951 1.3973 2.4492 -0.1389 -1.1553 0.2177  1363 THR B OG1 
22796 C CG2 . THR C 1363 ? 3.0683 1.4043 2.3878 -0.1351 -1.0894 0.2017  1363 THR B CG2 
22797 N N   . VAL C 1364 ? 2.3473 0.6146 1.6728 -0.1050 -1.1831 0.2384  1364 VAL B N   
22798 C CA  . VAL C 1364 ? 2.3728 0.6206 1.7141 -0.1034 -1.2214 0.2512  1364 VAL B CA  
22799 C C   . VAL C 1364 ? 2.4143 0.6296 1.7072 -0.0912 -1.2643 0.2441  1364 VAL B C   
22800 O O   . VAL C 1364 ? 2.4359 0.6369 1.6718 -0.0761 -1.2672 0.2315  1364 VAL B O   
22801 C CB  . VAL C 1364 ? 2.3818 0.6293 1.7332 -0.0961 -1.2160 0.2637  1364 VAL B CB  
22802 C CG1 . VAL C 1364 ? 2.4116 0.6380 1.7734 -0.0937 -1.2590 0.2759  1364 VAL B CG1 
22803 C CG2 . VAL C 1364 ? 2.3431 0.6203 1.7503 -0.1098 -1.1770 0.2741  1364 VAL B CG2 
22804 N N   . VAL C 1365 ? 2.9438 1.1469 2.2601 -0.0982 -1.2979 0.2525  1365 VAL B N   
22805 C CA  . VAL C 1365 ? 3.0157 1.1883 2.2883 -0.0891 -1.3373 0.2454  1365 VAL B CA  
22806 C C   . VAL C 1365 ? 3.1329 1.2903 2.4299 -0.0928 -1.3745 0.2599  1365 VAL B C   
22807 O O   . VAL C 1365 ? 3.1388 1.3123 2.4939 -0.1062 -1.3701 0.2737  1365 VAL B O   
22808 C CB  . VAL C 1365 ? 2.9336 1.1070 2.1959 -0.0958 -1.3374 0.2327  1365 VAL B CB  
22809 C CG1 . VAL C 1365 ? 2.8923 1.0709 2.2061 -0.1143 -1.3515 0.2409  1365 VAL B CG1 
22810 C CG2 . VAL C 1365 ? 2.9745 1.1180 2.1717 -0.0808 -1.3637 0.2196  1365 VAL B CG2 
22811 N N   . HIS C 1366 ? 3.1121 1.2389 2.3648 -0.0809 -1.4102 0.2573  1366 HIS B N   
22812 C CA  . HIS C 1366 ? 3.1395 1.2507 2.4101 -0.0843 -1.4481 0.2704  1366 HIS B CA  
22813 C C   . HIS C 1366 ? 3.1109 1.2048 2.3740 -0.0913 -1.4790 0.2651  1366 HIS B C   
22814 O O   . HIS C 1366 ? 3.1356 1.2104 2.3476 -0.0831 -1.4887 0.2505  1366 HIS B O   
22815 C CB  . HIS C 1366 ? 3.2325 1.3205 2.4608 -0.0679 -1.4683 0.2728  1366 HIS B CB  
22816 C CG  . HIS C 1366 ? 3.2503 1.3520 2.4780 -0.0593 -1.4384 0.2762  1366 HIS B CG  
22817 N ND1 . HIS C 1366 ? 3.2405 1.3508 2.4376 -0.0511 -1.4048 0.2630  1366 HIS B ND1 
22818 C CD2 . HIS C 1366 ? 3.2874 1.3957 2.5397 -0.0572 -1.4354 0.2912  1366 HIS B CD2 
22819 C CE1 . HIS C 1366 ? 3.2523 1.3729 2.4550 -0.0451 -1.3830 0.2692  1366 HIS B CE1 
22820 N NE2 . HIS C 1366 ? 3.2817 1.4013 2.5182 -0.0482 -1.4007 0.2867  1366 HIS B NE2 
22821 N N   . LYS C 1367 ? 3.0113 1.1117 2.3258 -0.1065 -1.4933 0.2768  1367 LYS B N   
22822 C CA  . LYS C 1367 ? 3.0627 1.1459 2.3732 -0.1143 -1.5243 0.2729  1367 LYS B CA  
22823 C C   . LYS C 1367 ? 3.1000 1.1640 2.4175 -0.1166 -1.5662 0.2847  1367 LYS B C   
22824 O O   . LYS C 1367 ? 3.1192 1.1863 2.4527 -0.1135 -1.5715 0.2978  1367 LYS B O   
22825 C CB  . LYS C 1367 ? 3.0569 1.1610 2.4131 -0.1320 -1.5069 0.2716  1367 LYS B CB  
22826 C CG  . LYS C 1367 ? 3.0319 1.1676 2.4571 -0.1455 -1.4802 0.2851  1367 LYS B CG  
22827 C CD  . LYS C 1367 ? 2.9950 1.1491 2.4528 -0.1615 -1.4587 0.2798  1367 LYS B CD  
22828 C CE  . LYS C 1367 ? 2.9889 1.1429 2.4015 -0.1541 -1.4388 0.2619  1367 LYS B CE  
22829 N NZ  . LYS C 1367 ? 2.9406 1.1195 2.3883 -0.1693 -1.4076 0.2583  1367 LYS B NZ  
22830 N N   . THR C 1368 ? 3.2490 1.0975 3.0279 -0.5080 -1.5010 0.1027  1368 THR B N   
22831 C CA  . THR C 1368 ? 3.2709 1.1176 3.0743 -0.5175 -1.5241 0.0866  1368 THR B CA  
22832 C C   . THR C 1368 ? 3.2742 1.1381 3.1217 -0.5387 -1.5308 0.1115  1368 THR B C   
22833 O O   . THR C 1368 ? 3.3428 1.2100 3.2136 -0.5486 -1.5494 0.1011  1368 THR B O   
22834 C CB  . THR C 1368 ? 3.3319 1.1393 3.1506 -0.5183 -1.5431 0.0635  1368 THR B CB  
22835 O OG1 . THR C 1368 ? 3.3547 1.1452 3.2134 -0.5330 -1.5475 0.0840  1368 THR B OG1 
22836 C CG2 . THR C 1368 ? 3.2973 1.0848 3.0773 -0.4987 -1.5348 0.0440  1368 THR B CG2 
22837 N N   . SER C 1369 ? 3.0007 0.8762 2.8601 -0.5458 -1.5160 0.1440  1369 SER B N   
22838 C CA  . SER C 1369 ? 3.0189 0.9072 2.9232 -0.5668 -1.5224 0.1690  1369 SER B CA  
22839 C C   . SER C 1369 ? 2.9736 0.8924 2.8772 -0.5709 -1.5012 0.2038  1369 SER B C   
22840 O O   . SER C 1369 ? 2.8847 0.8030 2.7668 -0.5622 -1.4824 0.2157  1369 SER B O   
22841 C CB  . SER C 1369 ? 3.0717 0.9270 3.0146 -0.5791 -1.5360 0.1730  1369 SER B CB  
22842 O OG  . SER C 1369 ? 3.1555 0.9825 3.1036 -0.5772 -1.5566 0.1415  1369 SER B OG  
22843 N N   . THR C 1370 ? 3.1510 1.0972 3.0789 -0.5843 -1.5046 0.2192  1370 THR B N   
22844 C CA  . THR C 1370 ? 3.1716 1.1470 3.1087 -0.5921 -1.4877 0.2538  1370 THR B CA  
22845 C C   . THR C 1370 ? 3.3265 1.2933 3.3131 -0.6127 -1.4964 0.2766  1370 THR B C   
22846 O O   . THR C 1370 ? 3.3248 1.3124 3.3258 -0.6217 -1.4843 0.3071  1370 THR B O   
22847 C CB  . THR C 1370 ? 3.1107 1.1249 3.0430 -0.5936 -1.4845 0.2584  1370 THR B CB  
22848 O OG1 . THR C 1370 ? 3.0347 1.0600 2.9190 -0.5740 -1.4714 0.2436  1370 THR B OG1 
22849 C CG2 . THR C 1370 ? 3.0705 1.1138 3.0209 -0.6049 -1.4702 0.2945  1370 THR B CG2 
22850 N N   . SER C 1371 ? 3.6583 1.5945 3.6713 -0.6202 -1.5172 0.2617  1371 SER B N   
22851 C CA  . SER C 1371 ? 3.8103 1.7342 3.8713 -0.6397 -1.5266 0.2817  1371 SER B CA  
22852 C C   . SER C 1371 ? 3.8429 1.7698 3.9054 -0.6412 -1.5076 0.3132  1371 SER B C   
22853 O O   . SER C 1371 ? 3.8766 1.8175 3.9707 -0.6569 -1.5052 0.3416  1371 SER B O   
22854 C CB  . SER C 1371 ? 3.9203 1.8025 3.9994 -0.6423 -1.5470 0.2596  1371 SER B CB  
22855 O OG  . SER C 1371 ? 3.9342 1.7905 3.9864 -0.6270 -1.5396 0.2493  1371 SER B OG  
22856 N N   . GLU C 1372 ? 3.9863 1.9012 4.0144 -0.6249 -1.4940 0.3081  1372 GLU B N   
22857 C CA  . GLU C 1372 ? 3.9928 1.9120 4.0168 -0.6240 -1.4748 0.3357  1372 GLU B CA  
22858 C C   . GLU C 1372 ? 3.8354 1.7958 3.8572 -0.6289 -1.4574 0.3633  1372 GLU B C   
22859 O O   . GLU C 1372 ? 3.8461 1.8178 3.9010 -0.6448 -1.4563 0.3912  1372 GLU B O   
22860 C CB  . GLU C 1372 ? 4.1050 2.0107 4.0849 -0.6033 -1.4619 0.3212  1372 GLU B CB  
22861 C CG  . GLU C 1372 ? 4.2015 2.1202 4.1388 -0.5870 -1.4573 0.2960  1372 GLU B CG  
22862 C CD  . GLU C 1372 ? 4.2553 2.1718 4.1468 -0.5677 -1.4379 0.2899  1372 GLU B CD  
22863 O OE1 . GLU C 1372 ? 4.3028 2.2016 4.1946 -0.5653 -1.4318 0.2985  1372 GLU B OE1 
22864 O OE2 . GLU C 1372 ? 4.2380 2.1709 4.0933 -0.5549 -1.4288 0.2765  1372 GLU B OE2 
22865 N N   . GLU C 1373 ? 3.4840 1.4662 3.4664 -0.6150 -1.4442 0.3542  1373 GLU B N   
22866 C CA  . GLU C 1373 ? 3.3159 1.3358 3.2833 -0.6137 -1.4232 0.3762  1373 GLU B CA  
22867 C C   . GLU C 1373 ? 3.2678 1.3147 3.2720 -0.6324 -1.4242 0.4036  1373 GLU B C   
22868 O O   . GLU C 1373 ? 3.3171 1.3558 3.3614 -0.6481 -1.4425 0.4060  1373 GLU B O   
22869 C CB  . GLU C 1373 ? 3.1996 1.2364 3.1255 -0.5976 -1.4159 0.3559  1373 GLU B CB  
22870 C CG  . GLU C 1373 ? 3.1099 1.1243 2.9944 -0.5778 -1.4115 0.3297  1373 GLU B CG  
22871 C CD  . GLU C 1373 ? 2.9962 1.0278 2.8398 -0.5621 -1.4038 0.3107  1373 GLU B CD  
22872 O OE1 . GLU C 1373 ? 2.9528 1.0131 2.8003 -0.5662 -1.4030 0.3166  1373 GLU B OE1 
22873 O OE2 . GLU C 1373 ? 2.9401 0.9568 2.7477 -0.5456 -1.3983 0.2903  1373 GLU B OE2 
22874 N N   . VAL C 1374 ? 2.7408 0.8203 2.7305 -0.6303 -1.4038 0.4239  1374 VAL B N   
22875 C CA  . VAL C 1374 ? 2.6894 0.7988 2.7086 -0.6461 -1.4004 0.4520  1374 VAL B CA  
22876 C C   . VAL C 1374 ? 2.6659 0.8013 2.6837 -0.6467 -1.4054 0.4434  1374 VAL B C   
22877 O O   . VAL C 1374 ? 2.6364 0.7868 2.6171 -0.6320 -1.3939 0.4326  1374 VAL B O   
22878 C CB  . VAL C 1374 ? 2.6173 0.7539 2.6156 -0.6412 -1.3740 0.4756  1374 VAL B CB  
22879 C CG1 . VAL C 1374 ? 2.6328 0.7907 2.6689 -0.6598 -1.3707 0.5095  1374 VAL B CG1 
22880 C CG2 . VAL C 1374 ? 2.5899 0.7079 2.5579 -0.6278 -1.3601 0.4730  1374 VAL B CG2 
22881 N N   . CYS C 1375 ? 3.6741 1.8176 3.7315 -0.6635 -1.4211 0.4500  1375 CYS B N   
22882 C CA  . CYS C 1375 ? 3.6438 1.8199 3.6990 -0.6641 -1.4214 0.4481  1375 CYS B CA  
22883 C C   . CYS C 1375 ? 3.6262 1.8397 3.6909 -0.6716 -1.4041 0.4807  1375 CYS B C   
22884 O O   . CYS C 1375 ? 3.6241 1.8416 3.7234 -0.6877 -1.4046 0.5057  1375 CYS B O   
22885 C CB  . CYS C 1375 ? 3.6848 1.8553 3.7684 -0.6742 -1.4473 0.4306  1375 CYS B CB  
22886 S SG  . CYS C 1375 ? 4.7009 2.8478 4.7507 -0.6565 -1.4605 0.3861  1375 CYS B SG  
22887 N N   . SER C 1376 ? 2.7136 0.9530 2.7447 -0.6588 -1.3877 0.4797  1376 SER B N   
22888 C CA  . SER C 1376 ? 2.7073 0.9852 2.7425 -0.6633 -1.3712 0.5060  1376 SER B CA  
22889 C C   . SER C 1376 ? 2.7837 1.0873 2.8248 -0.6648 -1.3800 0.4978  1376 SER B C   
22890 O O   . SER C 1376 ? 2.7976 1.1355 2.8477 -0.6700 -1.3705 0.5173  1376 SER B O   
22891 C CB  . SER C 1376 ? 2.6176 0.9057 2.6089 -0.6467 -1.3451 0.5101  1376 SER B CB  
22892 O OG  . SER C 1376 ? 2.5637 0.8197 2.5302 -0.6353 -1.3429 0.4950  1376 SER B OG  
22893 N N   . PHE C 1377 ? 3.0767 1.3639 3.1123 -0.6597 -1.3982 0.4684  1377 PHE B N   
22894 C CA  . PHE C 1377 ? 3.0801 1.3889 3.1235 -0.6615 -1.4105 0.4573  1377 PHE B CA  
22895 C C   . PHE C 1377 ? 3.1815 1.4723 3.2563 -0.6729 -1.4392 0.4389  1377 PHE B C   
22896 O O   . PHE C 1377 ? 3.2042 1.4615 3.2716 -0.6680 -1.4512 0.4158  1377 PHE B O   
22897 C CB  . PHE C 1377 ? 3.0177 1.3363 3.0147 -0.6404 -1.4012 0.4379  1377 PHE B CB  
22898 C CG  . PHE C 1377 ? 2.9771 1.3276 2.9532 -0.6331 -1.3765 0.4572  1377 PHE B CG  
22899 C CD1 . PHE C 1377 ? 2.9950 1.3823 2.9872 -0.6396 -1.3749 0.4714  1377 PHE B CD1 
22900 C CD2 . PHE C 1377 ? 2.9402 1.2845 2.8813 -0.6201 -1.3547 0.4613  1377 PHE B CD2 
22901 C CE1 . PHE C 1377 ? 2.9518 1.3684 2.9253 -0.6327 -1.3516 0.4891  1377 PHE B CE1 
22902 C CE2 . PHE C 1377 ? 2.8980 1.2714 2.8200 -0.6136 -1.3314 0.4785  1377 PHE B CE2 
22903 C CZ  . PHE C 1377 ? 2.9053 1.3145 2.8433 -0.6197 -1.3298 0.4925  1377 PHE B CZ  
22904 N N   . TYR C 1378 ? 3.2372 1.5513 3.3476 -0.6882 -1.4497 0.4493  1378 TYR B N   
22905 C CA  . TYR C 1378 ? 3.2679 1.5719 3.4078 -0.6994 -1.4763 0.4317  1378 TYR B CA  
22906 C C   . TYR C 1378 ? 3.2546 1.5688 3.3677 -0.6856 -1.4832 0.4042  1378 TYR B C   
22907 O O   . TYR C 1378 ? 3.1990 1.5449 3.2920 -0.6767 -1.4709 0.4095  1378 TYR B O   
22908 C CB  . TYR C 1378 ? 3.2899 1.6183 3.4776 -0.7212 -1.4837 0.4540  1378 TYR B CB  
22909 C CG  . TYR C 1378 ? 3.2610 1.5760 3.4833 -0.7380 -1.4826 0.4787  1378 TYR B CG  
22910 C CD1 . TYR C 1378 ? 3.2613 1.5356 3.4966 -0.7429 -1.4948 0.4691  1378 TYR B CD1 
22911 C CD2 . TYR C 1378 ? 3.2387 1.5821 3.4814 -0.7490 -1.4697 0.5117  1378 TYR B CD2 
22912 C CE1 . TYR C 1378 ? 3.2712 1.5328 3.5383 -0.7579 -1.4939 0.4922  1378 TYR B CE1 
22913 C CE2 . TYR C 1378 ? 3.2446 1.5764 3.5189 -0.7644 -1.4687 0.5350  1378 TYR B CE2 
22914 C CZ  . TYR C 1378 ? 3.2581 1.5486 3.5445 -0.7687 -1.4809 0.5254  1378 TYR B CZ  
22915 O OH  . TYR C 1378 ? 3.2586 1.5362 3.5763 -0.7835 -1.4801 0.5489  1378 TYR B OH  
22916 N N   . LEU C 1379 ? 3.1783 1.4657 3.2911 -0.6838 -1.5030 0.3752  1379 LEU B N   
22917 C CA  . LEU C 1379 ? 3.2550 1.5491 3.3423 -0.6707 -1.5116 0.3468  1379 LEU B CA  
22918 C C   . LEU C 1379 ? 3.4208 1.7054 3.5368 -0.6819 -1.5400 0.3250  1379 LEU B C   
22919 O O   . LEU C 1379 ? 3.4937 1.7589 3.6477 -0.6990 -1.5542 0.3281  1379 LEU B O   
22920 C CB  . LEU C 1379 ? 3.1890 1.4583 3.2294 -0.6495 -1.5035 0.3255  1379 LEU B CB  
22921 C CG  . LEU C 1379 ? 3.1025 1.3794 3.1073 -0.6355 -1.4757 0.3408  1379 LEU B CG  
22922 C CD1 . LEU C 1379 ? 3.0580 1.3089 3.0192 -0.6157 -1.4712 0.3160  1379 LEU B CD1 
22923 C CD2 . LEU C 1379 ? 3.0879 1.4070 3.0811 -0.6305 -1.4628 0.3533  1379 LEU B CD2 
22924 N N   . LYS C 1380 ? 3.5770 1.8757 3.6737 -0.6718 -1.5478 0.3028  1380 LYS B N   
22925 C CA  . LYS C 1380 ? 3.6541 1.9399 3.7641 -0.6763 -1.5737 0.2739  1380 LYS B CA  
22926 C C   . LYS C 1380 ? 3.6238 1.9211 3.6920 -0.6561 -1.5736 0.2490  1380 LYS B C   
22927 O O   . LYS C 1380 ? 3.5845 1.9164 3.6364 -0.6483 -1.5625 0.2578  1380 LYS B O   
22928 C CB  . LYS C 1380 ? 3.5276 1.8324 3.6877 -0.6987 -1.5911 0.2824  1380 LYS B CB  
22929 C CG  . LYS C 1380 ? 3.5952 1.9462 3.7648 -0.7031 -1.5805 0.3072  1380 LYS B CG  
22930 C CD  . LYS C 1380 ? 3.6415 2.0091 3.8633 -0.7266 -1.5982 0.3156  1380 LYS B CD  
22931 C CE  . LYS C 1380 ? 3.4127 1.8288 3.6423 -0.7294 -1.5889 0.3373  1380 LYS B CE  
22932 N NZ  . LYS C 1380 ? 3.4762 1.9108 3.7557 -0.7519 -1.6069 0.3434  1380 LYS B NZ  
22933 N N   . ILE C 1381 ? 2.8650 1.1324 2.9146 -0.6470 -1.5849 0.2187  1381 ILE B N   
22934 C CA  . ILE C 1381 ? 2.8266 1.1012 2.8375 -0.6284 -1.5873 0.1923  1381 ILE B CA  
22935 C C   . ILE C 1381 ? 2.9753 1.2313 2.9977 -0.6324 -1.6140 0.1598  1381 ILE B C   
22936 O O   . ILE C 1381 ? 3.0585 1.2797 3.0989 -0.6405 -1.6255 0.1503  1381 ILE B O   
22937 C CB  . ILE C 1381 ? 2.6541 0.9108 2.6158 -0.6067 -1.5691 0.1846  1381 ILE B CB  
22938 C CG1 . ILE C 1381 ? 2.6107 0.8938 2.5327 -0.5881 -1.5597 0.1762  1381 ILE B CG1 
22939 C CG2 . ILE C 1381 ? 2.6321 0.8487 2.5841 -0.6017 -1.5822 0.1554  1381 ILE B CG2 
22940 C CD1 . ILE C 1381 ? 2.5582 0.8226 2.4329 -0.5675 -1.5451 0.1640  1381 ILE B CD1 
22941 N N   . ASP C 1382 ? 3.7709 2.0506 3.7823 -0.6263 -1.6237 0.1428  1382 ASP B N   
22942 C CA  . ASP C 1382 ? 3.8561 2.1233 3.8743 -0.6285 -1.6487 0.1102  1382 ASP B CA  
22943 C C   . ASP C 1382 ? 3.8743 2.1709 3.8642 -0.6143 -1.6516 0.0936  1382 ASP B C   
22944 O O   . ASP C 1382 ? 3.8211 2.1539 3.8031 -0.6099 -1.6399 0.1105  1382 ASP B O   
22945 C CB  . ASP C 1382 ? 3.9733 2.2400 4.0465 -0.6536 -1.6698 0.1131  1382 ASP B CB  
22946 C CG  . ASP C 1382 ? 4.0290 2.3392 4.1276 -0.6650 -1.6692 0.1349  1382 ASP B CG  
22947 O OD1 . ASP C 1382 ? 3.9943 2.3161 4.1061 -0.6717 -1.6537 0.1663  1382 ASP B OD1 
22948 O OD2 . ASP C 1382 ? 4.1081 2.4418 4.2135 -0.6671 -1.6844 0.1206  1382 ASP B OD2 
22949 N N   . THR C 1383 ? 3.3506 1.6314 3.3247 -0.6066 -1.6670 0.0604  1383 THR B N   
22950 C CA  . THR C 1383 ? 3.3811 1.6867 3.3245 -0.5913 -1.6699 0.0425  1383 THR B CA  
22951 C C   . THR C 1383 ? 3.4624 1.7898 3.4370 -0.6046 -1.6949 0.0294  1383 THR B C   
22952 O O   . THR C 1383 ? 3.5037 1.8096 3.5026 -0.6162 -1.7161 0.0096  1383 THR B O   
22953 C CB  . THR C 1383 ? 3.3710 1.6497 3.2701 -0.5712 -1.6677 0.0152  1383 THR B CB  
22954 O OG1 . THR C 1383 ? 3.3948 1.6305 3.3076 -0.5782 -1.6758 0.0043  1383 THR B OG1 
22955 C CG2 . THR C 1383 ? 3.2740 1.5562 3.1309 -0.5525 -1.6398 0.0296  1383 THR B CG2 
22956 N N   . GLN C 1384 ? 3.4409 1.8113 3.4163 -0.6034 -1.6919 0.0411  1384 GLN B N   
22957 C CA  . GLN C 1384 ? 3.5648 1.9620 3.5716 -0.6168 -1.7139 0.0328  1384 GLN B CA  
22958 C C   . GLN C 1384 ? 3.6318 2.0414 3.6109 -0.6027 -1.7267 0.0017  1384 GLN B C   
22959 O O   . GLN C 1384 ? 3.5928 1.9881 3.5284 -0.5828 -1.7188 -0.0137 1384 GLN B O   
22960 C CB  . GLN C 1384 ? 3.5827 2.0212 3.6115 -0.6254 -1.7052 0.0638  1384 GLN B CB  
22961 C CG  . GLN C 1384 ? 3.6014 2.0298 3.6665 -0.6436 -1.6976 0.0929  1384 GLN B CG  
22962 C CD  . GLN C 1384 ? 3.6387 2.1087 3.7304 -0.6543 -1.6922 0.1213  1384 GLN B CD  
22963 O OE1 . GLN C 1384 ? 3.6310 2.1342 3.7007 -0.6417 -1.6808 0.1296  1384 GLN B OE1 
22964 N NE2 . GLN C 1384 ? 3.6769 2.1449 3.8165 -0.6775 -1.7000 0.1366  1384 GLN B NE2 
22965 N N   . ASP C 1385 ? 4.1310 2.5675 4.1349 -0.6131 -1.7466 -0.0077 1385 ASP B N   
22966 C CA  . ASP C 1385 ? 4.1951 2.6462 4.1742 -0.6005 -1.7599 -0.0370 1385 ASP B CA  
22967 C C   . ASP C 1385 ? 4.2188 2.7216 4.2015 -0.5990 -1.7635 -0.0303 1385 ASP B C   
22968 O O   . ASP C 1385 ? 4.2256 2.7461 4.1765 -0.5826 -1.7663 -0.0475 1385 ASP B O   
22969 C CB  . ASP C 1385 ? 4.2777 2.7026 4.2748 -0.6106 -1.7859 -0.0693 1385 ASP B CB  
22970 C CG  . ASP C 1385 ? 4.2627 2.6385 4.2401 -0.6034 -1.7820 -0.0839 1385 ASP B CG  
22971 O OD1 . ASP C 1385 ? 4.2369 2.6053 4.1675 -0.5815 -1.7714 -0.0959 1385 ASP B OD1 
22972 O OD2 . ASP C 1385 ? 4.2818 2.6267 4.2906 -0.6194 -1.7891 -0.0831 1385 ASP B OD2 
22973 N N   . ILE C 1386 ? 4.2111 2.7387 4.2321 -0.6158 -1.7630 -0.0049 1386 ILE B N   
22974 C CA  . ILE C 1386 ? 4.2223 2.8006 4.2504 -0.6154 -1.7650 0.0053  1386 ILE B CA  
22975 C C   . ILE C 1386 ? 4.1254 2.7266 4.1098 -0.5919 -1.7410 0.0197  1386 ILE B C   
22976 O O   . ILE C 1386 ? 4.0954 2.7025 4.0402 -0.5721 -1.7403 0.0016  1386 ILE B O   
22977 C CB  . ILE C 1386 ? 5.0356 3.6333 5.1147 -0.6387 -1.7666 0.0326  1386 ILE B CB  
22978 C CG1 . ILE C 1386 ? 5.0653 3.6455 5.1872 -0.6593 -1.7698 0.0215  1386 ILE B CG1 
22979 C CG2 . ILE C 1386 ? 5.0790 3.7349 5.1735 -0.6406 -1.7689 0.0350  1386 ILE B CG2 
22980 C CD1 . ILE C 1386 ? 5.0563 3.6740 5.2271 -0.6770 -1.7451 0.0438  1386 ILE B CD1 
22981 N N   . TYR C 1399 ? 4.3346 2.8900 4.1601 -0.5192 -1.7339 -0.0611 1399 TYR B N   
22982 C CA  . TYR C 1399 ? 4.3421 2.8584 4.1417 -0.5103 -1.7382 -0.0886 1399 TYR B CA  
22983 C C   . TYR C 1399 ? 4.1375 2.6124 3.9548 -0.5217 -1.7324 -0.0805 1399 TYR B C   
22984 O O   . TYR C 1399 ? 4.1711 2.6186 4.0119 -0.5348 -1.7500 -0.0979 1399 TYR B O   
22985 C CB  . TYR C 1399 ? 4.4776 2.9950 4.2201 -0.4829 -1.7194 -0.0928 1399 TYR B CB  
22986 C CG  . TYR C 1399 ? 4.6405 3.1180 4.3512 -0.4711 -1.7195 -0.1186 1399 TYR B CG  
22987 C CD1 . TYR C 1399 ? 4.7754 3.2326 4.4973 -0.4782 -1.7433 -0.1496 1399 TYR B CD1 
22988 C CD2 . TYR C 1399 ? 4.6328 3.0940 4.3014 -0.4526 -1.6954 -0.1123 1399 TYR B CD2 
22989 C CE1 . TYR C 1399 ? 4.8156 3.2371 4.5080 -0.4668 -1.7430 -0.1733 1399 TYR B CE1 
22990 C CE2 . TYR C 1399 ? 4.6688 3.0953 4.3082 -0.4415 -1.6949 -0.1355 1399 TYR B CE2 
22991 C CZ  . TYR C 1399 ? 4.7575 3.1643 4.4086 -0.4484 -1.7187 -0.1658 1399 TYR B CZ  
22992 O OH  . TYR C 1399 ? 4.7666 3.1394 4.3886 -0.4370 -1.7178 -0.1888 1399 TYR B OH  
22993 N N   . LYS C 1400 ? 3.6247 2.0959 3.4305 -0.5165 -1.7073 -0.0534 1400 LYS B N   
22994 C CA  . LYS C 1400 ? 3.3952 1.8324 3.2182 -0.5271 -1.6987 -0.0397 1400 LYS B CA  
22995 C C   . LYS C 1400 ? 3.1457 1.5906 2.9540 -0.5201 -1.6695 -0.0072 1400 LYS B C   
22996 O O   . LYS C 1400 ? 3.0872 1.5388 2.8525 -0.4995 -1.6515 -0.0056 1400 LYS B O   
22997 C CB  . LYS C 1400 ? 3.3570 1.7487 3.1628 -0.5217 -1.7039 -0.0653 1400 LYS B CB  
22998 C CG  . LYS C 1400 ? 3.3176 1.7018 3.0680 -0.4962 -1.6932 -0.0829 1400 LYS B CG  
22999 C CD  . LYS C 1400 ? 3.2850 1.6223 3.0224 -0.4926 -1.6952 -0.1029 1400 LYS B CD  
23000 C CE  . LYS C 1400 ? 3.3419 1.6591 3.1155 -0.5099 -1.7223 -0.1245 1400 LYS B CE  
23001 N NZ  . LYS C 1400 ? 3.3158 1.5868 3.0798 -0.5070 -1.7237 -0.1420 1400 LYS B NZ  
23002 N N   . ARG C 1401 ? 3.1919 1.6358 3.0367 -0.5376 -1.6650 0.0183  1401 ARG B N   
23003 C CA  . ARG C 1401 ? 2.9900 1.4464 2.8290 -0.5347 -1.6390 0.0515  1401 ARG B CA  
23004 C C   . ARG C 1401 ? 2.9420 1.3741 2.8109 -0.5510 -1.6330 0.0715  1401 ARG B C   
23005 O O   . ARG C 1401 ? 2.9959 1.4135 2.9042 -0.5702 -1.6507 0.0675  1401 ARG B O   
23006 C CB  . ARG C 1401 ? 2.8838 1.3888 2.7333 -0.5359 -1.6364 0.0693  1401 ARG B CB  
23007 C CG  . ARG C 1401 ? 2.7487 1.2723 2.6271 -0.5486 -1.6227 0.1055  1401 ARG B CG  
23008 C CD  . ARG C 1401 ? 2.7499 1.2821 2.6855 -0.5751 -1.6423 0.1125  1401 ARG B CD  
23009 N NE  . ARG C 1401 ? 2.7043 1.2767 2.6605 -0.5818 -1.6338 0.1408  1401 ARG B NE  
23010 C CZ  . ARG C 1401 ? 2.7057 1.2901 2.7098 -0.6040 -1.6417 0.1580  1401 ARG B CZ  
23011 N NH1 . ARG C 1401 ? 2.7398 1.2987 2.7785 -0.6228 -1.6585 0.1509  1401 ARG B NH1 
23012 N NH2 . ARG C 1401 ? 2.6829 1.3056 2.7008 -0.6073 -1.6324 0.1829  1401 ARG B NH2 
23013 N N   . ILE C 1402 ? 3.3422 1.7700 3.1907 -0.5426 -1.6074 0.0926  1402 ILE B N   
23014 C CA  . ILE C 1402 ? 3.2527 1.6569 3.1196 -0.5536 -1.5973 0.1121  1402 ILE B CA  
23015 C C   . ILE C 1402 ? 3.2426 1.6739 3.1405 -0.5673 -1.5874 0.1467  1402 ILE B C   
23016 O O   . ILE C 1402 ? 3.2019 1.6617 3.0826 -0.5579 -1.5696 0.1639  1402 ILE B O   
23017 C CB  . ILE C 1402 ? 3.1309 1.5133 2.9545 -0.5357 -1.5741 0.1137  1402 ILE B CB  
23018 C CG1 . ILE C 1402 ? 3.1255 1.4771 2.9195 -0.5229 -1.5826 0.0806  1402 ILE B CG1 
23019 C CG2 . ILE C 1402 ? 3.0780 1.4407 2.9191 -0.5460 -1.5619 0.1362  1402 ILE B CG2 
23020 C CD1 . ILE C 1402 ? 3.0509 1.3791 2.8044 -0.5065 -1.5601 0.0819  1402 ILE B CD1 
23021 N N   . VAL C 1403 ? 2.5644 0.9862 2.5079 -0.5893 -1.5986 0.1567  1403 VAL B N   
23022 C CA  . VAL C 1403 ? 2.5720 1.0149 2.5472 -0.6038 -1.5889 0.1903  1403 VAL B CA  
23023 C C   . VAL C 1403 ? 2.5912 1.0033 2.5798 -0.6128 -1.5801 0.2055  1403 VAL B C   
23024 O O   . VAL C 1403 ? 2.6431 1.0324 2.6652 -0.6292 -1.5963 0.2007  1403 VAL B O   
23025 C CB  . VAL C 1403 ? 2.6437 1.1072 2.6680 -0.6251 -1.6099 0.1934  1403 VAL B CB  
23026 C CG1 . VAL C 1403 ? 2.6319 1.1213 2.6850 -0.6381 -1.5979 0.2289  1403 VAL B CG1 
23027 C CG2 . VAL C 1403 ? 2.6925 1.1844 2.7077 -0.6180 -1.6229 0.1752  1403 VAL B CG2 
23028 N N   . ALA C 1404 ? 3.2354 1.6477 3.1982 -0.6022 -1.5543 0.2240  1404 ALA B N   
23029 C CA  . ALA C 1404 ? 3.1867 1.5733 3.1552 -0.6075 -1.5417 0.2408  1404 ALA B CA  
23030 C C   . ALA C 1404 ? 3.1641 1.5763 3.1524 -0.6171 -1.5254 0.2765  1404 ALA B C   
23031 O O   . ALA C 1404 ? 3.1152 1.5601 3.0885 -0.6089 -1.5114 0.2890  1404 ALA B O   
23032 C CB  . ALA C 1404 ? 3.0966 1.4616 3.0172 -0.5871 -1.5244 0.2318  1404 ALA B CB  
23033 N N   . CYS C 1405 ? 4.5254 2.9220 4.5463 -0.6337 -1.5265 0.2932  1405 CYS B N   
23034 C CA  . CYS C 1405 ? 4.5259 2.9468 4.5732 -0.6464 -1.5147 0.3270  1405 CYS B CA  
23035 C C   . CYS C 1405 ? 4.4654 2.8681 4.5071 -0.6466 -1.4958 0.3467  1405 CYS B C   
23036 O O   . CYS C 1405 ? 4.4709 2.8423 4.4872 -0.6364 -1.4912 0.3345  1405 CYS B O   
23037 C CB  . CYS C 1405 ? 4.5971 3.0234 4.6987 -0.6707 -1.5351 0.3337  1405 CYS B CB  
23038 S SG  . CYS C 1405 ? 4.9006 3.3348 5.0176 -0.6753 -1.5646 0.3043  1405 CYS B SG  
23039 N N   . ALA C 1406 ? 3.1800 1.6033 3.2469 -0.6590 -1.4856 0.3775  1406 ALA B N   
23040 C CA  . ALA C 1406 ? 3.0964 1.5089 3.1595 -0.6599 -1.4664 0.3995  1406 ALA B CA  
23041 C C   . ALA C 1406 ? 3.1305 1.5704 3.2293 -0.6768 -1.4599 0.4323  1406 ALA B C   
23042 O O   . ALA C 1406 ? 3.1275 1.6027 3.2367 -0.6797 -1.4601 0.4404  1406 ALA B O   
23043 C CB  . ALA C 1406 ? 2.9889 1.4056 3.0018 -0.6381 -1.4425 0.3988  1406 ALA B CB  
23044 N N   . SER C 1407 ? 3.3580 1.7823 3.4760 -0.6878 -1.4545 0.4513  1407 SER B N   
23045 C CA  . SER C 1407 ? 3.3566 1.8068 3.4971 -0.6993 -1.4406 0.4853  1407 SER B CA  
23046 C C   . SER C 1407 ? 3.3168 1.7495 3.4456 -0.6970 -1.4226 0.5014  1407 SER B C   
23047 O O   . SER C 1407 ? 3.3321 1.7293 3.4626 -0.6985 -1.4292 0.4930  1407 SER B O   
23048 C CB  . SER C 1407 ? 3.4024 1.8589 3.5972 -0.7236 -1.4576 0.4981  1407 SER B CB  
23049 O OG  . SER C 1407 ? 3.3648 1.8340 3.5785 -0.7343 -1.4427 0.5311  1407 SER B OG  
23050 N N   . TYR C 1408 ? 3.2994 1.7582 3.4175 -0.6937 -1.3999 0.5249  1408 TYR B N   
23051 C CA  . TYR C 1408 ? 3.2263 1.6726 3.3294 -0.6900 -1.3808 0.5402  1408 TYR B CA  
23052 C C   . TYR C 1408 ? 3.2367 1.6661 3.3791 -0.7091 -1.3880 0.5577  1408 TYR B C   
23053 O O   . TYR C 1408 ? 3.3015 1.7430 3.4860 -0.7273 -1.4004 0.5698  1408 TYR B O   
23054 C CB  . TYR C 1408 ? 3.1904 1.6703 3.2751 -0.6832 -1.3550 0.5616  1408 TYR B CB  
23055 C CG  . TYR C 1408 ? 3.1744 1.6438 3.2469 -0.6813 -1.3359 0.5783  1408 TYR B CG  
23056 C CD1 . TYR C 1408 ? 3.1736 1.6074 3.2232 -0.6722 -1.3355 0.5633  1408 TYR B CD1 
23057 C CD2 . TYR C 1408 ? 3.1745 1.6698 3.2590 -0.6889 -1.3188 0.6089  1408 TYR B CD2 
23058 C CE1 . TYR C 1408 ? 3.1574 1.5819 3.1961 -0.6705 -1.3187 0.5782  1408 TYR B CE1 
23059 C CE2 . TYR C 1408 ? 3.1594 1.6458 3.2327 -0.6874 -1.3016 0.6241  1408 TYR B CE2 
23060 C CZ  . TYR C 1408 ? 3.1577 1.6086 3.2079 -0.6781 -1.3017 0.6086  1408 TYR B CZ  
23061 O OH  . TYR C 1408 ? 3.1353 1.5781 3.1739 -0.6763 -1.2849 0.6232  1408 TYR B OH  
23062 N N   . LYS C 1409 ? 3.3409 1.7419 3.4693 -0.7045 -1.3808 0.5583  1409 LYS B N   
23063 C CA  . LYS C 1409 ? 3.3387 1.7225 3.4991 -0.7200 -1.3841 0.5768  1409 LYS B CA  
23064 C C   . LYS C 1409 ? 3.3409 1.7421 3.4936 -0.7198 -1.3594 0.6059  1409 LYS B C   
23065 O O   . LYS C 1409 ? 3.2929 1.6801 3.4145 -0.7074 -1.3451 0.6040  1409 LYS B O   
23066 C CB  . LYS C 1409 ? 3.2835 1.6224 3.4350 -0.7150 -1.3938 0.5577  1409 LYS B CB  
23067 C CG  . LYS C 1409 ? 3.2717 1.5876 3.4401 -0.7195 -1.4207 0.5312  1409 LYS B CG  
23068 C CD  . LYS C 1409 ? 3.2341 1.5048 3.3957 -0.7150 -1.4296 0.5137  1409 LYS B CD  
23069 C CE  . LYS C 1409 ? 3.2793 1.5288 3.4871 -0.7347 -1.4437 0.5262  1409 LYS B CE  
23070 N NZ  . LYS C 1409 ? 3.3009 1.5057 3.5098 -0.7323 -1.4587 0.5046  1409 LYS B NZ  
23071 N N   . PRO C 1410 ? 3.3349 1.7674 3.5161 -0.7336 -1.3543 0.6327  1410 PRO B N   
23072 C CA  . PRO C 1410 ? 3.3392 1.7915 3.5156 -0.7347 -1.3308 0.6616  1410 PRO B CA  
23073 C C   . PRO C 1410 ? 3.4253 1.8512 3.6085 -0.7394 -1.3276 0.6734  1410 PRO B C   
23074 O O   . PRO C 1410 ? 3.4611 1.8701 3.6811 -0.7549 -1.3434 0.6793  1410 PRO B O   
23075 C CB  . PRO C 1410 ? 3.3391 1.8251 3.5551 -0.7524 -1.3332 0.6854  1410 PRO B CB  
23076 C CG  . PRO C 1410 ? 3.3697 1.8632 3.5959 -0.7537 -1.3516 0.6660  1410 PRO B CG  
23077 C CD  . PRO C 1410 ? 3.3991 1.8524 3.6174 -0.7485 -1.3698 0.6364  1410 PRO B CD  
23078 N N   . SER C 1411 ? 3.6213 2.0437 3.7693 -0.7261 -1.3075 0.6762  1411 SER B N   
23079 C CA  . SER C 1411 ? 3.7688 2.1728 3.9204 -0.7295 -1.3006 0.6911  1411 SER B CA  
23080 C C   . SER C 1411 ? 3.9437 2.3735 4.1270 -0.7459 -1.2923 0.7262  1411 SER B C   
23081 O O   . SER C 1411 ? 3.9391 2.4043 4.1270 -0.7490 -1.2836 0.7390  1411 SER B O   
23082 C CB  . SER C 1411 ? 3.7254 2.1254 3.8298 -0.7109 -1.2793 0.6859  1411 SER B CB  
23083 O OG  . SER C 1411 ? 3.7104 2.0866 3.7829 -0.6949 -1.2852 0.6540  1411 SER B OG  
23084 N N   . ARG C 1412 ? 3.7639 2.1767 3.9686 -0.7560 -1.2944 0.7423  1412 ARG B N   
23085 C CA  . ARG C 1412 ? 3.9448 2.3806 4.1818 -0.7725 -1.2877 0.7762  1412 ARG B CA  
23086 C C   . ARG C 1412 ? 3.8926 2.3668 4.1077 -0.7663 -1.2626 0.7925  1412 ARG B C   
23087 O O   . ARG C 1412 ? 3.8618 2.3378 4.0348 -0.7489 -1.2476 0.7808  1412 ARG B O   
23088 C CB  . ARG C 1412 ? 4.1299 2.5420 4.3814 -0.7793 -1.2881 0.7913  1412 ARG B CB  
23089 C CG  . ARG C 1412 ? 4.2374 2.6336 4.4485 -0.7625 -1.2735 0.7840  1412 ARG B CG  
23090 C CD  . ARG C 1412 ? 4.3924 2.7751 4.6186 -0.7698 -1.2698 0.8056  1412 ARG B CD  
23091 N NE  . ARG C 1412 ? 4.4466 2.8336 4.6351 -0.7560 -1.2480 0.8092  1412 ARG B NE  
23092 C CZ  . ARG C 1412 ? 4.5305 2.9111 4.7223 -0.7585 -1.2398 0.8281  1412 ARG B CZ  
23093 N NH1 . ARG C 1412 ? 4.6088 2.9774 4.8402 -0.7742 -1.2514 0.8458  1412 ARG B NH1 
23094 N NH2 . ARG C 1412 ? 4.5136 2.9002 4.6693 -0.7455 -1.2199 0.8293  1412 ARG B NH2 
23095 N N   . GLU C 1413 ? 3.8223 2.3270 4.0667 -0.7808 -1.2581 0.8190  1413 GLU B N   
23096 C CA  . GLU C 1413 ? 3.7519 2.2945 3.9806 -0.7771 -1.2343 0.8374  1413 GLU B CA  
23097 C C   . GLU C 1413 ? 3.5377 2.1025 3.7447 -0.7661 -1.2299 0.8223  1413 GLU B C   
23098 O O   . GLU C 1413 ? 3.4884 2.0875 3.6880 -0.7645 -1.2124 0.8369  1413 GLU B O   
23099 C CB  . GLU C 1413 ? 3.8491 2.3857 4.0429 -0.7649 -1.2138 0.8415  1413 GLU B CB  
23100 C CG  . GLU C 1413 ? 3.9969 2.5085 4.2061 -0.7723 -1.2176 0.8537  1413 GLU B CG  
23101 C CD  . GLU C 1413 ? 4.1149 2.6476 4.3606 -0.7906 -1.2134 0.8886  1413 GLU B CD  
23102 O OE1 . GLU C 1413 ? 4.1294 2.6991 4.3744 -0.7929 -1.1976 0.9062  1413 GLU B OE1 
23103 O OE2 . GLU C 1413 ? 4.1859 2.6980 4.4611 -0.8026 -1.2256 0.8987  1413 GLU B OE2 
23104 N N   . GLU C 1414 ? 3.4579 2.0034 3.6542 -0.7581 -1.2452 0.7931  1414 GLU B N   
23105 C CA  . GLU C 1414 ? 3.2524 1.8164 3.4232 -0.7451 -1.2406 0.7768  1414 GLU B CA  
23106 C C   . GLU C 1414 ? 3.2153 1.8074 3.4165 -0.7560 -1.2507 0.7825  1414 GLU B C   
23107 O O   . GLU C 1414 ? 3.2605 1.8474 3.5019 -0.7726 -1.2693 0.7875  1414 GLU B O   
23108 C CB  . GLU C 1414 ? 3.1377 1.6715 3.2772 -0.7291 -1.2497 0.7425  1414 GLU B CB  
23109 C CG  . GLU C 1414 ? 2.9704 1.4906 3.0650 -0.7118 -1.2313 0.7347  1414 GLU B CG  
23110 C CD  . GLU C 1414 ? 2.8891 1.3756 2.9563 -0.6977 -1.2419 0.7017  1414 GLU B CD  
23111 O OE1 . GLU C 1414 ? 2.9041 1.3744 2.9895 -0.7024 -1.2646 0.6854  1414 GLU B OE1 
23112 O OE2 . GLU C 1414 ? 2.8331 1.3095 2.8608 -0.6820 -1.2275 0.6917  1414 GLU B OE2 
23113 N N   . SER C 1415 ? 3.7103 2.3325 3.8922 -0.7466 -1.2380 0.7819  1415 SER B N   
23114 C CA  . SER C 1415 ? 3.7209 2.3743 3.9292 -0.7555 -1.2450 0.7886  1415 SER B CA  
23115 C C   . SER C 1415 ? 3.7600 2.4003 3.9795 -0.7564 -1.2701 0.7637  1415 SER B C   
23116 O O   . SER C 1415 ? 3.7610 2.3732 3.9559 -0.7445 -1.2778 0.7374  1415 SER B O   
23117 C CB  . SER C 1415 ? 3.6641 2.3523 3.8464 -0.7433 -1.2237 0.7940  1415 SER B CB  
23118 O OG  . SER C 1415 ? 3.6862 2.4054 3.8928 -0.7505 -1.2307 0.7993  1415 SER B OG  
23119 N N   . SER C 1416 ? 3.3199 1.9820 3.5770 -0.7710 -1.2827 0.7721  1416 SER B N   
23120 C CA  . SER C 1416 ? 3.3791 2.0335 3.6521 -0.7745 -1.3072 0.7506  1416 SER B CA  
23121 C C   . SER C 1416 ? 3.3617 2.0248 3.5993 -0.7554 -1.3052 0.7273  1416 SER B C   
23122 O O   . SER C 1416 ? 3.3850 2.0357 3.6238 -0.7532 -1.3244 0.7033  1416 SER B O   
23123 C CB  . SER C 1416 ? 3.4553 2.1364 3.7767 -0.7948 -1.3185 0.7676  1416 SER B CB  
23124 O OG  . SER C 1416 ? 3.4598 2.1838 3.7779 -0.7917 -1.3036 0.7821  1416 SER B OG  
23125 N N   . SER C 1417 ? 3.6704 2.3550 3.8765 -0.7415 -1.2819 0.7342  1417 SER B N   
23126 C CA  . SER C 1417 ? 3.6555 2.3521 3.8300 -0.7238 -1.2788 0.7152  1417 SER B CA  
23127 C C   . SER C 1417 ? 3.6209 2.2820 3.7691 -0.7114 -1.2912 0.6829  1417 SER B C   
23128 O O   . SER C 1417 ? 3.6921 2.3583 3.8272 -0.7019 -1.2997 0.6629  1417 SER B O   
23129 C CB  . SER C 1417 ? 3.6122 2.3317 3.7530 -0.7094 -1.2500 0.7263  1417 SER B CB  
23130 O OG  . SER C 1417 ? 3.5600 2.2547 3.6645 -0.6970 -1.2357 0.7200  1417 SER B OG  
23131 N N   . GLY C 1418 ? 3.5617 2.1875 3.7032 -0.7116 -1.2930 0.6776  1418 GLY B N   
23132 C CA  . GLY C 1418 ? 3.4721 2.0639 3.5873 -0.6993 -1.3034 0.6472  1418 GLY B CA  
23133 C C   . GLY C 1418 ? 3.3817 1.9685 3.4455 -0.6777 -1.2821 0.6386  1418 GLY B C   
23134 O O   . GLY C 1418 ? 3.3079 1.9082 3.3593 -0.6749 -1.2597 0.6574  1418 GLY B O   
23135 N N   . SER C 1419 ? 3.2120 1.7803 3.2456 -0.6626 -1.2884 0.6100  1419 SER B N   
23136 C CA  . SER C 1419 ? 3.1247 1.6783 3.1101 -0.6432 -1.2708 0.5987  1419 SER B CA  
23137 C C   . SER C 1419 ? 3.0044 1.5856 2.9574 -0.6288 -1.2456 0.6061  1419 SER B C   
23138 O O   . SER C 1419 ? 3.0174 1.6320 2.9816 -0.6311 -1.2418 0.6176  1419 SER B O   
23139 C CB  . SER C 1419 ? 3.1386 1.6623 3.1023 -0.6319 -1.2858 0.5656  1419 SER B CB  
23140 O OG  . SER C 1419 ? 3.0750 1.5761 2.9993 -0.6171 -1.2718 0.5555  1419 SER B OG  
23141 N N   . SER C 1420 ? 2.7806 1.3470 2.6942 -0.6143 -1.2281 0.5997  1420 SER B N   
23142 C CA  . SER C 1420 ? 2.6956 1.2800 2.5714 -0.5979 -1.2041 0.6007  1420 SER B CA  
23143 C C   . SER C 1420 ? 2.7139 1.2881 2.5582 -0.5809 -1.2103 0.5719  1420 SER B C   
23144 O O   . SER C 1420 ? 2.7868 1.3471 2.6432 -0.5836 -1.2333 0.5542  1420 SER B O   
23145 C CB  . SER C 1420 ? 2.5968 1.1675 2.4454 -0.5912 -1.1830 0.6062  1420 SER B CB  
23146 O OG  . SER C 1420 ? 2.5456 1.0839 2.3628 -0.5782 -1.1863 0.5807  1420 SER B OG  
23147 N N   . HIS C 1421 ? 2.7485 1.3285 2.5517 -0.5633 -1.1897 0.5669  1421 HIS B N   
23148 C CA  . HIS C 1421 ? 2.7191 1.2889 2.4884 -0.5457 -1.1929 0.5403  1421 HIS B CA  
23149 C C   . HIS C 1421 ? 2.6545 1.1853 2.4149 -0.5430 -1.2090 0.5161  1421 HIS B C   
23150 O O   . HIS C 1421 ? 2.5770 1.0852 2.3271 -0.5427 -1.2020 0.5162  1421 HIS B O   
23151 C CB  . HIS C 1421 ? 2.7179 1.2983 2.4448 -0.5283 -1.1652 0.5417  1421 HIS B CB  
23152 C CG  . HIS C 1421 ? 2.7089 1.2683 2.3935 -0.5095 -1.1635 0.5149  1421 HIS B CG  
23153 N ND1 . HIS C 1421 ? 2.6580 1.2001 2.3065 -0.4981 -1.1450 0.5093  1421 HIS B ND1 
23154 C CD2 . HIS C 1421 ? 2.7381 1.2926 2.4108 -0.5000 -1.1777 0.4924  1421 HIS B CD2 
23155 C CE1 . HIS C 1421 ? 2.6714 1.1980 2.2876 -0.4826 -1.1476 0.4846  1421 HIS B CE1 
23156 N NE2 . HIS C 1421 ? 2.7164 1.2499 2.3462 -0.4833 -1.1675 0.4740  1421 HIS B NE2 
23157 N N   . ALA C 1422 ? 2.5812 1.1052 2.3460 -0.5411 -1.2305 0.4952  1422 ALA B N   
23158 C CA  . ALA C 1422 ? 2.6421 1.1307 2.4058 -0.5410 -1.2494 0.4721  1422 ALA B CA  
23159 C C   . ALA C 1422 ? 2.7093 1.1911 2.4514 -0.5279 -1.2621 0.4436  1422 ALA B C   
23160 O O   . ALA C 1422 ? 2.7094 1.2159 2.4463 -0.5219 -1.2619 0.4421  1422 ALA B O   
23161 C CB  . ALA C 1422 ? 2.6606 1.1414 2.4722 -0.5618 -1.2708 0.4794  1422 ALA B CB  
23162 N N   . VAL C 1423 ? 2.9505 1.3988 2.6808 -0.5236 -1.2733 0.4214  1423 VAL B N   
23163 C CA  . VAL C 1423 ? 3.0109 1.4478 2.7188 -0.5110 -1.2860 0.3922  1423 VAL B CA  
23164 C C   . VAL C 1423 ? 3.0832 1.5003 2.8201 -0.5219 -1.3158 0.3756  1423 VAL B C   
23165 O O   . VAL C 1423 ? 3.1197 1.5212 2.8862 -0.5365 -1.3244 0.3835  1423 VAL B O   
23166 C CB  . VAL C 1423 ? 2.7463 1.1598 2.4074 -0.4929 -1.2717 0.3759  1423 VAL B CB  
23167 C CG1 . VAL C 1423 ? 2.6978 1.1241 2.3366 -0.4865 -1.2421 0.3946  1423 VAL B CG1 
23168 C CG2 . VAL C 1423 ? 2.7479 1.1250 2.4139 -0.4971 -1.2822 0.3642  1423 VAL B CG2 
23169 N N   . MET C 1424 ? 2.8412 1.2594 2.5697 -0.5148 -1.3312 0.3529  1424 MET B N   
23170 C CA  . MET C 1424 ? 2.8271 1.2223 2.5738 -0.5215 -1.3582 0.3312  1424 MET B CA  
23171 C C   . MET C 1424 ? 2.8509 1.2234 2.5576 -0.5035 -1.3604 0.3011  1424 MET B C   
23172 O O   . MET C 1424 ? 2.8610 1.2469 2.5347 -0.4876 -1.3512 0.2929  1424 MET B O   
23173 C CB  . MET C 1424 ? 2.7850 1.2031 2.5638 -0.5321 -1.3781 0.3304  1424 MET B CB  
23174 C CG  . MET C 1424 ? 2.7569 1.2024 2.5717 -0.5480 -1.3735 0.3607  1424 MET B CG  
23175 S SD  . MET C 1424 ? 2.8922 1.3545 2.7581 -0.5676 -1.4020 0.3601  1424 MET B SD  
23176 C CE  . MET C 1424 ? 2.8453 1.2642 2.7338 -0.5792 -1.4255 0.3420  1424 MET B CE  
23177 N N   . ASP C 1425 ? 2.5048 0.8426 2.2141 -0.5057 -1.3719 0.2856  1425 ASP B N   
23178 C CA  . ASP C 1425 ? 2.5277 0.8409 2.1990 -0.4890 -1.3726 0.2578  1425 ASP B CA  
23179 C C   . ASP C 1425 ? 2.6235 0.9141 2.3099 -0.4935 -1.4003 0.2319  1425 ASP B C   
23180 O O   . ASP C 1425 ? 2.6536 0.9199 2.3651 -0.5050 -1.4115 0.2312  1425 ASP B O   
23181 C CB  . ASP C 1425 ? 2.5007 0.7908 2.1506 -0.4830 -1.3549 0.2619  1425 ASP B CB  
23182 C CG  . ASP C 1425 ? 2.5436 0.8078 2.1552 -0.4663 -1.3551 0.2338  1425 ASP B CG  
23183 O OD1 . ASP C 1425 ? 2.5207 0.7932 2.0927 -0.4498 -1.3377 0.2295  1425 ASP B OD1 
23184 O OD2 . ASP C 1425 ? 2.5976 0.8330 2.2192 -0.4697 -1.3717 0.2168  1425 ASP B OD2 
23185 N N   . ILE C 1426 ? 2.4190 0.7182 2.0901 -0.4842 -1.4111 0.2106  1426 ILE B N   
23186 C CA  . ILE C 1426 ? 2.4478 0.7279 2.1285 -0.4865 -1.4370 0.1829  1426 ILE B CA  
23187 C C   . ILE C 1426 ? 2.4556 0.7162 2.0928 -0.4672 -1.4355 0.1548  1426 ILE B C   
23188 O O   . ILE C 1426 ? 2.4471 0.7231 2.0498 -0.4514 -1.4252 0.1484  1426 ILE B O   
23189 C CB  . ILE C 1426 ? 2.4596 0.7651 2.1629 -0.4936 -1.4555 0.1781  1426 ILE B CB  
23190 C CG1 . ILE C 1426 ? 2.4506 0.7800 2.1957 -0.5121 -1.4558 0.2067  1426 ILE B CG1 
23191 C CG2 . ILE C 1426 ? 2.5054 0.7888 2.2256 -0.4998 -1.4826 0.1519  1426 ILE B CG2 
23192 C CD1 . ILE C 1426 ? 2.4812 0.8322 2.2559 -0.5225 -1.4776 0.2011  1426 ILE B CD1 
23193 N N   . SER C 1427 ? 3.1945 1.4205 2.8345 -0.4687 -1.4455 0.1389  1427 SER B N   
23194 C CA  . SER C 1427 ? 3.1890 1.3925 2.7946 -0.4531 -1.4489 0.1094  1427 SER B CA  
23195 C C   . SER C 1427 ? 3.2443 1.4517 2.8608 -0.4552 -1.4741 0.0861  1427 SER B C   
23196 O O   . SER C 1427 ? 3.2857 1.4947 2.9434 -0.4723 -1.4927 0.0887  1427 SER B O   
23197 C CB  . SER C 1427 ? 3.0681 1.2341 2.6795 -0.4564 -1.4515 0.1034  1427 SER B CB  
23198 O OG  . SER C 1427 ? 3.0942 1.2362 2.6801 -0.4440 -1.4599 0.0725  1427 SER B OG  
23199 N N   . LEU C 1428 ? 2.8375 1.0473 2.4178 -0.4384 -1.4746 0.0637  1428 LEU B N   
23200 C CA  . LEU C 1428 ? 2.8936 1.1096 2.4806 -0.4389 -1.4982 0.0400  1428 LEU B CA  
23201 C C   . LEU C 1428 ? 2.9369 1.1209 2.5093 -0.4318 -1.5117 0.0078  1428 LEU B C   
23202 O O   . LEU C 1428 ? 2.9020 1.0740 2.4336 -0.4146 -1.4998 -0.0048 1428 LEU B O   
23203 C CB  . LEU C 1428 ? 2.8465 1.0956 2.4073 -0.4260 -1.4914 0.0391  1428 LEU B CB  
23204 C CG  . LEU C 1428 ? 2.7994 1.0822 2.3811 -0.4348 -1.4821 0.0694  1428 LEU B CG  
23205 C CD1 . LEU C 1428 ? 2.7848 1.0988 2.3359 -0.4195 -1.4704 0.0715  1428 LEU B CD1 
23206 C CD2 . LEU C 1428 ? 2.8093 1.1016 2.4426 -0.4564 -1.5044 0.0747  1428 LEU B CD2 
23207 N N   . PRO C 1429 ? 2.8073 0.9781 2.4129 -0.4451 -1.5368 -0.0063 1429 PRO B N   
23208 C CA  . PRO C 1429 ? 2.8292 0.9666 2.4303 -0.4422 -1.5523 -0.0361 1429 PRO B CA  
23209 C C   . PRO C 1429 ? 2.8344 0.9708 2.3869 -0.4205 -1.5477 -0.0602 1429 PRO B C   
23210 O O   . PRO C 1429 ? 2.8160 0.9804 2.3521 -0.4127 -1.5468 -0.0628 1429 PRO B O   
23211 C CB  . PRO C 1429 ? 2.8836 1.0253 2.5229 -0.4576 -1.5800 -0.0478 1429 PRO B CB  
23212 C CG  . PRO C 1429 ? 2.8763 1.0435 2.5509 -0.4737 -1.5780 -0.0183 1429 PRO B CG  
23213 C CD  . PRO C 1429 ? 2.8170 1.0099 2.4648 -0.4629 -1.5526 0.0037  1429 PRO B CD  
23214 N N   . THR C 1430 ? 3.3718 1.4776 2.9018 -0.4106 -1.5450 -0.0777 1430 THR B N   
23215 C CA  . THR C 1430 ? 3.3836 1.4899 2.8637 -0.3889 -1.5354 -0.0962 1430 THR B CA  
23216 C C   . THR C 1430 ? 3.4840 1.6155 2.9519 -0.3823 -1.5477 -0.1132 1430 THR B C   
23217 O O   . THR C 1430 ? 3.5809 1.7080 3.0664 -0.3885 -1.5714 -0.1341 1430 THR B O   
23218 C CB  . THR C 1430 ? 3.3720 1.4409 2.8342 -0.3807 -1.5369 -0.1184 1430 THR B CB  
23219 O OG1 . THR C 1430 ? 3.3326 1.3814 2.8093 -0.3877 -1.5262 -0.1006 1430 THR B OG1 
23220 C CG2 . THR C 1430 ? 3.3275 1.3979 2.7367 -0.3582 -1.5214 -0.1317 1430 THR B CG2 
23221 N N   . GLY C 1431 ? 3.2366 1.3952 2.6754 -0.3699 -1.5311 -0.1031 1431 GLY B N   
23222 C CA  . GLY C 1431 ? 3.2821 1.4695 2.7090 -0.3630 -1.5395 -0.1135 1431 GLY B CA  
23223 C C   . GLY C 1431 ? 3.3375 1.5512 2.8042 -0.3790 -1.5558 -0.1037 1431 GLY B C   
23224 O O   . GLY C 1431 ? 3.3489 1.5617 2.8335 -0.3857 -1.5797 -0.1238 1431 GLY B O   
23225 N N   . ILE C 1432 ? 2.7787 1.0166 2.2593 -0.3852 -1.5428 -0.0735 1432 ILE B N   
23226 C CA  . ILE C 1432 ? 2.7561 1.0216 2.2760 -0.4010 -1.5565 -0.0613 1432 ILE B CA  
23227 C C   . ILE C 1432 ? 2.7313 1.0331 2.2464 -0.3979 -1.5387 -0.0337 1432 ILE B C   
23228 O O   . ILE C 1432 ? 2.7535 1.0714 2.3039 -0.4131 -1.5397 -0.0113 1432 ILE B O   
23229 C CB  . ILE C 1432 ? 2.7596 1.0092 2.3296 -0.4241 -1.5682 -0.0507 1432 ILE B CB  
23230 C CG1 . ILE C 1432 ? 2.7671 0.9778 2.3433 -0.4274 -1.5837 -0.0757 1432 ILE B CG1 
23231 C CG2 . ILE C 1432 ? 2.8889 1.1660 2.4999 -0.4407 -1.5856 -0.0430 1432 ILE B CG2 
23232 C CD1 . ILE C 1432 ? 2.8582 1.0691 2.4534 -0.4344 -1.6121 -0.1016 1432 ILE B CD1 
23233 N N   . SER C 1433 ? 4.0763 2.3911 3.5485 -0.3781 -1.5227 -0.0355 1433 SER B N   
23234 C CA  . SER C 1433 ? 4.0304 2.3801 3.4942 -0.3726 -1.5061 -0.0122 1433 SER B CA  
23235 C C   . SER C 1433 ? 4.0282 2.4039 3.5370 -0.3908 -1.5146 0.0086  1433 SER B C   
23236 O O   . SER C 1433 ? 4.0731 2.4531 3.6141 -0.4041 -1.5386 -0.0014 1433 SER B O   
23237 C CB  . SER C 1433 ? 4.0811 2.4521 3.5105 -0.3545 -1.5069 -0.0269 1433 SER B CB  
23238 O OG  . SER C 1433 ? 4.0845 2.4388 3.4667 -0.3351 -1.4912 -0.0385 1433 SER B OG  
23239 N N   . ALA C 1434 ? 2.9651 1.3593 2.4755 -0.3913 -1.4943 0.0374  1434 ALA B N   
23240 C CA  . ALA C 1434 ? 3.0099 1.4291 2.5622 -0.4083 -1.4995 0.0596  1434 ALA B CA  
23241 C C   . ALA C 1434 ? 3.0273 1.4867 2.5693 -0.3995 -1.4916 0.0715  1434 ALA B C   
23242 O O   . ALA C 1434 ? 3.0245 1.4904 2.5257 -0.3803 -1.4746 0.0706  1434 ALA B O   
23243 C CB  . ALA C 1434 ? 2.9816 1.3907 2.5503 -0.4184 -1.4834 0.0853  1434 ALA B CB  
23244 N N   . ASN C 1435 ? 2.8938 1.3800 2.4738 -0.4140 -1.5032 0.0841  1435 ASN B N   
23245 C CA  . ASN C 1435 ? 2.9216 1.4485 2.4979 -0.4072 -1.5016 0.0922  1435 ASN B CA  
23246 C C   . ASN C 1435 ? 2.8460 1.3915 2.4010 -0.3960 -1.4727 0.1176  1435 ASN B C   
23247 O O   . ASN C 1435 ? 2.8175 1.3864 2.3983 -0.4057 -1.4667 0.1423  1435 ASN B O   
23248 C CB  . ASN C 1435 ? 2.9797 1.5305 2.6052 -0.4270 -1.5224 0.0988  1435 ASN B CB  
23249 C CG  . ASN C 1435 ? 3.0360 1.6262 2.6578 -0.4195 -1.5311 0.0947  1435 ASN B CG  
23250 O OD1 . ASN C 1435 ? 3.0093 1.6205 2.6028 -0.4033 -1.5137 0.1046  1435 ASN B OD1 
23251 N ND2 . ASN C 1435 ? 3.1243 1.7244 2.7750 -0.4314 -1.5581 0.0799  1435 ASN B ND2 
23252 N N   . GLU C 1436 ? 3.0098 1.5461 2.5178 -0.3755 -1.4551 0.1109  1436 GLU B N   
23253 C CA  . GLU C 1436 ? 2.9862 1.5381 2.4712 -0.3638 -1.4269 0.1330  1436 GLU B CA  
23254 C C   . GLU C 1436 ? 2.9855 1.5779 2.4959 -0.3698 -1.4260 0.1553  1436 GLU B C   
23255 O O   . GLU C 1436 ? 2.9534 1.5554 2.4761 -0.3755 -1.4094 0.1810  1436 GLU B O   
23256 C CB  . GLU C 1436 ? 3.0290 1.5802 2.4627 -0.3394 -1.4149 0.1197  1436 GLU B CB  
23257 C CG  . GLU C 1436 ? 3.0167 1.5765 2.4227 -0.3266 -1.3830 0.1410  1436 GLU B CG  
23258 C CD  . GLU C 1436 ? 2.9890 1.5154 2.3765 -0.3248 -1.3643 0.1434  1436 GLU B CD  
23259 O OE1 . GLU C 1436 ? 3.0180 1.5149 2.4133 -0.3324 -1.3764 0.1283  1436 GLU B OE1 
23260 O OE2 . GLU C 1436 ? 2.9215 1.4511 2.2868 -0.3157 -1.3376 0.1598  1436 GLU B OE2 
23261 N N   . GLU C 1437 ? 3.0551 1.6725 2.5733 -0.3684 -1.4440 0.1453  1437 GLU B N   
23262 C CA  . GLU C 1437 ? 3.0455 1.7039 2.5862 -0.3725 -1.4439 0.1650  1437 GLU B CA  
23263 C C   . GLU C 1437 ? 3.0714 1.7343 2.6627 -0.3968 -1.4514 0.1827  1437 GLU B C   
23264 O O   . GLU C 1437 ? 3.0567 1.7453 2.6655 -0.4017 -1.4404 0.2079  1437 GLU B O   
23265 C CB  . GLU C 1437 ? 3.1358 1.8197 2.6767 -0.3672 -1.4647 0.1481  1437 GLU B CB  
23266 C CG  . GLU C 1437 ? 3.7269 2.3927 3.2295 -0.3510 -1.4719 0.1180  1437 GLU B CG  
23267 C CD  . GLU C 1437 ? 3.6360 2.3044 3.0882 -0.3262 -1.4484 0.1197  1437 GLU B CD  
23268 O OE1 . GLU C 1437 ? 3.5915 2.2827 3.0389 -0.3201 -1.4290 0.1430  1437 GLU B OE1 
23269 O OE2 . GLU C 1437 ? 3.5938 2.2415 3.0113 -0.3128 -1.4492 0.0976  1437 GLU B OE2 
23270 N N   . ASP C 1438 ? 3.2885 1.9261 2.9036 -0.4120 -1.4697 0.1698  1438 ASP B N   
23271 C CA  . ASP C 1438 ? 3.3061 1.9484 2.9712 -0.4358 -1.4796 0.1849  1438 ASP B CA  
23272 C C   . ASP C 1438 ? 3.2194 1.8626 2.8895 -0.4397 -1.4552 0.2145  1438 ASP B C   
23273 O O   . ASP C 1438 ? 3.2213 1.8906 2.9229 -0.4516 -1.4538 0.2367  1438 ASP B O   
23274 C CB  . ASP C 1438 ? 3.3572 1.9651 3.0429 -0.4500 -1.4994 0.1671  1438 ASP B CB  
23275 C CG  . ASP C 1438 ? 3.4370 2.0555 3.1484 -0.4598 -1.5294 0.1477  1438 ASP B CG  
23276 O OD1 . ASP C 1438 ? 3.4687 2.1239 3.1871 -0.4578 -1.5353 0.1513  1438 ASP B OD1 
23277 O OD2 . ASP C 1438 ? 3.4625 2.0530 3.1870 -0.4692 -1.5471 0.1287  1438 ASP B OD2 
23278 N N   . LEU C 1439 ? 2.6986 1.3142 2.3374 -0.4297 -1.4361 0.2145  1439 LEU B N   
23279 C CA  . LEU C 1439 ? 2.5804 1.1893 2.2241 -0.4352 -1.4138 0.2398  1439 LEU B CA  
23280 C C   . LEU C 1439 ? 2.5293 1.1711 2.1634 -0.4268 -1.3915 0.2639  1439 LEU B C   
23281 O O   . LEU C 1439 ? 2.5067 1.1646 2.1691 -0.4392 -1.3845 0.2885  1439 LEU B O   
23282 C CB  . LEU C 1439 ? 2.4909 1.0616 2.1023 -0.4262 -1.4002 0.2309  1439 LEU B CB  
23283 C CG  . LEU C 1439 ? 2.4896 1.0244 2.1044 -0.4314 -1.4195 0.2057  1439 LEU B CG  
23284 C CD1 . LEU C 1439 ? 2.4467 0.9489 2.0210 -0.4174 -1.4044 0.1946  1439 LEU B CD1 
23285 C CD2 . LEU C 1439 ? 2.4884 1.0124 2.1513 -0.4553 -1.4348 0.2131  1439 LEU B CD2 
23286 N N   . LYS C 1440 ? 2.9348 1.5860 2.5292 -0.4056 -1.3808 0.2564  1440 LYS B N   
23287 C CA  . LYS C 1440 ? 2.9425 1.6261 2.5250 -0.3950 -1.3613 0.2758  1440 LYS B CA  
23288 C C   . LYS C 1440 ? 2.9442 1.6644 2.5695 -0.4091 -1.3712 0.2935  1440 LYS B C   
23289 O O   . LYS C 1440 ? 2.9025 1.6489 2.5300 -0.4063 -1.3543 0.3159  1440 LYS B O   
23290 C CB  . LYS C 1440 ? 3.0334 1.7255 2.5760 -0.3726 -1.3593 0.2597  1440 LYS B CB  
23291 C CG  . LYS C 1440 ? 3.0861 1.7458 2.5832 -0.3566 -1.3479 0.2425  1440 LYS B CG  
23292 C CD  . LYS C 1440 ? 3.1003 1.7566 2.5700 -0.3460 -1.3153 0.2602  1440 LYS B CD  
23293 C CE  . LYS C 1440 ? 3.1805 1.8314 2.5986 -0.3216 -1.3008 0.2478  1440 LYS B CE  
23294 N NZ  . LYS C 1440 ? 3.2390 1.8661 2.6381 -0.3154 -1.3177 0.2176  1440 LYS B NZ  
23295 N N   . ALA C 1441 ? 2.6701 1.3917 2.3293 -0.4243 -1.3987 0.2825  1441 ALA B N   
23296 C CA  . ALA C 1441 ? 2.7322 1.4881 2.4340 -0.4390 -1.4119 0.2956  1441 ALA B CA  
23297 C C   . ALA C 1441 ? 2.7575 1.5147 2.4922 -0.4567 -1.4030 0.3214  1441 ALA B C   
23298 O O   . ALA C 1441 ? 2.7741 1.5619 2.5246 -0.4599 -1.3923 0.3450  1441 ALA B O   
23299 C CB  . ALA C 1441 ? 2.7972 1.5499 2.5249 -0.4509 -1.4445 0.2734  1441 ALA B CB  
23300 N N   . LEU C 1442 ? 2.9286 1.6514 2.6727 -0.4678 -1.4078 0.3161  1442 LEU B N   
23301 C CA  . LEU C 1442 ? 2.9190 1.6353 2.6919 -0.4848 -1.4005 0.3377  1442 LEU B CA  
23302 C C   . LEU C 1442 ? 2.9530 1.6808 2.7077 -0.4763 -1.3694 0.3623  1442 LEU B C   
23303 O O   . LEU C 1442 ? 2.9979 1.7494 2.7800 -0.4871 -1.3624 0.3869  1442 LEU B O   
23304 C CB  . LEU C 1442 ? 2.8615 1.5341 2.6347 -0.4917 -1.4082 0.3237  1442 LEU B CB  
23305 C CG  . LEU C 1442 ? 2.9062 1.5648 2.7020 -0.5026 -1.4393 0.2999  1442 LEU B CG  
23306 C CD1 . LEU C 1442 ? 2.9006 1.5153 2.6747 -0.4977 -1.4440 0.2769  1442 LEU B CD1 
23307 C CD2 . LEU C 1442 ? 2.9381 1.6048 2.7888 -0.5282 -1.4545 0.3133  1442 LEU B CD2 
23308 N N   . VAL C 1443 ? 2.9155 1.6281 2.6244 -0.4569 -1.3507 0.3555  1443 VAL B N   
23309 C CA  . VAL C 1443 ? 2.8954 1.6146 2.5842 -0.4486 -1.3203 0.3766  1443 VAL B CA  
23310 C C   . VAL C 1443 ? 2.9054 1.6612 2.5811 -0.4353 -1.3069 0.3881  1443 VAL B C   
23311 O O   . VAL C 1443 ? 2.8839 1.6600 2.5688 -0.4379 -1.2894 0.4124  1443 VAL B O   
23312 C CB  . VAL C 1443 ? 2.8564 1.5414 2.5021 -0.4346 -1.3039 0.3655  1443 VAL B CB  
23313 C CG1 . VAL C 1443 ? 2.8876 1.5376 2.5332 -0.4389 -1.3236 0.3409  1443 VAL B CG1 
23314 C CG2 . VAL C 1443 ? 2.8548 1.5478 2.4555 -0.4107 -1.2890 0.3578  1443 VAL B CG2 
23315 N N   . GLU C 1444 ? 3.2027 1.9672 2.8572 -0.4208 -1.3150 0.3707  1444 GLU B N   
23316 C CA  . GLU C 1444 ? 3.2402 2.0335 2.8725 -0.4037 -1.2992 0.3793  1444 GLU B CA  
23317 C C   . GLU C 1444 ? 3.2323 2.0678 2.8990 -0.4122 -1.3019 0.4000  1444 GLU B C   
23318 O O   . GLU C 1444 ? 3.2184 2.0814 2.8731 -0.3990 -1.2970 0.4030  1444 GLU B O   
23319 C CB  . GLU C 1444 ? 3.3718 2.1630 2.9714 -0.3854 -1.3078 0.3550  1444 GLU B CB  
23320 C CG  . GLU C 1444 ? 3.4533 2.2643 3.0183 -0.3635 -1.2871 0.3613  1444 GLU B CG  
23321 C CD  . GLU C 1444 ? 3.5281 2.3229 3.0496 -0.3436 -1.2882 0.3370  1444 GLU B CD  
23322 O OE1 . GLU C 1444 ? 3.5219 2.2814 3.0268 -0.3433 -1.2904 0.3206  1444 GLU B OE1 
23323 O OE2 . GLU C 1444 ? 3.5807 2.3983 3.0844 -0.3281 -1.2864 0.3348  1444 GLU B OE2 
23324 N N   . GLY C 1445 ? 3.4509 2.2922 3.1601 -0.4336 -1.3089 0.4149  1445 GLY B N   
23325 C CA  . GLY C 1445 ? 3.5148 2.3965 3.2582 -0.4425 -1.3121 0.4342  1445 GLY B CA  
23326 C C   . GLY C 1445 ? 3.5147 2.4055 3.2888 -0.4588 -1.3007 0.4614  1445 GLY B C   
23327 O O   . GLY C 1445 ? 3.4944 2.3585 3.2738 -0.4688 -1.2967 0.4645  1445 GLY B O   
23328 N N   . VAL C 1446 ? 2.4361 1.3661 2.2300 -0.4608 -1.2952 0.4811  1446 VAL B N   
23329 C CA  . VAL C 1446 ? 2.4248 1.3723 2.2538 -0.4774 -1.2872 0.5080  1446 VAL B CA  
23330 C C   . VAL C 1446 ? 2.4314 1.3708 2.3052 -0.5024 -1.3103 0.5076  1446 VAL B C   
23331 O O   . VAL C 1446 ? 2.4015 1.3480 2.3054 -0.5185 -1.3055 0.5282  1446 VAL B O   
23332 C CB  . VAL C 1446 ? 2.4793 1.4738 2.3219 -0.4736 -1.2811 0.5256  1446 VAL B CB  
23333 C CG1 . VAL C 1446 ? 2.4824 1.4983 2.3661 -0.4925 -1.2765 0.5524  1446 VAL B CG1 
23334 C CG2 . VAL C 1446 ? 2.4502 1.4519 2.2498 -0.4493 -1.2554 0.5292  1446 VAL B CG2 
23335 N N   . ASP C 1447 ? 3.8154 2.7405 3.6944 -0.5058 -1.3354 0.4841  1447 ASP B N   
23336 C CA  . ASP C 1447 ? 3.8564 2.7623 3.7706 -0.5278 -1.3552 0.4801  1447 ASP B CA  
23337 C C   . ASP C 1447 ? 3.7973 2.6569 3.6865 -0.5246 -1.3509 0.4669  1447 ASP B C   
23338 O O   . ASP C 1447 ? 3.8207 2.6551 3.7212 -0.5337 -1.3710 0.4495  1447 ASP B O   
23339 C CB  . ASP C 1447 ? 3.9632 2.8787 3.9017 -0.5360 -1.3860 0.4620  1447 ASP B CB  
23340 C CG  . ASP C 1447 ? 4.0049 2.9025 3.9086 -0.5197 -1.3962 0.4320  1447 ASP B CG  
23341 O OD1 . ASP C 1447 ? 3.9569 2.8364 3.8172 -0.5013 -1.3788 0.4259  1447 ASP B OD1 
23342 O OD2 . ASP C 1447 ? 4.0753 2.9776 3.9952 -0.5255 -1.4215 0.4142  1447 ASP B OD2 
23343 N N   . GLN C 1448 ? 2.7044 1.5531 2.5598 -0.5115 -1.3246 0.4747  1448 GLN B N   
23344 C CA  . GLN C 1448 ? 2.6488 1.4552 2.4758 -0.5057 -1.3189 0.4611  1448 GLN B CA  
23345 C C   . GLN C 1448 ? 2.6269 1.4081 2.4818 -0.5253 -1.3265 0.4659  1448 GLN B C   
23346 O O   . GLN C 1448 ? 2.6100 1.3937 2.4777 -0.5341 -1.3117 0.4883  1448 GLN B O   
23347 C CB  . GLN C 1448 ? 2.5931 1.3935 2.3763 -0.4870 -1.2889 0.4670  1448 GLN B CB  
23348 C CG  . GLN C 1448 ? 2.5722 1.3863 2.3627 -0.4918 -1.2646 0.4959  1448 GLN B CG  
23349 C CD  . GLN C 1448 ? 2.5338 1.3385 2.2778 -0.4725 -1.2359 0.4975  1448 GLN B CD  
23350 O OE1 . GLN C 1448 ? 2.5042 1.2758 2.2220 -0.4666 -1.2307 0.4850  1448 GLN B OE1 
23351 N NE2 . GLN C 1448 ? 2.5250 1.3589 2.2588 -0.4625 -1.2172 0.5125  1448 GLN B NE2 
23352 N N   . LEU C 1449 ? 2.9122 1.6690 2.7756 -0.5314 -1.3498 0.4440  1449 LEU B N   
23353 C CA  . LEU C 1449 ? 2.9306 1.6591 2.8204 -0.5493 -1.3618 0.4432  1449 LEU B CA  
23354 C C   . LEU C 1449 ? 2.8224 1.5133 2.6806 -0.5408 -1.3488 0.4360  1449 LEU B C   
23355 O O   . LEU C 1449 ? 2.7843 1.4543 2.6590 -0.5532 -1.3485 0.4439  1449 LEU B O   
23356 C CB  . LEU C 1449 ? 3.0574 1.7765 2.9683 -0.5580 -1.3927 0.4205  1449 LEU B CB  
23357 C CG  . LEU C 1449 ? 3.1319 1.8093 3.0517 -0.5677 -1.4063 0.4064  1449 LEU B CG  
23358 C CD1 . LEU C 1449 ? 3.1398 1.8098 3.0911 -0.5861 -1.4006 0.4300  1449 LEU B CD1 
23359 C CD2 . LEU C 1449 ? 3.2209 1.8920 3.1616 -0.5759 -1.4370 0.3827  1449 LEU B CD2 
23360 N N   . PHE C 1450 ? 2.8253 1.5083 2.6383 -0.5196 -1.3388 0.4204  1450 PHE B N   
23361 C CA  . PHE C 1450 ? 2.7416 1.3954 2.5182 -0.5081 -1.3211 0.4157  1450 PHE B CA  
23362 C C   . PHE C 1450 ? 2.7080 1.3803 2.4480 -0.4890 -1.2970 0.4218  1450 PHE B C   
23363 O O   . PHE C 1450 ? 2.7320 1.4376 2.4778 -0.4857 -1.2957 0.4299  1450 PHE B O   
23364 C CB  . PHE C 1450 ? 2.7301 1.3503 2.4855 -0.5005 -1.3351 0.3854  1450 PHE B CB  
23365 C CG  . PHE C 1450 ? 2.7592 1.3602 2.5494 -0.5180 -1.3603 0.3761  1450 PHE B CG  
23366 C CD1 . PHE C 1450 ? 2.8376 1.4529 2.6551 -0.5267 -1.3845 0.3667  1450 PHE B CD1 
23367 C CD2 . PHE C 1450 ? 2.7285 1.2981 2.5256 -0.5263 -1.3598 0.3774  1450 PHE B CD2 
23368 C CE1 . PHE C 1450 ? 2.8671 1.4642 2.7179 -0.5434 -1.4077 0.3577  1450 PHE B CE1 
23369 C CE2 . PHE C 1450 ? 2.7698 1.3208 2.6002 -0.5425 -1.3828 0.3694  1450 PHE B CE2 
23370 C CZ  . PHE C 1450 ? 2.8363 1.4006 2.6938 -0.5513 -1.4067 0.3593  1450 PHE B CZ  
23371 N N   . THR C 1451 ? 2.4181 1.0687 2.1201 -0.4759 -1.2781 0.4173  1451 THR B N   
23372 C CA  . THR C 1451 ? 2.3405 1.0064 2.0083 -0.4588 -1.2519 0.4258  1451 THR B CA  
23373 C C   . THR C 1451 ? 2.3056 0.9448 1.9259 -0.4403 -1.2422 0.4057  1451 THR B C   
23374 O O   . THR C 1451 ? 2.2755 0.9222 1.8617 -0.4239 -1.2212 0.4079  1451 THR B O   
23375 C CB  . THR C 1451 ? 2.2605 0.9329 1.9352 -0.4654 -1.2298 0.4518  1451 THR B CB  
23376 O OG1 . THR C 1451 ? 2.2068 0.8452 1.8712 -0.4679 -1.2252 0.4469  1451 THR B OG1 
23377 C CG2 . THR C 1451 ? 2.2798 0.9746 2.0042 -0.4862 -1.2393 0.4728  1451 THR B CG2 
23378 N N   . ASP C 1452 ? 2.9290 1.5364 2.5473 -0.4430 -1.2572 0.3861  1452 ASP B N   
23379 C CA  . ASP C 1452 ? 2.9139 1.4972 2.4884 -0.4254 -1.2513 0.3643  1452 ASP B CA  
23380 C C   . ASP C 1452 ? 2.9654 1.5199 2.5447 -0.4292 -1.2752 0.3396  1452 ASP B C   
23381 O O   . ASP C 1452 ? 2.9571 1.4928 2.5613 -0.4438 -1.2854 0.3409  1452 ASP B O   
23382 C CB  . ASP C 1452 ? 2.7985 1.3673 2.3458 -0.4187 -1.2244 0.3730  1452 ASP B CB  
23383 C CG  . ASP C 1452 ? 2.7194 1.2797 2.2166 -0.3965 -1.2092 0.3582  1452 ASP B CG  
23384 O OD1 . ASP C 1452 ? 2.7212 1.2531 2.1974 -0.3899 -1.2157 0.3362  1452 ASP B OD1 
23385 O OD2 . ASP C 1452 ? 2.6632 1.2450 2.1421 -0.3856 -1.1907 0.3684  1452 ASP B OD2 
23386 N N   . TYR C 1453 ? 3.1842 1.7364 2.7393 -0.4155 -1.2839 0.3171  1453 TYR B N   
23387 C CA  . TYR C 1453 ? 3.2136 1.7389 2.7660 -0.4155 -1.3052 0.2902  1453 TYR B CA  
23388 C C   . TYR C 1453 ? 3.1764 1.6802 2.6792 -0.3959 -1.2909 0.2737  1453 TYR B C   
23389 O O   . TYR C 1453 ? 3.1516 1.6673 2.6243 -0.3817 -1.2689 0.2807  1453 TYR B O   
23390 C CB  . TYR C 1453 ? 3.2748 1.8181 2.8410 -0.4161 -1.3288 0.2766  1453 TYR B CB  
23391 C CG  . TYR C 1453 ? 3.2941 1.8468 2.8209 -0.3949 -1.3243 0.2615  1453 TYR B CG  
23392 C CD1 . TYR C 1453 ? 3.3095 1.8879 2.8166 -0.3828 -1.3035 0.2762  1453 TYR B CD1 
23393 C CD2 . TYR C 1453 ? 3.3376 1.8735 2.8472 -0.3870 -1.3408 0.2327  1453 TYR B CD2 
23394 C CE1 . TYR C 1453 ? 3.3393 1.9256 2.8103 -0.3631 -1.2989 0.2633  1453 TYR B CE1 
23395 C CE2 . TYR C 1453 ? 3.3713 1.9159 2.8445 -0.3675 -1.3365 0.2194  1453 TYR B CE2 
23396 C CZ  . TYR C 1453 ? 3.3513 1.9209 2.8054 -0.3556 -1.3156 0.2353  1453 TYR B CZ  
23397 O OH  . TYR C 1453 ? 3.3268 1.9049 2.7445 -0.3358 -1.3106 0.2233  1453 TYR B OH  
23398 N N   . GLN C 1454 ? 3.2121 1.6842 2.7064 -0.3949 -1.3027 0.2517  1454 GLN B N   
23399 C CA  . GLN C 1454 ? 3.1873 1.6406 2.6350 -0.3759 -1.2924 0.2327  1454 GLN B CA  
23400 C C   . GLN C 1454 ? 3.2114 1.6317 2.6569 -0.3771 -1.3102 0.2075  1454 GLN B C   
23401 O O   . GLN C 1454 ? 3.1934 1.5923 2.6580 -0.3888 -1.3149 0.2096  1454 GLN B O   
23402 C CB  . GLN C 1454 ? 3.1378 1.5839 2.5601 -0.3690 -1.2631 0.2463  1454 GLN B CB  
23403 C CG  . GLN C 1454 ? 3.1263 1.5596 2.5745 -0.3849 -1.2595 0.2623  1454 GLN B CG  
23404 C CD  . GLN C 1454 ? 3.0956 1.5145 2.5143 -0.3771 -1.2333 0.2684  1454 GLN B CD  
23405 O OE1 . GLN C 1454 ? 3.0883 1.4859 2.4726 -0.3641 -1.2280 0.2500  1454 GLN B OE1 
23406 N NE2 . GLN C 1454 ? 3.0725 1.5033 2.5048 -0.3853 -1.2171 0.2939  1454 GLN B NE2 
23407 N N   . ILE C 1455 ? 3.4102 1.8268 2.8314 -0.3642 -1.3197 0.1836  1455 ILE B N   
23408 C CA  . ILE C 1455 ? 3.4225 1.8088 2.8387 -0.3635 -1.3367 0.1572  1455 ILE B CA  
23409 C C   . ILE C 1455 ? 3.3730 1.7348 2.7469 -0.3486 -1.3190 0.1467  1455 ILE B C   
23410 O O   . ILE C 1455 ? 3.3674 1.7320 2.7035 -0.3310 -1.3107 0.1346  1455 ILE B O   
23411 C CB  . ILE C 1455 ? 3.5761 1.9704 2.9883 -0.3577 -1.3579 0.1344  1455 ILE B CB  
23412 C CG1 . ILE C 1455 ? 3.6224 2.0360 3.0811 -0.3751 -1.3804 0.1402  1455 ILE B CG1 
23413 C CG2 . ILE C 1455 ? 3.5981 1.9598 2.9932 -0.3520 -1.3700 0.1052  1455 ILE B CG2 
23414 C CD1 . ILE C 1455 ? 3.6248 2.0782 3.0913 -0.3743 -1.3741 0.1592  1455 ILE B CD1 
23415 N N   . LYS C 1456 ? 3.1429 1.4812 2.5231 -0.3554 -1.3131 0.1514  1456 LYS B N   
23416 C CA  . LYS C 1456 ? 3.1116 1.4258 2.4536 -0.3422 -1.2983 0.1395  1456 LYS B CA  
23417 C C   . LYS C 1456 ? 3.0838 1.3655 2.4297 -0.3448 -1.3163 0.1163  1456 LYS B C   
23418 O O   . LYS C 1456 ? 3.0719 1.3439 2.4548 -0.3605 -1.3339 0.1175  1456 LYS B O   
23419 C CB  . LYS C 1456 ? 3.1058 1.4185 2.4409 -0.3434 -1.2724 0.1615  1456 LYS B CB  
23420 C CG  . LYS C 1456 ? 3.1517 1.4496 2.4400 -0.3261 -1.2517 0.1515  1456 LYS B CG  
23421 C CD  . LYS C 1456 ? 3.1516 1.4458 2.4349 -0.3287 -1.2277 0.1711  1456 LYS B CD  
23422 C CE  . LYS C 1456 ? 3.1525 1.4336 2.3884 -0.3116 -1.2065 0.1607  1456 LYS B CE  
23423 N NZ  . LYS C 1456 ? 3.1606 1.4618 2.3660 -0.2967 -1.1919 0.1614  1456 LYS B NZ  
23424 N N   . ASP C 1457 ? 3.5164 1.7818 2.8234 -0.3287 -1.3114 0.0950  1457 ASP B N   
23425 C CA  . ASP C 1457 ? 3.5480 1.7814 2.8505 -0.3275 -1.3244 0.0713  1457 ASP B CA  
23426 C C   . ASP C 1457 ? 3.5472 1.7708 2.8950 -0.3455 -1.3502 0.0686  1457 ASP B C   
23427 O O   . ASP C 1457 ? 3.5276 1.7303 2.8928 -0.3547 -1.3519 0.0726  1457 ASP B O   
23428 C CB  . ASP C 1457 ? 3.5470 1.7588 2.8281 -0.3224 -1.3045 0.0744  1457 ASP B CB  
23429 C CG  . ASP C 1457 ? 3.5687 1.7885 2.8038 -0.3046 -1.2783 0.0757  1457 ASP B CG  
23430 O OD1 . ASP C 1457 ? 3.6308 1.8534 2.8369 -0.2904 -1.2799 0.0577  1457 ASP B OD1 
23431 O OD2 . ASP C 1457 ? 3.5266 1.7497 2.7545 -0.3049 -1.2559 0.0947  1457 ASP B OD2 
23432 N N   . GLY C 1458 ? 2.8618 1.1016 2.2291 -0.3506 -1.3699 0.0623  1458 GLY B N   
23433 C CA  . GLY C 1458 ? 2.8634 1.0926 2.2709 -0.3665 -1.3965 0.0544  1458 GLY B CA  
23434 C C   . GLY C 1458 ? 2.8269 1.0684 2.2803 -0.3865 -1.4008 0.0796  1458 GLY B C   
23435 O O   . GLY C 1458 ? 2.8506 1.0805 2.3399 -0.4014 -1.4211 0.0758  1458 GLY B O   
23436 N N   . HIS C 1459 ? 3.0723 1.3372 2.5253 -0.3873 -1.3818 0.1057  1459 HIS B N   
23437 C CA  . HIS C 1459 ? 3.0615 1.3375 2.5571 -0.4062 -1.3845 0.1302  1459 HIS B CA  
23438 C C   . HIS C 1459 ? 3.0262 1.3399 2.5290 -0.4075 -1.3779 0.1490  1459 HIS B C   
23439 O O   . HIS C 1459 ? 2.9787 1.3083 2.4498 -0.3934 -1.3590 0.1539  1459 HIS B O   
23440 C CB  . HIS C 1459 ? 3.0305 1.2931 2.5260 -0.4097 -1.3659 0.1485  1459 HIS B CB  
23441 C CG  . HIS C 1459 ? 3.0851 1.3108 2.5762 -0.4091 -1.3713 0.1330  1459 HIS B CG  
23442 N ND1 . HIS C 1459 ? 3.1352 1.3417 2.6634 -0.4247 -1.3897 0.1318  1459 HIS B ND1 
23443 C CD2 . HIS C 1459 ? 3.0839 1.2883 2.5384 -0.3949 -1.3600 0.1189  1459 HIS B CD2 
23444 C CE1 . HIS C 1459 ? 3.1290 1.3041 2.6435 -0.4195 -1.3897 0.1175  1459 HIS B CE1 
23445 N NE2 . HIS C 1459 ? 3.0974 1.2711 2.5673 -0.4015 -1.3719 0.1094  1459 HIS B NE2 
23446 N N   . VAL C 1460 ? 3.0674 1.3949 2.6133 -0.4248 -1.3936 0.1594  1460 VAL B N   
23447 C CA  . VAL C 1460 ? 3.0906 1.4549 2.6521 -0.4296 -1.3883 0.1809  1460 VAL B CA  
23448 C C   . VAL C 1460 ? 3.1012 1.4704 2.6814 -0.4404 -1.3720 0.2108  1460 VAL B C   
23449 O O   . VAL C 1460 ? 3.1342 1.4893 2.7473 -0.4563 -1.3812 0.2179  1460 VAL B O   
23450 C CB  . VAL C 1460 ? 3.1557 1.5343 2.7572 -0.4442 -1.4145 0.1772  1460 VAL B CB  
23451 C CG1 . VAL C 1460 ? 3.1485 1.5562 2.7838 -0.4583 -1.4096 0.2071  1460 VAL B CG1 
23452 C CG2 . VAL C 1460 ? 3.2034 1.5970 2.7864 -0.4324 -1.4261 0.1560  1460 VAL B CG2 
23453 N N   . ILE C 1461 ? 2.9983 1.3879 2.5583 -0.4319 -1.3478 0.2287  1461 ILE B N   
23454 C CA  . ILE C 1461 ? 2.9345 1.3296 2.5078 -0.4406 -1.3298 0.2567  1461 ILE B CA  
23455 C C   . ILE C 1461 ? 2.9321 1.3650 2.5208 -0.4453 -1.3201 0.2817  1461 ILE B C   
23456 O O   . ILE C 1461 ? 2.9047 1.3575 2.4668 -0.4318 -1.3045 0.2854  1461 ILE B O   
23457 C CB  . ILE C 1461 ? 2.8214 1.2003 2.3569 -0.4279 -1.3058 0.2574  1461 ILE B CB  
23458 C CG1 . ILE C 1461 ? 2.8162 1.1574 2.3505 -0.4298 -1.3147 0.2415  1461 ILE B CG1 
23459 C CG2 . ILE C 1461 ? 2.7369 1.1311 2.2812 -0.4342 -1.2847 0.2871  1461 ILE B CG2 
23460 C CD1 . ILE C 1461 ? 2.7776 1.1003 2.2694 -0.4145 -1.2948 0.2339  1461 ILE B CD1 
23461 N N   . LEU C 1462 ? 2.9251 1.3672 2.5576 -0.4645 -1.3291 0.2992  1462 LEU B N   
23462 C CA  . LEU C 1462 ? 2.9442 1.4229 2.5982 -0.4714 -1.3242 0.3219  1462 LEU B CA  
23463 C C   . LEU C 1462 ? 2.9361 1.4219 2.6010 -0.4794 -1.3044 0.3504  1462 LEU B C   
23464 O O   . LEU C 1462 ? 2.9282 1.3944 2.6116 -0.4910 -1.3071 0.3565  1462 LEU B O   
23465 C CB  . LEU C 1462 ? 2.9701 1.4586 2.6689 -0.4886 -1.3506 0.3209  1462 LEU B CB  
23466 C CG  . LEU C 1462 ? 2.8333 1.3274 2.5220 -0.4801 -1.3684 0.2963  1462 LEU B CG  
23467 C CD1 . LEU C 1462 ? 2.8984 1.3966 2.6311 -0.4980 -1.3960 0.2917  1462 LEU B CD1 
23468 C CD2 . LEU C 1462 ? 2.8224 1.3502 2.4911 -0.4673 -1.3547 0.3042  1462 LEU B CD2 
23469 N N   . GLN C 1463 ? 2.8529 1.3673 2.5068 -0.4731 -1.2847 0.3679  1463 GLN B N   
23470 C CA  . GLN C 1463 ? 2.7856 1.3123 2.4521 -0.4814 -1.2657 0.3964  1463 GLN B CA  
23471 C C   . GLN C 1463 ? 2.7709 1.3336 2.4723 -0.4931 -1.2690 0.4173  1463 GLN B C   
23472 O O   . GLN C 1463 ? 2.7718 1.3554 2.4776 -0.4900 -1.2793 0.4113  1463 GLN B O   
23473 C CB  . GLN C 1463 ? 2.7525 1.2812 2.3773 -0.4652 -1.2359 0.4020  1463 GLN B CB  
23474 C CG  . GLN C 1463 ? 2.7323 1.2309 2.3363 -0.4620 -1.2237 0.3986  1463 GLN B CG  
23475 C CD  . GLN C 1463 ? 2.7225 1.2257 2.2849 -0.4457 -1.1950 0.4023  1463 GLN B CD  
23476 O OE1 . GLN C 1463 ? 2.7044 1.1842 2.2342 -0.4346 -1.1863 0.3883  1463 GLN B OE1 
23477 N NE2 . GLN C 1463 ? 2.7353 1.2693 2.2988 -0.4441 -1.1799 0.4208  1463 GLN B NE2 
23478 N N   . LEU C 1464 ? 2.9689 1.5392 2.6944 -0.5065 -1.2599 0.4420  1464 LEU B N   
23479 C CA  . LEU C 1464 ? 2.9830 1.5869 2.7429 -0.5190 -1.2605 0.4647  1464 LEU B CA  
23480 C C   . LEU C 1464 ? 2.9751 1.5804 2.7515 -0.5307 -1.2461 0.4901  1464 LEU B C   
23481 O O   . LEU C 1464 ? 2.9154 1.4949 2.6798 -0.5302 -1.2387 0.4888  1464 LEU B O   
23482 C CB  . LEU C 1464 ? 3.0469 1.6536 2.8477 -0.5346 -1.2894 0.4591  1464 LEU B CB  
23483 C CG  . LEU C 1464 ? 3.0353 1.6065 2.8529 -0.5453 -1.3084 0.4461  1464 LEU B CG  
23484 C CD1 . LEU C 1464 ? 2.9750 1.5247 2.7928 -0.5509 -1.2959 0.4586  1464 LEU B CD1 
23485 C CD2 . LEU C 1464 ? 3.1024 1.6826 2.9680 -0.5646 -1.3334 0.4483  1464 LEU B CD2 
23486 N N   . ASN C 1465 ? 3.0495 1.6861 2.8551 -0.5416 -1.2430 0.5131  1465 ASN B N   
23487 C CA  . ASN C 1465 ? 3.0666 1.7129 2.8856 -0.5511 -1.2257 0.5401  1465 ASN B CA  
23488 C C   . ASN C 1465 ? 3.0992 1.7312 2.9565 -0.5716 -1.2383 0.5504  1465 ASN B C   
23489 O O   . ASN C 1465 ? 3.0581 1.6831 2.9155 -0.5762 -1.2244 0.5655  1465 ASN B O   
23490 C CB  . ASN C 1465 ? 3.0953 1.7832 2.9285 -0.5533 -1.2159 0.5607  1465 ASN B CB  
23491 C CG  . ASN C 1465 ? 3.0962 1.8002 2.8990 -0.5346 -1.2091 0.5497  1465 ASN B CG  
23492 O OD1 . ASN C 1465 ? 3.0343 1.7537 2.8136 -0.5236 -1.1853 0.5599  1465 ASN B OD1 
23493 N ND2 . ASN C 1465 ? 3.1379 1.8382 2.9405 -0.5306 -1.2297 0.5285  1465 ASN B ND2 
23494 N N   . SER C 1466 ? 3.1853 1.8137 3.0754 -0.5839 -1.2644 0.5427  1466 SER B N   
23495 C CA  . SER C 1466 ? 3.2455 1.8620 3.1763 -0.6047 -1.2775 0.5538  1466 SER B CA  
23496 C C   . SER C 1466 ? 3.2826 1.8762 3.2321 -0.6118 -1.3065 0.5321  1466 SER B C   
23497 O O   . SER C 1466 ? 3.2799 1.8716 3.2141 -0.6018 -1.3175 0.5096  1466 SER B O   
23498 C CB  . SER C 1466 ? 3.2997 1.9503 3.2689 -0.6206 -1.2754 0.5818  1466 SER B CB  
23499 O OG  . SER C 1466 ? 3.3640 2.0036 3.3738 -0.6411 -1.2886 0.5929  1466 SER B OG  
23500 N N   . ILE C 1467 ? 2.8827 1.4582 2.8648 -0.6287 -1.3185 0.5388  1467 ILE B N   
23501 C CA  . ILE C 1467 ? 2.9666 1.5224 2.9743 -0.6388 -1.3465 0.5212  1467 ILE B CA  
23502 C C   . ILE C 1467 ? 3.0447 1.6083 3.1036 -0.6626 -1.3565 0.5426  1467 ILE B C   
23503 O O   . ILE C 1467 ? 3.0984 1.6342 3.1775 -0.6736 -1.3678 0.5414  1467 ILE B O   
23504 C CB  . ILE C 1467 ? 2.9039 1.4156 2.8941 -0.6333 -1.3530 0.5009  1467 ILE B CB  
23505 C CG1 . ILE C 1467 ? 2.7995 1.3015 2.7366 -0.6099 -1.3388 0.4831  1467 ILE B CG1 
23506 C CG2 . ILE C 1467 ? 2.9869 1.4793 3.0007 -0.6419 -1.3822 0.4795  1467 ILE B CG2 
23507 C CD1 . ILE C 1467 ? 2.7708 1.2318 2.6908 -0.6033 -1.3490 0.4579  1467 ILE B CD1 
23508 N N   . PRO C 1468 ? 2.6258 1.2273 2.7062 -0.6704 -1.3519 0.5627  1468 PRO B N   
23509 C CA  . PRO C 1468 ? 2.6477 1.2627 2.7762 -0.6929 -1.3575 0.5872  1468 PRO B CA  
23510 C C   . PRO C 1468 ? 2.7111 1.3004 2.8774 -0.7107 -1.3826 0.5801  1468 PRO B C   
23511 O O   . PRO C 1468 ? 2.7067 1.2749 2.8700 -0.7080 -1.4014 0.5538  1468 PRO B O   
23512 C CB  . PRO C 1468 ? 2.6709 1.3294 2.8130 -0.6950 -1.3571 0.5964  1468 PRO B CB  
23513 C CG  . PRO C 1468 ? 2.6191 1.2905 2.7143 -0.6724 -1.3362 0.5918  1468 PRO B CG  
23514 C CD  . PRO C 1468 ? 2.5985 1.2337 2.6569 -0.6571 -1.3393 0.5642  1468 PRO B CD  
23515 N N   . SER C 1469 ? 2.7488 1.3397 2.9503 -0.7288 -1.3819 0.6042  1469 SER B N   
23516 C CA  . SER C 1469 ? 2.8184 1.3783 3.0508 -0.7441 -1.4005 0.6006  1469 SER B CA  
23517 C C   . SER C 1469 ? 2.9066 1.4852 3.1892 -0.7656 -1.4168 0.6116  1469 SER B C   
23518 O O   . SER C 1469 ? 2.9794 1.5376 3.2956 -0.7821 -1.4309 0.6150  1469 SER B O   
23519 C CB  . SER C 1469 ? 2.7886 1.3296 3.0214 -0.7479 -1.3871 0.6193  1469 SER B CB  
23520 O OG  . SER C 1469 ? 2.7262 1.2575 2.9123 -0.7283 -1.3677 0.6137  1469 SER B OG  
23521 N N   . SER C 1470 ? 3.6477 2.2656 3.9362 -0.7657 -1.4144 0.6181  1470 SER B N   
23522 C CA  . SER C 1470 ? 3.7108 2.3491 4.0453 -0.7851 -1.4318 0.6245  1470 SER B CA  
23523 C C   . SER C 1470 ? 3.7326 2.3500 4.0770 -0.7880 -1.4589 0.5943  1470 SER B C   
23524 O O   . SER C 1470 ? 3.8055 2.4156 4.1912 -0.8073 -1.4778 0.5949  1470 SER B O   
23525 C CB  . SER C 1470 ? 3.7267 2.4124 4.0596 -0.7811 -1.4224 0.6353  1470 SER B CB  
23526 O OG  . SER C 1470 ? 3.7113 2.4014 3.9969 -0.7575 -1.4116 0.6193  1470 SER B OG  
23527 N N   . ASP C 1471 ? 3.2719 1.8795 3.5773 -0.7686 -1.4602 0.5679  1471 ASP B N   
23528 C CA  . ASP C 1471 ? 3.3102 1.8964 3.6158 -0.7675 -1.4838 0.5360  1471 ASP B CA  
23529 C C   . ASP C 1471 ? 3.1788 1.7426 3.4327 -0.7439 -1.4762 0.5134  1471 ASP B C   
23530 O O   . ASP C 1471 ? 3.0831 1.6470 3.3061 -0.7311 -1.4536 0.5239  1471 ASP B O   
23531 C CB  . ASP C 1471 ? 3.4423 2.0619 3.7640 -0.7713 -1.4979 0.5278  1471 ASP B CB  
23532 C CG  . ASP C 1471 ? 3.4750 2.1300 3.7646 -0.7535 -1.4815 0.5309  1471 ASP B CG  
23533 O OD1 . ASP C 1471 ? 3.5413 2.2338 3.8502 -0.7592 -1.4854 0.5385  1471 ASP B OD1 
23534 O OD2 . ASP C 1471 ? 3.4198 2.0657 3.6655 -0.7338 -1.4646 0.5258  1471 ASP B OD2 
23535 N N   . PHE C 1472 ? 2.9973 1.5423 3.2414 -0.7381 -1.4944 0.4824  1472 PHE B N   
23536 C CA  . PHE C 1472 ? 2.8897 1.4151 3.0841 -0.7154 -1.4876 0.4600  1472 PHE B CA  
23537 C C   . PHE C 1472 ? 2.8315 1.3896 2.9924 -0.6976 -1.4728 0.4600  1472 PHE B C   
23538 O O   . PHE C 1472 ? 2.8290 1.4245 3.0041 -0.7022 -1.4665 0.4784  1472 PHE B O   
23539 C CB  . PHE C 1472 ? 2.9291 1.4281 3.1212 -0.7135 -1.5110 0.4261  1472 PHE B CB  
23540 C CG  . PHE C 1472 ? 2.9412 1.3989 3.1534 -0.7246 -1.5232 0.4200  1472 PHE B CG  
23541 C CD1 . PHE C 1472 ? 2.9982 1.4537 3.2588 -0.7478 -1.5325 0.4372  1472 PHE B CD1 
23542 C CD2 . PHE C 1472 ? 2.9255 1.3464 3.1091 -0.7120 -1.5259 0.3963  1472 PHE B CD2 
23543 C CE1 . PHE C 1472 ? 3.0263 1.4426 3.3062 -0.7578 -1.5439 0.4317  1472 PHE B CE1 
23544 C CE2 . PHE C 1472 ? 2.9527 1.3350 3.1552 -0.7217 -1.5374 0.3901  1472 PHE B CE2 
23545 C CZ  . PHE C 1472 ? 3.0034 1.3829 3.2542 -0.7445 -1.5464 0.4080  1472 PHE B CZ  
23546 N N   . LEU C 1473 ? 3.6547 2.1976 3.7710 -0.6770 -1.4674 0.4388  1473 LEU B N   
23547 C CA  . LEU C 1473 ? 3.6376 2.2061 3.7186 -0.6582 -1.4560 0.4333  1473 LEU B CA  
23548 C C   . LEU C 1473 ? 3.6816 2.2270 3.7312 -0.6432 -1.4670 0.3992  1473 LEU B C   
23549 O O   . LEU C 1473 ? 3.6541 2.1665 3.6788 -0.6344 -1.4617 0.3883  1473 LEU B O   
23550 C CB  . LEU C 1473 ? 3.5183 2.0939 3.5694 -0.6462 -1.4261 0.4524  1473 LEU B CB  
23551 C CG  . LEU C 1473 ? 3.4869 2.0820 3.4946 -0.6240 -1.4105 0.4462  1473 LEU B CG  
23552 C CD1 . LEU C 1473 ? 3.4527 2.0789 3.4579 -0.6224 -1.3863 0.4751  1473 LEU B CD1 
23553 C CD2 . LEU C 1473 ? 3.4451 2.0088 3.4075 -0.6056 -1.4024 0.4263  1473 LEU B CD2 
23554 N N   . CYS C 1474 ? 3.0319 1.5950 3.0830 -0.6405 -1.4825 0.3822  1474 CYS B N   
23555 C CA  . CYS C 1474 ? 3.0274 1.5691 3.0538 -0.6286 -1.4964 0.3486  1474 CYS B CA  
23556 C C   . CYS C 1474 ? 3.0336 1.5944 3.0202 -0.6073 -1.4908 0.3343  1474 CYS B C   
23557 O O   . CYS C 1474 ? 3.0670 1.6650 3.0587 -0.6059 -1.4897 0.3422  1474 CYS B O   
23558 C CB  . CYS C 1474 ? 3.0670 1.5984 3.1299 -0.6450 -1.5260 0.3318  1474 CYS B CB  
23559 S SG  . CYS C 1474 ? 3.2235 1.7067 3.3097 -0.6596 -1.5349 0.3295  1474 CYS B SG  
23560 N N   . VAL C 1475 ? 3.3468 1.8809 3.2941 -0.5907 -1.4874 0.3130  1475 VAL B N   
23561 C CA  . VAL C 1475 ? 3.3674 1.9117 3.2738 -0.5695 -1.4839 0.2949  1475 VAL B CA  
23562 C C   . VAL C 1475 ? 3.4736 2.0112 3.3871 -0.5712 -1.5113 0.2651  1475 VAL B C   
23563 O O   . VAL C 1475 ? 3.5073 2.0253 3.4521 -0.5871 -1.5305 0.2568  1475 VAL B O   
23564 C CB  . VAL C 1475 ? 3.2743 1.7908 3.1352 -0.5516 -1.4662 0.2868  1475 VAL B CB  
23565 C CG1 . VAL C 1475 ? 3.2795 1.7529 3.1481 -0.5585 -1.4772 0.2728  1475 VAL B CG1 
23566 C CG2 . VAL C 1475 ? 3.2626 1.7858 3.0800 -0.5295 -1.4633 0.2662  1475 VAL B CG2 
23567 N N   . ARG C 1476 ? 3.1413 1.6955 3.0263 -0.5551 -1.5132 0.2490  1476 ARG B N   
23568 C CA  . ARG C 1476 ? 3.1758 1.7207 3.0584 -0.5531 -1.5371 0.2176  1476 ARG B CA  
23569 C C   . ARG C 1476 ? 3.1099 1.6642 2.9457 -0.5294 -1.5312 0.2005  1476 ARG B C   
23570 O O   . ARG C 1476 ? 3.0528 1.6382 2.8730 -0.5189 -1.5174 0.2132  1476 ARG B O   
23571 C CB  . ARG C 1476 ? 3.2850 1.8531 3.2119 -0.5711 -1.5605 0.2164  1476 ARG B CB  
23572 C CG  . ARG C 1476 ? 3.3492 1.9601 3.2948 -0.5763 -1.5521 0.2428  1476 ARG B CG  
23573 C CD  . ARG C 1476 ? 3.4227 2.0321 3.4108 -0.5979 -1.5499 0.2683  1476 ARG B CD  
23574 N NE  . ARG C 1476 ? 3.4668 2.1096 3.4589 -0.5974 -1.5303 0.2984  1476 ARG B NE  
23575 C CZ  . ARG C 1476 ? 3.5323 2.1896 3.5646 -0.6162 -1.5295 0.3230  1476 ARG B CZ  
23576 N NH1 . ARG C 1476 ? 3.5889 2.2298 3.6615 -0.6372 -1.5473 0.3214  1476 ARG B NH1 
23577 N NH2 . ARG C 1476 ? 3.5064 2.1947 3.5387 -0.6138 -1.5106 0.3490  1476 ARG B NH2 
23578 N N   . PHE C 1477 ? 3.5430 2.0695 3.3571 -0.5210 -1.5418 0.1717  1477 PHE B N   
23579 C CA  . PHE C 1477 ? 3.5228 2.0526 3.2910 -0.4984 -1.5377 0.1523  1477 PHE B CA  
23580 C C   . PHE C 1477 ? 3.5763 2.0831 3.3399 -0.4972 -1.5608 0.1179  1477 PHE B C   
23581 O O   . PHE C 1477 ? 3.6033 2.0821 3.3906 -0.5107 -1.5743 0.1094  1477 PHE B O   
23582 C CB  . PHE C 1477 ? 3.4243 1.9393 3.1500 -0.4810 -1.5099 0.1597  1477 PHE B CB  
23583 C CG  . PHE C 1477 ? 3.4040 1.8757 3.1233 -0.4828 -1.5075 0.1517  1477 PHE B CG  
23584 C CD1 . PHE C 1477 ? 3.4000 1.8469 3.0789 -0.4660 -1.5042 0.1290  1477 PHE B CD1 
23585 C CD2 . PHE C 1477 ? 3.3880 1.8445 3.1414 -0.5008 -1.5083 0.1673  1477 PHE B CD2 
23586 C CE1 . PHE C 1477 ? 3.3793 1.7876 3.0526 -0.4670 -1.5019 0.1218  1477 PHE B CE1 
23587 C CE2 . PHE C 1477 ? 3.3752 1.7928 3.1228 -0.5017 -1.5061 0.1604  1477 PHE B CE2 
23588 C CZ  . PHE C 1477 ? 3.3648 1.7585 3.0723 -0.4846 -1.5029 0.1375  1477 PHE B CZ  
23589 N N   . ARG C 1478 ? 2.6937 1.2122 2.4266 -0.4809 -1.5652 0.0983  1478 ARG B N   
23590 C CA  . ARG C 1478 ? 2.7406 1.2441 2.4714 -0.4804 -1.5888 0.0655  1478 ARG B CA  
23591 C C   . ARG C 1478 ? 2.7143 1.1886 2.3983 -0.4612 -1.5800 0.0456  1478 ARG B C   
23592 O O   . ARG C 1478 ? 2.5979 1.0711 2.2480 -0.4461 -1.5558 0.0567  1478 ARG B O   
23593 C CB  . ARG C 1478 ? 2.7945 1.3359 2.5300 -0.4782 -1.6033 0.0575  1478 ARG B CB  
23594 C CG  . ARG C 1478 ? 2.8133 1.3906 2.5846 -0.4917 -1.6010 0.0857  1478 ARG B CG  
23595 C CD  . ARG C 1478 ? 2.9019 1.5221 2.6794 -0.4895 -1.6130 0.0823  1478 ARG B CD  
23596 N NE  . ARG C 1478 ? 2.8767 1.5232 2.6174 -0.4685 -1.5943 0.0914  1478 ARG B NE  
23597 C CZ  . ARG C 1478 ? 2.9056 1.5946 2.6533 -0.4660 -1.5969 0.1001  1478 ARG B CZ  
23598 N NH1 . ARG C 1478 ? 2.9788 1.6901 2.7693 -0.4839 -1.6173 0.1009  1478 ARG B NH1 
23599 N NH2 . ARG C 1478 ? 2.8694 1.5790 2.5818 -0.4457 -1.5788 0.1082  1478 ARG B NH2 
23600 N N   . ILE C 1479 ? 3.0341 1.4841 2.7170 -0.4621 -1.5992 0.0163  1479 ILE B N   
23601 C CA  . ILE C 1479 ? 3.0938 1.5120 2.7362 -0.4459 -1.5921 -0.0033 1479 ILE B CA  
23602 C C   . ILE C 1479 ? 3.2193 1.6290 2.8467 -0.4387 -1.6129 -0.0394 1479 ILE B C   
23603 O O   . ILE C 1479 ? 3.3016 1.7098 2.9596 -0.4525 -1.6373 -0.0543 1479 ILE B O   
23604 C CB  . ILE C 1479 ? 3.0786 1.4578 2.7305 -0.4538 -1.5850 0.0026  1479 ILE B CB  
23605 C CG1 . ILE C 1479 ? 3.1403 1.5061 2.8428 -0.4774 -1.6066 0.0006  1479 ILE B CG1 
23606 C CG2 . ILE C 1479 ? 3.0349 1.4208 2.6826 -0.4527 -1.5583 0.0348  1479 ILE B CG2 
23607 C CD1 . ILE C 1479 ? 3.1089 1.4362 2.8219 -0.4849 -1.6020 0.0048  1479 ILE B CD1 
23608 N N   . PHE C 1480 ? 3.8862 2.2903 3.4657 -0.4171 -1.6022 -0.0532 1480 PHE B N   
23609 C CA  . PHE C 1480 ? 4.0547 2.4542 3.6127 -0.4069 -1.6185 -0.0864 1480 PHE B CA  
23610 C C   . PHE C 1480 ? 3.9703 2.3332 3.4934 -0.3937 -1.6110 -0.1048 1480 PHE B C   
23611 O O   . PHE C 1480 ? 3.9182 2.2807 3.4002 -0.3754 -1.5903 -0.1012 1480 PHE B O   
23612 C CB  . PHE C 1480 ? 4.3050 2.7413 3.8356 -0.3910 -1.6147 -0.0874 1480 PHE B CB  
23613 C CG  . PHE C 1480 ? 4.3608 2.8168 3.8728 -0.3811 -1.5874 -0.0586 1480 PHE B CG  
23614 C CD1 . PHE C 1480 ? 4.3022 2.7371 3.7834 -0.3696 -1.5630 -0.0503 1480 PHE B CD1 
23615 C CD2 . PHE C 1480 ? 4.4051 2.9016 3.9307 -0.3833 -1.5861 -0.0403 1480 PHE B CD2 
23616 C CE1 . PHE C 1480 ? 4.2347 2.6875 3.6993 -0.3609 -1.5378 -0.0247 1480 PHE B CE1 
23617 C CE2 . PHE C 1480 ? 4.3305 2.8450 3.8397 -0.3740 -1.5610 -0.0144 1480 PHE B CE2 
23618 C CZ  . PHE C 1480 ? 4.2503 2.7424 3.7287 -0.3629 -1.5367 -0.0068 1480 PHE B CZ  
23619 N N   . GLU C 1481 ? 3.2974 1.6297 2.8369 -0.4028 -1.6281 -0.1251 1481 GLU B N   
23620 C CA  . GLU C 1481 ? 3.2718 1.5681 2.7817 -0.3914 -1.6225 -0.1434 1481 GLU B CA  
23621 C C   . GLU C 1481 ? 3.2559 1.5627 2.7142 -0.3676 -1.6117 -0.1557 1481 GLU B C   
23622 O O   . GLU C 1481 ? 3.3218 1.6465 2.7711 -0.3619 -1.6259 -0.1740 1481 GLU B O   
23623 C CB  . GLU C 1481 ? 3.3445 1.6145 2.8743 -0.4010 -1.6480 -0.1721 1481 GLU B CB  
23624 C CG  . GLU C 1481 ? 3.7713 2.0278 3.3534 -0.4250 -1.6600 -0.1618 1481 GLU B CG  
23625 C CD  . GLU C 1481 ? 3.8339 2.0603 3.4345 -0.4337 -1.6834 -0.1905 1481 GLU B CD  
23626 O OE1 . GLU C 1481 ? 3.8610 2.0671 3.4314 -0.4204 -1.6859 -0.2164 1481 GLU B OE1 
23627 O OE2 . GLU C 1481 ? 3.8552 2.0779 3.5013 -0.4543 -1.6991 -0.1867 1481 GLU B OE2 
23628 N N   . LEU C 1482 ? 3.2002 1.4969 2.6250 -0.3539 -1.5866 -0.1451 1482 LEU B N   
23629 C CA  . LEU C 1482 ? 3.1646 1.4676 2.5385 -0.3308 -1.5738 -0.1558 1482 LEU B CA  
23630 C C   . LEU C 1482 ? 3.1660 1.4417 2.5190 -0.3225 -1.5854 -0.1896 1482 LEU B C   
23631 O O   . LEU C 1482 ? 3.1869 1.4683 2.5006 -0.3046 -1.5817 -0.2052 1482 LEU B O   
23632 C CB  . LEU C 1482 ? 3.0992 1.3991 2.4460 -0.3203 -1.5426 -0.1333 1482 LEU B CB  
23633 C CG  . LEU C 1482 ? 3.1021 1.3997 2.3944 -0.2967 -1.5227 -0.1401 1482 LEU B CG  
23634 C CD1 . LEU C 1482 ? 3.0256 1.3360 2.3019 -0.2901 -1.4932 -0.1105 1482 LEU B CD1 
23635 C CD2 . LEU C 1482 ? 3.1104 1.3702 2.3816 -0.2900 -1.5218 -0.1617 1482 LEU B CD2 
23636 N N   . PHE C 1483 ? 3.3102 1.5561 2.6893 -0.3354 -1.5991 -0.2007 1483 PHE B N   
23637 C CA  . PHE C 1483 ? 3.3445 1.5665 2.7114 -0.3302 -1.6150 -0.2351 1483 PHE B CA  
23638 C C   . PHE C 1483 ? 3.4120 1.6027 2.8158 -0.3471 -1.6330 -0.2463 1483 PHE B C   
23639 O O   . PHE C 1483 ? 3.4062 1.5942 2.8500 -0.3651 -1.6363 -0.2280 1483 PHE B O   
23640 C CB  . PHE C 1483 ? 3.2661 1.4725 2.5820 -0.3087 -1.5977 -0.2467 1483 PHE B CB  
23641 C CG  . PHE C 1483 ? 3.1550 1.3390 2.4630 -0.3072 -1.5753 -0.2292 1483 PHE B CG  
23642 C CD1 . PHE C 1483 ? 3.1142 1.2858 2.4605 -0.3248 -1.5752 -0.2102 1483 PHE B CD1 
23643 C CD2 . PHE C 1483 ? 3.1005 1.2763 2.3631 -0.2884 -1.5543 -0.2317 1483 PHE B CD2 
23644 C CE1 . PHE C 1483 ? 3.0081 1.1605 2.3473 -0.3234 -1.5547 -0.1939 1483 PHE B CE1 
23645 C CE2 . PHE C 1483 ? 3.0082 1.1647 2.2639 -0.2874 -1.5339 -0.2162 1483 PHE B CE2 
23646 C CZ  . PHE C 1483 ? 2.9618 1.1069 2.2558 -0.3048 -1.5342 -0.1973 1483 PHE B CZ  
23647 N N   . GLU C 1484 ? 3.9866 2.1534 3.3758 -0.3407 -1.6444 -0.2770 1484 GLU B N   
23648 C CA  . GLU C 1484 ? 4.0864 2.2273 3.5097 -0.3556 -1.6664 -0.2942 1484 GLU B CA  
23649 C C   . GLU C 1484 ? 4.0373 2.1418 3.4670 -0.3589 -1.6560 -0.2868 1484 GLU B C   
23650 O O   . GLU C 1484 ? 4.0343 2.1184 3.4309 -0.3445 -1.6444 -0.2971 1484 GLU B O   
23651 C CB  . GLU C 1484 ? 4.2553 2.3901 3.6620 -0.3475 -1.6853 -0.3322 1484 GLU B CB  
23652 C CG  . GLU C 1484 ? 4.3971 2.5687 3.8056 -0.3476 -1.7012 -0.3420 1484 GLU B CG  
23653 C CD  . GLU C 1484 ? 4.4408 2.6405 3.8032 -0.3268 -1.6866 -0.3401 1484 GLU B CD  
23654 O OE1 . GLU C 1484 ? 4.4038 2.5956 3.7329 -0.3127 -1.6631 -0.3298 1484 GLU B OE1 
23655 O OE2 . GLU C 1484 ? 4.4978 2.7278 3.8576 -0.3245 -1.6987 -0.3487 1484 GLU B OE2 
23656 N N   . VAL C 1485 ? 3.5214 1.6191 2.9944 -0.3781 -1.6601 -0.2682 1485 VAL B N   
23657 C CA  . VAL C 1485 ? 3.4305 1.4983 2.9131 -0.3826 -1.6486 -0.2547 1485 VAL B CA  
23658 C C   . VAL C 1485 ? 3.4515 1.4877 2.9698 -0.3970 -1.6689 -0.2696 1485 VAL B C   
23659 O O   . VAL C 1485 ? 3.4731 1.5159 3.0315 -0.4146 -1.6867 -0.2681 1485 VAL B O   
23660 C CB  . VAL C 1485 ? 3.5962 1.6805 3.0991 -0.3926 -1.6335 -0.2170 1485 VAL B CB  
23661 C CG1 . VAL C 1485 ? 3.5229 1.6253 2.9851 -0.3759 -1.6069 -0.2013 1485 VAL B CG1 
23662 C CG2 . VAL C 1485 ? 3.6383 1.7512 3.1780 -0.4086 -1.6486 -0.2077 1485 VAL B CG2 
23663 N N   . GLY C 1486 ? 3.6530 1.6549 3.1570 -0.3897 -1.6656 -0.2836 1486 GLY B N   
23664 C CA  . GLY C 1486 ? 3.6925 1.6609 3.2256 -0.4005 -1.6842 -0.3010 1486 GLY B CA  
23665 C C   . GLY C 1486 ? 3.6547 1.6147 3.2365 -0.4217 -1.6878 -0.2773 1486 GLY B C   
23666 O O   . GLY C 1486 ? 3.6632 1.6493 3.2637 -0.4315 -1.6835 -0.2520 1486 GLY B O   
23667 N N   . PHE C 1487 ? 3.9953 1.9193 3.5985 -0.4289 -1.6961 -0.2853 1487 PHE B N   
23668 C CA  . PHE C 1487 ? 3.9811 1.8937 3.6265 -0.4471 -1.6958 -0.2603 1487 PHE B CA  
23669 C C   . PHE C 1487 ? 3.8507 1.7781 3.4805 -0.4420 -1.6691 -0.2275 1487 PHE B C   
23670 O O   . PHE C 1487 ? 3.7917 1.7050 3.3909 -0.4280 -1.6523 -0.2268 1487 PHE B O   
23671 C CB  . PHE C 1487 ? 4.0556 1.9244 3.7143 -0.4495 -1.7021 -0.2724 1487 PHE B CB  
23672 C CG  . PHE C 1487 ? 4.1414 1.9905 3.7713 -0.4347 -1.7101 -0.3090 1487 PHE B CG  
23673 C CD1 . PHE C 1487 ? 4.2340 2.0573 3.8870 -0.4422 -1.7326 -0.3351 1487 PHE B CD1 
23674 C CD2 . PHE C 1487 ? 4.1214 1.9778 3.7010 -0.4133 -1.6947 -0.3176 1487 PHE B CD2 
23675 C CE1 . PHE C 1487 ? 4.2877 2.0936 3.9139 -0.4284 -1.7397 -0.3693 1487 PHE B CE1 
23676 C CE2 . PHE C 1487 ? 4.1757 2.0152 3.7285 -0.3996 -1.7017 -0.3510 1487 PHE B CE2 
23677 C CZ  . PHE C 1487 ? 4.2569 2.0714 3.8328 -0.4070 -1.7243 -0.3770 1487 PHE B CZ  
23678 N N   . LEU C 1488 ? 3.6923 1.6487 3.3422 -0.4529 -1.6648 -0.2009 1488 LEU B N   
23679 C CA  . LEU C 1488 ? 3.5926 1.5651 3.2284 -0.4486 -1.6392 -0.1694 1488 LEU B CA  
23680 C C   . LEU C 1488 ? 3.5706 1.5280 3.2378 -0.4622 -1.6319 -0.1420 1488 LEU B C   
23681 O O   . LEU C 1488 ? 3.6203 1.5712 3.3318 -0.4809 -1.6470 -0.1362 1488 LEU B O   
23682 C CB  . LEU C 1488 ? 3.5601 1.5758 3.1915 -0.4488 -1.6335 -0.1540 1488 LEU B CB  
23683 C CG  . LEU C 1488 ? 3.5634 1.6043 3.2363 -0.4680 -1.6402 -0.1311 1488 LEU B CG  
23684 C CD1 . LEU C 1488 ? 3.5378 1.5666 3.2468 -0.4842 -1.6349 -0.1034 1488 LEU B CD1 
23685 C CD2 . LEU C 1488 ? 3.5222 1.6027 3.1731 -0.4598 -1.6253 -0.1152 1488 LEU B CD2 
23686 N N   . SER C 1489 ? 3.0263 0.9789 2.6705 -0.4528 -1.6087 -0.1253 1489 SER B N   
23687 C CA  . SER C 1489 ? 2.9426 0.8872 2.6119 -0.4640 -1.5980 -0.0953 1489 SER B CA  
23688 C C   . SER C 1489 ? 2.8672 0.8482 2.5453 -0.4709 -1.5858 -0.0647 1489 SER B C   
23689 O O   . SER C 1489 ? 2.8453 0.8499 2.4900 -0.4581 -1.5698 -0.0598 1489 SER B O   
23690 C CB  . SER C 1489 ? 2.8382 0.7614 2.4796 -0.4512 -1.5793 -0.0926 1489 SER B CB  
23691 O OG  . SER C 1489 ? 2.7577 0.7036 2.3644 -0.4390 -1.5554 -0.0778 1489 SER B OG  
23692 N N   . PRO C 1490 ? 3.3777 1.3631 3.1011 -0.4910 -1.5933 -0.0443 1490 PRO B N   
23693 C CA  . PRO C 1490 ? 3.3216 1.3431 3.0616 -0.5005 -1.5871 -0.0178 1490 PRO B CA  
23694 C C   . PRO C 1490 ? 3.2674 1.3083 2.9759 -0.4890 -1.5593 0.0038  1490 PRO B C   
23695 O O   . PRO C 1490 ? 3.1983 1.2220 2.8796 -0.4772 -1.5445 0.0027  1490 PRO B O   
23696 C CB  . PRO C 1490 ? 3.3288 1.3398 3.1183 -0.5220 -1.5941 0.0029  1490 PRO B CB  
23697 C CG  . PRO C 1490 ? 3.3980 1.3718 3.2037 -0.5263 -1.6127 -0.0198 1490 PRO B CG  
23698 C CD  . PRO C 1490 ? 3.3838 1.3381 3.1454 -0.5055 -1.6062 -0.0434 1490 PRO B CD  
23699 N N   . ALA C 1491 ? 3.3779 1.4548 3.0899 -0.4922 -1.5521 0.0224  1491 ALA B N   
23700 C CA  . ALA C 1491 ? 3.3157 1.4113 3.0040 -0.4839 -1.5253 0.0462  1491 ALA B CA  
23701 C C   . ALA C 1491 ? 3.3380 1.4385 3.0614 -0.5006 -1.5185 0.0788  1491 ALA B C   
23702 O O   . ALA C 1491 ? 3.3470 1.4296 3.1080 -0.5161 -1.5327 0.0814  1491 ALA B O   
23703 C CB  . ALA C 1491 ? 3.2785 1.4103 2.9452 -0.4750 -1.5187 0.0475  1491 ALA B CB  
23704 N N   . THR C 1492 ? 3.0442 1.1690 2.7555 -0.4974 -1.4967 0.1036  1492 THR B N   
23705 C CA  . THR C 1492 ? 3.0045 1.1317 2.7420 -0.5104 -1.4863 0.1346  1492 THR B CA  
23706 C C   . THR C 1492 ? 3.0168 1.1830 2.7628 -0.5157 -1.4748 0.1607  1492 THR B C   
23707 O O   . THR C 1492 ? 2.9844 1.1706 2.6978 -0.5024 -1.4570 0.1652  1492 THR B O   
23708 C CB  . THR C 1492 ? 2.8917 0.9998 2.6033 -0.5004 -1.4664 0.1406  1492 THR B CB  
23709 O OG1 . THR C 1492 ? 2.7011 0.8229 2.3660 -0.4815 -1.4469 0.1368  1492 THR B OG1 
23710 C CG2 . THR C 1492 ? 2.7778 0.8464 2.4881 -0.4975 -1.4790 0.1173  1492 THR B CG2 
23711 N N   . PHE C 1493 ? 3.0524 1.2292 2.8427 -0.5350 -1.4851 0.1777  1493 PHE B N   
23712 C CA  . PHE C 1493 ? 2.9991 1.2122 2.8003 -0.5410 -1.4734 0.2047  1493 PHE B CA  
23713 C C   . PHE C 1493 ? 2.9965 1.2064 2.8076 -0.5476 -1.4561 0.2330  1493 PHE B C   
23714 O O   . PHE C 1493 ? 3.0231 1.2169 2.8694 -0.5630 -1.4653 0.2423  1493 PHE B O   
23715 C CB  . PHE C 1493 ? 2.9777 1.2080 2.8220 -0.5587 -1.4933 0.2085  1493 PHE B CB  
23716 C CG  . PHE C 1493 ? 2.8913 1.1577 2.7545 -0.5680 -1.4824 0.2391  1493 PHE B CG  
23717 C CD1 . PHE C 1493 ? 2.8098 1.1040 2.6429 -0.5552 -1.4614 0.2500  1493 PHE B CD1 
23718 C CD2 . PHE C 1493 ? 2.9127 1.1855 2.8248 -0.5897 -1.4934 0.2566  1493 PHE B CD2 
23719 C CE1 . PHE C 1493 ? 2.7965 1.1243 2.6478 -0.5636 -1.4513 0.2778  1493 PHE B CE1 
23720 C CE2 . PHE C 1493 ? 2.8847 1.1916 2.8153 -0.5985 -1.4838 0.2843  1493 PHE B CE2 
23721 C CZ  . PHE C 1493 ? 2.8342 1.1688 2.7343 -0.5853 -1.4627 0.2949  1493 PHE B CZ  
23722 N N   . THR C 1494 ? 2.6193 0.8445 2.3992 -0.5359 -1.4311 0.2463  1494 THR B N   
23723 C CA  . THR C 1494 ? 2.5639 0.7910 2.3486 -0.5406 -1.4117 0.2743  1494 THR B CA  
23724 C C   . THR C 1494 ? 2.4879 0.7543 2.2758 -0.5434 -1.3955 0.3006  1494 THR B C   
23725 O O   . THR C 1494 ? 2.4716 0.7609 2.2374 -0.5329 -1.3895 0.2957  1494 THR B O   
23726 C CB  . THR C 1494 ? 2.4844 0.6885 2.2308 -0.5253 -1.3954 0.2667  1494 THR B CB  
23727 O OG1 . THR C 1494 ? 2.4274 0.6357 2.1780 -0.5300 -1.3766 0.2937  1494 THR B OG1 
23728 C CG2 . THR C 1494 ? 2.4411 0.6543 2.1398 -0.5048 -1.3831 0.2510  1494 THR B CG2 
23729 N N   . VAL C 1495 ? 2.7639 1.0386 2.5810 -0.5579 -1.3892 0.3287  1495 VAL B N   
23730 C CA  . VAL C 1495 ? 2.8147 1.1262 2.6378 -0.5617 -1.3735 0.3551  1495 VAL B CA  
23731 C C   . VAL C 1495 ? 2.8117 1.1250 2.6374 -0.5662 -1.3530 0.3825  1495 VAL B C   
23732 O O   . VAL C 1495 ? 2.8831 1.1862 2.7423 -0.5816 -1.3592 0.3971  1495 VAL B O   
23733 C CB  . VAL C 1495 ? 2.6703 1.0041 2.5365 -0.5788 -1.3900 0.3648  1495 VAL B CB  
23734 C CG1 . VAL C 1495 ? 2.8175 1.1364 2.7284 -0.5991 -1.4018 0.3786  1495 VAL B CG1 
23735 C CG2 . VAL C 1495 ? 2.6578 1.0322 2.5231 -0.5786 -1.3738 0.3870  1495 VAL B CG2 
23736 N N   . TYR C 1496 ? 2.9922 1.3185 2.7823 -0.5527 -1.3284 0.3894  1496 TYR B N   
23737 C CA  . TYR C 1496 ? 2.9307 1.2620 2.7183 -0.5552 -1.3069 0.4141  1496 TYR B CA  
23738 C C   . TYR C 1496 ? 2.9027 1.2705 2.6791 -0.5517 -1.2854 0.4340  1496 TYR B C   
23739 O O   . TYR C 1496 ? 2.8895 1.2751 2.6464 -0.5413 -1.2822 0.4252  1496 TYR B O   
23740 C CB  . TYR C 1496 ? 2.8695 1.1731 2.6243 -0.5429 -1.2960 0.4031  1496 TYR B CB  
23741 C CG  . TYR C 1496 ? 2.8598 1.1612 2.5654 -0.5217 -1.2846 0.3823  1496 TYR B CG  
23742 C CD1 . TYR C 1496 ? 2.8417 1.1697 2.5298 -0.5131 -1.2768 0.3812  1496 TYR B CD1 
23743 C CD2 . TYR C 1496 ? 2.8413 1.1141 2.5179 -0.5099 -1.2809 0.3646  1496 TYR B CD2 
23744 C CE1 . TYR C 1496 ? 2.8043 1.1297 2.4474 -0.4937 -1.2657 0.3631  1496 TYR B CE1 
23745 C CE2 . TYR C 1496 ? 2.8105 1.0811 2.4421 -0.4908 -1.2698 0.3460  1496 TYR B CE2 
23746 C CZ  . TYR C 1496 ? 2.7966 1.0932 2.4117 -0.4830 -1.2622 0.3457  1496 TYR B CZ  
23747 O OH  . TYR C 1496 ? 2.7720 1.0665 2.3431 -0.4642 -1.2509 0.3283  1496 TYR B OH  
23748 N N   . GLU C 1497 ? 3.2754 1.6543 3.0646 -0.5603 -1.2706 0.4609  1497 GLU B N   
23749 C CA  . GLU C 1497 ? 3.2239 1.6373 3.0070 -0.5591 -1.2493 0.4829  1497 GLU B CA  
23750 C C   . GLU C 1497 ? 3.1559 1.5699 2.8915 -0.5412 -1.2239 0.4791  1497 GLU B C   
23751 O O   . GLU C 1497 ? 3.0922 1.4875 2.8128 -0.5379 -1.2140 0.4795  1497 GLU B O   
23752 C CB  . GLU C 1497 ? 3.1976 1.6219 3.0148 -0.5764 -1.2444 0.5130  1497 GLU B CB  
23753 C CG  . GLU C 1497 ? 3.1711 1.6340 2.9955 -0.5801 -1.2286 0.5371  1497 GLU B CG  
23754 C CD  . GLU C 1497 ? 3.1693 1.6432 3.0362 -0.6001 -1.2308 0.5649  1497 GLU B CD  
23755 O OE1 . GLU C 1497 ? 3.1469 1.5970 3.0347 -0.6101 -1.2426 0.5660  1497 GLU B OE1 
23756 O OE2 . GLU C 1497 ? 3.1870 1.6933 3.0668 -0.6059 -1.2208 0.5857  1497 GLU B OE2 
23757 N N   . TYR C 1498 ? 3.0562 1.4923 2.7690 -0.5298 -1.2131 0.4761  1498 TYR B N   
23758 C CA  . TYR C 1498 ? 3.0352 1.4683 2.7008 -0.5115 -1.1914 0.4674  1498 TYR B CA  
23759 C C   . TYR C 1498 ? 2.9741 1.4029 2.6322 -0.5135 -1.1718 0.4835  1498 TYR B C   
23760 O O   . TYR C 1498 ? 2.9277 1.3336 2.5596 -0.5046 -1.1652 0.4715  1498 TYR B O   
23761 C CB  . TYR C 1498 ? 3.0447 1.5077 2.6920 -0.5017 -1.1774 0.4714  1498 TYR B CB  
23762 C CG  . TYR C 1498 ? 3.0424 1.4980 2.6396 -0.4812 -1.1595 0.4559  1498 TYR B CG  
23763 C CD1 . TYR C 1498 ? 3.0882 1.5198 2.6618 -0.4697 -1.1700 0.4278  1498 TYR B CD1 
23764 C CD2 . TYR C 1498 ? 3.0098 1.4825 2.5835 -0.4737 -1.1321 0.4689  1498 TYR B CD2 
23765 C CE1 . TYR C 1498 ? 3.0749 1.4998 2.6034 -0.4515 -1.1538 0.4139  1498 TYR B CE1 
23766 C CE2 . TYR C 1498 ? 3.0013 1.4666 2.5300 -0.4557 -1.1158 0.4547  1498 TYR B CE2 
23767 C CZ  . TYR C 1498 ? 3.0385 1.4798 2.5449 -0.4447 -1.1267 0.4275  1498 TYR B CZ  
23768 O OH  . TYR C 1498 ? 3.0428 1.4765 2.5047 -0.4270 -1.1104 0.4135  1498 TYR B OH  
23769 N N   . HIS C 1499 ? 2.6992 1.1511 2.3810 -0.5253 -1.1628 0.5108  1499 HIS B N   
23770 C CA  . HIS C 1499 ? 2.6293 1.0827 2.3006 -0.5260 -1.1413 0.5271  1499 HIS B CA  
23771 C C   . HIS C 1499 ? 2.6839 1.1123 2.3710 -0.5350 -1.1490 0.5301  1499 HIS B C   
23772 O O   . HIS C 1499 ? 2.7062 1.1277 2.3741 -0.5308 -1.1327 0.5345  1499 HIS B O   
23773 C CB  . HIS C 1499 ? 2.5493 1.0379 2.2328 -0.5326 -1.1244 0.5544  1499 HIS B CB  
23774 C CG  . HIS C 1499 ? 2.4824 0.9913 2.1350 -0.5184 -1.1064 0.5513  1499 HIS B CG  
23775 N ND1 . HIS C 1499 ? 2.4982 1.0398 2.1646 -0.5216 -1.1016 0.5662  1499 HIS B ND1 
23776 C CD2 . HIS C 1499 ? 2.4580 0.9587 2.0668 -0.5005 -1.0923 0.5347  1499 HIS B CD2 
23777 C CE1 . HIS C 1499 ? 2.4940 1.0460 2.1263 -0.5061 -1.0850 0.5592  1499 HIS B CE1 
23778 N NE2 . HIS C 1499 ? 2.4653 0.9927 2.0623 -0.4932 -1.0790 0.5402  1499 HIS B NE2 
23779 N N   . ARG C 1500 ? 2.6603 1.0749 2.3816 -0.5469 -1.1736 0.5273  1500 ARG B N   
23780 C CA  . ARG C 1500 ? 2.6618 1.0492 2.3975 -0.5543 -1.1822 0.5282  1500 ARG B CA  
23781 C C   . ARG C 1500 ? 2.6683 1.0243 2.4111 -0.5536 -1.2074 0.5034  1500 ARG B C   
23782 O O   . ARG C 1500 ? 2.7316 1.0836 2.5113 -0.5668 -1.2285 0.5051  1500 ARG B O   
23783 C CB  . ARG C 1500 ? 2.7066 1.1060 2.4822 -0.5730 -1.1830 0.5576  1500 ARG B CB  
23784 C CG  . ARG C 1500 ? 2.7269 1.1627 2.5229 -0.5816 -1.1779 0.5781  1500 ARG B CG  
23785 C CD  . ARG C 1500 ? 2.8060 1.2432 2.6503 -0.5998 -1.2002 0.5872  1500 ARG B CD  
23786 N NE  . ARG C 1500 ? 2.8348 1.2881 2.7081 -0.6150 -1.1932 0.6177  1500 ARG B NE  
23787 C CZ  . ARG C 1500 ? 2.8846 1.3397 2.8021 -0.6329 -1.2093 0.6312  1500 ARG B CZ  
23788 N NH1 . ARG C 1500 ? 2.9117 1.3533 2.8503 -0.6383 -1.2336 0.6162  1500 ARG B NH1 
23789 N NH2 . ARG C 1500 ? 2.9107 1.3816 2.8515 -0.6456 -1.2007 0.6597  1500 ARG B NH2 
23790 N N   . PRO C 1501 ? 2.7111 1.0449 2.4180 -0.5382 -1.2045 0.4800  1501 PRO B N   
23791 C CA  . PRO C 1501 ? 2.7411 1.0431 2.4418 -0.5323 -1.2233 0.4521  1501 PRO B CA  
23792 C C   . PRO C 1501 ? 2.8182 1.0956 2.5513 -0.5450 -1.2398 0.4558  1501 PRO B C   
23793 O O   . PRO C 1501 ? 2.8329 1.0807 2.5642 -0.5416 -1.2549 0.4350  1501 PRO B O   
23794 C CB  . PRO C 1501 ? 2.6991 0.9884 2.3527 -0.5143 -1.2064 0.4370  1501 PRO B CB  
23795 C CG  . PRO C 1501 ? 2.6610 0.9798 2.2923 -0.5081 -1.1813 0.4507  1501 PRO B CG  
23796 C CD  . PRO C 1501 ? 2.6599 1.0024 2.3259 -0.5243 -1.1780 0.4809  1501 PRO B CD  
23797 N N   . ASP C 1502 ? 2.9442 1.2344 2.7076 -0.5597 -1.2364 0.4832  1502 ASP B N   
23798 C CA  . ASP C 1502 ? 3.0249 1.2941 2.8195 -0.5720 -1.2490 0.4912  1502 ASP B CA  
23799 C C   . ASP C 1502 ? 3.1284 1.3924 2.9616 -0.5849 -1.2750 0.4865  1502 ASP B C   
23800 O O   . ASP C 1502 ? 3.1937 1.4316 3.0503 -0.5925 -1.2923 0.4816  1502 ASP B O   
23801 C CB  . ASP C 1502 ? 3.0191 1.3064 2.8292 -0.5822 -1.2334 0.5237  1502 ASP B CB  
23802 C CG  . ASP C 1502 ? 2.9425 1.2500 2.7156 -0.5708 -1.2051 0.5311  1502 ASP B CG  
23803 O OD1 . ASP C 1502 ? 2.8770 1.1733 2.6109 -0.5545 -1.1966 0.5112  1502 ASP B OD1 
23804 O OD2 . ASP C 1502 ? 2.9399 1.2744 2.7237 -0.5784 -1.1911 0.5567  1502 ASP B OD2 
23805 N N   . LYS C 1503 ? 3.1385 1.4275 2.9772 -0.5868 -1.2776 0.4871  1503 LYS B N   
23806 C CA  . LYS C 1503 ? 3.2627 1.5549 3.1405 -0.6009 -1.3002 0.4867  1503 LYS B CA  
23807 C C   . LYS C 1503 ? 3.1303 1.4005 3.0049 -0.5957 -1.3224 0.4546  1503 LYS B C   
23808 O O   . LYS C 1503 ? 3.1225 1.4010 3.0218 -0.6043 -1.3397 0.4499  1503 LYS B O   
23809 C CB  . LYS C 1503 ? 3.3144 1.6462 3.2017 -0.6058 -1.2930 0.5031  1503 LYS B CB  
23810 C CG  . LYS C 1503 ? 3.3413 1.6957 3.2485 -0.6176 -1.2782 0.5371  1503 LYS B CG  
23811 C CD  . LYS C 1503 ? 3.3444 1.6811 3.2438 -0.6167 -1.2667 0.5469  1503 LYS B CD  
23812 C CE  . LYS C 1503 ? 3.4260 1.7643 3.3687 -0.6362 -1.2719 0.5734  1503 LYS B CE  
23813 N NZ  . LYS C 1503 ? 3.4580 1.7765 3.3959 -0.6358 -1.2638 0.5821  1503 LYS B NZ  
23814 N N   . GLN C 1504 ? 3.1486 1.3913 2.9936 -0.5821 -1.3222 0.4327  1504 GLN B N   
23815 C CA  . GLN C 1504 ? 3.0859 1.3095 2.9188 -0.5737 -1.3396 0.4003  1504 GLN B CA  
23816 C C   . GLN C 1504 ? 3.1574 1.3590 3.0274 -0.5866 -1.3665 0.3905  1504 GLN B C   
23817 O O   . GLN C 1504 ? 2.9199 1.0896 2.7926 -0.5862 -1.3743 0.3806  1504 GLN B O   
23818 C CB  . GLN C 1504 ? 3.0450 1.2451 2.8360 -0.5556 -1.3309 0.3801  1504 GLN B CB  
23819 C CG  . GLN C 1504 ? 3.5678 1.7811 3.3155 -0.5376 -1.3197 0.3639  1504 GLN B CG  
23820 C CD  . GLN C 1504 ? 3.2466 1.4445 2.9513 -0.5206 -1.3029 0.3528  1504 GLN B CD  
23821 O OE1 . GLN C 1504 ? 3.1533 1.3614 2.8206 -0.5056 -1.2899 0.3426  1504 GLN B OE1 
23822 N NE2 . GLN C 1504 ? 3.2666 1.4402 2.9766 -0.5229 -1.3029 0.3553  1504 GLN B NE2 
23823 N N   . CYS C 1505 ? 2.9670 1.1858 2.8651 -0.5978 -1.3806 0.3925  1505 CYS B N   
23824 C CA  . CYS C 1505 ? 3.0517 1.2507 2.9781 -0.6071 -1.4077 0.3749  1505 CYS B CA  
23825 C C   . CYS C 1505 ? 3.0779 1.2684 2.9777 -0.5933 -1.4187 0.3408  1505 CYS B C   
23826 O O   . CYS C 1505 ? 3.0168 1.2317 2.9094 -0.5898 -1.4205 0.3349  1505 CYS B O   
23827 C CB  . CYS C 1505 ? 3.1006 1.3200 3.0723 -0.6268 -1.4201 0.3909  1505 CYS B CB  
23828 S SG  . CYS C 1505 ? 3.8372 2.0257 3.8514 -0.6423 -1.4521 0.3747  1505 CYS B SG  
23829 N N   . THR C 1506 ? 2.9801 1.1360 2.8665 -0.5856 -1.4260 0.3191  1506 THR B N   
23830 C CA  . THR C 1506 ? 3.0241 1.1670 2.8812 -0.5709 -1.4348 0.2857  1506 THR B CA  
23831 C C   . THR C 1506 ? 3.1108 1.2312 2.9982 -0.5811 -1.4628 0.2666  1506 THR B C   
23832 O O   . THR C 1506 ? 3.1308 1.2312 3.0511 -0.5944 -1.4719 0.2751  1506 THR B O   
23833 C CB  . THR C 1506 ? 3.0372 1.1573 2.8548 -0.5538 -1.4211 0.2744  1506 THR B CB  
23834 O OG1 . THR C 1506 ? 3.0277 1.1696 2.8163 -0.5445 -1.3949 0.2907  1506 THR B OG1 
23835 C CG2 . THR C 1506 ? 3.0408 1.1443 2.8290 -0.5389 -1.4307 0.2394  1506 THR B CG2 
23836 N N   . MET C 1507 ? 3.1379 1.2620 3.0145 -0.5749 -1.4761 0.2411  1507 MET B N   
23837 C CA  . MET C 1507 ? 3.1682 1.2741 3.0725 -0.5845 -1.5033 0.2205  1507 MET B CA  
23838 C C   . MET C 1507 ? 3.1502 1.2487 3.0300 -0.5720 -1.5163 0.1850  1507 MET B C   
23839 O O   . MET C 1507 ? 3.0852 1.2085 2.9409 -0.5620 -1.5117 0.1782  1507 MET B O   
23840 C CB  . MET C 1507 ? 3.1838 1.3122 3.1312 -0.6039 -1.5152 0.2354  1507 MET B CB  
23841 C CG  . MET C 1507 ? 3.2586 1.3710 3.2328 -0.6136 -1.5425 0.2130  1507 MET B CG  
23842 S SD  . MET C 1507 ? 3.1550 1.3058 3.1654 -0.6306 -1.5530 0.2261  1507 MET B SD  
23843 C CE  . MET C 1507 ? 3.0366 1.2281 3.0143 -0.6182 -1.5254 0.2474  1507 MET B CE  
23844 N N   . PHE C 1508 ? 3.3691 1.4334 3.2574 -0.5732 -1.5331 0.1630  1508 PHE B N   
23845 C CA  . PHE C 1508 ? 3.4383 1.4907 3.3077 -0.5631 -1.5481 0.1276  1508 PHE B CA  
23846 C C   . PHE C 1508 ? 3.6190 1.6904 3.5135 -0.5739 -1.5683 0.1184  1508 PHE B C   
23847 O O   . PHE C 1508 ? 3.7187 1.7977 3.6556 -0.5930 -1.5770 0.1350  1508 PHE B O   
23848 C CB  . PHE C 1508 ? 3.4003 1.4097 3.2777 -0.5636 -1.5609 0.1089  1508 PHE B CB  
23849 C CG  . PHE C 1508 ? 3.2633 1.2523 3.1027 -0.5461 -1.5457 0.1017  1508 PHE B CG  
23850 C CD1 . PHE C 1508 ? 3.2278 1.2323 3.0205 -0.5273 -1.5291 0.0954  1508 PHE B CD1 
23851 C CD2 . PHE C 1508 ? 3.2377 1.1920 3.0878 -0.5482 -1.5482 0.1005  1508 PHE B CD2 
23852 C CE1 . PHE C 1508 ? 3.1863 1.1727 2.9437 -0.5115 -1.5149 0.0883  1508 PHE B CE1 
23853 C CE2 . PHE C 1508 ? 3.2035 1.1404 3.0187 -0.5320 -1.5343 0.0935  1508 PHE B CE2 
23854 C CZ  . PHE C 1508 ? 3.1722 1.1256 2.9409 -0.5138 -1.5176 0.0872  1508 PHE B CZ  
23855 N N   . TYR C 1509 ? 2.7472 0.8260 2.6164 -0.5621 -1.5760 0.0920  1509 TYR B N   
23856 C CA  . TYR C 1509 ? 2.7792 0.8735 2.6702 -0.5712 -1.5975 0.0780  1509 TYR B CA  
23857 C C   . TYR C 1509 ? 2.8445 0.9347 2.7010 -0.5547 -1.6058 0.0435  1509 TYR B C   
23858 O O   . TYR C 1509 ? 2.8250 0.9129 2.6379 -0.5356 -1.5906 0.0365  1509 TYR B O   
23859 C CB  . TYR C 1509 ? 3.2364 1.3740 3.1373 -0.5770 -1.5907 0.1005  1509 TYR B CB  
23860 C CG  . TYR C 1509 ? 3.1452 1.3080 3.0020 -0.5578 -1.5771 0.0950  1509 TYR B CG  
23861 C CD1 . TYR C 1509 ? 3.1457 1.3442 3.0054 -0.5587 -1.5818 0.0959  1509 TYR B CD1 
23862 C CD2 . TYR C 1509 ? 3.1027 1.2528 2.9145 -0.5382 -1.5600 0.0880  1509 TYR B CD2 
23863 C CE1 . TYR C 1509 ? 3.1228 1.3438 2.9415 -0.5403 -1.5693 0.0910  1509 TYR B CE1 
23864 C CE2 . TYR C 1509 ? 3.0730 1.2448 2.8438 -0.5203 -1.5473 0.0826  1509 TYR B CE2 
23865 C CZ  . TYR C 1509 ? 3.0873 1.2944 2.8614 -0.5211 -1.5519 0.0844  1509 TYR B CZ  
23866 O OH  . TYR C 1509 ? 3.0549 1.2841 2.7888 -0.5029 -1.5393 0.0799  1509 TYR B OH  
23867 N N   . SER C 1510 ? 3.6726 1.7620 3.5484 -0.5623 -1.6297 0.0218  1510 SER B N   
23868 C CA  . SER C 1510 ? 3.6897 1.7780 3.5347 -0.5477 -1.6393 -0.0116 1510 SER B CA  
23869 C C   . SER C 1510 ? 3.7548 1.8777 3.6070 -0.5510 -1.6521 -0.0190 1510 SER B C   
23870 O O   . SER C 1510 ? 3.7702 1.9069 3.6630 -0.5695 -1.6648 -0.0096 1510 SER B O   
23871 C CB  . SER C 1510 ? 3.7366 1.7848 3.5873 -0.5483 -1.6566 -0.0402 1510 SER B CB  
23872 O OG  . SER C 1510 ? 3.7297 1.7736 3.5400 -0.5297 -1.6590 -0.0702 1510 SER B OG  
23873 N N   . THR C 1511 ? 3.0617 1.1988 2.8734 -0.5327 -1.6483 -0.0360 1511 THR B N   
23874 C CA  . THR C 1511 ? 3.0980 1.2736 2.9066 -0.5312 -1.6542 -0.0386 1511 THR B CA  
23875 C C   . THR C 1511 ? 3.2912 1.4628 3.1138 -0.5366 -1.6815 -0.0694 1511 THR B C   
23876 O O   . THR C 1511 ? 3.3398 1.5386 3.1510 -0.5309 -1.6888 -0.0811 1511 THR B O   
23877 C CB  . THR C 1511 ? 2.9855 1.1792 2.7418 -0.5077 -1.6353 -0.0405 1511 THR B CB  
23878 O OG1 . THR C 1511 ? 2.9776 1.2138 2.7353 -0.5077 -1.6329 -0.0280 1511 THR B OG1 
23879 C CG2 . THR C 1511 ? 2.9943 1.1715 2.7158 -0.4915 -1.6434 -0.0758 1511 THR B CG2 
23880 N N   . SER C 1512 ? 3.6929 1.8305 3.5405 -0.5475 -1.6966 -0.0827 1512 SER B N   
23881 C CA  . SER C 1512 ? 3.8899 2.0198 3.7499 -0.5525 -1.7225 -0.1144 1512 SER B CA  
23882 C C   . SER C 1512 ? 4.0640 2.1621 3.9677 -0.5718 -1.7388 -0.1185 1512 SER B C   
23883 O O   . SER C 1512 ? 4.0428 2.1118 3.9530 -0.5742 -1.7301 -0.1074 1512 SER B O   
23884 C CB  . SER C 1512 ? 3.8891 2.0034 3.7048 -0.5319 -1.7233 -0.1456 1512 SER B CB  
23885 O OG  . SER C 1512 ? 3.8795 1.9504 3.6948 -0.5307 -1.7242 -0.1567 1512 SER B OG  
23886 N N   . ASN C 1513 ? 4.6999 2.8036 4.6333 -0.5854 -1.7625 -0.1350 1513 ASN B N   
23887 C CA  . ASN C 1513 ? 4.8861 2.9603 4.8632 -0.6048 -1.7797 -0.1408 1513 ASN B CA  
23888 C C   . ASN C 1513 ? 5.0179 3.0566 4.9820 -0.5975 -1.7932 -0.1771 1513 ASN B C   
23889 O O   . ASN C 1513 ? 5.0944 3.1019 5.0900 -0.6108 -1.8071 -0.1861 1513 ASN B O   
23890 C CB  . ASN C 1513 ? 4.9903 3.0899 5.0096 -0.6251 -1.7979 -0.1383 1513 ASN B CB  
23891 C CG  . ASN C 1513 ? 4.9836 3.1286 5.0034 -0.6262 -1.7856 -0.1102 1513 ASN B CG  
23892 O OD1 . ASN C 1513 ? 4.9173 3.0669 4.9342 -0.6250 -1.7653 -0.0801 1513 ASN B OD1 
23893 N ND2 . ASN C 1513 ? 5.0467 3.2260 5.0696 -0.6281 -1.7977 -0.1202 1513 ASN B ND2 
23894 N N   . ILE C 1514 ? 4.4371 2.4802 4.3545 -0.5761 -1.7885 -0.1974 1514 ILE B N   
23895 C CA  . ILE C 1514 ? 4.5125 2.5264 4.4129 -0.5671 -1.8011 -0.2340 1514 ILE B CA  
23896 C C   . ILE C 1514 ? 4.5150 2.4822 4.4218 -0.5677 -1.7973 -0.2348 1514 ILE B C   
23897 O O   . ILE C 1514 ? 4.4475 2.4051 4.3352 -0.5584 -1.7765 -0.2162 1514 ILE B O   
23898 C CB  . ILE C 1514 ? 4.6618 2.6897 4.5069 -0.5423 -1.7930 -0.2523 1514 ILE B CB  
23899 C CG1 . ILE C 1514 ? 4.6363 2.7125 4.4727 -0.5399 -1.7930 -0.2461 1514 ILE B CG1 
23900 C CG2 . ILE C 1514 ? 4.7434 2.7471 4.5755 -0.5354 -1.8100 -0.2926 1514 ILE B CG2 
23901 C CD1 . ILE C 1514 ? 4.6021 2.6938 4.3853 -0.5159 -1.7854 -0.2628 1514 ILE B CD1 
23902 N N   . SER D 1    ? 5.7454 4.2552 5.5843 0.0957  -0.4836 -0.3412 129  SER Y N   
23903 C CA  . SER D 1    ? 5.7194 4.3263 5.5832 0.0804  -0.4409 -0.3525 129  SER Y CA  
23904 C C   . SER D 1    ? 5.7526 4.3729 5.5458 0.0802  -0.4157 -0.3463 129  SER Y C   
23905 O O   . SER D 1    ? 5.7368 4.3882 5.5188 0.0649  -0.3833 -0.3572 129  SER Y O   
23906 C CB  . SER D 1    ? 3.2742 1.9077 3.1837 0.0601  -0.4199 -0.3724 129  SER Y CB  
23907 O OG  . SER D 1    ? 3.3040 1.8800 3.1643 0.0549  -0.4166 -0.3747 129  SER Y OG  
23908 N N   . SER D 2    ? 4.0714 2.6676 3.8187 0.0971  -0.4306 -0.3290 130  SER Y N   
23909 C CA  . SER D 2    ? 4.1090 2.7176 3.7913 0.0989  -0.4083 -0.3215 130  SER Y CA  
23910 C C   . SER D 2    ? 4.0986 2.8132 3.8120 0.0864  -0.3695 -0.3312 130  SER Y C   
23911 O O   . SER D 2    ? 4.0609 2.8355 3.8366 0.0836  -0.3672 -0.3369 130  SER Y O   
23912 C CB  . SER D 2    ? 4.1198 2.6861 3.7566 0.1202  -0.4339 -0.3011 130  SER Y CB  
23913 O OG  . SER D 2    ? 4.1268 2.6873 3.6934 0.1233  -0.4156 -0.2927 130  SER Y OG  
23914 N N   . GLU D 3    ? 3.9914 2.7272 3.6613 0.0789  -0.3391 -0.3335 131  GLU Y N   
23915 C CA  . GLU D 3    ? 3.9515 2.7851 3.6448 0.0668  -0.3022 -0.3429 131  GLU Y CA  
23916 C C   . GLU D 3    ? 3.9630 2.8103 3.5979 0.0736  -0.2865 -0.3320 131  GLU Y C   
23917 O O   . GLU D 3    ? 3.9830 2.8397 3.5857 0.0639  -0.2596 -0.3378 131  GLU Y O   
23918 C CB  . GLU D 3    ? 3.9306 2.7933 3.6441 0.0450  -0.2732 -0.3625 131  GLU Y CB  
23919 C CG  . GLU D 3    ? 3.8862 2.7638 3.6701 0.0341  -0.2782 -0.3769 131  GLU Y CG  
23920 C CD  . GLU D 3    ? 3.8618 2.7765 3.6649 0.0120  -0.2460 -0.3965 131  GLU Y CD  
23921 O OE1 . GLU D 3    ? 3.8742 2.7874 3.6317 0.0058  -0.2236 -0.3986 131  GLU Y OE1 
23922 O OE2 . GLU D 3    ? 3.8290 2.7737 3.6937 0.0005  -0.2425 -0.4102 131  GLU Y OE2 
23923 N N   . THR D 4    ? 4.2275 3.0760 3.8505 0.0902  -0.3024 -0.3167 132  THR Y N   
23924 C CA  . THR D 4    ? 4.2271 3.0870 3.7964 0.0980  -0.2889 -0.3054 132  THR Y CA  
23925 C C   . THR D 4    ? 4.1569 3.1207 3.7549 0.0886  -0.2561 -0.3133 132  THR Y C   
23926 O O   . THR D 4    ? 4.1134 3.1372 3.7689 0.0853  -0.2550 -0.3192 132  THR Y O   
23927 C CB  . THR D 4    ? 4.2589 3.0735 3.7981 0.1203  -0.3193 -0.2849 132  THR Y CB  
23928 O OG1 . THR D 4    ? 4.3075 3.0213 3.8123 0.1290  -0.3499 -0.2774 132  THR Y OG1 
23929 C CG2 . THR D 4    ? 4.2636 3.0919 3.7490 0.1279  -0.3036 -0.2734 132  THR Y CG2 
23930 N N   . ASN D 5    ? 4.1602 3.1435 3.7182 0.0839  -0.2292 -0.3139 133  ASN Y N   
23931 C CA  . ASN D 5    ? 4.0746 3.1525 3.6530 0.0765  -0.1997 -0.3201 133  ASN Y CA  
23932 C C   . ASN D 5    ? 4.0305 3.1229 3.5787 0.0927  -0.2029 -0.3032 133  ASN Y C   
23933 O O   . ASN D 5    ? 4.0861 3.1680 3.5845 0.0958  -0.1890 -0.2971 133  ASN Y O   
23934 C CB  . ASN D 5    ? 4.0607 3.1627 3.6238 0.0598  -0.1658 -0.3334 133  ASN Y CB  
23935 C CG  . ASN D 5    ? 4.0533 3.0874 3.5447 0.0655  -0.1627 -0.3244 133  ASN Y CG  
23936 O OD1 . ASN D 5    ? 4.0586 3.0069 3.5139 0.0766  -0.1877 -0.3135 133  ASN Y OD1 
23937 N ND2 . ASN D 5    ? 4.0452 3.1159 3.5155 0.0578  -0.1317 -0.3293 133  ASN Y ND2 
23938 N N   . THR D 6    ? 4.0195 3.1351 3.5991 0.1030  -0.2205 -0.2960 134  THR Y N   
23939 C CA  . THR D 6    ? 3.9481 3.0790 3.5044 0.1191  -0.2255 -0.2798 134  THR Y CA  
23940 C C   . THR D 6    ? 3.8708 3.0922 3.4372 0.1132  -0.1954 -0.2843 134  THR Y C   
23941 O O   . THR D 6    ? 3.8117 3.0967 3.4192 0.0974  -0.1750 -0.3004 134  THR Y O   
23942 C CB  . THR D 6    ? 4.2209 3.3491 3.8110 0.1318  -0.2534 -0.2713 134  THR Y CB  
23943 O OG1 . THR D 6    ? 4.2254 3.3969 3.8076 0.1432  -0.2499 -0.2598 134  THR Y OG1 
23944 C CG2 . THR D 6    ? 4.1741 3.3504 3.8351 0.1193  -0.2504 -0.2867 134  THR Y CG2 
23945 N N   . HIS D 7    ? 5.7084 4.9347 5.2376 0.1261  -0.1935 -0.2700 135  HIS Y N   
23946 C CA  . HIS D 7    ? 5.6909 4.9994 5.2262 0.1224  -0.1671 -0.2726 135  HIS Y CA  
23947 C C   . HIS D 7    ? 5.6556 5.0036 5.2063 0.1363  -0.1772 -0.2608 135  HIS Y C   
23948 O O   . HIS D 7    ? 5.6734 4.9774 5.1914 0.1537  -0.1959 -0.2435 135  HIS Y O   
23949 C CB  . HIS D 7    ? 3.7247 3.0150 3.2038 0.1236  -0.1492 -0.2678 135  HIS Y CB  
23950 C CG  . HIS D 7    ? 3.7288 2.9842 3.1908 0.1095  -0.1352 -0.2797 135  HIS Y CG  
23951 N ND1 . HIS D 7    ? 3.7094 3.0218 3.1988 0.0905  -0.1076 -0.2983 135  HIS Y ND1 
23952 C CD2 . HIS D 7    ? 3.7524 2.9199 3.1707 0.1118  -0.1449 -0.2757 135  HIS Y CD2 
23953 C CE1 . HIS D 7    ? 3.7189 2.9813 3.1841 0.0815  -0.1001 -0.3053 135  HIS Y CE1 
23954 N NE2 . HIS D 7    ? 3.7458 2.9193 3.1668 0.0943  -0.1223 -0.2917 135  HIS Y NE2 
23955 N N   . LEU D 8    ? 2.7307 2.1599 2.3295 0.1286  -0.1645 -0.2703 136  LEU Y N   
23956 C CA  . LEU D 8    ? 2.6743 2.1482 2.2885 0.1405  -0.1703 -0.2603 136  LEU Y CA  
23957 C C   . LEU D 8    ? 2.6646 2.2203 2.2802 0.1371  -0.1446 -0.2630 136  LEU Y C   
23958 O O   . LEU D 8    ? 2.6379 2.2464 2.2757 0.1207  -0.1222 -0.2790 136  LEU Y O   
23959 C CB  . LEU D 8    ? 2.5766 2.0673 2.2460 0.1394  -0.1844 -0.2651 136  LEU Y CB  
23960 C CG  . LEU D 8    ? 2.4780 1.9942 2.1996 0.1212  -0.1769 -0.2847 136  LEU Y CG  
23961 C CD1 . LEU D 8    ? 2.4792 2.0050 2.2480 0.1259  -0.1934 -0.2838 136  LEU Y CD1 
23962 C CD2 . LEU D 8    ? 2.4851 1.9364 2.1956 0.1133  -0.1828 -0.2915 136  LEU Y CD2 
23963 N N   . PHE D 9    ? 3.8309 3.3955 3.4225 0.1529  -0.1489 -0.2471 137  PHE Y N   
23964 C CA  . PHE D 9    ? 3.8327 3.4719 3.4244 0.1523  -0.1277 -0.2475 137  PHE Y CA  
23965 C C   . PHE D 9    ? 3.7671 3.4722 3.4029 0.1531  -0.1284 -0.2496 137  PHE Y C   
23966 O O   . PHE D 9    ? 3.7297 3.4156 3.3779 0.1643  -0.1486 -0.2404 137  PHE Y O   
23967 C CB  . PHE D 9    ? 3.9150 3.5313 3.4561 0.1686  -0.1292 -0.2294 137  PHE Y CB  
23968 C CG  . PHE D 9    ? 4.0131 3.5450 3.5048 0.1724  -0.1355 -0.2229 137  PHE Y CG  
23969 C CD1 . PHE D 9    ? 3.9978 3.5011 3.4858 0.1578  -0.1267 -0.2360 137  PHE Y CD1 
23970 C CD2 . PHE D 9    ? 4.0552 3.5349 3.5022 0.1905  -0.1498 -0.2036 137  PHE Y CD2 
23971 C CE1 . PHE D 9    ? 4.0334 3.4559 3.4728 0.1615  -0.1322 -0.2297 137  PHE Y CE1 
23972 C CE2 . PHE D 9    ? 4.0962 3.4947 3.4938 0.1941  -0.1554 -0.1974 137  PHE Y CE2 
23973 C CZ  . PHE D 9    ? 4.0787 3.4480 3.4717 0.1797  -0.1466 -0.2104 137  PHE Y CZ  
23974 N N   . VAL D 10   ? 2.9423 2.7237 2.6013 0.1410  -0.1061 -0.2621 138  VAL Y N   
23975 C CA  . VAL D 10   ? 2.8556 2.7030 2.5504 0.1414  -0.1035 -0.2644 138  VAL Y CA  
23976 C C   . VAL D 10   ? 2.8932 2.7907 2.5685 0.1502  -0.0928 -0.2555 138  VAL Y C   
23977 O O   . VAL D 10   ? 2.9266 2.8389 2.5797 0.1460  -0.0767 -0.2581 138  VAL Y O   
23978 C CB  . VAL D 10   ? 2.7688 2.6672 2.5073 0.1204  -0.0875 -0.2862 138  VAL Y CB  
23979 C CG1 . VAL D 10   ? 2.7180 2.7022 2.4746 0.1171  -0.0717 -0.2911 138  VAL Y CG1 
23980 C CG2 . VAL D 10   ? 2.7028 2.5740 2.4779 0.1167  -0.1019 -0.2916 138  VAL Y CG2 
23981 N N   . ASN D 11   ? 3.0791 3.0011 2.7636 0.1627  -0.1016 -0.2450 139  ASN Y N   
23982 C CA  . ASN D 11   ? 3.0797 3.0541 2.7504 0.1716  -0.0925 -0.2366 139  ASN Y CA  
23983 C C   . ASN D 11   ? 3.0250 3.0595 2.7279 0.1734  -0.0920 -0.2377 139  ASN Y C   
23984 O O   . ASN D 11   ? 3.0063 3.0213 2.7171 0.1849  -0.1081 -0.2275 139  ASN Y O   
23985 C CB  . ASN D 11   ? 3.1179 3.0452 2.7461 0.1916  -0.1054 -0.2153 139  ASN Y CB  
23986 C CG  . ASN D 11   ? 3.1857 3.0353 2.7814 0.1922  -0.1123 -0.2122 139  ASN Y CG  
23987 O OD1 . ASN D 11   ? 3.2074 3.0542 2.7846 0.1838  -0.0972 -0.2186 139  ASN Y OD1 
23988 N ND2 . ASN D 11   ? 3.2202 3.0045 2.8084 0.2022  -0.1354 -0.2023 139  ASN Y ND2 
23989 N N   . LYS D 12   ? 3.2567 3.3625 2.9775 0.1620  -0.0734 -0.2501 140  LYS Y N   
23990 C CA  . LYS D 12   ? 3.1648 3.3273 2.9107 0.1637  -0.0716 -0.2509 140  LYS Y CA  
23991 C C   . LYS D 12   ? 3.1544 3.3414 2.8760 0.1814  -0.0734 -0.2340 140  LYS Y C   
23992 O O   . LYS D 12   ? 3.1814 3.3814 2.8779 0.1841  -0.0647 -0.2304 140  LYS Y O   
23993 C CB  . LYS D 12   ? 3.0930 3.3194 2.8675 0.1440  -0.0525 -0.2717 140  LYS Y CB  
23994 C CG  . LYS D 12   ? 3.0899 3.2940 2.8871 0.1254  -0.0482 -0.2893 140  LYS Y CG  
23995 C CD  . LYS D 12   ? 2.9741 3.2397 2.8053 0.1068  -0.0321 -0.3092 140  LYS Y CD  
23996 C CE  . LYS D 12   ? 2.8825 3.1507 2.7467 0.1056  -0.0386 -0.3121 140  LYS Y CE  
23997 N NZ  . LYS D 12   ? 2.8026 3.1118 2.6998 0.0848  -0.0234 -0.3335 140  LYS Y NZ  
23998 N N   . VAL D 13   ? 3.5403 3.7322 3.2701 0.1937  -0.0842 -0.2235 141  VAL Y N   
23999 C CA  . VAL D 13   ? 3.5662 3.7811 3.2741 0.2110  -0.0863 -0.2071 141  VAL Y CA  
24000 C C   . VAL D 13   ? 3.4956 3.7850 3.2219 0.2089  -0.0764 -0.2117 141  VAL Y C   
24001 O O   . VAL D 13   ? 3.3991 3.6954 3.1394 0.2159  -0.0834 -0.2065 141  VAL Y O   
24002 C CB  . VAL D 13   ? 3.6168 3.7778 3.3112 0.2302  -0.1068 -0.1880 141  VAL Y CB  
24003 C CG1 . VAL D 13   ? 3.6441 3.8227 3.3106 0.2480  -0.1079 -0.1705 141  VAL Y CG1 
24004 C CG2 . VAL D 13   ? 3.7128 3.7961 3.3895 0.2317  -0.1190 -0.1842 141  VAL Y CG2 
24005 N N   . TYR D 14   ? 5.5378 5.8815 5.2638 0.1992  -0.0602 -0.2219 142  TYR Y N   
24006 C CA  . TYR D 14   ? 5.4554 5.8697 5.1936 0.1978  -0.0516 -0.2259 142  TYR Y CA  
24007 C C   . TYR D 14   ? 5.4876 5.9175 5.2007 0.2174  -0.0559 -0.2073 142  TYR Y C   
24008 O O   . TYR D 14   ? 5.4817 5.9660 5.1897 0.2174  -0.0464 -0.2089 142  TYR Y O   
24009 C CB  . TYR D 14   ? 3.2748 3.7417 3.0234 0.1799  -0.0340 -0.2445 142  TYR Y CB  
24010 C CG  . TYR D 14   ? 3.2682 3.7290 3.0442 0.1593  -0.0277 -0.2644 142  TYR Y CG  
24011 C CD1 . TYR D 14   ? 3.1788 3.6774 2.9828 0.1483  -0.0220 -0.2771 142  TYR Y CD1 
24012 C CD2 . TYR D 14   ? 3.3523 3.7676 3.1250 0.1509  -0.0268 -0.2704 142  TYR Y CD2 
24013 C CE1 . TYR D 14   ? 3.1705 3.6627 3.0003 0.1292  -0.0154 -0.2954 142  TYR Y CE1 
24014 C CE2 . TYR D 14   ? 3.3457 3.7545 3.1440 0.1323  -0.0209 -0.2883 142  TYR Y CE2 
24015 C CZ  . TYR D 14   ? 3.2533 3.7011 3.0810 0.1214  -0.0151 -0.3009 142  TYR Y CZ  
24016 O OH  . TYR D 14   ? 3.2454 3.6860 3.0990 0.1028  -0.0085 -0.3188 142  TYR Y OH  
24017 N N   . GLY D 15   ? 2.9490 3.3309 2.6475 0.2341  -0.0707 -0.1899 143  GLY Y N   
24018 C CA  . GLY D 15   ? 2.9983 3.3847 2.6699 0.2535  -0.0754 -0.1709 143  GLY Y CA  
24019 C C   . GLY D 15   ? 3.1311 3.5052 2.7756 0.2555  -0.0698 -0.1671 143  GLY Y C   
24020 O O   . GLY D 15   ? 3.2232 3.5502 2.8603 0.2492  -0.0706 -0.1710 143  GLY Y O   
24021 N N   . GLY D 16   ? 1.8952 2.3102 1.5250 0.2643  -0.0637 -0.1595 144  GLY Y N   
24022 C CA  . GLY D 16   ? 1.9884 2.4005 1.5958 0.2656  -0.0552 -0.1570 144  GLY Y CA  
24023 C C   . GLY D 16   ? 1.9712 2.3956 1.5904 0.2455  -0.0414 -0.1766 144  GLY Y C   
24024 O O   . GLY D 16   ? 1.9694 2.4230 1.5825 0.2421  -0.0289 -0.1807 144  GLY Y O   
24025 N N   . ASN D 17   ? 4.8546 5.2578 4.4934 0.2319  -0.0432 -0.1893 145  ASN Y N   
24026 C CA  . ASN D 17   ? 4.8181 5.2233 4.4692 0.2121  -0.0313 -0.2082 145  ASN Y CA  
24027 C C   . ASN D 17   ? 4.7974 5.1326 4.4478 0.2078  -0.0404 -0.2099 145  ASN Y C   
24028 O O   . ASN D 17   ? 4.7869 5.0914 4.4433 0.2145  -0.0546 -0.2031 145  ASN Y O   
24029 C CB  . ASN D 17   ? 2.5114 2.9783 2.1954 0.1963  -0.0224 -0.2266 145  ASN Y CB  
24030 C CG  . ASN D 17   ? 2.4333 2.9680 2.1201 0.2025  -0.0185 -0.2236 145  ASN Y CG  
24031 O OD1 . ASN D 17   ? 2.4538 3.0088 2.1244 0.2103  -0.0137 -0.2167 145  ASN Y OD1 
24032 N ND2 . ASN D 17   ? 2.3417 2.9106 2.0489 0.1992  -0.0203 -0.2289 145  ASN Y ND2 
24033 N N   . LEU D 18   ? 2.5163 2.8259 2.1600 0.1966  -0.0320 -0.2192 146  LEU Y N   
24034 C CA  . LEU D 18   ? 2.5028 2.7517 2.1494 0.1891  -0.0390 -0.2245 146  LEU Y CA  
24035 C C   . LEU D 18   ? 2.4815 2.7316 2.1340 0.1701  -0.0236 -0.2424 146  LEU Y C   
24036 O O   . LEU D 18   ? 2.4963 2.7438 2.1285 0.1692  -0.0125 -0.2423 146  LEU Y O   
24037 C CB  . LEU D 18   ? 2.5853 2.7580 2.1988 0.2046  -0.0540 -0.2066 146  LEU Y CB  
24038 C CG  . LEU D 18   ? 2.6214 2.7244 2.2278 0.1969  -0.0594 -0.2118 146  LEU Y CG  
24039 C CD1 . LEU D 18   ? 2.6781 2.7642 2.2615 0.1891  -0.0445 -0.2175 146  LEU Y CD1 
24040 C CD2 . LEU D 18   ? 2.5618 2.6715 2.2061 0.1817  -0.0609 -0.2280 146  LEU Y CD2 
24041 N N   . ASP D 19   ? 2.2830 2.5368 1.9647 0.1547  -0.0222 -0.2581 147  ASP Y N   
24042 C CA  . ASP D 19   ? 2.2823 2.5281 1.9718 0.1360  -0.0095 -0.2755 147  ASP Y CA  
24043 C C   . ASP D 19   ? 2.3943 2.5612 2.0774 0.1356  -0.0224 -0.2735 147  ASP Y C   
24044 O O   . ASP D 19   ? 2.3795 2.5328 2.0854 0.1339  -0.0335 -0.2759 147  ASP Y O   
24045 C CB  . ASP D 19   ? 2.1185 2.4277 1.8459 0.1177  0.0027  -0.2959 147  ASP Y CB  
24046 C CG  . ASP D 19   ? 1.9836 2.3712 1.7180 0.1195  0.0117  -0.2971 147  ASP Y CG  
24047 O OD1 . ASP D 19   ? 1.9821 2.3882 1.6978 0.1249  0.0194  -0.2922 147  ASP Y OD1 
24048 O OD2 . ASP D 19   ? 1.8865 2.3163 1.6452 0.1155  0.0110  -0.3031 147  ASP Y OD2 
24049 N N   . ALA D 20   ? 2.6059 2.7200 2.2574 0.1377  -0.0209 -0.2690 148  ALA Y N   
24050 C CA  . ALA D 20   ? 2.6938 2.7250 2.3299 0.1398  -0.0348 -0.2647 148  ALA Y CA  
24051 C C   . ALA D 20   ? 2.7359 2.7424 2.3727 0.1224  -0.0230 -0.2804 148  ALA Y C   
24052 O O   . ALA D 20   ? 2.7969 2.8120 2.4172 0.1165  -0.0059 -0.2853 148  ALA Y O   
24053 C CB  . ALA D 20   ? 2.7536 2.7286 2.3454 0.1588  -0.0462 -0.2439 148  ALA Y CB  
24054 N N   . SER D 21   ? 2.9686 2.9440 2.6259 0.1143  -0.0320 -0.2883 149  SER Y N   
24055 C CA  . SER D 21   ? 2.9579 2.9050 2.6185 0.0980  -0.0232 -0.3031 149  SER Y CA  
24056 C C   . SER D 21   ? 2.9120 2.7667 2.5461 0.1064  -0.0423 -0.2929 149  SER Y C   
24057 O O   . SER D 21   ? 2.8732 2.6992 2.5118 0.1180  -0.0637 -0.2822 149  SER Y O   
24058 C CB  . SER D 21   ? 2.9365 2.9193 2.6447 0.0817  -0.0194 -0.3209 149  SER Y CB  
24059 O OG  . SER D 21   ? 2.9197 2.9822 2.6542 0.0787  -0.0104 -0.3263 149  SER Y OG  
24060 N N   . ILE D 22   ? 3.3357 3.1427 2.9418 0.1008  -0.0350 -0.2961 150  ILE Y N   
24061 C CA  . ILE D 22   ? 3.2623 2.9786 2.8447 0.1054  -0.0527 -0.2899 150  ILE Y CA  
24062 C C   . ILE D 22   ? 3.2094 2.9156 2.8200 0.0872  -0.0486 -0.3080 150  ILE Y C   
24063 O O   . ILE D 22   ? 3.2028 2.9495 2.8278 0.0708  -0.0262 -0.3242 150  ILE Y O   
24064 C CB  . ILE D 22   ? 3.1018 2.7592 2.6281 0.1121  -0.0485 -0.2802 150  ILE Y CB  
24065 C CG1 . ILE D 22   ? 3.0421 2.6676 2.5602 0.0963  -0.0348 -0.2943 150  ILE Y CG1 
24066 C CG2 . ILE D 22   ? 3.1852 2.8880 2.6938 0.1182  -0.0323 -0.2740 150  ILE Y CG2 
24067 C CD1 . ILE D 22   ? 2.8977 2.4387 2.4031 0.0979  -0.0552 -0.2918 150  ILE Y CD1 
24068 N N   . ASP D 23   ? 3.3049 2.9568 2.9243 0.0901  -0.0702 -0.3057 151  ASP Y N   
24069 C CA  . ASP D 23   ? 3.2668 2.9171 2.9218 0.0734  -0.0677 -0.3229 151  ASP Y CA  
24070 C C   . ASP D 23   ? 3.3712 2.9341 3.0157 0.0785  -0.0917 -0.3177 151  ASP Y C   
24071 O O   . ASP D 23   ? 3.3818 2.8823 2.9848 0.0935  -0.1080 -0.3017 151  ASP Y O   
24072 C CB  . ASP D 23   ? 3.1237 2.8423 2.8324 0.0671  -0.0658 -0.3319 151  ASP Y CB  
24073 C CG  . ASP D 23   ? 3.0196 2.7596 2.7673 0.0462  -0.0534 -0.3531 151  ASP Y CG  
24074 O OD1 . ASP D 23   ? 3.0427 2.7582 2.7766 0.0351  -0.0418 -0.3624 151  ASP Y OD1 
24075 O OD2 . ASP D 23   ? 2.9230 2.7037 2.7145 0.0409  -0.0545 -0.3605 151  ASP Y OD2 
24076 N N   . SER D 24   ? 3.0675 2.6254 2.7495 0.0661  -0.0944 -0.3312 152  SER Y N   
24077 C CA  . SER D 24   ? 3.2041 2.6801 2.8802 0.0690  -0.1168 -0.3285 152  SER Y CA  
24078 C C   . SER D 24   ? 3.2999 2.7810 3.0298 0.0660  -0.1319 -0.3346 152  SER Y C   
24079 O O   . SER D 24   ? 3.2334 2.7807 3.0080 0.0545  -0.1181 -0.3474 152  SER Y O   
24080 C CB  . SER D 24   ? 3.2166 2.6574 2.8746 0.0554  -0.1037 -0.3398 152  SER Y CB  
24081 O OG  . SER D 24   ? 3.2086 2.7018 2.9101 0.0354  -0.0842 -0.3603 152  SER Y OG  
24082 N N   . PHE D 25   ? 3.9558 3.3656 3.6812 0.0763  -0.1602 -0.3258 153  PHE Y N   
24083 C CA  . PHE D 25   ? 4.0489 3.4507 3.8256 0.0729  -0.1756 -0.3324 153  PHE Y CA  
24084 C C   . PHE D 25   ? 4.1426 3.4737 3.9118 0.0669  -0.1855 -0.3381 153  PHE Y C   
24085 O O   . PHE D 25   ? 4.1645 3.4512 3.8856 0.0671  -0.1818 -0.3352 153  PHE Y O   
24086 C CB  . PHE D 25   ? 4.1250 3.5053 3.9098 0.0914  -0.2031 -0.3170 153  PHE Y CB  
24087 C CG  . PHE D 25   ? 4.1692 3.5378 4.0093 0.0892  -0.2200 -0.3231 153  PHE Y CG  
24088 C CD1 . PHE D 25   ? 4.1210 3.5546 4.0136 0.0836  -0.2110 -0.3309 153  PHE Y CD1 
24089 C CD2 . PHE D 25   ? 4.2474 3.5376 4.0862 0.0933  -0.2453 -0.3208 153  PHE Y CD2 
24090 C CE1 . PHE D 25   ? 4.1070 3.5285 4.0519 0.0815  -0.2249 -0.3368 153  PHE Y CE1 
24091 C CE2 . PHE D 25   ? 4.2294 3.5092 4.1224 0.0914  -0.2609 -0.3267 153  PHE Y CE2 
24092 C CZ  . PHE D 25   ? 4.1545 3.5001 4.1013 0.0854  -0.2499 -0.3347 153  PHE Y CZ  
24093 N N   . SER D 26   ? 5.5760 4.8952 5.3923 0.0615  -0.1975 -0.3464 154  SER Y N   
24094 C CA  . SER D 26   ? 5.6131 4.8636 5.4253 0.0566  -0.2094 -0.3514 154  SER Y CA  
24095 C C   . SER D 26   ? 5.6327 4.8373 5.4786 0.0651  -0.2413 -0.3473 154  SER Y C   
24096 O O   . SER D 26   ? 5.5791 4.8165 5.4842 0.0573  -0.2403 -0.3578 154  SER Y O   
24097 C CB  . SER D 26   ? 3.0915 2.3772 2.9291 0.0343  -0.1829 -0.3722 154  SER Y CB  
24098 O OG  . SER D 26   ? 3.0675 2.3873 2.8706 0.0275  -0.1556 -0.3753 154  SER Y OG  
24099 N N   . ILE D 27   ? 3.3673 2.4950 3.1743 0.0813  -0.2694 -0.3319 155  ILE Y N   
24100 C CA  . ILE D 27   ? 3.4069 2.4797 3.2388 0.0915  -0.3036 -0.3264 155  ILE Y CA  
24101 C C   . ILE D 27   ? 3.4606 2.4774 3.3008 0.0826  -0.3126 -0.3360 155  ILE Y C   
24102 O O   . ILE D 27   ? 3.4916 2.4512 3.2804 0.0834  -0.3152 -0.3328 155  ILE Y O   
24103 C CB  . ILE D 27   ? 3.4053 2.4166 3.1877 0.1130  -0.3312 -0.3056 155  ILE Y CB  
24104 C CG1 . ILE D 27   ? 3.3855 2.4494 3.1480 0.1214  -0.3186 -0.2954 155  ILE Y CG1 
24105 C CG2 . ILE D 27   ? 3.4144 2.3787 3.2298 0.1241  -0.3672 -0.3000 155  ILE Y CG2 
24106 C CD1 . ILE D 27   ? 3.4152 2.4218 3.1218 0.1414  -0.3407 -0.2751 155  ILE Y CD1 
24107 N N   . ASN D 28   ? 6.4997 5.5314 6.4044 0.0744  -0.3169 -0.3477 156  ASN Y N   
24108 C CA  . ASN D 28   ? 6.5782 5.5700 6.5007 0.0633  -0.3208 -0.3597 156  ASN Y CA  
24109 C C   . ASN D 28   ? 6.6134 5.5507 6.5418 0.0662  -0.3290 -0.3430 156  ASN Y C   
24110 O O   . ASN D 28   ? 6.6046 5.5246 6.5629 0.0551  -0.3246 -0.3498 156  ASN Y O   
24111 C CB  . ASN D 28   ? 3.7292 2.7879 3.7197 0.0450  -0.2985 -0.3788 156  ASN Y CB  
24112 C CG  . ASN D 28   ? 3.7216 2.8668 3.7110 0.0339  -0.2618 -0.3861 156  ASN Y CG  
24113 O OD1 . ASN D 28   ? 3.7386 2.8906 3.6751 0.0366  -0.2492 -0.3798 156  ASN Y OD1 
24114 N ND2 . ASN D 28   ? 3.6617 2.8729 3.7096 0.0215  -0.2445 -0.3997 156  ASN Y ND2 
24115 N N   . LYS D 29   ? 3.9073 2.7743 3.8042 0.0947  -0.3868 -0.3346 157  LYS Y N   
24116 C CA  . LYS D 29   ? 3.9789 2.7684 3.8832 0.1078  -0.4279 -0.3267 157  LYS Y CA  
24117 C C   . LYS D 29   ? 4.0596 2.7810 3.8916 0.1266  -0.4515 -0.3071 157  LYS Y C   
24118 O O   . LYS D 29   ? 4.0748 2.8124 3.8543 0.1293  -0.4343 -0.2998 157  LYS Y O   
24119 C CB  . LYS D 29   ? 3.9565 2.7776 3.9326 0.1121  -0.4412 -0.3282 157  LYS Y CB  
24120 C CG  . LYS D 29   ? 3.9236 2.8013 3.9745 0.0940  -0.4212 -0.3478 157  LYS Y CG  
24121 C CD  . LYS D 29   ? 3.8871 2.8043 4.0059 0.0979  -0.4282 -0.3490 157  LYS Y CD  
24122 C CE  . LYS D 29   ? 3.8699 2.7227 4.0251 0.1081  -0.4673 -0.3459 157  LYS Y CE  
24123 N NZ  . LYS D 29   ? 3.8320 2.7232 4.0556 0.1114  -0.4718 -0.3478 157  LYS Y NZ  
24124 N N   . GLU D 30   ? 4.2004 2.8445 4.0302 0.1393  -0.4909 -0.2991 158  GLU Y N   
24125 C CA  . GLU D 30   ? 4.2757 2.8480 4.0395 0.1580  -0.5178 -0.2804 158  GLU Y CA  
24126 C C   . GLU D 30   ? 4.2522 2.8421 4.0324 0.1735  -0.5346 -0.2683 158  GLU Y C   
24127 O O   . GLU D 30   ? 4.2871 2.8484 4.0115 0.1875  -0.5443 -0.2528 158  GLU Y O   
24128 C CB  . GLU D 30   ? 4.3725 2.8456 4.1188 0.1640  -0.5536 -0.2778 158  GLU Y CB  
24129 C CG  . GLU D 30   ? 4.4151 2.8816 4.2392 0.1617  -0.5756 -0.2872 158  GLU Y CG  
24130 C CD  . GLU D 30   ? 4.4899 2.8544 4.2948 0.1716  -0.6175 -0.2817 158  GLU Y CD  
24131 O OE1 . GLU D 30   ? 4.5309 2.8280 4.2583 0.1792  -0.6279 -0.2712 158  GLU Y OE1 
24132 O OE2 . GLU D 30   ? 4.5050 2.8556 4.3722 0.1719  -0.6401 -0.2880 158  GLU Y OE2 
24133 N N   . GLU D 31   ? 5.8651 4.5011 5.7222 0.1706  -0.5369 -0.2759 159  GLU Y N   
24134 C CA  . GLU D 31   ? 5.8105 4.4757 5.6936 0.1829  -0.5473 -0.2670 159  GLU Y CA  
24135 C C   . GLU D 31   ? 5.7007 4.4552 5.6585 0.1708  -0.5223 -0.2804 159  GLU Y C   
24136 O O   . GLU D 31   ? 5.6704 4.4345 5.6834 0.1589  -0.5196 -0.2948 159  GLU Y O   
24137 C CB  . GLU D 31   ? 5.8473 4.4407 5.7456 0.1984  -0.5932 -0.2586 159  GLU Y CB  
24138 C CG  . GLU D 31   ? 5.8352 4.4224 5.8116 0.1917  -0.6077 -0.2717 159  GLU Y CG  
24139 C CD  . GLU D 31   ? 5.8902 4.4092 5.8515 0.1864  -0.6223 -0.2776 159  GLU Y CD  
24140 O OE1 . GLU D 31   ? 5.9469 4.4083 5.8336 0.1912  -0.6292 -0.2691 159  GLU Y OE1 
24141 O OE2 . GLU D 31   ? 5.8811 4.4025 5.9050 0.1774  -0.6267 -0.2906 159  GLU Y OE2 
24142 N N   . VAL D 32   ? 5.8313 4.6501 5.7899 0.1735  -0.5035 -0.2758 160  VAL Y N   
24143 C CA  . VAL D 32   ? 5.7182 4.6219 5.7403 0.1619  -0.4775 -0.2882 160  VAL Y CA  
24144 C C   . VAL D 32   ? 5.6822 4.6146 5.7362 0.1737  -0.4863 -0.2803 160  VAL Y C   
24145 O O   . VAL D 32   ? 5.7150 4.6289 5.7286 0.1893  -0.4990 -0.2644 160  VAL Y O   
24146 C CB  . VAL D 32   ? 2.8926 1.8665 2.8930 0.1482  -0.4359 -0.2953 160  VAL Y CB  
24147 C CG1 . VAL D 32   ? 2.8129 1.8717 2.8766 0.1364  -0.4106 -0.3079 160  VAL Y CG1 
24148 C CG2 . VAL D 32   ? 2.9049 1.8548 2.8796 0.1350  -0.4243 -0.3048 160  VAL Y CG2 
24149 N N   . SER D 33   ? 4.6589 3.6354 4.7858 0.1659  -0.4784 -0.2918 161  SER Y N   
24150 C CA  . SER D 33   ? 4.6061 3.6177 4.7699 0.1746  -0.4811 -0.2868 161  SER Y CA  
24151 C C   . SER D 33   ? 4.5749 3.6541 4.7089 0.1748  -0.4526 -0.2817 161  SER Y C   
24152 O O   . SER D 33   ? 4.5485 3.6815 4.6776 0.1603  -0.4208 -0.2916 161  SER Y O   
24153 C CB  . SER D 33   ? 4.5231 3.5681 4.7713 0.1637  -0.4738 -0.3022 161  SER Y CB  
24154 O OG  . SER D 33   ? 4.4638 3.5445 4.7473 0.1714  -0.4732 -0.2979 161  SER Y OG  
24155 N N   . LEU D 34   ? 3.7253 2.8008 3.8401 0.1914  -0.4648 -0.2665 162  LEU Y N   
24156 C CA  . LEU D 34   ? 3.6953 2.8325 3.7841 0.1940  -0.4412 -0.2601 162  LEU Y CA  
24157 C C   . LEU D 34   ? 3.5991 2.8173 3.7413 0.1801  -0.4110 -0.2740 162  LEU Y C   
24158 O O   . LEU D 34   ? 3.5545 2.8342 3.6789 0.1764  -0.3846 -0.2739 162  LEU Y O   
24159 C CB  . LEU D 34   ? 3.7271 2.8436 3.8004 0.2144  -0.4625 -0.2425 162  LEU Y CB  
24160 C CG  . LEU D 34   ? 3.7219 2.8897 3.7615 0.2215  -0.4444 -0.2320 162  LEU Y CG  
24161 C CD1 . LEU D 34   ? 3.7556 2.9341 3.7331 0.2166  -0.4253 -0.2301 162  LEU Y CD1 
24162 C CD2 . LEU D 34   ? 3.7658 2.8944 3.7864 0.2424  -0.4712 -0.2141 162  LEU Y CD2 
24163 N N   . LYS D 35   ? 4.7519 3.9678 4.9595 0.1725  -0.4155 -0.2861 163  LYS Y N   
24164 C CA  . LYS D 35   ? 4.6689 3.9532 4.9286 0.1570  -0.3867 -0.3016 163  LYS Y CA  
24165 C C   . LYS D 35   ? 4.6764 3.9915 4.9169 0.1392  -0.3598 -0.3139 163  LYS Y C   
24166 O O   . LYS D 35   ? 4.6674 4.0471 4.8966 0.1316  -0.3312 -0.3177 163  LYS Y O   
24167 C CB  . LYS D 35   ? 4.6178 3.8823 4.9508 0.1525  -0.3988 -0.3123 163  LYS Y CB  
24168 C CG  . LYS D 35   ? 4.5161 3.8442 4.9040 0.1346  -0.3683 -0.3300 163  LYS Y CG  
24169 C CD  . LYS D 35   ? 4.4730 3.7730 4.9306 0.1282  -0.3797 -0.3421 163  LYS Y CD  
24170 C CE  . LYS D 35   ? 4.3836 3.7445 4.8945 0.1100  -0.3480 -0.3599 163  LYS Y CE  
24171 N NZ  . LYS D 35   ? 4.3293 3.7418 4.8579 0.1141  -0.3328 -0.3569 163  LYS Y NZ  
24172 N N   . GLU D 36   ? 4.5217 3.7890 4.7585 0.1327  -0.3697 -0.3201 164  GLU Y N   
24173 C CA  . GLU D 36   ? 4.5332 3.8213 4.7509 0.1159  -0.3460 -0.3319 164  GLU Y CA  
24174 C C   . GLU D 36   ? 4.4831 3.7865 4.6310 0.1201  -0.3340 -0.3222 164  GLU Y C   
24175 O O   . GLU D 36   ? 4.4313 3.7831 4.5654 0.1069  -0.3055 -0.3310 164  GLU Y O   
24176 C CB  . GLU D 36   ? 4.6763 3.8990 4.8963 0.1112  -0.3632 -0.3376 164  GLU Y CB  
24177 C CG  . GLU D 36   ? 4.7321 3.9401 5.0247 0.1056  -0.3738 -0.3488 164  GLU Y CG  
24178 C CD  . GLU D 36   ? 4.9107 4.0537 5.2038 0.1013  -0.3912 -0.3541 164  GLU Y CD  
24179 O OE1 . GLU D 36   ? 5.0354 4.1320 5.2686 0.1066  -0.4016 -0.3460 164  GLU Y OE1 
24180 O OE2 . GLU D 36   ? 4.9213 4.0580 5.2740 0.0927  -0.3942 -0.3664 164  GLU Y OE2 
24181 N N   . LEU D 37   ? 3.3093 2.5707 3.4148 0.1386  -0.3560 -0.3042 165  LEU Y N   
24182 C CA  . LEU D 37   ? 3.2901 2.5614 3.3301 0.1451  -0.3466 -0.2930 165  LEU Y CA  
24183 C C   . LEU D 37   ? 3.2386 2.5942 3.2875 0.1415  -0.3193 -0.2949 165  LEU Y C   
24184 O O   . LEU D 37   ? 3.2361 2.6331 3.2543 0.1345  -0.2954 -0.2975 165  LEU Y O   
24185 C CB  . LEU D 37   ? 3.2863 2.4996 3.2887 0.1666  -0.3764 -0.2732 165  LEU Y CB  
24186 C CG  . LEU D 37   ? 3.2804 2.4728 3.2075 0.1737  -0.3735 -0.2613 165  LEU Y CG  
24187 C CD1 . LEU D 37   ? 3.3091 2.4562 3.2091 0.1642  -0.3729 -0.2682 165  LEU Y CD1 
24188 C CD2 . LEU D 37   ? 3.2993 2.4384 3.1918 0.1950  -0.4019 -0.2417 165  LEU Y CD2 
24189 N N   . ASP D 38   ? 4.1278 3.5072 4.2208 0.1464  -0.3236 -0.2939 166  ASP Y N   
24190 C CA  . ASP D 38   ? 4.0923 3.5449 4.1939 0.1461  -0.3021 -0.2935 166  ASP Y CA  
24191 C C   . ASP D 38   ? 4.0511 3.5682 4.1907 0.1258  -0.2722 -0.3126 166  ASP Y C   
24192 O O   . ASP D 38   ? 4.0204 3.5999 4.1471 0.1210  -0.2484 -0.3147 166  ASP Y O   
24193 C CB  . ASP D 38   ? 4.0862 3.5339 4.2176 0.1600  -0.3184 -0.2844 166  ASP Y CB  
24194 C CG  . ASP D 38   ? 4.1092 3.5913 4.2081 0.1725  -0.3124 -0.2705 166  ASP Y CG  
24195 O OD1 . ASP D 38   ? 4.1440 3.6552 4.1993 0.1700  -0.2955 -0.2684 166  ASP Y OD1 
24196 O OD2 . ASP D 38   ? 4.1041 3.5838 4.2219 0.1848  -0.3243 -0.2619 166  ASP Y OD2 
24197 N N   . PHE D 39   ? 4.4608 3.9626 4.6469 0.1139  -0.2736 -0.3266 167  PHE Y N   
24198 C CA  . PHE D 39   ? 4.4497 4.0087 4.6735 0.0938  -0.2454 -0.3456 167  PHE Y CA  
24199 C C   . PHE D 39   ? 4.4254 4.0085 4.6142 0.0806  -0.2239 -0.3537 167  PHE Y C   
24200 O O   . PHE D 39   ? 4.4095 4.0545 4.6115 0.0662  -0.1968 -0.3661 167  PHE Y O   
24201 C CB  . PHE D 39   ? 4.4924 4.0259 4.7761 0.0843  -0.2521 -0.3587 167  PHE Y CB  
24202 C CG  . PHE D 39   ? 4.4944 4.0843 4.8176 0.0633  -0.2225 -0.3785 167  PHE Y CG  
24203 C CD1 . PHE D 39   ? 4.5227 4.1196 4.8377 0.0467  -0.2069 -0.3917 167  PHE Y CD1 
24204 C CD2 . PHE D 39   ? 4.4595 4.0937 4.8267 0.0600  -0.2097 -0.3842 167  PHE Y CD2 
24205 C CE1 . PHE D 39   ? 4.4915 4.1391 4.8416 0.0272  -0.1800 -0.4101 167  PHE Y CE1 
24206 C CE2 . PHE D 39   ? 4.4307 4.1138 4.8311 0.0405  -0.1824 -0.4025 167  PHE Y CE2 
24207 C CZ  . PHE D 39   ? 4.4433 4.1335 4.8354 0.0241  -0.1679 -0.4154 167  PHE Y CZ  
24208 N N   . LYS D 40   ? 3.8933 3.4257 4.0374 0.0853  -0.2360 -0.3469 168  LYS Y N   
24209 C CA  . LYS D 40   ? 3.8304 3.3793 3.9392 0.0737  -0.2163 -0.3539 168  LYS Y CA  
24210 C C   . LYS D 40   ? 3.7864 3.3790 3.8505 0.0798  -0.2023 -0.3448 168  LYS Y C   
24211 O O   . LYS D 40   ? 3.7511 3.3988 3.8090 0.0671  -0.1762 -0.3547 168  LYS Y O   
24212 C CB  . LYS D 40   ? 3.8714 3.3456 3.9501 0.0754  -0.2329 -0.3512 168  LYS Y CB  
24213 C CG  . LYS D 40   ? 3.8362 3.2732 3.9593 0.0662  -0.2427 -0.3630 168  LYS Y CG  
24214 C CD  . LYS D 40   ? 3.8795 3.2599 3.9704 0.0616  -0.2482 -0.3655 168  LYS Y CD  
24215 C CE  . LYS D 40   ? 3.8499 3.2092 3.9885 0.0483  -0.2505 -0.3808 168  LYS Y CE  
24216 N NZ  . LYS D 40   ? 3.9133 3.2201 4.0202 0.0426  -0.2533 -0.3842 168  LYS Y NZ  
24217 N N   . ILE D 41   ? 3.3028 2.8715 3.3383 0.0991  -0.2200 -0.3263 169  ILE Y N   
24218 C CA  . ILE D 41   ? 3.2580 2.8623 3.2510 0.1074  -0.2097 -0.3156 169  ILE Y CA  
24219 C C   . ILE D 41   ? 3.2106 2.9011 3.2266 0.0990  -0.1844 -0.3239 169  ILE Y C   
24220 O O   . ILE D 41   ? 3.2315 2.9678 3.2279 0.0902  -0.1624 -0.3298 169  ILE Y O   
24221 C CB  . ILE D 41   ? 3.1989 2.7627 3.1654 0.1303  -0.2345 -0.2944 169  ILE Y CB  
24222 C CG1 . ILE D 41   ? 3.2150 2.6916 3.1510 0.1385  -0.2595 -0.2862 169  ILE Y CG1 
24223 C CG2 . ILE D 41   ? 3.1910 2.7933 3.1165 0.1390  -0.2232 -0.2833 169  ILE Y CG2 
24224 C CD1 . ILE D 41   ? 3.2287 2.6862 3.1148 0.1332  -0.2492 -0.2871 169  ILE Y CD1 
24225 N N   . ARG D 42   ? 3.9725 3.6833 4.0301 0.1013  -0.1876 -0.3248 170  ARG Y N   
24226 C CA  . ARG D 42   ? 3.9403 3.7274 4.0213 0.0928  -0.1645 -0.3334 170  ARG Y CA  
24227 C C   . ARG D 42   ? 3.8801 3.7021 3.9865 0.0699  -0.1418 -0.3548 170  ARG Y C   
24228 O O   . ARG D 42   ? 3.8507 3.7358 3.9551 0.0606  -0.1194 -0.3626 170  ARG Y O   
24229 C CB  . ARG D 42   ? 3.9593 3.7538 4.0799 0.1001  -0.1723 -0.3301 170  ARG Y CB  
24230 C CG  . ARG D 42   ? 4.0506 3.8051 4.2212 0.0950  -0.1844 -0.3384 170  ARG Y CG  
24231 C CD  . ARG D 42   ? 4.0737 3.8426 4.2866 0.1007  -0.1875 -0.3367 170  ARG Y CD  
24232 N NE  . ARG D 42   ? 4.1403 3.8590 4.3982 0.1009  -0.2054 -0.3404 170  ARG Y NE  
24233 C CZ  . ARG D 42   ? 4.1352 3.8530 4.4363 0.1058  -0.2110 -0.3398 170  ARG Y CZ  
24234 N NH1 . ARG D 42   ? 4.1009 3.8641 4.4036 0.1109  -0.1995 -0.3353 170  ARG Y NH1 
24235 N NH2 . ARG D 42   ? 4.1523 3.8229 4.4959 0.1056  -0.2279 -0.3438 170  ARG Y NH2 
24236 N N   . GLN D 43   ? 3.1199 2.9001 3.2495 0.0609  -0.1483 -0.3643 171  GLN Y N   
24237 C CA  . GLN D 43   ? 3.0852 2.8933 3.2425 0.0388  -0.1276 -0.3852 171  GLN Y CA  
24238 C C   . GLN D 43   ? 3.0951 2.9447 3.2181 0.0292  -0.1059 -0.3911 171  GLN Y C   
24239 O O   . GLN D 43   ? 3.0514 2.9593 3.1913 0.0138  -0.0826 -0.4056 171  GLN Y O   
24240 C CB  . GLN D 43   ? 3.0874 2.8337 3.2628 0.0332  -0.1407 -0.3915 171  GLN Y CB  
24241 C CG  . GLN D 43   ? 3.0315 2.8002 3.2513 0.0117  -0.1230 -0.4130 171  GLN Y CG  
24242 C CD  . GLN D 43   ? 3.0331 2.7410 3.2615 0.0059  -0.1344 -0.4189 171  GLN Y CD  
24243 O OE1 . GLN D 43   ? 3.0758 2.7467 3.2635 0.0088  -0.1407 -0.4138 171  GLN Y OE1 
24244 N NE2 . GLN D 43   ? 2.9864 2.6829 3.2679 -0.0023 -0.1365 -0.4297 171  GLN Y NE2 
24245 N N   . HIS D 44   ? 5.9899 5.8072 6.0648 0.0384  -0.1138 -0.3800 172  HIS Y N   
24246 C CA  . HIS D 44   ? 5.9993 5.8472 6.0386 0.0315  -0.0953 -0.3836 172  HIS Y CA  
24247 C C   . HIS D 44   ? 6.0173 5.9258 6.0394 0.0380  -0.0845 -0.3770 172  HIS Y C   
24248 O O   . HIS D 44   ? 6.0084 5.9769 6.0337 0.0256  -0.0624 -0.3884 172  HIS Y O   
24249 C CB  . HIS D 44   ? 3.8635 3.6494 3.8570 0.0398  -0.1074 -0.3734 172  HIS Y CB  
24250 C CG  . HIS D 44   ? 3.8833 3.6105 3.8870 0.0321  -0.1159 -0.3810 172  HIS Y CG  
24251 N ND1 . HIS D 44   ? 3.9188 3.5696 3.9106 0.0447  -0.1428 -0.3696 172  HIS Y ND1 
24252 C CD2 . HIS D 44   ? 3.8729 3.6068 3.8980 0.0131  -0.1014 -0.3991 172  HIS Y CD2 
24253 C CE1 . HIS D 44   ? 3.9309 3.5428 3.9356 0.0342  -0.1450 -0.3799 172  HIS Y CE1 
24254 N NE2 . HIS D 44   ? 3.9024 3.5637 3.9278 0.0149  -0.1197 -0.3978 172  HIS Y NE2 
24255 N N   . LEU D 45   ? 3.1182 3.0100 3.1214 0.0575  -0.1008 -0.3586 173  LEU Y N   
24256 C CA  . LEU D 45   ? 3.1179 3.0659 3.1092 0.0651  -0.0926 -0.3514 173  LEU Y CA  
24257 C C   . LEU D 45   ? 3.0512 3.0655 3.0807 0.0511  -0.0738 -0.3665 173  LEU Y C   
24258 O O   . LEU D 45   ? 3.0150 3.0894 3.0349 0.0463  -0.0567 -0.3707 173  LEU Y O   
24259 C CB  . LEU D 45   ? 3.1253 3.0448 3.1082 0.0865  -0.1140 -0.3320 173  LEU Y CB  
24260 C CG  . LEU D 45   ? 3.1899 3.0415 3.1324 0.1013  -0.1339 -0.3161 173  LEU Y CG  
24261 C CD1 . LEU D 45   ? 3.2018 3.0201 3.1468 0.1203  -0.1569 -0.2997 173  LEU Y CD1 
24262 C CD2 . LEU D 45   ? 3.2364 3.1072 3.1320 0.1052  -0.1231 -0.3095 173  LEU Y CD2 
24263 N N   . VAL D 46   ? 3.5755 3.5763 3.6481 0.0446  -0.0775 -0.3749 174  VAL Y N   
24264 C CA  . VAL D 46   ? 3.4470 3.5015 3.5577 0.0311  -0.0603 -0.3894 174  VAL Y CA  
24265 C C   . VAL D 46   ? 3.4191 3.5103 3.5352 0.0097  -0.0379 -0.4088 174  VAL Y C   
24266 O O   . VAL D 46   ? 3.3288 3.4794 3.4571 -0.0008 -0.0196 -0.4194 174  VAL Y O   
24267 C CB  . VAL D 46   ? 3.5022 3.5270 3.6602 0.0291  -0.0692 -0.3940 174  VAL Y CB  
24268 C CG1 . VAL D 46   ? 3.4087 3.4815 3.6051 0.0103  -0.0477 -0.4132 174  VAL Y CG1 
24269 C CG2 . VAL D 46   ? 3.4996 3.5078 3.6603 0.0483  -0.0862 -0.3775 174  VAL Y CG2 
24270 N N   . LYS D 47   ? 5.1068 5.1625 5.2123 0.0030  -0.0388 -0.4137 175  LYS Y N   
24271 C CA  . LYS D 47   ? 5.0578 5.1477 5.1717 -0.0180 -0.0170 -0.4330 175  LYS Y CA  
24272 C C   . LYS D 47   ? 5.0589 5.1688 5.1324 -0.0189 -0.0070 -0.4320 175  LYS Y C   
24273 O O   . LYS D 47   ? 5.0380 5.1729 5.1153 -0.0360 0.0108  -0.4478 175  LYS Y O   
24274 C CB  . LYS D 47   ? 5.0940 5.1371 5.2313 -0.0295 -0.0197 -0.4441 175  LYS Y CB  
24275 C CG  . LYS D 47   ? 5.0269 5.0609 5.2154 -0.0354 -0.0226 -0.4521 175  LYS Y CG  
24276 C CD  . LYS D 47   ? 2.0018 1.9843 2.2112 -0.0437 -0.0286 -0.4603 175  LYS Y CD  
24277 C CE  . LYS D 47   ? 1.9872 1.9937 2.2438 -0.0642 -0.0117 -0.4811 175  LYS Y CE  
24278 N NZ  . LYS D 47   ? 1.9601 2.0249 2.2443 -0.0724 0.0049  -0.4902 175  LYS Y NZ  
24279 N N   . ASN D 48   ? 3.3899 3.4867 3.4264 -0.0010 -0.0179 -0.4139 176  ASN Y N   
24280 C CA  . ASN D 48   ? 3.4059 3.5149 3.4037 -0.0003 -0.0091 -0.4114 176  ASN Y CA  
24281 C C   . ASN D 48   ? 3.3428 3.4814 3.3096 0.0153  -0.0108 -0.3963 176  ASN Y C   
24282 O O   . ASN D 48   ? 3.3383 3.5164 3.2872 0.0109  0.0036  -0.4001 176  ASN Y O   
24283 C CB  . ASN D 48   ? 3.5085 3.5480 3.4818 0.0025  -0.0185 -0.4068 176  ASN Y CB  
24284 C CG  . ASN D 48   ? 3.5010 3.5116 3.5011 -0.0133 -0.0157 -0.4220 176  ASN Y CG  
24285 O OD1 . ASN D 48   ? 3.5209 3.5375 3.5163 -0.0275 -0.0004 -0.4346 176  ASN Y OD1 
24286 N ND2 . ASN D 48   ? 3.4699 3.4488 3.5000 -0.0109 -0.0300 -0.4212 176  ASN Y ND2 
24287 N N   . TYR D 49   ? 2.7290 2.8480 2.6902 0.0334  -0.0281 -0.3794 177  TYR Y N   
24288 C CA  . TYR D 49   ? 2.7232 2.8651 2.6538 0.0492  -0.0306 -0.3639 177  TYR Y CA  
24289 C C   . TYR D 49   ? 2.6798 2.8710 2.6274 0.0544  -0.0295 -0.3610 177  TYR Y C   
24290 O O   . TYR D 49   ? 2.7085 2.9070 2.6358 0.0710  -0.0371 -0.3452 177  TYR Y O   
24291 C CB  . TYR D 49   ? 2.7452 2.8219 2.6434 0.0686  -0.0511 -0.3439 177  TYR Y CB  
24292 C CG  . TYR D 49   ? 2.7398 2.7744 2.6074 0.0659  -0.0492 -0.3441 177  TYR Y CG  
24293 C CD1 . TYR D 49   ? 2.7242 2.6938 2.5943 0.0622  -0.0594 -0.3468 177  TYR Y CD1 
24294 C CD2 . TYR D 49   ? 2.7422 2.8015 2.5791 0.0667  -0.0364 -0.3421 177  TYR Y CD2 
24295 C CE1 . TYR D 49   ? 2.7449 2.6729 2.5841 0.0595  -0.0567 -0.3472 177  TYR Y CE1 
24296 C CE2 . TYR D 49   ? 2.7672 2.7862 2.5755 0.0637  -0.0324 -0.3428 177  TYR Y CE2 
24297 C CZ  . TYR D 49   ? 2.7613 2.7139 2.5694 0.0601  -0.0423 -0.3452 177  TYR Y CZ  
24298 O OH  . TYR D 49   ? 2.7846 2.6940 2.5618 0.0571  -0.0377 -0.3459 177  TYR Y OH  
24299 N N   . GLY D 50   ? 3.5330 3.7562 3.5170 0.0400  -0.0194 -0.3764 178  GLY Y N   
24300 C CA  . GLY D 50   ? 3.4891 3.7573 3.4894 0.0430  -0.0162 -0.3755 178  GLY Y CA  
24301 C C   . GLY D 50   ? 3.5558 3.7901 3.5556 0.0622  -0.0352 -0.3577 178  GLY Y C   
24302 O O   . GLY D 50   ? 3.5357 3.7797 3.5100 0.0782  -0.0413 -0.3423 178  GLY Y O   
24303 N N   . LEU D 51   ? 3.1671 3.3606 3.1967 0.0607  -0.0448 -0.3601 179  LEU Y N   
24304 C CA  . LEU D 51   ? 3.2400 3.4062 3.2795 0.0765  -0.0612 -0.3465 179  LEU Y CA  
24305 C C   . LEU D 51   ? 3.2308 3.4139 3.3154 0.0669  -0.0541 -0.3581 179  LEU Y C   
24306 O O   . LEU D 51   ? 3.2049 3.3864 3.3172 0.0499  -0.0453 -0.3746 179  LEU Y O   
24307 C CB  . LEU D 51   ? 3.3238 3.4138 3.3569 0.0872  -0.0835 -0.3358 179  LEU Y CB  
24308 C CG  . LEU D 51   ? 3.2967 3.3567 3.3544 0.0991  -0.0998 -0.3268 179  LEU Y CG  
24309 C CD1 . LEU D 51   ? 3.2755 3.3625 3.3150 0.1155  -0.1021 -0.3117 179  LEU Y CD1 
24310 C CD2 . LEU D 51   ? 3.3766 3.3599 3.4315 0.1082  -0.1235 -0.3183 179  LEU Y CD2 
24311 N N   . TYR D 52   ? 3.4795 3.6767 3.5709 0.0779  -0.0573 -0.3492 180  TYR Y N   
24312 C CA  . TYR D 52   ? 3.4820 3.6975 3.6136 0.0698  -0.0484 -0.3593 180  TYR Y CA  
24313 C C   . TYR D 52   ? 3.4759 3.7559 3.6126 0.0527  -0.0242 -0.3756 180  TYR Y C   
24314 O O   . TYR D 52   ? 3.4332 3.7286 3.6028 0.0418  -0.0131 -0.3875 180  TYR Y O   
24315 C CB  . TYR D 52   ? 3.5151 3.6814 3.6865 0.0625  -0.0557 -0.3676 180  TYR Y CB  
24316 C CG  . TYR D 52   ? 3.5997 3.7058 3.7753 0.0799  -0.0803 -0.3522 180  TYR Y CG  
24317 C CD1 . TYR D 52   ? 3.6054 3.7130 3.7713 0.0976  -0.0890 -0.3364 180  TYR Y CD1 
24318 C CD2 . TYR D 52   ? 3.6686 3.7157 3.8577 0.0788  -0.0955 -0.3536 180  TYR Y CD2 
24319 C CE1 . TYR D 52   ? 3.6654 3.7184 3.8356 0.1135  -0.1119 -0.3228 180  TYR Y CE1 
24320 C CE2 . TYR D 52   ? 3.7310 3.7222 3.9237 0.0949  -0.1197 -0.3398 180  TYR Y CE2 
24321 C CZ  . TYR D 52   ? 3.7242 3.7192 3.9080 0.1121  -0.1278 -0.3246 180  TYR Y CZ  
24322 O OH  . TYR D 52   ? 3.7796 3.7193 3.9675 0.1280  -0.1523 -0.3113 180  TYR Y OH  
24323 N N   . LYS D 53   ? 2.9950 3.3113 3.0998 0.0502  -0.0162 -0.3764 181  LYS Y N   
24324 C CA  . LYS D 53   ? 2.9682 3.3483 3.0729 0.0358  0.0045  -0.3905 181  LYS Y CA  
24325 C C   . LYS D 53   ? 2.9463 3.3700 3.0165 0.0475  0.0059  -0.3794 181  LYS Y C   
24326 O O   . LYS D 53   ? 2.9739 3.4163 3.0171 0.0478  0.0080  -0.3781 181  LYS Y O   
24327 C CB  . LYS D 53   ? 3.0488 3.4387 3.1547 0.0172  0.0159  -0.4071 181  LYS Y CB  
24328 C CG  . LYS D 53   ? 3.0957 3.4382 3.2310 0.0063  0.0132  -0.4171 181  LYS Y CG  
24329 C CD  . LYS D 53   ? 3.1144 3.4523 3.2924 -0.0018 0.0184  -0.4267 181  LYS Y CD  
24330 C CE  . LYS D 53   ? 3.0592 3.4516 3.2514 -0.0211 0.0413  -0.4457 181  LYS Y CE  
24331 N NZ  . LYS D 53   ? 3.0494 3.4340 3.2819 -0.0277 0.0473  -0.4537 181  LYS Y NZ  
24332 N N   . GLY D 54   ? 3.4458 3.8848 3.5181 0.0572  0.0051  -0.3716 182  GLY Y N   
24333 C CA  . GLY D 54   ? 3.4126 3.8921 3.4542 0.0692  0.0057  -0.3605 182  GLY Y CA  
24334 C C   . GLY D 54   ? 3.4179 3.8658 3.4435 0.0925  -0.0116 -0.3382 182  GLY Y C   
24335 O O   . GLY D 54   ? 3.3929 3.8058 3.4386 0.0992  -0.0197 -0.3328 182  GLY Y O   
24336 N N   . THR D 55   ? 3.2409 3.7014 3.2316 0.1047  -0.0168 -0.3257 183  THR Y N   
24337 C CA  . THR D 55   ? 3.2820 3.7146 3.2530 0.1271  -0.0327 -0.3039 183  THR Y CA  
24338 C C   . THR D 55   ? 3.4065 3.7731 3.3757 0.1335  -0.0488 -0.2963 183  THR Y C   
24339 O O   . THR D 55   ? 3.4651 3.8010 3.4160 0.1513  -0.0632 -0.2787 183  THR Y O   
24340 C CB  . THR D 55   ? 3.1953 3.6659 3.1300 0.1376  -0.0315 -0.2935 183  THR Y CB  
24341 O OG1 . THR D 55   ? 3.2114 3.7005 3.1353 0.1262  -0.0237 -0.3034 183  THR Y OG1 
24342 C CG2 . THR D 55   ? 3.1176 3.6426 3.0508 0.1381  -0.0217 -0.2950 183  THR Y CG2 
24343 N N   . THR D 56   ? 5.4609 5.8048 5.4482 0.1186  -0.0463 -0.3098 184  THR Y N   
24344 C CA  . THR D 56   ? 5.5689 5.8473 5.5537 0.1236  -0.0621 -0.3038 184  THR Y CA  
24345 C C   . THR D 56   ? 5.5834 5.8149 5.6010 0.1262  -0.0740 -0.3029 184  THR Y C   
24346 O O   . THR D 56   ? 5.5331 5.7705 5.5870 0.1124  -0.0657 -0.3175 184  THR Y O   
24347 C CB  . THR D 56   ? 5.6055 5.8754 5.5893 0.1077  -0.0552 -0.3174 184  THR Y CB  
24348 O OG1 . THR D 56   ? 2.3994 2.7311 2.3860 0.0921  -0.0349 -0.3326 184  THR Y OG1 
24349 C CG2 . THR D 56   ? 2.4324 2.6658 2.3776 0.1181  -0.0655 -0.3051 184  THR Y CG2 
24350 N N   . LYS D 57   ? 3.2076 3.3910 3.2131 0.1439  -0.0937 -0.2859 185  LYS Y N   
24351 C CA  . LYS D 57   ? 3.2235 3.3580 3.2598 0.1488  -0.1083 -0.2833 185  LYS Y CA  
24352 C C   . LYS D 57   ? 3.2480 3.3323 3.2636 0.1702  -0.1311 -0.2628 185  LYS Y C   
24353 O O   . LYS D 57   ? 3.2895 3.3184 3.3231 0.1744  -0.1482 -0.2601 185  LYS Y O   
24354 C CB  . LYS D 57   ? 3.1756 3.3404 3.2469 0.1448  -0.0981 -0.2898 185  LYS Y CB  
24355 C CG  . LYS D 57   ? 3.1715 3.3765 3.2235 0.1570  -0.0932 -0.2786 185  LYS Y CG  
24356 C CD  . LYS D 57   ? 3.1057 3.3362 3.1898 0.1528  -0.0819 -0.2853 185  LYS Y CD  
24357 C CE  . LYS D 57   ? 3.0550 3.3403 3.1476 0.1334  -0.0587 -0.3036 185  LYS Y CE  
24358 N NZ  . LYS D 57   ? 2.9781 3.2947 3.0885 0.1317  -0.0458 -0.3073 185  LYS Y NZ  
24359 N N   . TYR D 58   ? 3.6724 3.7757 3.6509 0.1838  -0.1318 -0.2485 186  TYR Y N   
24360 C CA  . TYR D 58   ? 3.6963 3.7556 3.6523 0.2044  -0.1520 -0.2286 186  TYR Y CA  
24361 C C   . TYR D 58   ? 3.7523 3.7776 3.6667 0.2098  -0.1606 -0.2204 186  TYR Y C   
24362 O O   . TYR D 58   ? 3.7459 3.8046 3.6302 0.2092  -0.1493 -0.2189 186  TYR Y O   
24363 C CB  . TYR D 58   ? 3.6493 3.7450 3.5918 0.2181  -0.1486 -0.2161 186  TYR Y CB  
24364 C CG  . TYR D 58   ? 3.6131 3.6658 3.5331 0.2395  -0.1684 -0.1956 186  TYR Y CG  
24365 C CD1 . TYR D 58   ? 3.5885 3.6018 3.5335 0.2483  -0.1838 -0.1900 186  TYR Y CD1 
24366 C CD2 . TYR D 58   ? 3.6188 3.6688 3.4934 0.2506  -0.1717 -0.1823 186  TYR Y CD2 
24367 C CE1 . TYR D 58   ? 3.5646 3.5374 3.4886 0.2676  -0.2025 -0.1715 186  TYR Y CE1 
24368 C CE2 . TYR D 58   ? 3.5959 3.6050 3.4481 0.2699  -0.1894 -0.1636 186  TYR Y CE2 
24369 C CZ  . TYR D 58   ? 3.5693 3.5399 3.4457 0.2783  -0.2053 -0.1583 186  TYR Y CZ  
24370 O OH  . TYR D 58   ? 3.5439 3.4734 3.3980 0.2972  -0.2234 -0.1401 186  TYR Y OH  
24371 N N   . GLY D 59   ? 3.2876 3.2451 3.2002 0.2155  -0.1806 -0.2149 187  GLY Y N   
24372 C CA  . GLY D 59   ? 3.3558 3.2709 3.2276 0.2205  -0.1895 -0.2073 187  GLY Y CA  
24373 C C   . GLY D 59   ? 3.3618 3.1975 3.2321 0.2296  -0.2154 -0.1994 187  GLY Y C   
24374 O O   . GLY D 59   ? 3.3244 3.1388 3.2280 0.2332  -0.2278 -0.1990 187  GLY Y O   
24375 N N   . LYS D 60   ? 3.2201 3.0103 3.0514 0.2332  -0.2237 -0.1932 188  LYS Y N   
24376 C CA  . LYS D 60   ? 3.2650 2.9750 3.0868 0.2425  -0.2500 -0.1849 188  LYS Y CA  
24377 C C   . LYS D 60   ? 3.2927 2.9584 3.0871 0.2351  -0.2520 -0.1893 188  LYS Y C   
24378 O O   . LYS D 60   ? 3.3516 3.0167 3.1021 0.2375  -0.2443 -0.1837 188  LYS Y O   
24379 C CB  . LYS D 60   ? 3.3134 2.9967 3.1026 0.2640  -0.2654 -0.1639 188  LYS Y CB  
24380 C CG  . LYS D 60   ? 3.2867 2.9920 3.1042 0.2740  -0.2703 -0.1575 188  LYS Y CG  
24381 C CD  . LYS D 60   ? 3.2720 2.9341 3.1315 0.2745  -0.2899 -0.1612 188  LYS Y CD  
24382 C CE  . LYS D 60   ? 3.2412 2.9099 3.1205 0.2882  -0.2984 -0.1512 188  LYS Y CE  
24383 N NZ  . LYS D 60   ? 3.1718 2.9136 3.0775 0.2824  -0.2760 -0.1578 188  LYS Y NZ  
24384 N N   . ILE D 61   ? 4.7741 4.4016 4.5953 0.2262  -0.2619 -0.1996 189  ILE Y N   
24385 C CA  . ILE D 61   ? 4.7942 4.3736 4.5922 0.2189  -0.2653 -0.2045 189  ILE Y CA  
24386 C C   . ILE D 61   ? 4.8602 4.3595 4.6190 0.2350  -0.2918 -0.1885 189  ILE Y C   
24387 O O   . ILE D 61   ? 4.8625 4.3227 4.6390 0.2447  -0.3150 -0.1822 189  ILE Y O   
24388 C CB  . ILE D 61   ? 4.7378 4.3055 4.5815 0.2035  -0.2668 -0.2216 189  ILE Y CB  
24389 C CG1 . ILE D 61   ? 4.6547 4.2956 4.5468 0.1909  -0.2463 -0.2356 189  ILE Y CG1 
24390 C CG2 . ILE D 61   ? 4.7716 4.3121 4.5932 0.1915  -0.2604 -0.2305 189  ILE Y CG2 
24391 C CD1 . ILE D 61   ? 4.6121 4.2435 4.5532 0.1761  -0.2469 -0.2523 189  ILE Y CD1 
24392 N N   . THR D 62   ? 6.0537 5.5268 5.7593 0.2375  -0.2882 -0.1822 190  THR Y N   
24393 C CA  . THR D 62   ? 6.1452 5.5414 5.8060 0.2531  -0.3118 -0.1662 190  THR Y CA  
24394 C C   . THR D 62   ? 6.2205 5.5479 5.8566 0.2471  -0.3211 -0.1705 190  THR Y C   
24395 O O   . THR D 62   ? 6.2563 5.5783 5.8538 0.2418  -0.3062 -0.1719 190  THR Y O   
24396 C CB  . THR D 62   ? 3.6398 3.0482 3.2505 0.2648  -0.3031 -0.1515 190  THR Y CB  
24397 O OG1 . THR D 62   ? 3.6759 3.0958 3.2553 0.2549  -0.2816 -0.1573 190  THR Y OG1 
24398 C CG2 . THR D 62   ? 3.5872 3.0700 3.2209 0.2691  -0.2906 -0.1486 190  THR Y CG2 
24399 N N   . ILE D 63   ? 4.9024 4.1758 4.5610 0.2483  -0.3457 -0.1725 191  ILE Y N   
24400 C CA  . ILE D 63   ? 4.9984 4.2020 4.6356 0.2433  -0.3574 -0.1766 191  ILE Y CA  
24401 C C   . ILE D 63   ? 5.1273 4.2566 4.6987 0.2577  -0.3744 -0.1602 191  ILE Y C   
24402 O O   . ILE D 63   ? 5.1733 4.2691 4.7346 0.2738  -0.3970 -0.1464 191  ILE Y O   
24403 C CB  . ILE D 63   ? 4.3039 3.4693 3.9875 0.2409  -0.3811 -0.1837 191  ILE Y CB  
24404 C CG1 . ILE D 63   ? 4.1588 3.3925 3.9115 0.2296  -0.3678 -0.1977 191  ILE Y CG1 
24405 C CG2 . ILE D 63   ? 4.3613 3.4678 4.0278 0.2319  -0.3874 -0.1914 191  ILE Y CG2 
24406 C CD1 . ILE D 63   ? 4.0901 3.2891 3.8926 0.2252  -0.3876 -0.2067 191  ILE Y CD1 
24407 N N   . ASN D 64   ? 5.1654 4.2675 4.6917 0.2516  -0.3629 -0.1622 192  ASN Y N   
24408 C CA  . ASN D 64   ? 5.2655 4.2861 4.7264 0.2632  -0.3787 -0.1485 192  ASN Y CA  
24409 C C   . ASN D 64   ? 5.3271 4.2653 4.7847 0.2625  -0.4056 -0.1512 192  ASN Y C   
24410 O O   . ASN D 64   ? 5.2905 4.2325 4.7761 0.2480  -0.3997 -0.1662 192  ASN Y O   
24411 C CB  . ASN D 64   ? 5.2903 4.3177 4.7006 0.2579  -0.3520 -0.1484 192  ASN Y CB  
24412 C CG  . ASN D 64   ? 5.2965 4.3944 4.7016 0.2619  -0.3296 -0.1427 192  ASN Y CG  
24413 O OD1 . ASN D 64   ? 5.2988 4.4329 4.7296 0.2707  -0.3358 -0.1363 192  ASN Y OD1 
24414 N ND2 . ASN D 64   ? 5.2962 4.4134 4.6689 0.2554  -0.3031 -0.1451 192  ASN Y ND2 
24415 N N   . LEU D 65   ? 6.7350 5.7878 6.3021 0.2288  -0.3275 -0.1105 193  LEU Y N   
24416 C CA  . LEU D 65   ? 6.7376 5.7621 6.3354 0.2199  -0.3226 -0.1050 193  LEU Y CA  
24417 C C   . LEU D 65   ? 6.7626 5.7846 6.3563 0.2151  -0.2995 -0.0835 193  LEU Y C   
24418 O O   . LEU D 65   ? 6.7700 5.7578 6.3614 0.2082  -0.2947 -0.0850 193  LEU Y O   
24419 C CB  . LEU D 65   ? 6.7074 5.7171 6.3423 0.2287  -0.3460 -0.1032 193  LEU Y CB  
24420 C CG  . LEU D 65   ? 6.6771 5.6988 6.3380 0.2312  -0.3669 -0.1243 193  LEU Y CG  
24421 C CD1 . LEU D 65   ? 6.6497 5.6733 6.3518 0.2404  -0.3828 -0.1174 193  LEU Y CD1 
24422 C CD2 . LEU D 65   ? 6.6679 5.6624 6.3379 0.2209  -0.3744 -0.1458 193  LEU Y CD2 
24423 N N   . LYS D 66   ? 4.6988 3.3856 4.0012 0.3058  -0.4831 -0.1080 194  LYS Y N   
24424 C CA  . LYS D 66   ? 4.8105 3.4134 4.0357 0.3178  -0.4970 -0.0933 194  LYS Y CA  
24425 C C   . LYS D 66   ? 4.8348 3.4663 4.0236 0.3278  -0.4808 -0.0800 194  LYS Y C   
24426 O O   . LYS D 66   ? 4.7712 3.4850 3.9972 0.3268  -0.4630 -0.0814 194  LYS Y O   
24427 C CB  . LYS D 66   ? 4.8935 3.4160 4.1147 0.3307  -0.5411 -0.0852 194  LYS Y CB  
24428 C CG  . LYS D 66   ? 5.0164 3.4381 4.1563 0.3404  -0.5585 -0.0731 194  LYS Y CG  
24429 C CD  . LYS D 66   ? 5.1243 3.5126 4.2281 0.3277  -0.5426 -0.0817 194  LYS Y CD  
24430 C CE  . LYS D 66   ? 5.2380 3.5369 4.2519 0.3368  -0.5497 -0.0688 194  LYS Y CE  
24431 N NZ  . LYS D 66   ? 5.2827 3.6091 4.2601 0.3451  -0.5301 -0.0566 194  LYS Y NZ  
24432 N N   . ASP D 67   ? 3.7974 2.3594 2.9130 0.3375  -0.4869 -0.0670 195  ASP Y N   
24433 C CA  . ASP D 67   ? 3.8269 2.4088 2.9012 0.3463  -0.4690 -0.0545 195  ASP Y CA  
24434 C C   . ASP D 67   ? 3.9003 2.5188 2.9983 0.3601  -0.4792 -0.0435 195  ASP Y C   
24435 O O   . ASP D 67   ? 3.9506 2.5665 3.0082 0.3707  -0.4724 -0.0302 195  ASP Y O   
24436 C CB  . ASP D 67   ? 3.8132 2.3018 2.8022 0.3544  -0.4761 -0.0426 195  ASP Y CB  
24437 C CG  . ASP D 67   ? 3.7092 2.1894 2.6617 0.3415  -0.4468 -0.0504 195  ASP Y CG  
24438 O OD1 . ASP D 67   ? 3.6382 2.1860 2.5954 0.3351  -0.4125 -0.0538 195  ASP Y OD1 
24439 O OD2 . ASP D 67   ? 3.7122 2.1170 2.6310 0.3379  -0.4581 -0.0532 195  ASP Y OD2 
24440 N N   . GLY D 68   ? 5.6399 4.2920 4.8033 0.3598  -0.4942 -0.0491 196  GLY Y N   
24441 C CA  . GLY D 68   ? 5.7025 4.3876 4.8905 0.3726  -0.5036 -0.0393 196  GLY Y CA  
24442 C C   . GLY D 68   ? 5.5769 4.3187 4.8453 0.3686  -0.5097 -0.0487 196  GLY Y C   
24443 O O   . GLY D 68   ? 5.5770 4.3378 4.8683 0.3797  -0.5209 -0.0408 196  GLY Y O   
24444 N N   . GLU D 69   ? 6.8241 6.1828 6.6047 0.1984  -0.1848 0.0122  197  GLU Y N   
24445 C CA  . GLU D 69   ? 6.7992 6.1293 6.5747 0.2102  -0.2107 -0.0012 197  GLU Y CA  
24446 C C   . GLU D 69   ? 6.7870 6.1228 6.5359 0.2128  -0.2260 -0.0228 197  GLU Y C   
24447 O O   . GLU D 69   ? 6.8004 6.1491 6.5470 0.1993  -0.2120 -0.0359 197  GLU Y O   
24448 C CB  . GLU D 69   ? 4.4535 3.2197 3.8696 0.3424  -0.5301 -0.0850 197  GLU Y CB  
24449 C CG  . GLU D 69   ? 4.4192 3.2055 3.9056 0.3445  -0.5477 -0.0895 197  GLU Y CG  
24450 C CD  . GLU D 69   ? 4.4233 3.1321 3.9216 0.3469  -0.5834 -0.0918 197  GLU Y CD  
24451 O OE1 . GLU D 69   ? 4.4586 3.0877 3.8996 0.3535  -0.6021 -0.0839 197  GLU Y OE1 
24452 O OE2 . GLU D 69   ? 4.3929 3.1192 3.9576 0.3421  -0.5927 -0.1019 197  GLU Y OE2 
24453 N N   . LYS D 70   ? 4.5958 3.5741 4.0634 0.3379  -0.4641 -0.0863 198  LYS Y N   
24454 C CA  . LYS D 70   ? 4.4404 3.5125 3.9441 0.3262  -0.4322 -0.0967 198  LYS Y CA  
24455 C C   . LYS D 70   ? 4.3427 3.4613 3.9148 0.3257  -0.4363 -0.1023 198  LYS Y C   
24456 O O   . LYS D 70   ? 4.3503 3.4725 3.9296 0.3393  -0.4476 -0.0914 198  LYS Y O   
24457 C CB  . LYS D 70   ? 4.3779 3.4911 3.8434 0.3324  -0.4104 -0.0866 198  LYS Y CB  
24458 C CG  . LYS D 70   ? 4.3462 3.4191 3.7450 0.3327  -0.4017 -0.0812 198  LYS Y CG  
24459 C CD  . LYS D 70   ? 4.2636 3.3947 3.6388 0.3346  -0.3739 -0.0757 198  LYS Y CD  
24460 C CE  . LYS D 70   ? 4.2310 3.3546 3.5835 0.3536  -0.3842 -0.0572 198  LYS Y CE  
24461 N NZ  . LYS D 70   ? 4.2097 3.2414 3.5046 0.3654  -0.4056 -0.0441 198  LYS Y NZ  
24462 N N   . GLN D 71   ? 6.6304 5.8362 6.2875 0.2913  -0.3891 -0.1080 199  GLN Y N   
24463 C CA  . GLN D 71   ? 6.5809 5.7792 6.2725 0.3053  -0.4239 -0.1263 199  GLN Y CA  
24464 C C   . GLN D 71   ? 6.4754 5.7517 6.2000 0.2896  -0.3952 -0.1431 199  GLN Y C   
24465 O O   . GLN D 71   ? 6.4654 5.7596 6.1673 0.2785  -0.3752 -0.1500 199  GLN Y O   
24466 C CB  . GLN D 71   ? 3.9511 3.0867 3.6744 0.3060  -0.4553 -0.1329 199  GLN Y CB  
24467 C CG  . GLN D 71   ? 4.0289 3.0999 3.7217 0.2999  -0.4655 -0.1372 199  GLN Y CG  
24468 C CD  . GLN D 71   ? 4.0262 3.0499 3.7620 0.2965  -0.4905 -0.1457 199  GLN Y CD  
24469 O OE1 . GLN D 71   ? 3.9748 3.0357 3.7683 0.2841  -0.4813 -0.1603 199  GLN Y OE1 
24470 N NE2 . GLN D 71   ? 4.0502 2.9905 3.7573 0.3074  -0.5224 -0.1366 199  GLN Y NE2 
24471 N N   . GLU D 72   ? 4.6289 3.9523 4.4086 0.2872  -0.3904 -0.1491 200  GLU Y N   
24472 C CA  . GLU D 72   ? 4.5141 3.9185 4.3263 0.2724  -0.3603 -0.1628 200  GLU Y CA  
24473 C C   . GLU D 72   ? 4.4175 3.8445 4.2988 0.2639  -0.3603 -0.1757 200  GLU Y C   
24474 O O   . GLU D 72   ? 4.3879 3.7722 4.2972 0.2706  -0.3838 -0.1735 200  GLU Y O   
24475 C CB  . GLU D 72   ? 4.5043 3.9680 4.2985 0.2797  -0.3428 -0.1538 200  GLU Y CB  
24476 C CG  . GLU D 72   ? 4.5667 4.0095 4.2961 0.2905  -0.3430 -0.1392 200  GLU Y CG  
24477 C CD  . GLU D 72   ? 4.5709 4.0543 4.2865 0.3035  -0.3361 -0.1261 200  GLU Y CD  
24478 O OE1 . GLU D 72   ? 4.5156 4.0577 4.2679 0.3009  -0.3239 -0.1307 200  GLU Y OE1 
24479 O OE2 . GLU D 72   ? 4.6346 4.0897 4.3015 0.3164  -0.3424 -0.1112 200  GLU Y OE2 
24480 N N   . ILE D 73   ? 4.3284 3.8230 4.2372 0.2492  -0.3335 -0.1894 201  ILE Y N   
24481 C CA  . ILE D 73   ? 4.2489 3.7728 4.2216 0.2398  -0.3278 -0.2024 201  ILE Y CA  
24482 C C   . ILE D 73   ? 4.2449 3.8506 4.2284 0.2344  -0.3000 -0.2066 201  ILE Y C   
24483 O O   . ILE D 73   ? 4.2381 3.8877 4.2134 0.2210  -0.2772 -0.2167 201  ILE Y O   
24484 C CB  . ILE D 73   ? 4.1627 3.6770 4.1635 0.2216  -0.3229 -0.2203 201  ILE Y CB  
24485 C CG1 . ILE D 73   ? 4.1840 3.6178 4.1614 0.2255  -0.3478 -0.2165 201  ILE Y CG1 
24486 C CG2 . ILE D 73   ? 4.0815 3.6151 4.1502 0.2136  -0.3202 -0.2327 201  ILE Y CG2 
24487 C CD1 . ILE D 73   ? 4.1543 3.5799 4.1326 0.2084  -0.3382 -0.2311 201  ILE Y CD1 
24488 N N   . ASP D 74   ? 3.3853 3.0107 3.3866 0.2448  -0.3021 -0.1992 202  ASP Y N   
24489 C CA  . ASP D 74   ? 3.4039 3.1034 3.4104 0.2415  -0.2773 -0.2015 202  ASP Y CA  
24490 C C   . ASP D 74   ? 3.4038 3.1460 3.4438 0.2203  -0.2553 -0.2219 202  ASP Y C   
24491 O O   . ASP D 74   ? 3.3600 3.0836 3.4444 0.2114  -0.2595 -0.2333 202  ASP Y O   
24492 C CB  . ASP D 74   ? 3.3984 3.1080 3.4318 0.2530  -0.2823 -0.1941 202  ASP Y CB  
24493 C CG  . ASP D 74   ? 3.3885 3.1718 3.4218 0.2510  -0.2575 -0.1953 202  ASP Y CG  
24494 O OD1 . ASP D 74   ? 3.3322 3.1314 3.3942 0.2562  -0.2558 -0.1934 202  ASP Y OD1 
24495 O OD2 . ASP D 74   ? 3.3899 3.2146 3.3947 0.2441  -0.2398 -0.1983 202  ASP Y OD2 
24496 N N   . LEU D 75   ? 3.8867 3.6848 3.9053 0.2122  -0.2322 -0.2266 203  LEU Y N   
24497 C CA  . LEU D 75   ? 3.9123 3.7574 3.9589 0.1920  -0.2094 -0.2458 203  LEU Y CA  
24498 C C   . LEU D 75   ? 3.9122 3.8101 3.9875 0.1908  -0.1947 -0.2492 203  LEU Y C   
24499 O O   . LEU D 75   ? 3.8423 3.7804 3.9450 0.1748  -0.1755 -0.2650 203  LEU Y O   
24500 C CB  . LEU D 75   ? 3.8849 3.7626 3.8954 0.1831  -0.1924 -0.2504 203  LEU Y CB  
24501 C CG  . LEU D 75   ? 3.9034 3.7263 3.8825 0.1838  -0.2047 -0.2474 203  LEU Y CG  
24502 C CD1 . LEU D 75   ? 3.9116 3.7685 3.8588 0.1742  -0.1857 -0.2531 203  LEU Y CD1 
24503 C CD2 . LEU D 75   ? 3.8792 3.6559 3.8922 0.1743  -0.2153 -0.2584 203  LEU Y CD2 
24504 N N   . GLY D 76   ? 3.7608 3.6567 3.8279 0.2078  -0.2033 -0.2342 204  GLY Y N   
24505 C CA  . GLY D 76   ? 3.7618 3.6977 3.8556 0.2088  -0.1917 -0.2356 204  GLY Y CA  
24506 C C   . GLY D 76   ? 3.8304 3.7416 3.9807 0.2036  -0.1967 -0.2448 204  GLY Y C   
24507 O O   . GLY D 76   ? 3.7598 3.7043 3.9405 0.1988  -0.1823 -0.2515 204  GLY Y O   
24508 N N   . ASP D 77   ? 3.6271 3.4787 3.7917 0.2043  -0.2169 -0.2455 205  ASP Y N   
24509 C CA  . ASP D 77   ? 3.6911 3.5140 3.9124 0.2008  -0.2246 -0.2534 205  ASP Y CA  
24510 C C   . ASP D 77   ? 3.7525 3.5146 3.9866 0.1972  -0.2445 -0.2578 205  ASP Y C   
24511 O O   . ASP D 77   ? 3.8049 3.5220 4.0048 0.2079  -0.2651 -0.2464 205  ASP Y O   
24512 C CB  . ASP D 77   ? 3.7518 3.5580 3.9864 0.2180  -0.2372 -0.2405 205  ASP Y CB  
24513 C CG  . ASP D 77   ? 3.7655 3.5737 4.0627 0.2119  -0.2315 -0.2511 205  ASP Y CG  
24514 O OD1 . ASP D 77   ? 3.7432 3.5749 4.0700 0.1940  -0.2138 -0.2684 205  ASP Y OD1 
24515 O OD2 . ASP D 77   ? 3.7954 3.5811 4.1126 0.2248  -0.2437 -0.2425 205  ASP Y OD2 
24516 N N   . LYS D 78   ? 3.7836 3.5435 4.0664 0.1822  -0.2382 -0.2745 206  LYS Y N   
24517 C CA  . LYS D 78   ? 3.7762 3.4791 4.0797 0.1780  -0.2568 -0.2803 206  LYS Y CA  
24518 C C   . LYS D 78   ? 3.7375 3.3906 4.0811 0.1894  -0.2812 -0.2751 206  LYS Y C   
24519 O O   . LYS D 78   ? 3.7359 3.3524 4.1201 0.1833  -0.2923 -0.2842 206  LYS Y O   
24520 C CB  . LYS D 78   ? 3.7499 3.4742 4.0879 0.1559  -0.2379 -0.3013 206  LYS Y CB  
24521 C CG  . LYS D 78   ? 3.7092 3.4719 4.0998 0.1466  -0.2181 -0.3131 206  LYS Y CG  
24522 C CD  . LYS D 78   ? 3.6822 3.4689 4.1000 0.1242  -0.1973 -0.3337 206  LYS Y CD  
24523 C CE  . LYS D 78   ? 3.6313 3.4552 4.0967 0.1148  -0.1757 -0.3453 206  LYS Y CE  
24524 N NZ  . LYS D 78   ? 3.5815 3.3669 4.0977 0.1229  -0.1911 -0.3432 206  LYS Y NZ  
24525 N N   . LEU D 79   ? 4.6669 4.3191 5.0002 0.2061  -0.2894 -0.2605 207  LEU Y N   
24526 C CA  . LEU D 79   ? 4.6007 4.2129 4.9743 0.2175  -0.3103 -0.2554 207  LEU Y CA  
24527 C C   . LEU D 79   ? 4.5978 4.1354 4.9624 0.2278  -0.3454 -0.2475 207  LEU Y C   
24528 O O   . LEU D 79   ? 4.6057 4.1054 4.9952 0.2401  -0.3672 -0.2406 207  LEU Y O   
24529 C CB  . LEU D 79   ? 4.5935 4.2291 4.9556 0.2322  -0.3069 -0.2422 207  LEU Y CB  
24530 C CG  . LEU D 79   ? 4.5805 4.1900 4.9868 0.2439  -0.3214 -0.2373 207  LEU Y CG  
24531 C CD1 . LEU D 79   ? 4.5276 4.1491 5.0043 0.2309  -0.3081 -0.2542 207  LEU Y CD1 
24532 C CD2 . LEU D 79   ? 4.5853 4.2229 4.9664 0.2579  -0.3149 -0.2232 207  LEU Y CD2 
24533 N N   . GLN D 80   ? 4.1928 3.7081 4.5213 0.2229  -0.3511 -0.2486 208  GLN Y N   
24534 C CA  . GLN D 80   ? 4.1919 3.6332 4.5042 0.2321  -0.3842 -0.2411 208  GLN Y CA  
24535 C C   . GLN D 80   ? 4.1492 3.5509 4.5170 0.2234  -0.3979 -0.2543 208  GLN Y C   
24536 O O   . GLN D 80   ? 4.1560 3.5433 4.5169 0.2121  -0.3966 -0.2632 208  GLN Y O   
24537 C CB  . GLN D 80   ? 4.2127 3.6423 4.4572 0.2316  -0.3841 -0.2355 208  GLN Y CB  
24538 C CG  . GLN D 80   ? 4.2643 3.7222 4.4512 0.2424  -0.3754 -0.2208 208  GLN Y CG  
24539 C CD  . GLN D 80   ? 4.2913 3.8273 4.4704 0.2310  -0.3401 -0.2279 208  GLN Y CD  
24540 O OE1 . GLN D 80   ? 4.3113 3.8809 4.5254 0.2143  -0.3210 -0.2443 208  GLN Y OE1 
24541 N NE2 . GLN D 80   ? 4.2987 3.8629 4.4315 0.2401  -0.3318 -0.2158 208  GLN Y NE2 
24542 N N   . PHE D 81   ? 3.7939 3.1771 4.2173 0.2290  -0.4111 -0.2555 209  PHE Y N   
24543 C CA  . PHE D 81   ? 3.7689 3.1204 4.2543 0.2204  -0.4221 -0.2690 209  PHE Y CA  
24544 C C   . PHE D 81   ? 3.8680 3.1400 4.3592 0.2324  -0.4630 -0.2622 209  PHE Y C   
24545 O O   . PHE D 81   ? 3.8796 3.1183 4.4073 0.2249  -0.4748 -0.2727 209  PHE Y O   
24546 C CB  . PHE D 81   ? 3.6478 3.0346 4.2042 0.2140  -0.4050 -0.2799 209  PHE Y CB  
24547 C CG  . PHE D 81   ? 3.5811 2.9647 4.1540 0.2298  -0.4146 -0.2690 209  PHE Y CG  
24548 C CD1 . PHE D 81   ? 3.5862 2.9111 4.1883 0.2424  -0.4480 -0.2634 209  PHE Y CD1 
24549 C CD2 . PHE D 81   ? 3.5154 2.9545 4.0760 0.2319  -0.3900 -0.2648 209  PHE Y CD2 
24550 C CE1 . PHE D 81   ? 3.5621 2.8844 4.1810 0.2566  -0.4561 -0.2540 209  PHE Y CE1 
24551 C CE2 . PHE D 81   ? 3.4918 2.9275 4.0673 0.2463  -0.3975 -0.2549 209  PHE Y CE2 
24552 C CZ  . PHE D 81   ? 3.5204 2.8981 4.1259 0.2584  -0.4300 -0.2497 209  PHE Y CZ  
24553 N N   . GLU D 82   ? 3.7890 3.0299 4.2445 0.2508  -0.4851 -0.2450 210  GLU Y N   
24554 C CA  . GLU D 82   ? 3.8902 3.0537 4.3469 0.2635  -0.5260 -0.2376 210  GLU Y CA  
24555 C C   . GLU D 82   ? 3.9497 3.0668 4.3396 0.2658  -0.5418 -0.2308 210  GLU Y C   
24556 O O   . GLU D 82   ? 4.0128 3.0674 4.4089 0.2679  -0.5702 -0.2320 210  GLU Y O   
24557 C CB  . GLU D 82   ? 3.9716 3.1193 4.4270 0.2825  -0.5439 -0.2229 210  GLU Y CB  
24558 C CG  . GLU D 82   ? 4.1099 3.2210 4.4883 0.2979  -0.5628 -0.2044 210  GLU Y CG  
24559 C CD  . GLU D 82   ? 4.1577 3.3217 4.4775 0.2971  -0.5343 -0.1974 210  GLU Y CD  
24560 O OE1 . GLU D 82   ? 4.1096 3.3404 4.4505 0.2883  -0.5027 -0.2043 210  GLU Y OE1 
24561 O OE2 . GLU D 82   ? 4.2417 3.3792 4.4939 0.3053  -0.5437 -0.1850 210  GLU Y OE2 
24562 N N   . ARG D 83   ? 3.9370 3.0837 4.2631 0.2657  -0.5232 -0.2236 211  ARG Y N   
24563 C CA  . ARG D 83   ? 3.9382 3.0451 4.1961 0.2676  -0.5330 -0.2168 211  ARG Y CA  
24564 C C   . ARG D 83   ? 3.9236 3.0333 4.1869 0.2496  -0.5201 -0.2318 211  ARG Y C   
24565 O O   . ARG D 83   ? 3.9593 3.0232 4.1776 0.2496  -0.5320 -0.2291 211  ARG Y O   
24566 C CB  . ARG D 83   ? 3.8896 3.0298 4.0817 0.2736  -0.5157 -0.2045 211  ARG Y CB  
24567 C CG  . ARG D 83   ? 3.8528 3.0793 4.0559 0.2620  -0.4758 -0.2123 211  ARG Y CG  
24568 C CD  . ARG D 83   ? 3.8248 3.0816 3.9639 0.2687  -0.4610 -0.1998 211  ARG Y CD  
24569 N NE  . ARG D 83   ? 3.7212 2.9532 3.8393 0.2884  -0.4802 -0.1824 211  ARG Y NE  
24570 C CZ  . ARG D 83   ? 3.6731 2.9410 3.8162 0.2954  -0.4735 -0.1781 211  ARG Y CZ  
24571 N NH1 . ARG D 83   ? 3.7044 3.0332 3.8927 0.2842  -0.4480 -0.1899 211  ARG Y NH1 
24572 N NH2 . ARG D 83   ? 3.6123 2.8537 3.7339 0.3134  -0.4919 -0.1621 211  ARG Y NH2 
24573 N N   . MET D 84   ? 4.7198 3.8818 5.0370 0.2341  -0.4951 -0.2477 212  MET Y N   
24574 C CA  . MET D 84   ? 4.6965 3.8672 5.0260 0.2156  -0.4801 -0.2635 212  MET Y CA  
24575 C C   . MET D 84   ? 4.7107 3.8079 5.0566 0.2159  -0.5107 -0.2672 212  MET Y C   
24576 O O   . MET D 84   ? 4.7351 3.8273 5.0874 0.2020  -0.5029 -0.2791 212  MET Y O   
24577 C CB  . MET D 84   ? 4.6100 3.8466 4.9999 0.1996  -0.4495 -0.2800 212  MET Y CB  
24578 C CG  . MET D 84   ? 4.5734 3.8867 4.9375 0.1913  -0.4122 -0.2822 212  MET Y CG  
24579 S SD  . MET D 84   ? 4.2120 3.5949 4.6438 0.1716  -0.3774 -0.3025 212  MET Y SD  
24580 C CE  . MET D 84   ? 2.9543 2.4166 3.3399 0.1666  -0.3416 -0.3007 212  MET Y CE  
24581 N N   . GLY D 85   ? 4.0928 3.1331 4.4460 0.2319  -0.5459 -0.2571 213  GLY Y N   
24582 C CA  . GLY D 85   ? 4.1190 3.0827 4.4793 0.2352  -0.5799 -0.2580 213  GLY Y CA  
24583 C C   . GLY D 85   ? 4.1971 3.1061 4.4754 0.2432  -0.5964 -0.2458 213  GLY Y C   
24584 O O   . GLY D 85   ? 4.2384 3.0911 4.5045 0.2409  -0.6149 -0.2487 213  GLY Y O   
24585 N N   . ASP D 86   ? 4.8721 3.7970 5.0937 0.2526  -0.5890 -0.2321 214  ASP Y N   
24586 C CA  . ASP D 86   ? 4.9253 3.8046 5.0640 0.2602  -0.5991 -0.2197 214  ASP Y CA  
24587 C C   . ASP D 86   ? 4.9669 3.8374 5.0814 0.2454  -0.5857 -0.2297 214  ASP Y C   
24588 O O   . ASP D 86   ? 4.9420 3.8678 5.0871 0.2289  -0.5562 -0.2439 214  ASP Y O   
24589 C CB  . ASP D 86   ? 4.8490 3.7729 4.9395 0.2668  -0.5786 -0.2080 214  ASP Y CB  
24590 C CG  . ASP D 86   ? 4.8474 3.7121 4.8676 0.2840  -0.6021 -0.1895 214  ASP Y CG  
24591 O OD1 . ASP D 86   ? 4.8770 3.6779 4.8548 0.2851  -0.6191 -0.1870 214  ASP Y OD1 
24592 O OD2 . ASP D 86   ? 4.8199 3.7011 4.8256 0.2963  -0.6028 -0.1774 214  ASP Y OD2 
24593 N N   . VAL D 87   ? 4.9925 3.7916 5.0512 0.2513  -0.6070 -0.2224 215  VAL Y N   
24594 C CA  . VAL D 87   ? 4.9560 3.7394 4.9861 0.2383  -0.5952 -0.2308 215  VAL Y CA  
24595 C C   . VAL D 87   ? 4.9571 3.7096 4.8970 0.2446  -0.5926 -0.2183 215  VAL Y C   
24596 O O   . VAL D 87   ? 4.9748 3.6858 4.8740 0.2611  -0.6141 -0.2026 215  VAL Y O   
24597 C CB  . VAL D 87   ? 5.4425 4.1593 5.5003 0.2362  -0.6241 -0.2379 215  VAL Y CB  
24598 C CG1 . VAL D 87   ? 5.3949 4.1503 5.5438 0.2257  -0.6181 -0.2535 215  VAL Y CG1 
24599 C CG2 . VAL D 87   ? 5.4948 4.1300 5.5304 0.2553  -0.6685 -0.2239 215  VAL Y CG2 
24600 N N   . LEU D 88   ? 5.2101 3.9826 5.1196 0.2313  -0.5655 -0.2255 216  LEU Y N   
24601 C CA  . LEU D 88   ? 5.1959 3.9480 5.0229 0.2355  -0.5565 -0.2150 216  LEU Y CA  
24602 C C   . LEU D 88   ? 5.1825 3.8778 4.9679 0.2281  -0.5585 -0.2194 216  LEU Y C   
24603 O O   . LEU D 88   ? 5.1501 3.8464 4.9723 0.2149  -0.5544 -0.2337 216  LEU Y O   
24604 C CB  . LEU D 88   ? 5.1331 3.9704 4.9504 0.2282  -0.5167 -0.2169 216  LEU Y CB  
24605 C CG  . LEU D 88   ? 5.0678 3.9609 4.9062 0.2370  -0.5107 -0.2095 216  LEU Y CG  
24606 C CD1 . LEU D 88   ? 5.0985 3.9352 4.9043 0.2579  -0.5420 -0.1912 216  LEU Y CD1 
24607 C CD2 . LEU D 88   ? 4.9787 3.9212 4.9002 0.2298  -0.5062 -0.2215 216  LEU Y CD2 
24608 N N   . ASN D 89   ? 5.4229 4.0682 5.1306 0.2367  -0.5637 -0.2069 217  ASN Y N   
24609 C CA  . ASN D 89   ? 5.4440 4.0258 5.1015 0.2318  -0.5665 -0.2088 217  ASN Y CA  
24610 C C   . ASN D 89   ? 5.4262 4.0543 5.0554 0.2174  -0.5254 -0.2163 217  ASN Y C   
24611 O O   . ASN D 89   ? 5.4024 4.0744 5.0039 0.2196  -0.5036 -0.2102 217  ASN Y O   
24612 C CB  . ASN D 89   ? 5.5159 4.0087 5.1014 0.2489  -0.5954 -0.1915 217  ASN Y CB  
24613 C CG  . ASN D 89   ? 5.5532 4.0115 5.1621 0.2654  -0.6337 -0.1816 217  ASN Y CG  
24614 O OD1 . ASN D 89   ? 5.5321 4.0209 5.2140 0.2635  -0.6422 -0.1890 217  ASN Y OD1 
24615 N ND2 . ASN D 89   ? 5.6093 4.0026 5.1565 0.2814  -0.6564 -0.1653 217  ASN Y ND2 
24616 N N   . SER D 90   ? 4.1566 2.7733 3.7930 0.2029  -0.5156 -0.2296 218  SER Y N   
24617 C CA  . SER D 90   ? 4.1739 2.8445 3.7998 0.1865  -0.4750 -0.2404 218  SER Y CA  
24618 C C   . SER D 90   ? 4.2648 2.9185 3.8124 0.1900  -0.4588 -0.2309 218  SER Y C   
24619 O O   . SER D 90   ? 4.2302 2.9506 3.7722 0.1857  -0.4290 -0.2317 218  SER Y O   
24620 C CB  . SER D 90   ? 4.1378 2.7912 3.7853 0.1709  -0.4699 -0.2561 218  SER Y CB  
24621 O OG  . SER D 90   ? 4.0694 2.7820 3.7970 0.1603  -0.4627 -0.2700 218  SER Y OG  
24622 N N   . LYS D 91   ? 3.2369 1.8003 2.7240 0.1977  -0.4781 -0.2223 219  LYS Y N   
24623 C CA  . LYS D 91   ? 3.3643 1.9036 2.7754 0.1992  -0.4603 -0.2150 219  LYS Y CA  
24624 C C   . LYS D 91   ? 3.3078 1.8368 2.6771 0.2168  -0.4692 -0.1965 219  LYS Y C   
24625 O O   . LYS D 91   ? 3.3689 1.8779 2.6744 0.2202  -0.4552 -0.1884 219  LYS Y O   
24626 C CB  . LYS D 91   ? 3.6174 2.0640 2.9786 0.1977  -0.4726 -0.2152 219  LYS Y CB  
24627 C CG  . LYS D 91   ? 3.8714 2.3257 3.2771 0.1810  -0.4660 -0.2333 219  LYS Y CG  
24628 C CD  . LYS D 91   ? 3.8800 2.3245 3.3498 0.1842  -0.4975 -0.2367 219  LYS Y CD  
24629 C CE  . LYS D 91   ? 3.9545 2.4195 3.4771 0.1670  -0.4876 -0.2553 219  LYS Y CE  
24630 N NZ  . LYS D 91   ? 3.9894 2.4314 3.5697 0.1718  -0.5213 -0.2574 219  LYS Y NZ  
24631 N N   . ASP D 92   ? 4.1948 2.7393 3.6031 0.2274  -0.4910 -0.1904 220  ASP Y N   
24632 C CA  . ASP D 92   ? 4.1405 2.6810 3.5189 0.2443  -0.5007 -0.1735 220  ASP Y CA  
24633 C C   . ASP D 92   ? 4.0587 2.6856 3.4380 0.2409  -0.4653 -0.1731 220  ASP Y C   
24634 O O   . ASP D 92   ? 4.1029 2.7186 3.4239 0.2466  -0.4530 -0.1632 220  ASP Y O   
24635 C CB  . ASP D 92   ? 4.1136 2.6514 3.5416 0.2552  -0.5324 -0.1691 220  ASP Y CB  
24636 C CG  . ASP D 92   ? 4.1679 2.6058 3.5770 0.2654  -0.5746 -0.1629 220  ASP Y CG  
24637 O OD1 . ASP D 92   ? 4.2192 2.5917 3.5820 0.2622  -0.5788 -0.1639 220  ASP Y OD1 
24638 O OD2 . ASP D 92   ? 4.1663 2.5896 3.6061 0.2768  -0.6039 -0.1570 220  ASP Y OD2 
24639 N N   . ILE D 93   ? 5.6463 4.3580 5.0925 0.2316  -0.4494 -0.1842 221  ILE Y N   
24640 C CA  . ILE D 93   ? 5.5421 4.3419 4.9989 0.2285  -0.4187 -0.1848 221  ILE Y CA  
24641 C C   . ILE D 93   ? 5.4940 4.2950 4.8912 0.2248  -0.3914 -0.1826 221  ILE Y C   
24642 O O   . ILE D 93   ? 5.5279 4.2915 4.8978 0.2157  -0.3835 -0.1892 221  ILE Y O   
24643 C CB  . ILE D 93   ? 4.9642 3.8474 4.4931 0.2123  -0.3983 -0.2025 221  ILE Y CB  
24644 C CG1 . ILE D 93   ? 4.9063 3.7816 4.4964 0.2146  -0.4240 -0.2063 221  ILE Y CG1 
24645 C CG2 . ILE D 93   ? 4.9655 3.9391 4.5075 0.2107  -0.3707 -0.2023 221  ILE Y CG2 
24646 C CD1 . ILE D 93   ? 4.8152 3.7700 4.4766 0.1995  -0.4044 -0.2230 221  ILE Y CD1 
24647 N N   . ASN D 94   ? 5.0793 3.9219 4.4570 0.2320  -0.3769 -0.1733 222  ASN Y N   
24648 C CA  . ASN D 94   ? 5.0577 3.9063 4.3832 0.2290  -0.3497 -0.1711 222  ASN Y CA  
24649 C C   . ASN D 94   ? 4.9944 3.9412 4.3516 0.2150  -0.3128 -0.1834 222  ASN Y C   
24650 O O   . ASN D 94   ? 4.9517 3.9074 4.2974 0.2015  -0.2893 -0.1941 222  ASN Y O   
24651 C CB  . ASN D 94   ? 2.8777 1.6951 2.1493 0.2469  -0.3577 -0.1516 222  ASN Y CB  
24652 C CG  . ASN D 94   ? 2.9011 1.7070 2.1133 0.2447  -0.3321 -0.1485 222  ASN Y CG  
24653 O OD1 . ASN D 94   ? 2.8722 1.7472 2.0895 0.2409  -0.3041 -0.1504 222  ASN Y OD1 
24654 N ND2 . ASN D 94   ? 2.9552 1.6721 2.1105 0.2471  -0.3415 -0.1440 222  ASN Y ND2 
24655 N N   . LYS D 95   ? 5.5493 4.5682 4.9456 0.2183  -0.3080 -0.1820 223  LYS Y N   
24656 C CA  . LYS D 95   ? 5.4758 4.5896 4.9008 0.2068  -0.2755 -0.1924 223  LYS Y CA  
24657 C C   . LYS D 95   ? 5.3431 4.5245 4.8248 0.2090  -0.2784 -0.1937 223  LYS Y C   
24658 O O   . LYS D 95   ? 5.3550 4.5361 4.8306 0.2242  -0.2917 -0.1798 223  LYS Y O   
24659 C CB  . LYS D 95   ? 3.3940 2.5235 2.7712 0.2122  -0.2554 -0.1834 223  LYS Y CB  
24660 C CG  . LYS D 95   ? 3.4091 2.4861 2.7323 0.2072  -0.2431 -0.1845 223  LYS Y CG  
24661 C CD  . LYS D 95   ? 3.4160 2.4941 2.6889 0.2164  -0.2284 -0.1722 223  LYS Y CD  
24662 C CE  . LYS D 95   ? 3.4452 2.4711 2.6655 0.2102  -0.2128 -0.1745 223  LYS Y CE  
24663 N NZ  . LYS D 95   ? 3.4786 2.4040 2.6652 0.2132  -0.2364 -0.1712 223  LYS Y NZ  
24664 N N   . ILE D 96   ? 3.9391 3.1772 3.4747 0.1937  -0.2653 -0.2104 224  ILE Y N   
24665 C CA  . ILE D 96   ? 3.9127 3.2181 3.4998 0.1945  -0.2638 -0.2127 224  ILE Y CA  
24666 C C   . ILE D 96   ? 3.9634 3.3432 3.5425 0.1947  -0.2387 -0.2108 224  ILE Y C   
24667 O O   . ILE D 96   ? 3.9919 3.3847 3.5427 0.1879  -0.2178 -0.2144 224  ILE Y O   
24668 C CB  . ILE D 96   ? 3.6370 2.9756 3.2838 0.1777  -0.2577 -0.2316 224  ILE Y CB  
24669 C CG1 . ILE D 96   ? 3.6423 2.9062 3.2973 0.1767  -0.2818 -0.2344 224  ILE Y CG1 
24670 C CG2 . ILE D 96   ? 3.5630 2.9625 3.2605 0.1793  -0.2573 -0.2332 224  ILE Y CG2 
24671 C CD1 . ILE D 96   ? 3.5604 2.8527 3.2749 0.1604  -0.2759 -0.2528 224  ILE Y CD1 
24672 N N   . GLU D 97   ? 6.0687 5.4960 5.6730 0.2025  -0.2409 -0.2052 225  GLU Y N   
24673 C CA  . GLU D 97   ? 6.1095 5.6055 5.7060 0.2050  -0.2204 -0.2016 225  GLU Y CA  
24674 C C   . GLU D 97   ? 6.0958 5.6554 5.7370 0.2072  -0.2192 -0.2025 225  GLU Y C   
24675 O O   . GLU D 97   ? 6.1074 5.6464 5.7575 0.2204  -0.2392 -0.1918 225  GLU Y O   
24676 C CB  . GLU D 97   ? 4.0251 3.4851 3.5658 0.2220  -0.2267 -0.1826 225  GLU Y CB  
24677 C CG  . GLU D 97   ? 4.0874 3.4968 3.5780 0.2190  -0.2198 -0.1819 225  GLU Y CG  
24678 C CD  . GLU D 97   ? 4.1129 3.4560 3.5482 0.2370  -0.2356 -0.1624 225  GLU Y CD  
24679 O OE1 . GLU D 97   ? 4.1196 3.4586 3.5565 0.2520  -0.2522 -0.1493 225  GLU Y OE1 
24680 O OE2 . GLU D 97   ? 4.1278 3.4215 3.5173 0.2359  -0.2306 -0.1605 225  GLU Y OE2 
24681 N N   . VAL D 98   ? 4.4952 4.1310 4.1629 0.1943  -0.1954 -0.2153 226  VAL Y N   
24682 C CA  . VAL D 98   ? 4.4501 4.1480 4.1586 0.1945  -0.1914 -0.2178 226  VAL Y CA  
24683 C C   . VAL D 98   ? 4.4812 4.2423 4.1746 0.1999  -0.1752 -0.2117 226  VAL Y C   
24684 O O   . VAL D 98   ? 4.4898 4.2626 4.1523 0.1978  -0.1609 -0.2114 226  VAL Y O   
24685 C CB  . VAL D 98   ? 4.8362 4.5736 4.5936 0.1748  -0.1785 -0.2386 226  VAL Y CB  
24686 C CG1 . VAL D 98   ? 4.7702 4.5588 4.5688 0.1759  -0.1768 -0.2406 226  VAL Y CG1 
24687 C CG2 . VAL D 98   ? 4.8409 4.5168 4.6130 0.1683  -0.1927 -0.2457 226  VAL Y CG2 
24688 N N   . THR D 99   ? 4.4227 4.2234 4.1390 0.2070  -0.1773 -0.2071 227  THR Y N   
24689 C CA  . THR D 99   ? 4.4570 4.3205 4.1636 0.2127  -0.1635 -0.2015 227  THR Y CA  
24690 C C   . THR D 99   ? 4.4559 4.3790 4.2054 0.2079  -0.1568 -0.2090 227  THR Y C   
24691 O O   . THR D 99   ? 4.4489 4.3535 4.2243 0.2126  -0.1703 -0.2067 227  THR Y O   
24692 C CB  . THR D 99   ? 4.4572 4.2924 4.1279 0.2342  -0.1769 -0.1797 227  THR Y CB  
24693 O OG1 . THR D 99   ? 4.5043 4.2805 4.1318 0.2385  -0.1823 -0.1727 227  THR Y OG1 
24694 C CG2 . THR D 99   ? 4.4392 4.3399 4.1007 0.2401  -0.1625 -0.1740 227  THR Y CG2 
24695 N N   . LEU D 100  ? 5.0260 5.0191 4.7826 0.1988  -0.1358 -0.2181 228  LEU Y N   
24696 C CA  . LEU D 100  ? 4.9574 5.0054 4.7540 0.1898  -0.1264 -0.2293 228  LEU Y CA  
24697 C C   . LEU D 100  ? 4.9197 5.0214 4.7130 0.2001  -0.1213 -0.2206 228  LEU Y C   
24698 O O   . LEU D 100  ? 4.9410 5.0700 4.7064 0.2059  -0.1139 -0.2138 228  LEU Y O   
24699 C CB  . LEU D 100  ? 2.4586 2.5460 2.2720 0.1682  -0.1066 -0.2500 228  LEU Y CB  
24700 C CG  . LEU D 100  ? 2.5245 2.5639 2.3364 0.1569  -0.1081 -0.2594 228  LEU Y CG  
24701 C CD1 . LEU D 100  ? 2.4681 2.5499 2.3063 0.1347  -0.0887 -0.2813 228  LEU Y CD1 
24702 C CD2 . LEU D 100  ? 2.5328 2.5061 2.3597 0.1616  -0.1290 -0.2556 228  LEU Y CD2 
24703 N N   . LYS D 101  ? 5.5473 5.6633 5.3700 0.2021  -0.1246 -0.2211 229  LYS Y N   
24704 C CA  . LYS D 101  ? 5.4787 5.6474 5.3008 0.2102  -0.1184 -0.2147 229  LYS Y CA  
24705 C C   . LYS D 101  ? 5.2854 5.5065 5.1423 0.1964  -0.1042 -0.2301 229  LYS Y C   
24706 O O   . LYS D 101  ? 5.2231 5.4282 5.1122 0.1927  -0.1082 -0.2355 229  LYS Y O   
24707 C CB  . LYS D 101  ? 2.9482 3.0856 2.7660 0.2297  -0.1353 -0.1968 229  LYS Y CB  
24708 C CG  . LYS D 101  ? 2.8509 3.0399 2.6786 0.2354  -0.1282 -0.1935 229  LYS Y CG  
24709 C CD  . LYS D 101  ? 2.8660 3.0301 2.6787 0.2569  -0.1428 -0.1732 229  LYS Y CD  
24710 C CE  . LYS D 101  ? 2.7736 2.9917 2.5868 0.2638  -0.1340 -0.1682 229  LYS Y CE  
24711 N NZ  . LYS D 101  ? 2.7897 2.9823 2.5862 0.2853  -0.1477 -0.1479 229  LYS Y NZ  
24712 N N   . GLN D 102  ? 4.1167 4.3993 3.9669 0.1892  -0.0876 -0.2373 230  GLN Y N   
24713 C CA  . GLN D 102  ? 3.9479 4.2838 3.8241 0.1774  -0.0736 -0.2507 230  GLN Y CA  
24714 C C   . GLN D 102  ? 3.8774 4.2483 3.7451 0.1909  -0.0732 -0.2392 230  GLN Y C   
24715 O O   . GLN D 102  ? 3.7917 4.2204 3.6579 0.1857  -0.0604 -0.2454 230  GLN Y O   
24716 C CB  . GLN D 102  ? 3.8827 4.2656 3.7590 0.1597  -0.0561 -0.2675 230  GLN Y CB  
24717 C CG  . GLN D 102  ? 3.8721 4.2275 3.7643 0.1427  -0.0528 -0.2828 230  GLN Y CG  
24718 C CD  . GLN D 102  ? 3.8085 4.2119 3.7012 0.1252  -0.0350 -0.2996 230  GLN Y CD  
24719 O OE1 . GLN D 102  ? 3.7373 4.1993 3.6324 0.1207  -0.0238 -0.3056 230  GLN Y OE1 
24720 N NE2 . GLN D 102  ? 3.8460 4.2235 3.7360 0.1153  -0.0325 -0.3075 230  GLN Y NE2 
# 
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  ?    ?   ?   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 ?    ?   ?   A . n 
A 1 1516 ILE 1516 1516 ?    ?   ?   A . n 
A 1 1517 GLN 1517 1517 ?    ?   ?   A . n 
A 1 1518 LYS 1518 1518 ?    ?   ?   A . n 
A 1 1519 VAL 1519 1519 ?    ?   ?   A . n 
A 1 1520 CYS 1520 1520 ?    ?   ?   A . n 
A 1 1521 GLU 1521 1521 ?    ?   ?   A . n 
A 1 1522 GLY 1522 1522 ?    ?   ?   A . n 
A 1 1523 ALA 1523 1523 ?    ?   ?   A . n 
A 1 1524 ALA 1524 1524 ?    ?   ?   A . n 
A 1 1525 CYS 1525 1525 ?    ?   ?   A . n 
A 1 1526 LYS 1526 1526 ?    ?   ?   A . n 
A 1 1527 CYS 1527 1527 ?    ?   ?   A . n 
A 1 1528 VAL 1528 1528 ?    ?   ?   A . n 
A 1 1529 GLU 1529 1529 ?    ?   ?   A . n 
A 1 1530 ALA 1530 1530 ?    ?   ?   A . n 
A 1 1531 ASP 1531 1531 ?    ?   ?   A . n 
A 1 1532 CYS 1532 1532 ?    ?   ?   A . n 
A 1 1533 GLY 1533 1533 ?    ?   ?   A . n 
A 1 1534 GLN 1534 1534 ?    ?   ?   A . n 
A 1 1535 MET 1535 1535 ?    ?   ?   A . n 
A 1 1536 GLN 1536 1536 ?    ?   ?   A . n 
A 1 1537 GLU 1537 1537 ?    ?   ?   A . n 
A 1 1538 GLU 1538 1538 ?    ?   ?   A . n 
A 1 1539 LEU 1539 1539 ?    ?   ?   A . n 
A 1 1540 ASP 1540 1540 ?    ?   ?   A . n 
A 1 1541 LEU 1541 1541 ?    ?   ?   A . n 
A 1 1542 THR 1542 1542 ?    ?   ?   A . n 
A 1 1543 ILE 1543 1543 ?    ?   ?   A . n 
A 1 1544 SER 1544 1544 ?    ?   ?   A . n 
A 1 1545 ALA 1545 1545 ?    ?   ?   A . n 
A 1 1546 GLU 1546 1546 ?    ?   ?   A . n 
A 1 1547 THR 1547 1547 ?    ?   ?   A . n 
A 1 1548 ARG 1548 1548 ?    ?   ?   A . n 
A 1 1549 LYS 1549 1549 ?    ?   ?   A . n 
A 1 1550 GLN 1550 1550 ?    ?   ?   A . n 
A 1 1551 THR 1551 1551 ?    ?   ?   A . n 
A 1 1552 ALA 1552 1552 ?    ?   ?   A . n 
A 1 1553 CYS 1553 1553 ?    ?   ?   A . n 
A 1 1554 LYS 1554 1554 ?    ?   ?   A . n 
A 1 1555 PRO 1555 1555 ?    ?   ?   A . n 
A 1 1556 GLU 1556 1556 ?    ?   ?   A . n 
A 1 1557 ILE 1557 1557 ?    ?   ?   A . n 
A 1 1558 ALA 1558 1558 ?    ?   ?   A . n 
A 1 1559 TYR 1559 1559 ?    ?   ?   A . n 
A 1 1560 ALA 1560 1560 ?    ?   ?   A . n 
A 1 1561 TYR 1561 1561 ?    ?   ?   A . n 
A 1 1562 LYS 1562 1562 ?    ?   ?   A . n 
A 1 1563 VAL 1563 1563 ?    ?   ?   A . n 
A 1 1564 SER 1564 1564 ?    ?   ?   A . n 
A 1 1565 ILE 1565 1565 ?    ?   ?   A . n 
A 1 1566 THR 1566 1566 ?    ?   ?   A . n 
A 1 1567 SER 1567 1567 ?    ?   ?   A . n 
A 1 1568 ILE 1568 1568 ?    ?   ?   A . n 
A 1 1569 THR 1569 1569 ?    ?   ?   A . n 
A 1 1570 VAL 1570 1570 ?    ?   ?   A . n 
A 1 1571 GLU 1571 1571 ?    ?   ?   A . n 
A 1 1572 ASN 1572 1572 ?    ?   ?   A . n 
A 1 1573 VAL 1573 1573 ?    ?   ?   A . n 
A 1 1574 PHE 1574 1574 ?    ?   ?   A . n 
A 1 1575 VAL 1575 1575 ?    ?   ?   A . n 
A 1 1576 LYS 1576 1576 ?    ?   ?   A . n 
A 1 1577 TYR 1577 1577 ?    ?   ?   A . n 
A 1 1578 LYS 1578 1578 ?    ?   ?   A . n 
A 1 1579 ALA 1579 1579 ?    ?   ?   A . n 
A 1 1580 THR 1580 1580 ?    ?   ?   A . n 
A 1 1581 LEU 1581 1581 ?    ?   ?   A . n 
A 1 1582 LEU 1582 1582 ?    ?   ?   A . n 
A 1 1583 ASP 1583 1583 ?    ?   ?   A . n 
A 1 1584 ILE 1584 1584 ?    ?   ?   A . n 
A 1 1585 TYR 1585 1585 ?    ?   ?   A . n 
A 1 1586 LYS 1586 1586 ?    ?   ?   A . n 
A 1 1587 THR 1587 1587 ?    ?   ?   A . n 
A 1 1588 GLY 1588 1588 ?    ?   ?   A . n 
A 1 1589 GLU 1589 1589 ?    ?   ?   A . n 
A 1 1590 ALA 1590 1590 ?    ?   ?   A . n 
A 1 1591 VAL 1591 1591 ?    ?   ?   A . n 
A 1 1592 ALA 1592 1592 ?    ?   ?   A . n 
A 1 1593 GLU 1593 1593 ?    ?   ?   A . n 
A 1 1594 LYS 1594 1594 ?    ?   ?   A . n 
A 1 1595 ASP 1595 1595 ?    ?   ?   A . n 
A 1 1596 SER 1596 1596 ?    ?   ?   A . n 
A 1 1597 GLU 1597 1597 ?    ?   ?   A . n 
A 1 1598 ILE 1598 1598 ?    ?   ?   A . n 
A 1 1599 THR 1599 1599 ?    ?   ?   A . n 
A 1 1600 PHE 1600 1600 ?    ?   ?   A . n 
A 1 1601 ILE 1601 1601 ?    ?   ?   A . n 
A 1 1602 LYS 1602 1602 ?    ?   ?   A . n 
A 1 1603 LYS 1603 1603 ?    ?   ?   A . n 
A 1 1604 VAL 1604 1604 ?    ?   ?   A . n 
A 1 1605 THR 1605 1605 ?    ?   ?   A . n 
A 1 1606 CYS 1606 1606 ?    ?   ?   A . n 
A 1 1607 THR 1607 1607 ?    ?   ?   A . n 
A 1 1608 ASN 1608 1608 ?    ?   ?   A . n 
A 1 1609 ALA 1609 1609 ?    ?   ?   A . n 
A 1 1610 GLU 1610 1610 ?    ?   ?   A . n 
A 1 1611 LEU 1611 1611 ?    ?   ?   A . n 
A 1 1612 VAL 1612 1612 ?    ?   ?   A . n 
A 1 1613 LYS 1613 1613 ?    ?   ?   A . n 
A 1 1614 GLY 1614 1614 ?    ?   ?   A . n 
A 1 1615 ARG 1615 1615 ?    ?   ?   A . n 
A 1 1616 GLN 1616 1616 ?    ?   ?   A . n 
A 1 1617 TYR 1617 1617 ?    ?   ?   A . n 
A 1 1618 LEU 1618 1618 ?    ?   ?   A . n 
A 1 1619 ILE 1619 1619 ?    ?   ?   A . n 
A 1 1620 MET 1620 1620 ?    ?   ?   A . n 
A 1 1621 GLY 1621 1621 ?    ?   ?   A . n 
A 1 1622 LYS 1622 1622 ?    ?   ?   A . n 
A 1 1623 GLU 1623 1623 ?    ?   ?   A . n 
A 1 1624 ALA 1624 1624 ?    ?   ?   A . n 
A 1 1625 LEU 1625 1625 ?    ?   ?   A . n 
A 1 1626 GLN 1626 1626 ?    ?   ?   A . n 
A 1 1627 ILE 1627 1627 ?    ?   ?   A . n 
A 1 1628 LYS 1628 1628 ?    ?   ?   A . n 
A 1 1629 TYR 1629 1629 ?    ?   ?   A . n 
A 1 1630 ASN 1630 1630 ?    ?   ?   A . n 
A 1 1631 PHE 1631 1631 ?    ?   ?   A . n 
A 1 1632 SER 1632 1632 ?    ?   ?   A . n 
A 1 1633 PHE 1633 1633 ?    ?   ?   A . n 
A 1 1634 ARG 1634 1634 ?    ?   ?   A . n 
A 1 1635 TYR 1635 1635 ?    ?   ?   A . n 
A 1 1636 ILE 1636 1636 ?    ?   ?   A . n 
A 1 1637 TYR 1637 1637 ?    ?   ?   A . n 
A 1 1638 PRO 1638 1638 ?    ?   ?   A . n 
A 1 1639 LEU 1639 1639 ?    ?   ?   A . n 
A 1 1640 ASP 1640 1640 ?    ?   ?   A . n 
A 1 1641 SER 1641 1641 ?    ?   ?   A . n 
A 1 1642 LEU 1642 1642 ?    ?   ?   A . n 
A 1 1643 THR 1643 1643 ?    ?   ?   A . n 
A 1 1644 TRP 1644 1644 ?    ?   ?   A . n 
A 1 1645 ILE 1645 1645 ?    ?   ?   A . n 
A 1 1646 GLU 1646 1646 ?    ?   ?   A . n 
A 1 1647 TYR 1647 1647 ?    ?   ?   A . n 
A 1 1648 TRP 1648 1648 ?    ?   ?   A . n 
A 1 1649 PRO 1649 1649 ?    ?   ?   A . n 
A 1 1650 ARG 1650 1650 ?    ?   ?   A . n 
A 1 1651 ASP 1651 1651 ?    ?   ?   A . n 
A 1 1652 THR 1652 1652 ?    ?   ?   A . n 
A 1 1653 THR 1653 1653 ?    ?   ?   A . n 
A 1 1654 CYS 1654 1654 ?    ?   ?   A . n 
A 1 1655 SER 1655 1655 ?    ?   ?   A . n 
A 1 1656 SER 1656 1656 ?    ?   ?   A . n 
A 1 1657 CYS 1657 1657 ?    ?   ?   A . n 
A 1 1658 GLN 1658 1658 ?    ?   ?   A . n 
A 1 1659 ALA 1659 1659 ?    ?   ?   A . n 
A 1 1660 PHE 1660 1660 ?    ?   ?   A . n 
A 1 1661 LEU 1661 1661 ?    ?   ?   A . n 
A 1 1662 ALA 1662 1662 ?    ?   ?   A . n 
A 1 1663 ASN 1663 1663 ?    ?   ?   A . n 
A 1 1664 LEU 1664 1664 ?    ?   ?   A . n 
A 1 1665 ASP 1665 1665 ?    ?   ?   A . n 
A 1 1666 GLU 1666 1666 ?    ?   ?   A . n 
A 1 1667 PHE 1667 1667 ?    ?   ?   A . n 
A 1 1668 ALA 1668 1668 ?    ?   ?   A . n 
A 1 1669 GLU 1669 1669 ?    ?   ?   A . n 
A 1 1670 ASP 1670 1670 ?    ?   ?   A . n 
A 1 1671 ILE 1671 1671 ?    ?   ?   A . n 
A 1 1672 PHE 1672 1672 ?    ?   ?   A . n 
A 1 1673 LEU 1673 1673 ?    ?   ?   A . n 
A 1 1674 ASN 1674 1674 ?    ?   ?   A . n 
A 1 1675 GLY 1675 1675 ?    ?   ?   A . n 
A 1 1676 CYS 1676 1676 ?    ?   ?   A . n 
B 2 1    SER 1    129  129  SER SER X . n 
B 2 2    SER 2    130  130  SER SER X . n 
B 2 3    GLU 3    131  131  GLU GLU X . n 
B 2 4    THR 4    132  132  THR THR X . n 
B 2 5    ASN 5    133  133  ASN ASN X . n 
B 2 6    THR 6    134  134  THR THR X . n 
B 2 7    HIS 7    135  135  HIS HIS X . n 
B 2 8    LEU 8    136  136  LEU LEU X . n 
B 2 9    PHE 9    137  137  PHE PHE X . n 
B 2 10   VAL 10   138  138  VAL VAL X . n 
B 2 11   ASN 11   139  139  ASN ASN X . n 
B 2 12   LYS 12   140  140  LYS LYS X . n 
B 2 13   VAL 13   141  141  VAL VAL X . n 
B 2 14   TYR 14   142  142  TYR TYR X . n 
B 2 15   GLY 15   143  143  GLY GLY X . n 
B 2 16   GLY 16   144  144  GLY GLY X . n 
B 2 17   ASN 17   145  145  ASN ASN X . n 
B 2 18   LEU 18   146  146  LEU LEU X . n 
B 2 19   ASP 19   147  147  ASP ASP X . n 
B 2 20   ALA 20   148  148  ALA ALA X . n 
B 2 21   SER 21   149  149  SER SER X . n 
B 2 22   ILE 22   150  150  ILE ILE X . n 
B 2 23   ASP 23   151  151  ASP ASP X . n 
B 2 24   SER 24   152  152  SER SER X . n 
B 2 25   PHE 25   153  153  PHE PHE X . n 
B 2 26   SER 26   154  154  SER SER X . n 
B 2 27   ILE 27   155  155  ILE ILE X . n 
B 2 28   ASN 28   156  156  ASN ASN X . n 
B 2 29   LYS 29   157  157  LYS LYS X . n 
B 2 30   GLU 30   158  158  GLU GLU X . n 
B 2 31   GLU 31   159  159  GLU GLU X . n 
B 2 32   VAL 32   160  160  VAL VAL X . n 
B 2 33   SER 33   161  161  SER SER X . n 
B 2 34   LEU 34   162  162  LEU LEU X . n 
B 2 35   LYS 35   163  163  LYS LYS X . n 
B 2 36   GLU 36   164  164  GLU GLU X . n 
B 2 37   LEU 37   165  165  LEU LEU X . n 
B 2 38   ASP 38   166  166  ASP ASP X . n 
B 2 39   PHE 39   167  167  PHE PHE X . n 
B 2 40   LYS 40   168  168  LYS LYS X . n 
B 2 41   ILE 41   169  169  ILE ILE X . n 
B 2 42   ARG 42   170  170  ARG ARG X . n 
B 2 43   GLN 43   171  171  GLN GLN X . n 
B 2 44   HIS 44   172  172  HIS HIS X . n 
B 2 45   LEU 45   173  173  LEU LEU X . n 
B 2 46   VAL 46   174  174  VAL VAL X . n 
B 2 47   LYS 47   175  175  LYS LYS X . n 
B 2 48   ASN 48   176  176  ASN ASN X . n 
B 2 49   TYR 49   177  177  TYR TYR X . n 
B 2 50   GLY 50   178  178  GLY GLY X . n 
B 2 51   LEU 51   179  179  LEU LEU X . n 
B 2 52   TYR 52   180  180  TYR TYR X . n 
B 2 53   LYS 53   181  181  LYS LYS X . n 
B 2 54   GLY 54   182  182  GLY GLY X . n 
B 2 55   THR 55   183  183  THR THR X . n 
B 2 56   THR 56   184  184  THR THR X . n 
B 2 57   LYS 57   185  185  LYS LYS X . n 
B 2 58   TYR 58   186  186  TYR TYR X . n 
B 2 59   GLY 59   187  187  GLY GLY X . n 
B 2 60   LYS 60   188  188  LYS LYS X . n 
B 2 61   ILE 61   189  189  ILE ILE X . n 
B 2 62   THR 62   190  190  THR THR X . n 
B 2 63   ILE 63   191  191  ILE ILE X . n 
B 2 64   ASN 64   192  192  ASN ASN X . n 
B 2 65   LEU 65   193  193  LEU LEU X . n 
B 2 66   LYS 66   194  194  LYS LYS X . n 
B 2 67   ASP 67   195  195  ASP ASP X . n 
B 2 68   GLY 68   196  196  GLY GLY X . n 
B 2 69   GLU 69   197  197  GLU GLU X . n 
B 2 70   LYS 70   198  198  LYS LYS X . n 
B 2 71   GLN 71   199  199  GLN GLN X . n 
B 2 72   GLU 72   200  200  GLU GLU X . n 
B 2 73   ILE 73   201  201  ILE ILE X . n 
B 2 74   ASP 74   202  202  ASP ASP X . n 
B 2 75   LEU 75   203  203  LEU LEU X . n 
B 2 76   GLY 76   204  204  GLY GLY X . n 
B 2 77   ASP 77   205  205  ASP ASP X . n 
B 2 78   LYS 78   206  206  LYS LYS X . n 
B 2 79   LEU 79   207  207  LEU LEU X . n 
B 2 80   GLN 80   208  208  GLN GLN X . n 
B 2 81   PHE 81   209  209  PHE PHE X . n 
B 2 82   GLU 82   210  210  GLU GLU X . n 
B 2 83   ARG 83   211  211  ARG ARG X . n 
B 2 84   MET 84   212  212  MET MET X . n 
B 2 85   GLY 85   213  213  GLY GLY X . n 
B 2 86   ASP 86   214  214  ASP ASP X . n 
B 2 87   VAL 87   215  215  VAL VAL X . n 
B 2 88   LEU 88   216  216  LEU LEU X . n 
B 2 89   ASN 89   217  217  ASN ASN X . n 
B 2 90   SER 90   218  218  SER SER X . n 
B 2 91   LYS 91   219  219  LYS LYS X . n 
B 2 92   ASP 92   220  220  ASP ASP X . n 
B 2 93   ILE 93   221  221  ILE ILE X . n 
B 2 94   ASN 94   222  222  ASN ASN X . n 
B 2 95   LYS 95   223  223  LYS LYS X . n 
B 2 96   ILE 96   224  224  ILE ILE X . n 
B 2 97   GLU 97   225  225  GLU GLU X . n 
B 2 98   VAL 98   226  226  VAL VAL X . n 
B 2 99   THR 99   227  227  THR THR X . n 
B 2 100  LEU 100  228  228  LEU LEU X . n 
B 2 101  LYS 101  229  229  LYS LYS X . n 
B 2 102  GLN 102  230  230  GLN GLN X . n 
B 2 103  ILE 103  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  ?    ?   ?   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 ?    ?   ?   B . n 
C 1 1516 ILE 1516 1516 ?    ?   ?   B . n 
C 1 1517 GLN 1517 1517 ?    ?   ?   B . n 
C 1 1518 LYS 1518 1518 ?    ?   ?   B . n 
C 1 1519 VAL 1519 1519 ?    ?   ?   B . n 
C 1 1520 CYS 1520 1520 ?    ?   ?   B . n 
C 1 1521 GLU 1521 1521 ?    ?   ?   B . n 
C 1 1522 GLY 1522 1522 ?    ?   ?   B . n 
C 1 1523 ALA 1523 1523 ?    ?   ?   B . n 
C 1 1524 ALA 1524 1524 ?    ?   ?   B . n 
C 1 1525 CYS 1525 1525 ?    ?   ?   B . n 
C 1 1526 LYS 1526 1526 ?    ?   ?   B . n 
C 1 1527 CYS 1527 1527 ?    ?   ?   B . n 
C 1 1528 VAL 1528 1528 ?    ?   ?   B . n 
C 1 1529 GLU 1529 1529 ?    ?   ?   B . n 
C 1 1530 ALA 1530 1530 ?    ?   ?   B . n 
C 1 1531 ASP 1531 1531 ?    ?   ?   B . n 
C 1 1532 CYS 1532 1532 ?    ?   ?   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    SER 1    129  129  SER SER Y . n 
D 2 2    SER 2    130  130  SER SER Y . n 
D 2 3    GLU 3    131  131  GLU GLU Y . n 
D 2 4    THR 4    132  132  THR THR Y . n 
D 2 5    ASN 5    133  133  ASN ASN Y . n 
D 2 6    THR 6    134  134  THR THR Y . n 
D 2 7    HIS 7    135  135  HIS HIS Y . n 
D 2 8    LEU 8    136  136  LEU LEU Y . n 
D 2 9    PHE 9    137  137  PHE PHE Y . n 
D 2 10   VAL 10   138  138  VAL VAL Y . n 
D 2 11   ASN 11   139  139  ASN ASN Y . n 
D 2 12   LYS 12   140  140  LYS LYS Y . n 
D 2 13   VAL 13   141  141  VAL VAL Y . n 
D 2 14   TYR 14   142  142  TYR TYR Y . n 
D 2 15   GLY 15   143  143  GLY GLY Y . n 
D 2 16   GLY 16   144  144  GLY GLY Y . n 
D 2 17   ASN 17   145  145  ASN ASN Y . n 
D 2 18   LEU 18   146  146  LEU LEU Y . n 
D 2 19   ASP 19   147  147  ASP ASP Y . n 
D 2 20   ALA 20   148  148  ALA ALA Y . n 
D 2 21   SER 21   149  149  SER SER Y . n 
D 2 22   ILE 22   150  150  ILE ILE Y . n 
D 2 23   ASP 23   151  151  ASP ASP Y . n 
D 2 24   SER 24   152  152  SER SER Y . n 
D 2 25   PHE 25   153  153  PHE PHE Y . n 
D 2 26   SER 26   154  154  SER SER Y . n 
D 2 27   ILE 27   155  155  ILE ILE Y . n 
D 2 28   ASN 28   156  156  ASN ASN Y . n 
D 2 29   LYS 29   157  157  LYS LYS Y . n 
D 2 30   GLU 30   158  158  GLU GLU Y . n 
D 2 31   GLU 31   159  159  GLU GLU Y . n 
D 2 32   VAL 32   160  160  VAL VAL Y . n 
D 2 33   SER 33   161  161  SER SER Y . n 
D 2 34   LEU 34   162  162  LEU LEU Y . n 
D 2 35   LYS 35   163  163  LYS LYS Y . n 
D 2 36   GLU 36   164  164  GLU GLU Y . n 
D 2 37   LEU 37   165  165  LEU LEU Y . n 
D 2 38   ASP 38   166  166  ASP ASP Y . n 
D 2 39   PHE 39   167  167  PHE PHE Y . n 
D 2 40   LYS 40   168  168  LYS LYS Y . n 
D 2 41   ILE 41   169  169  ILE ILE Y . n 
D 2 42   ARG 42   170  170  ARG ARG Y . n 
D 2 43   GLN 43   171  171  GLN GLN Y . n 
D 2 44   HIS 44   172  172  HIS HIS Y . n 
D 2 45   LEU 45   173  173  LEU LEU Y . n 
D 2 46   VAL 46   174  174  VAL VAL Y . n 
D 2 47   LYS 47   175  175  LYS LYS Y . n 
D 2 48   ASN 48   176  176  ASN ASN Y . n 
D 2 49   TYR 49   177  177  TYR TYR Y . n 
D 2 50   GLY 50   178  178  GLY GLY Y . n 
D 2 51   LEU 51   179  179  LEU LEU Y . n 
D 2 52   TYR 52   180  180  TYR TYR Y . n 
D 2 53   LYS 53   181  181  LYS LYS Y . n 
D 2 54   GLY 54   182  182  GLY GLY Y . n 
D 2 55   THR 55   183  183  THR THR Y . n 
D 2 56   THR 56   184  184  THR THR Y . n 
D 2 57   LYS 57   185  185  LYS LYS Y . n 
D 2 58   TYR 58   186  186  TYR TYR Y . n 
D 2 59   GLY 59   187  187  GLY GLY Y . n 
D 2 60   LYS 60   188  188  LYS LYS Y . n 
D 2 61   ILE 61   189  189  ILE ILE Y . n 
D 2 62   THR 62   190  190  THR THR Y . n 
D 2 63   ILE 63   191  191  ILE ILE Y . n 
D 2 64   ASN 64   192  192  ASN ASN Y . n 
D 2 65   LEU 65   193  193  LEU LEU Y . n 
D 2 66   LYS 66   194  194  LYS LYS Y . n 
D 2 67   ASP 67   195  195  ASP ASP Y . n 
D 2 68   GLY 68   196  196  GLY GLY Y . n 
D 2 69   GLU 69   197  197  GLU GLU Y . n 
D 2 70   LYS 70   198  198  LYS LYS Y . n 
D 2 71   GLN 71   199  199  GLN GLN Y . n 
D 2 72   GLU 72   200  200  GLU GLU Y . n 
D 2 73   ILE 73   201  201  ILE ILE Y . n 
D 2 74   ASP 74   202  202  ASP ASP Y . n 
D 2 75   LEU 75   203  203  LEU LEU Y . n 
D 2 76   GLY 76   204  204  GLY GLY Y . n 
D 2 77   ASP 77   205  205  ASP ASP Y . n 
D 2 78   LYS 78   206  206  LYS LYS Y . n 
D 2 79   LEU 79   207  207  LEU LEU Y . n 
D 2 80   GLN 80   208  208  GLN GLN Y . n 
D 2 81   PHE 81   209  209  PHE PHE Y . n 
D 2 82   GLU 82   210  210  GLU GLU Y . n 
D 2 83   ARG 83   211  211  ARG ARG Y . n 
D 2 84   MET 84   212  212  MET MET Y . n 
D 2 85   GLY 85   213  213  GLY GLY Y . n 
D 2 86   ASP 86   214  214  ASP ASP Y . n 
D 2 87   VAL 87   215  215  VAL VAL Y . n 
D 2 88   LEU 88   216  216  LEU LEU Y . n 
D 2 89   ASN 89   217  217  ASN ASN Y . n 
D 2 90   SER 90   218  218  SER SER Y . n 
D 2 91   LYS 91   219  219  LYS LYS Y . n 
D 2 92   ASP 92   220  220  ASP ASP Y . n 
D 2 93   ILE 93   221  221  ILE ILE Y . n 
D 2 94   ASN 94   222  222  ASN ASN Y . n 
D 2 95   LYS 95   223  223  LYS LYS Y . n 
D 2 96   ILE 96   224  224  ILE ILE Y . n 
D 2 97   GLU 97   225  225  GLU GLU Y . n 
D 2 98   VAL 98   226  226  VAL VAL Y . n 
D 2 99   THR 99   227  227  THR THR Y . n 
D 2 100  LEU 100  228  228  LEU LEU Y . n 
D 2 101  LYS 101  229  229  LYS LYS Y . n 
D 2 102  GLN 102  230  230  GLN GLN Y . n 
D 2 103  ILE 103  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 3 CD  1 1678 2    CD  CD  A . 
G 3 CD  1 1679 3    CD  CD  A . 
H 4 NAG 1 2001 2001 NAG NAG A . 
I 4 NAG 2 2002 2002 NAG NAG A . 
J 4 NAG 1 1680 1    NAG NAG A . 
K 3 CD  1 1677 2    CD  CD  B . 
L 3 CD  1 1678 3    CD  CD  B . 
M 4 NAG 1 2001 2001 NAG NAG B . 
N 4 NAG 2 2002 2002 NAG NAG B . 
O 4 NAG 1 1679 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 911 A ASN 911 ? ASN 'GLYCOSYLATION SITE' 
2 C ASN 911 B ASN 911 ? ASN 'GLYCOSYLATION SITE' 
3 A ASN 741 A ASN 741 ? ASN 'GLYCOSYLATION SITE' 
4 C ASN 741 B ASN 741 ? 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_defined_assembly ? dimeric 2 
2 author_defined_assembly ? 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 
2 1 C,D,K,L,M,N,O   
# 
_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  OD2 ? A ASP 264 ? A ASP 264 ? 1_555 CD ? G CD . ? A CD 1679 ? 1_555 ND1 ? A HIS 753 ? A HIS 753 ? 1_555 127.7 ? 
2  OD1 ? A ASP 471 ? A ASP 471 ? 1_555 CD ? F CD . ? A CD 1678 ? 1_555 OE1 ? A GLU 480 ? A GLU 480 ? 1_555 102.5 ? 
3  OD1 ? A ASP 471 ? A ASP 471 ? 1_555 CD ? F CD . ? A CD 1678 ? 1_555 OD2 ? A ASP 471 ? A ASP 471 ? 1_555 55.3  ? 
4  OE1 ? A GLU 480 ? A GLU 480 ? 1_555 CD ? F CD . ? A CD 1678 ? 1_555 OD2 ? A ASP 471 ? A ASP 471 ? 1_555 157.5 ? 
5  OD1 ? A ASP 471 ? A ASP 471 ? 1_555 CD ? F CD . ? A CD 1678 ? 1_555 OE2 ? A GLU 480 ? A GLU 480 ? 1_555 130.6 ? 
6  OE1 ? A GLU 480 ? A GLU 480 ? 1_555 CD ? F CD . ? A CD 1678 ? 1_555 OE2 ? A GLU 480 ? A GLU 480 ? 1_555 54.2  ? 
7  OD2 ? A ASP 471 ? A ASP 471 ? 1_555 CD ? F CD . ? A CD 1678 ? 1_555 OE2 ? A GLU 480 ? A GLU 480 ? 1_555 140.6 ? 
8  OD1 ? C ASP 471 ? B ASP 471 ? 1_555 CD ? K CD . ? B CD 1677 ? 1_555 OE1 ? C GLU 480 ? B GLU 480 ? 1_555 117.1 ? 
9  OD1 ? C ASP 471 ? B ASP 471 ? 1_555 CD ? K CD . ? B CD 1677 ? 1_555 OE2 ? C GLU 480 ? B GLU 480 ? 1_555 125.5 ? 
10 OE1 ? C GLU 480 ? B GLU 480 ? 1_555 CD ? K CD . ? B CD 1677 ? 1_555 OE2 ? C GLU 480 ? B GLU 480 ? 1_555 54.5  ? 
11 OD1 ? C ASP 471 ? B ASP 471 ? 1_555 CD ? K CD . ? B CD 1677 ? 1_555 OD2 ? C ASP 471 ? B ASP 471 ? 1_555 54.8  ? 
12 OE1 ? C GLU 480 ? B GLU 480 ? 1_555 CD ? K CD . ? B CD 1677 ? 1_555 OD2 ? C ASP 471 ? B ASP 471 ? 1_555 171.5 ? 
13 OE2 ? C GLU 480 ? B GLU 480 ? 1_555 CD ? K CD . ? B CD 1677 ? 1_555 OD2 ? C ASP 471 ? B ASP 471 ? 1_555 130.9 ? 
14 ND1 ? C HIS 753 ? B HIS 753 ? 1_555 CD ? L CD . ? B CD 1678 ? 1_555 OD2 ? C ASP 264 ? B ASP 264 ? 1_555 122.8 ? 
15 OE1 ? C GLU 247 ? B GLU 247 ? 1_555 CD ? E CD . ? A CD 1677 ? 1_555 OE1 ? A GLU 247 ? A GLU 247 ? 1_555 166.6 ? 
# 
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 2009-12-01 
2 'Structure model' 1 1 2011-07-13 
3 'Structure model' 1 2 2017-11-01 
# 
_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' 'Refinement description'    
# 
_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            software 
# 
loop_
_software.name 
_software.classification 
_software.version 
_software.citation_id 
_software.pdbx_ordinal 
PHASER phasing          .                        ? 1 
PHENIX refinement       '(phenix.refine: 1.5_2)' ? 2 
XDS    'data reduction' .                        ? 3 
XSCALE 'data scaling'   .                        ? 4 
# 
_pdbx_entry_details.entry_id             3KM9 
_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_close_contact.id               1 
_pdbx_validate_close_contact.PDB_model_num    1 
_pdbx_validate_close_contact.auth_atom_id_1   O 
_pdbx_validate_close_contact.auth_asym_id_1   A 
_pdbx_validate_close_contact.auth_comp_id_1   ASP 
_pdbx_validate_close_contact.auth_seq_id_1    317 
_pdbx_validate_close_contact.PDB_ins_code_1   ? 
_pdbx_validate_close_contact.label_alt_id_1   ? 
_pdbx_validate_close_contact.auth_atom_id_2   N 
_pdbx_validate_close_contact.auth_asym_id_2   A 
_pdbx_validate_close_contact.auth_comp_id_2   ASN 
_pdbx_validate_close_contact.auth_seq_id_2    319 
_pdbx_validate_close_contact.PDB_ins_code_2   ? 
_pdbx_validate_close_contact.label_alt_id_2   ? 
_pdbx_validate_close_contact.dist             2.18 
# 
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 CB A ASP 264  ? ? CG A ASP 264  ? ? OD1 A ASP 264  ? ? 110.59 118.30 -7.71  0.90 N 
2  1 C  A VAL 386  ? ? N  A PRO 387  ? ? CA  A PRO 387  ? ? 129.56 119.30 10.26  1.50 Y 
3  1 C  A VAL 535  ? ? N  A PRO 536  ? ? CA  A PRO 536  ? ? 107.91 119.30 -11.39 1.50 Y 
4  1 CA A LEU 640  ? ? CB A LEU 640  ? ? CG  A LEU 640  ? ? 130.28 115.30 14.98  2.30 N 
5  1 C  A LEU 1003 ? ? N  A PRO 1004 ? ? CA  A PRO 1004 ? ? 134.15 119.30 14.85  1.50 Y 
6  1 C  A LEU 1003 ? ? N  A PRO 1004 ? ? CD  A PRO 1004 ? ? 115.33 128.40 -13.07 2.10 Y 
7  1 C  A ARG 1500 ? ? N  A PRO 1501 ? ? CA  A PRO 1501 ? ? 130.03 119.30 10.73  1.50 Y 
8  1 C  B VAL 386  ? ? N  B PRO 387  ? ? CA  B PRO 387  ? ? 128.46 119.30 9.16   1.50 Y 
9  1 C  B ASP 405  ? ? N  B PRO 406  ? ? CA  B PRO 406  ? ? 128.31 119.30 9.01   1.50 Y 
10 1 CA B LEU 640  ? ? CB B LEU 640  ? ? CG  B LEU 640  ? ? 131.94 115.30 16.64  2.30 N 
11 1 C  B LEU 1003 ? ? N  B PRO 1004 ? ? CA  B PRO 1004 ? ? 131.58 119.30 12.28  1.50 Y 
12 1 CB B VAL 1374 ? ? CA B VAL 1374 ? ? C   B VAL 1374 ? ? 98.85  111.40 -12.55 1.90 N 
13 1 C  B ARG 1500 ? ? N  B PRO 1501 ? ? CA  B PRO 1501 ? ? 131.21 119.30 11.91  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   ? ? -52.66  175.26  
2   1 SER A 36   ? ? -68.37  64.75   
3   1 GLU A 48   ? ? -58.98  105.99  
4   1 TYR A 59   ? ? 1.25    -117.49 
5   1 LYS A 62   ? ? -66.66  47.35   
6   1 LYS A 78   ? ? 43.69   28.43   
7   1 PHE A 79   ? ? 57.57   71.03   
8   1 LEU A 85   ? ? -66.75  -159.76 
9   1 THR A 86   ? ? 160.98  107.55  
10  1 PRO A 89   ? ? -69.87  75.90   
11  1 LYS A 90   ? ? -74.08  -105.61 
12  1 GLN A 91   ? ? -44.89  108.26  
13  1 PRO A 93   ? ? -68.95  98.00   
14  1 VAL A 99   ? ? 68.87   -20.64  
15  1 SER A 100  ? ? -64.71  96.76   
16  1 TYR A 101  ? ? 103.53  138.43  
17  1 PHE A 111  ? ? 174.94  -175.00 
18  1 PRO A 118  ? ? -48.08  160.45  
19  1 ASP A 122  ? ? -104.20 65.23   
20  1 HIS A 129  ? ? -63.87  79.76   
21  1 ASP A 138  ? ? 86.81   4.00    
22  1 VAL A 141  ? ? -59.78  90.68   
23  1 ASP A 150  ? ? -26.34  -42.02  
24  1 PRO A 154  ? ? -29.99  -44.74  
25  1 ALA A 155  ? ? 71.13   33.34   
26  1 LYS A 156  ? ? -38.04  138.16  
27  1 THR A 162  ? ? -160.46 79.23   
28  1 ASP A 165  ? ? -42.89  156.74  
29  1 PRO A 166  ? ? -56.09  11.84   
30  1 GLU A 170  ? ? -36.45  162.90  
31  1 VAL A 171  ? ? -147.23 -10.97  
32  1 ASP A 172  ? ? -165.85 -150.81 
33  1 MET A 173  ? ? 163.72  169.42  
34  1 VAL A 174  ? ? 164.45  152.75  
35  1 GLU A 176  ? ? -171.47 -178.35 
36  1 PHE A 185  ? ? -59.45  -178.16 
37  1 ASN A 193  ? ? -165.69 85.20   
38  1 GLU A 207  ? ? -60.74  -156.40 
39  1 PHE A 209  ? ? 109.27  119.76  
40  1 PHE A 217  ? ? -178.10 137.37  
41  1 ILE A 231  ? ? -170.58 111.20  
42  1 TYR A 235  ? ? -124.28 -160.79 
43  1 PHE A 237  ? ? -134.54 -156.36 
44  1 TYR A 240  ? ? -47.92  -14.61  
45  1 PHE A 243  ? ? -143.83 -16.99  
46  1 ARG A 253  ? ? -171.21 136.50  
47  1 TYR A 256  ? ? -82.84  43.72   
48  1 THR A 261  ? ? -109.59 -111.74 
49  1 ARG A 272  ? ? 166.22  175.11  
50  1 MET A 282  ? ? -39.30  -177.69 
51  1 ASN A 289  ? ? 47.74   111.52  
52  1 MET A 291  ? ? 49.20   108.10  
53  1 ALA A 297  ? ? 178.11  -168.94 
54  1 ASP A 302  ? ? -49.59  96.83   
55  1 GLU A 304  ? ? -44.59  -79.78  
56  1 THR A 305  ? ? -29.55  -89.92  
57  1 ALA A 306  ? ? -62.65  61.53   
58  1 VAL A 307  ? ? -168.16 -38.86  
59  1 LYS A 308  ? ? -43.83  -82.95  
60  1 SER A 311  ? ? 179.78  -175.94 
61  1 GLU A 316  ? ? -44.01  -99.24  
62  1 ASP A 317  ? ? 8.58    -78.34  
63  1 LEU A 318  ? ? -52.37  23.41   
64  1 ASN A 320  ? ? -142.15 16.89   
65  1 LYS A 321  ? ? -102.81 -163.21 
66  1 PHE A 336  ? ? -63.96  -174.03 
67  1 PRO A 351  ? ? -68.86  3.98    
68  1 LEU A 356  ? ? -39.13  155.41  
69  1 ALA A 358  ? ? 31.65   52.20   
70  1 GLN A 374  ? ? -160.47 104.47  
71  1 SER A 378  ? ? -55.68  -9.94   
72  1 VAL A 388  ? ? -155.05 62.72   
73  1 LEU A 390  ? ? -110.28 77.81   
74  1 ASN A 398  ? ? -67.24  13.41   
75  1 LEU A 404  ? ? -68.29  -173.49 
76  1 SER A 409  ? ? -111.95 -166.82 
77  1 PRO A 425  ? ? -55.56  83.42   
78  1 SER A 426  ? ? -5.77   -42.47  
79  1 VAL A 428  ? ? -66.75  -179.29 
80  1 THR A 429  ? ? -154.01 -84.54  
81  1 LYS A 436  ? ? -178.93 142.39  
82  1 ALA A 439  ? ? -33.04  140.66  
83  1 GLU A 445  ? ? -24.92  -57.88  
84  1 TYR A 452  ? ? -149.32 -150.86 
85  1 TYR A 457  ? ? -50.13  83.35   
86  1 SER A 461  ? ? -62.19  5.89    
87  1 GLN A 462  ? ? 61.41   -0.49   
88  1 TRP A 469  ? ? 178.98  164.61  
89  1 LEU A 477  ? ? -33.40  154.90  
90  1 GLU A 480  ? ? -47.85  -167.75 
91  1 VAL A 486  ? ? -117.69 79.92   
92  1 LYS A 489  ? ? -11.78  130.78  
93  1 SER A 490  ? ? 104.69  -65.26  
94  1 PRO A 491  ? ? -21.43  120.17  
95  1 LYS A 495  ? ? -68.42  31.84   
96  1 THR A 497  ? ? -67.56  -80.73  
97  1 SER A 505  ? ? -166.06 117.12  
98  1 ILE A 510  ? ? -148.89 -15.46  
99  1 SER A 519  ? ? -38.36  -93.02  
100 1 ASP A 520  ? ? -30.72  -94.01  
101 1 SER A 522  ? ? -60.27  -115.01 
102 1 TYR A 523  ? ? -57.50  -173.77 
103 1 GLN A 532  ? ? -38.69  -31.64  
104 1 ASN A 533  ? ? -68.37  3.92    
105 1 VAL A 535  ? ? -28.31  -56.82  
106 1 SER A 537  ? ? -148.98 -158.74 
107 1 SER A 538  ? ? 172.65  149.02  
108 1 GLN A 570  ? ? -68.40  98.85   
109 1 ASP A 580  ? ? -93.92  33.48   
110 1 ALA A 581  ? ? -176.68 147.17  
111 1 PRO A 584  ? ? -67.13  94.55   
112 1 ALA A 601  ? ? -157.16 83.38   
113 1 ALA A 603  ? ? -172.14 95.06   
114 1 SER A 607  ? ? -49.22  -9.47   
115 1 VAL A 609  ? ? -31.55  -85.00  
116 1 TYR A 610  ? ? -40.12  -91.65  
117 1 VAL A 612  ? ? -48.56  102.46  
118 1 GLN A 613  ? ? 47.26   79.60   
119 1 LYS A 617  ? ? 32.56   -113.96 
120 1 PRO A 619  ? ? -76.75  -72.36  
121 1 GLN A 625  ? ? -64.03  -85.30  
122 1 PHE A 626  ? ? -29.42  -66.86  
123 1 GLU A 628  ? ? -119.91 55.12   
124 1 LEU A 640  ? ? -146.33 -21.67  
125 1 HIS A 647  ? ? -64.91  -77.22  
126 1 LEU A 648  ? ? -44.45  -15.15  
127 1 ALA A 657  ? ? 166.05  -56.31  
128 1 ASP A 660  ? ? -66.40  22.85   
129 1 ASP A 661  ? ? -61.00  -158.14 
130 1 SER A 662  ? ? 174.95  67.60   
131 1 GLN A 663  ? ? -19.23  111.88  
132 1 GLU A 664  ? ? 70.54   -73.02  
133 1 ASN A 665  ? ? -125.64 -118.89 
134 1 ASP A 666  ? ? -173.05 76.53   
135 1 GLU A 667  ? ? 31.34   93.44   
136 1 PRO A 668  ? ? -64.11  36.57   
137 1 CYS A 669  ? ? -30.07  142.14  
138 1 LYS A 670  ? ? -156.64 86.90   
139 1 GLU A 671  ? ? 71.69   48.64   
140 1 LYS A 691  ? ? -167.28 0.02    
141 1 HIS A 692  ? ? 176.72  153.08  
142 1 TYR A 700  ? ? -50.90  -88.93  
143 1 CYS A 704  ? ? 9.62    -100.10 
144 1 VAL A 705  ? ? -159.93 65.25   
145 1 THR A 710  ? ? -57.01  179.89  
146 1 ARG A 717  ? ? -53.89  -2.87   
147 1 SER A 719  ? ? -99.54  -84.65  
148 1 LEU A 720  ? ? -2.56   -47.66  
149 1 PHE A 728  ? ? -76.51  -79.47  
150 1 HIS A 753  ? ? -160.09 89.01   
151 1 LEU A 758  ? ? 177.88  97.33   
152 1 PRO A 759  ? ? -58.58  13.88   
153 1 PRO A 763  ? ? -65.60  92.58   
154 1 ILE A 765  ? ? -165.15 115.75  
155 1 ARG A 766  ? ? -86.74  42.76   
156 1 PRO A 770  ? ? -39.34  148.39  
157 1 SER A 772  ? ? -72.55  -160.38 
158 1 TRP A 773  ? ? -172.13 -173.49 
159 1 ARG A 782  ? ? 83.89   -30.18  
160 1 LYS A 784  ? ? -164.96 119.98  
161 1 PHE A 788  ? ? -179.67 149.33  
162 1 SER A 793  ? ? 166.51  148.63  
163 1 SER A 805  ? ? -152.35 -153.66 
164 1 THR A 814  ? ? -54.94  -177.15 
165 1 VAL A 815  ? ? -157.68 86.85   
166 1 ALA A 817  ? ? -178.53 59.87   
167 1 PHE A 820  ? ? 177.99  140.97  
168 1 TYR A 831  ? ? -62.37  -70.74  
169 1 ARG A 835  ? ? -35.60  140.12  
170 1 MET A 853  ? ? -170.10 -178.68 
171 1 PHE A 855  ? ? -126.56 -169.78 
172 1 CYS A 856  ? ? -176.58 85.79   
173 1 GLU A 863  ? ? 3.09    -85.30  
174 1 SER A 892  ? ? -159.50 -136.42 
175 1 LEU A 901  ? ? -166.84 106.66  
176 1 HIS A 908  ? ? -119.17 -158.22 
177 1 ASN A 909  ? ? 59.02   118.95  
178 1 PRO A 931  ? ? -115.14 -155.28 
179 1 TYR A 939  ? ? -59.85  -8.70   
180 1 ARG A 956  ? ? -164.98 108.65  
181 1 LEU A 965  ? ? -63.43  9.23    
182 1 PRO A 969  ? ? -42.35  161.50  
183 1 LYS A 970  ? ? 49.20   27.63   
184 1 LEU A 982  ? ? 85.49   152.25  
185 1 SER A 993  ? ? -164.22 -32.26  
186 1 ILE A 997  ? ? -48.31  159.68  
187 1 LYS A 1005 ? ? -67.78  0.77    
188 1 SER A 1007 ? ? -52.44  -179.46 
189 1 MET A 1013 ? ? -59.27  -4.73   
190 1 VAL A 1016 ? ? -55.55  -81.12  
191 1 PRO A 1017 ? ? -39.75  -36.76  
192 1 ASN A 1029 ? ? -6.11   108.10  
193 1 SER A 1036 ? ? -69.38  -163.03 
194 1 SER A 1055 ? ? -38.51  -21.41  
195 1 MET A 1057 ? ? -29.20  -47.89  
196 1 ASN A 1061 ? ? -73.21  -162.43 
197 1 TYR A 1064 ? ? 85.52   -6.52   
198 1 VAL A 1068 ? ? -56.95  -71.16  
199 1 LYS A 1070 ? ? -38.28  128.35  
200 1 GLN A 1097 ? ? -53.52  -81.46  
201 1 SER A 1099 ? ? -63.50  -70.65  
202 1 CYS A 1101 ? ? -46.81  -74.46  
203 1 LEU A 1105 ? ? -54.10  -4.30   
204 1 LEU A 1113 ? ? -46.92  163.85  
205 1 ASP A 1114 ? ? -68.05  39.56   
206 1 ASN A 1115 ? ? -161.21 21.47   
207 1 SER A 1122 ? ? -58.94  -177.66 
208 1 ARG A 1153 ? ? -58.12  -78.21  
209 1 PHE A 1156 ? ? -35.82  -37.76  
210 1 THR A 1166 ? ? -37.31  -80.46  
211 1 GLU A 1177 ? ? -59.95  7.32    
212 1 ASN A 1178 ? ? -150.62 5.77    
213 1 PRO A 1181 ? ? -59.43  73.64   
214 1 ALA A 1216 ? ? -47.84  172.88  
215 1 PRO A 1222 ? ? -58.60  172.91  
216 1 ASN A 1231 ? ? -56.64  -153.10 
217 1 LEU A 1232 ? ? -167.26 89.92   
218 1 GLN A 1233 ? ? 59.13   9.31    
219 1 SER A 1238 ? ? -66.03  83.02   
220 1 VAL A 1239 ? ? -104.79 46.54   
221 1 PRO A 1240 ? ? -51.79  64.10   
222 1 MET A 1247 ? ? -50.28  -76.63  
223 1 ASP A 1263 ? ? -65.73  32.60   
224 1 ILE A 1264 ? ? -22.66  -25.28  
225 1 LEU A 1274 ? ? -55.53  -70.14  
226 1 SER A 1275 ? ? -50.74  19.89   
227 1 GLU A 1276 ? ? -141.33 -5.82   
228 1 GLN A 1278 ? ? -33.51  133.66  
229 1 TYR A 1280 ? ? -23.31  126.45  
230 1 PHE A 1284 ? ? 10.16   -89.87  
231 1 SER A 1286 ? ? 36.33   -159.23 
232 1 THR A 1287 ? ? -105.78 -70.65  
233 1 THR A 1290 ? ? -66.25  2.09    
234 1 LEU A 1297 ? ? -32.70  -20.16  
235 1 VAL A 1304 ? ? -56.23  -170.32 
236 1 LEU A 1307 ? ? -118.32 78.75   
237 1 ARG A 1308 ? ? -12.88  114.68  
238 1 SER A 1310 ? ? -169.16 30.40   
239 1 MET A 1311 ? ? -50.66  -154.05 
240 1 ASP A 1312 ? ? -177.58 61.03   
241 1 THR A 1329 ? ? -159.07 -158.61 
242 1 PHE A 1333 ? ? -141.18 -22.21  
243 1 LEU A 1341 ? ? -71.41  -84.55  
244 1 LEU A 1342 ? ? -51.64  -169.37 
245 1 SER A 1349 ? ? -171.02 61.92   
246 1 THR A 1350 ? ? -48.87  160.93  
247 1 PHE A 1352 ? ? -75.28  -107.64 
248 1 GLU A 1372 ? ? -59.40  -70.70  
249 1 GLU A 1373 ? ? -39.04  170.55  
250 1 LYS A 1400 ? ? -171.09 129.78  
251 1 GLU A 1413 ? ? 76.88   -11.88  
252 1 HIS A 1421 ? ? -37.14  122.15  
253 1 ILE A 1432 ? ? -155.46 40.43   
254 1 SER A 1433 ? ? -21.15  142.63  
255 1 LYS A 1440 ? ? -39.99  -29.23  
256 1 GLU A 1444 ? ? -67.72  17.93   
257 1 ASP A 1447 ? ? -97.03  34.23   
258 1 THR A 1451 ? ? -147.17 -14.83  
259 1 GLN A 1454 ? ? -177.60 119.24  
260 1 ASP A 1457 ? ? 13.82   69.32   
261 1 PRO A 1468 ? ? -38.72  156.73  
262 1 GLU A 1481 ? ? -42.08  104.29  
263 1 PRO A 1490 ? ? -47.99  165.51  
264 1 ALA A 1491 ? ? -94.16  -154.21 
265 1 PRO A 1501 ? ? -52.46  1.59    
266 1 TYR X 142  ? ? -82.59  46.28   
267 1 ASN X 176  ? ? -135.33 -41.22  
268 1 THR X 183  ? ? -67.87  3.45    
269 1 LYS X 185  ? ? 174.72  -26.64  
270 1 LEU X 193  ? ? -135.97 -36.84  
271 1 ASP X 195  ? ? -65.08  18.25   
272 1 LYS X 206  ? ? -86.52  30.43   
273 1 LYS X 223  ? ? -160.46 118.40  
274 1 PRO B 28   ? ? -49.84  -176.77 
275 1 SER B 36   ? ? -63.52  70.58   
276 1 TYR B 59   ? ? -3.07   -117.12 
277 1 LYS B 62   ? ? -66.29  47.61   
278 1 LYS B 78   ? ? 39.69   29.42   
279 1 LEU B 85   ? ? -66.22  -166.70 
280 1 THR B 86   ? ? 168.45  105.49  
281 1 LYS B 90   ? ? -73.56  -99.66  
282 1 VAL B 99   ? ? 69.38   -16.64  
283 1 SER B 100  ? ? -69.31  92.63   
284 1 TYR B 101  ? ? 106.73  127.35  
285 1 PHE B 111  ? ? 174.41  -170.70 
286 1 PRO B 118  ? ? -49.19  156.10  
287 1 ASP B 122  ? ? -106.35 63.46   
288 1 PRO B 137  ? ? -37.41  129.23  
289 1 ASP B 138  ? ? 85.67   1.16    
290 1 VAL B 141  ? ? -65.79  93.27   
291 1 ASP B 150  ? ? -30.98  -37.13  
292 1 LEU B 152  ? ? 38.65   45.86   
293 1 LYS B 156  ? ? -33.42  137.49  
294 1 THR B 162  ? ? -162.59 81.38   
295 1 ASP B 165  ? ? -49.28  157.85  
296 1 PRO B 166  ? ? -55.44  10.49   
297 1 GLU B 170  ? ? -39.15  161.63  
298 1 VAL B 171  ? ? -149.39 -2.94   
299 1 ASP B 172  ? ? -171.88 -157.36 
300 1 MET B 173  ? ? 167.30  170.65  
301 1 VAL B 174  ? ? 163.34  156.80  
302 1 GLU B 176  ? ? -173.73 -174.03 
303 1 PHE B 185  ? ? -68.55  -179.26 
304 1 ASP B 187  ? ? -34.92  142.29  
305 1 GLU B 207  ? ? -56.78  -155.94 
306 1 PHE B 209  ? ? 110.23  121.31  
307 1 PHE B 217  ? ? -175.33 134.06  
308 1 ILE B 231  ? ? -167.97 119.13  
309 1 PHE B 237  ? ? -129.23 -161.30 
310 1 TYR B 240  ? ? -53.47  -0.98   
311 1 PHE B 243  ? ? -157.30 -16.33  
312 1 ARG B 253  ? ? -173.87 135.87  
313 1 TYR B 256  ? ? -82.20  44.35   
314 1 THR B 261  ? ? -107.15 -110.76 
315 1 ARG B 272  ? ? 179.59  -167.58 
316 1 GLU B 273  ? ? -130.69 -51.66  
317 1 MET B 282  ? ? -40.07  -176.23 
318 1 ASN B 289  ? ? 39.39   110.88  
319 1 MET B 291  ? ? 51.11   106.52  
320 1 ALA B 297  ? ? -176.71 -168.70 
321 1 ASP B 302  ? ? -49.79  96.99   
322 1 GLU B 304  ? ? -47.52  -83.40  
323 1 THR B 305  ? ? -24.09  -88.17  
324 1 ALA B 306  ? ? -62.82  54.56   
325 1 VAL B 307  ? ? -164.86 -34.94  
326 1 LYS B 308  ? ? -45.21  -79.62  
327 1 TYR B 312  ? ? -59.88  5.48    
328 1 ASN B 320  ? ? -165.89 13.45   
329 1 LYS B 321  ? ? -95.64  -155.73 
330 1 PRO B 343  ? ? -55.01  -70.35  
331 1 PRO B 351  ? ? -58.68  -1.26   
332 1 ASN B 355  ? ? -164.95 119.87  
333 1 LEU B 356  ? ? -40.14  155.91  
334 1 ALA B 358  ? ? 37.65   52.41   
335 1 LEU B 361  ? ? -104.13 41.34   
336 1 SER B 378  ? ? -46.29  -6.22   
337 1 VAL B 388  ? ? -156.80 59.27   
338 1 ASN B 398  ? ? -67.02  15.56   
339 1 GLN B 399  ? ? 35.98   52.00   
340 1 PRO B 425  ? ? -55.04  82.28   
341 1 SER B 426  ? ? -3.39   -44.99  
342 1 THR B 429  ? ? -150.16 -78.53  
343 1 LYS B 436  ? ? -172.17 142.35  
344 1 ALA B 439  ? ? -32.99  142.72  
345 1 GLU B 444  ? ? -42.05  -70.02  
346 1 GLU B 445  ? ? -18.60  -64.31  
347 1 TYR B 452  ? ? -151.99 -152.00 
348 1 ARG B 453  ? ? -171.88 134.44  
349 1 TYR B 457  ? ? -43.70  77.85   
350 1 SER B 459  ? ? -176.20 119.90  
351 1 SER B 461  ? ? -62.32  4.74    
352 1 GLN B 462  ? ? 66.22   -4.65   
353 1 TRP B 469  ? ? 175.22  160.64  
354 1 GLU B 480  ? ? -56.90  -172.28 
355 1 VAL B 486  ? ? -113.76 79.05   
356 1 LYS B 489  ? ? -19.60  130.56  
357 1 SER B 490  ? ? 108.17  -64.78  
358 1 PRO B 491  ? ? -19.64  120.06  
359 1 LYS B 495  ? ? -63.82  37.22   
360 1 THR B 497  ? ? -73.75  -76.91  
361 1 ILE B 510  ? ? -141.20 -22.68  
362 1 PHE B 512  ? ? 179.28  160.67  
363 1 PHE B 518  ? ? -68.79  97.58   
364 1 SER B 519  ? ? -37.79  -78.84  
365 1 ASP B 520  ? ? -44.12  -91.96  
366 1 SER B 522  ? ? -53.04  -109.74 
367 1 TYR B 523  ? ? -73.57  -168.87 
368 1 GLN B 532  ? ? -39.09  -36.49  
369 1 SER B 537  ? ? -137.47 -155.89 
370 1 SER B 538  ? ? 173.40  156.69  
371 1 GLU B 565  ? ? -67.03  54.66   
372 1 PRO B 584  ? ? -67.79  97.52   
373 1 ALA B 601  ? ? -154.27 81.35   
374 1 ALA B 603  ? ? -170.82 96.25   
375 1 SER B 607  ? ? -43.06  -14.12  
376 1 VAL B 609  ? ? -25.70  -93.40  
377 1 TYR B 610  ? ? -34.75  -94.29  
378 1 VAL B 612  ? ? -46.18  98.33   
379 1 GLN B 613  ? ? 49.36   78.15   
380 1 LYS B 617  ? ? 25.98   -115.38 
381 1 PRO B 619  ? ? -76.91  -71.35  
382 1 GLN B 625  ? ? -66.13  -81.27  
383 1 LEU B 627  ? ? -46.79  -13.03  
384 1 LEU B 640  ? ? -149.37 -25.57  
385 1 HIS B 647  ? ? -65.50  -74.26  
386 1 LEU B 648  ? ? -49.60  -12.86  
387 1 ALA B 657  ? ? 161.19  -64.35  
388 1 ASP B 660  ? ? -65.65  20.05   
389 1 ASP B 661  ? ? -58.46  -160.99 
390 1 SER B 662  ? ? 179.35  67.04   
391 1 GLN B 663  ? ? -20.79  109.17  
392 1 GLU B 664  ? ? 77.98   -77.85  
393 1 ASN B 665  ? ? -123.95 -112.25 
394 1 ASP B 666  ? ? -177.16 73.51   
395 1 GLU B 667  ? ? 29.22   94.34   
396 1 PRO B 668  ? ? -63.89  37.61   
397 1 CYS B 669  ? ? -33.71  148.00  
398 1 LYS B 670  ? ? -162.38 88.18   
399 1 GLU B 671  ? ? 75.06   44.50   
400 1 LYS B 691  ? ? -169.96 6.05    
401 1 HIS B 692  ? ? 172.39  154.78  
402 1 TYR B 700  ? ? -47.92  -89.26  
403 1 ASP B 701  ? ? -49.01  -16.97  
404 1 CYS B 704  ? ? 10.66   -114.28 
405 1 THR B 710  ? ? -54.62  -176.73 
406 1 ARG B 717  ? ? -54.38  -7.38   
407 1 SER B 719  ? ? -96.16  -81.41  
408 1 LEU B 720  ? ? -6.15   -46.62  
409 1 HIS B 753  ? ? -158.88 84.72   
410 1 LEU B 758  ? ? 177.38  96.60   
411 1 PRO B 759  ? ? -57.87  12.80   
412 1 PRO B 763  ? ? -64.19  94.56   
413 1 ARG B 766  ? ? -89.61  39.89   
414 1 PRO B 770  ? ? -42.42  150.47  
415 1 SER B 772  ? ? -75.80  -161.13 
416 1 TRP B 773  ? ? -172.57 -175.76 
417 1 ARG B 782  ? ? 83.47   -27.45  
418 1 LYS B 784  ? ? -165.90 117.62  
419 1 PHE B 788  ? ? 176.87  151.75  
420 1 SER B 793  ? ? 169.03  143.25  
421 1 SER B 805  ? ? -158.98 -155.16 
422 1 THR B 814  ? ? -52.42  -178.41 
423 1 VAL B 815  ? ? -154.64 85.24   
424 1 ALA B 817  ? ? 176.76  68.89   
425 1 PHE B 820  ? ? 177.23  142.82  
426 1 PHE B 855  ? ? -128.06 -164.91 
427 1 CYS B 856  ? ? -178.37 82.73   
428 1 GLU B 863  ? ? 13.66   -88.86  
429 1 SER B 892  ? ? -158.89 -135.68 
430 1 LEU B 895  ? ? -45.49  156.61  
431 1 LEU B 901  ? ? -161.34 107.16  
432 1 HIS B 908  ? ? -118.73 -161.82 
433 1 ASN B 909  ? ? 60.90   120.49  
434 1 PRO B 931  ? ? -113.07 -154.43 
435 1 ILE B 949  ? ? -21.81  -33.73  
436 1 THR B 952  ? ? 166.20  163.70  
437 1 ARG B 956  ? ? -169.19 111.93  
438 1 LEU B 965  ? ? -69.78  10.22   
439 1 PRO B 969  ? ? -45.66  155.02  
440 1 LYS B 970  ? ? 58.32   19.01   
441 1 LEU B 977  ? ? -153.56 87.70   
442 1 LEU B 982  ? ? 93.38   143.48  
443 1 SER B 993  ? ? -162.70 -35.57  
444 1 SER B 1007 ? ? -59.22  -175.89 
445 1 GLU B 1009 ? ? -23.81  -60.94  
446 1 MET B 1013 ? ? -65.90  4.08    
447 1 VAL B 1016 ? ? -59.09  -76.78  
448 1 PRO B 1017 ? ? -38.65  -26.94  
449 1 ASN B 1029 ? ? -5.38   112.00  
450 1 HIS B 1030 ? ? -147.11 13.21   
451 1 SER B 1036 ? ? -78.86  -164.89 
452 1 SER B 1055 ? ? -46.51  -16.51  
453 1 MET B 1057 ? ? -29.36  -43.57  
454 1 ASN B 1061 ? ? -70.56  -161.62 
455 1 TYR B 1064 ? ? 86.10   -1.36   
456 1 VAL B 1068 ? ? -45.19  -81.88  
457 1 LYS B 1070 ? ? -37.16  128.79  
458 1 ARG B 1084 ? ? -35.77  -75.11  
459 1 GLN B 1097 ? ? -52.81  -90.31  
460 1 CYS B 1101 ? ? -43.12  -70.36  
461 1 LEU B 1105 ? ? -52.93  -2.60   
462 1 ASP B 1114 ? ? -74.79  41.25   
463 1 ASN B 1115 ? ? -162.22 18.18   
464 1 SER B 1122 ? ? -56.14  174.79  
465 1 ARG B 1153 ? ? -46.90  -75.75  
466 1 PHE B 1156 ? ? -39.65  -38.18  
467 1 VAL B 1162 ? ? -41.18  -78.30  
468 1 THR B 1166 ? ? -45.64  -71.50  
469 1 GLU B 1177 ? ? -60.22  11.86   
470 1 ASN B 1178 ? ? -155.52 -0.78   
471 1 PRO B 1181 ? ? -63.79  73.13   
472 1 ALA B 1192 ? ? -65.56  -75.37  
473 1 SER B 1196 ? ? -38.81  -34.31  
474 1 LEU B 1197 ? ? -96.59  46.16   
475 1 ALA B 1216 ? ? -47.61  174.52  
476 1 VAL B 1218 ? ? 178.95  169.37  
477 1 ASN B 1231 ? ? -57.55  -152.56 
478 1 LEU B 1232 ? ? -169.40 85.74   
479 1 LYS B 1235 ? ? 39.76   55.22   
480 1 SER B 1238 ? ? -69.81  81.05   
481 1 VAL B 1239 ? ? -101.46 45.77   
482 1 PRO B 1240 ? ? -50.56  67.61   
483 1 MET B 1247 ? ? -51.50  -72.03  
484 1 ASP B 1263 ? ? -70.95  35.27   
485 1 ILE B 1264 ? ? -22.38  -24.26  
486 1 ASN B 1268 ? ? -43.06  -19.51  
487 1 TYR B 1280 ? ? -19.65  118.02  
488 1 PHE B 1284 ? ? 10.24   -84.29  
489 1 SER B 1286 ? ? 41.57   -157.75 
490 1 LEU B 1297 ? ? -39.04  -14.49  
491 1 VAL B 1304 ? ? -56.14  -170.97 
492 1 ARG B 1308 ? ? -19.01  118.88  
493 1 SER B 1310 ? ? -176.09 35.54   
494 1 MET B 1311 ? ? -53.81  -158.56 
495 1 ASP B 1312 ? ? -172.34 55.44   
496 1 SER B 1316 ? ? -172.92 147.15  
497 1 THR B 1329 ? ? -165.62 -159.52 
498 1 LYS B 1331 ? ? -68.90  -72.59  
499 1 PHE B 1333 ? ? -148.38 -21.05  
500 1 PRO B 1337 ? ? -64.60  -178.96 
501 1 LEU B 1341 ? ? -67.44  -87.76  
502 1 LEU B 1342 ? ? -49.99  -173.32 
503 1 SER B 1349 ? ? -171.40 79.08   
504 1 PHE B 1352 ? ? -77.52  -102.87 
505 1 GLU B 1372 ? ? -56.08  -70.85  
506 1 GLU B 1373 ? ? -42.46  174.64  
507 1 LYS B 1400 ? ? -174.34 130.36  
508 1 ALA B 1406 ? ? -174.92 145.21  
509 1 ARG B 1412 ? ? -49.14  153.51  
510 1 GLU B 1413 ? ? 73.97   -13.19  
511 1 ILE B 1432 ? ? -150.51 41.76   
512 1 SER B 1433 ? ? -15.93  141.66  
513 1 ASN B 1435 ? ? -67.13  76.63   
514 1 GLU B 1444 ? ? -69.46  22.62   
515 1 ASP B 1447 ? ? -93.46  36.56   
516 1 THR B 1451 ? ? -144.98 -6.47   
517 1 GLN B 1454 ? ? -173.89 124.43  
518 1 ASP B 1457 ? ? 19.13   63.21   
519 1 PRO B 1468 ? ? -38.96  153.99  
520 1 PHE B 1483 ? ? -171.26 -172.40 
521 1 PRO B 1501 ? ? -56.66  7.36    
522 1 GLN B 1504 ? ? -68.88  87.84   
523 1 TYR Y 142  ? ? -80.48  46.31   
524 1 ASN Y 176  ? ? -142.14 -34.00  
525 1 LYS Y 185  ? ? 177.18  -27.54  
526 1 LEU Y 193  ? ? -135.81 -36.78  
527 1 ASP Y 195  ? ? -61.46  16.64   
528 1 MET Y 212  ? ? -59.05  -5.56   
529 1 ILE Y 221  ? ? -38.61  142.75  
# 
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  ? ? 138.70  
2 1 LEU B 651  ? ? THR B 652  ? ? 144.53  
3 1 THR B 1179 ? ? LEU B 1180 ? ? -149.08 
# 
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 LEU 749  ? A LEU 749  
33  1 Y 1 A PRO 871  ? A PRO 871  
34  1 Y 1 A VAL 872  ? A VAL 872  
35  1 Y 1 A ILE 873  ? A ILE 873  
36  1 Y 1 A ASP 874  ? A ASP 874  
37  1 Y 1 A HIS 875  ? A HIS 875  
38  1 Y 1 A GLN 876  ? A GLN 876  
39  1 Y 1 A GLY 877  ? A GLY 877  
40  1 Y 1 A THR 878  ? A THR 878  
41  1 Y 1 A LYS 879  ? A LYS 879  
42  1 Y 1 A SER 880  ? A SER 880  
43  1 Y 1 A SER 881  ? A SER 881  
44  1 Y 1 A GLU 1387 ? A GLU 1387 
45  1 Y 1 A ALA 1388 ? A ALA 1388 
46  1 Y 1 A SER 1389 ? A SER 1389 
47  1 Y 1 A HIS 1390 ? A HIS 1390 
48  1 Y 1 A TYR 1391 ? A TYR 1391 
49  1 Y 1 A ARG 1392 ? A ARG 1392 
50  1 Y 1 A GLY 1393 ? A GLY 1393 
51  1 Y 1 A TYR 1394 ? A TYR 1394 
52  1 Y 1 A GLY 1395 ? A GLY 1395 
53  1 Y 1 A ASN 1396 ? A ASN 1396 
54  1 Y 1 A SER 1397 ? A SER 1397 
55  1 Y 1 A ASP 1398 ? A ASP 1398 
56  1 Y 1 A LYS 1515 ? A LYS 1515 
57  1 Y 1 A ILE 1516 ? A ILE 1516 
58  1 Y 1 A GLN 1517 ? A GLN 1517 
59  1 Y 1 A LYS 1518 ? A LYS 1518 
60  1 Y 1 A VAL 1519 ? A VAL 1519 
61  1 Y 1 A CYS 1520 ? A CYS 1520 
62  1 Y 1 A GLU 1521 ? A GLU 1521 
63  1 Y 1 A GLY 1522 ? A GLY 1522 
64  1 Y 1 A ALA 1523 ? A ALA 1523 
65  1 Y 1 A ALA 1524 ? A ALA 1524 
66  1 Y 1 A CYS 1525 ? A CYS 1525 
67  1 Y 1 A LYS 1526 ? A LYS 1526 
68  1 Y 1 A CYS 1527 ? A CYS 1527 
69  1 Y 1 A VAL 1528 ? A VAL 1528 
70  1 Y 1 A GLU 1529 ? A GLU 1529 
71  1 Y 1 A ALA 1530 ? A ALA 1530 
72  1 Y 1 A ASP 1531 ? A ASP 1531 
73  1 Y 1 A CYS 1532 ? A CYS 1532 
74  1 Y 1 A GLY 1533 ? A GLY 1533 
75  1 Y 1 A GLN 1534 ? A GLN 1534 
76  1 Y 1 A MET 1535 ? A MET 1535 
77  1 Y 1 A GLN 1536 ? A GLN 1536 
78  1 Y 1 A GLU 1537 ? A GLU 1537 
79  1 Y 1 A GLU 1538 ? A GLU 1538 
80  1 Y 1 A LEU 1539 ? A LEU 1539 
81  1 Y 1 A ASP 1540 ? A ASP 1540 
82  1 Y 1 A LEU 1541 ? A LEU 1541 
83  1 Y 1 A THR 1542 ? A THR 1542 
84  1 Y 1 A ILE 1543 ? A ILE 1543 
85  1 Y 1 A SER 1544 ? A SER 1544 
86  1 Y 1 A ALA 1545 ? A ALA 1545 
87  1 Y 1 A GLU 1546 ? A GLU 1546 
88  1 Y 1 A THR 1547 ? A THR 1547 
89  1 Y 1 A ARG 1548 ? A ARG 1548 
90  1 Y 1 A LYS 1549 ? A LYS 1549 
91  1 Y 1 A GLN 1550 ? A GLN 1550 
92  1 Y 1 A THR 1551 ? A THR 1551 
93  1 Y 1 A ALA 1552 ? A ALA 1552 
94  1 Y 1 A CYS 1553 ? A CYS 1553 
95  1 Y 1 A LYS 1554 ? A LYS 1554 
96  1 Y 1 A PRO 1555 ? A PRO 1555 
97  1 Y 1 A GLU 1556 ? A GLU 1556 
98  1 Y 1 A ILE 1557 ? A ILE 1557 
99  1 Y 1 A ALA 1558 ? A ALA 1558 
100 1 Y 1 A TYR 1559 ? A TYR 1559 
101 1 Y 1 A ALA 1560 ? A ALA 1560 
102 1 Y 1 A TYR 1561 ? A TYR 1561 
103 1 Y 1 A LYS 1562 ? A LYS 1562 
104 1 Y 1 A VAL 1563 ? A VAL 1563 
105 1 Y 1 A SER 1564 ? A SER 1564 
106 1 Y 1 A ILE 1565 ? A ILE 1565 
107 1 Y 1 A THR 1566 ? A THR 1566 
108 1 Y 1 A SER 1567 ? A SER 1567 
109 1 Y 1 A ILE 1568 ? A ILE 1568 
110 1 Y 1 A THR 1569 ? A THR 1569 
111 1 Y 1 A VAL 1570 ? A VAL 1570 
112 1 Y 1 A GLU 1571 ? A GLU 1571 
113 1 Y 1 A ASN 1572 ? A ASN 1572 
114 1 Y 1 A VAL 1573 ? A VAL 1573 
115 1 Y 1 A PHE 1574 ? A PHE 1574 
116 1 Y 1 A VAL 1575 ? A VAL 1575 
117 1 Y 1 A LYS 1576 ? A LYS 1576 
118 1 Y 1 A TYR 1577 ? A TYR 1577 
119 1 Y 1 A LYS 1578 ? A LYS 1578 
120 1 Y 1 A ALA 1579 ? A ALA 1579 
121 1 Y 1 A THR 1580 ? A THR 1580 
122 1 Y 1 A LEU 1581 ? A LEU 1581 
123 1 Y 1 A LEU 1582 ? A LEU 1582 
124 1 Y 1 A ASP 1583 ? A ASP 1583 
125 1 Y 1 A ILE 1584 ? A ILE 1584 
126 1 Y 1 A TYR 1585 ? A TYR 1585 
127 1 Y 1 A LYS 1586 ? A LYS 1586 
128 1 Y 1 A THR 1587 ? A THR 1587 
129 1 Y 1 A GLY 1588 ? A GLY 1588 
130 1 Y 1 A GLU 1589 ? A GLU 1589 
131 1 Y 1 A ALA 1590 ? A ALA 1590 
132 1 Y 1 A VAL 1591 ? A VAL 1591 
133 1 Y 1 A ALA 1592 ? A ALA 1592 
134 1 Y 1 A GLU 1593 ? A GLU 1593 
135 1 Y 1 A LYS 1594 ? A LYS 1594 
136 1 Y 1 A ASP 1595 ? A ASP 1595 
137 1 Y 1 A SER 1596 ? A SER 1596 
138 1 Y 1 A GLU 1597 ? A GLU 1597 
139 1 Y 1 A ILE 1598 ? A ILE 1598 
140 1 Y 1 A THR 1599 ? A THR 1599 
141 1 Y 1 A PHE 1600 ? A PHE 1600 
142 1 Y 1 A ILE 1601 ? A ILE 1601 
143 1 Y 1 A LYS 1602 ? A LYS 1602 
144 1 Y 1 A LYS 1603 ? A LYS 1603 
145 1 Y 1 A VAL 1604 ? A VAL 1604 
146 1 Y 1 A THR 1605 ? A THR 1605 
147 1 Y 1 A CYS 1606 ? A CYS 1606 
148 1 Y 1 A THR 1607 ? A THR 1607 
149 1 Y 1 A ASN 1608 ? A ASN 1608 
150 1 Y 1 A ALA 1609 ? A ALA 1609 
151 1 Y 1 A GLU 1610 ? A GLU 1610 
152 1 Y 1 A LEU 1611 ? A LEU 1611 
153 1 Y 1 A VAL 1612 ? A VAL 1612 
154 1 Y 1 A LYS 1613 ? A LYS 1613 
155 1 Y 1 A GLY 1614 ? A GLY 1614 
156 1 Y 1 A ARG 1615 ? A ARG 1615 
157 1 Y 1 A GLN 1616 ? A GLN 1616 
158 1 Y 1 A TYR 1617 ? A TYR 1617 
159 1 Y 1 A LEU 1618 ? A LEU 1618 
160 1 Y 1 A ILE 1619 ? A ILE 1619 
161 1 Y 1 A MET 1620 ? A MET 1620 
162 1 Y 1 A GLY 1621 ? A GLY 1621 
163 1 Y 1 A LYS 1622 ? A LYS 1622 
164 1 Y 1 A GLU 1623 ? A GLU 1623 
165 1 Y 1 A ALA 1624 ? A ALA 1624 
166 1 Y 1 A LEU 1625 ? A LEU 1625 
167 1 Y 1 A GLN 1626 ? A GLN 1626 
168 1 Y 1 A ILE 1627 ? A ILE 1627 
169 1 Y 1 A LYS 1628 ? A LYS 1628 
170 1 Y 1 A TYR 1629 ? A TYR 1629 
171 1 Y 1 A ASN 1630 ? A ASN 1630 
172 1 Y 1 A PHE 1631 ? A PHE 1631 
173 1 Y 1 A SER 1632 ? A SER 1632 
174 1 Y 1 A PHE 1633 ? A PHE 1633 
175 1 Y 1 A ARG 1634 ? A ARG 1634 
176 1 Y 1 A TYR 1635 ? A TYR 1635 
177 1 Y 1 A ILE 1636 ? A ILE 1636 
178 1 Y 1 A TYR 1637 ? A TYR 1637 
179 1 Y 1 A PRO 1638 ? A PRO 1638 
180 1 Y 1 A LEU 1639 ? A LEU 1639 
181 1 Y 1 A ASP 1640 ? A ASP 1640 
182 1 Y 1 A SER 1641 ? A SER 1641 
183 1 Y 1 A LEU 1642 ? A LEU 1642 
184 1 Y 1 A THR 1643 ? A THR 1643 
185 1 Y 1 A TRP 1644 ? A TRP 1644 
186 1 Y 1 A ILE 1645 ? A ILE 1645 
187 1 Y 1 A GLU 1646 ? A GLU 1646 
188 1 Y 1 A TYR 1647 ? A TYR 1647 
189 1 Y 1 A TRP 1648 ? A TRP 1648 
190 1 Y 1 A PRO 1649 ? A PRO 1649 
191 1 Y 1 A ARG 1650 ? A ARG 1650 
192 1 Y 1 A ASP 1651 ? A ASP 1651 
193 1 Y 1 A THR 1652 ? A THR 1652 
194 1 Y 1 A THR 1653 ? A THR 1653 
195 1 Y 1 A CYS 1654 ? A CYS 1654 
196 1 Y 1 A SER 1655 ? A SER 1655 
197 1 Y 1 A SER 1656 ? A SER 1656 
198 1 Y 1 A CYS 1657 ? A CYS 1657 
199 1 Y 1 A GLN 1658 ? A GLN 1658 
200 1 Y 1 A ALA 1659 ? A ALA 1659 
201 1 Y 1 A PHE 1660 ? A PHE 1660 
202 1 Y 1 A LEU 1661 ? A LEU 1661 
203 1 Y 1 A ALA 1662 ? A ALA 1662 
204 1 Y 1 A ASN 1663 ? A ASN 1663 
205 1 Y 1 A LEU 1664 ? A LEU 1664 
206 1 Y 1 A ASP 1665 ? A ASP 1665 
207 1 Y 1 A GLU 1666 ? A GLU 1666 
208 1 Y 1 A PHE 1667 ? A PHE 1667 
209 1 Y 1 A ALA 1668 ? A ALA 1668 
210 1 Y 1 A GLU 1669 ? A GLU 1669 
211 1 Y 1 A ASP 1670 ? A ASP 1670 
212 1 Y 1 A ILE 1671 ? A ILE 1671 
213 1 Y 1 A PHE 1672 ? A PHE 1672 
214 1 Y 1 A LEU 1673 ? A LEU 1673 
215 1 Y 1 A ASN 1674 ? A ASN 1674 
216 1 Y 1 A GLY 1675 ? A GLY 1675 
217 1 Y 1 A CYS 1676 ? A CYS 1676 
218 1 Y 1 X ILE 231  ? B ILE 103  
219 1 Y 1 B MET 1    ? C MET 1    
220 1 Y 1 B GLY 2    ? C GLY 2    
221 1 Y 1 B LEU 3    ? C LEU 3    
222 1 Y 1 B LEU 4    ? C LEU 4    
223 1 Y 1 B GLY 5    ? C GLY 5    
224 1 Y 1 B ILE 6    ? C ILE 6    
225 1 Y 1 B LEU 7    ? C LEU 7    
226 1 Y 1 B CYS 8    ? C CYS 8    
227 1 Y 1 B PHE 9    ? C PHE 9    
228 1 Y 1 B LEU 10   ? C LEU 10   
229 1 Y 1 B ILE 11   ? C ILE 11   
230 1 Y 1 B PHE 12   ? C PHE 12   
231 1 Y 1 B LEU 13   ? C LEU 13   
232 1 Y 1 B GLY 14   ? C GLY 14   
233 1 Y 1 B LYS 15   ? C LYS 15   
234 1 Y 1 B THR 16   ? C THR 16   
235 1 Y 1 B TRP 17   ? C TRP 17   
236 1 Y 1 B GLY 18   ? C GLY 18   
237 1 Y 1 B GLN 19   ? C GLN 19   
238 1 Y 1 B GLU 20   ? C GLU 20   
239 1 Y 1 B GLN 21   ? C GLN 21   
240 1 Y 1 B ARG 674  ? C ARG 674  
241 1 Y 1 B PRO 675  ? C PRO 675  
242 1 Y 1 B ARG 676  ? C ARG 676  
243 1 Y 1 B ARG 677  ? C ARG 677  
244 1 Y 1 B THR 678  ? C THR 678  
245 1 Y 1 B HIS 744  ? C HIS 744  
246 1 Y 1 B LYS 745  ? C LYS 745  
247 1 Y 1 B ASP 746  ? C ASP 746  
248 1 Y 1 B MET 747  ? C MET 747  
249 1 Y 1 B GLN 748  ? C GLN 748  
250 1 Y 1 B LEU 749  ? C LEU 749  
251 1 Y 1 B PRO 871  ? C PRO 871  
252 1 Y 1 B VAL 872  ? C VAL 872  
253 1 Y 1 B ILE 873  ? C ILE 873  
254 1 Y 1 B ASP 874  ? C ASP 874  
255 1 Y 1 B HIS 875  ? C HIS 875  
256 1 Y 1 B GLN 876  ? C GLN 876  
257 1 Y 1 B GLY 877  ? C GLY 877  
258 1 Y 1 B THR 878  ? C THR 878  
259 1 Y 1 B LYS 879  ? C LYS 879  
260 1 Y 1 B SER 880  ? C SER 880  
261 1 Y 1 B SER 881  ? C SER 881  
262 1 Y 1 B GLU 1387 ? C GLU 1387 
263 1 Y 1 B ALA 1388 ? C ALA 1388 
264 1 Y 1 B SER 1389 ? C SER 1389 
265 1 Y 1 B HIS 1390 ? C HIS 1390 
266 1 Y 1 B TYR 1391 ? C TYR 1391 
267 1 Y 1 B ARG 1392 ? C ARG 1392 
268 1 Y 1 B GLY 1393 ? C GLY 1393 
269 1 Y 1 B TYR 1394 ? C TYR 1394 
270 1 Y 1 B GLY 1395 ? C GLY 1395 
271 1 Y 1 B ASN 1396 ? C ASN 1396 
272 1 Y 1 B SER 1397 ? C SER 1397 
273 1 Y 1 B ASP 1398 ? C ASP 1398 
274 1 Y 1 B LYS 1515 ? C LYS 1515 
275 1 Y 1 B ILE 1516 ? C ILE 1516 
276 1 Y 1 B GLN 1517 ? C GLN 1517 
277 1 Y 1 B LYS 1518 ? C LYS 1518 
278 1 Y 1 B VAL 1519 ? C VAL 1519 
279 1 Y 1 B CYS 1520 ? C CYS 1520 
280 1 Y 1 B GLU 1521 ? C GLU 1521 
281 1 Y 1 B GLY 1522 ? C GLY 1522 
282 1 Y 1 B ALA 1523 ? C ALA 1523 
283 1 Y 1 B ALA 1524 ? C ALA 1524 
284 1 Y 1 B CYS 1525 ? C CYS 1525 
285 1 Y 1 B LYS 1526 ? C LYS 1526 
286 1 Y 1 B CYS 1527 ? C CYS 1527 
287 1 Y 1 B VAL 1528 ? C VAL 1528 
288 1 Y 1 B GLU 1529 ? C GLU 1529 
289 1 Y 1 B ALA 1530 ? C ALA 1530 
290 1 Y 1 B ASP 1531 ? C ASP 1531 
291 1 Y 1 B CYS 1532 ? C CYS 1532 
292 1 Y 1 B GLY 1533 ? C GLY 1533 
293 1 Y 1 B GLN 1534 ? C GLN 1534 
294 1 Y 1 B MET 1535 ? C MET 1535 
295 1 Y 1 B GLN 1536 ? C GLN 1536 
296 1 Y 1 B GLU 1537 ? C GLU 1537 
297 1 Y 1 B GLU 1538 ? C GLU 1538 
298 1 Y 1 B LEU 1539 ? C LEU 1539 
299 1 Y 1 B ASP 1540 ? C ASP 1540 
300 1 Y 1 B LEU 1541 ? C LEU 1541 
301 1 Y 1 B THR 1542 ? C THR 1542 
302 1 Y 1 B ILE 1543 ? C ILE 1543 
303 1 Y 1 B SER 1544 ? C SER 1544 
304 1 Y 1 B ALA 1545 ? C ALA 1545 
305 1 Y 1 B GLU 1546 ? C GLU 1546 
306 1 Y 1 B THR 1547 ? C THR 1547 
307 1 Y 1 B ARG 1548 ? C ARG 1548 
308 1 Y 1 B LYS 1549 ? C LYS 1549 
309 1 Y 1 B GLN 1550 ? C GLN 1550 
310 1 Y 1 B THR 1551 ? C THR 1551 
311 1 Y 1 B ALA 1552 ? C ALA 1552 
312 1 Y 1 B CYS 1553 ? C CYS 1553 
313 1 Y 1 B LYS 1554 ? C LYS 1554 
314 1 Y 1 B PRO 1555 ? C PRO 1555 
315 1 Y 1 B GLU 1556 ? C GLU 1556 
316 1 Y 1 B ILE 1557 ? C ILE 1557 
317 1 Y 1 B ALA 1558 ? C ALA 1558 
318 1 Y 1 B TYR 1559 ? C TYR 1559 
319 1 Y 1 B ALA 1560 ? C ALA 1560 
320 1 Y 1 B TYR 1561 ? C TYR 1561 
321 1 Y 1 B LYS 1562 ? C LYS 1562 
322 1 Y 1 B VAL 1563 ? C VAL 1563 
323 1 Y 1 B SER 1564 ? C SER 1564 
324 1 Y 1 B ILE 1565 ? C ILE 1565 
325 1 Y 1 B THR 1566 ? C THR 1566 
326 1 Y 1 B SER 1567 ? C SER 1567 
327 1 Y 1 B ILE 1568 ? C ILE 1568 
328 1 Y 1 B THR 1569 ? C THR 1569 
329 1 Y 1 B VAL 1570 ? C VAL 1570 
330 1 Y 1 B GLU 1571 ? C GLU 1571 
331 1 Y 1 B ASN 1572 ? C ASN 1572 
332 1 Y 1 B VAL 1573 ? C VAL 1573 
333 1 Y 1 B PHE 1574 ? C PHE 1574 
334 1 Y 1 B VAL 1575 ? C VAL 1575 
335 1 Y 1 B LYS 1576 ? C LYS 1576 
336 1 Y 1 B TYR 1577 ? C TYR 1577 
337 1 Y 1 B LYS 1578 ? C LYS 1578 
338 1 Y 1 B ALA 1579 ? C ALA 1579 
339 1 Y 1 B THR 1580 ? C THR 1580 
340 1 Y 1 B LEU 1581 ? C LEU 1581 
341 1 Y 1 B LEU 1582 ? C LEU 1582 
342 1 Y 1 B ASP 1583 ? C ASP 1583 
343 1 Y 1 B ILE 1584 ? C ILE 1584 
344 1 Y 1 B TYR 1585 ? C TYR 1585 
345 1 Y 1 B LYS 1586 ? C LYS 1586 
346 1 Y 1 B THR 1587 ? C THR 1587 
347 1 Y 1 B GLY 1588 ? C GLY 1588 
348 1 Y 1 B GLU 1589 ? C GLU 1589 
349 1 Y 1 B ALA 1590 ? C ALA 1590 
350 1 Y 1 B VAL 1591 ? C VAL 1591 
351 1 Y 1 B ALA 1592 ? C ALA 1592 
352 1 Y 1 B GLU 1593 ? C GLU 1593 
353 1 Y 1 B LYS 1594 ? C LYS 1594 
354 1 Y 1 B ASP 1595 ? C ASP 1595 
355 1 Y 1 B SER 1596 ? C SER 1596 
356 1 Y 1 B GLU 1597 ? C GLU 1597 
357 1 Y 1 B ILE 1598 ? C ILE 1598 
358 1 Y 1 B THR 1599 ? C THR 1599 
359 1 Y 1 B PHE 1600 ? C PHE 1600 
360 1 Y 1 B ILE 1601 ? C ILE 1601 
361 1 Y 1 B LYS 1602 ? C LYS 1602 
362 1 Y 1 B LYS 1603 ? C LYS 1603 
363 1 Y 1 B VAL 1604 ? C VAL 1604 
364 1 Y 1 B THR 1605 ? C THR 1605 
365 1 Y 1 B CYS 1606 ? C CYS 1606 
366 1 Y 1 B THR 1607 ? C THR 1607 
367 1 Y 1 B ASN 1608 ? C ASN 1608 
368 1 Y 1 B ALA 1609 ? C ALA 1609 
369 1 Y 1 B GLU 1610 ? C GLU 1610 
370 1 Y 1 B LEU 1611 ? C LEU 1611 
371 1 Y 1 B VAL 1612 ? C VAL 1612 
372 1 Y 1 B LYS 1613 ? C LYS 1613 
373 1 Y 1 B GLY 1614 ? C GLY 1614 
374 1 Y 1 B ARG 1615 ? C ARG 1615 
375 1 Y 1 B GLN 1616 ? C GLN 1616 
376 1 Y 1 B TYR 1617 ? C TYR 1617 
377 1 Y 1 B LEU 1618 ? C LEU 1618 
378 1 Y 1 B ILE 1619 ? C ILE 1619 
379 1 Y 1 B MET 1620 ? C MET 1620 
380 1 Y 1 B GLY 1621 ? C GLY 1621 
381 1 Y 1 B LYS 1622 ? C LYS 1622 
382 1 Y 1 B GLU 1623 ? C GLU 1623 
383 1 Y 1 B ALA 1624 ? C ALA 1624 
384 1 Y 1 B LEU 1625 ? C LEU 1625 
385 1 Y 1 B GLN 1626 ? C GLN 1626 
386 1 Y 1 B ILE 1627 ? C ILE 1627 
387 1 Y 1 B LYS 1628 ? C LYS 1628 
388 1 Y 1 B TYR 1629 ? C TYR 1629 
389 1 Y 1 B ASN 1630 ? C ASN 1630 
390 1 Y 1 B PHE 1631 ? C PHE 1631 
391 1 Y 1 B SER 1632 ? C SER 1632 
392 1 Y 1 B PHE 1633 ? C PHE 1633 
393 1 Y 1 B ARG 1634 ? C ARG 1634 
394 1 Y 1 B TYR 1635 ? C TYR 1635 
395 1 Y 1 B ILE 1636 ? C ILE 1636 
396 1 Y 1 B TYR 1637 ? C TYR 1637 
397 1 Y 1 B PRO 1638 ? C PRO 1638 
398 1 Y 1 B LEU 1639 ? C LEU 1639 
399 1 Y 1 B ASP 1640 ? C ASP 1640 
400 1 Y 1 B SER 1641 ? C SER 1641 
401 1 Y 1 B LEU 1642 ? C LEU 1642 
402 1 Y 1 B THR 1643 ? C THR 1643 
403 1 Y 1 B TRP 1644 ? C TRP 1644 
404 1 Y 1 B ILE 1645 ? C ILE 1645 
405 1 Y 1 B GLU 1646 ? C GLU 1646 
406 1 Y 1 B TYR 1647 ? C TYR 1647 
407 1 Y 1 B TRP 1648 ? C TRP 1648 
408 1 Y 1 B PRO 1649 ? C PRO 1649 
409 1 Y 1 B ARG 1650 ? C ARG 1650 
410 1 Y 1 B ASP 1651 ? C ASP 1651 
411 1 Y 1 B THR 1652 ? C THR 1652 
412 1 Y 1 B THR 1653 ? C THR 1653 
413 1 Y 1 B CYS 1654 ? C CYS 1654 
414 1 Y 1 B SER 1655 ? C SER 1655 
415 1 Y 1 B SER 1656 ? C SER 1656 
416 1 Y 1 B CYS 1657 ? C CYS 1657 
417 1 Y 1 B GLN 1658 ? C GLN 1658 
418 1 Y 1 B ALA 1659 ? C ALA 1659 
419 1 Y 1 B PHE 1660 ? C PHE 1660 
420 1 Y 1 B LEU 1661 ? C LEU 1661 
421 1 Y 1 B ALA 1662 ? C ALA 1662 
422 1 Y 1 B ASN 1663 ? C ASN 1663 
423 1 Y 1 B LEU 1664 ? C LEU 1664 
424 1 Y 1 B ASP 1665 ? C ASP 1665 
425 1 Y 1 B GLU 1666 ? C GLU 1666 
426 1 Y 1 B PHE 1667 ? C PHE 1667 
427 1 Y 1 B ALA 1668 ? C ALA 1668 
428 1 Y 1 B GLU 1669 ? C GLU 1669 
429 1 Y 1 B ASP 1670 ? C ASP 1670 
430 1 Y 1 B ILE 1671 ? C ILE 1671 
431 1 Y 1 B PHE 1672 ? C PHE 1672 
432 1 Y 1 B LEU 1673 ? C LEU 1673 
433 1 Y 1 B ASN 1674 ? C ASN 1674 
434 1 Y 1 B GLY 1675 ? C GLY 1675 
435 1 Y 1 B CYS 1676 ? C CYS 1676 
436 1 Y 1 Y ILE 231  ? D ILE 103  
# 
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 
# 
