data_3BVT
# 
_entry.id   3BVT 
# 
_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   3BVT         
RCSB  RCSB046018   
WWPDB D_1000046018 
# 
loop_
_pdbx_database_related.db_name 
_pdbx_database_related.db_id 
_pdbx_database_related.details 
_pdbx_database_related.content_type 
PDB 1HTY 'dGMII + Tris'                                                                                       unspecified 
PDB 1HWW 'dGMII + Swainsonine'                                                                                unspecified 
PDB 1HXK 'dGMII + Deoxymannojirimicin'                                                                        unspecified 
PDB 1PS2 'dGMII + Kifunensine'                                                                                unspecified 
PDB 1QWN 'dGMII + 5fluoro-Gulosylfluoride'                                                                    unspecified 
PDB 1QX1 'dGMII + 2F-mannosylF'                                                                               unspecified 
PDB 1R33 'dGMII + 5-thio-D-mannopyranosylamine'                                                               unspecified 
PDB 1R34 'dGMII + 5-thio-D-mannopyranosylamidinium salt'                                                      unspecified 
PDB 1TQS 'dGMII + Salacinol'                                                                                  unspecified 
PDB 1TQT 'dGMII + Diastereomer of Salacinol'                                                                  unspecified 
PDB 1TQU 'dGMII + Ghavamiol'                                                                                  unspecified 
PDB 1TQV 'dGMII + Blintol'                                                                                    unspecified 
PDB 1TQW 'dGMII + Blintol Diastereomer'                                                                       unspecified 
PDB 2ALW 'dGMII + Noeuromycin'                                                                                unspecified 
PDB 2F18 'dGMII + (2R,3R,4S)-2-({[(1R)-2-hydroxy-1-phenylethyl]amino}methyl)pyrrolidine-3,4-diol'             unspecified 
PDB 2F1A 'dGMII + (2R,3R,4S)-2-({[(1S)-2-hydroxy-1-phenylethyl]amino}methyl)pyrrolidine-3,4-diol'             unspecified 
PDB 2F1B 'dGMII + (2R,3R,4S,5R)-2-({[(1R)-2-hydroxy-1-phenylethyl]amino}methyl)-5-methylpyrrolidine-3,4-diol' unspecified 
PDB 2F7O 'dGMII + Mannostatin A'                                                                              unspecified 
PDB 2F7P 'dGMII + Benzyl-mannostatin A'                                                                       unspecified 
PDB 2F7Q 'dGMII + Aminocyclopentitetrol'                                                                      unspecified 
PDB 2F7R 'dGMII + Benzyl-aminocyclopentitetrol'                                                               unspecified 
PDB 3BUB 'dGMII empty active site'                                                                            unspecified 
PDB 3BUD 'dGMII nucleophile mutant D204A empty active site'                                                   unspecified 
PDB 3BUI 'dGMII nucleophile mutant D204A + tris'                                                              unspecified 
PDB 3BUP 'dGMII acid-base catalyst mutant D341N + mannose'                                                    unspecified 
PDB 3BUQ 'dGMII nucleophile mutant D204A + mannose'                                                           unspecified 
PDB 3BVU 'dGMII_D204A + substrate WZ2'                                                                        unspecified 
PDB 3BVV 'dGMII_D204A + substrate WZ3'                                                                        unspecified 
PDB 3BVW 'dGMII_D204A + substrate WZ4'                                                                        unspecified 
PDB 3BVX 'dGMII_D204A + substrate WZ5'                                                                        unspecified 
# 
_pdbx_database_status.entry_id                        3BVT 
_pdbx_database_status.deposit_site                    RCSB 
_pdbx_database_status.process_site                    RCSB 
_pdbx_database_status.recvd_initial_deposition_date   2008-01-07 
_pdbx_database_status.status_code                     REL 
_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 
'Kuntz, D.A.' 1 
'Rose, D.R.'  2 
# 
_citation.id                        primary 
_citation.title                     
;Probing the substrate specificity of Golgi alpha-mannosidase II by use of synthetic oligosaccharides and a catalytic nucleophile mutant.
;
_citation.journal_abbrev            J.Am.Chem.Soc. 
_citation.journal_volume            130 
_citation.page_first                8975 
_citation.page_last                 8983 
_citation.year                      2008 
_citation.journal_id_ASTM           JACSAT 
_citation.country                   US 
_citation.journal_id_ISSN           0002-7863 
_citation.journal_id_CSD            0004 
_citation.book_publisher            ? 
_citation.pdbx_database_id_PubMed   18558690 
_citation.pdbx_database_id_DOI      10.1021/ja711248y 
# 
loop_
_citation_author.citation_id 
_citation_author.name 
_citation_author.ordinal 
primary 'Zhong, W.'     1 
primary 'Kuntz, D.A.'   2 
primary 'Ember, B.'     3 
primary 'Singh, H.'     4 
primary 'Moremen, K.W.' 5 
primary 'Rose, D.R.'    6 
primary 'Boons, G.J.'   7 
# 
_cell.length_a           69.040 
_cell.length_b           109.847 
_cell.length_c           138.627 
_cell.angle_alpha        90.000 
_cell.angle_beta         90.000 
_cell.angle_gamma        90.000 
_cell.entry_id           3BVT 
_cell.pdbx_unique_axis   ? 
_cell.Z_PDB              4 
_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.space_group_name_H-M             'P 21 21 21' 
_symmetry.entry_id                         3BVT 
_symmetry.Int_Tables_number                19 
_symmetry.pdbx_full_space_group_name_H-M   ? 
_symmetry.cell_setting                     ? 
_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     man 'Alpha-mannosidase 2'                                              119657.602 1    3.2.1.114 D204A 
'Catalytic domain; UNP residues 76-1108' ? 
2 non-polymer man N-ACETYL-D-GLUCOSAMINE                                             221.208    1    ?         ?     ? ? 
3 non-polymer syn 'PHOSPHATE ION'                                                    94.971     1    ?         ?     ? ? 
4 non-polymer syn 'ZINC ION'                                                         65.409     1    ?         ?     ? ? 
5 non-polymer syn '(4R)-2-METHYLPENTANE-2,4-DIOL'                                    118.174    1    ?         ?     ? ? 
6 non-polymer syn 'methyl 3-S-alpha-D-mannopyranosyl-3-thio-alpha-D-mannopyranoside' 372.389    1    ?         ?     ? ? 
7 non-polymer syn '(4S)-2-METHYL-2,4-PENTANEDIOL'                                    118.174    2    ?         ?     ? ? 
8 water       nat water                                                              18.015     1453 ?         ?     ? ? 
# 
_entity_name_com.entity_id   1 
_entity_name_com.name        
'Alpha-mannosidase II, Mannosyl-oligosaccharide 1,3-1,6-alpha-mannosidase, MAN II, Golgi alpha-mannosidase II, AMAN II' 
# 
_entity_poly.entity_id                      1 
_entity_poly.type                           'polypeptide(L)' 
_entity_poly.nstd_linkage                   no 
_entity_poly.nstd_monomer                   no 
_entity_poly.pdbx_seq_one_letter_code       
;RSSHHHHHHGEFDDPIRPPLKVARSPRPGQCQDVVQDVPNVDVQMLELYDRMSFKDIDGGVWKQGWNIKYDPLKYNAHHK
LKVFVVPHSHNDPGWIQTFEEYYQHDTKHILSNALRHLHDNPEMKFIWAEISYFARFYHDLGENKKLQMKSIVKNGQLEF
VTGGWVMPDEANSHWRNVLLQLTEGQTWLKQFMNVTPTASWAIAPFGHSPTMPYILQKSGFKNMLIQRTHYSVKKELAQQ
RQLEFLWRQIWDNKGDTALFTHMMPFYSYDIPHTCGPDPKVCCQFDFKRMGSFGLSCPWKVPPRTISDQNVAARSDLLVD
QWKKKAELYRTNVLLIPLGDDFRFKQNTEWDVQRVNYERLFEHINSQAHFNVQAQFGTLQEYFDAVHQAERAGQAEFPTL
SGDFFTYADRSDNYWSGYYTSRPYHKRMDRVLMHYVRAAEMLSAWHSWDGMARIEERLEQARRELSLFQHHDGITGTAKT
HVVVDYEQRMQEALKACQMVMQQSVYRLLTKPSIYSPDFSFSYFTLDDSRWPGSGVEDSRTTIILGEDILPSKHVVMHNT
LPHWREQLVDFYVSSPFVSVTDLANNPVEAQVSPVWSWHHDTLTKTIHPQGSTTKYRIIFKARVPPMGLATYVLTISDSK
PEHTSYASNLLLRKNPTSLPLGQYPEDVKFGDPREISLRVGNGPTLAFSEQGLLKSIQLTQDSPHVPVHFKFLKYGVRSH
GDRSGAYLFLPNGPASPVELGQPVVLVTKGKLESSVSVGLPSVVHQTIMRGGAPEIRNLVDIGSLDNTEIVMRLETHIDS
GDIFYTDLNGLQFIKRRRLDKLPLQANYYPIPSGMFIEDANTRLTLLTGQPLGGSSLASGELEIMQDRRLASDDERGLGQ
GVLDNKPVLHIYRLVLEKVNNCVRPSKLHPAGYLTSAAHKASQSLLDPLDKFIFAENEWIGAQGQFGGDHPSAREDLDVS
VMRRLTKSSAKTQRVGYVLHRTNLMQCGTPEEHTQKLDVCHLLPNVARCERTTLTFLQNLEHLDGMVAPEVCPMETAAYV
SSHSS
;
_entity_poly.pdbx_seq_one_letter_code_can   
;RSSHHHHHHGEFDDPIRPPLKVARSPRPGQCQDVVQDVPNVDVQMLELYDRMSFKDIDGGVWKQGWNIKYDPLKYNAHHK
LKVFVVPHSHNDPGWIQTFEEYYQHDTKHILSNALRHLHDNPEMKFIWAEISYFARFYHDLGENKKLQMKSIVKNGQLEF
VTGGWVMPDEANSHWRNVLLQLTEGQTWLKQFMNVTPTASWAIAPFGHSPTMPYILQKSGFKNMLIQRTHYSVKKELAQQ
RQLEFLWRQIWDNKGDTALFTHMMPFYSYDIPHTCGPDPKVCCQFDFKRMGSFGLSCPWKVPPRTISDQNVAARSDLLVD
QWKKKAELYRTNVLLIPLGDDFRFKQNTEWDVQRVNYERLFEHINSQAHFNVQAQFGTLQEYFDAVHQAERAGQAEFPTL
SGDFFTYADRSDNYWSGYYTSRPYHKRMDRVLMHYVRAAEMLSAWHSWDGMARIEERLEQARRELSLFQHHDGITGTAKT
HVVVDYEQRMQEALKACQMVMQQSVYRLLTKPSIYSPDFSFSYFTLDDSRWPGSGVEDSRTTIILGEDILPSKHVVMHNT
LPHWREQLVDFYVSSPFVSVTDLANNPVEAQVSPVWSWHHDTLTKTIHPQGSTTKYRIIFKARVPPMGLATYVLTISDSK
PEHTSYASNLLLRKNPTSLPLGQYPEDVKFGDPREISLRVGNGPTLAFSEQGLLKSIQLTQDSPHVPVHFKFLKYGVRSH
GDRSGAYLFLPNGPASPVELGQPVVLVTKGKLESSVSVGLPSVVHQTIMRGGAPEIRNLVDIGSLDNTEIVMRLETHIDS
GDIFYTDLNGLQFIKRRRLDKLPLQANYYPIPSGMFIEDANTRLTLLTGQPLGGSSLASGELEIMQDRRLASDDERGLGQ
GVLDNKPVLHIYRLVLEKVNNCVRPSKLHPAGYLTSAAHKASQSLLDPLDKFIFAENEWIGAQGQFGGDHPSAREDLDVS
VMRRLTKSSAKTQRVGYVLHRTNLMQCGTPEEHTQKLDVCHLLPNVARCERTTLTFLQNLEHLDGMVAPEVCPMETAAYV
SSHSS
;
_entity_poly.pdbx_strand_id                 A 
_entity_poly.pdbx_target_identifier         ? 
# 
loop_
_entity_poly_seq.entity_id 
_entity_poly_seq.num 
_entity_poly_seq.mon_id 
_entity_poly_seq.hetero 
1 1    ARG n 
1 2    SER n 
1 3    SER n 
1 4    HIS n 
1 5    HIS n 
1 6    HIS n 
1 7    HIS n 
1 8    HIS n 
1 9    HIS n 
1 10   GLY n 
1 11   GLU n 
1 12   PHE n 
1 13   ASP n 
1 14   ASP n 
1 15   PRO n 
1 16   ILE n 
1 17   ARG n 
1 18   PRO n 
1 19   PRO n 
1 20   LEU n 
1 21   LYS n 
1 22   VAL n 
1 23   ALA n 
1 24   ARG n 
1 25   SER n 
1 26   PRO n 
1 27   ARG n 
1 28   PRO n 
1 29   GLY n 
1 30   GLN n 
1 31   CYS n 
1 32   GLN n 
1 33   ASP n 
1 34   VAL n 
1 35   VAL n 
1 36   GLN n 
1 37   ASP n 
1 38   VAL n 
1 39   PRO n 
1 40   ASN n 
1 41   VAL n 
1 42   ASP n 
1 43   VAL n 
1 44   GLN n 
1 45   MET n 
1 46   LEU n 
1 47   GLU n 
1 48   LEU n 
1 49   TYR n 
1 50   ASP n 
1 51   ARG n 
1 52   MET n 
1 53   SER n 
1 54   PHE n 
1 55   LYS n 
1 56   ASP n 
1 57   ILE n 
1 58   ASP n 
1 59   GLY n 
1 60   GLY n 
1 61   VAL n 
1 62   TRP n 
1 63   LYS n 
1 64   GLN n 
1 65   GLY n 
1 66   TRP n 
1 67   ASN n 
1 68   ILE n 
1 69   LYS n 
1 70   TYR n 
1 71   ASP n 
1 72   PRO n 
1 73   LEU n 
1 74   LYS n 
1 75   TYR n 
1 76   ASN n 
1 77   ALA n 
1 78   HIS n 
1 79   HIS n 
1 80   LYS n 
1 81   LEU n 
1 82   LYS n 
1 83   VAL n 
1 84   PHE n 
1 85   VAL n 
1 86   VAL n 
1 87   PRO n 
1 88   HIS n 
1 89   SER n 
1 90   HIS n 
1 91   ASN n 
1 92   ASP n 
1 93   PRO n 
1 94   GLY n 
1 95   TRP n 
1 96   ILE n 
1 97   GLN n 
1 98   THR n 
1 99   PHE n 
1 100  GLU n 
1 101  GLU n 
1 102  TYR n 
1 103  TYR n 
1 104  GLN n 
1 105  HIS n 
1 106  ASP n 
1 107  THR n 
1 108  LYS n 
1 109  HIS n 
1 110  ILE n 
1 111  LEU n 
1 112  SER n 
1 113  ASN n 
1 114  ALA n 
1 115  LEU n 
1 116  ARG n 
1 117  HIS n 
1 118  LEU n 
1 119  HIS n 
1 120  ASP n 
1 121  ASN n 
1 122  PRO n 
1 123  GLU n 
1 124  MET n 
1 125  LYS n 
1 126  PHE n 
1 127  ILE n 
1 128  TRP n 
1 129  ALA n 
1 130  GLU n 
1 131  ILE n 
1 132  SER n 
1 133  TYR n 
1 134  PHE n 
1 135  ALA n 
1 136  ARG n 
1 137  PHE n 
1 138  TYR n 
1 139  HIS n 
1 140  ASP n 
1 141  LEU n 
1 142  GLY n 
1 143  GLU n 
1 144  ASN n 
1 145  LYS n 
1 146  LYS n 
1 147  LEU n 
1 148  GLN n 
1 149  MET n 
1 150  LYS n 
1 151  SER n 
1 152  ILE n 
1 153  VAL n 
1 154  LYS n 
1 155  ASN n 
1 156  GLY n 
1 157  GLN n 
1 158  LEU n 
1 159  GLU n 
1 160  PHE n 
1 161  VAL n 
1 162  THR n 
1 163  GLY n 
1 164  GLY n 
1 165  TRP n 
1 166  VAL n 
1 167  MET n 
1 168  PRO n 
1 169  ASP n 
1 170  GLU n 
1 171  ALA n 
1 172  ASN n 
1 173  SER n 
1 174  HIS n 
1 175  TRP n 
1 176  ARG n 
1 177  ASN n 
1 178  VAL n 
1 179  LEU n 
1 180  LEU n 
1 181  GLN n 
1 182  LEU n 
1 183  THR n 
1 184  GLU n 
1 185  GLY n 
1 186  GLN n 
1 187  THR n 
1 188  TRP n 
1 189  LEU n 
1 190  LYS n 
1 191  GLN n 
1 192  PHE n 
1 193  MET n 
1 194  ASN n 
1 195  VAL n 
1 196  THR n 
1 197  PRO n 
1 198  THR n 
1 199  ALA n 
1 200  SER n 
1 201  TRP n 
1 202  ALA n 
1 203  ILE n 
1 204  ALA n 
1 205  PRO n 
1 206  PHE n 
1 207  GLY n 
1 208  HIS n 
1 209  SER n 
1 210  PRO n 
1 211  THR n 
1 212  MET n 
1 213  PRO n 
1 214  TYR n 
1 215  ILE n 
1 216  LEU n 
1 217  GLN n 
1 218  LYS n 
1 219  SER n 
1 220  GLY n 
1 221  PHE n 
1 222  LYS n 
1 223  ASN n 
1 224  MET n 
1 225  LEU n 
1 226  ILE n 
1 227  GLN n 
1 228  ARG n 
1 229  THR n 
1 230  HIS n 
1 231  TYR n 
1 232  SER n 
1 233  VAL n 
1 234  LYS n 
1 235  LYS n 
1 236  GLU n 
1 237  LEU n 
1 238  ALA n 
1 239  GLN n 
1 240  GLN n 
1 241  ARG n 
1 242  GLN n 
1 243  LEU n 
1 244  GLU n 
1 245  PHE n 
1 246  LEU n 
1 247  TRP n 
1 248  ARG n 
1 249  GLN n 
1 250  ILE n 
1 251  TRP n 
1 252  ASP n 
1 253  ASN n 
1 254  LYS n 
1 255  GLY n 
1 256  ASP n 
1 257  THR n 
1 258  ALA n 
1 259  LEU n 
1 260  PHE n 
1 261  THR n 
1 262  HIS n 
1 263  MET n 
1 264  MET n 
1 265  PRO n 
1 266  PHE n 
1 267  TYR n 
1 268  SER n 
1 269  TYR n 
1 270  ASP n 
1 271  ILE n 
1 272  PRO n 
1 273  HIS n 
1 274  THR n 
1 275  CYS n 
1 276  GLY n 
1 277  PRO n 
1 278  ASP n 
1 279  PRO n 
1 280  LYS n 
1 281  VAL n 
1 282  CYS n 
1 283  CYS n 
1 284  GLN n 
1 285  PHE n 
1 286  ASP n 
1 287  PHE n 
1 288  LYS n 
1 289  ARG n 
1 290  MET n 
1 291  GLY n 
1 292  SER n 
1 293  PHE n 
1 294  GLY n 
1 295  LEU n 
1 296  SER n 
1 297  CYS n 
1 298  PRO n 
1 299  TRP n 
1 300  LYS n 
1 301  VAL n 
1 302  PRO n 
1 303  PRO n 
1 304  ARG n 
1 305  THR n 
1 306  ILE n 
1 307  SER n 
1 308  ASP n 
1 309  GLN n 
1 310  ASN n 
1 311  VAL n 
1 312  ALA n 
1 313  ALA n 
1 314  ARG n 
1 315  SER n 
1 316  ASP n 
1 317  LEU n 
1 318  LEU n 
1 319  VAL n 
1 320  ASP n 
1 321  GLN n 
1 322  TRP n 
1 323  LYS n 
1 324  LYS n 
1 325  LYS n 
1 326  ALA n 
1 327  GLU n 
1 328  LEU n 
1 329  TYR n 
1 330  ARG n 
1 331  THR n 
1 332  ASN n 
1 333  VAL n 
1 334  LEU n 
1 335  LEU n 
1 336  ILE n 
1 337  PRO n 
1 338  LEU n 
1 339  GLY n 
1 340  ASP n 
1 341  ASP n 
1 342  PHE n 
1 343  ARG n 
1 344  PHE n 
1 345  LYS n 
1 346  GLN n 
1 347  ASN n 
1 348  THR n 
1 349  GLU n 
1 350  TRP n 
1 351  ASP n 
1 352  VAL n 
1 353  GLN n 
1 354  ARG n 
1 355  VAL n 
1 356  ASN n 
1 357  TYR n 
1 358  GLU n 
1 359  ARG n 
1 360  LEU n 
1 361  PHE n 
1 362  GLU n 
1 363  HIS n 
1 364  ILE n 
1 365  ASN n 
1 366  SER n 
1 367  GLN n 
1 368  ALA n 
1 369  HIS n 
1 370  PHE n 
1 371  ASN n 
1 372  VAL n 
1 373  GLN n 
1 374  ALA n 
1 375  GLN n 
1 376  PHE n 
1 377  GLY n 
1 378  THR n 
1 379  LEU n 
1 380  GLN n 
1 381  GLU n 
1 382  TYR n 
1 383  PHE n 
1 384  ASP n 
1 385  ALA n 
1 386  VAL n 
1 387  HIS n 
1 388  GLN n 
1 389  ALA n 
1 390  GLU n 
1 391  ARG n 
1 392  ALA n 
1 393  GLY n 
1 394  GLN n 
1 395  ALA n 
1 396  GLU n 
1 397  PHE n 
1 398  PRO n 
1 399  THR n 
1 400  LEU n 
1 401  SER n 
1 402  GLY n 
1 403  ASP n 
1 404  PHE n 
1 405  PHE n 
1 406  THR n 
1 407  TYR n 
1 408  ALA n 
1 409  ASP n 
1 410  ARG n 
1 411  SER n 
1 412  ASP n 
1 413  ASN n 
1 414  TYR n 
1 415  TRP n 
1 416  SER n 
1 417  GLY n 
1 418  TYR n 
1 419  TYR n 
1 420  THR n 
1 421  SER n 
1 422  ARG n 
1 423  PRO n 
1 424  TYR n 
1 425  HIS n 
1 426  LYS n 
1 427  ARG n 
1 428  MET n 
1 429  ASP n 
1 430  ARG n 
1 431  VAL n 
1 432  LEU n 
1 433  MET n 
1 434  HIS n 
1 435  TYR n 
1 436  VAL n 
1 437  ARG n 
1 438  ALA n 
1 439  ALA n 
1 440  GLU n 
1 441  MET n 
1 442  LEU n 
1 443  SER n 
1 444  ALA n 
1 445  TRP n 
1 446  HIS n 
1 447  SER n 
1 448  TRP n 
1 449  ASP n 
1 450  GLY n 
1 451  MET n 
1 452  ALA n 
1 453  ARG n 
1 454  ILE n 
1 455  GLU n 
1 456  GLU n 
1 457  ARG n 
1 458  LEU n 
1 459  GLU n 
1 460  GLN n 
1 461  ALA n 
1 462  ARG n 
1 463  ARG n 
1 464  GLU n 
1 465  LEU n 
1 466  SER n 
1 467  LEU n 
1 468  PHE n 
1 469  GLN n 
1 470  HIS n 
1 471  HIS n 
1 472  ASP n 
1 473  GLY n 
1 474  ILE n 
1 475  THR n 
1 476  GLY n 
1 477  THR n 
1 478  ALA n 
1 479  LYS n 
1 480  THR n 
1 481  HIS n 
1 482  VAL n 
1 483  VAL n 
1 484  VAL n 
1 485  ASP n 
1 486  TYR n 
1 487  GLU n 
1 488  GLN n 
1 489  ARG n 
1 490  MET n 
1 491  GLN n 
1 492  GLU n 
1 493  ALA n 
1 494  LEU n 
1 495  LYS n 
1 496  ALA n 
1 497  CYS n 
1 498  GLN n 
1 499  MET n 
1 500  VAL n 
1 501  MET n 
1 502  GLN n 
1 503  GLN n 
1 504  SER n 
1 505  VAL n 
1 506  TYR n 
1 507  ARG n 
1 508  LEU n 
1 509  LEU n 
1 510  THR n 
1 511  LYS n 
1 512  PRO n 
1 513  SER n 
1 514  ILE n 
1 515  TYR n 
1 516  SER n 
1 517  PRO n 
1 518  ASP n 
1 519  PHE n 
1 520  SER n 
1 521  PHE n 
1 522  SER n 
1 523  TYR n 
1 524  PHE n 
1 525  THR n 
1 526  LEU n 
1 527  ASP n 
1 528  ASP n 
1 529  SER n 
1 530  ARG n 
1 531  TRP n 
1 532  PRO n 
1 533  GLY n 
1 534  SER n 
1 535  GLY n 
1 536  VAL n 
1 537  GLU n 
1 538  ASP n 
1 539  SER n 
1 540  ARG n 
1 541  THR n 
1 542  THR n 
1 543  ILE n 
1 544  ILE n 
1 545  LEU n 
1 546  GLY n 
1 547  GLU n 
1 548  ASP n 
1 549  ILE n 
1 550  LEU n 
1 551  PRO n 
1 552  SER n 
1 553  LYS n 
1 554  HIS n 
1 555  VAL n 
1 556  VAL n 
1 557  MET n 
1 558  HIS n 
1 559  ASN n 
1 560  THR n 
1 561  LEU n 
1 562  PRO n 
1 563  HIS n 
1 564  TRP n 
1 565  ARG n 
1 566  GLU n 
1 567  GLN n 
1 568  LEU n 
1 569  VAL n 
1 570  ASP n 
1 571  PHE n 
1 572  TYR n 
1 573  VAL n 
1 574  SER n 
1 575  SER n 
1 576  PRO n 
1 577  PHE n 
1 578  VAL n 
1 579  SER n 
1 580  VAL n 
1 581  THR n 
1 582  ASP n 
1 583  LEU n 
1 584  ALA n 
1 585  ASN n 
1 586  ASN n 
1 587  PRO n 
1 588  VAL n 
1 589  GLU n 
1 590  ALA n 
1 591  GLN n 
1 592  VAL n 
1 593  SER n 
1 594  PRO n 
1 595  VAL n 
1 596  TRP n 
1 597  SER n 
1 598  TRP n 
1 599  HIS n 
1 600  HIS n 
1 601  ASP n 
1 602  THR n 
1 603  LEU n 
1 604  THR n 
1 605  LYS n 
1 606  THR n 
1 607  ILE n 
1 608  HIS n 
1 609  PRO n 
1 610  GLN n 
1 611  GLY n 
1 612  SER n 
1 613  THR n 
1 614  THR n 
1 615  LYS n 
1 616  TYR n 
1 617  ARG n 
1 618  ILE n 
1 619  ILE n 
1 620  PHE n 
1 621  LYS n 
1 622  ALA n 
1 623  ARG n 
1 624  VAL n 
1 625  PRO n 
1 626  PRO n 
1 627  MET n 
1 628  GLY n 
1 629  LEU n 
1 630  ALA n 
1 631  THR n 
1 632  TYR n 
1 633  VAL n 
1 634  LEU n 
1 635  THR n 
1 636  ILE n 
1 637  SER n 
1 638  ASP n 
1 639  SER n 
1 640  LYS n 
1 641  PRO n 
1 642  GLU n 
1 643  HIS n 
1 644  THR n 
1 645  SER n 
1 646  TYR n 
1 647  ALA n 
1 648  SER n 
1 649  ASN n 
1 650  LEU n 
1 651  LEU n 
1 652  LEU n 
1 653  ARG n 
1 654  LYS n 
1 655  ASN n 
1 656  PRO n 
1 657  THR n 
1 658  SER n 
1 659  LEU n 
1 660  PRO n 
1 661  LEU n 
1 662  GLY n 
1 663  GLN n 
1 664  TYR n 
1 665  PRO n 
1 666  GLU n 
1 667  ASP n 
1 668  VAL n 
1 669  LYS n 
1 670  PHE n 
1 671  GLY n 
1 672  ASP n 
1 673  PRO n 
1 674  ARG n 
1 675  GLU n 
1 676  ILE n 
1 677  SER n 
1 678  LEU n 
1 679  ARG n 
1 680  VAL n 
1 681  GLY n 
1 682  ASN n 
1 683  GLY n 
1 684  PRO n 
1 685  THR n 
1 686  LEU n 
1 687  ALA n 
1 688  PHE n 
1 689  SER n 
1 690  GLU n 
1 691  GLN n 
1 692  GLY n 
1 693  LEU n 
1 694  LEU n 
1 695  LYS n 
1 696  SER n 
1 697  ILE n 
1 698  GLN n 
1 699  LEU n 
1 700  THR n 
1 701  GLN n 
1 702  ASP n 
1 703  SER n 
1 704  PRO n 
1 705  HIS n 
1 706  VAL n 
1 707  PRO n 
1 708  VAL n 
1 709  HIS n 
1 710  PHE n 
1 711  LYS n 
1 712  PHE n 
1 713  LEU n 
1 714  LYS n 
1 715  TYR n 
1 716  GLY n 
1 717  VAL n 
1 718  ARG n 
1 719  SER n 
1 720  HIS n 
1 721  GLY n 
1 722  ASP n 
1 723  ARG n 
1 724  SER n 
1 725  GLY n 
1 726  ALA n 
1 727  TYR n 
1 728  LEU n 
1 729  PHE n 
1 730  LEU n 
1 731  PRO n 
1 732  ASN n 
1 733  GLY n 
1 734  PRO n 
1 735  ALA n 
1 736  SER n 
1 737  PRO n 
1 738  VAL n 
1 739  GLU n 
1 740  LEU n 
1 741  GLY n 
1 742  GLN n 
1 743  PRO n 
1 744  VAL n 
1 745  VAL n 
1 746  LEU n 
1 747  VAL n 
1 748  THR n 
1 749  LYS n 
1 750  GLY n 
1 751  LYS n 
1 752  LEU n 
1 753  GLU n 
1 754  SER n 
1 755  SER n 
1 756  VAL n 
1 757  SER n 
1 758  VAL n 
1 759  GLY n 
1 760  LEU n 
1 761  PRO n 
1 762  SER n 
1 763  VAL n 
1 764  VAL n 
1 765  HIS n 
1 766  GLN n 
1 767  THR n 
1 768  ILE n 
1 769  MET n 
1 770  ARG n 
1 771  GLY n 
1 772  GLY n 
1 773  ALA n 
1 774  PRO n 
1 775  GLU n 
1 776  ILE n 
1 777  ARG n 
1 778  ASN n 
1 779  LEU n 
1 780  VAL n 
1 781  ASP n 
1 782  ILE n 
1 783  GLY n 
1 784  SER n 
1 785  LEU n 
1 786  ASP n 
1 787  ASN n 
1 788  THR n 
1 789  GLU n 
1 790  ILE n 
1 791  VAL n 
1 792  MET n 
1 793  ARG n 
1 794  LEU n 
1 795  GLU n 
1 796  THR n 
1 797  HIS n 
1 798  ILE n 
1 799  ASP n 
1 800  SER n 
1 801  GLY n 
1 802  ASP n 
1 803  ILE n 
1 804  PHE n 
1 805  TYR n 
1 806  THR n 
1 807  ASP n 
1 808  LEU n 
1 809  ASN n 
1 810  GLY n 
1 811  LEU n 
1 812  GLN n 
1 813  PHE n 
1 814  ILE n 
1 815  LYS n 
1 816  ARG n 
1 817  ARG n 
1 818  ARG n 
1 819  LEU n 
1 820  ASP n 
1 821  LYS n 
1 822  LEU n 
1 823  PRO n 
1 824  LEU n 
1 825  GLN n 
1 826  ALA n 
1 827  ASN n 
1 828  TYR n 
1 829  TYR n 
1 830  PRO n 
1 831  ILE n 
1 832  PRO n 
1 833  SER n 
1 834  GLY n 
1 835  MET n 
1 836  PHE n 
1 837  ILE n 
1 838  GLU n 
1 839  ASP n 
1 840  ALA n 
1 841  ASN n 
1 842  THR n 
1 843  ARG n 
1 844  LEU n 
1 845  THR n 
1 846  LEU n 
1 847  LEU n 
1 848  THR n 
1 849  GLY n 
1 850  GLN n 
1 851  PRO n 
1 852  LEU n 
1 853  GLY n 
1 854  GLY n 
1 855  SER n 
1 856  SER n 
1 857  LEU n 
1 858  ALA n 
1 859  SER n 
1 860  GLY n 
1 861  GLU n 
1 862  LEU n 
1 863  GLU n 
1 864  ILE n 
1 865  MET n 
1 866  GLN n 
1 867  ASP n 
1 868  ARG n 
1 869  ARG n 
1 870  LEU n 
1 871  ALA n 
1 872  SER n 
1 873  ASP n 
1 874  ASP n 
1 875  GLU n 
1 876  ARG n 
1 877  GLY n 
1 878  LEU n 
1 879  GLY n 
1 880  GLN n 
1 881  GLY n 
1 882  VAL n 
1 883  LEU n 
1 884  ASP n 
1 885  ASN n 
1 886  LYS n 
1 887  PRO n 
1 888  VAL n 
1 889  LEU n 
1 890  HIS n 
1 891  ILE n 
1 892  TYR n 
1 893  ARG n 
1 894  LEU n 
1 895  VAL n 
1 896  LEU n 
1 897  GLU n 
1 898  LYS n 
1 899  VAL n 
1 900  ASN n 
1 901  ASN n 
1 902  CYS n 
1 903  VAL n 
1 904  ARG n 
1 905  PRO n 
1 906  SER n 
1 907  LYS n 
1 908  LEU n 
1 909  HIS n 
1 910  PRO n 
1 911  ALA n 
1 912  GLY n 
1 913  TYR n 
1 914  LEU n 
1 915  THR n 
1 916  SER n 
1 917  ALA n 
1 918  ALA n 
1 919  HIS n 
1 920  LYS n 
1 921  ALA n 
1 922  SER n 
1 923  GLN n 
1 924  SER n 
1 925  LEU n 
1 926  LEU n 
1 927  ASP n 
1 928  PRO n 
1 929  LEU n 
1 930  ASP n 
1 931  LYS n 
1 932  PHE n 
1 933  ILE n 
1 934  PHE n 
1 935  ALA n 
1 936  GLU n 
1 937  ASN n 
1 938  GLU n 
1 939  TRP n 
1 940  ILE n 
1 941  GLY n 
1 942  ALA n 
1 943  GLN n 
1 944  GLY n 
1 945  GLN n 
1 946  PHE n 
1 947  GLY n 
1 948  GLY n 
1 949  ASP n 
1 950  HIS n 
1 951  PRO n 
1 952  SER n 
1 953  ALA n 
1 954  ARG n 
1 955  GLU n 
1 956  ASP n 
1 957  LEU n 
1 958  ASP n 
1 959  VAL n 
1 960  SER n 
1 961  VAL n 
1 962  MET n 
1 963  ARG n 
1 964  ARG n 
1 965  LEU n 
1 966  THR n 
1 967  LYS n 
1 968  SER n 
1 969  SER n 
1 970  ALA n 
1 971  LYS n 
1 972  THR n 
1 973  GLN n 
1 974  ARG n 
1 975  VAL n 
1 976  GLY n 
1 977  TYR n 
1 978  VAL n 
1 979  LEU n 
1 980  HIS n 
1 981  ARG n 
1 982  THR n 
1 983  ASN n 
1 984  LEU n 
1 985  MET n 
1 986  GLN n 
1 987  CYS n 
1 988  GLY n 
1 989  THR n 
1 990  PRO n 
1 991  GLU n 
1 992  GLU n 
1 993  HIS n 
1 994  THR n 
1 995  GLN n 
1 996  LYS n 
1 997  LEU n 
1 998  ASP n 
1 999  VAL n 
1 1000 CYS n 
1 1001 HIS n 
1 1002 LEU n 
1 1003 LEU n 
1 1004 PRO n 
1 1005 ASN n 
1 1006 VAL n 
1 1007 ALA n 
1 1008 ARG n 
1 1009 CYS n 
1 1010 GLU n 
1 1011 ARG n 
1 1012 THR n 
1 1013 THR n 
1 1014 LEU n 
1 1015 THR n 
1 1016 PHE n 
1 1017 LEU n 
1 1018 GLN n 
1 1019 ASN n 
1 1020 LEU n 
1 1021 GLU n 
1 1022 HIS n 
1 1023 LEU n 
1 1024 ASP n 
1 1025 GLY n 
1 1026 MET n 
1 1027 VAL n 
1 1028 ALA n 
1 1029 PRO n 
1 1030 GLU n 
1 1031 VAL n 
1 1032 CYS n 
1 1033 PRO n 
1 1034 MET n 
1 1035 GLU n 
1 1036 THR n 
1 1037 ALA n 
1 1038 ALA n 
1 1039 TYR n 
1 1040 VAL n 
1 1041 SER n 
1 1042 SER n 
1 1043 HIS n 
1 1044 SER n 
1 1045 SER n 
# 
_entity_src_gen.entity_id                          1 
_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               'Fruit fly' 
_entity_src_gen.gene_src_genus                     ? 
_entity_src_gen.pdbx_gene_src_gene                 'alpha-Man-II, GmII' 
_entity_src_gen.gene_src_species                   ? 
_entity_src_gen.gene_src_strain                    ? 
_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      'Drosophila melanogaster' 
_entity_src_gen.pdbx_gene_src_ncbi_taxonomy_id     ? 
_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      'Drosophila melanogaster' 
_entity_src_gen.pdbx_host_org_ncbi_taxonomy_id     ? 
_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               'S2 cells' 
_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          'Stable transfection 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                       pMTBIP_NHIS 
_entity_src_gen.plasmid_details                    ? 
_entity_src_gen.pdbx_description                   ? 
# 
_struct_ref.id                         1 
_struct_ref.db_name                    UNP 
_struct_ref.db_code                    MAN2_DROME 
_struct_ref.pdbx_db_accession          Q24451 
_struct_ref.entity_id                  1 
_struct_ref.pdbx_seq_one_letter_code   
;DDPIRPPLKVARSPRPGQCQDVVQDVPNVDVQMLELYDRMSFKDIDGGVWKQGWNIKYDPLKYNAHHKLKVFVVPHSHND
PGWIQTFEEYYQHDTKHILSNALRHLHDNPEMKFIWAEISYFARFYHDLGENKKLQMKSIVKNGQLEFVTGGWVMPDEAN
SHWRNVLLQLTEGQTWLKQFMNVTPTASWAIDPFGHSPTMPYILQKSGFKNMLIQRTHYSVKKELAQQRQLEFLWRQIWD
NKGDTALFTHMMPFYSYDIPHTCGPDPKVCCQFDFKRMGSFGLSCPWKVPPRTISDQNVAARSDLLVDQWKKKAELYRTN
VLLIPLGDDFRFKQNTEWDVQRVNYERLFEHINSQAHFNVQAQFGTLQEYFDAVHQAERAGQAEFPTLSGDFFTYADRSD
NYWSGYYTSRPYHKRMDRVLMHYVRAAEMLSAWHSWDGMARIEERLEQARRELSLFQHHDGITGTAKTHVVVDYEQRMQE
ALKACQMVMQQSVYRLLTKPSIYSPDFSFSYFTLDDSRWPGSGVEDSRTTIILGEDILPSKHVVMHNTLPHWREQLVDFY
VSSPFVSVTDLANNPVEAQVSPVWSWHHDTLTKTIHPQGSTTKYRIIFKARVPPMGLATYVLTISDSKPEHTSYASNLLL
RKNPTSLPLGQYPEDVKFGDPREISLRVGNGPTLAFSEQGLLKSIQLTQDSPHVPVHFKFLKYGVRSHGDRSGAYLFLPN
GPASPVELGQPVVLVTKGKLESSVSVGLPSVVHQTIMRGGAPEIRNLVDIGSLDNTEIVMRLETHIDSGDIFYTDLNGLQ
FIKRRRLDKLPLQANYYPIPSGMFIEDANTRLTLLTGQPLGGSSLASGELEIMQDRRLASDDERGLGQGVLDNKPVLHIY
RLVLEKVNNCVRPSELHPAGYLTSAAHKASQSLLDPLDKFIFAENEWIGAQGQFGGDHPSAREDLDVSVMRRLTKSSAKT
QRVGYVLHRTNLMQCGTPEEHTQKLDVCHLLPNVARCERTTLTFLQNLEHLDGMVAPEVCPMETAAYVSSHSS
;
_struct_ref.pdbx_align_begin           76 
_struct_ref.pdbx_db_isoform            ? 
# 
_struct_ref_seq.align_id                      1 
_struct_ref_seq.ref_id                        1 
_struct_ref_seq.pdbx_PDB_id_code              3BVT 
_struct_ref_seq.pdbx_strand_id                A 
_struct_ref_seq.seq_align_beg                 13 
_struct_ref_seq.pdbx_seq_align_beg_ins_code   ? 
_struct_ref_seq.seq_align_end                 1045 
_struct_ref_seq.pdbx_seq_align_end_ins_code   ? 
_struct_ref_seq.pdbx_db_accession             Q24451 
_struct_ref_seq.db_align_beg                  76 
_struct_ref_seq.pdbx_db_align_beg_ins_code    ? 
_struct_ref_seq.db_align_end                  1108 
_struct_ref_seq.pdbx_db_align_end_ins_code    ? 
_struct_ref_seq.pdbx_auth_seq_align_beg       13 
_struct_ref_seq.pdbx_auth_seq_align_end       1045 
# 
loop_
_struct_ref_seq_dif.align_id 
_struct_ref_seq_dif.pdbx_pdb_id_code 
_struct_ref_seq_dif.mon_id 
_struct_ref_seq_dif.pdbx_pdb_strand_id 
_struct_ref_seq_dif.seq_num 
_struct_ref_seq_dif.pdbx_pdb_ins_code 
_struct_ref_seq_dif.pdbx_seq_db_name 
_struct_ref_seq_dif.pdbx_seq_db_accession_code 
_struct_ref_seq_dif.db_mon_id 
_struct_ref_seq_dif.pdbx_seq_db_seq_num 
_struct_ref_seq_dif.details 
_struct_ref_seq_dif.pdbx_auth_seq_num 
_struct_ref_seq_dif.pdbx_ordinal 
1 3BVT ARG A 1   ? UNP Q24451 ?   ?   'EXPRESSION TAG' 1   1  
1 3BVT SER A 2   ? UNP Q24451 ?   ?   'EXPRESSION TAG' 2   2  
1 3BVT SER A 3   ? UNP Q24451 ?   ?   'EXPRESSION TAG' 3   3  
1 3BVT HIS A 4   ? UNP Q24451 ?   ?   'EXPRESSION TAG' 4   4  
1 3BVT HIS A 5   ? UNP Q24451 ?   ?   'EXPRESSION TAG' 5   5  
1 3BVT HIS A 6   ? UNP Q24451 ?   ?   'EXPRESSION TAG' 6   6  
1 3BVT HIS A 7   ? UNP Q24451 ?   ?   'EXPRESSION TAG' 7   7  
1 3BVT HIS A 8   ? UNP Q24451 ?   ?   'EXPRESSION TAG' 8   8  
1 3BVT HIS A 9   ? UNP Q24451 ?   ?   'EXPRESSION TAG' 9   9  
1 3BVT GLY A 10  ? UNP Q24451 ?   ?   'EXPRESSION TAG' 10  10 
1 3BVT GLU A 11  ? UNP Q24451 ?   ?   'EXPRESSION TAG' 11  11 
1 3BVT PHE A 12  ? UNP Q24451 ?   ?   'EXPRESSION TAG' 12  12 
1 3BVT ALA A 204 ? UNP Q24451 ASP 267 ENGINEERED       204 13 
1 3BVT LYS A 907 ? UNP Q24451 GLU 970 'SEE REMARK 999' 907 14 
# 
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 
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 
HOH non-polymer         . WATER                                                              ? 'H2 O'           18.015  
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 
MPD non-polymer         . '(4S)-2-METHYL-2,4-PENTANEDIOL'                                    ? 'C6 H14 O2'      118.174 
MRD non-polymer         . '(4R)-2-METHYLPENTANE-2,4-DIOL'                                    ? 'C6 H14 O2'      118.174 
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 
PO4 non-polymer         . 'PHOSPHATE ION'                                                    ? 'O4 P -3'        94.971  
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 
WZ1 non-polymer         . 'methyl 3-S-alpha-D-mannopyranosyl-3-thio-alpha-D-mannopyranoside' 
'Methyl(alpha-D-mannopyranosyl)-(1->3)-S-alpha-D-mannopyranoside' 'C13 H24 O10 S'  372.389 
ZN  non-polymer         . 'ZINC ION'                                                         ? 'Zn 2'           65.409  
# 
_exptl.crystals_number   1 
_exptl.entry_id          3BVT 
_exptl.method            'X-RAY DIFFRACTION' 
# 
_exptl_crystal.id                    1 
_exptl_crystal.density_Matthews      2.20 
_exptl_crystal.density_meas          ? 
_exptl_crystal.density_percent_sol   44.00 
_exptl_crystal.description           ? 
_exptl_crystal.F_000                 ? 
_exptl_crystal.preparation           ? 
# 
_exptl_crystal_grow.crystal_id      1 
_exptl_crystal_grow.method          'VAPOR DIFFUSION, HANGING DROP' 
_exptl_crystal_grow.pH              7.0 
_exptl_crystal_grow.temp            293 
_exptl_crystal_grow.temp_details    ? 
_exptl_crystal_grow.pdbx_details    
;TRIS, NACL, PEG6000, MPD. Crystals washed in 
phosphate buffered reservoir solution before 
soaking with substrate for 24 hrs, pH 7.0, VAPOR DIFFUSION, HANGING DROP, temperature 293K
;
_exptl_crystal_grow.pdbx_pH_range   . 
# 
_diffrn.id                     1 
_diffrn.ambient_temp           100 
_diffrn.ambient_temp_details   ? 
_diffrn.crystal_id             1 
# 
_diffrn_detector.diffrn_id              1 
_diffrn_detector.detector               CCD 
_diffrn_detector.type                   'ADSC QUANTUM 4' 
_diffrn_detector.pdbx_collection_date   2006-06-01 
_diffrn_detector.details                ? 
# 
_diffrn_radiation.diffrn_id                        1 
_diffrn_radiation.pdbx_diffrn_protocol             'SINGLE WAVELENGTH' 
_diffrn_radiation.monochromator                    ? 
_diffrn_radiation.wavelength_id                    1 
_diffrn_radiation.pdbx_monochromatic_or_laue_m_l   M 
_diffrn_radiation.pdbx_scattering_type             x-ray 
# 
_diffrn_radiation_wavelength.id           1 
_diffrn_radiation_wavelength.wavelength   0.977 
_diffrn_radiation_wavelength.wt           1.0 
# 
_diffrn_source.diffrn_id                   1 
_diffrn_source.source                      SYNCHROTRON 
_diffrn_source.type                        'CHESS BEAMLINE A1' 
_diffrn_source.pdbx_synchrotron_site       CHESS 
_diffrn_source.pdbx_synchrotron_beamline   A1 
_diffrn_source.pdbx_wavelength             ? 
_diffrn_source.pdbx_wavelength_list        0.977 
# 
_reflns.entry_id                     3BVT 
_reflns.d_resolution_high            1.300 
_reflns.d_resolution_low             20.000 
_reflns.number_obs                   256264 
_reflns.pdbx_Rmerge_I_obs            0.068 
_reflns.pdbx_netI_over_sigmaI        12.900 
_reflns.pdbx_chi_squared             1.058 
_reflns.percent_possible_obs         99.800 
_reflns.observed_criterion_sigma_F   0 
_reflns.observed_criterion_sigma_I   0 
_reflns.number_all                   256778 
_reflns.pdbx_Rsym_value              ? 
_reflns.B_iso_Wilson_estimate        ? 
_reflns.pdbx_redundancy              6.7 
_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_scaling_rejects         ? 
_reflns.pdbx_ordinal                 1 
_reflns.pdbx_diffrn_id               1 
# 
_reflns_shell.d_res_high             1.30 
_reflns_shell.d_res_low              1.33 
_reflns_shell.number_measured_obs    ? 
_reflns_shell.number_measured_all    ? 
_reflns_shell.number_unique_obs      ? 
_reflns_shell.Rmerge_I_obs           0.887 
_reflns_shell.meanI_over_sigI_obs    2.6 
_reflns_shell.pdbx_Rsym_value        ? 
_reflns_shell.pdbx_chi_squared       1.216 
_reflns_shell.pdbx_redundancy        5.5 
_reflns_shell.percent_possible_obs   ? 
_reflns_shell.number_unique_all      16843 
_reflns_shell.percent_possible_all   99.60 
_reflns_shell.pdbx_ordinal           1 
_reflns_shell.pdbx_diffrn_id         1 
# 
_refine.entry_id                                 3BVT 
_refine.ls_d_res_high                            1.300 
_refine.ls_d_res_low                             19.840 
_refine.pdbx_ls_sigma_F                          0.00 
_refine.ls_percent_reflns_obs                    99.650 
_refine.ls_number_reflns_obs                     256139 
_refine.pdbx_ls_cross_valid_method               THROUGHOUT 
_refine.pdbx_R_Free_selection_details            RANDOM 
_refine.details                                  'HYDROGENS HAVE BEEN ADDED IN THE RIDING POSITIONS' 
_refine.ls_R_factor_obs                          0.174 
_refine.ls_R_factor_R_work                       0.174 
_refine.ls_R_factor_R_free                       0.192 
_refine.ls_percent_reflns_R_free                 1.500 
_refine.ls_number_reflns_R_free                  3801 
_refine.B_iso_mean                               16.953 
_refine.aniso_B[1][1]                            0.000 
_refine.aniso_B[2][2]                            0.000 
_refine.aniso_B[3][3]                            0.000 
_refine.aniso_B[1][2]                            0.000 
_refine.aniso_B[1][3]                            0.000 
_refine.aniso_B[2][3]                            0.000 
_refine.correlation_coeff_Fo_to_Fc               0.970 
_refine.correlation_coeff_Fo_to_Fc_free          0.966 
_refine.pdbx_overall_ESU_R                       0.049 
_refine.pdbx_overall_ESU_R_Free                  0.050 
_refine.overall_SU_ML                            0.035 
_refine.overall_SU_B                             0.807 
_refine.solvent_model_details                    MASK 
_refine.pdbx_solvent_vdw_probe_radii             1.200 
_refine.pdbx_solvent_ion_probe_radii             0.800 
_refine.pdbx_solvent_shrinkage_radii             0.800 
_refine.pdbx_method_to_determine_struct          'MOLECULAR REPLACEMENT' 
_refine.pdbx_stereochemistry_target_values       'Engh & Huber' 
_refine.pdbx_ls_sigma_I                          ? 
_refine.ls_number_reflns_all                     257039 
_refine.ls_R_factor_all                          ? 
_refine.ls_redundancy_reflns_obs                 ? 
_refine.pdbx_data_cutoff_high_absF               ? 
_refine.pdbx_data_cutoff_low_absF                ? 
_refine.ls_number_parameters                     ? 
_refine.ls_number_restraints                     ? 
_refine.ls_R_factor_R_free_error                 ? 
_refine.ls_R_factor_R_free_error_details         ? 
_refine.pdbx_starting_model                      'PDB entry 1HTY' 
_refine.pdbx_stereochem_target_val_spec_case     ? 
_refine.solvent_model_param_bsol                 ? 
_refine.solvent_model_param_ksol                 ? 
_refine.occupancy_max                            ? 
_refine.occupancy_min                            ? 
_refine.pdbx_isotropic_thermal_model             ? 
_refine.B_iso_min                                ? 
_refine.B_iso_max                                ? 
_refine.overall_SU_R_Cruickshank_DPI             ? 
_refine.overall_SU_R_free                        ? 
_refine.pdbx_data_cutoff_high_rms_absF           ? 
_refine.ls_wR_factor_R_free                      ? 
_refine.ls_wR_factor_R_work                      ? 
_refine.overall_FOM_free_R_set                   ? 
_refine.overall_FOM_work_R_set                   ? 
_refine.pdbx_overall_phase_error                 ? 
_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_analyze.entry_id                        3BVT 
_refine_analyze.Luzzati_coordinate_error_obs    0.141 
_refine_analyze.Luzzati_sigma_a_obs             ? 
_refine_analyze.Luzzati_d_res_low_obs           ? 
_refine_analyze.Luzzati_coordinate_error_free   ? 
_refine_analyze.Luzzati_sigma_a_free            ? 
_refine_analyze.Luzzati_d_res_low_free          ? 
_refine_analyze.number_disordered_residues      ? 
_refine_analyze.occupancy_sum_non_hydrogen      ? 
_refine_analyze.occupancy_sum_hydrogen          ? 
_refine_analyze.pdbx_Luzzati_d_res_high_obs     ? 
_refine_analyze.pdbx_refine_id                  'X-RAY DIFFRACTION' 
# 
_refine_hist.pdbx_refine_id                   'X-RAY DIFFRACTION' 
_refine_hist.cycle_id                         LAST 
_refine_hist.pdbx_number_atoms_protein        8194 
_refine_hist.pdbx_number_atoms_nucleic_acid   0 
_refine_hist.pdbx_number_atoms_ligand         68 
_refine_hist.number_atoms_solvent             1453 
_refine_hist.number_atoms_total               9715 
_refine_hist.d_res_high                       1.300 
_refine_hist.d_res_low                        19.840 
# 
loop_
_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_refine_id 
_refine_ls_restr.pdbx_restraint_function 
r_bond_refined_d         8777  0.014  0.021  ? 'X-RAY DIFFRACTION' ? 
r_angle_refined_deg      11979 1.520  1.943  ? 'X-RAY DIFFRACTION' ? 
r_dihedral_angle_1_deg   1089  6.087  5.000  ? 'X-RAY DIFFRACTION' ? 
r_dihedral_angle_2_deg   432   37.004 23.681 ? 'X-RAY DIFFRACTION' ? 
r_dihedral_angle_3_deg   1488  12.160 15.000 ? 'X-RAY DIFFRACTION' ? 
r_dihedral_angle_4_deg   60    18.705 15.000 ? 'X-RAY DIFFRACTION' ? 
r_chiral_restr           1277  0.101  0.200  ? 'X-RAY DIFFRACTION' ? 
r_gen_planes_refined     6816  0.008  0.020  ? 'X-RAY DIFFRACTION' ? 
r_nbd_refined            4324  0.203  0.200  ? 'X-RAY DIFFRACTION' ? 
r_nbtor_refined          6031  0.311  0.200  ? 'X-RAY DIFFRACTION' ? 
r_xyhbond_nbd_refined    1242  0.142  0.200  ? 'X-RAY DIFFRACTION' ? 
r_metal_ion_refined      1     0.019  0.200  ? 'X-RAY DIFFRACTION' ? 
r_symmetry_vdw_refined   82    0.212  0.200  ? 'X-RAY DIFFRACTION' ? 
r_symmetry_hbond_refined 69    0.116  0.200  ? 'X-RAY DIFFRACTION' ? 
r_mcbond_it              5361  1.031  1.500  ? 'X-RAY DIFFRACTION' ? 
r_mcangle_it             8534  1.636  2.000  ? 'X-RAY DIFFRACTION' ? 
r_scbond_it              3868  2.320  3.000  ? 'X-RAY DIFFRACTION' ? 
r_scangle_it             3421  3.539  4.500  ? 'X-RAY DIFFRACTION' ? 
# 
_refine_ls_shell.d_res_high                       1.30 
_refine_ls_shell.d_res_low                        1.335 
_refine_ls_shell.pdbx_total_number_of_bins_used   20 
_refine_ls_shell.percent_reflns_obs               97.360 
_refine_ls_shell.number_reflns_R_work             17986 
_refine_ls_shell.R_factor_all                     ? 
_refine_ls_shell.R_factor_R_work                  0.256 
_refine_ls_shell.R_factor_R_free                  0.283 
_refine_ls_shell.percent_reflns_R_free            ? 
_refine_ls_shell.number_reflns_R_free             274 
_refine_ls_shell.R_factor_R_free_error            ? 
_refine_ls_shell.number_reflns_all                18260 
_refine_ls_shell.number_reflns_obs                ? 
_refine_ls_shell.redundancy_reflns_obs            ? 
_refine_ls_shell.pdbx_refine_id                   'X-RAY DIFFRACTION' 
# 
_struct.entry_id                  3BVT 
_struct.title                     
;GOLGI MANNOSIDASE II D204A catalytic nucleophile mutant complex with Methyl (alpha-D-mannopyranosyl)-(1->3)-S-alpha-D-mannopyranoside
;
_struct.pdbx_descriptor           'Alpha-mannosidase 2 (E.C.3.2.1.114)' 
_struct.pdbx_model_details        ? 
_struct.pdbx_CASP_flag            ? 
_struct.pdbx_model_type_details   ? 
# 
_struct_keywords.entry_id        3BVT 
_struct_keywords.pdbx_keywords   HYDROLASE 
_struct_keywords.text            
'FAMILY 38 GLYCOYSL HYDROLASE, Glycosidase, Golgi apparatus, Membrane, Signal-anchor, Transmembrane, HYDROLASE' 
# 
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 3 ? 
D N N 4 ? 
E N N 5 ? 
F N N 6 ? 
G N N 7 ? 
H N N 7 ? 
I N N 8 ? 
# 
_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  MET A 45   ? MET A 52   ? MET A 45   MET A 52   1 ? 8  
HELX_P HELX_P2  2  ASP A 71   ? TYR A 75   ? ASP A 71   TYR A 75   5 ? 5  
HELX_P HELX_P3  3  THR A 98   ? ASP A 106  ? THR A 98   ASP A 106  1 ? 9  
HELX_P HELX_P4  4  ASP A 106  ? ASN A 121  ? ASP A 106  ASN A 121  1 ? 16 
HELX_P HELX_P5  5  GLU A 130  ? HIS A 139  ? GLU A 130  HIS A 139  1 ? 10 
HELX_P HELX_P6  6  GLY A 142  ? ASN A 155  ? GLY A 142  ASN A 155  1 ? 14 
HELX_P HELX_P7  7  HIS A 174  ? ASN A 194  ? HIS A 174  ASN A 194  1 ? 21 
HELX_P HELX_P8  8  PRO A 210  ? LYS A 218  ? PRO A 210  LYS A 218  1 ? 9  
HELX_P HELX_P9  9  HIS A 230  ? GLN A 240  ? HIS A 230  GLN A 240  1 ? 11 
HELX_P HELX_P10 10 ASP A 270  ? THR A 274  ? ASP A 270  THR A 274  5 ? 5  
HELX_P HELX_P11 11 ASP A 278  ? CYS A 283  ? ASP A 278  CYS A 283  1 ? 6  
HELX_P HELX_P12 12 GLN A 284  ? MET A 290  ? GLN A 284  MET A 290  5 ? 7  
HELX_P HELX_P13 13 ASN A 310  ? GLU A 327  ? ASN A 310  GLU A 327  1 ? 18 
HELX_P HELX_P14 14 GLN A 346  ? GLN A 367  ? GLN A 346  GLN A 367  1 ? 22 
HELX_P HELX_P15 15 ALA A 368  ? PHE A 370  ? ALA A 368  PHE A 370  5 ? 3  
HELX_P HELX_P16 16 THR A 378  ? ALA A 392  ? THR A 378  ALA A 392  1 ? 15 
HELX_P HELX_P17 17 SER A 416  ? THR A 420  ? SER A 416  THR A 420  5 ? 5  
HELX_P HELX_P18 18 ARG A 422  ? TRP A 445  ? ARG A 422  TRP A 445  1 ? 24 
HELX_P HELX_P19 19 ASP A 449  ? ALA A 452  ? ASP A 449  ALA A 452  5 ? 4  
HELX_P HELX_P20 20 ARG A 453  ? GLN A 469  ? ARG A 453  GLN A 469  1 ? 17 
HELX_P HELX_P21 21 LYS A 479  ? LEU A 509  ? LYS A 479  LEU A 509  1 ? 31 
HELX_P HELX_P22 22 PRO A 823  ? TYR A 828  ? PRO A 823  TYR A 828  5 ? 6  
HELX_P HELX_P23 23 THR A 915  ? ASP A 927  ? THR A 915  ASP A 927  1 ? 13 
HELX_P HELX_P24 24 ASP A 998  ? LEU A 1002 ? ASP A 998  LEU A 1002 5 ? 5  
HELX_P HELX_P25 25 ASP A 1024 ? VAL A 1027 ? ASP A 1024 VAL A 1027 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 31   SG  ? ? ? 1_555 A CYS 1032 SG  ? ? A CYS 31   A CYS 1032 1_555 ? ? ? ? ? ? ? 2.053 ? 
disulf2 disulf ? ? A CYS 275  SG  ? ? ? 1_555 A CYS 282  SG  ? ? A CYS 275  A CYS 282  1_555 ? ? ? ? ? ? ? 2.027 ? 
disulf3 disulf ? ? A CYS 283  SG  ? ? ? 1_555 A CYS 297  SG  ? ? A CYS 283  A CYS 297  1_555 ? ? ? ? ? ? ? 2.096 ? 
disulf4 disulf ? ? A CYS 902  SG  ? ? ? 1_555 A CYS 987  SG  ? ? A CYS 902  A CYS 987  1_555 ? ? ? ? ? ? ? 2.051 ? 
disulf5 disulf ? ? A CYS 1000 SG  ? ? ? 1_555 A CYS 1009 SG  ? ? A CYS 1000 A CYS 1009 1_555 ? ? ? ? ? ? ? 1.999 ? 
metalc1 metalc ? ? A HIS 90   NE2 ? ? ? 1_555 D ZN  .    ZN  ? ? A HIS 90   A ZN  1048 1_555 ? ? ? ? ? ? ? 2.075 ? 
metalc2 metalc ? ? A ASP 92   OD1 ? ? ? 1_555 D ZN  .    ZN  ? ? A ASP 92   A ZN  1048 1_555 ? ? ? ? ? ? ? 2.000 ? 
covale1 covale ? ? A ASN 194  ND2 ? ? ? 1_555 B NAG .    C1  ? ? A ASN 194  A NAG 1046 1_555 ? ? ? ? ? ? ? 1.485 ? 
metalc3 metalc ? ? A HIS 471  NE2 ? ? ? 1_555 D ZN  .    ZN  ? ? A HIS 471  A ZN  1048 1_555 ? ? ? ? ? ? ? 2.065 ? 
metalc4 metalc ? ? D ZN  .    ZN  ? ? ? 1_555 F WZ1 .    O32 ? ? A ZN  1048 A WZ1 1050 1_555 ? ? ? ? ? ? ? 2.129 ? 
metalc5 metalc ? ? D ZN  .    ZN  ? ? ? 1_555 F WZ1 .    O22 ? ? A ZN  1048 A WZ1 1050 1_555 ? ? ? ? ? ? ? 2.229 ? 
# 
loop_
_struct_conn_type.id 
_struct_conn_type.criteria 
_struct_conn_type.reference 
disulf ? ? 
metalc ? ? 
covale ? ? 
# 
loop_
_struct_mon_prot_cis.pdbx_id 
_struct_mon_prot_cis.label_comp_id 
_struct_mon_prot_cis.label_seq_id 
_struct_mon_prot_cis.label_asym_id 
_struct_mon_prot_cis.label_alt_id 
_struct_mon_prot_cis.pdbx_PDB_ins_code 
_struct_mon_prot_cis.auth_comp_id 
_struct_mon_prot_cis.auth_seq_id 
_struct_mon_prot_cis.auth_asym_id 
_struct_mon_prot_cis.pdbx_label_comp_id_2 
_struct_mon_prot_cis.pdbx_label_seq_id_2 
_struct_mon_prot_cis.pdbx_label_asym_id_2 
_struct_mon_prot_cis.pdbx_PDB_ins_code_2 
_struct_mon_prot_cis.pdbx_auth_comp_id_2 
_struct_mon_prot_cis.pdbx_auth_seq_id_2 
_struct_mon_prot_cis.pdbx_auth_asym_id_2 
_struct_mon_prot_cis.pdbx_PDB_model_num 
_struct_mon_prot_cis.pdbx_omega_angle 
1 PHE 405 A . ? PHE 405 A THR 406 A ? THR 406 A 1 -4.77 
2 TRP 531 A . ? TRP 531 A PRO 532 A ? PRO 532 A 1 -6.29 
# 
loop_
_struct_sheet.id 
_struct_sheet.type 
_struct_sheet.number_strands 
_struct_sheet.details 
A ? 6  ? 
B ? 3  ? 
C ? 2  ? 
D ? 6  ? 
E ? 5  ? 
F ? 5  ? 
G ? 12 ? 
H ? 5  ? 
I ? 8  ? 
J ? 5  ? 
# 
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  ? parallel      
A 2  3  ? parallel      
A 3  4  ? anti-parallel 
A 4  5  ? parallel      
A 5  6  ? parallel      
B 1  2  ? parallel      
B 2  3  ? parallel      
C 1  2  ? parallel      
D 1  2  ? anti-parallel 
D 2  3  ? anti-parallel 
D 3  4  ? anti-parallel 
D 4  5  ? anti-parallel 
D 5  6  ? anti-parallel 
E 1  2  ? anti-parallel 
E 2  3  ? anti-parallel 
E 3  4  ? anti-parallel 
E 4  5  ? anti-parallel 
F 1  2  ? parallel      
F 2  3  ? anti-parallel 
F 3  4  ? anti-parallel 
F 4  5  ? parallel      
G 1  2  ? parallel      
G 2  3  ? anti-parallel 
G 3  4  ? anti-parallel 
G 4  5  ? anti-parallel 
G 5  6  ? anti-parallel 
G 6  7  ? anti-parallel 
G 7  8  ? anti-parallel 
G 8  9  ? anti-parallel 
G 9  10 ? anti-parallel 
G 10 11 ? anti-parallel 
G 11 12 ? anti-parallel 
H 1  2  ? anti-parallel 
H 2  3  ? anti-parallel 
H 3  4  ? anti-parallel 
H 4  5  ? anti-parallel 
I 1  2  ? anti-parallel 
I 2  3  ? anti-parallel 
I 3  4  ? anti-parallel 
I 4  5  ? anti-parallel 
I 5  6  ? anti-parallel 
I 6  7  ? anti-parallel 
I 7  8  ? anti-parallel 
J 1  2  ? anti-parallel 
J 2  3  ? anti-parallel 
J 3  4  ? anti-parallel 
J 4  5  ? 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  VAL A 43   ? GLN A 44   ? VAL A 43   GLN A 44   
A 2  THR A 399  ? SER A 401  ? THR A 399  SER A 401  
A 3  GLU A 244  ? TRP A 247  ? GLU A 244  TRP A 247  
A 4  LEU A 259  ? MET A 263  ? LEU A 259  MET A 263  
A 5  ASN A 223  ? ILE A 226  ? ASN A 223  ILE A 226  
A 6  ALA A 199  ? ALA A 202  ? ALA A 199  ALA A 202  
B 1  VAL A 333  ? ASP A 341  ? VAL A 333  ASP A 341  
B 2  LEU A 81   ? HIS A 90   ? LEU A 81   HIS A 90   
B 3  VAL A 372  ? PHE A 376  ? VAL A 372  PHE A 376  
C 1  PHE A 126  ? TRP A 128  ? PHE A 126  TRP A 128  
C 2  LEU A 158  ? PHE A 160  ? LEU A 158  PHE A 160  
D 1  PHE A 524  ? ASP A 527  ? PHE A 524  ASP A 527  
D 2  ASP A 930  ? PHE A 934  ? ASP A 930  PHE A 934  
D 3  SER A 552  ? ASN A 559  ? SER A 552  ASN A 559  
D 4  GLY A 628  ? ILE A 636  ? GLY A 628  ILE A 636  
D 5  VAL A 578  ? ASP A 582  ? VAL A 578  ASP A 582  
D 6  PRO A 587  ? VAL A 588  ? PRO A 587  VAL A 588  
E 1  PHE A 524  ? ASP A 527  ? PHE A 524  ASP A 527  
E 2  ASP A 930  ? PHE A 934  ? ASP A 930  PHE A 934  
E 3  SER A 552  ? ASN A 559  ? SER A 552  ASN A 559  
E 4  GLY A 628  ? ILE A 636  ? GLY A 628  ILE A 636  
E 5  GLN A 945  ? PHE A 946  ? GLN A 945  PHE A 946  
F 1  THR A 542  ? ILE A 543  ? THR A 542  ILE A 543  
F 2  ARG A 565  ? VAL A 573  ? ARG A 565  VAL A 573  
F 3  THR A 606  ? VAL A 624  ? THR A 606  VAL A 624  
F 4  ALA A 590  ? ASP A 601  ? ALA A 590  ASP A 601  
F 5  THR A 644  ? TYR A 646  ? THR A 644  TYR A 646  
G 1  LYS A 669  ? GLY A 671  ? LYS A 669  GLY A 671  
G 2  SER A 648  ? LEU A 652  ? SER A 648  LEU A 652  
G 3  VAL A 745  ? LYS A 749  ? VAL A 745  LYS A 749  
G 4  SER A 754  ? LEU A 760  ? SER A 754  LEU A 760  
G 5  VAL A 763  ? MET A 769  ? VAL A 763  MET A 769  
G 6  GLU A 775  ? VAL A 780  ? GLU A 775  VAL A 780  
G 7  VAL A 888  ? LYS A 898  ? VAL A 888  LYS A 898  
G 8  THR A 842  ? THR A 848  ? THR A 842  THR A 848  
G 9  GLY A 834  ? GLU A 838  ? GLY A 834  GLU A 838  
G 10 ILE A 803  ? LEU A 808  ? ILE A 803  LEU A 808  
G 11 GLN A 812  ? ARG A 817  ? GLN A 812  ARG A 817  
G 12 ALA A 911  ? GLY A 912  ? ALA A 911  GLY A 912  
H 1  ILE A 676  ? ARG A 679  ? ILE A 676  ARG A 679  
H 2  THR A 685  ? PHE A 688  ? THR A 685  PHE A 688  
H 3  LEU A 694  ? GLN A 698  ? LEU A 694  GLN A 698  
H 4  VAL A 706  ? TYR A 715  ? VAL A 706  TYR A 715  
H 5  SER A 736  ? PRO A 737  ? SER A 736  PRO A 737  
I 1  ILE A 676  ? ARG A 679  ? ILE A 676  ARG A 679  
I 2  THR A 685  ? PHE A 688  ? THR A 685  PHE A 688  
I 3  LEU A 694  ? GLN A 698  ? LEU A 694  GLN A 698  
I 4  VAL A 706  ? TYR A 715  ? VAL A 706  TYR A 715  
I 5  THR A 788  ? THR A 796  ? THR A 788  THR A 796  
I 6  GLU A 861  ? ARG A 869  ? GLU A 861  ARG A 869  
I 7  LEU A 852  ? SER A 855  ? LEU A 852  SER A 855  
I 8  TYR A 829  ? ILE A 831  ? TYR A 829  ILE A 831  
J 1  LEU A 957  ? ARG A 964  ? LEU A 957  ARG A 964  
J 2  GLN A 973  ? ARG A 981  ? GLN A 973  ARG A 981  
J 3  THR A 1036 ? HIS A 1043 ? THR A 1036 HIS A 1043 
J 4  VAL A 1006 ? THR A 1012 ? VAL A 1006 THR A 1012 
J 5  ASN A 1019 ? HIS A 1022 ? ASN A 1019 HIS A 1022 
# 
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  N VAL A 43   ? N VAL A 43   O SER A 401  ? O SER A 401  
A 2  3  O LEU A 400  ? O LEU A 400  N LEU A 246  ? N LEU A 246  
A 3  4  N PHE A 245  ? N PHE A 245  O THR A 261  ? O THR A 261  
A 4  5  O HIS A 262  ? O HIS A 262  N MET A 224  ? N MET A 224  
A 5  6  O LEU A 225  ? O LEU A 225  N ALA A 202  ? N ALA A 202  
B 1  2  O LEU A 334  ? O LEU A 334  N LYS A 82   ? N LYS A 82   
B 2  3  N VAL A 85   ? N VAL A 85   O GLN A 375  ? O GLN A 375  
C 1  2  N PHE A 126  ? N PHE A 126  O GLU A 159  ? O GLU A 159  
D 1  2  N THR A 525  ? N THR A 525  O ILE A 933  ? O ILE A 933  
D 2  3  O PHE A 932  ? O PHE A 932  N VAL A 556  ? N VAL A 556  
D 3  4  N VAL A 555  ? N VAL A 555  O TYR A 632  ? O TYR A 632  
D 4  5  O VAL A 633  ? O VAL A 633  N THR A 581  ? N THR A 581  
D 5  6  N VAL A 580  ? N VAL A 580  O VAL A 588  ? O VAL A 588  
E 1  2  N THR A 525  ? N THR A 525  O ILE A 933  ? O ILE A 933  
E 2  3  O PHE A 932  ? O PHE A 932  N VAL A 556  ? N VAL A 556  
E 3  4  N VAL A 555  ? N VAL A 555  O TYR A 632  ? O TYR A 632  
E 4  5  N LEU A 629  ? N LEU A 629  O PHE A 946  ? O PHE A 946  
F 1  2  N ILE A 543  ? N ILE A 543  O TYR A 572  ? O TYR A 572  
F 2  3  N ARG A 565  ? N ARG A 565  O VAL A 624  ? O VAL A 624  
F 3  4  O GLN A 610  ? O GLN A 610  N SER A 597  ? N SER A 597  
F 4  5  N VAL A 592  ? N VAL A 592  O SER A 645  ? O SER A 645  
G 1  2  O LYS A 669  ? O LYS A 669  N LEU A 651  ? N LEU A 651  
G 2  3  N LEU A 652  ? N LEU A 652  O VAL A 745  ? O VAL A 745  
G 3  4  N LEU A 746  ? N LEU A 746  O SER A 757  ? O SER A 757  
G 4  5  N SER A 754  ? N SER A 754  O MET A 769  ? O MET A 769  
G 5  6  N ILE A 768  ? N ILE A 768  O GLU A 775  ? O GLU A 775  
G 6  7  N VAL A 780  ? N VAL A 780  O VAL A 888  ? O VAL A 888  
G 7  8  O VAL A 895  ? O VAL A 895  N THR A 845  ? N THR A 845  
G 8  9  O LEU A 846  ? O LEU A 846  N MET A 835  ? N MET A 835  
G 9  10 O PHE A 836  ? O PHE A 836  N TYR A 805  ? N TYR A 805  
G 10 11 N PHE A 804  ? N PHE A 804  O ARG A 816  ? O ARG A 816  
G 11 12 N PHE A 813  ? N PHE A 813  O GLY A 912  ? O GLY A 912  
H 1  2  N ILE A 676  ? N ILE A 676  O PHE A 688  ? O PHE A 688  
H 2  3  N ALA A 687  ? N ALA A 687  O LYS A 695  ? O LYS A 695  
H 3  4  N ILE A 697  ? N ILE A 697  O VAL A 706  ? O VAL A 706  
H 4  5  N LYS A 714  ? N LYS A 714  O SER A 736  ? O SER A 736  
I 1  2  N ILE A 676  ? N ILE A 676  O PHE A 688  ? O PHE A 688  
I 2  3  N ALA A 687  ? N ALA A 687  O LYS A 695  ? O LYS A 695  
I 3  4  N ILE A 697  ? N ILE A 697  O VAL A 706  ? O VAL A 706  
I 4  5  N LYS A 711  ? N LYS A 711  O ARG A 793  ? O ARG A 793  
I 5  6  N ILE A 790  ? N ILE A 790  O GLN A 866  ? O GLN A 866  
I 6  7  O MET A 865  ? O MET A 865  N GLY A 853  ? N GLY A 853  
I 7  8  O GLY A 854  ? O GLY A 854  N TYR A 829  ? N TYR A 829  
J 1  2  N ARG A 963  ? N ARG A 963  O GLY A 976  ? O GLY A 976  
J 2  3  N LEU A 979  ? N LEU A 979  O ALA A 1037 ? O ALA A 1037 
J 3  4  O SER A 1042 ? O SER A 1042 N ALA A 1007 ? N ALA A 1007 
J 4  5  N ARG A 1011 ? N ARG A 1011 O LEU A 1020 ? O LEU A 1020 
# 
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 ? ? ? ? 4  'BINDING SITE FOR RESIDUE NAG A 1046' 
AC2 Software ? ? ? ? 9  'BINDING SITE FOR RESIDUE PO4 A 1047' 
AC3 Software ? ? ? ? 3  'BINDING SITE FOR RESIDUE ZN A 1048'  
AC4 Software ? ? ? ? 7  'BINDING SITE FOR RESIDUE MRD A 1049' 
AC5 Software ? ? ? ? 18 'BINDING SITE FOR RESIDUE WZ1 A 1050' 
AC6 Software ? ? ? ? 5  'BINDING SITE FOR RESIDUE MPD A 1051' 
AC7 Software ? ? ? ? 5  'BINDING SITE FOR RESIDUE MPD A 1052' 
# 
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 4  LYS A 154 ? LYS A 154  . ? 1_555 ? 
2  AC1 4  ASN A 194 ? ASN A 194  . ? 1_555 ? 
3  AC1 4  HOH I .   ? HOH A 1650 . ? 1_555 ? 
4  AC1 4  HOH I .   ? HOH A 1651 . ? 1_555 ? 
5  AC2 9  ARG A 770 ? ARG A 770  . ? 1_555 ? 
6  AC2 9  ARG A 893 ? ARG A 893  . ? 1_555 ? 
7  AC2 9  SER A 924 ? SER A 924  . ? 1_555 ? 
8  AC2 9  HOH I .   ? HOH A 2071 . ? 1_555 ? 
9  AC2 9  HOH I .   ? HOH A 2084 . ? 1_555 ? 
10 AC2 9  HOH I .   ? HOH A 2085 . ? 1_555 ? 
11 AC2 9  HOH I .   ? HOH A 2087 . ? 1_555 ? 
12 AC2 9  HOH I .   ? HOH A 2092 . ? 1_555 ? 
13 AC2 9  HOH I .   ? HOH A 2099 . ? 1_555 ? 
14 AC3 3  HIS A 90  ? HIS A 90   . ? 1_555 ? 
15 AC3 3  ASP A 92  ? ASP A 92   . ? 1_555 ? 
16 AC3 3  HIS A 471 ? HIS A 471  . ? 1_555 ? 
17 AC4 7  LYS A 63  ? LYS A 63   . ? 1_555 ? 
18 AC4 7  GLN A 64  ? GLN A 64   . ? 1_555 ? 
19 AC4 7  HIS A 273 ? HIS A 273  . ? 1_555 ? 
20 AC4 7  HOH I .   ? HOH A 1166 . ? 1_555 ? 
21 AC4 7  HOH I .   ? HOH A 1705 . ? 1_555 ? 
22 AC4 7  HOH I .   ? HOH A 1707 . ? 1_555 ? 
23 AC4 7  HOH I .   ? HOH A 1709 . ? 1_555 ? 
24 AC5 18 HIS A 90  ? HIS A 90   . ? 1_555 ? 
25 AC5 18 ASP A 92  ? ASP A 92   . ? 1_555 ? 
26 AC5 18 TRP A 95  ? TRP A 95   . ? 1_555 ? 
27 AC5 18 ALA A 204 ? ALA A 204  . ? 1_555 ? 
28 AC5 18 ARG A 228 ? ARG A 228  . ? 1_555 ? 
29 AC5 18 SER A 268 ? SER A 268  . ? 1_555 ? 
30 AC5 18 TYR A 269 ? TYR A 269  . ? 1_555 ? 
31 AC5 18 ASP A 270 ? ASP A 270  . ? 1_555 ? 
32 AC5 18 ASP A 341 ? ASP A 341  . ? 1_555 ? 
33 AC5 18 TRP A 415 ? TRP A 415  . ? 1_555 ? 
34 AC5 18 HIS A 471 ? HIS A 471  . ? 1_555 ? 
35 AC5 18 ASP A 472 ? ASP A 472  . ? 1_555 ? 
36 AC5 18 TYR A 727 ? TYR A 727  . ? 1_555 ? 
37 AC5 18 GLU A 875 ? GLU A 875  . ? 1_555 ? 
38 AC5 18 ARG A 876 ? ARG A 876  . ? 1_555 ? 
39 AC5 18 HOH I .   ? HOH A 1194 . ? 1_555 ? 
40 AC5 18 HOH I .   ? HOH A 1197 . ? 1_555 ? 
41 AC5 18 HOH I .   ? HOH A 1843 . ? 1_555 ? 
42 AC6 5  TYR A 435 ? TYR A 435  . ? 1_555 ? 
43 AC6 5  LEU A 494 ? LEU A 494  . ? 1_555 ? 
44 AC6 5  GLN A 498 ? GLN A 498  . ? 1_555 ? 
45 AC6 5  TRP A 531 ? TRP A 531  . ? 1_555 ? 
46 AC6 5  HOH I .   ? HOH A 1582 . ? 1_555 ? 
47 AC7 5  ASP A 106 ? ASP A 106  . ? 1_555 ? 
48 AC7 5  ASP A 341 ? ASP A 341  . ? 1_555 ? 
49 AC7 5  HOH I .   ? HOH A 1215 . ? 1_555 ? 
50 AC7 5  HOH I .   ? HOH A 1852 . ? 1_555 ? 
51 AC7 5  HOH I .   ? HOH A 1853 . ? 1_555 ? 
# 
_database_PDB_matrix.entry_id          3BVT 
_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]   0.000000 
_database_PDB_matrix.origx_vector[2]   0.000000 
_database_PDB_matrix.origx_vector[3]   0.000000 
# 
_atom_sites.entry_id                    3BVT 
_atom_sites.fract_transf_matrix[1][1]   0.014484 
_atom_sites.fract_transf_matrix[1][2]   0.000000 
_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]   0.009104 
_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]   0.007214 
_atom_sites.fract_transf_vector[1]      0.000000 
_atom_sites.fract_transf_vector[2]      0.000000 
_atom_sites.fract_transf_vector[3]      0.000000 
# 
loop_
_atom_type.symbol 
C  
N  
O  
P  
S  
ZN 
# 
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   . GLN A 1 30   ? 46.912 34.412  -18.809 1.00 34.96 ? 30   GLN A N   1 
ATOM   2    C  CA  . GLN A 1 30   ? 45.485 34.221  -19.207 1.00 34.40 ? 30   GLN A CA  1 
ATOM   3    C  C   . GLN A 1 30   ? 44.559 35.217  -18.524 1.00 33.05 ? 30   GLN A C   1 
ATOM   4    O  O   . GLN A 1 30   ? 44.157 35.036  -17.371 1.00 33.96 ? 30   GLN A O   1 
ATOM   5    C  CB  . GLN A 1 30   ? 45.013 32.807  -18.914 1.00 35.00 ? 30   GLN A CB  1 
ATOM   6    C  CG  . GLN A 1 30   ? 43.754 32.468  -19.678 1.00 37.88 ? 30   GLN A CG  1 
ATOM   7    C  CD  . GLN A 1 30   ? 42.992 31.316  -19.069 1.00 42.15 ? 30   GLN A CD  1 
ATOM   8    O  OE1 . GLN A 1 30   ? 41.810 31.460  -18.739 1.00 43.68 ? 30   GLN A OE1 1 
ATOM   9    N  NE2 . GLN A 1 30   ? 43.656 30.167  -18.917 1.00 43.17 ? 30   GLN A NE2 1 
ATOM   10   N  N   . CYS A 1 31   ? 44.208 36.260  -19.262 1.00 30.64 ? 31   CYS A N   1 
ATOM   11   C  CA  . CYS A 1 31   ? 43.459 37.373  -18.710 1.00 27.88 ? 31   CYS A CA  1 
ATOM   12   C  C   . CYS A 1 31   ? 41.972 37.079  -18.687 1.00 26.14 ? 31   CYS A C   1 
ATOM   13   O  O   . CYS A 1 31   ? 41.450 36.475  -19.632 1.00 26.00 ? 31   CYS A O   1 
ATOM   14   C  CB  . CYS A 1 31   ? 43.734 38.595  -19.564 1.00 27.57 ? 31   CYS A CB  1 
ATOM   15   S  SG  . CYS A 1 31   ? 45.471 39.077  -19.466 1.00 28.18 ? 31   CYS A SG  1 
ATOM   16   N  N   . GLN A 1 32   ? 41.296 37.510  -17.623 1.00 23.81 ? 32   GLN A N   1 
ATOM   17   C  CA  . GLN A 1 32   ? 39.831 37.528  -17.584 1.00 22.53 ? 32   GLN A CA  1 
ATOM   18   C  C   . GLN A 1 32   ? 39.306 38.438  -18.681 1.00 20.66 ? 32   GLN A C   1 
ATOM   19   O  O   . GLN A 1 32   ? 39.882 39.495  -18.967 1.00 19.26 ? 32   GLN A O   1 
ATOM   20   C  CB  . GLN A 1 32   ? 39.307 38.095  -16.262 1.00 23.35 ? 32   GLN A CB  1 
ATOM   21   C  CG  . GLN A 1 32   ? 39.193 37.112  -15.127 1.00 26.30 ? 32   GLN A CG  1 
ATOM   22   C  CD  . GLN A 1 32   ? 38.141 37.536  -14.087 1.00 28.65 ? 32   GLN A CD  1 
ATOM   23   O  OE1 . GLN A 1 32   ? 37.013 37.033  -14.104 1.00 30.18 ? 32   GLN A OE1 1 
ATOM   24   N  NE2 . GLN A 1 32   ? 38.509 38.464  -13.194 1.00 29.33 ? 32   GLN A NE2 1 
ATOM   25   N  N   . ASP A 1 33   ? 38.201 38.029  -19.283 1.00 19.22 ? 33   ASP A N   1 
ATOM   26   C  CA  . ASP A 1 33   ? 37.535 38.839  -20.298 1.00 17.83 ? 33   ASP A CA  1 
ATOM   27   C  C   . ASP A 1 33   ? 36.601 39.814  -19.582 1.00 17.79 ? 33   ASP A C   1 
ATOM   28   O  O   . ASP A 1 33   ? 35.656 39.394  -18.934 1.00 19.65 ? 33   ASP A O   1 
ATOM   29   C  CB  . ASP A 1 33   ? 36.747 37.894  -21.219 1.00 18.15 ? 33   ASP A CB  1 
ATOM   30   C  CG  . ASP A 1 33   ? 36.095 38.592  -22.389 1.00 21.10 ? 33   ASP A CG  1 
ATOM   31   O  OD1 . ASP A 1 33   ? 35.551 39.714  -22.248 1.00 19.86 ? 33   ASP A OD1 1 
ATOM   32   O  OD2 . ASP A 1 33   ? 36.005 38.019  -23.497 1.00 24.10 ? 33   ASP A OD2 1 
ATOM   33   N  N   . VAL A 1 34   ? 36.830 41.114  -19.740 1.00 13.77 ? 34   VAL A N   1 
ATOM   34   C  CA  . VAL A 1 34   ? 36.095 42.130  -18.973 1.00 12.16 ? 34   VAL A CA  1 
ATOM   35   C  C   . VAL A 1 34   ? 34.890 42.680  -19.715 1.00 11.76 ? 34   VAL A C   1 
ATOM   36   O  O   . VAL A 1 34   ? 34.184 43.547  -19.220 1.00 11.03 ? 34   VAL A O   1 
ATOM   37   C  CB  . VAL A 1 34   ? 37.010 43.283  -18.497 1.00 11.89 ? 34   VAL A CB  1 
ATOM   38   C  CG1 . VAL A 1 34   ? 38.180 42.709  -17.750 1.00 13.29 ? 34   VAL A CG1 1 
ATOM   39   C  CG2 . VAL A 1 34   ? 37.548 44.101  -19.674 1.00 12.14 ? 34   VAL A CG2 1 
ATOM   40   N  N   . VAL A 1 35   ? 34.629 42.127  -20.901 1.00 11.89 ? 35   VAL A N   1 
ATOM   41   C  CA  . VAL A 1 35   ? 33.540 42.601  -21.745 1.00 11.69 ? 35   VAL A CA  1 
ATOM   42   C  C   . VAL A 1 35   ? 32.364 41.637  -21.924 1.00 11.30 ? 35   VAL A C   1 
ATOM   43   O  O   . VAL A 1 35   ? 31.220 42.041  -21.873 1.00 11.45 ? 35   VAL A O   1 
ATOM   44   C  CB  . VAL A 1 35   ? 34.073 42.963  -23.138 1.00 11.20 ? 35   VAL A CB  1 
ATOM   45   C  CG1 . VAL A 1 35   ? 32.927 43.355  -24.099 1.00 13.21 ? 35   VAL A CG1 1 
ATOM   46   C  CG2 . VAL A 1 35   ? 35.139 44.074  -23.042 1.00 13.42 ? 35   VAL A CG2 1 
ATOM   47   N  N   . GLN A 1 36   ? 32.687 40.359  -22.134 1.00 12.91 ? 36   GLN A N   1 
ATOM   48   C  CA  . GLN A 1 36   ? 31.706 39.409  -22.689 1.00 15.16 ? 36   GLN A CA  1 
ATOM   49   C  C   . GLN A 1 36   ? 31.042 38.499  -21.672 1.00 17.96 ? 36   GLN A C   1 
ATOM   50   O  O   . GLN A 1 36   ? 30.070 37.817  -22.008 1.00 20.88 ? 36   GLN A O   1 
ATOM   51   C  CB  . GLN A 1 36   ? 32.402 38.577  -23.755 1.00 14.87 ? 36   GLN A CB  1 
ATOM   52   C  CG  . GLN A 1 36   ? 33.050 39.405  -24.830 1.00 17.09 ? 36   GLN A CG  1 
ATOM   53   C  CD  . GLN A 1 36   ? 33.525 38.561  -25.983 1.00 17.38 ? 36   GLN A CD  1 
ATOM   54   O  OE1 . GLN A 1 36   ? 32.786 38.370  -26.949 1.00 20.00 ? 36   GLN A OE1 1 
ATOM   55   N  NE2 . GLN A 1 36   ? 34.759 38.092  -25.917 1.00 17.85 ? 36   GLN A NE2 1 
ATOM   56   N  N   . ASP A 1 37   ? 31.538 38.482  -20.442 1.00 18.30 ? 37   ASP A N   1 
ATOM   57   C  CA  . ASP A 1 37   ? 30.996 37.607  -19.398 1.00 19.48 ? 37   ASP A CA  1 
ATOM   58   C  C   . ASP A 1 37   ? 30.346 38.458  -18.298 1.00 18.58 ? 37   ASP A C   1 
ATOM   59   O  O   . ASP A 1 37   ? 31.054 39.125  -17.549 1.00 21.41 ? 37   ASP A O   1 
ATOM   60   C  CB  . ASP A 1 37   ? 32.122 36.750  -18.779 1.00 20.38 ? 37   ASP A CB  1 
ATOM   61   C  CG  . ASP A 1 37   ? 32.790 35.812  -19.777 1.00 23.67 ? 37   ASP A CG  1 
ATOM   62   O  OD1 . ASP A 1 37   ? 32.074 35.201  -20.599 1.00 27.86 ? 37   ASP A OD1 1 
ATOM   63   O  OD2 . ASP A 1 37   ? 34.036 35.625  -19.797 1.00 26.48 ? 37   ASP A OD2 1 
ATOM   64   N  N   . VAL A 1 38   ? 29.028 38.419  -18.181 1.00 17.41 ? 38   VAL A N   1 
ATOM   65   C  CA  . VAL A 1 38   ? 28.342 39.213  -17.136 1.00 16.66 ? 38   VAL A CA  1 
ATOM   66   C  C   . VAL A 1 38   ? 28.509 38.504  -15.784 1.00 16.31 ? 38   VAL A C   1 
ATOM   67   O  O   . VAL A 1 38   ? 28.097 37.341  -15.645 1.00 16.53 ? 38   VAL A O   1 
ATOM   68   C  CB  . VAL A 1 38   ? 26.847 39.393  -17.444 1.00 16.66 ? 38   VAL A CB  1 
ATOM   69   C  CG1 . VAL A 1 38   ? 26.118 40.110  -16.304 1.00 17.44 ? 38   VAL A CG1 1 
ATOM   70   C  CG2 . VAL A 1 38   ? 26.637 40.073  -18.822 1.00 17.83 ? 38   VAL A CG2 1 
ATOM   71   N  N   . PRO A 1 39   ? 29.147 39.138  -14.798 1.00 14.72 ? 39   PRO A N   1 
ATOM   72   C  CA  . PRO A 1 39   ? 29.336 38.474  -13.500 1.00 14.00 ? 39   PRO A CA  1 
ATOM   73   C  C   . PRO A 1 39   ? 28.015 38.126  -12.856 1.00 14.09 ? 39   PRO A C   1 
ATOM   74   O  O   . PRO A 1 39   ? 27.036 38.833  -12.937 1.00 14.13 ? 39   PRO A O   1 
ATOM   75   C  CB  . PRO A 1 39   ? 30.048 39.550  -12.672 1.00 14.04 ? 39   PRO A CB  1 
ATOM   76   C  CG  . PRO A 1 39   ? 30.828 40.327  -13.715 1.00 14.19 ? 39   PRO A CG  1 
ATOM   77   C  CD  . PRO A 1 39   ? 29.821 40.464  -14.841 1.00 14.33 ? 39   PRO A CD  1 
ATOM   78   N  N   . ASN A 1 40   ? 27.997 36.958  -12.219 1.00 14.87 ? 40   ASN A N   1 
ATOM   79   C  CA  . ASN A 1 40   ? 26.854 36.568  -11.429 1.00 16.08 ? 40   ASN A CA  1 
ATOM   80   C  C   . ASN A 1 40   ? 27.112 36.929  -9.959  1.00 14.70 ? 40   ASN A C   1 
ATOM   81   O  O   . ASN A 1 40   ? 28.008 36.349  -9.313  1.00 16.10 ? 40   ASN A O   1 
ATOM   82   C  CB  . ASN A 1 40   ? 26.589 35.068  -11.630 1.00 17.87 ? 40   ASN A CB  1 
ATOM   83   C  CG  . ASN A 1 40   ? 25.469 34.548  -10.779 1.00 22.11 ? 40   ASN A CG  1 
ATOM   84   O  OD1 . ASN A 1 40   ? 24.463 35.223  -10.553 1.00 27.06 ? 40   ASN A OD1 1 
ATOM   85   N  ND2 . ASN A 1 40   ? 25.629 33.315  -10.304 1.00 28.32 ? 40   ASN A ND2 1 
ATOM   86   N  N   . VAL A 1 41   ? 26.384 37.938  -9.487  1.00 13.49 ? 41   VAL A N   1 
ATOM   87   C  CA  . VAL A 1 41   ? 26.546 38.421  -8.100  1.00 12.38 ? 41   VAL A CA  1 
ATOM   88   C  C   . VAL A 1 41   ? 25.205 38.399  -7.401  1.00 12.79 ? 41   VAL A C   1 
ATOM   89   O  O   . VAL A 1 41   ? 24.146 38.514  -8.038  1.00 13.18 ? 41   VAL A O   1 
ATOM   90   C  CB  . VAL A 1 41   ? 27.186 39.856  -8.061  1.00 11.75 ? 41   VAL A CB  1 
ATOM   91   C  CG1 . VAL A 1 41   ? 28.610 39.780  -8.567  1.00 13.22 ? 41   VAL A CG1 1 
ATOM   92   C  CG2 . VAL A 1 41   ? 26.335 40.851  -8.874  1.00 12.47 ? 41   VAL A CG2 1 
ATOM   93   N  N   . ASP A 1 42   ? 25.203 38.272  -6.083  1.00 11.86 ? 42   ASP A N   1 
ATOM   94   C  CA  . ASP A 1 42   ? 23.951 38.315  -5.339  1.00 11.70 ? 42   ASP A CA  1 
ATOM   95   C  C   . ASP A 1 42   ? 23.256 39.670  -5.384  1.00 11.42 ? 42   ASP A C   1 
ATOM   96   O  O   . ASP A 1 42   ? 22.044 39.756  -5.437  1.00 12.58 ? 42   ASP A O   1 
ATOM   97   C  CB  . ASP A 1 42   ? 24.178 37.883  -3.892  1.00 12.25 ? 42   ASP A CB  1 
ATOM   98   C  CG  . ASP A 1 42   ? 24.700 36.472  -3.795  1.00 15.42 ? 42   ASP A CG  1 
ATOM   99   O  OD1 . ASP A 1 42   ? 24.059 35.580  -4.377  1.00 19.82 ? 42   ASP A OD1 1 
ATOM   100  O  OD2 . ASP A 1 42   ? 25.741 36.240  -3.166  1.00 15.41 ? 42   ASP A OD2 1 
ATOM   101  N  N   . VAL A 1 43   ? 24.044 40.735  -5.317  1.00 10.27 ? 43   VAL A N   1 
ATOM   102  C  CA  . VAL A 1 43   ? 23.498 42.094  -5.319  1.00 10.14 ? 43   VAL A CA  1 
ATOM   103  C  C   . VAL A 1 43   ? 24.258 42.849  -6.399  1.00 9.56  ? 43   VAL A C   1 
ATOM   104  O  O   . VAL A 1 43   ? 25.496 42.965  -6.330  1.00 10.01 ? 43   VAL A O   1 
ATOM   105  C  CB  . VAL A 1 43   ? 23.692 42.796  -3.971  1.00 10.26 ? 43   VAL A CB  1 
ATOM   106  C  CG1 . VAL A 1 43   ? 23.124 44.211  -4.059  1.00 12.18 ? 43   VAL A CG1 1 
ATOM   107  C  CG2 . VAL A 1 43   ? 23.017 41.993  -2.837  1.00 12.41 ? 43   VAL A CG2 1 
ATOM   108  N  N   . GLN A 1 44   ? 23.545 43.374  -7.394  1.00 9.31  ? 44   GLN A N   1 
ATOM   109  C  CA  . GLN A 1 44   ? 24.173 44.215  -8.402  1.00 9.83  ? 44   GLN A CA  1 
ATOM   110  C  C   . GLN A 1 44   ? 23.456 45.542  -8.298  1.00 8.75  ? 44   GLN A C   1 
ATOM   111  O  O   . GLN A 1 44   ? 22.250 45.610  -8.420  1.00 9.19  ? 44   GLN A O   1 
ATOM   112  C  CB  . GLN A 1 44   ? 24.001 43.579  -9.780  1.00 9.80  ? 44   GLN A CB  1 
ATOM   113  C  CG  . GLN A 1 44   ? 25.084 43.991  -10.765 1.00 9.67  ? 44   GLN A CG  1 
ATOM   114  C  CD  . GLN A 1 44   ? 25.163 45.504  -10.938 1.00 9.62  ? 44   GLN A CD  1 
ATOM   115  O  OE1 . GLN A 1 44   ? 24.156 46.145  -11.261 1.00 9.66  ? 44   GLN A OE1 1 
ATOM   116  N  NE2 . GLN A 1 44   ? 26.349 46.085  -10.646 1.00 8.95  ? 44   GLN A NE2 1 
ATOM   117  N  N   . MET A 1 45   ? 24.189 46.605  -7.964  1.00 8.86  ? 45   MET A N   1 
ATOM   118  C  CA  . MET A 1 45   ? 23.517 47.811  -7.509  1.00 8.91  ? 45   MET A CA  1 
ATOM   119  C  C   . MET A 1 45   ? 22.599 48.470  -8.554  1.00 8.30  ? 45   MET A C   1 
ATOM   120  O  O   . MET A 1 45   ? 21.617 49.089  -8.182  1.00 9.34  ? 45   MET A O   1 
ATOM   121  C  CB  . MET A 1 45   ? 24.524 48.823  -6.930  1.00 8.77  ? 45   MET A CB  1 
ATOM   122  C  CG  . MET A 1 45   ? 25.162 48.349  -5.634  1.00 9.54  ? 45   MET A CG  1 
ATOM   123  S  SD  . MET A 1 45   ? 23.917 48.093  -4.315  1.00 11.37 ? 45   MET A SD  1 
ATOM   124  C  CE  . MET A 1 45   ? 23.201 49.747  -4.164  1.00 13.86 ? 45   MET A CE  1 
ATOM   125  N  N   . LEU A 1 46   ? 22.973 48.380  -9.818  1.00 8.60  ? 46   LEU A N   1 
ATOM   126  C  CA  . LEU A 1 46   ? 22.091 48.959  -10.873 1.00 9.35  ? 46   LEU A CA  1 
ATOM   127  C  C   . LEU A 1 46   ? 20.749 48.184  -10.907 1.00 10.32 ? 46   LEU A C   1 
ATOM   128  O  O   . LEU A 1 46   ? 19.676 48.770  -11.001 1.00 10.54 ? 46   LEU A O   1 
ATOM   129  C  CB  . LEU A 1 46   ? 22.770 48.898  -12.210 1.00 10.38 ? 46   LEU A CB  1 
ATOM   130  C  CG  . LEU A 1 46   ? 22.010 49.669  -13.310 1.00 10.64 ? 46   LEU A CG  1 
ATOM   131  C  CD1 . LEU A 1 46   ? 22.040 51.205  -13.079 1.00 10.80 ? 46   LEU A CD1 1 
ATOM   132  C  CD2 . LEU A 1 46   ? 22.574 49.310  -14.634 1.00 12.87 ? 46   LEU A CD2 1 
ATOM   133  N  N   . GLU A 1 47   ? 20.841 46.866  -10.784 1.00 10.17 ? 47   GLU A N   1 
ATOM   134  C  CA  . GLU A 1 47   ? 19.636 46.014  -10.798 1.00 11.81 ? 47   GLU A CA  1 
ATOM   135  C  C   . GLU A 1 47   ? 18.835 46.307  -9.549  1.00 11.70 ? 47   GLU A C   1 
ATOM   136  O  O   . GLU A 1 47   ? 17.603 46.439  -9.585  1.00 12.45 ? 47   GLU A O   1 
ATOM   137  C  CB  . GLU A 1 47   ? 20.052 44.547  -10.877 1.00 12.73 ? 47   GLU A CB  1 
ATOM   138  C  CG  . GLU A 1 47   ? 18.916 43.564  -11.140 1.00 16.57 ? 47   GLU A CG  1 
ATOM   139  C  CD  . GLU A 1 47   ? 18.126 43.207  -9.909  1.00 21.40 ? 47   GLU A CD  1 
ATOM   140  O  OE1 . GLU A 1 47   ? 18.608 43.353  -8.750  1.00 20.00 ? 47   GLU A OE1 1 
ATOM   141  O  OE2 . GLU A 1 47   ? 16.967 42.757  -10.100 1.00 24.00 ? 47   GLU A OE2 1 
ATOM   142  N  N   . LEU A 1 48   ? 19.504 46.453  -8.414  1.00 11.15 ? 48   LEU A N   1 
ATOM   143  C  CA  . LEU A 1 48   ? 18.809 46.778  -7.189  1.00 12.18 ? 48   LEU A CA  1 
ATOM   144  C  C   . LEU A 1 48   ? 18.062 48.099  -7.295  1.00 11.56 ? 48   LEU A C   1 
ATOM   145  O  O   . LEU A 1 48   ? 16.896 48.215  -6.909  1.00 12.47 ? 48   LEU A O   1 
ATOM   146  C  CB  . LEU A 1 48   ? 19.793 46.845  -6.011  1.00 12.31 ? 48   LEU A CB  1 
ATOM   147  C  CG  . LEU A 1 48   ? 19.122 46.979  -4.658  1.00 13.49 ? 48   LEU A CG  1 
ATOM   148  C  CD1 . LEU A 1 48   ? 18.129 45.833  -4.404  1.00 20.88 ? 48   LEU A CD1 1 
ATOM   149  C  CD2 . LEU A 1 48   ? 20.138 47.101  -3.505  1.00 16.39 ? 48   LEU A CD2 1 
ATOM   150  N  N   . TYR A 1 49   ? 18.732 49.127  -7.817  1.00 10.57 ? 49   TYR A N   1 
ATOM   151  C  CA  . TYR A 1 49   ? 18.109 50.431  -8.056  1.00 10.74 ? 49   TYR A CA  1 
ATOM   152  C  C   . TYR A 1 49   ? 16.850 50.330  -8.947  1.00 11.74 ? 49   TYR A C   1 
ATOM   153  O  O   . TYR A 1 49   ? 15.866 51.003  -8.686  1.00 12.19 ? 49   TYR A O   1 
ATOM   154  C  CB  . TYR A 1 49   ? 19.149 51.399  -8.659  1.00 10.09 ? 49   TYR A CB  1 
ATOM   155  C  CG  . TYR A 1 49   ? 19.684 52.327  -7.600  1.00 10.37 ? 49   TYR A CG  1 
ATOM   156  C  CD1 . TYR A 1 49   ? 20.161 51.848  -6.374  1.00 10.14 ? 49   TYR A CD1 1 
ATOM   157  C  CD2 . TYR A 1 49   ? 19.696 53.699  -7.820  1.00 10.91 ? 49   TYR A CD2 1 
ATOM   158  C  CE1 . TYR A 1 49   ? 20.595 52.708  -5.393  1.00 9.80  ? 49   TYR A CE1 1 
ATOM   159  C  CE2 . TYR A 1 49   ? 20.158 54.580  -6.850  1.00 9.77  ? 49   TYR A CE2 1 
ATOM   160  C  CZ  . TYR A 1 49   ? 20.588 54.069  -5.622  1.00 8.46  ? 49   TYR A CZ  1 
ATOM   161  O  OH  . TYR A 1 49   ? 20.985 54.885  -4.613  1.00 10.38 ? 49   TYR A OH  1 
ATOM   162  N  N   . ASP A 1 50   ? 16.888 49.484  -9.958  1.00 12.11 ? 50   ASP A N   1 
ATOM   163  C  CA  . ASP A 1 50   ? 15.761 49.374  -10.890 1.00 14.63 ? 50   ASP A CA  1 
ATOM   164  C  C   . ASP A 1 50   ? 14.533 48.801  -10.146 1.00 15.58 ? 50   ASP A C   1 
ATOM   165  O  O   . ASP A 1 50   ? 13.390 49.215  -10.437 1.00 16.49 ? 50   ASP A O   1 
ATOM   166  C  CB  . ASP A 1 50   ? 16.208 48.517  -12.067 1.00 15.78 ? 50   ASP A CB  1 
ATOM   167  C  CG  . ASP A 1 50   ? 15.371 48.713  -13.308 1.00 20.17 ? 50   ASP A CG  1 
ATOM   168  O  OD1 . ASP A 1 50   ? 14.661 49.735  -13.419 1.00 24.39 ? 50   ASP A OD1 1 
ATOM   169  O  OD2 . ASP A 1 50   ? 15.436 47.888  -14.250 1.00 25.55 ? 50   ASP A OD2 1 
ATOM   170  N  N   . ARG A 1 51   ? 14.771 47.893  -9.198  1.00 15.66 ? 51   ARG A N   1 
ATOM   171  C  CA  . ARG A 1 51   ? 13.717 47.195  -8.423  1.00 18.77 ? 51   ARG A CA  1 
ATOM   172  C  C   . ARG A 1 51   ? 13.195 47.959  -7.224  1.00 17.76 ? 51   ARG A C   1 
ATOM   173  O  O   . ARG A 1 51   ? 12.024 47.828  -6.878  1.00 19.39 ? 51   ARG A O   1 
ATOM   174  C  CB  . ARG A 1 51   ? 14.249 45.854  -7.866  1.00 19.10 ? 51   ARG A CB  1 
ATOM   175  C  CG  . ARG A 1 51   ? 14.394 44.746  -8.840  1.00 23.52 ? 51   ARG A CG  1 
ATOM   176  C  CD  . ARG A 1 51   ? 15.015 43.475  -8.217  1.00 24.34 ? 51   ARG A CD  1 
ATOM   177  N  NE  . ARG A 1 51   ? 14.930 43.462  -6.761  1.00 31.45 ? 51   ARG A NE  1 
ATOM   178  C  CZ  . ARG A 1 51   ? 15.960 43.289  -5.945  1.00 33.89 ? 51   ARG A CZ  1 
ATOM   179  N  NH1 . ARG A 1 51   ? 17.183 43.081  -6.431  1.00 34.76 ? 51   ARG A NH1 1 
ATOM   180  N  NH2 . ARG A 1 51   ? 15.762 43.312  -4.631  1.00 36.47 ? 51   ARG A NH2 1 
ATOM   181  N  N   . MET A 1 52   ? 14.052 48.719  -6.530  1.00 16.10 ? 52   MET A N   1 
ATOM   182  C  CA  A MET A 1 52   ? 13.659 49.383  -5.286  0.50 16.60 ? 52   MET A CA  1 
ATOM   183  C  CA  B MET A 1 52   ? 13.676 49.403  -5.287  0.50 15.90 ? 52   MET A CA  1 
ATOM   184  C  C   . MET A 1 52   ? 12.643 50.502  -5.462  1.00 15.79 ? 52   MET A C   1 
ATOM   185  O  O   . MET A 1 52   ? 12.660 51.208  -6.454  1.00 15.96 ? 52   MET A O   1 
ATOM   186  C  CB  A MET A 1 52   ? 14.890 49.978  -4.603  0.50 16.49 ? 52   MET A CB  1 
ATOM   187  C  CB  B MET A 1 52   ? 14.904 50.076  -4.677  0.50 15.73 ? 52   MET A CB  1 
ATOM   188  C  CG  A MET A 1 52   ? 15.756 48.970  -3.876  0.50 16.95 ? 52   MET A CG  1 
ATOM   189  C  CG  B MET A 1 52   ? 15.939 49.148  -4.090  0.50 15.27 ? 52   MET A CG  1 
ATOM   190  S  SD  A MET A 1 52   ? 17.279 49.732  -3.257  0.50 17.87 ? 52   MET A SD  1 
ATOM   191  S  SD  B MET A 1 52   ? 17.487 50.059  -3.773  0.50 14.98 ? 52   MET A SD  1 
ATOM   192  C  CE  A MET A 1 52   ? 16.635 50.961  -2.193  0.50 18.99 ? 52   MET A CE  1 
ATOM   193  C  CE  B MET A 1 52   ? 16.977 51.298  -2.618  0.50 13.96 ? 52   MET A CE  1 
ATOM   194  N  N   . SER A 1 53   ? 11.776 50.684  -4.458  1.00 15.96 ? 53   SER A N   1 
ATOM   195  C  CA  A SER A 1 53   ? 10.741 51.711  -4.493  0.50 16.98 ? 53   SER A CA  1 
ATOM   196  C  CA  B SER A 1 53   ? 10.750 51.729  -4.525  0.50 16.92 ? 53   SER A CA  1 
ATOM   197  C  C   . SER A 1 53   ? 11.174 53.074  -3.914  1.00 16.69 ? 53   SER A C   1 
ATOM   198  O  O   . SER A 1 53   ? 10.557 54.102  -4.176  1.00 17.63 ? 53   SER A O   1 
ATOM   199  C  CB  A SER A 1 53   ? 9.492  51.176  -3.772  0.50 16.99 ? 53   SER A CB  1 
ATOM   200  C  CB  B SER A 1 53   ? 9.432  51.255  -3.884  0.50 17.13 ? 53   SER A CB  1 
ATOM   201  O  OG  A SER A 1 53   ? 9.005  50.029  -4.463  0.50 19.55 ? 53   SER A OG  1 
ATOM   202  O  OG  B SER A 1 53   ? 9.518  51.210  -2.481  0.50 18.84 ? 53   SER A OG  1 
ATOM   203  N  N   . PHE A 1 54   ? 12.196 53.061  -3.067  1.00 15.57 ? 54   PHE A N   1 
ATOM   204  C  CA  . PHE A 1 54   ? 12.733 54.283  -2.448  1.00 14.79 ? 54   PHE A CA  1 
ATOM   205  C  C   . PHE A 1 54   ? 11.697 55.069  -1.640  1.00 15.83 ? 54   PHE A C   1 
ATOM   206  O  O   . PHE A 1 54   ? 11.797 56.287  -1.497  1.00 16.10 ? 54   PHE A O   1 
ATOM   207  C  CB  . PHE A 1 54   ? 13.398 55.223  -3.496  1.00 14.32 ? 54   PHE A CB  1 
ATOM   208  C  CG  . PHE A 1 54   ? 14.666 54.665  -4.125  1.00 12.50 ? 54   PHE A CG  1 
ATOM   209  C  CD1 . PHE A 1 54   ? 14.607 53.833  -5.229  1.00 13.50 ? 54   PHE A CD1 1 
ATOM   210  C  CD2 . PHE A 1 54   ? 15.918 55.015  -3.608  1.00 12.78 ? 54   PHE A CD2 1 
ATOM   211  C  CE1 . PHE A 1 54   ? 15.765 53.316  -5.816  1.00 12.43 ? 54   PHE A CE1 1 
ATOM   212  C  CE2 . PHE A 1 54   ? 17.068 54.554  -4.193  1.00 13.64 ? 54   PHE A CE2 1 
ATOM   213  C  CZ  . PHE A 1 54   ? 17.010 53.691  -5.295  1.00 13.50 ? 54   PHE A CZ  1 
ATOM   214  N  N   . LYS A 1 55   ? 10.708 54.383  -1.066  1.00 16.30 ? 55   LYS A N   1 
ATOM   215  C  CA  . LYS A 1 55   ? 9.744  55.123  -0.243  1.00 17.54 ? 55   LYS A CA  1 
ATOM   216  C  C   . LYS A 1 55   ? 10.343 55.593  1.063   1.00 17.89 ? 55   LYS A C   1 
ATOM   217  O  O   . LYS A 1 55   ? 11.061 54.873  1.733   1.00 19.73 ? 55   LYS A O   1 
ATOM   218  C  CB  . LYS A 1 55   ? 8.481  54.296  0.052   1.00 17.82 ? 55   LYS A CB  1 
ATOM   219  C  CG  . LYS A 1 55   ? 7.732  53.813  -1.174  1.00 18.98 ? 55   LYS A CG  1 
ATOM   220  C  CD  . LYS A 1 55   ? 7.442  54.920  -2.178  1.00 19.73 ? 55   LYS A CD  1 
ATOM   221  C  CE  . LYS A 1 55   ? 6.587  54.419  -3.349  1.00 23.74 ? 55   LYS A CE  1 
ATOM   222  N  NZ  . LYS A 1 55   ? 6.298  55.513  -4.336  1.00 24.53 ? 55   LYS A NZ  1 
ATOM   223  N  N   . ASP A 1 56   ? 10.025 56.813  1.440   1.00 17.48 ? 56   ASP A N   1 
ATOM   224  C  CA  . ASP A 1 56   ? 10.590 57.420  2.616   1.00 18.42 ? 56   ASP A CA  1 
ATOM   225  C  C   . ASP A 1 56   ? 9.535  57.433  3.729   1.00 19.61 ? 56   ASP A C   1 
ATOM   226  O  O   . ASP A 1 56   ? 8.921  58.464  4.022   1.00 21.07 ? 56   ASP A O   1 
ATOM   227  C  CB  . ASP A 1 56   ? 11.117 58.820  2.257   1.00 17.84 ? 56   ASP A CB  1 
ATOM   228  C  CG  . ASP A 1 56   ? 11.725 59.543  3.436   1.00 17.38 ? 56   ASP A CG  1 
ATOM   229  O  OD1 . ASP A 1 56   ? 12.234 58.882  4.366   1.00 16.87 ? 56   ASP A OD1 1 
ATOM   230  O  OD2 . ASP A 1 56   ? 11.717 60.789  3.521   1.00 20.01 ? 56   ASP A OD2 1 
ATOM   231  N  N   . ILE A 1 57   ? 9.348  56.285  4.364   1.00 20.01 ? 57   ILE A N   1 
ATOM   232  C  CA  . ILE A 1 57   ? 8.309  56.179  5.383   1.00 21.45 ? 57   ILE A CA  1 
ATOM   233  C  C   . ILE A 1 57   ? 8.912  56.208  6.776   1.00 21.50 ? 57   ILE A C   1 
ATOM   234  O  O   . ILE A 1 57   ? 10.067 55.775  6.986   1.00 21.08 ? 57   ILE A O   1 
ATOM   235  C  CB  . ILE A 1 57   ? 7.396  54.941  5.155   1.00 22.86 ? 57   ILE A CB  1 
ATOM   236  C  CG1 . ILE A 1 57   ? 8.165  53.637  5.303   1.00 23.92 ? 57   ILE A CG1 1 
ATOM   237  C  CG2 . ILE A 1 57   ? 6.691  55.023  3.771   1.00 23.22 ? 57   ILE A CG2 1 
ATOM   238  C  CD1 . ILE A 1 57   ? 7.310  52.464  5.800   1.00 27.80 ? 57   ILE A CD1 1 
ATOM   239  N  N   . ASP A 1 58   ? 8.137  56.734  7.722   1.00 20.83 ? 58   ASP A N   1 
ATOM   240  C  CA  . ASP A 1 58   ? 8.524  56.767  9.127   1.00 21.39 ? 58   ASP A CA  1 
ATOM   241  C  C   . ASP A 1 58   ? 8.538  55.342  9.676   1.00 20.60 ? 58   ASP A C   1 
ATOM   242  O  O   . ASP A 1 58   ? 7.485  54.721  9.862   1.00 20.74 ? 58   ASP A O   1 
ATOM   243  C  CB  . ASP A 1 58   ? 7.544  57.664  9.900   1.00 21.99 ? 58   ASP A CB  1 
ATOM   244  C  CG  . ASP A 1 58   ? 7.950  57.892  11.338  1.00 25.54 ? 58   ASP A CG  1 
ATOM   245  O  OD1 . ASP A 1 58   ? 8.820  57.168  11.878  1.00 24.35 ? 58   ASP A OD1 1 
ATOM   246  O  OD2 . ASP A 1 58   ? 7.434  58.810  12.017  1.00 28.97 ? 58   ASP A OD2 1 
ATOM   247  N  N   . GLY A 1 59   ? 9.728  54.804  9.914   1.00 19.40 ? 59   GLY A N   1 
ATOM   248  C  CA  . GLY A 1 59   ? 9.844  53.456  10.422  1.00 17.93 ? 59   GLY A CA  1 
ATOM   249  C  C   . GLY A 1 59   ? 9.769  53.341  11.943  1.00 16.40 ? 59   GLY A C   1 
ATOM   250  O  O   . GLY A 1 59   ? 9.996  52.254  12.469  1.00 16.92 ? 59   GLY A O   1 
ATOM   251  N  N   . GLY A 1 60   ? 9.505  54.445  12.640  1.00 16.23 ? 60   GLY A N   1 
ATOM   252  C  CA  . GLY A 1 60   ? 9.510  54.432  14.091  1.00 17.34 ? 60   GLY A CA  1 
ATOM   253  C  C   . GLY A 1 60   ? 10.787 55.026  14.692  1.00 16.21 ? 60   GLY A C   1 
ATOM   254  O  O   . GLY A 1 60   ? 11.326 56.019  14.172  1.00 16.89 ? 60   GLY A O   1 
ATOM   255  N  N   . VAL A 1 61   ? 11.248 54.485  15.818  1.00 15.74 ? 61   VAL A N   1 
ATOM   256  C  CA  . VAL A 1 61   ? 12.483 55.001  16.432  1.00 14.57 ? 61   VAL A CA  1 
ATOM   257  C  C   . VAL A 1 61   ? 13.660 54.917  15.435  1.00 13.96 ? 61   VAL A C   1 
ATOM   258  O  O   . VAL A 1 61   ? 14.472 55.850  15.354  1.00 14.35 ? 61   VAL A O   1 
ATOM   259  C  CB  . VAL A 1 61   ? 12.821 54.357  17.806  1.00 15.57 ? 61   VAL A CB  1 
ATOM   260  C  CG1 . VAL A 1 61   ? 11.749 54.712  18.843  1.00 16.13 ? 61   VAL A CG1 1 
ATOM   261  C  CG2 . VAL A 1 61   ? 13.028 52.849  17.714  1.00 16.13 ? 61   VAL A CG2 1 
ATOM   262  N  N   . TRP A 1 62   ? 13.719 53.839  14.673  1.00 13.47 ? 62   TRP A N   1 
ATOM   263  C  CA  . TRP A 1 62   ? 14.645 53.768  13.543  1.00 12.92 ? 62   TRP A CA  1 
ATOM   264  C  C   . TRP A 1 62   ? 13.905 54.413  12.396  1.00 13.51 ? 62   TRP A C   1 
ATOM   265  O  O   . TRP A 1 62   ? 13.124 53.758  11.690  1.00 13.32 ? 62   TRP A O   1 
ATOM   266  C  CB  . TRP A 1 62   ? 15.057 52.320  13.242  1.00 12.84 ? 62   TRP A CB  1 
ATOM   267  C  CG  . TRP A 1 62   ? 16.032 52.213  12.097  1.00 11.27 ? 62   TRP A CG  1 
ATOM   268  C  CD1 . TRP A 1 62   ? 16.718 53.259  11.478  1.00 11.65 ? 62   TRP A CD1 1 
ATOM   269  C  CD2 . TRP A 1 62   ? 16.400 51.031  11.407  1.00 11.42 ? 62   TRP A CD2 1 
ATOM   270  N  NE1 . TRP A 1 62   ? 17.474 52.759  10.447  1.00 11.20 ? 62   TRP A NE1 1 
ATOM   271  C  CE2 . TRP A 1 62   ? 17.308 51.401  10.375  1.00 12.04 ? 62   TRP A CE2 1 
ATOM   272  C  CE3 . TRP A 1 62   ? 16.049 49.677  11.536  1.00 10.40 ? 62   TRP A CE3 1 
ATOM   273  C  CZ2 . TRP A 1 62   ? 17.862 50.470  9.488   1.00 11.69 ? 62   TRP A CZ2 1 
ATOM   274  C  CZ3 . TRP A 1 62   ? 16.591 48.753  10.674  1.00 12.05 ? 62   TRP A CZ3 1 
ATOM   275  C  CH2 . TRP A 1 62   ? 17.502 49.143  9.655   1.00 11.57 ? 62   TRP A CH2 1 
ATOM   276  N  N   . LYS A 1 63   ? 14.129 55.717  12.206  1.00 13.01 ? 63   LYS A N   1 
ATOM   277  C  CA  . LYS A 1 63   ? 13.224 56.499  11.341  1.00 14.58 ? 63   LYS A CA  1 
ATOM   278  C  C   . LYS A 1 63   ? 13.198 56.012  9.911   1.00 14.61 ? 63   LYS A C   1 
ATOM   279  O  O   . LYS A 1 63   ? 12.170 56.101  9.225   1.00 15.37 ? 63   LYS A O   1 
ATOM   280  C  CB  . LYS A 1 63   ? 13.560 57.992  11.388  1.00 14.85 ? 63   LYS A CB  1 
ATOM   281  C  CG  . LYS A 1 63   ? 13.181 58.683  12.707  1.00 19.66 ? 63   LYS A CG  1 
ATOM   282  C  CD  . LYS A 1 63   ? 11.688 59.065  12.741  1.00 23.24 ? 63   LYS A CD  1 
ATOM   283  C  CE  . LYS A 1 63   ? 11.282 59.766  14.049  1.00 24.92 ? 63   LYS A CE  1 
ATOM   284  N  NZ  . LYS A 1 63   ? 11.383 58.903  15.302  1.00 29.01 ? 63   LYS A NZ  1 
ATOM   285  N  N   . GLN A 1 64   ? 14.321 55.486  9.434   1.00 12.84 ? 64   GLN A N   1 
ATOM   286  C  CA  . GLN A 1 64   ? 14.398 55.033  8.060   1.00 12.48 ? 64   GLN A CA  1 
ATOM   287  C  C   . GLN A 1 64   ? 14.467 53.522  7.913   1.00 12.20 ? 64   GLN A C   1 
ATOM   288  O  O   . GLN A 1 64   ? 14.778 52.995  6.841   1.00 11.89 ? 64   GLN A O   1 
ATOM   289  C  CB  . GLN A 1 64   ? 15.596 55.698  7.354   1.00 12.13 ? 64   GLN A CB  1 
ATOM   290  C  CG  . GLN A 1 64   ? 15.511 57.194  7.388   1.00 12.61 ? 64   GLN A CG  1 
ATOM   291  C  CD  . GLN A 1 64   ? 16.876 57.881  7.244   1.00 11.77 ? 64   GLN A CD  1 
ATOM   292  O  OE1 . GLN A 1 64   ? 17.837 57.536  7.967   1.00 12.32 ? 64   GLN A OE1 1 
ATOM   293  N  NE2 . GLN A 1 64   ? 16.940 58.866  6.367   1.00 12.02 ? 64   GLN A NE2 1 
ATOM   294  N  N   . GLY A 1 65   ? 14.111 52.823  9.001   1.00 13.10 ? 65   GLY A N   1 
ATOM   295  C  CA  . GLY A 1 65   ? 14.073 51.368  8.997   1.00 13.06 ? 65   GLY A CA  1 
ATOM   296  C  C   . GLY A 1 65   ? 12.711 50.817  9.420   1.00 13.78 ? 65   GLY A C   1 
ATOM   297  O  O   . GLY A 1 65   ? 11.679 51.196  8.839   1.00 14.94 ? 65   GLY A O   1 
ATOM   298  N  N   . TRP A 1 66   ? 12.733 49.926  10.400  1.00 14.35 ? 66   TRP A N   1 
ATOM   299  C  CA  . TRP A 1 66   ? 11.496 49.298  10.917  1.00 14.40 ? 66   TRP A CA  1 
ATOM   300  C  C   . TRP A 1 66   ? 11.782 48.944  12.354  1.00 15.07 ? 66   TRP A C   1 
ATOM   301  O  O   . TRP A 1 66   ? 12.915 49.079  12.828  1.00 14.47 ? 66   TRP A O   1 
ATOM   302  C  CB  . TRP A 1 66   ? 11.118 48.066  10.086  1.00 15.00 ? 66   TRP A CB  1 
ATOM   303  C  CG  . TRP A 1 66   ? 12.066 46.907  10.233  1.00 14.62 ? 66   TRP A CG  1 
ATOM   304  C  CD1 . TRP A 1 66   ? 11.954 45.858  11.110  1.00 14.41 ? 66   TRP A CD1 1 
ATOM   305  C  CD2 . TRP A 1 66   ? 13.292 46.688  9.518   1.00 13.89 ? 66   TRP A CD2 1 
ATOM   306  N  NE1 . TRP A 1 66   ? 13.021 45.003  10.991  1.00 15.67 ? 66   TRP A NE1 1 
ATOM   307  C  CE2 . TRP A 1 66   ? 13.855 45.481  10.005  1.00 13.28 ? 66   TRP A CE2 1 
ATOM   308  C  CE3 . TRP A 1 66   ? 13.968 47.375  8.483   1.00 14.49 ? 66   TRP A CE3 1 
ATOM   309  C  CZ2 . TRP A 1 66   ? 15.056 44.942  9.503   1.00 16.01 ? 66   TRP A CZ2 1 
ATOM   310  C  CZ3 . TRP A 1 66   ? 15.161 46.834  7.987   1.00 14.52 ? 66   TRP A CZ3 1 
ATOM   311  C  CH2 . TRP A 1 66   ? 15.703 45.643  8.512   1.00 14.54 ? 66   TRP A CH2 1 
ATOM   312  N  N   . ASN A 1 67   ? 10.745 48.512  13.091  1.00 15.59 ? 67   ASN A N   1 
ATOM   313  C  CA  . ASN A 1 67   ? 10.923 48.075  14.478  1.00 15.64 ? 67   ASN A CA  1 
ATOM   314  C  C   . ASN A 1 67   ? 11.507 46.670  14.505  1.00 15.77 ? 67   ASN A C   1 
ATOM   315  O  O   . ASN A 1 67   ? 10.806 45.677  14.242  1.00 15.93 ? 67   ASN A O   1 
ATOM   316  C  CB  . ASN A 1 67   ? 9.569  48.040  15.226  1.00 17.01 ? 67   ASN A CB  1 
ATOM   317  C  CG  . ASN A 1 67   ? 8.982  49.404  15.479  1.00 19.85 ? 67   ASN A CG  1 
ATOM   318  O  OD1 . ASN A 1 67   ? 9.672  50.432  15.554  1.00 21.92 ? 67   ASN A OD1 1 
ATOM   319  N  ND2 . ASN A 1 67   ? 7.658  49.420  15.666  1.00 23.62 ? 67   ASN A ND2 1 
ATOM   320  N  N   . ILE A 1 68   ? 12.791 46.570  14.821  1.00 14.86 ? 68   ILE A N   1 
ATOM   321  C  CA  . ILE A 1 68   ? 13.489 45.312  14.780  1.00 14.78 ? 68   ILE A CA  1 
ATOM   322  C  C   . ILE A 1 68   ? 13.038 44.444  15.954  1.00 15.73 ? 68   ILE A C   1 
ATOM   323  O  O   . ILE A 1 68   ? 12.979 44.896  17.095  1.00 16.11 ? 68   ILE A O   1 
ATOM   324  C  CB  . ILE A 1 68   ? 15.046 45.521  14.851  1.00 14.88 ? 68   ILE A CB  1 
ATOM   325  C  CG1 . ILE A 1 68   ? 15.560 46.390  13.683  1.00 14.42 ? 68   ILE A CG1 1 
ATOM   326  C  CG2 . ILE A 1 68   ? 15.767 44.182  14.896  1.00 16.02 ? 68   ILE A CG2 1 
ATOM   327  C  CD1 . ILE A 1 68   ? 17.028 46.903  13.879  1.00 13.28 ? 68   ILE A CD1 1 
ATOM   328  N  N   . LYS A 1 69   ? 12.789 43.183  15.628  1.00 17.25 ? 69   LYS A N   1 
ATOM   329  C  CA  . LYS A 1 69   ? 12.448 42.166  16.634  1.00 19.20 ? 69   LYS A CA  1 
ATOM   330  C  C   . LYS A 1 69   ? 13.497 41.076  16.628  1.00 18.57 ? 69   LYS A C   1 
ATOM   331  O  O   . LYS A 1 69   ? 14.050 40.764  15.589  1.00 18.27 ? 69   LYS A O   1 
ATOM   332  C  CB  . LYS A 1 69   ? 11.063 41.591  16.327  1.00 19.99 ? 69   LYS A CB  1 
ATOM   333  C  CG  . LYS A 1 69   ? 9.935  42.604  16.592  1.00 23.06 ? 69   LYS A CG  1 
ATOM   334  C  CD  . LYS A 1 69   ? 8.610  42.254  15.875  1.00 24.60 ? 69   LYS A CD  1 
ATOM   335  C  CE  . LYS A 1 69   ? 8.058  40.856  16.244  1.00 30.14 ? 69   LYS A CE  1 
ATOM   336  N  NZ  . LYS A 1 69   ? 6.924  40.426  15.359  1.00 30.15 ? 69   LYS A NZ  1 
ATOM   337  N  N   . TYR A 1 70   ? 13.791 40.508  17.796  1.00 18.52 ? 70   TYR A N   1 
ATOM   338  C  CA  . TYR A 1 70   ? 14.698 39.358  17.853  1.00 19.13 ? 70   TYR A CA  1 
ATOM   339  C  C   . TYR A 1 70   ? 14.125 38.300  18.775  1.00 20.92 ? 70   TYR A C   1 
ATOM   340  O  O   . TYR A 1 70   ? 13.343 38.620  19.669  1.00 20.98 ? 70   TYR A O   1 
ATOM   341  C  CB  . TYR A 1 70   ? 16.108 39.775  18.315  1.00 18.82 ? 70   TYR A CB  1 
ATOM   342  C  CG  . TYR A 1 70   ? 16.164 40.412  19.676  1.00 17.84 ? 70   TYR A CG  1 
ATOM   343  C  CD1 . TYR A 1 70   ? 15.929 41.766  19.835  1.00 17.70 ? 70   TYR A CD1 1 
ATOM   344  C  CD2 . TYR A 1 70   ? 16.434 39.650  20.820  1.00 18.80 ? 70   TYR A CD2 1 
ATOM   345  C  CE1 . TYR A 1 70   ? 15.967 42.370  21.074  1.00 19.09 ? 70   TYR A CE1 1 
ATOM   346  C  CE2 . TYR A 1 70   ? 16.483 40.240  22.072  1.00 20.06 ? 70   TYR A CE2 1 
ATOM   347  C  CZ  . TYR A 1 70   ? 16.247 41.600  22.198  1.00 19.23 ? 70   TYR A CZ  1 
ATOM   348  O  OH  . TYR A 1 70   ? 16.273 42.212  23.442  1.00 20.57 ? 70   TYR A OH  1 
ATOM   349  N  N   . ASP A 1 71   ? 14.528 37.060  18.535  1.00 22.82 ? 71   ASP A N   1 
ATOM   350  C  CA  . ASP A 1 71   ? 14.173 35.940  19.398  1.00 24.38 ? 71   ASP A CA  1 
ATOM   351  C  C   . ASP A 1 71   ? 15.161 35.914  20.555  1.00 24.99 ? 71   ASP A C   1 
ATOM   352  O  O   . ASP A 1 71   ? 16.346 35.634  20.343  1.00 24.26 ? 71   ASP A O   1 
ATOM   353  C  CB  . ASP A 1 71   ? 14.243 34.640  18.606  1.00 25.30 ? 71   ASP A CB  1 
ATOM   354  C  CG  . ASP A 1 71   ? 13.815 33.417  19.429  1.00 27.75 ? 71   ASP A CG  1 
ATOM   355  O  OD1 . ASP A 1 71   ? 13.656 33.514  20.667  1.00 29.97 ? 71   ASP A OD1 1 
ATOM   356  O  OD2 . ASP A 1 71   ? 13.632 32.309  18.901  1.00 31.74 ? 71   ASP A OD2 1 
ATOM   357  N  N   . PRO A 1 72   ? 14.699 36.190  21.781  1.00 25.83 ? 72   PRO A N   1 
ATOM   358  C  CA  . PRO A 1 72   ? 15.617 36.216  22.927  1.00 26.14 ? 72   PRO A CA  1 
ATOM   359  C  C   . PRO A 1 72   ? 16.359 34.885  23.118  1.00 26.07 ? 72   PRO A C   1 
ATOM   360  O  O   . PRO A 1 72   ? 17.441 34.878  23.704  1.00 27.16 ? 72   PRO A O   1 
ATOM   361  C  CB  . PRO A 1 72   ? 14.706 36.545  24.118  1.00 26.33 ? 72   PRO A CB  1 
ATOM   362  C  CG  . PRO A 1 72   ? 13.339 36.202  23.656  1.00 27.41 ? 72   PRO A CG  1 
ATOM   363  C  CD  . PRO A 1 72   ? 13.312 36.486  22.187  1.00 26.12 ? 72   PRO A CD  1 
ATOM   364  N  N   . LEU A 1 73   ? 15.814 33.795  22.580  1.00 26.30 ? 73   LEU A N   1 
ATOM   365  C  CA  . LEU A 1 73   ? 16.436 32.475  22.687  1.00 26.46 ? 73   LEU A CA  1 
ATOM   366  C  C   . LEU A 1 73   ? 17.510 32.183  21.629  1.00 25.73 ? 73   LEU A C   1 
ATOM   367  O  O   . LEU A 1 73   ? 18.131 31.113  21.640  1.00 25.83 ? 73   LEU A O   1 
ATOM   368  C  CB  . LEU A 1 73   ? 15.361 31.384  22.644  1.00 27.08 ? 73   LEU A CB  1 
ATOM   369  C  CG  . LEU A 1 73   ? 14.297 31.406  23.739  1.00 28.88 ? 73   LEU A CG  1 
ATOM   370  C  CD1 . LEU A 1 73   ? 13.308 30.262  23.501  1.00 30.95 ? 73   LEU A CD1 1 
ATOM   371  C  CD2 . LEU A 1 73   ? 14.953 31.309  25.121  1.00 30.76 ? 73   LEU A CD2 1 
ATOM   372  N  N   . LYS A 1 74   ? 17.742 33.135  20.721  1.00 24.79 ? 74   LYS A N   1 
ATOM   373  C  CA  . LYS A 1 74   ? 18.821 33.004  19.736  1.00 23.94 ? 74   LYS A CA  1 
ATOM   374  C  C   . LYS A 1 74   ? 20.202 32.849  20.367  1.00 23.11 ? 74   LYS A C   1 
ATOM   375  O  O   . LYS A 1 74   ? 21.055 32.122  19.846  1.00 23.54 ? 74   LYS A O   1 
ATOM   376  C  CB  . LYS A 1 74   ? 18.843 34.231  18.826  1.00 23.97 ? 74   LYS A CB  1 
ATOM   377  C  CG  . LYS A 1 74   ? 19.885 34.163  17.727  1.00 25.02 ? 74   LYS A CG  1 
ATOM   378  C  CD  . LYS A 1 74   ? 19.683 35.347  16.789  1.00 26.74 ? 74   LYS A CD  1 
ATOM   379  C  CE  . LYS A 1 74   ? 20.437 35.183  15.492  1.00 29.50 ? 74   LYS A CE  1 
ATOM   380  N  NZ  . LYS A 1 74   ? 19.983 36.250  14.544  1.00 31.20 ? 74   LYS A NZ  1 
ATOM   381  N  N   A TYR A 1 75   ? 20.460 33.584  21.449  0.50 23.37 ? 75   TYR A N   1 
ATOM   382  N  N   B TYR A 1 75   ? 20.392 33.540  21.485  0.50 22.87 ? 75   TYR A N   1 
ATOM   383  C  CA  A TYR A 1 75   ? 21.748 33.485  22.149  0.50 22.69 ? 75   TYR A CA  1 
ATOM   384  C  CA  B TYR A 1 75   ? 21.625 33.461  22.247  0.50 21.85 ? 75   TYR A CA  1 
ATOM   385  C  C   A TYR A 1 75   ? 21.578 32.783  23.502  0.50 23.11 ? 75   TYR A C   1 
ATOM   386  C  C   B TYR A 1 75   ? 21.431 32.536  23.425  0.50 22.45 ? 75   TYR A C   1 
ATOM   387  O  O   A TYR A 1 75   ? 20.613 33.057  24.221  0.50 23.13 ? 75   TYR A O   1 
ATOM   388  O  O   B TYR A 1 75   ? 20.324 32.395  23.946  0.50 22.55 ? 75   TYR A O   1 
ATOM   389  C  CB  A TYR A 1 75   ? 22.442 34.863  22.276  0.50 22.44 ? 75   TYR A CB  1 
ATOM   390  C  CB  B TYR A 1 75   ? 22.065 34.857  22.693  0.50 20.69 ? 75   TYR A CB  1 
ATOM   391  C  CG  A TYR A 1 75   ? 22.750 35.489  20.921  0.50 20.77 ? 75   TYR A CG  1 
ATOM   392  C  CG  B TYR A 1 75   ? 22.103 35.769  21.507  0.50 18.54 ? 75   TYR A CG  1 
ATOM   393  C  CD1 A TYR A 1 75   ? 23.792 35.007  20.133  0.50 20.15 ? 75   TYR A CD1 1 
ATOM   394  C  CD1 B TYR A 1 75   ? 23.121 35.666  20.569  0.50 15.87 ? 75   TYR A CD1 1 
ATOM   395  C  CD2 A TYR A 1 75   ? 21.975 36.538  20.410  0.50 20.64 ? 75   TYR A CD2 1 
ATOM   396  C  CD2 B TYR A 1 75   ? 21.075 36.667  21.270  0.50 17.88 ? 75   TYR A CD2 1 
ATOM   397  C  CE1 A TYR A 1 75   ? 24.060 35.545  18.873  0.50 20.96 ? 75   TYR A CE1 1 
ATOM   398  C  CE1 B TYR A 1 75   ? 23.132 36.478  19.434  0.50 16.33 ? 75   TYR A CE1 1 
ATOM   399  C  CE2 A TYR A 1 75   ? 22.244 37.092  19.148  0.50 20.32 ? 75   TYR A CE2 1 
ATOM   400  C  CE2 B TYR A 1 75   ? 21.077 37.486  20.142  0.50 16.13 ? 75   TYR A CE2 1 
ATOM   401  C  CZ  A TYR A 1 75   ? 23.288 36.580  18.386  0.50 20.20 ? 75   TYR A CZ  1 
ATOM   402  C  CZ  B TYR A 1 75   ? 22.107 37.390  19.237  0.50 16.49 ? 75   TYR A CZ  1 
ATOM   403  O  OH  A TYR A 1 75   ? 23.570 37.108  17.137  0.50 22.34 ? 75   TYR A OH  1 
ATOM   404  O  OH  B TYR A 1 75   ? 22.099 38.193  18.133  0.50 17.36 ? 75   TYR A OH  1 
ATOM   405  N  N   . ASN A 1 76   ? 22.515 31.878  23.807  1.00 22.88 ? 76   ASN A N   1 
ATOM   406  C  CA  . ASN A 1 76   ? 22.515 31.023  25.010  1.00 24.08 ? 76   ASN A CA  1 
ATOM   407  C  C   . ASN A 1 76   ? 23.967 30.768  25.438  1.00 25.01 ? 76   ASN A C   1 
ATOM   408  O  O   . ASN A 1 76   ? 24.902 31.290  24.822  1.00 24.69 ? 76   ASN A O   1 
ATOM   409  C  CB  . ASN A 1 76   ? 21.784 29.692  24.734  1.00 24.63 ? 76   ASN A CB  1 
ATOM   410  C  CG  . ASN A 1 76   ? 22.359 28.951  23.552  1.00 24.52 ? 76   ASN A CG  1 
ATOM   411  O  OD1 . ASN A 1 76   ? 23.550 28.676  23.500  1.00 27.05 ? 76   ASN A OD1 1 
ATOM   412  N  ND2 . ASN A 1 76   ? 21.505 28.622  22.590  1.00 30.40 ? 76   ASN A ND2 1 
ATOM   413  N  N   . ALA A 1 77   ? 24.176 29.956  26.480  1.00 26.29 ? 77   ALA A N   1 
ATOM   414  C  CA  . ALA A 1 77   ? 25.530 29.706  26.987  1.00 27.32 ? 77   ALA A CA  1 
ATOM   415  C  C   . ALA A 1 77   ? 26.492 29.211  25.907  1.00 27.69 ? 77   ALA A C   1 
ATOM   416  O  O   . ALA A 1 77   ? 27.691 29.490  25.960  1.00 28.54 ? 77   ALA A O   1 
ATOM   417  C  CB  . ALA A 1 77   ? 25.490 28.715  28.152  1.00 27.70 ? 77   ALA A CB  1 
ATOM   418  N  N   . HIS A 1 78   ? 25.965 28.499  24.917  1.00 28.44 ? 78   HIS A N   1 
ATOM   419  C  CA  . HIS A 1 78   ? 26.817 27.879  23.896  1.00 29.09 ? 78   HIS A CA  1 
ATOM   420  C  C   . HIS A 1 78   ? 26.971 28.738  22.654  1.00 28.14 ? 78   HIS A C   1 
ATOM   421  O  O   . HIS A 1 78   ? 27.730 28.401  21.738  1.00 29.01 ? 78   HIS A O   1 
ATOM   422  C  CB  . HIS A 1 78   ? 26.286 26.483  23.536  1.00 29.92 ? 78   HIS A CB  1 
ATOM   423  C  CG  . HIS A 1 78   ? 25.942 25.654  24.735  1.00 33.35 ? 78   HIS A CG  1 
ATOM   424  N  ND1 . HIS A 1 78   ? 26.875 25.307  25.691  1.00 37.12 ? 78   HIS A ND1 1 
ATOM   425  C  CD2 . HIS A 1 78   ? 24.763 25.135  25.151  1.00 36.47 ? 78   HIS A CD2 1 
ATOM   426  C  CE1 . HIS A 1 78   ? 26.288 24.589  26.633  1.00 37.70 ? 78   HIS A CE1 1 
ATOM   427  N  NE2 . HIS A 1 78   ? 25.005 24.475  26.333  1.00 39.03 ? 78   HIS A NE2 1 
ATOM   428  N  N   . HIS A 1 79   ? 26.247 29.847  22.628  1.00 26.26 ? 79   HIS A N   1 
ATOM   429  C  CA  . HIS A 1 79   ? 26.235 30.721  21.468  1.00 23.55 ? 79   HIS A CA  1 
ATOM   430  C  C   . HIS A 1 79   ? 25.947 32.140  21.943  1.00 20.33 ? 79   HIS A C   1 
ATOM   431  O  O   . HIS A 1 79   ? 24.800 32.578  21.981  1.00 20.22 ? 79   HIS A O   1 
ATOM   432  C  CB  . HIS A 1 79   ? 25.164 30.262  20.484  1.00 24.11 ? 79   HIS A CB  1 
ATOM   433  C  CG  . HIS A 1 79   ? 25.144 31.046  19.207  1.00 25.42 ? 79   HIS A CG  1 
ATOM   434  N  ND1 . HIS A 1 79   ? 26.129 30.926  18.247  1.00 28.36 ? 79   HIS A ND1 1 
ATOM   435  C  CD2 . HIS A 1 79   ? 24.255 31.946  18.726  1.00 26.79 ? 79   HIS A CD2 1 
ATOM   436  C  CE1 . HIS A 1 79   ? 25.853 31.734  17.237  1.00 26.54 ? 79   HIS A CE1 1 
ATOM   437  N  NE2 . HIS A 1 79   ? 24.723 32.366  17.503  1.00 28.40 ? 79   HIS A NE2 1 
ATOM   438  N  N   . LYS A 1 80   ? 27.006 32.820  22.355  1.00 19.08 ? 80   LYS A N   1 
ATOM   439  C  CA  . LYS A 1 80   ? 26.867 34.151  22.908  1.00 17.51 ? 80   LYS A CA  1 
ATOM   440  C  C   . LYS A 1 80   ? 27.056 35.214  21.823  1.00 15.79 ? 80   LYS A C   1 
ATOM   441  O  O   . LYS A 1 80   ? 27.644 34.949  20.756  1.00 16.83 ? 80   LYS A O   1 
ATOM   442  C  CB  . LYS A 1 80   ? 27.892 34.362  24.010  1.00 17.71 ? 80   LYS A CB  1 
ATOM   443  C  CG  . LYS A 1 80   ? 27.778 33.308  25.118  1.00 20.26 ? 80   LYS A CG  1 
ATOM   444  C  CD  . LYS A 1 80   ? 28.990 33.353  25.979  1.00 25.24 ? 80   LYS A CD  1 
ATOM   445  C  CE  . LYS A 1 80   ? 29.036 34.610  26.798  1.00 25.35 ? 80   LYS A CE  1 
ATOM   446  N  NZ  . LYS A 1 80   ? 30.008 34.411  27.933  1.00 29.28 ? 80   LYS A NZ  1 
ATOM   447  N  N   . LEU A 1 81   ? 26.553 36.401  22.097  1.00 13.55 ? 81   LEU A N   1 
ATOM   448  C  CA  . LEU A 1 81   ? 26.824 37.547  21.223  1.00 12.01 ? 81   LEU A CA  1 
ATOM   449  C  C   . LEU A 1 81   ? 28.122 38.200  21.683  1.00 12.86 ? 81   LEU A C   1 
ATOM   450  O  O   . LEU A 1 81   ? 28.228 38.604  22.844  1.00 12.45 ? 81   LEU A O   1 
ATOM   451  C  CB  . LEU A 1 81   ? 25.662 38.511  21.326  1.00 13.05 ? 81   LEU A CB  1 
ATOM   452  C  CG  . LEU A 1 81   ? 25.754 39.770  20.440  1.00 12.72 ? 81   LEU A CG  1 
ATOM   453  C  CD1 . LEU A 1 81   ? 25.743 39.386  18.945  1.00 13.39 ? 81   LEU A CD1 1 
ATOM   454  C  CD2 . LEU A 1 81   ? 24.643 40.747  20.760  1.00 15.89 ? 81   LEU A CD2 1 
ATOM   455  N  N   . LYS A 1 82   ? 29.103 38.279  20.780  1.00 11.24 ? 82   LYS A N   1 
ATOM   456  C  CA  . LYS A 1 82   ? 30.385 38.870  21.100  1.00 11.20 ? 82   LYS A CA  1 
ATOM   457  C  C   . LYS A 1 82   ? 30.323 40.291  20.583  1.00 11.26 ? 82   LYS A C   1 
ATOM   458  O  O   . LYS A 1 82   ? 30.082 40.501  19.384  1.00 12.73 ? 82   LYS A O   1 
ATOM   459  C  CB  . LYS A 1 82   ? 31.516 38.110  20.404  1.00 12.47 ? 82   LYS A CB  1 
ATOM   460  C  CG  . LYS A 1 82   ? 31.625 36.636  20.783  1.00 19.00 ? 82   LYS A CG  1 
ATOM   461  C  CD  . LYS A 1 82   ? 31.471 36.350  22.263  1.00 28.48 ? 82   LYS A CD  1 
ATOM   462  C  CE  . LYS A 1 82   ? 31.524 34.836  22.518  1.00 30.90 ? 82   LYS A CE  1 
ATOM   463  N  NZ  . LYS A 1 82   ? 30.838 34.016  21.451  1.00 33.09 ? 82   LYS A NZ  1 
ATOM   464  N  N   . VAL A 1 83   ? 30.505 41.271  21.464  1.00 9.80  ? 83   VAL A N   1 
ATOM   465  C  CA  . VAL A 1 83   ? 30.339 42.683  21.118  1.00 10.14 ? 83   VAL A CA  1 
ATOM   466  C  C   . VAL A 1 83   ? 31.684 43.395  21.254  1.00 10.44 ? 83   VAL A C   1 
ATOM   467  O  O   . VAL A 1 83   ? 32.328 43.345  22.326  1.00 10.78 ? 83   VAL A O   1 
ATOM   468  C  CB  . VAL A 1 83   ? 29.308 43.324  22.029  1.00 9.29  ? 83   VAL A CB  1 
ATOM   469  C  CG1 . VAL A 1 83   ? 29.123 44.821  21.702  1.00 10.82 ? 83   VAL A CG1 1 
ATOM   470  C  CG2 . VAL A 1 83   ? 27.951 42.604  21.915  1.00 10.78 ? 83   VAL A CG2 1 
ATOM   471  N  N   . PHE A 1 84   ? 32.117 44.077  20.180  1.00 9.87  ? 84   PHE A N   1 
ATOM   472  C  CA  . PHE A 1 84   ? 33.340 44.895  20.185  1.00 9.98  ? 84   PHE A CA  1 
ATOM   473  C  C   . PHE A 1 84   ? 32.956 46.356  20.124  1.00 10.48 ? 84   PHE A C   1 
ATOM   474  O  O   . PHE A 1 84   ? 32.405 46.831  19.116  1.00 9.74  ? 84   PHE A O   1 
ATOM   475  C  CB  . PHE A 1 84   ? 34.205 44.514  18.984  1.00 11.01 ? 84   PHE A CB  1 
ATOM   476  C  CG  . PHE A 1 84   ? 34.820 43.159  19.122  1.00 11.26 ? 84   PHE A CG  1 
ATOM   477  C  CD1 . PHE A 1 84   ? 35.905 42.974  19.975  1.00 15.08 ? 84   PHE A CD1 1 
ATOM   478  C  CD2 . PHE A 1 84   ? 34.319 42.065  18.437  1.00 13.46 ? 84   PHE A CD2 1 
ATOM   479  C  CE1 . PHE A 1 84   ? 36.501 41.713  20.147  1.00 15.28 ? 84   PHE A CE1 1 
ATOM   480  C  CE2 . PHE A 1 84   ? 34.904 40.791  18.602  1.00 16.85 ? 84   PHE A CE2 1 
ATOM   481  C  CZ  . PHE A 1 84   ? 36.011 40.628  19.430  1.00 16.32 ? 84   PHE A CZ  1 
ATOM   482  N  N   . VAL A 1 85   ? 33.231 47.066  21.210  1.00 9.15  ? 85   VAL A N   1 
ATOM   483  C  CA  . VAL A 1 85   ? 33.005 48.486  21.277  1.00 9.21  ? 85   VAL A CA  1 
ATOM   484  C  C   . VAL A 1 85   ? 34.311 49.149  20.888  1.00 9.11  ? 85   VAL A C   1 
ATOM   485  O  O   . VAL A 1 85   ? 35.327 48.957  21.541  1.00 9.17  ? 85   VAL A O   1 
ATOM   486  C  CB  . VAL A 1 85   ? 32.569 48.917  22.699  1.00 9.31  ? 85   VAL A CB  1 
ATOM   487  C  CG1 . VAL A 1 85   ? 32.411 50.446  22.824  1.00 11.40 ? 85   VAL A CG1 1 
ATOM   488  C  CG2 . VAL A 1 85   ? 31.264 48.220  23.066  1.00 10.99 ? 85   VAL A CG2 1 
ATOM   489  N  N   . VAL A 1 86   ? 34.269 49.912  19.783  1.00 8.52  ? 86   VAL A N   1 
ATOM   490  C  CA  . VAL A 1 86   ? 35.497 50.411  19.160  1.00 8.69  ? 86   VAL A CA  1 
ATOM   491  C  C   . VAL A 1 86   ? 35.588 51.939  19.256  1.00 8.09  ? 86   VAL A C   1 
ATOM   492  O  O   . VAL A 1 86   ? 34.933 52.657  18.494  1.00 8.09  ? 86   VAL A O   1 
ATOM   493  C  CB  . VAL A 1 86   ? 35.543 49.978  17.690  1.00 8.21  ? 86   VAL A CB  1 
ATOM   494  C  CG1 . VAL A 1 86   ? 36.846 50.467  17.032  1.00 9.88  ? 86   VAL A CG1 1 
ATOM   495  C  CG2 . VAL A 1 86   ? 35.514 48.439  17.595  1.00 10.32 ? 86   VAL A CG2 1 
ATOM   496  N  N   . PRO A 1 87   ? 36.338 52.455  20.231  1.00 7.87  ? 87   PRO A N   1 
ATOM   497  C  CA  . PRO A 1 87   ? 36.437 53.919  20.397  1.00 8.01  ? 87   PRO A CA  1 
ATOM   498  C  C   . PRO A 1 87   ? 37.180 54.552  19.217  1.00 7.57  ? 87   PRO A C   1 
ATOM   499  O  O   . PRO A 1 87   ? 38.184 54.005  18.725  1.00 8.03  ? 87   PRO A O   1 
ATOM   500  C  CB  . PRO A 1 87   ? 37.268 54.089  21.701  1.00 8.04  ? 87   PRO A CB  1 
ATOM   501  C  CG  . PRO A 1 87   ? 37.047 52.737  22.410  1.00 10.49 ? 87   PRO A CG  1 
ATOM   502  C  CD  . PRO A 1 87   ? 37.060 51.723  21.297  1.00 9.61  ? 87   PRO A CD  1 
ATOM   503  N  N   . HIS A 1 88   ? 36.673 55.704  18.806  1.00 7.21  ? 88   HIS A N   1 
ATOM   504  C  CA  . HIS A 1 88   ? 37.254 56.401  17.637  1.00 7.90  ? 88   HIS A CA  1 
ATOM   505  C  C   . HIS A 1 88   ? 36.992 57.891  17.738  1.00 8.37  ? 88   HIS A C   1 
ATOM   506  O  O   . HIS A 1 88   ? 36.181 58.337  18.537  1.00 8.21  ? 88   HIS A O   1 
ATOM   507  C  CB  . HIS A 1 88   ? 36.678 55.802  16.332  1.00 8.02  ? 88   HIS A CB  1 
ATOM   508  C  CG  . HIS A 1 88   ? 35.246 56.126  16.073  1.00 7.65  ? 88   HIS A CG  1 
ATOM   509  N  ND1 . HIS A 1 88   ? 34.851 57.180  15.270  1.00 7.81  ? 88   HIS A ND1 1 
ATOM   510  C  CD2 . HIS A 1 88   ? 34.114 55.532  16.516  1.00 7.54  ? 88   HIS A CD2 1 
ATOM   511  C  CE1 . HIS A 1 88   ? 33.530 57.202  15.220  1.00 8.81  ? 88   HIS A CE1 1 
ATOM   512  N  NE2 . HIS A 1 88   ? 33.061 56.209  15.969  1.00 9.86  ? 88   HIS A NE2 1 
ATOM   513  N  N   . SER A 1 89   ? 37.702 58.661  16.914  1.00 8.05  ? 89   SER A N   1 
ATOM   514  C  CA  . SER A 1 89   ? 37.601 60.095  16.910  1.00 7.98  ? 89   SER A CA  1 
ATOM   515  C  C   . SER A 1 89   ? 37.772 60.575  15.446  1.00 7.52  ? 89   SER A C   1 
ATOM   516  O  O   . SER A 1 89   ? 38.850 60.364  14.875  1.00 8.38  ? 89   SER A O   1 
ATOM   517  C  CB  . SER A 1 89   ? 38.720 60.673  17.768  1.00 9.04  ? 89   SER A CB  1 
ATOM   518  O  OG  . SER A 1 89   ? 38.710 62.074  17.717  1.00 8.59  ? 89   SER A OG  1 
ATOM   519  N  N   . HIS A 1 90   ? 36.733 61.161  14.875  1.00 7.85  ? 90   HIS A N   1 
ATOM   520  C  CA  . HIS A 1 90   ? 36.816 61.584  13.480  1.00 7.73  ? 90   HIS A CA  1 
ATOM   521  C  C   . HIS A 1 90   ? 37.502 62.951  13.406  1.00 7.23  ? 90   HIS A C   1 
ATOM   522  O  O   . HIS A 1 90   ? 36.978 63.925  13.892  1.00 8.30  ? 90   HIS A O   1 
ATOM   523  C  CB  . HIS A 1 90   ? 35.422 61.615  12.874  1.00 8.37  ? 90   HIS A CB  1 
ATOM   524  C  CG  . HIS A 1 90   ? 35.429 61.976  11.421  1.00 7.28  ? 90   HIS A CG  1 
ATOM   525  N  ND1 . HIS A 1 90   ? 35.900 61.113  10.448  1.00 7.72  ? 90   HIS A ND1 1 
ATOM   526  C  CD2 . HIS A 1 90   ? 35.007 63.088  10.780  1.00 9.35  ? 90   HIS A CD2 1 
ATOM   527  C  CE1 . HIS A 1 90   ? 35.770 61.709  9.264   1.00 7.76  ? 90   HIS A CE1 1 
ATOM   528  N  NE2 . HIS A 1 90   ? 35.236 62.897  9.438   1.00 7.74  ? 90   HIS A NE2 1 
ATOM   529  N  N   . ASN A 1 91   ? 38.677 62.986  12.780  1.00 8.18  ? 91   ASN A N   1 
ATOM   530  C  CA  . ASN A 1 91   ? 39.459 64.205  12.711  1.00 8.38  ? 91   ASN A CA  1 
ATOM   531  C  C   . ASN A 1 91   ? 39.605 64.667  11.279  1.00 9.42  ? 91   ASN A C   1 
ATOM   532  O  O   . ASN A 1 91   ? 40.402 64.110  10.513  1.00 12.80 ? 91   ASN A O   1 
ATOM   533  C  CB  . ASN A 1 91   ? 40.856 63.967  13.299  1.00 8.78  ? 91   ASN A CB  1 
ATOM   534  C  CG  . ASN A 1 91   ? 40.855 63.926  14.824  1.00 9.38  ? 91   ASN A CG  1 
ATOM   535  O  OD1 . ASN A 1 91   ? 41.415 64.809  15.489  1.00 9.61  ? 91   ASN A OD1 1 
ATOM   536  N  ND2 . ASN A 1 91   ? 40.214 62.915  15.384  1.00 9.10  ? 91   ASN A ND2 1 
ATOM   537  N  N   . ASP A 1 92   ? 38.895 65.713  10.932  1.00 7.58  ? 92   ASP A N   1 
ATOM   538  C  CA  . ASP A 1 92   ? 38.953 66.259  9.573   1.00 7.59  ? 92   ASP A CA  1 
ATOM   539  C  C   . ASP A 1 92   ? 40.203 67.080  9.370   1.00 7.66  ? 92   ASP A C   1 
ATOM   540  O  O   . ASP A 1 92   ? 40.399 68.058  10.109  1.00 8.05  ? 92   ASP A O   1 
ATOM   541  C  CB  . ASP A 1 92   ? 37.756 67.154  9.378   1.00 7.87  ? 92   ASP A CB  1 
ATOM   542  C  CG  . ASP A 1 92   ? 36.492 66.355  9.233   1.00 8.71  ? 92   ASP A CG  1 
ATOM   543  O  OD1 . ASP A 1 92   ? 36.510 65.446  8.398   1.00 8.61  ? 92   ASP A OD1 1 
ATOM   544  O  OD2 . ASP A 1 92   ? 35.485 66.546  9.951   1.00 11.91 ? 92   ASP A OD2 1 
ATOM   545  N  N   . PRO A 1 93   ? 41.052 66.705  8.392   1.00 7.72  ? 93   PRO A N   1 
ATOM   546  C  CA  . PRO A 1 93   ? 42.259 67.504  8.047   1.00 7.83  ? 93   PRO A CA  1 
ATOM   547  C  C   . PRO A 1 93   ? 41.877 68.784  7.272   1.00 8.50  ? 93   PRO A C   1 
ATOM   548  O  O   . PRO A 1 93   ? 42.207 68.958  6.075   1.00 10.22 ? 93   PRO A O   1 
ATOM   549  C  CB  . PRO A 1 93   ? 43.110 66.517  7.212   1.00 8.67  ? 93   PRO A CB  1 
ATOM   550  C  CG  . PRO A 1 93   ? 42.504 65.153  7.460   1.00 11.24 ? 93   PRO A CG  1 
ATOM   551  C  CD  . PRO A 1 93   ? 41.027 65.428  7.634   1.00 7.90  ? 93   PRO A CD  1 
ATOM   552  N  N   . GLY A 1 94   ? 41.164 69.675  7.960   1.00 8.11  ? 94   GLY A N   1 
ATOM   553  C  CA  . GLY A 1 94   ? 40.566 70.878  7.369   1.00 8.03  ? 94   GLY A CA  1 
ATOM   554  C  C   . GLY A 1 94   ? 39.087 70.642  7.126   1.00 8.96  ? 94   GLY A C   1 
ATOM   555  O  O   . GLY A 1 94   ? 38.681 69.577  6.617   1.00 9.30  ? 94   GLY A O   1 
ATOM   556  N  N   . TRP A 1 95   ? 38.286 71.626  7.522   1.00 8.34  ? 95   TRP A N   1 
ATOM   557  C  CA  . TRP A 1 95   ? 36.849 71.665  7.210   1.00 8.44  ? 95   TRP A CA  1 
ATOM   558  C  C   . TRP A 1 95   ? 36.323 73.044  7.630   1.00 8.48  ? 95   TRP A C   1 
ATOM   559  O  O   . TRP A 1 95   ? 36.279 73.962  6.841   1.00 9.81  ? 95   TRP A O   1 
ATOM   560  C  CB  . TRP A 1 95   ? 36.048 70.510  7.865   1.00 8.49  ? 95   TRP A CB  1 
ATOM   561  C  CG  . TRP A 1 95   ? 34.585 70.599  7.528   1.00 8.85  ? 95   TRP A CG  1 
ATOM   562  C  CD1 . TRP A 1 95   ? 34.031 70.992  6.356   1.00 8.77  ? 95   TRP A CD1 1 
ATOM   563  C  CD2 . TRP A 1 95   ? 33.503 70.285  8.397   1.00 9.31  ? 95   TRP A CD2 1 
ATOM   564  N  NE1 . TRP A 1 95   ? 32.659 70.970  6.436   1.00 8.66  ? 95   TRP A NE1 1 
ATOM   565  C  CE2 . TRP A 1 95   ? 32.315 70.525  7.684   1.00 8.88  ? 95   TRP A CE2 1 
ATOM   566  C  CE3 . TRP A 1 95   ? 33.425 69.830  9.731   1.00 10.76 ? 95   TRP A CE3 1 
ATOM   567  C  CZ2 . TRP A 1 95   ? 31.039 70.331  8.258   1.00 9.98  ? 95   TRP A CZ2 1 
ATOM   568  C  CZ3 . TRP A 1 95   ? 32.152 69.634  10.297  1.00 12.07 ? 95   TRP A CZ3 1 
ATOM   569  C  CH2 . TRP A 1 95   ? 30.991 69.875  9.562   1.00 12.61 ? 95   TRP A CH2 1 
ATOM   570  N  N   . ILE A 1 96   ? 35.996 73.177  8.922   1.00 9.11  ? 96   ILE A N   1 
ATOM   571  C  CA  . ILE A 1 96   ? 35.582 74.460  9.522   1.00 11.48 ? 96   ILE A CA  1 
ATOM   572  C  C   . ILE A 1 96   ? 36.784 75.262  10.003  1.00 11.03 ? 96   ILE A C   1 
ATOM   573  O  O   . ILE A 1 96   ? 36.704 76.492  10.147  1.00 12.87 ? 96   ILE A O   1 
ATOM   574  C  CB  . ILE A 1 96   ? 34.655 74.235  10.775  1.00 13.67 ? 96   ILE A CB  1 
ATOM   575  C  CG1 . ILE A 1 96   ? 33.424 73.420  10.441  1.00 17.01 ? 96   ILE A CG1 1 
ATOM   576  C  CG2 . ILE A 1 96   ? 34.284 75.563  11.469  1.00 16.15 ? 96   ILE A CG2 1 
ATOM   577  C  CD1 . ILE A 1 96   ? 32.820 73.839  9.161   1.00 15.77 ? 96   ILE A CD1 1 
ATOM   578  N  N   A GLN A 1 97   ? 37.877 74.581  10.289  0.50 9.71  ? 97   GLN A N   1 
ATOM   579  N  N   B GLN A 1 97   ? 37.872 74.560  10.280  0.50 9.71  ? 97   GLN A N   1 
ATOM   580  C  CA  A GLN A 1 97   ? 39.162 75.222  10.560  0.50 9.74  ? 97   GLN A CA  1 
ATOM   581  C  CA  B GLN A 1 97   ? 39.178 75.134  10.615  0.50 9.43  ? 97   GLN A CA  1 
ATOM   582  C  C   A GLN A 1 97   ? 40.181 74.609  9.615   0.50 9.14  ? 97   GLN A C   1 
ATOM   583  C  C   B GLN A 1 97   ? 40.198 74.572  9.640   0.50 9.09  ? 97   GLN A C   1 
ATOM   584  O  O   A GLN A 1 97   ? 39.910 73.594  8.969   0.50 8.70  ? 97   GLN A O   1 
ATOM   585  O  O   B GLN A 1 97   ? 39.945 73.550  8.998   0.50 8.51  ? 97   GLN A O   1 
ATOM   586  C  CB  A GLN A 1 97   ? 39.592 75.003  12.011  0.50 10.17 ? 97   GLN A CB  1 
ATOM   587  C  CB  B GLN A 1 97   ? 39.575 74.753  12.046  0.50 10.44 ? 97   GLN A CB  1 
ATOM   588  C  CG  A GLN A 1 97   ? 38.529 75.366  13.045  0.50 11.67 ? 97   GLN A CG  1 
ATOM   589  C  CG  B GLN A 1 97   ? 38.676 75.374  13.102  0.50 12.81 ? 97   GLN A CG  1 
ATOM   590  C  CD  A GLN A 1 97   ? 39.039 75.238  14.467  0.50 11.91 ? 97   GLN A CD  1 
ATOM   591  C  CD  B GLN A 1 97   ? 38.891 76.863  13.193  0.50 15.15 ? 97   GLN A CD  1 
ATOM   592  O  OE1 A GLN A 1 97   ? 40.154 75.660  14.786  0.50 15.88 ? 97   GLN A OE1 1 
ATOM   593  O  OE1 B GLN A 1 97   ? 39.766 77.324  13.929  0.50 18.09 ? 97   GLN A OE1 1 
ATOM   594  N  NE2 A GLN A 1 97   ? 38.229 74.652  15.324  0.50 13.08 ? 97   GLN A NE2 1 
ATOM   595  N  NE2 B GLN A 1 97   ? 38.089 77.623  12.464  0.50 16.87 ? 97   GLN A NE2 1 
ATOM   596  N  N   . THR A 1 98   ? 41.359 75.212  9.530   1.00 8.74  ? 98   THR A N   1 
ATOM   597  C  CA  . THR A 1 98   ? 42.421 74.639  8.710   1.00 8.62  ? 98   THR A CA  1 
ATOM   598  C  C   . THR A 1 98   ? 43.017 73.431  9.424   1.00 8.60  ? 98   THR A C   1 
ATOM   599  O  O   . THR A 1 98   ? 42.776 73.216  10.626  1.00 8.36  ? 98   THR A O   1 
ATOM   600  C  CB  . THR A 1 98   ? 43.529 75.618  8.444   1.00 8.56  ? 98   THR A CB  1 
ATOM   601  O  OG1 . THR A 1 98   ? 44.120 75.921  9.712   1.00 9.50  ? 98   THR A OG1 1 
ATOM   602  C  CG2 . THR A 1 98   ? 43.015 76.931  7.861   1.00 10.31 ? 98   THR A CG2 1 
ATOM   603  N  N   . PHE A 1 99   ? 43.782 72.633  8.684   1.00 8.21  ? 99   PHE A N   1 
ATOM   604  C  CA  . PHE A 1 99   ? 44.538 71.546  9.259   1.00 8.26  ? 99   PHE A CA  1 
ATOM   605  C  C   . PHE A 1 99   ? 45.320 71.995  10.491  1.00 8.27  ? 99   PHE A C   1 
ATOM   606  O  O   . PHE A 1 99   ? 45.234 71.377  11.562  1.00 8.89  ? 99   PHE A O   1 
ATOM   607  C  CB  . PHE A 1 99   ? 45.500 70.950  8.209   1.00 8.73  ? 99   PHE A CB  1 
ATOM   608  C  CG  . PHE A 1 99   ? 46.368 69.867  8.733   1.00 7.65  ? 99   PHE A CG  1 
ATOM   609  C  CD1 . PHE A 1 99   ? 47.602 70.154  9.326   1.00 9.31  ? 99   PHE A CD1 1 
ATOM   610  C  CD2 . PHE A 1 99   ? 45.976 68.534  8.625   1.00 9.14  ? 99   PHE A CD2 1 
ATOM   611  C  CE1 . PHE A 1 99   ? 48.401 69.140  9.830   1.00 10.77 ? 99   PHE A CE1 1 
ATOM   612  C  CE2 . PHE A 1 99   ? 46.759 67.515  9.098   1.00 9.32  ? 99   PHE A CE2 1 
ATOM   613  C  CZ  . PHE A 1 99   ? 47.989 67.801  9.695   1.00 9.32  ? 99   PHE A CZ  1 
ATOM   614  N  N   . GLU A 1 100  ? 46.094 73.067  10.354  1.00 8.70  ? 100  GLU A N   1 
ATOM   615  C  CA  . GLU A 1 100  ? 46.925 73.479  11.476  1.00 9.30  ? 100  GLU A CA  1 
ATOM   616  C  C   . GLU A 1 100  ? 46.099 74.027  12.645  1.00 8.71  ? 100  GLU A C   1 
ATOM   617  O  O   . GLU A 1 100  ? 46.445 73.771  13.806  1.00 9.43  ? 100  GLU A O   1 
ATOM   618  C  CB  . GLU A 1 100  ? 47.984 74.492  11.007  1.00 10.32 ? 100  GLU A CB  1 
ATOM   619  C  CG  . GLU A 1 100  ? 48.991 74.866  12.095  1.00 12.80 ? 100  GLU A CG  1 
ATOM   620  C  CD  . GLU A 1 100  ? 49.865 73.722  12.560  1.00 13.87 ? 100  GLU A CD  1 
ATOM   621  O  OE1 . GLU A 1 100  ? 50.018 72.686  11.872  1.00 13.99 ? 100  GLU A OE1 1 
ATOM   622  O  OE2 . GLU A 1 100  ? 50.479 73.867  13.656  1.00 14.33 ? 100  GLU A OE2 1 
ATOM   623  N  N   . GLU A 1 101  ? 45.014 74.733  12.366  1.00 8.81  ? 101  GLU A N   1 
ATOM   624  C  CA  . GLU A 1 101  ? 44.133 75.197  13.443  1.00 10.53 ? 101  GLU A CA  1 
ATOM   625  C  C   . GLU A 1 101  ? 43.526 74.059  14.216  1.00 9.99  ? 101  GLU A C   1 
ATOM   626  O  O   . GLU A 1 101  ? 43.541 74.060  15.459  1.00 9.64  ? 101  GLU A O   1 
ATOM   627  C  CB  . GLU A 1 101  ? 43.008 76.050  12.862  1.00 11.04 ? 101  GLU A CB  1 
ATOM   628  C  CG  . GLU A 1 101  ? 43.411 77.471  12.466  1.00 14.53 ? 101  GLU A CG  1 
ATOM   629  C  CD  . GLU A 1 101  ? 42.395 78.200  11.572  1.00 15.53 ? 101  GLU A CD  1 
ATOM   630  O  OE1 . GLU A 1 101  ? 41.392 77.644  11.034  1.00 13.19 ? 101  GLU A OE1 1 
ATOM   631  O  OE2 . GLU A 1 101  ? 42.593 79.434  11.402  1.00 22.76 ? 101  GLU A OE2 1 
ATOM   632  N  N   . TYR A 1 102  ? 42.990 73.063  13.531  1.00 8.41  ? 102  TYR A N   1 
ATOM   633  C  CA  . TYR A 1 102  ? 42.453 71.899  14.230  1.00 8.51  ? 102  TYR A CA  1 
ATOM   634  C  C   . TYR A 1 102  ? 43.550 71.182  15.019  1.00 8.87  ? 102  TYR A C   1 
ATOM   635  O  O   . TYR A 1 102  ? 43.301 70.693  16.106  1.00 9.26  ? 102  TYR A O   1 
ATOM   636  C  CB  . TYR A 1 102  ? 41.862 70.908  13.239  1.00 9.29  ? 102  TYR A CB  1 
ATOM   637  C  CG  . TYR A 1 102  ? 40.434 71.111  12.783  1.00 8.94  ? 102  TYR A CG  1 
ATOM   638  C  CD1 . TYR A 1 102  ? 39.386 71.305  13.674  1.00 9.31  ? 102  TYR A CD1 1 
ATOM   639  C  CD2 . TYR A 1 102  ? 40.127 71.000  11.443  1.00 8.16  ? 102  TYR A CD2 1 
ATOM   640  C  CE1 . TYR A 1 102  ? 38.069 71.436  13.213  1.00 9.90  ? 102  TYR A CE1 1 
ATOM   641  C  CE2 . TYR A 1 102  ? 38.840 71.105  10.985  1.00 9.16  ? 102  TYR A CE2 1 
ATOM   642  C  CZ  . TYR A 1 102  ? 37.813 71.314  11.863  1.00 9.47  ? 102  TYR A CZ  1 
ATOM   643  O  OH  . TYR A 1 102  ? 36.542 71.422  11.369  1.00 10.53 ? 102  TYR A OH  1 
ATOM   644  N  N   . TYR A 1 103  ? 44.742 71.082  14.443  1.00 9.07  ? 103  TYR A N   1 
ATOM   645  C  CA  . TYR A 1 103  ? 45.804 70.373  15.106  1.00 9.42  ? 103  TYR A CA  1 
ATOM   646  C  C   . TYR A 1 103  ? 46.110 71.055  16.451  1.00 10.42 ? 103  TYR A C   1 
ATOM   647  O  O   . TYR A 1 103  ? 46.216 70.411  17.456  1.00 10.13 ? 103  TYR A O   1 
ATOM   648  C  CB  . TYR A 1 103  ? 47.062 70.343  14.248  1.00 10.31 ? 103  TYR A CB  1 
ATOM   649  C  CG  . TYR A 1 103  ? 48.220 69.701  15.010  1.00 9.39  ? 103  TYR A CG  1 
ATOM   650  C  CD1 . TYR A 1 103  ? 48.246 68.342  15.290  1.00 9.21  ? 103  TYR A CD1 1 
ATOM   651  C  CD2 . TYR A 1 103  ? 49.252 70.470  15.514  1.00 10.33 ? 103  TYR A CD2 1 
ATOM   652  C  CE1 . TYR A 1 103  ? 49.249 67.785  16.003  1.00 10.39 ? 103  TYR A CE1 1 
ATOM   653  C  CE2 . TYR A 1 103  ? 50.292 69.904  16.244  1.00 11.02 ? 103  TYR A CE2 1 
ATOM   654  C  CZ  . TYR A 1 103  ? 50.271 68.577  16.513  1.00 10.09 ? 103  TYR A CZ  1 
ATOM   655  O  OH  . TYR A 1 103  ? 51.274 67.974  17.229  1.00 12.77 ? 103  TYR A OH  1 
ATOM   656  N  N   . GLN A 1 104  ? 46.205 72.380  16.400  1.00 10.17 ? 104  GLN A N   1 
ATOM   657  C  CA  . GLN A 1 104  ? 46.568 73.122  17.623  1.00 11.46 ? 104  GLN A CA  1 
ATOM   658  C  C   . GLN A 1 104  ? 45.445 73.089  18.634  1.00 12.21 ? 104  GLN A C   1 
ATOM   659  O  O   . GLN A 1 104  ? 45.699 73.029  19.863  1.00 13.83 ? 104  GLN A O   1 
ATOM   660  C  CB  . GLN A 1 104  ? 46.921 74.567  17.255  1.00 12.00 ? 104  GLN A CB  1 
ATOM   661  C  CG  . GLN A 1 104  ? 48.255 74.692  16.494  1.00 13.55 ? 104  GLN A CG  1 
ATOM   662  C  CD  . GLN A 1 104  ? 49.426 74.195  17.297  1.00 13.75 ? 104  GLN A CD  1 
ATOM   663  O  OE1 . GLN A 1 104  ? 49.414 74.291  18.530  1.00 14.94 ? 104  GLN A OE1 1 
ATOM   664  N  NE2 . GLN A 1 104  ? 50.432 73.666  16.635  1.00 14.17 ? 104  GLN A NE2 1 
ATOM   665  N  N   . HIS A 1 105  ? 44.210 73.204  18.165  1.00 12.02 ? 105  HIS A N   1 
ATOM   666  C  CA  . HIS A 1 105  ? 43.073 73.367  19.091  1.00 13.30 ? 105  HIS A CA  1 
ATOM   667  C  C   . HIS A 1 105  ? 42.522 72.046  19.584  1.00 13.87 ? 105  HIS A C   1 
ATOM   668  O  O   . HIS A 1 105  ? 41.999 71.972  20.705  1.00 15.03 ? 105  HIS A O   1 
ATOM   669  C  CB  . HIS A 1 105  ? 41.956 74.185  18.446  1.00 15.00 ? 105  HIS A CB  1 
ATOM   670  C  CG  . HIS A 1 105  ? 42.392 75.542  17.968  1.00 20.60 ? 105  HIS A CG  1 
ATOM   671  N  ND1 . HIS A 1 105  ? 41.808 76.170  16.888  1.00 26.21 ? 105  HIS A ND1 1 
ATOM   672  C  CD2 . HIS A 1 105  ? 43.362 76.377  18.410  1.00 25.34 ? 105  HIS A CD2 1 
ATOM   673  C  CE1 . HIS A 1 105  ? 42.397 77.338  16.692  1.00 26.60 ? 105  HIS A CE1 1 
ATOM   674  N  NE2 . HIS A 1 105  ? 43.342 77.488  17.602  1.00 26.98 ? 105  HIS A NE2 1 
ATOM   675  N  N   . ASP A 1 106  ? 42.641 70.996  18.771  1.00 12.70 ? 106  ASP A N   1 
ATOM   676  C  CA  . ASP A 1 106  ? 41.945 69.745  19.068  1.00 11.95 ? 106  ASP A CA  1 
ATOM   677  C  C   . ASP A 1 106  ? 42.824 68.516  18.952  1.00 10.22 ? 106  ASP A C   1 
ATOM   678  O  O   . ASP A 1 106  ? 43.036 67.782  19.932  1.00 10.23 ? 106  ASP A O   1 
ATOM   679  C  CB  . ASP A 1 106  ? 40.743 69.578  18.125  1.00 13.19 ? 106  ASP A CB  1 
ATOM   680  C  CG  . ASP A 1 106  ? 39.718 70.624  18.349  1.00 17.69 ? 106  ASP A CG  1 
ATOM   681  O  OD1 . ASP A 1 106  ? 38.963 70.475  19.337  1.00 20.20 ? 106  ASP A OD1 1 
ATOM   682  O  OD2 . ASP A 1 106  ? 39.629 71.635  17.604  1.00 20.98 ? 106  ASP A OD2 1 
ATOM   683  N  N   . THR A 1 107  ? 43.360 68.267  17.754  1.00 9.85  ? 107  THR A N   1 
ATOM   684  C  CA  . THR A 1 107  ? 43.940 66.943  17.480  1.00 8.99  ? 107  THR A CA  1 
ATOM   685  C  C   . THR A 1 107  ? 45.196 66.660  18.321  1.00 9.05  ? 107  THR A C   1 
ATOM   686  O  O   . THR A 1 107  ? 45.426 65.523  18.757  1.00 8.54  ? 107  THR A O   1 
ATOM   687  C  CB  . THR A 1 107  ? 44.232 66.801  15.983  1.00 9.00  ? 107  THR A CB  1 
ATOM   688  O  OG1 . THR A 1 107  ? 43.010 67.052  15.287  1.00 9.57  ? 107  THR A OG1 1 
ATOM   689  C  CG2 . THR A 1 107  ? 44.717 65.363  15.640  1.00 10.50 ? 107  THR A CG2 1 
ATOM   690  N  N   . LYS A 1 108  ? 46.012 67.688  18.570  1.00 9.02  ? 108  LYS A N   1 
ATOM   691  C  CA  . LYS A 1 108  ? 47.200 67.392  19.359  1.00 10.23 ? 108  LYS A CA  1 
ATOM   692  C  C   . LYS A 1 108  ? 46.839 66.953  20.776  1.00 9.38  ? 108  LYS A C   1 
ATOM   693  O  O   . LYS A 1 108  ? 47.540 66.130  21.334  1.00 11.02 ? 108  LYS A O   1 
ATOM   694  C  CB  . LYS A 1 108  ? 48.207 68.559  19.345  1.00 10.85 ? 108  LYS A CB  1 
ATOM   695  C  CG  . LYS A 1 108  ? 47.905 69.724  20.251  1.00 13.62 ? 108  LYS A CG  1 
ATOM   696  C  CD  . LYS A 1 108  ? 49.012 70.789  20.072  1.00 13.68 ? 108  LYS A CD  1 
ATOM   697  C  CE  . LYS A 1 108  ? 48.833 71.927  21.034  1.00 15.99 ? 108  LYS A CE  1 
ATOM   698  N  NZ  . LYS A 1 108  ? 49.990 72.904  20.901  1.00 18.06 ? 108  LYS A NZ  1 
ATOM   699  N  N   . HIS A 1 109  ? 45.745 67.494  21.286  1.00 9.60  ? 109  HIS A N   1 
ATOM   700  C  CA  . HIS A 1 109  ? 45.246 67.111  22.618  1.00 10.31 ? 109  HIS A CA  1 
ATOM   701  C  C   . HIS A 1 109  ? 44.647 65.724  22.613  1.00 10.03 ? 109  HIS A C   1 
ATOM   702  O  O   . HIS A 1 109  ? 44.885 64.918  23.526  1.00 10.04 ? 109  HIS A O   1 
ATOM   703  C  CB  . HIS A 1 109  ? 44.245 68.145  23.109  1.00 11.48 ? 109  HIS A CB  1 
ATOM   704  C  CG  . HIS A 1 109  ? 44.833 69.512  23.171  1.00 13.97 ? 109  HIS A CG  1 
ATOM   705  N  ND1 . HIS A 1 109  ? 45.883 69.817  24.014  1.00 19.31 ? 109  HIS A ND1 1 
ATOM   706  C  CD2 . HIS A 1 109  ? 44.599 70.619  22.429  1.00 17.64 ? 109  HIS A CD2 1 
ATOM   707  C  CE1 . HIS A 1 109  ? 46.238 71.076  23.814  1.00 18.17 ? 109  HIS A CE1 1 
ATOM   708  N  NE2 . HIS A 1 109  ? 45.471 71.585  22.866  1.00 20.57 ? 109  HIS A NE2 1 
ATOM   709  N  N   . ILE A 1 110  ? 43.865 65.416  21.573  1.00 9.75  ? 110  ILE A N   1 
ATOM   710  C  CA  . ILE A 1 110  ? 43.306 64.075  21.425  1.00 9.27  ? 110  ILE A CA  1 
ATOM   711  C  C   . ILE A 1 110  ? 44.417 63.023  21.413  1.00 9.75  ? 110  ILE A C   1 
ATOM   712  O  O   . ILE A 1 110  ? 44.362 62.011  22.121  1.00 9.78  ? 110  ILE A O   1 
ATOM   713  C  CB  . ILE A 1 110  ? 42.460 63.976  20.131  1.00 9.07  ? 110  ILE A CB  1 
ATOM   714  C  CG1 . ILE A 1 110  ? 41.230 64.861  20.235  1.00 8.46  ? 110  ILE A CG1 1 
ATOM   715  C  CG2 . ILE A 1 110  ? 42.063 62.509  19.819  1.00 9.47  ? 110  ILE A CG2 1 
ATOM   716  C  CD1 . ILE A 1 110  ? 40.493 65.132  18.894  1.00 9.17  ? 110  ILE A CD1 1 
ATOM   717  N  N   . LEU A 1 111  ? 45.446 63.226  20.602  1.00 9.49  ? 111  LEU A N   1 
ATOM   718  C  CA  . LEU A 1 111  ? 46.508 62.245  20.517  1.00 8.99  ? 111  LEU A CA  1 
ATOM   719  C  C   . LEU A 1 111  ? 47.380 62.169  21.776  1.00 9.40  ? 111  LEU A C   1 
ATOM   720  O  O   . LEU A 1 111  ? 47.782 61.079  22.191  1.00 9.83  ? 111  LEU A O   1 
ATOM   721  C  CB  . LEU A 1 111  ? 47.369 62.507  19.264  1.00 8.74  ? 111  LEU A CB  1 
ATOM   722  C  CG  . LEU A 1 111  ? 46.639 62.183  17.952  1.00 9.67  ? 111  LEU A CG  1 
ATOM   723  C  CD1 . LEU A 1 111  ? 47.426 62.687  16.752  1.00 10.66 ? 111  LEU A CD1 1 
ATOM   724  C  CD2 . LEU A 1 111  ? 46.414 60.718  17.855  1.00 11.66 ? 111  LEU A CD2 1 
ATOM   725  N  N   . SER A 1 112  ? 47.662 63.325  22.380  1.00 9.97  ? 112  SER A N   1 
ATOM   726  C  CA  A SER A 1 112  ? 48.423 63.321  23.619  0.50 11.20 ? 112  SER A CA  1 
ATOM   727  C  CA  B SER A 1 112  ? 48.376 63.399  23.660  0.50 11.63 ? 112  SER A CA  1 
ATOM   728  C  C   . SER A 1 112  ? 47.639 62.616  24.739  1.00 11.33 ? 112  SER A C   1 
ATOM   729  O  O   . SER A 1 112  ? 48.222 61.807  25.489  1.00 12.19 ? 112  SER A O   1 
ATOM   730  C  CB  A SER A 1 112  ? 48.811 64.741  24.002  0.50 11.34 ? 112  SER A CB  1 
ATOM   731  C  CB  B SER A 1 112  ? 48.489 64.862  24.079  0.50 11.89 ? 112  SER A CB  1 
ATOM   732  O  OG  A SER A 1 112  ? 49.550 64.713  25.199  0.50 11.87 ? 112  SER A OG  1 
ATOM   733  O  OG  B SER A 1 112  ? 49.431 65.502  23.266  0.50 15.17 ? 112  SER A OG  1 
ATOM   734  N  N   . ASN A 1 113  ? 46.339 62.871  24.826  1.00 11.09 ? 113  ASN A N   1 
ATOM   735  C  CA  . ASN A 1 113  ? 45.555 62.218  25.865  1.00 12.28 ? 113  ASN A CA  1 
ATOM   736  C  C   . ASN A 1 113  ? 45.295 60.762  25.534  1.00 12.46 ? 113  ASN A C   1 
ATOM   737  O  O   . ASN A 1 113  ? 45.247 59.916  26.444  1.00 12.68 ? 113  ASN A O   1 
ATOM   738  C  CB  . ASN A 1 113  ? 44.322 63.049  26.199  1.00 13.12 ? 113  ASN A CB  1 
ATOM   739  C  CG  . ASN A 1 113  ? 44.723 64.392  26.849  1.00 14.17 ? 113  ASN A CG  1 
ATOM   740  O  OD1 . ASN A 1 113  ? 45.832 64.509  27.428  1.00 19.52 ? 113  ASN A OD1 1 
ATOM   741  N  ND2 . ASN A 1 113  ? 43.870 65.394  26.746  1.00 15.79 ? 113  ASN A ND2 1 
ATOM   742  N  N   . ALA A 1 114  ? 45.238 60.403  24.241  1.00 11.60 ? 114  ALA A N   1 
ATOM   743  C  CA  . ALA A 1 114  ? 45.105 58.988  23.899  1.00 11.93 ? 114  ALA A CA  1 
ATOM   744  C  C   . ALA A 1 114  ? 46.342 58.225  24.333  1.00 11.56 ? 114  ALA A C   1 
ATOM   745  O  O   . ALA A 1 114  ? 46.255 57.113  24.867  1.00 12.32 ? 114  ALA A O   1 
ATOM   746  C  CB  . ALA A 1 114  ? 44.911 58.813  22.384  1.00 12.02 ? 114  ALA A CB  1 
ATOM   747  N  N   . LEU A 1 115  ? 47.513 58.826  24.129  1.00 11.28 ? 115  LEU A N   1 
ATOM   748  C  CA  . LEU A 1 115  ? 48.751 58.199  24.532  1.00 12.60 ? 115  LEU A CA  1 
ATOM   749  C  C   . LEU A 1 115  ? 48.761 57.923  26.048  1.00 13.14 ? 115  LEU A C   1 
ATOM   750  O  O   . LEU A 1 115  ? 49.028 56.802  26.473  1.00 14.27 ? 115  LEU A O   1 
ATOM   751  C  CB  . LEU A 1 115  ? 49.940 59.048  24.082  1.00 13.21 ? 115  LEU A CB  1 
ATOM   752  C  CG  . LEU A 1 115  ? 51.325 58.504  24.475  1.00 13.69 ? 115  LEU A CG  1 
ATOM   753  C  CD1 . LEU A 1 115  ? 51.567 57.078  24.021  1.00 16.76 ? 115  LEU A CD1 1 
ATOM   754  C  CD2 . LEU A 1 115  ? 52.403 59.441  23.929  1.00 15.21 ? 115  LEU A CD2 1 
ATOM   755  N  N   . ARG A 1 116  ? 48.379 58.927  26.820  1.00 13.19 ? 116  ARG A N   1 
ATOM   756  C  CA  . ARG A 1 116  ? 48.390 58.787  28.273  1.00 14.01 ? 116  ARG A CA  1 
ATOM   757  C  C   . ARG A 1 116  ? 47.348 57.763  28.729  1.00 13.22 ? 116  ARG A C   1 
ATOM   758  O  O   . ARG A 1 116  ? 47.654 56.834  29.500  1.00 13.49 ? 116  ARG A O   1 
ATOM   759  C  CB  . ARG A 1 116  ? 48.121 60.146  28.871  1.00 15.96 ? 116  ARG A CB  1 
ATOM   760  C  CG  . ARG A 1 116  ? 47.769 60.149  30.342  1.00 20.49 ? 116  ARG A CG  1 
ATOM   761  C  CD  . ARG A 1 116  ? 47.057 61.433  30.763  1.00 26.58 ? 116  ARG A CD  1 
ATOM   762  N  NE  . ARG A 1 116  ? 46.562 61.375  32.137  1.00 30.91 ? 116  ARG A NE  1 
ATOM   763  C  CZ  . ARG A 1 116  ? 46.097 62.423  32.812  1.00 32.28 ? 116  ARG A CZ  1 
ATOM   764  N  NH1 . ARG A 1 116  ? 46.059 63.626  32.250  1.00 31.83 ? 116  ARG A NH1 1 
ATOM   765  N  NH2 . ARG A 1 116  ? 45.669 62.265  34.061  1.00 33.76 ? 116  ARG A NH2 1 
ATOM   766  N  N   . HIS A 1 117  ? 46.117 57.917  28.262  1.00 12.79 ? 117  HIS A N   1 
ATOM   767  C  CA  A HIS A 1 117  ? 45.054 57.048  28.731  0.50 12.73 ? 117  HIS A CA  1 
ATOM   768  C  CA  B HIS A 1 117  ? 45.028 57.072  28.716  0.50 13.33 ? 117  HIS A CA  1 
ATOM   769  C  C   . HIS A 1 117  ? 45.193 55.617  28.310  1.00 13.05 ? 117  HIS A C   1 
ATOM   770  O  O   . HIS A 1 117  ? 44.909 54.723  29.104  1.00 13.46 ? 117  HIS A O   1 
ATOM   771  C  CB  A HIS A 1 117  ? 43.690 57.611  28.398  0.50 12.98 ? 117  HIS A CB  1 
ATOM   772  C  CB  B HIS A 1 117  ? 43.684 57.620  28.256  0.50 13.97 ? 117  HIS A CB  1 
ATOM   773  C  CG  A HIS A 1 117  ? 43.358 58.810  29.217  0.50 11.16 ? 117  HIS A CG  1 
ATOM   774  C  CG  B HIS A 1 117  ? 42.564 57.314  29.196  0.50 15.08 ? 117  HIS A CG  1 
ATOM   775  N  ND1 A HIS A 1 117  ? 42.751 58.721  30.453  0.50 11.42 ? 117  HIS A ND1 1 
ATOM   776  N  ND1 B HIS A 1 117  ? 42.275 58.092  30.299  0.50 15.29 ? 117  HIS A ND1 1 
ATOM   777  C  CD2 A HIS A 1 117  ? 43.595 60.121  29.005  0.50 11.58 ? 117  HIS A CD2 1 
ATOM   778  C  CD2 B HIS A 1 117  ? 41.676 56.293  29.214  0.50 17.12 ? 117  HIS A CD2 1 
ATOM   779  C  CE1 A HIS A 1 117  ? 42.619 59.934  30.957  0.50 10.93 ? 117  HIS A CE1 1 
ATOM   780  C  CE1 B HIS A 1 117  ? 41.249 57.566  30.949  0.50 16.38 ? 117  HIS A CE1 1 
ATOM   781  N  NE2 A HIS A 1 117  ? 43.109 60.800  30.094  0.50 11.74 ? 117  HIS A NE2 1 
ATOM   782  N  NE2 B HIS A 1 117  ? 40.862 56.482  30.303  0.50 16.26 ? 117  HIS A NE2 1 
ATOM   783  N  N   . LEU A 1 118  ? 45.629 55.362  27.072  1.00 11.60 ? 118  LEU A N   1 
ATOM   784  C  CA  . LEU A 1 118  ? 45.887 54.002  26.664  1.00 11.78 ? 118  LEU A CA  1 
ATOM   785  C  C   . LEU A 1 118  ? 47.058 53.406  27.436  1.00 11.92 ? 118  LEU A C   1 
ATOM   786  O  O   . LEU A 1 118  ? 47.002 52.244  27.867  1.00 13.23 ? 118  LEU A O   1 
ATOM   787  C  CB  . LEU A 1 118  ? 46.151 53.929  25.140  1.00 11.16 ? 118  LEU A CB  1 
ATOM   788  C  CG  . LEU A 1 118  ? 44.895 54.305  24.308  1.00 13.99 ? 118  LEU A CG  1 
ATOM   789  C  CD1 . LEU A 1 118  ? 45.274 54.522  22.814  1.00 14.21 ? 118  LEU A CD1 1 
ATOM   790  C  CD2 . LEU A 1 118  ? 43.796 53.291  24.415  1.00 14.85 ? 118  LEU A CD2 1 
ATOM   791  N  N   . HIS A 1 119  ? 48.117 54.175  27.613  1.00 12.78 ? 119  HIS A N   1 
ATOM   792  C  CA  . HIS A 1 119  ? 49.243 53.662  28.390  1.00 13.70 ? 119  HIS A CA  1 
ATOM   793  C  C   . HIS A 1 119  ? 48.769 53.199  29.773  1.00 14.69 ? 119  HIS A C   1 
ATOM   794  O  O   . HIS A 1 119  ? 49.075 52.083  30.187  1.00 15.22 ? 119  HIS A O   1 
ATOM   795  C  CB  . HIS A 1 119  ? 50.324 54.728  28.496  1.00 15.74 ? 119  HIS A CB  1 
ATOM   796  C  CG  . HIS A 1 119  ? 51.485 54.325  29.346  1.00 19.02 ? 119  HIS A CG  1 
ATOM   797  N  ND1 . HIS A 1 119  ? 51.675 54.813  30.625  1.00 24.91 ? 119  HIS A ND1 1 
ATOM   798  C  CD2 . HIS A 1 119  ? 52.513 53.476  29.108  1.00 23.97 ? 119  HIS A CD2 1 
ATOM   799  C  CE1 . HIS A 1 119  ? 52.778 54.287  31.133  1.00 25.30 ? 119  HIS A CE1 1 
ATOM   800  N  NE2 . HIS A 1 119  ? 53.302 53.467  30.238  1.00 25.29 ? 119  HIS A NE2 1 
ATOM   801  N  N   . ASP A 1 120  ? 47.968 54.025  30.423  1.00 14.84 ? 120  ASP A N   1 
ATOM   802  C  CA  . ASP A 1 120  ? 47.561 53.779  31.805  1.00 15.85 ? 120  ASP A CA  1 
ATOM   803  C  C   . ASP A 1 120  ? 46.426 52.769  31.959  1.00 16.20 ? 120  ASP A C   1 
ATOM   804  O  O   . ASP A 1 120  ? 46.174 52.314  33.088  1.00 16.52 ? 120  ASP A O   1 
ATOM   805  C  CB  . ASP A 1 120  ? 47.123 55.096  32.449  1.00 16.49 ? 120  ASP A CB  1 
ATOM   806  C  CG  . ASP A 1 120  ? 48.280 56.027  32.742  1.00 18.86 ? 120  ASP A CG  1 
ATOM   807  O  OD1 . ASP A 1 120  ? 49.447 55.601  32.651  1.00 22.50 ? 120  ASP A OD1 1 
ATOM   808  O  OD2 . ASP A 1 120  ? 48.092 57.213  33.065  1.00 21.92 ? 120  ASP A OD2 1 
ATOM   809  N  N   . ASN A 1 121  ? 45.708 52.429  30.883  1.00 15.22 ? 121  ASN A N   1 
ATOM   810  C  CA  . ASN A 1 121  ? 44.543 51.549  30.940  1.00 14.38 ? 121  ASN A CA  1 
ATOM   811  C  C   . ASN A 1 121  ? 44.655 50.454  29.901  1.00 14.68 ? 121  ASN A C   1 
ATOM   812  O  O   . ASN A 1 121  ? 44.150 50.610  28.782  1.00 14.61 ? 121  ASN A O   1 
ATOM   813  C  CB  . ASN A 1 121  ? 43.259 52.354  30.734  1.00 13.74 ? 121  ASN A CB  1 
ATOM   814  C  CG  . ASN A 1 121  ? 43.035 53.350  31.845  1.00 14.58 ? 121  ASN A CG  1 
ATOM   815  O  OD1 . ASN A 1 121  ? 42.524 52.984  32.932  1.00 17.37 ? 121  ASN A OD1 1 
ATOM   816  N  ND2 . ASN A 1 121  ? 43.429 54.600  31.629  1.00 13.77 ? 121  ASN A ND2 1 
ATOM   817  N  N   . PRO A 1 122  ? 45.340 49.369  30.220  1.00 14.17 ? 122  PRO A N   1 
ATOM   818  C  CA  . PRO A 1 122  ? 45.716 48.360  29.220  1.00 14.65 ? 122  PRO A CA  1 
ATOM   819  C  C   . PRO A 1 122  ? 44.582 47.704  28.424  1.00 14.92 ? 122  PRO A C   1 
ATOM   820  O  O   . PRO A 1 122  ? 44.868 47.207  27.321  1.00 16.16 ? 122  PRO A O   1 
ATOM   821  C  CB  . PRO A 1 122  ? 46.517 47.326  30.035  1.00 15.64 ? 122  PRO A CB  1 
ATOM   822  C  CG  . PRO A 1 122  ? 47.009 48.118  31.183  1.00 16.37 ? 122  PRO A CG  1 
ATOM   823  C  CD  . PRO A 1 122  ? 45.876 49.031  31.566  1.00 14.23 ? 122  PRO A CD  1 
ATOM   824  N  N   . GLU A 1 123  ? 43.354 47.684  28.940  1.00 14.09 ? 123  GLU A N   1 
ATOM   825  C  CA  . GLU A 1 123  ? 42.223 47.119  28.182  1.00 15.18 ? 123  GLU A CA  1 
ATOM   826  C  C   . GLU A 1 123  ? 41.504 48.111  27.265  1.00 14.15 ? 123  GLU A C   1 
ATOM   827  O  O   . GLU A 1 123  ? 40.662 47.707  26.451  1.00 14.24 ? 123  GLU A O   1 
ATOM   828  C  CB  . GLU A 1 123  ? 41.193 46.429  29.103  1.00 16.25 ? 123  GLU A CB  1 
ATOM   829  C  CG  . GLU A 1 123  ? 41.723 45.271  29.959  1.00 21.58 ? 123  GLU A CG  1 
ATOM   830  C  CD  . GLU A 1 123  ? 42.278 44.126  29.141  1.00 27.82 ? 123  GLU A CD  1 
ATOM   831  O  OE1 . GLU A 1 123  ? 41.570 43.622  28.242  1.00 29.57 ? 123  GLU A OE1 1 
ATOM   832  O  OE2 . GLU A 1 123  ? 43.434 43.713  29.400  1.00 33.45 ? 123  GLU A OE2 1 
ATOM   833  N  N   . MET A 1 124  ? 41.810 49.396  27.420  1.00 12.68 ? 124  MET A N   1 
ATOM   834  C  CA  . MET A 1 124  ? 41.229 50.426  26.555  1.00 12.30 ? 124  MET A CA  1 
ATOM   835  C  C   . MET A 1 124  ? 41.845 50.343  25.150  1.00 12.09 ? 124  MET A C   1 
ATOM   836  O  O   . MET A 1 124  ? 42.983 49.979  25.009  1.00 11.50 ? 124  MET A O   1 
ATOM   837  C  CB  . MET A 1 124  ? 41.450 51.816  27.152  1.00 13.72 ? 124  MET A CB  1 
ATOM   838  C  CG  . MET A 1 124  ? 40.708 52.960  26.467  1.00 15.20 ? 124  MET A CG  1 
ATOM   839  S  SD  . MET A 1 124  ? 38.933 52.643  26.334  1.00 14.50 ? 124  MET A SD  1 
ATOM   840  C  CE  . MET A 1 124  ? 38.417 54.171  25.505  1.00 15.73 ? 124  MET A CE  1 
ATOM   841  N  N   . LYS A 1 125  ? 41.037 50.675  24.142  1.00 11.09 ? 125  LYS A N   1 
ATOM   842  C  CA  . LYS A 1 125  ? 41.446 50.592  22.736  1.00 11.02 ? 125  LYS A CA  1 
ATOM   843  C  C   . LYS A 1 125  ? 41.047 51.855  22.025  1.00 10.29 ? 125  LYS A C   1 
ATOM   844  O  O   . LYS A 1 125  ? 40.202 52.621  22.489  1.00 10.06 ? 125  LYS A O   1 
ATOM   845  C  CB  . LYS A 1 125  ? 40.726 49.428  22.053  1.00 11.96 ? 125  LYS A CB  1 
ATOM   846  C  CG  . LYS A 1 125  ? 40.853 48.062  22.730  1.00 16.21 ? 125  LYS A CG  1 
ATOM   847  C  CD  . LYS A 1 125  ? 42.224 47.531  22.511  1.00 18.37 ? 125  LYS A CD  1 
ATOM   848  C  CE  . LYS A 1 125  ? 42.554 46.350  23.415  1.00 24.84 ? 125  LYS A CE  1 
ATOM   849  N  NZ  . LYS A 1 125  ? 41.896 45.122  22.958  1.00 26.83 ? 125  LYS A NZ  1 
ATOM   850  N  N   . PHE A 1 126  ? 41.661 52.069  20.844  1.00 9.96  ? 126  PHE A N   1 
ATOM   851  C  CA  . PHE A 1 126  ? 41.357 53.301  20.074  1.00 9.15  ? 126  PHE A CA  1 
ATOM   852  C  C   . PHE A 1 126  ? 41.832 53.054  18.660  1.00 8.29  ? 126  PHE A C   1 
ATOM   853  O  O   . PHE A 1 126  ? 42.896 52.461  18.471  1.00 9.75  ? 126  PHE A O   1 
ATOM   854  C  CB  . PHE A 1 126  ? 42.130 54.491  20.687  1.00 9.70  ? 126  PHE A CB  1 
ATOM   855  C  CG  . PHE A 1 126  ? 41.745 55.879  20.213  1.00 8.54  ? 126  PHE A CG  1 
ATOM   856  C  CD1 . PHE A 1 126  ? 40.445 56.342  20.239  1.00 9.19  ? 126  PHE A CD1 1 
ATOM   857  C  CD2 . PHE A 1 126  ? 42.774 56.801  19.879  1.00 10.55 ? 126  PHE A CD2 1 
ATOM   858  C  CE1 . PHE A 1 126  ? 40.157 57.685  19.881  1.00 9.85  ? 126  PHE A CE1 1 
ATOM   859  C  CE2 . PHE A 1 126  ? 42.496 58.101  19.542  1.00 9.82  ? 126  PHE A CE2 1 
ATOM   860  C  CZ  . PHE A 1 126  ? 41.200 58.550  19.512  1.00 9.23  ? 126  PHE A CZ  1 
ATOM   861  N  N   . ILE A 1 127  ? 41.045 53.508  17.695  1.00 8.74  ? 127  ILE A N   1 
ATOM   862  C  CA  . ILE A 1 127  ? 41.479 53.424  16.288  1.00 8.07  ? 127  ILE A CA  1 
ATOM   863  C  C   . ILE A 1 127  ? 41.761 54.819  15.739  1.00 7.91  ? 127  ILE A C   1 
ATOM   864  O  O   . ILE A 1 127  ? 41.129 55.792  16.133  1.00 8.39  ? 127  ILE A O   1 
ATOM   865  C  CB  . ILE A 1 127  ? 40.480 52.673  15.383  1.00 8.44  ? 127  ILE A CB  1 
ATOM   866  C  CG1 . ILE A 1 127  ? 39.075 53.288  15.407  1.00 8.59  ? 127  ILE A CG1 1 
ATOM   867  C  CG2 . ILE A 1 127  ? 40.437 51.177  15.777  1.00 8.98  ? 127  ILE A CG2 1 
ATOM   868  C  CD1 . ILE A 1 127  ? 38.150 52.711  14.298  1.00 9.65  ? 127  ILE A CD1 1 
ATOM   869  N  N   . TRP A 1 128  ? 42.695 54.876  14.783  1.00 7.33  ? 128  TRP A N   1 
ATOM   870  C  CA  . TRP A 1 128  ? 43.092 56.155  14.178  1.00 7.54  ? 128  TRP A CA  1 
ATOM   871  C  C   . TRP A 1 128  ? 43.213 55.996  12.675  1.00 7.07  ? 128  TRP A C   1 
ATOM   872  O  O   . TRP A 1 128  ? 43.858 55.070  12.212  1.00 7.43  ? 128  TRP A O   1 
ATOM   873  C  CB  . TRP A 1 128  ? 44.440 56.625  14.752  1.00 7.90  ? 128  TRP A CB  1 
ATOM   874  C  CG  . TRP A 1 128  ? 44.680 58.047  14.392  1.00 7.16  ? 128  TRP A CG  1 
ATOM   875  C  CD1 . TRP A 1 128  ? 45.386 58.539  13.299  1.00 7.33  ? 128  TRP A CD1 1 
ATOM   876  C  CD2 . TRP A 1 128  ? 44.108 59.162  15.047  1.00 7.40  ? 128  TRP A CD2 1 
ATOM   877  N  NE1 . TRP A 1 128  ? 45.295 59.914  13.288  1.00 7.88  ? 128  TRP A NE1 1 
ATOM   878  C  CE2 . TRP A 1 128  ? 44.500 60.326  14.336  1.00 8.03  ? 128  TRP A CE2 1 
ATOM   879  C  CE3 . TRP A 1 128  ? 43.277 59.299  16.183  1.00 8.30  ? 128  TRP A CE3 1 
ATOM   880  C  CZ2 . TRP A 1 128  ? 44.120 61.597  14.731  1.00 8.58  ? 128  TRP A CZ2 1 
ATOM   881  C  CZ3 . TRP A 1 128  ? 42.891 60.545  16.564  1.00 8.66  ? 128  TRP A CZ3 1 
ATOM   882  C  CH2 . TRP A 1 128  ? 43.319 61.698  15.838  1.00 8.78  ? 128  TRP A CH2 1 
ATOM   883  N  N   . ALA A 1 129  ? 42.621 56.947  11.953  1.00 7.79  ? 129  ALA A N   1 
ATOM   884  C  CA  . ALA A 1 129  ? 42.566 56.891  10.491  1.00 8.40  ? 129  ALA A CA  1 
ATOM   885  C  C   . ALA A 1 129  ? 43.516 57.857  9.750   1.00 9.40  ? 129  ALA A C   1 
ATOM   886  O  O   . ALA A 1 129  ? 44.115 57.460  8.743   1.00 10.11 ? 129  ALA A O   1 
ATOM   887  C  CB  . ALA A 1 129  ? 41.123 57.146  10.008  1.00 9.85  ? 129  ALA A CB  1 
ATOM   888  N  N   . GLU A 1 130  ? 43.627 59.103  10.207  1.00 8.53  ? 130  GLU A N   1 
ATOM   889  C  CA  . GLU A 1 130  ? 44.203 60.190  9.374   1.00 8.68  ? 130  GLU A CA  1 
ATOM   890  C  C   . GLU A 1 130  ? 45.696 60.338  9.690   1.00 7.84  ? 130  GLU A C   1 
ATOM   891  O  O   . GLU A 1 130  ? 46.086 60.928  10.724  1.00 8.13  ? 130  GLU A O   1 
ATOM   892  C  CB  . GLU A 1 130  ? 43.469 61.506  9.619   1.00 10.14 ? 130  GLU A CB  1 
ATOM   893  C  CG  . GLU A 1 130  ? 41.950 61.411  9.336   1.00 10.86 ? 130  GLU A CG  1 
ATOM   894  C  CD  . GLU A 1 130  ? 41.082 60.992  10.513  1.00 13.97 ? 130  GLU A CD  1 
ATOM   895  O  OE1 . GLU A 1 130  ? 41.656 60.722  11.605  1.00 13.29 ? 130  GLU A OE1 1 
ATOM   896  O  OE2 . GLU A 1 130  ? 39.822 60.935  10.362  1.00 15.18 ? 130  GLU A OE2 1 
ATOM   897  N  N   . ILE A 1 131  ? 46.565 59.814  8.838   1.00 7.01  ? 131  ILE A N   1 
ATOM   898  C  CA  . ILE A 1 131  ? 47.987 59.813  9.131   1.00 7.27  ? 131  ILE A CA  1 
ATOM   899  C  C   . ILE A 1 131  ? 48.610 61.182  8.977   1.00 7.75  ? 131  ILE A C   1 
ATOM   900  O  O   . ILE A 1 131  ? 49.625 61.461  9.651   1.00 9.02  ? 131  ILE A O   1 
ATOM   901  C  CB  . ILE A 1 131  ? 48.705 58.704  8.326   1.00 8.27  ? 131  ILE A CB  1 
ATOM   902  C  CG1 . ILE A 1 131  ? 48.065 57.344  8.625   1.00 8.64  ? 131  ILE A CG1 1 
ATOM   903  C  CG2 . ILE A 1 131  ? 50.199 58.658  8.632   1.00 9.25  ? 131  ILE A CG2 1 
ATOM   904  C  CD1 . ILE A 1 131  ? 47.944 57.016  10.144  1.00 10.93 ? 131  ILE A CD1 1 
ATOM   905  N  N   . SER A 1 132  ? 48.019 62.073  8.203   1.00 6.95  ? 132  SER A N   1 
ATOM   906  C  CA  . SER A 1 132  ? 48.530 63.445  8.148   1.00 7.26  ? 132  SER A CA  1 
ATOM   907  C  C   . SER A 1 132  ? 48.627 64.041  9.559   1.00 7.50  ? 132  SER A C   1 
ATOM   908  O  O   . SER A 1 132  ? 49.684 64.608  9.922   1.00 8.82  ? 132  SER A O   1 
ATOM   909  C  CB  . SER A 1 132  ? 47.635 64.295  7.249   1.00 7.43  ? 132  SER A CB  1 
ATOM   910  O  OG  . SER A 1 132  ? 46.272 64.253  7.669   1.00 7.51  ? 132  SER A OG  1 
ATOM   911  N  N   . TYR A 1 133  ? 47.574 63.884  10.362  1.00 7.46  ? 133  TYR A N   1 
ATOM   912  C  CA  . TYR A 1 133  ? 47.604 64.370  11.742  1.00 7.66  ? 133  TYR A CA  1 
ATOM   913  C  C   . TYR A 1 133  ? 48.560 63.574  12.609  1.00 7.85  ? 133  TYR A C   1 
ATOM   914  O  O   . TYR A 1 133  ? 49.250 64.175  13.463  1.00 8.99  ? 133  TYR A O   1 
ATOM   915  C  CB  . TYR A 1 133  ? 46.224 64.299  12.374  1.00 7.75  ? 133  TYR A CB  1 
ATOM   916  C  CG  . TYR A 1 133  ? 45.317 65.465  12.049  1.00 6.61  ? 133  TYR A CG  1 
ATOM   917  C  CD1 . TYR A 1 133  ? 45.712 66.786  12.305  1.00 8.99  ? 133  TYR A CD1 1 
ATOM   918  C  CD2 . TYR A 1 133  ? 44.047 65.246  11.506  1.00 7.10  ? 133  TYR A CD2 1 
ATOM   919  C  CE1 . TYR A 1 133  ? 44.861 67.833  12.045  1.00 9.25  ? 133  TYR A CE1 1 
ATOM   920  C  CE2 . TYR A 1 133  ? 43.199 66.280  11.236  1.00 7.67  ? 133  TYR A CE2 1 
ATOM   921  C  CZ  . TYR A 1 133  ? 43.604 67.581  11.508  1.00 8.88  ? 133  TYR A CZ  1 
ATOM   922  O  OH  . TYR A 1 133  ? 42.792 68.652  11.233  1.00 9.19  ? 133  TYR A OH  1 
ATOM   923  N  N   . PHE A 1 134  ? 48.614 62.268  12.422  1.00 7.42  ? 134  PHE A N   1 
ATOM   924  C  CA  . PHE A 1 134  ? 49.433 61.448  13.297  1.00 8.53  ? 134  PHE A CA  1 
ATOM   925  C  C   . PHE A 1 134  ? 50.895 61.774  13.083  1.00 9.50  ? 134  PHE A C   1 
ATOM   926  O  O   . PHE A 1 134  ? 51.676 61.887  14.064  1.00 9.82  ? 134  PHE A O   1 
ATOM   927  C  CB  . PHE A 1 134  ? 49.144 59.954  13.116  1.00 8.66  ? 134  PHE A CB  1 
ATOM   928  C  CG  . PHE A 1 134  ? 49.707 59.129  14.232  1.00 9.15  ? 134  PHE A CG  1 
ATOM   929  C  CD1 . PHE A 1 134  ? 48.959 58.929  15.397  1.00 10.28 ? 134  PHE A CD1 1 
ATOM   930  C  CD2 . PHE A 1 134  ? 50.992 58.649  14.158  1.00 12.74 ? 134  PHE A CD2 1 
ATOM   931  C  CE1 . PHE A 1 134  ? 49.516 58.201  16.471  1.00 11.71 ? 134  PHE A CE1 1 
ATOM   932  C  CE2 . PHE A 1 134  ? 51.568 57.926  15.234  1.00 11.91 ? 134  PHE A CE2 1 
ATOM   933  C  CZ  . PHE A 1 134  ? 50.799 57.685  16.381  1.00 12.29 ? 134  PHE A CZ  1 
ATOM   934  N  N   . ALA A 1 135  ? 51.299 61.951  11.827  1.00 9.30  ? 135  ALA A N   1 
ATOM   935  C  CA  . ALA A 1 135  ? 52.684 62.311  11.498  1.00 10.13 ? 135  ALA A CA  1 
ATOM   936  C  C   . ALA A 1 135  ? 52.997 63.699  12.053  1.00 10.17 ? 135  ALA A C   1 
ATOM   937  O  O   . ALA A 1 135  ? 54.095 63.903  12.616  1.00 12.64 ? 135  ALA A O   1 
ATOM   938  C  CB  . ALA A 1 135  ? 52.894 62.262  9.997   1.00 11.02 ? 135  ALA A CB  1 
ATOM   939  N  N   . ARG A 1 136  ? 52.079 64.642  11.917  1.00 10.12 ? 136  ARG A N   1 
ATOM   940  C  CA  . ARG A 1 136  ? 52.224 66.010  12.470  1.00 11.77 ? 136  ARG A CA  1 
ATOM   941  C  C   . ARG A 1 136  ? 52.479 65.970  13.991  1.00 12.53 ? 136  ARG A C   1 
ATOM   942  O  O   . ARG A 1 136  ? 53.298 66.742  14.519  1.00 14.85 ? 136  ARG A O   1 
ATOM   943  C  CB  . ARG A 1 136  ? 50.981 66.858  12.159  1.00 12.63 ? 136  ARG A CB  1 
ATOM   944  C  CG  . ARG A 1 136  ? 50.966 68.269  12.799  1.00 12.56 ? 136  ARG A CG  1 
ATOM   945  C  CD  . ARG A 1 136  ? 51.859 69.289  12.068  1.00 14.25 ? 136  ARG A CD  1 
ATOM   946  N  NE  . ARG A 1 136  ? 51.855 70.581  12.769  1.00 14.17 ? 136  ARG A NE  1 
ATOM   947  C  CZ  . ARG A 1 136  ? 52.587 70.856  13.838  1.00 14.52 ? 136  ARG A CZ  1 
ATOM   948  N  NH1 . ARG A 1 136  ? 53.416 69.955  14.342  1.00 15.17 ? 136  ARG A NH1 1 
ATOM   949  N  NH2 . ARG A 1 136  ? 52.471 72.051  14.402  1.00 13.85 ? 136  ARG A NH2 1 
ATOM   950  N  N   . PHE A 1 137  ? 51.794 65.071  14.699  1.00 11.24 ? 137  PHE A N   1 
ATOM   951  C  CA  . PHE A 1 137  ? 51.907 64.906  16.139  1.00 11.24 ? 137  PHE A CA  1 
ATOM   952  C  C   . PHE A 1 137  ? 53.204 64.190  16.499  1.00 11.87 ? 137  PHE A C   1 
ATOM   953  O  O   . PHE A 1 137  ? 53.979 64.674  17.356  1.00 12.69 ? 137  PHE A O   1 
ATOM   954  C  CB  . PHE A 1 137  ? 50.717 64.076  16.610  1.00 10.23 ? 137  PHE A CB  1 
ATOM   955  C  CG  . PHE A 1 137  ? 50.748 63.798  18.071  1.00 11.74 ? 137  PHE A CG  1 
ATOM   956  C  CD1 . PHE A 1 137  ? 50.467 64.825  18.976  1.00 11.61 ? 137  PHE A CD1 1 
ATOM   957  C  CD2 . PHE A 1 137  ? 51.033 62.538  18.527  1.00 12.04 ? 137  PHE A CD2 1 
ATOM   958  C  CE1 . PHE A 1 137  ? 50.466 64.584  20.336  1.00 13.91 ? 137  PHE A CE1 1 
ATOM   959  C  CE2 . PHE A 1 137  ? 51.084 62.302  19.953  1.00 14.12 ? 137  PHE A CE2 1 
ATOM   960  C  CZ  . PHE A 1 137  ? 50.781 63.335  20.808  1.00 12.81 ? 137  PHE A CZ  1 
ATOM   961  N  N   . TYR A 1 138  ? 53.474 63.052  15.845  1.00 12.53 ? 138  TYR A N   1 
ATOM   962  C  CA  A TYR A 1 138  ? 54.557 62.165  16.237  0.50 14.55 ? 138  TYR A CA  1 
ATOM   963  C  CA  B TYR A 1 138  ? 54.594 62.159  16.177  0.50 14.91 ? 138  TYR A CA  1 
ATOM   964  C  C   . TYR A 1 138  ? 55.910 62.878  16.107  1.00 16.09 ? 138  TYR A C   1 
ATOM   965  O  O   . TYR A 1 138  ? 56.804 62.712  16.976  1.00 16.33 ? 138  TYR A O   1 
ATOM   966  C  CB  A TYR A 1 138  ? 54.493 60.862  15.422  0.50 13.90 ? 138  TYR A CB  1 
ATOM   967  C  CB  B TYR A 1 138  ? 54.679 61.002  15.188  0.50 14.65 ? 138  TYR A CB  1 
ATOM   968  C  CG  A TYR A 1 138  ? 55.496 59.805  15.830  0.50 12.76 ? 138  TYR A CG  1 
ATOM   969  C  CG  B TYR A 1 138  ? 55.897 60.102  15.366  0.50 14.75 ? 138  TYR A CG  1 
ATOM   970  C  CD1 A TYR A 1 138  ? 55.195 58.858  16.818  0.50 9.90  ? 138  TYR A CD1 1 
ATOM   971  C  CD1 B TYR A 1 138  ? 57.077 60.344  14.672  0.50 14.30 ? 138  TYR A CD1 1 
ATOM   972  C  CD2 A TYR A 1 138  ? 56.710 59.716  15.179  0.50 12.24 ? 138  TYR A CD2 1 
ATOM   973  C  CD2 B TYR A 1 138  ? 55.838 58.990  16.193  0.50 15.58 ? 138  TYR A CD2 1 
ATOM   974  C  CE1 A TYR A 1 138  ? 56.135 57.892  17.187  0.50 11.55 ? 138  TYR A CE1 1 
ATOM   975  C  CE1 B TYR A 1 138  ? 58.177 59.501  14.830  0.50 15.33 ? 138  TYR A CE1 1 
ATOM   976  C  CE2 A TYR A 1 138  ? 57.651 58.768  15.534  0.50 11.77 ? 138  TYR A CE2 1 
ATOM   977  C  CE2 B TYR A 1 138  ? 56.925 58.151  16.349  0.50 15.40 ? 138  TYR A CE2 1 
ATOM   978  C  CZ  A TYR A 1 138  ? 57.356 57.847  16.519  0.50 13.06 ? 138  TYR A CZ  1 
ATOM   979  C  CZ  B TYR A 1 138  ? 58.084 58.408  15.662  0.50 15.34 ? 138  TYR A CZ  1 
ATOM   980  O  OH  A TYR A 1 138  ? 58.304 56.904  16.859  0.50 13.97 ? 138  TYR A OH  1 
ATOM   981  O  OH  B TYR A 1 138  ? 59.155 57.579  15.827  0.50 17.70 ? 138  TYR A OH  1 
ATOM   982  N  N   . HIS A 1 139  ? 56.079 63.674  15.064  1.00 16.44 ? 139  HIS A N   1 
ATOM   983  C  CA  . HIS A 1 139  ? 57.360 64.322  14.859  1.00 18.79 ? 139  HIS A CA  1 
ATOM   984  C  C   . HIS A 1 139  ? 57.596 65.452  15.886  1.00 19.56 ? 139  HIS A C   1 
ATOM   985  O  O   . HIS A 1 139  ? 58.735 65.940  16.015  1.00 21.72 ? 139  HIS A O   1 
ATOM   986  C  CB  . HIS A 1 139  ? 57.486 64.765  13.399  1.00 19.02 ? 139  HIS A CB  1 
ATOM   987  C  CG  . HIS A 1 139  ? 57.671 63.624  12.439  1.00 20.25 ? 139  HIS A CG  1 
ATOM   988  N  ND1 . HIS A 1 139  ? 58.728 62.741  12.523  1.00 22.66 ? 139  HIS A ND1 1 
ATOM   989  C  CD2 . HIS A 1 139  ? 56.926 63.217  11.381  1.00 20.01 ? 139  HIS A CD2 1 
ATOM   990  C  CE1 . HIS A 1 139  ? 58.635 61.849  11.549  1.00 23.55 ? 139  HIS A CE1 1 
ATOM   991  N  NE2 . HIS A 1 139  ? 57.567 62.132  10.825  1.00 21.36 ? 139  HIS A NE2 1 
ATOM   992  N  N   . ASP A 1 140  ? 56.567 65.869  16.624  1.00 19.13 ? 140  ASP A N   1 
ATOM   993  C  CA  . ASP A 1 140  ? 56.765 66.830  17.723  1.00 19.70 ? 140  ASP A CA  1 
ATOM   994  C  C   . ASP A 1 140  ? 56.968 66.195  19.093  1.00 18.06 ? 140  ASP A C   1 
ATOM   995  O  O   . ASP A 1 140  ? 57.206 66.899  20.093  1.00 18.75 ? 140  ASP A O   1 
ATOM   996  C  CB  . ASP A 1 140  ? 55.614 67.794  17.801  1.00 20.37 ? 140  ASP A CB  1 
ATOM   997  C  CG  . ASP A 1 140  ? 55.747 68.932  16.811  1.00 23.21 ? 140  ASP A CG  1 
ATOM   998  O  OD1 . ASP A 1 140  ? 56.626 68.859  15.923  1.00 25.55 ? 140  ASP A OD1 1 
ATOM   999  O  OD2 . ASP A 1 140  ? 55.028 69.934  16.866  1.00 23.86 ? 140  ASP A OD2 1 
ATOM   1000 N  N   . LEU A 1 141  ? 56.880 64.877  19.158  1.00 17.06 ? 141  LEU A N   1 
ATOM   1001 C  CA  . LEU A 1 141  ? 57.111 64.144  20.397  1.00 17.54 ? 141  LEU A CA  1 
ATOM   1002 C  C   . LEU A 1 141  ? 58.592 63.999  20.719  1.00 18.24 ? 141  LEU A C   1 
ATOM   1003 O  O   . LEU A 1 141  ? 59.402 63.801  19.855  1.00 19.16 ? 141  LEU A O   1 
ATOM   1004 C  CB  . LEU A 1 141  ? 56.520 62.745  20.304  1.00 17.14 ? 141  LEU A CB  1 
ATOM   1005 C  CG  . LEU A 1 141  ? 55.006 62.605  20.291  1.00 18.34 ? 141  LEU A CG  1 
ATOM   1006 C  CD1 . LEU A 1 141  ? 54.655 61.148  20.186  1.00 17.44 ? 141  LEU A CD1 1 
ATOM   1007 C  CD2 . LEU A 1 141  ? 54.361 63.240  21.526  1.00 17.60 ? 141  LEU A CD2 1 
ATOM   1008 N  N   . GLY A 1 142  ? 58.905 64.067  22.008  1.00 18.92 ? 142  GLY A N   1 
ATOM   1009 C  CA  . GLY A 1 142  ? 60.200 63.640  22.508  1.00 20.76 ? 142  GLY A CA  1 
ATOM   1010 C  C   . GLY A 1 142  ? 60.329 62.132  22.412  1.00 21.15 ? 142  GLY A C   1 
ATOM   1011 O  O   . GLY A 1 142  ? 59.315 61.411  22.305  1.00 21.38 ? 142  GLY A O   1 
ATOM   1012 N  N   . GLU A 1 143  ? 61.565 61.653  22.458  1.00 21.34 ? 143  GLU A N   1 
ATOM   1013 C  CA  . GLU A 1 143  ? 61.881 60.245  22.271  1.00 21.96 ? 143  GLU A CA  1 
ATOM   1014 C  C   . GLU A 1 143  ? 61.168 59.358  23.283  1.00 21.59 ? 143  GLU A C   1 
ATOM   1015 O  O   . GLU A 1 143  ? 60.681 58.280  22.928  1.00 20.79 ? 143  GLU A O   1 
ATOM   1016 C  CB  . GLU A 1 143  ? 63.404 60.024  22.312  1.00 23.24 ? 143  GLU A CB  1 
ATOM   1017 C  CG  . GLU A 1 143  ? 63.869 58.674  21.768  1.00 27.03 ? 143  GLU A CG  1 
ATOM   1018 C  CD  . GLU A 1 143  ? 63.513 58.432  20.303  1.00 31.88 ? 143  GLU A CD  1 
ATOM   1019 O  OE1 . GLU A 1 143  ? 63.354 59.408  19.522  1.00 34.48 ? 143  GLU A OE1 1 
ATOM   1020 O  OE2 . GLU A 1 143  ? 63.405 57.244  19.928  1.00 35.62 ? 143  GLU A OE2 1 
ATOM   1021 N  N   . ASN A 1 144  ? 61.089 59.801  24.524  1.00 21.82 ? 144  ASN A N   1 
ATOM   1022 C  CA  . ASN A 1 144  ? 60.392 59.059  25.557  1.00 22.31 ? 144  ASN A CA  1 
ATOM   1023 C  C   . ASN A 1 144  ? 58.949 58.737  25.125  1.00 20.81 ? 144  ASN A C   1 
ATOM   1024 O  O   . ASN A 1 144  ? 58.519 57.591  25.184  1.00 20.19 ? 144  ASN A O   1 
ATOM   1025 C  CB  . ASN A 1 144  ? 60.438 59.876  26.857  1.00 23.46 ? 144  ASN A CB  1 
ATOM   1026 C  CG  . ASN A 1 144  ? 59.832 59.164  28.033  1.00 28.42 ? 144  ASN A CG  1 
ATOM   1027 O  OD1 . ASN A 1 144  ? 60.420 58.240  28.598  1.00 34.55 ? 144  ASN A OD1 1 
ATOM   1028 N  ND2 . ASN A 1 144  ? 58.663 59.623  28.448  1.00 32.22 ? 144  ASN A ND2 1 
ATOM   1029 N  N   . LYS A 1 145  ? 58.233 59.762  24.674  1.00 20.06 ? 145  LYS A N   1 
ATOM   1030 C  CA  . LYS A 1 145  ? 56.846 59.613  24.221  1.00 18.49 ? 145  LYS A CA  1 
ATOM   1031 C  C   . LYS A 1 145  ? 56.725 58.827  22.900  1.00 17.78 ? 145  LYS A C   1 
ATOM   1032 O  O   . LYS A 1 145  ? 55.776 58.047  22.759  1.00 16.82 ? 145  LYS A O   1 
ATOM   1033 C  CB  . LYS A 1 145  ? 56.125 60.964  24.123  1.00 18.64 ? 145  LYS A CB  1 
ATOM   1034 C  CG  . LYS A 1 145  ? 55.920 61.675  25.464  1.00 21.27 ? 145  LYS A CG  1 
ATOM   1035 C  CD  . LYS A 1 145  ? 54.687 61.168  26.188  1.00 26.95 ? 145  LYS A CD  1 
ATOM   1036 C  CE  . LYS A 1 145  ? 54.360 62.056  27.384  1.00 30.49 ? 145  LYS A CE  1 
ATOM   1037 N  NZ  . LYS A 1 145  ? 55.078 61.609  28.610  1.00 34.62 ? 145  LYS A NZ  1 
ATOM   1038 N  N   . LYS A 1 146  ? 57.659 59.025  21.964  1.00 17.28 ? 146  LYS A N   1 
ATOM   1039 C  CA  . LYS A 1 146  ? 57.692 58.213  20.732  1.00 17.32 ? 146  LYS A CA  1 
ATOM   1040 C  C   . LYS A 1 146  ? 57.740 56.732  21.077  1.00 17.50 ? 146  LYS A C   1 
ATOM   1041 O  O   . LYS A 1 146  ? 56.991 55.920  20.507  1.00 17.01 ? 146  LYS A O   1 
ATOM   1042 C  CB  . LYS A 1 146  ? 58.853 58.569  19.810  1.00 17.05 ? 146  LYS A CB  1 
ATOM   1043 C  CG  . LYS A 1 146  ? 58.764 59.906  19.117  1.00 16.28 ? 146  LYS A CG  1 
ATOM   1044 C  CD  . LYS A 1 146  ? 59.942 60.068  18.153  1.00 17.09 ? 146  LYS A CD  1 
ATOM   1045 C  CE  . LYS A 1 146  ? 59.822 61.337  17.292  1.00 20.10 ? 146  LYS A CE  1 
ATOM   1046 N  NZ  . LYS A 1 146  ? 61.085 61.589  16.573  1.00 24.53 ? 146  LYS A NZ  1 
ATOM   1047 N  N   . LEU A 1 147  ? 58.598 56.369  22.029  1.00 18.00 ? 147  LEU A N   1 
ATOM   1048 C  CA  . LEU A 1 147  ? 58.732 54.972  22.448  1.00 17.89 ? 147  LEU A CA  1 
ATOM   1049 C  C   . LEU A 1 147  ? 57.439 54.443  23.102  1.00 17.41 ? 147  LEU A C   1 
ATOM   1050 O  O   . LEU A 1 147  ? 57.014 53.316  22.806  1.00 17.74 ? 147  LEU A O   1 
ATOM   1051 C  CB  . LEU A 1 147  ? 59.955 54.789  23.384  1.00 18.81 ? 147  LEU A CB  1 
ATOM   1052 C  CG  . LEU A 1 147  ? 61.351 54.855  22.756  1.00 21.20 ? 147  LEU A CG  1 
ATOM   1053 C  CD1 . LEU A 1 147  ? 62.392 54.910  23.855  1.00 23.24 ? 147  LEU A CD1 1 
ATOM   1054 C  CD2 . LEU A 1 147  ? 61.624 53.668  21.849  1.00 24.09 ? 147  LEU A CD2 1 
ATOM   1055 N  N   . GLN A 1 148  ? 56.823 55.246  23.968  1.00 17.11 ? 148  GLN A N   1 
ATOM   1056 C  CA  . GLN A 1 148  ? 55.541 54.878  24.566  1.00 17.41 ? 148  GLN A CA  1 
ATOM   1057 C  C   . GLN A 1 148  ? 54.467 54.677  23.485  1.00 16.24 ? 148  GLN A C   1 
ATOM   1058 O  O   . GLN A 1 148  ? 53.681 53.748  23.573  1.00 16.24 ? 148  GLN A O   1 
ATOM   1059 C  CB  . GLN A 1 148  ? 55.072 55.944  25.527  1.00 18.34 ? 148  GLN A CB  1 
ATOM   1060 C  CG  . GLN A 1 148  ? 55.798 55.978  26.843  1.00 22.84 ? 148  GLN A CG  1 
ATOM   1061 C  CD  . GLN A 1 148  ? 55.082 56.870  27.829  1.00 27.82 ? 148  GLN A CD  1 
ATOM   1062 O  OE1 . GLN A 1 148  ? 54.219 57.674  27.440  1.00 31.09 ? 148  GLN A OE1 1 
ATOM   1063 N  NE2 . GLN A 1 148  ? 55.421 56.732  29.110  1.00 30.50 ? 148  GLN A NE2 1 
ATOM   1064 N  N   . MET A 1 149  ? 54.462 55.561  22.487  1.00 15.33 ? 149  MET A N   1 
ATOM   1065 C  CA  . MET A 1 149  ? 53.512 55.433  21.369  1.00 14.34 ? 149  MET A CA  1 
ATOM   1066 C  C   . MET A 1 149  ? 53.739 54.141  20.590  1.00 14.83 ? 149  MET A C   1 
ATOM   1067 O  O   . MET A 1 149  ? 52.786 53.396  20.297  1.00 14.16 ? 149  MET A O   1 
ATOM   1068 C  CB  . MET A 1 149  ? 53.639 56.640  20.454  1.00 15.18 ? 149  MET A CB  1 
ATOM   1069 C  CG  . MET A 1 149  ? 52.621 56.668  19.312  1.00 13.79 ? 149  MET A CG  1 
ATOM   1070 S  SD  . MET A 1 149  ? 50.921 56.874  19.910  1.00 16.06 ? 149  MET A SD  1 
ATOM   1071 C  CE  . MET A 1 149  ? 50.779 58.650  19.990  1.00 19.26 ? 149  MET A CE  1 
ATOM   1072 N  N   . LYS A 1 150  ? 54.995 53.855  20.245  1.00 15.15 ? 150  LYS A N   1 
ATOM   1073 C  CA  . LYS A 1 150  ? 55.283 52.628  19.500  1.00 16.17 ? 150  LYS A CA  1 
ATOM   1074 C  C   . LYS A 1 150  ? 54.810 51.405  20.288  1.00 15.67 ? 150  LYS A C   1 
ATOM   1075 O  O   . LYS A 1 150  ? 54.335 50.434  19.698  1.00 16.11 ? 150  LYS A O   1 
ATOM   1076 C  CB  . LYS A 1 150  ? 56.759 52.471  19.111  1.00 16.67 ? 150  LYS A CB  1 
ATOM   1077 C  CG  . LYS A 1 150  ? 57.282 53.502  18.149  1.00 19.58 ? 150  LYS A CG  1 
ATOM   1078 C  CD  . LYS A 1 150  ? 58.739 53.207  17.861  1.00 26.28 ? 150  LYS A CD  1 
ATOM   1079 C  CE  . LYS A 1 150  ? 59.591 54.420  18.131  1.00 31.04 ? 150  LYS A CE  1 
ATOM   1080 N  NZ  . LYS A 1 150  ? 61.015 54.169  17.772  1.00 33.39 ? 150  LYS A NZ  1 
ATOM   1081 N  N   A SER A 1 151  ? 54.906 51.465  21.615  0.50 15.66 ? 151  SER A N   1 
ATOM   1082 N  N   B SER A 1 151  ? 54.932 51.457  21.614  0.50 15.54 ? 151  SER A N   1 
ATOM   1083 C  CA  A SER A 1 151  ? 54.535 50.342  22.478  0.50 15.86 ? 151  SER A CA  1 
ATOM   1084 C  CA  B SER A 1 151  ? 54.528 50.334  22.457  0.50 15.61 ? 151  SER A CA  1 
ATOM   1085 C  C   A SER A 1 151  ? 53.018 50.077  22.547  0.50 15.06 ? 151  SER A C   1 
ATOM   1086 C  C   B SER A 1 151  ? 53.022 50.078  22.419  0.50 14.80 ? 151  SER A C   1 
ATOM   1087 O  O   A SER A 1 151  ? 52.581 48.926  22.600  0.50 15.27 ? 151  SER A O   1 
ATOM   1088 O  O   B SER A 1 151  ? 52.604 48.926  22.247  0.50 14.86 ? 151  SER A O   1 
ATOM   1089 C  CB  A SER A 1 151  ? 55.124 50.535  23.880  0.50 16.66 ? 151  SER A CB  1 
ATOM   1090 C  CB  B SER A 1 151  ? 55.012 50.495  23.901  0.50 16.45 ? 151  SER A CB  1 
ATOM   1091 O  OG  A SER A 1 151  ? 54.343 51.435  24.639  0.50 17.82 ? 151  SER A OG  1 
ATOM   1092 O  OG  B SER A 1 151  ? 54.952 49.242  24.567  0.50 16.95 ? 151  SER A OG  1 
ATOM   1093 N  N   . ILE A 1 152  ? 52.215 51.137  22.562  1.00 14.37 ? 152  ILE A N   1 
ATOM   1094 C  CA  . ILE A 1 152  ? 50.752 50.959  22.535  1.00 13.77 ? 152  ILE A CA  1 
ATOM   1095 C  C   . ILE A 1 152  ? 50.241 50.558  21.138  1.00 12.62 ? 152  ILE A C   1 
ATOM   1096 O  O   . ILE A 1 152  ? 49.163 49.978  21.028  1.00 14.02 ? 152  ILE A O   1 
ATOM   1097 C  CB  . ILE A 1 152  ? 49.941 52.141  23.146  1.00 13.97 ? 152  ILE A CB  1 
ATOM   1098 C  CG1 . ILE A 1 152  ? 50.165 53.444  22.404  1.00 14.88 ? 152  ILE A CG1 1 
ATOM   1099 C  CG2 . ILE A 1 152  ? 50.263 52.277  24.657  1.00 14.80 ? 152  ILE A CG2 1 
ATOM   1100 C  CD1 . ILE A 1 152  ? 49.110 54.522  22.695  1.00 14.42 ? 152  ILE A CD1 1 
ATOM   1101 N  N   . VAL A 1 153  ? 51.021 50.859  20.105  1.00 12.86 ? 153  VAL A N   1 
ATOM   1102 C  CA  . VAL A 1 153  ? 50.736 50.336  18.757  1.00 13.89 ? 153  VAL A CA  1 
ATOM   1103 C  C   . VAL A 1 153  ? 51.131 48.871  18.650  1.00 15.11 ? 153  VAL A C   1 
ATOM   1104 O  O   . VAL A 1 153  ? 50.334 48.028  18.210  1.00 14.99 ? 153  VAL A O   1 
ATOM   1105 C  CB  . VAL A 1 153  ? 51.400 51.209  17.678  1.00 13.42 ? 153  VAL A CB  1 
ATOM   1106 C  CG1 . VAL A 1 153  ? 51.259 50.579  16.285  1.00 14.93 ? 153  VAL A CG1 1 
ATOM   1107 C  CG2 . VAL A 1 153  ? 50.781 52.586  17.697  1.00 13.41 ? 153  VAL A CG2 1 
ATOM   1108 N  N   A LYS A 1 154  ? 52.351 48.550  19.074  0.50 15.66 ? 154  LYS A N   1 
ATOM   1109 N  N   B LYS A 1 154  ? 52.356 48.552  19.066  0.50 15.67 ? 154  LYS A N   1 
ATOM   1110 C  CA  A LYS A 1 154  ? 52.837 47.173  19.003  0.50 17.04 ? 154  LYS A CA  1 
ATOM   1111 C  CA  B LYS A 1 154  ? 52.829 47.168  19.024  0.50 17.05 ? 154  LYS A CA  1 
ATOM   1112 C  C   A LYS A 1 154  ? 51.997 46.182  19.826  0.50 17.19 ? 154  LYS A C   1 
ATOM   1113 C  C   B LYS A 1 154  ? 51.915 46.207  19.785  0.50 17.22 ? 154  LYS A C   1 
ATOM   1114 O  O   A LYS A 1 154  ? 51.842 45.023  19.423  0.50 17.93 ? 154  LYS A O   1 
ATOM   1115 O  O   B LYS A 1 154  ? 51.637 45.099  19.309  0.50 18.06 ? 154  LYS A O   1 
ATOM   1116 C  CB  A LYS A 1 154  ? 54.317 47.113  19.395  0.50 17.49 ? 154  LYS A CB  1 
ATOM   1117 C  CB  B LYS A 1 154  ? 54.257 47.063  19.562  0.50 17.53 ? 154  LYS A CB  1 
ATOM   1118 C  CG  A LYS A 1 154  ? 55.025 45.814  18.993  0.50 19.97 ? 154  LYS A CG  1 
ATOM   1119 C  CG  B LYS A 1 154  ? 54.875 45.689  19.326  0.50 19.86 ? 154  LYS A CG  1 
ATOM   1120 C  CD  A LYS A 1 154  ? 56.540 45.986  18.891  0.50 22.58 ? 154  LYS A CD  1 
ATOM   1121 C  CD  B LYS A 1 154  ? 56.314 45.636  19.769  0.50 21.53 ? 154  LYS A CD  1 
ATOM   1122 C  CE  A LYS A 1 154  ? 57.193 46.431  20.193  0.50 24.79 ? 154  LYS A CE  1 
ATOM   1123 C  CE  B LYS A 1 154  ? 57.013 44.389  19.231  0.50 22.69 ? 154  LYS A CE  1 
ATOM   1124 N  NZ  A LYS A 1 154  ? 56.653 45.768  21.414  0.50 26.42 ? 154  LYS A NZ  1 
ATOM   1125 N  NZ  B LYS A 1 154  ? 57.189 44.419  17.744  0.50 23.93 ? 154  LYS A NZ  1 
ATOM   1126 N  N   . ASN A 1 155  ? 51.447 46.630  20.955  1.00 17.45 ? 155  ASN A N   1 
ATOM   1127 C  CA  . ASN A 1 155  ? 50.588 45.787  21.805  1.00 17.94 ? 155  ASN A CA  1 
ATOM   1128 C  C   . ASN A 1 155  ? 49.108 45.780  21.384  1.00 17.71 ? 155  ASN A C   1 
ATOM   1129 O  O   . ASN A 1 155  ? 48.287 45.109  22.002  1.00 18.57 ? 155  ASN A O   1 
ATOM   1130 C  CB  . ASN A 1 155  ? 50.736 46.152  23.307  1.00 19.82 ? 155  ASN A CB  1 
ATOM   1131 C  CG  . ASN A 1 155  ? 49.885 47.358  23.732  1.00 21.63 ? 155  ASN A CG  1 
ATOM   1132 O  OD1 . ASN A 1 155  ? 49.145 47.918  22.932  1.00 23.74 ? 155  ASN A OD1 1 
ATOM   1133 N  ND2 . ASN A 1 155  ? 49.990 47.761  25.002  1.00 22.42 ? 155  ASN A ND2 1 
ATOM   1134 N  N   . GLY A 1 156  ? 48.766 46.555  20.354  1.00 14.86 ? 156  GLY A N   1 
ATOM   1135 C  CA  . GLY A 1 156  ? 47.432 46.514  19.750  1.00 15.14 ? 156  GLY A CA  1 
ATOM   1136 C  C   . GLY A 1 156  ? 46.372 47.350  20.423  1.00 14.17 ? 156  GLY A C   1 
ATOM   1137 O  O   . GLY A 1 156  ? 45.190 47.206  20.090  1.00 15.87 ? 156  GLY A O   1 
ATOM   1138 N  N   . GLN A 1 157  ? 46.737 48.229  21.339  1.00 12.19 ? 157  GLN A N   1 
ATOM   1139 C  CA  . GLN A 1 157  ? 45.760 49.127  21.918  1.00 11.53 ? 157  GLN A CA  1 
ATOM   1140 C  C   . GLN A 1 157  ? 45.354 50.262  20.991  1.00 10.65 ? 157  GLN A C   1 
ATOM   1141 O  O   . GLN A 1 157  ? 44.207 50.617  20.934  1.00 10.70 ? 157  GLN A O   1 
ATOM   1142 C  CB  . GLN A 1 157  ? 46.296 49.741  23.200  1.00 11.14 ? 157  GLN A CB  1 
ATOM   1143 C  CG  . GLN A 1 157  ? 46.244 48.836  24.409  1.00 12.56 ? 157  GLN A CG  1 
ATOM   1144 C  CD  . GLN A 1 157  ? 46.646 49.580  25.657  1.00 11.48 ? 157  GLN A CD  1 
ATOM   1145 O  OE1 . GLN A 1 157  ? 47.794 49.570  26.049  1.00 14.15 ? 157  GLN A OE1 1 
ATOM   1146 N  NE2 . GLN A 1 157  ? 45.705 50.268  26.244  1.00 12.61 ? 157  GLN A NE2 1 
ATOM   1147 N  N   . LEU A 1 158  ? 46.346 50.869  20.346  1.00 10.35 ? 158  LEU A N   1 
ATOM   1148 C  CA  A LEU A 1 158  ? 46.065 51.871  19.321  0.50 10.11 ? 158  LEU A CA  1 
ATOM   1149 C  CA  B LEU A 1 158  ? 46.120 51.880  19.318  0.50 9.54  ? 158  LEU A CA  1 
ATOM   1150 C  C   . LEU A 1 158  ? 46.296 51.195  17.981  1.00 9.94  ? 158  LEU A C   1 
ATOM   1151 O  O   . LEU A 1 158  ? 47.361 50.652  17.700  1.00 11.01 ? 158  LEU A O   1 
ATOM   1152 C  CB  A LEU A 1 158  ? 46.920 53.127  19.498  0.50 10.71 ? 158  LEU A CB  1 
ATOM   1153 C  CB  B LEU A 1 158  ? 47.154 52.983  19.450  0.50 9.51  ? 158  LEU A CB  1 
ATOM   1154 C  CG  A LEU A 1 158  ? 46.555 54.330  18.611  0.50 12.64 ? 158  LEU A CG  1 
ATOM   1155 C  CG  B LEU A 1 158  ? 47.106 54.064  18.372  0.50 9.37  ? 158  LEU A CG  1 
ATOM   1156 C  CD1 A LEU A 1 158  ? 47.017 55.640  19.235  0.50 15.66 ? 158  LEU A CD1 1 
ATOM   1157 C  CD1 B LEU A 1 158  ? 45.716 54.712  18.366  0.50 9.48  ? 158  LEU A CD1 1 
ATOM   1158 C  CD2 A LEU A 1 158  ? 47.120 54.164  17.204  0.50 16.08 ? 158  LEU A CD2 1 
ATOM   1159 C  CD2 B LEU A 1 158  ? 48.199 55.088  18.628  0.50 10.01 ? 158  LEU A CD2 1 
ATOM   1160 N  N   . GLU A 1 159  ? 45.246 51.211  17.171  1.00 9.05  ? 159  GLU A N   1 
ATOM   1161 C  CA  . GLU A 1 159  ? 45.299 50.540  15.874  1.00 9.60  ? 159  GLU A CA  1 
ATOM   1162 C  C   . GLU A 1 159  ? 44.980 51.525  14.764  1.00 8.75  ? 159  GLU A C   1 
ATOM   1163 O  O   . GLU A 1 159  ? 43.983 52.249  14.796  1.00 9.13  ? 159  GLU A O   1 
ATOM   1164 C  CB  . GLU A 1 159  ? 44.284 49.405  15.830  1.00 10.47 ? 159  GLU A CB  1 
ATOM   1165 C  CG  . GLU A 1 159  ? 44.274 48.633  14.526  1.00 11.59 ? 159  GLU A CG  1 
ATOM   1166 C  CD  . GLU A 1 159  ? 43.291 47.497  14.578  1.00 14.36 ? 159  GLU A CD  1 
ATOM   1167 O  OE1 . GLU A 1 159  ? 43.584 46.479  15.263  1.00 14.21 ? 159  GLU A OE1 1 
ATOM   1168 O  OE2 . GLU A 1 159  ? 42.229 47.630  13.955  1.00 12.28 ? 159  GLU A OE2 1 
ATOM   1169 N  N   . PHE A 1 160  ? 45.833 51.520  13.753  1.00 7.88  ? 160  PHE A N   1 
ATOM   1170 C  CA  . PHE A 1 160  ? 45.611 52.330  12.565  1.00 8.07  ? 160  PHE A CA  1 
ATOM   1171 C  C   . PHE A 1 160  ? 44.660 51.611  11.628  1.00 8.08  ? 160  PHE A C   1 
ATOM   1172 O  O   . PHE A 1 160  ? 44.817 50.415  11.355  1.00 8.31  ? 160  PHE A O   1 
ATOM   1173 C  CB  . PHE A 1 160  ? 46.938 52.703  11.891  1.00 8.81  ? 160  PHE A CB  1 
ATOM   1174 C  CG  . PHE A 1 160  ? 47.813 53.528  12.768  1.00 8.47  ? 160  PHE A CG  1 
ATOM   1175 C  CD1 . PHE A 1 160  ? 47.544 54.865  12.973  1.00 9.65  ? 160  PHE A CD1 1 
ATOM   1176 C  CD2 . PHE A 1 160  ? 48.854 52.936  13.459  1.00 9.89  ? 160  PHE A CD2 1 
ATOM   1177 C  CE1 . PHE A 1 160  ? 48.318 55.620  13.831  1.00 10.25 ? 160  PHE A CE1 1 
ATOM   1178 C  CE2 . PHE A 1 160  ? 49.639 53.683  14.295  1.00 10.59 ? 160  PHE A CE2 1 
ATOM   1179 C  CZ  . PHE A 1 160  ? 49.364 55.014  14.483  1.00 11.05 ? 160  PHE A CZ  1 
ATOM   1180 N  N   . VAL A 1 161  ? 43.699 52.379  11.140  1.00 7.28  ? 161  VAL A N   1 
ATOM   1181 C  CA  . VAL A 1 161  ? 42.705 51.877  10.207  1.00 7.30  ? 161  VAL A CA  1 
ATOM   1182 C  C   . VAL A 1 161  ? 42.869 52.671  8.915   1.00 7.28  ? 161  VAL A C   1 
ATOM   1183 O  O   . VAL A 1 161  ? 43.012 53.891  8.920   1.00 8.95  ? 161  VAL A O   1 
ATOM   1184 C  CB  . VAL A 1 161  ? 41.253 51.958  10.791  1.00 7.73  ? 161  VAL A CB  1 
ATOM   1185 C  CG1 . VAL A 1 161  ? 41.133 50.969  11.940  1.00 8.72  ? 161  VAL A CG1 1 
ATOM   1186 C  CG2 . VAL A 1 161  ? 40.895 53.335  11.282  1.00 7.95  ? 161  VAL A CG2 1 
ATOM   1187 N  N   . THR A 1 162  ? 42.939 51.908  7.814   1.00 7.67  ? 162  THR A N   1 
ATOM   1188 C  CA  . THR A 1 162  ? 43.292 52.414  6.463   1.00 8.13  ? 162  THR A CA  1 
ATOM   1189 C  C   . THR A 1 162  ? 44.758 52.829  6.407   1.00 7.19  ? 162  THR A C   1 
ATOM   1190 O  O   . THR A 1 162  ? 45.562 52.284  5.650   1.00 8.49  ? 162  THR A O   1 
ATOM   1191 C  CB  . THR A 1 162  ? 42.404 53.548  5.941   1.00 8.51  ? 162  THR A CB  1 
ATOM   1192 O  OG1 . THR A 1 162  ? 41.019 53.172  6.056   1.00 9.46  ? 162  THR A OG1 1 
ATOM   1193 C  CG2 . THR A 1 162  ? 42.671 53.761  4.410   1.00 10.84 ? 162  THR A CG2 1 
ATOM   1194 N  N   . GLY A 1 163  ? 45.069 53.887  7.135   1.00 7.37  ? 163  GLY A N   1 
ATOM   1195 C  CA  . GLY A 1 163  ? 46.440 54.393  7.179   1.00 7.53  ? 163  GLY A CA  1 
ATOM   1196 C  C   . GLY A 1 163  ? 46.799 55.300  6.017   1.00 6.73  ? 163  GLY A C   1 
ATOM   1197 O  O   . GLY A 1 163  ? 47.972 55.505  5.712   1.00 8.23  ? 163  GLY A O   1 
ATOM   1198 N  N   . GLY A 1 164  ? 45.784 55.858  5.349   1.00 6.46  ? 164  GLY A N   1 
ATOM   1199 C  CA  . GLY A 1 164  ? 46.039 56.906  4.378   1.00 6.85  ? 164  GLY A CA  1 
ATOM   1200 C  C   . GLY A 1 164  ? 46.355 58.243  5.015   1.00 6.63  ? 164  GLY A C   1 
ATOM   1201 O  O   . GLY A 1 164  ? 46.077 58.478  6.211   1.00 6.82  ? 164  GLY A O   1 
ATOM   1202 N  N   . TRP A 1 165  ? 46.959 59.147  4.231   1.00 6.12  ? 165  TRP A N   1 
ATOM   1203 C  CA  . TRP A 1 165  ? 47.201 60.496  4.713   1.00 5.74  ? 165  TRP A CA  1 
ATOM   1204 C  C   . TRP A 1 165  ? 45.884 61.107  5.187   1.00 6.26  ? 165  TRP A C   1 
ATOM   1205 O  O   . TRP A 1 165  ? 45.859 61.867  6.179   1.00 6.81  ? 165  TRP A O   1 
ATOM   1206 C  CB  . TRP A 1 165  ? 47.798 61.303  3.566   1.00 6.77  ? 165  TRP A CB  1 
ATOM   1207 C  CG  . TRP A 1 165  ? 48.636 62.444  4.005   1.00 7.05  ? 165  TRP A CG  1 
ATOM   1208 C  CD1 . TRP A 1 165  ? 48.437 63.770  3.717   1.00 8.54  ? 165  TRP A CD1 1 
ATOM   1209 C  CD2 . TRP A 1 165  ? 49.835 62.384  4.806   1.00 7.62  ? 165  TRP A CD2 1 
ATOM   1210 N  NE1 . TRP A 1 165  ? 49.451 64.539  4.259   1.00 9.64  ? 165  TRP A NE1 1 
ATOM   1211 C  CE2 . TRP A 1 165  ? 50.302 63.718  4.945   1.00 7.73  ? 165  TRP A CE2 1 
ATOM   1212 C  CE3 . TRP A 1 165  ? 50.570 61.340  5.380   1.00 9.27  ? 165  TRP A CE3 1 
ATOM   1213 C  CZ2 . TRP A 1 165  ? 51.477 64.038  5.691   1.00 10.17 ? 165  TRP A CZ2 1 
ATOM   1214 C  CZ3 . TRP A 1 165  ? 51.739 61.670  6.117   1.00 11.78 ? 165  TRP A CZ3 1 
ATOM   1215 C  CH2 . TRP A 1 165  ? 52.163 63.001  6.227   1.00 10.30 ? 165  TRP A CH2 1 
ATOM   1216 N  N   . VAL A 1 166  ? 44.787 60.800  4.467   1.00 5.73  ? 166  VAL A N   1 
ATOM   1217 C  CA  . VAL A 1 166  ? 43.451 61.314  4.792   1.00 6.37  ? 166  VAL A CA  1 
ATOM   1218 C  C   . VAL A 1 166  ? 42.453 60.171  4.638   1.00 6.24  ? 166  VAL A C   1 
ATOM   1219 O  O   . VAL A 1 166  ? 42.832 59.052  4.311   1.00 6.99  ? 166  VAL A O   1 
ATOM   1220 C  CB  . VAL A 1 166  ? 43.034 62.500  3.868   1.00 6.35  ? 166  VAL A CB  1 
ATOM   1221 C  CG1 . VAL A 1 166  ? 44.020 63.674  3.984   1.00 7.13  ? 166  VAL A CG1 1 
ATOM   1222 C  CG2 . VAL A 1 166  ? 42.985 62.036  2.404   1.00 7.58  ? 166  VAL A CG2 1 
ATOM   1223 N  N   . MET A 1 167  ? 41.182 60.491  4.908   1.00 6.60  ? 167  MET A N   1 
ATOM   1224 C  CA  . MET A 1 167  ? 40.073 59.622  4.528   1.00 5.75  ? 167  MET A CA  1 
ATOM   1225 C  C   . MET A 1 167  ? 39.445 60.277  3.300   1.00 5.75  ? 167  MET A C   1 
ATOM   1226 O  O   . MET A 1 167  ? 38.697 61.257  3.441   1.00 6.66  ? 167  MET A O   1 
ATOM   1227 C  CB  . MET A 1 167  ? 39.082 59.586  5.679   1.00 6.69  ? 167  MET A CB  1 
ATOM   1228 C  CG  . MET A 1 167  ? 37.823 58.741  5.417   1.00 6.84  ? 167  MET A CG  1 
ATOM   1229 S  SD  . MET A 1 167  ? 36.641 58.796  6.770   1.00 8.23  ? 167  MET A SD  1 
ATOM   1230 C  CE  . MET A 1 167  ? 37.606 58.072  8.093   1.00 9.44  ? 167  MET A CE  1 
ATOM   1231 N  N   . PRO A 1 168  ? 39.817 59.841  2.101   1.00 5.98  ? 168  PRO A N   1 
ATOM   1232 C  CA  . PRO A 1 168  ? 39.500 60.652  0.936   1.00 6.27  ? 168  PRO A CA  1 
ATOM   1233 C  C   . PRO A 1 168  ? 38.059 60.651  0.502   1.00 6.52  ? 168  PRO A C   1 
ATOM   1234 O  O   . PRO A 1 168  ? 37.326 59.694  0.719   1.00 6.38  ? 168  PRO A O   1 
ATOM   1235 C  CB  . PRO A 1 168  ? 40.363 60.020  -0.172  1.00 6.96  ? 168  PRO A CB  1 
ATOM   1236 C  CG  . PRO A 1 168  ? 40.488 58.597  0.235   1.00 8.23  ? 168  PRO A CG  1 
ATOM   1237 C  CD  . PRO A 1 168  ? 40.636 58.649  1.774   1.00 6.75  ? 168  PRO A CD  1 
ATOM   1238 N  N   . ASP A 1 169  ? 37.679 61.725  -0.174  1.00 6.27  ? 169  ASP A N   1 
ATOM   1239 C  CA  . ASP A 1 169  ? 36.500 61.690  -1.024  1.00 5.67  ? 169  ASP A CA  1 
ATOM   1240 C  C   . ASP A 1 169  ? 36.620 60.518  -1.977  1.00 6.41  ? 169  ASP A C   1 
ATOM   1241 O  O   . ASP A 1 169  ? 37.719 60.194  -2.428  1.00 6.04  ? 169  ASP A O   1 
ATOM   1242 C  CB  . ASP A 1 169  ? 36.476 62.992  -1.842  1.00 6.16  ? 169  ASP A CB  1 
ATOM   1243 C  CG  . ASP A 1 169  ? 35.320 63.079  -2.793  1.00 7.34  ? 169  ASP A CG  1 
ATOM   1244 O  OD1 . ASP A 1 169  ? 34.205 62.586  -2.469  1.00 7.80  ? 169  ASP A OD1 1 
ATOM   1245 O  OD2 . ASP A 1 169  ? 35.450 63.668  -3.882  1.00 8.69  ? 169  ASP A OD2 1 
ATOM   1246 N  N   . GLU A 1 170  ? 35.486 59.938  -2.333  1.00 5.99  ? 170  GLU A N   1 
ATOM   1247 C  CA  . GLU A 1 170  ? 35.445 58.815  -3.286  1.00 6.25  ? 170  GLU A CA  1 
ATOM   1248 C  C   . GLU A 1 170  ? 34.738 59.189  -4.589  1.00 5.78  ? 170  GLU A C   1 
ATOM   1249 O  O   . GLU A 1 170  ? 34.768 58.390  -5.528  1.00 6.57  ? 170  GLU A O   1 
ATOM   1250 C  CB  . GLU A 1 170  ? 34.827 57.573  -2.633  1.00 6.72  ? 170  GLU A CB  1 
ATOM   1251 C  CG  . GLU A 1 170  ? 35.593 57.179  -1.357  1.00 7.61  ? 170  GLU A CG  1 
ATOM   1252 C  CD  . GLU A 1 170  ? 35.081 55.928  -0.677  1.00 8.26  ? 170  GLU A CD  1 
ATOM   1253 O  OE1 . GLU A 1 170  ? 34.317 55.162  -1.313  1.00 9.01  ? 170  GLU A OE1 1 
ATOM   1254 O  OE2 . GLU A 1 170  ? 35.453 55.698  0.520   1.00 9.25  ? 170  GLU A OE2 1 
ATOM   1255 N  N   . ALA A 1 171  ? 34.168 60.385  -4.668  1.00 5.93  ? 171  ALA A N   1 
ATOM   1256 C  CA  . ALA A 1 171  ? 33.429 60.788  -5.859  1.00 5.75  ? 171  ALA A CA  1 
ATOM   1257 C  C   . ALA A 1 171  ? 34.299 61.529  -6.881  1.00 5.86  ? 171  ALA A C   1 
ATOM   1258 O  O   . ALA A 1 171  ? 34.308 61.233  -8.065  1.00 7.15  ? 171  ALA A O   1 
ATOM   1259 C  CB  . ALA A 1 171  ? 32.235 61.622  -5.492  1.00 6.89  ? 171  ALA A CB  1 
ATOM   1260 N  N   . ASN A 1 172  ? 35.020 62.550  -6.403  1.00 5.75  ? 172  ASN A N   1 
ATOM   1261 C  CA  . ASN A 1 172  ? 35.740 63.458  -7.301  1.00 6.11  ? 172  ASN A CA  1 
ATOM   1262 C  C   . ASN A 1 172  ? 37.195 63.080  -7.477  1.00 5.63  ? 172  ASN A C   1 
ATOM   1263 O  O   . ASN A 1 172  ? 37.871 63.540  -8.384  1.00 5.87  ? 172  ASN A O   1 
ATOM   1264 C  CB  . ASN A 1 172  ? 35.709 64.873  -6.715  1.00 5.92  ? 172  ASN A CB  1 
ATOM   1265 C  CG  . ASN A 1 172  ? 34.304 65.419  -6.596  1.00 8.34  ? 172  ASN A CG  1 
ATOM   1266 O  OD1 . ASN A 1 172  ? 33.621 65.620  -7.608  1.00 10.37 ? 172  ASN A OD1 1 
ATOM   1267 N  ND2 . ASN A 1 172  ? 33.873 65.703  -5.376  1.00 9.69  ? 172  ASN A ND2 1 
ATOM   1268 N  N   . SER A 1 173  ? 37.708 62.275  -6.565  1.00 5.97  ? 173  SER A N   1 
ATOM   1269 C  CA  . SER A 1 173  ? 39.151 61.930  -6.514  1.00 6.29  ? 173  SER A CA  1 
ATOM   1270 C  C   . SER A 1 173  ? 39.523 61.038  -7.685  1.00 5.79  ? 173  SER A C   1 
ATOM   1271 O  O   . SER A 1 173  ? 38.799 60.089  -8.045  1.00 6.68  ? 173  SER A O   1 
ATOM   1272 C  CB  . SER A 1 173  ? 39.456 61.251  -5.188  1.00 6.13  ? 173  SER A CB  1 
ATOM   1273 O  OG  . SER A 1 173  ? 38.558 60.141  -5.029  1.00 6.97  ? 173  SER A OG  1 
ATOM   1274 N  N   . HIS A 1 174  ? 40.686 61.295  -8.255  1.00 5.46  ? 174  HIS A N   1 
ATOM   1275 C  CA  . HIS A 1 174  ? 41.229 60.386  -9.242  1.00 5.18  ? 174  HIS A CA  1 
ATOM   1276 C  C   . HIS A 1 174  ? 41.882 59.200  -8.542  1.00 4.55  ? 174  HIS A C   1 
ATOM   1277 O  O   . HIS A 1 174  ? 42.539 59.376  -7.507  1.00 5.35  ? 174  HIS A O   1 
ATOM   1278 C  CB  . HIS A 1 174  ? 42.264 61.104  -10.093 1.00 5.52  ? 174  HIS A CB  1 
ATOM   1279 C  CG  . HIS A 1 174  ? 42.508 60.419  -11.384 1.00 5.96  ? 174  HIS A CG  1 
ATOM   1280 N  ND1 . HIS A 1 174  ? 43.254 59.266  -11.496 1.00 7.46  ? 174  HIS A ND1 1 
ATOM   1281 C  CD2 . HIS A 1 174  ? 42.041 60.709  -12.616 1.00 7.60  ? 174  HIS A CD2 1 
ATOM   1282 C  CE1 . HIS A 1 174  ? 43.244 58.877  -12.760 1.00 8.46  ? 174  HIS A CE1 1 
ATOM   1283 N  NE2 . HIS A 1 174  ? 42.500 59.726  -13.447 1.00 8.82  ? 174  HIS A NE2 1 
ATOM   1284 N  N   . TRP A 1 175  ? 41.749 58.002  -9.094  1.00 5.10  ? 175  TRP A N   1 
ATOM   1285 C  CA  . TRP A 1 175  ? 42.332 56.812  -8.469  1.00 5.26  ? 175  TRP A CA  1 
ATOM   1286 C  C   . TRP A 1 175  ? 43.818 56.987  -8.230  1.00 5.36  ? 175  TRP A C   1 
ATOM   1287 O  O   . TRP A 1 175  ? 44.356 56.479  -7.240  1.00 6.09  ? 175  TRP A O   1 
ATOM   1288 C  CB  . TRP A 1 175  ? 42.050 55.545  -9.289  1.00 5.61  ? 175  TRP A CB  1 
ATOM   1289 C  CG  . TRP A 1 175  ? 42.879 55.352  -10.529 1.00 6.02  ? 175  TRP A CG  1 
ATOM   1290 C  CD1 . TRP A 1 175  ? 42.556 55.726  -11.816 1.00 6.77  ? 175  TRP A CD1 1 
ATOM   1291 C  CD2 . TRP A 1 175  ? 44.171 54.725  -10.602 1.00 6.68  ? 175  TRP A CD2 1 
ATOM   1292 N  NE1 . TRP A 1 175  ? 43.580 55.344  -12.667 1.00 7.31  ? 175  TRP A NE1 1 
ATOM   1293 C  CE2 . TRP A 1 175  ? 44.570 54.732  -11.941 1.00 6.48  ? 175  TRP A CE2 1 
ATOM   1294 C  CE3 . TRP A 1 175  ? 45.033 54.143  -9.651  1.00 7.25  ? 175  TRP A CE3 1 
ATOM   1295 C  CZ2 . TRP A 1 175  ? 45.791 54.193  -12.377 1.00 7.71  ? 175  TRP A CZ2 1 
ATOM   1296 C  CZ3 . TRP A 1 175  ? 46.220 53.593  -10.083 1.00 8.11  ? 175  TRP A CZ3 1 
ATOM   1297 C  CH2 . TRP A 1 175  ? 46.603 53.657  -11.430 1.00 8.92  ? 175  TRP A CH2 1 
ATOM   1298 N  N   . ARG A 1 176  ? 44.504 57.696  -9.127  1.00 5.71  ? 176  ARG A N   1 
ATOM   1299 C  CA  . ARG A 1 176  ? 45.954 57.898  -8.936  1.00 6.49  ? 176  ARG A CA  1 
ATOM   1300 C  C   . ARG A 1 176  ? 46.218 58.652  -7.645  1.00 5.79  ? 176  ARG A C   1 
ATOM   1301 O  O   . ARG A 1 176  ? 47.234 58.384  -6.964  1.00 6.19  ? 176  ARG A O   1 
ATOM   1302 C  CB  . ARG A 1 176  ? 46.541 58.652  -10.165 1.00 7.36  ? 176  ARG A CB  1 
ATOM   1303 C  CG  . ARG A 1 176  ? 46.512 57.752  -11.410 1.00 8.54  ? 176  ARG A CG  1 
ATOM   1304 C  CD  . ARG A 1 176  ? 46.542 58.492  -12.758 1.00 10.60 ? 176  ARG A CD  1 
ATOM   1305 N  NE  . ARG A 1 176  ? 47.615 59.474  -12.823 1.00 11.22 ? 176  ARG A NE  1 
ATOM   1306 C  CZ  . ARG A 1 176  ? 47.763 60.350  -13.838 1.00 11.08 ? 176  ARG A CZ  1 
ATOM   1307 N  NH1 . ARG A 1 176  ? 46.846 60.332  -14.829 1.00 11.84 ? 176  ARG A NH1 1 
ATOM   1308 N  NH2 . ARG A 1 176  ? 48.742 61.267  -13.794 1.00 12.42 ? 176  ARG A NH2 1 
ATOM   1309 N  N   . ASN A 1 177  ? 45.374 59.605  -7.305  1.00 5.19  ? 177  ASN A N   1 
ATOM   1310 C  CA  . ASN A 1 177  ? 45.582 60.378  -6.076  1.00 5.64  ? 177  ASN A CA  1 
ATOM   1311 C  C   . ASN A 1 177  ? 45.058 59.660  -4.841  1.00 5.68  ? 177  ASN A C   1 
ATOM   1312 O  O   . ASN A 1 177  ? 45.601 59.829  -3.724  1.00 5.93  ? 177  ASN A O   1 
ATOM   1313 C  CB  . ASN A 1 177  ? 44.970 61.777  -6.203  1.00 6.46  ? 177  ASN A CB  1 
ATOM   1314 C  CG  . ASN A 1 177  ? 45.665 62.610  -7.221  1.00 6.59  ? 177  ASN A CG  1 
ATOM   1315 O  OD1 . ASN A 1 177  ? 46.835 62.414  -7.530  1.00 7.63  ? 177  ASN A OD1 1 
ATOM   1316 N  ND2 . ASN A 1 177  ? 44.926 63.566  -7.761  1.00 9.75  ? 177  ASN A ND2 1 
ATOM   1317 N  N   . VAL A 1 178  ? 44.092 58.790  -5.009  1.00 5.69  ? 178  VAL A N   1 
ATOM   1318 C  CA  . VAL A 1 178  ? 43.692 57.928  -3.906  1.00 5.86  ? 178  VAL A CA  1 
ATOM   1319 C  C   . VAL A 1 178  ? 44.861 57.017  -3.567  1.00 5.60  ? 178  VAL A C   1 
ATOM   1320 O  O   . VAL A 1 178  ? 45.189 56.855  -2.370  1.00 6.30  ? 178  VAL A O   1 
ATOM   1321 C  CB  . VAL A 1 178  ? 42.425 57.083  -4.257  1.00 6.13  ? 178  VAL A CB  1 
ATOM   1322 C  CG1 . VAL A 1 178  ? 42.131 56.076  -3.141  1.00 8.65  ? 178  VAL A CG1 1 
ATOM   1323 C  CG2 . VAL A 1 178  ? 41.193 57.995  -4.465  1.00 7.63  ? 178  VAL A CG2 1 
ATOM   1324 N  N   . LEU A 1 179  ? 45.515 56.462  -4.569  1.00 5.57  ? 179  LEU A N   1 
ATOM   1325 C  CA  . LEU A 1 179  ? 46.675 55.627  -4.305  1.00 6.28  ? 179  LEU A CA  1 
ATOM   1326 C  C   . LEU A 1 179  ? 47.817 56.449  -3.730  1.00 6.38  ? 179  LEU A C   1 
ATOM   1327 O  O   . LEU A 1 179  ? 48.507 55.982  -2.788  1.00 6.48  ? 179  LEU A O   1 
ATOM   1328 C  CB  . LEU A 1 179  ? 47.108 54.928  -5.611  1.00 6.22  ? 179  LEU A CB  1 
ATOM   1329 C  CG  . LEU A 1 179  ? 48.412 54.090  -5.471  1.00 6.55  ? 179  LEU A CG  1 
ATOM   1330 C  CD1 . LEU A 1 179  ? 48.305 53.000  -4.369  1.00 7.27  ? 179  LEU A CD1 1 
ATOM   1331 C  CD2 . LEU A 1 179  ? 48.801 53.504  -6.831  1.00 7.70  ? 179  LEU A CD2 1 
ATOM   1332 N  N   . LEU A 1 180  ? 48.011 57.674  -4.212  1.00 5.93  ? 180  LEU A N   1 
ATOM   1333 C  CA  . LEU A 1 180  ? 49.112 58.516  -3.736  1.00 6.20  ? 180  LEU A CA  1 
ATOM   1334 C  C   . LEU A 1 180  ? 48.944 58.764  -2.247  1.00 5.86  ? 180  LEU A C   1 
ATOM   1335 O  O   . LEU A 1 180  ? 49.917 58.583  -1.455  1.00 6.09  ? 180  LEU A O   1 
ATOM   1336 C  CB  . LEU A 1 180  ? 49.099 59.840  -4.496  1.00 6.47  ? 180  LEU A CB  1 
ATOM   1337 C  CG  . LEU A 1 180  ? 50.217 60.809  -4.136  1.00 7.87  ? 180  LEU A CG  1 
ATOM   1338 C  CD1 . LEU A 1 180  ? 51.478 60.335  -4.800  1.00 9.58  ? 180  LEU A CD1 1 
ATOM   1339 C  CD2 . LEU A 1 180  ? 49.883 62.208  -4.629  1.00 9.38  ? 180  LEU A CD2 1 
ATOM   1340 N  N   . GLN A 1 181  ? 47.751 59.157  -1.833  1.00 5.65  ? 181  GLN A N   1 
ATOM   1341 C  CA  . GLN A 1 181  ? 47.579 59.466  -0.409  1.00 5.93  ? 181  GLN A CA  1 
ATOM   1342 C  C   . GLN A 1 181  ? 47.635 58.233  0.489   1.00 5.71  ? 181  GLN A C   1 
ATOM   1343 O  O   . GLN A 1 181  ? 48.150 58.297  1.642   1.00 5.71  ? 181  GLN A O   1 
ATOM   1344 C  CB  . GLN A 1 181  ? 46.320 60.304  -0.197  1.00 5.67  ? 181  GLN A CB  1 
ATOM   1345 C  CG  . GLN A 1 181  ? 45.008 59.570  -0.406  1.00 6.22  ? 181  GLN A CG  1 
ATOM   1346 C  CD  . GLN A 1 181  ? 44.604 58.650  0.732   1.00 6.23  ? 181  GLN A CD  1 
ATOM   1347 O  OE1 . GLN A 1 181  ? 44.856 58.960  1.928   1.00 7.67  ? 181  GLN A OE1 1 
ATOM   1348 N  NE2 . GLN A 1 181  ? 43.966 57.535  0.402   1.00 7.45  ? 181  GLN A NE2 1 
ATOM   1349 N  N   . LEU A 1 182  ? 47.138 57.102  -0.017  1.00 5.92  ? 182  LEU A N   1 
ATOM   1350 C  CA  . LEU A 1 182  ? 47.239 55.840  0.713   1.00 6.43  ? 182  LEU A CA  1 
ATOM   1351 C  C   . LEU A 1 182  ? 48.693 55.502  0.912   1.00 5.93  ? 182  LEU A C   1 
ATOM   1352 O  O   . LEU A 1 182  ? 49.121 55.125  2.007   1.00 6.32  ? 182  LEU A O   1 
ATOM   1353 C  CB  . LEU A 1 182  ? 46.539 54.717  -0.039  1.00 6.29  ? 182  LEU A CB  1 
ATOM   1354 C  CG  . LEU A 1 182  ? 46.581 53.362  0.652   1.00 6.53  ? 182  LEU A CG  1 
ATOM   1355 C  CD1 . LEU A 1 182  ? 45.847 53.314  1.975   1.00 9.30  ? 182  LEU A CD1 1 
ATOM   1356 C  CD2 . LEU A 1 182  ? 45.996 52.298  -0.281  1.00 8.94  ? 182  LEU A CD2 1 
ATOM   1357 N  N   . THR A 1 183  ? 49.483 55.634  -0.144  1.00 6.20  ? 183  THR A N   1 
ATOM   1358 C  CA  . THR A 1 183  ? 50.904 55.307  -0.089  1.00 6.34  ? 183  THR A CA  1 
ATOM   1359 C  C   . THR A 1 183  ? 51.614 56.255  0.842   1.00 6.25  ? 183  THR A C   1 
ATOM   1360 O  O   . THR A 1 183  ? 52.532 55.831  1.591   1.00 6.73  ? 183  THR A O   1 
ATOM   1361 C  CB  . THR A 1 183  ? 51.508 55.366  -1.509  1.00 6.66  ? 183  THR A CB  1 
ATOM   1362 O  OG1 . THR A 1 183  ? 50.830 54.441  -2.370  1.00 7.19  ? 183  THR A OG1 1 
ATOM   1363 C  CG2 . THR A 1 183  ? 53.015 54.948  -1.493  1.00 8.31  ? 183  THR A CG2 1 
ATOM   1364 N  N   . GLU A 1 184  ? 51.261 57.524  0.838   1.00 6.19  ? 184  GLU A N   1 
ATOM   1365 C  CA  . GLU A 1 184  ? 51.970 58.485  1.685   1.00 7.45  ? 184  GLU A CA  1 
ATOM   1366 C  C   . GLU A 1 184  ? 51.769 58.104  3.161   1.00 7.58  ? 184  GLU A C   1 
ATOM   1367 O  O   . GLU A 1 184  ? 52.718 58.095  3.969   1.00 8.20  ? 184  GLU A O   1 
ATOM   1368 C  CB  . GLU A 1 184  ? 51.427 59.890  1.450   1.00 8.27  ? 184  GLU A CB  1 
ATOM   1369 C  CG  . GLU A 1 184  ? 52.322 61.025  1.931   1.00 9.78  ? 184  GLU A CG  1 
ATOM   1370 C  CD  . GLU A 1 184  ? 53.703 61.063  1.264   1.00 10.16 ? 184  GLU A CD  1 
ATOM   1371 O  OE1 . GLU A 1 184  ? 53.883 60.657  0.112   1.00 12.16 ? 184  GLU A OE1 1 
ATOM   1372 O  OE2 . GLU A 1 184  ? 54.619 61.531  1.947   1.00 13.83 ? 184  GLU A OE2 1 
ATOM   1373 N  N   . GLY A 1 185  ? 50.540 57.817  3.557   1.00 7.40  ? 185  GLY A N   1 
ATOM   1374 C  CA  . GLY A 1 185  ? 50.272 57.452  4.944   1.00 7.03  ? 185  GLY A CA  1 
ATOM   1375 C  C   . GLY A 1 185  ? 50.864 56.105  5.292   1.00 7.25  ? 185  GLY A C   1 
ATOM   1376 O  O   . GLY A 1 185  ? 51.463 55.944  6.390   1.00 7.97  ? 185  GLY A O   1 
ATOM   1377 N  N   . GLN A 1 186  ? 50.759 55.117  4.416   1.00 6.92  ? 186  GLN A N   1 
ATOM   1378 C  CA  . GLN A 1 186  ? 51.219 53.774  4.789   1.00 7.40  ? 186  GLN A CA  1 
ATOM   1379 C  C   . GLN A 1 186  ? 52.745 53.717  4.798   1.00 7.40  ? 186  GLN A C   1 
ATOM   1380 O  O   . GLN A 1 186  ? 53.344 52.942  5.576   1.00 7.84  ? 186  GLN A O   1 
ATOM   1381 C  CB  . GLN A 1 186  ? 50.661 52.682  3.869   1.00 6.88  ? 186  GLN A CB  1 
ATOM   1382 C  CG  . GLN A 1 186  ? 49.136 52.513  4.137   1.00 8.76  ? 186  GLN A CG  1 
ATOM   1383 C  CD  . GLN A 1 186  ? 48.718 51.104  3.912   1.00 9.89  ? 186  GLN A CD  1 
ATOM   1384 O  OE1 . GLN A 1 186  ? 49.345 50.433  3.119   1.00 12.83 ? 186  GLN A OE1 1 
ATOM   1385 N  NE2 . GLN A 1 186  ? 47.657 50.649  4.550   1.00 9.58  ? 186  GLN A NE2 1 
ATOM   1386 N  N   . THR A 1 187  ? 53.402 54.458  3.896   1.00 7.41  ? 187  THR A N   1 
ATOM   1387 C  CA  . THR A 1 187  ? 54.871 54.499  3.918   1.00 7.70  ? 187  THR A CA  1 
ATOM   1388 C  C   . THR A 1 187  ? 55.354 55.105  5.235   1.00 8.59  ? 187  THR A C   1 
ATOM   1389 O  O   . THR A 1 187  ? 56.304 54.564  5.850   1.00 9.24  ? 187  THR A O   1 
ATOM   1390 C  CB  . THR A 1 187  ? 55.382 55.249  2.709   1.00 7.43  ? 187  THR A CB  1 
ATOM   1391 O  OG1 . THR A 1 187  ? 54.912 54.564  1.529   1.00 7.90  ? 187  THR A OG1 1 
ATOM   1392 C  CG2 . THR A 1 187  ? 56.949 55.213  2.663   1.00 9.00  ? 187  THR A CG2 1 
ATOM   1393 N  N   . TRP A 1 188  ? 54.709 56.168  5.689   1.00 7.59  ? 188  TRP A N   1 
ATOM   1394 C  CA  . TRP A 1 188  ? 55.015 56.777  6.981   1.00 8.18  ? 188  TRP A CA  1 
ATOM   1395 C  C   . TRP A 1 188  ? 54.802 55.742  8.086   1.00 8.84  ? 188  TRP A C   1 
ATOM   1396 O  O   . TRP A 1 188  ? 55.703 55.515  8.932   1.00 9.23  ? 188  TRP A O   1 
ATOM   1397 C  CB  . TRP A 1 188  ? 54.132 58.026  7.223   1.00 9.11  ? 188  TRP A CB  1 
ATOM   1398 C  CG  . TRP A 1 188  ? 54.610 58.768  8.414   1.00 9.27  ? 188  TRP A CG  1 
ATOM   1399 C  CD1 . TRP A 1 188  ? 55.498 59.797  8.412   1.00 11.29 ? 188  TRP A CD1 1 
ATOM   1400 C  CD2 . TRP A 1 188  ? 54.300 58.487  9.791   1.00 9.25  ? 188  TRP A CD2 1 
ATOM   1401 N  NE1 . TRP A 1 188  ? 55.769 60.199  9.701   1.00 11.15 ? 188  TRP A NE1 1 
ATOM   1402 C  CE2 . TRP A 1 188  ? 55.047 59.412  10.570  1.00 9.57  ? 188  TRP A CE2 1 
ATOM   1403 C  CE3 . TRP A 1 188  ? 53.470 57.565  10.441  1.00 9.45  ? 188  TRP A CE3 1 
ATOM   1404 C  CZ2 . TRP A 1 188  ? 55.020 59.415  11.982  1.00 11.09 ? 188  TRP A CZ2 1 
ATOM   1405 C  CZ3 . TRP A 1 188  ? 53.466 57.554  11.853  1.00 10.30 ? 188  TRP A CZ3 1 
ATOM   1406 C  CH2 . TRP A 1 188  ? 54.222 58.496  12.589  1.00 9.87  ? 188  TRP A CH2 1 
ATOM   1407 N  N   . LEU A 1 189  ? 53.682 55.033  8.080   1.00 8.26  ? 189  LEU A N   1 
ATOM   1408 C  CA  . LEU A 1 189  ? 53.412 54.037  9.136   1.00 8.27  ? 189  LEU A CA  1 
ATOM   1409 C  C   . LEU A 1 189  ? 54.419 52.940  9.127   1.00 9.20  ? 189  LEU A C   1 
ATOM   1410 O  O   . LEU A 1 189  ? 54.812 52.464  10.230  1.00 10.11 ? 189  LEU A O   1 
ATOM   1411 C  CB  . LEU A 1 189  ? 52.000 53.435  9.032   1.00 8.68  ? 189  LEU A CB  1 
ATOM   1412 C  CG  . LEU A 1 189  ? 50.862 54.331  9.468   1.00 8.08  ? 189  LEU A CG  1 
ATOM   1413 C  CD1 . LEU A 1 189  ? 49.524 53.628  9.111   1.00 9.49  ? 189  LEU A CD1 1 
ATOM   1414 C  CD2 . LEU A 1 189  ? 50.954 54.581  11.006  1.00 9.40  ? 189  LEU A CD2 1 
ATOM   1415 N  N   . LYS A 1 190  ? 54.833 52.440  7.978   1.00 8.31  ? 190  LYS A N   1 
ATOM   1416 C  CA  . LYS A 1 190  ? 55.790 51.349  7.940   1.00 10.29 ? 190  LYS A CA  1 
ATOM   1417 C  C   . LYS A 1 190  ? 57.115 51.840  8.538   1.00 10.71 ? 190  LYS A C   1 
ATOM   1418 O  O   . LYS A 1 190  ? 57.732 51.121  9.358   1.00 11.91 ? 190  LYS A O   1 
ATOM   1419 C  CB  . LYS A 1 190  ? 55.995 50.811  6.526   1.00 11.59 ? 190  LYS A CB  1 
ATOM   1420 C  CG  . LYS A 1 190  ? 56.943 49.631  6.514   1.00 14.14 ? 190  LYS A CG  1 
ATOM   1421 C  CD  . LYS A 1 190  ? 57.058 48.992  5.163   1.00 20.91 ? 190  LYS A CD  1 
ATOM   1422 C  CE  . LYS A 1 190  ? 57.923 47.735  5.228   1.00 25.14 ? 190  LYS A CE  1 
ATOM   1423 N  NZ  . LYS A 1 190  ? 58.179 47.236  3.841   1.00 26.97 ? 190  LYS A NZ  1 
ATOM   1424 N  N   . GLN A 1 191  ? 57.538 53.032  8.163   1.00 11.28 ? 191  GLN A N   1 
ATOM   1425 C  CA  . GLN A 1 191  ? 58.845 53.543  8.583   1.00 14.52 ? 191  GLN A CA  1 
ATOM   1426 C  C   . GLN A 1 191  ? 58.859 53.806  10.076  1.00 14.33 ? 191  GLN A C   1 
ATOM   1427 O  O   . GLN A 1 191  ? 59.833 53.425  10.756  1.00 16.95 ? 191  GLN A O   1 
ATOM   1428 C  CB  . GLN A 1 191  ? 59.191 54.821  7.826   1.00 14.45 ? 191  GLN A CB  1 
ATOM   1429 C  CG  . GLN A 1 191  ? 60.544 55.430  8.214   1.00 20.03 ? 191  GLN A CG  1 
ATOM   1430 C  CD  . GLN A 1 191  ? 60.946 56.579  7.286   1.00 20.44 ? 191  GLN A CD  1 
ATOM   1431 O  OE1 . GLN A 1 191  ? 60.233 56.901  6.320   1.00 28.38 ? 191  GLN A OE1 1 
ATOM   1432 N  NE2 . GLN A 1 191  ? 62.087 57.198  7.580   1.00 27.80 ? 191  GLN A NE2 1 
ATOM   1433 N  N   . PHE A 1 192  ? 57.833 54.447  10.617  1.00 12.64 ? 192  PHE A N   1 
ATOM   1434 C  CA  . PHE A 1 192  ? 57.891 54.929  11.997  1.00 12.33 ? 192  PHE A CA  1 
ATOM   1435 C  C   . PHE A 1 192  ? 57.172 54.072  13.016  1.00 13.74 ? 192  PHE A C   1 
ATOM   1436 O  O   . PHE A 1 192  ? 57.586 54.034  14.182  1.00 15.36 ? 192  PHE A O   1 
ATOM   1437 C  CB  . PHE A 1 192  ? 57.427 56.373  12.075  1.00 12.36 ? 192  PHE A CB  1 
ATOM   1438 C  CG  . PHE A 1 192  ? 58.325 57.316  11.333  1.00 12.65 ? 192  PHE A CG  1 
ATOM   1439 C  CD1 . PHE A 1 192  ? 59.574 57.672  11.881  1.00 14.12 ? 192  PHE A CD1 1 
ATOM   1440 C  CD2 . PHE A 1 192  ? 57.990 57.791  10.064  1.00 13.08 ? 192  PHE A CD2 1 
ATOM   1441 C  CE1 . PHE A 1 192  ? 60.448 58.524  11.185  1.00 14.95 ? 192  PHE A CE1 1 
ATOM   1442 C  CE2 . PHE A 1 192  ? 58.860 58.638  9.365   1.00 14.17 ? 192  PHE A CE2 1 
ATOM   1443 C  CZ  . PHE A 1 192  ? 60.103 59.020  9.951   1.00 15.17 ? 192  PHE A CZ  1 
ATOM   1444 N  N   . MET A 1 193  ? 56.142 53.337  12.604  1.00 12.21 ? 193  MET A N   1 
ATOM   1445 C  CA  A MET A 1 193  ? 55.305 52.541  13.509  0.50 12.25 ? 193  MET A CA  1 
ATOM   1446 C  CA  B MET A 1 193  ? 55.343 52.539  13.530  0.50 12.85 ? 193  MET A CA  1 
ATOM   1447 C  C   . MET A 1 193  ? 55.452 51.047  13.242  1.00 12.66 ? 193  MET A C   1 
ATOM   1448 O  O   . MET A 1 193  ? 54.910 50.220  14.015  1.00 14.01 ? 193  MET A O   1 
ATOM   1449 C  CB  A MET A 1 193  ? 53.818 52.953  13.415  0.50 12.68 ? 193  MET A CB  1 
ATOM   1450 C  CB  B MET A 1 193  ? 53.881 53.008  13.519  0.50 13.56 ? 193  MET A CB  1 
ATOM   1451 C  CG  A MET A 1 193  ? 53.508 54.290  14.080  0.50 10.89 ? 193  MET A CG  1 
ATOM   1452 C  CG  B MET A 1 193  ? 53.758 54.522  13.616  0.50 14.54 ? 193  MET A CG  1 
ATOM   1453 S  SD  A MET A 1 193  ? 53.669 54.208  15.873  0.50 11.22 ? 193  MET A SD  1 
ATOM   1454 S  SD  B MET A 1 193  ? 54.599 55.271  15.020  0.50 20.68 ? 193  MET A SD  1 
ATOM   1455 C  CE  A MET A 1 193  ? 54.687 55.668  16.249  0.50 14.55 ? 193  MET A CE  1 
ATOM   1456 C  CE  B MET A 1 193  ? 53.450 54.812  16.229  0.50 15.61 ? 193  MET A CE  1 
ATOM   1457 N  N   . ASN A 1 194  ? 56.135 50.687  12.150  1.00 11.90 ? 194  ASN A N   1 
ATOM   1458 C  CA  . ASN A 1 194  ? 56.287 49.292  11.753  1.00 13.59 ? 194  ASN A CA  1 
ATOM   1459 C  C   . ASN A 1 194  ? 54.978 48.508  11.640  1.00 13.41 ? 194  ASN A C   1 
ATOM   1460 O  O   . ASN A 1 194  ? 54.878 47.358  12.083  1.00 13.59 ? 194  ASN A O   1 
ATOM   1461 C  CB  . ASN A 1 194  ? 57.211 48.572  12.759  1.00 14.03 ? 194  ASN A CB  1 
ATOM   1462 C  CG  . ASN A 1 194  ? 57.721 47.254  12.218  1.00 17.53 ? 194  ASN A CG  1 
ATOM   1463 O  OD1 . ASN A 1 194  ? 57.898 47.093  11.013  1.00 18.94 ? 194  ASN A OD1 1 
ATOM   1464 N  ND2 . ASN A 1 194  ? 57.973 46.299  13.115  1.00 20.69 ? 194  ASN A ND2 1 
ATOM   1465 N  N   . VAL A 1 195  ? 53.949 49.124  11.057  1.00 11.61 ? 195  VAL A N   1 
ATOM   1466 C  CA  . VAL A 1 195  ? 52.673 48.438  10.849  1.00 12.05 ? 195  VAL A CA  1 
ATOM   1467 C  C   . VAL A 1 195  ? 52.095 48.861  9.506   1.00 10.74 ? 195  VAL A C   1 
ATOM   1468 O  O   . VAL A 1 195  ? 52.362 49.973  9.043   1.00 10.39 ? 195  VAL A O   1 
ATOM   1469 C  CB  . VAL A 1 195  ? 51.632 48.804  11.940  1.00 12.54 ? 195  VAL A CB  1 
ATOM   1470 C  CG1 . VAL A 1 195  ? 51.976 48.242  13.341  1.00 16.88 ? 195  VAL A CG1 1 
ATOM   1471 C  CG2 . VAL A 1 195  ? 51.350 50.277  11.986  1.00 13.74 ? 195  VAL A CG2 1 
ATOM   1472 N  N   . THR A 1 196  ? 51.316 47.966  8.917   1.00 10.13 ? 196  THR A N   1 
ATOM   1473 C  CA  . THR A 1 196  ? 50.594 48.242  7.662   1.00 10.60 ? 196  THR A CA  1 
ATOM   1474 C  C   . THR A 1 196  ? 49.162 47.745  7.847   1.00 10.42 ? 196  THR A C   1 
ATOM   1475 O  O   . THR A 1 196  ? 48.939 46.535  7.913   1.00 10.80 ? 196  THR A O   1 
ATOM   1476 C  CB  . THR A 1 196  ? 51.250 47.506  6.475   1.00 11.65 ? 196  THR A CB  1 
ATOM   1477 O  OG1 . THR A 1 196  ? 52.622 47.938  6.312   1.00 12.92 ? 196  THR A OG1 1 
ATOM   1478 C  CG2 . THR A 1 196  ? 50.540 47.848  5.172   1.00 13.62 ? 196  THR A CG2 1 
ATOM   1479 N  N   . PRO A 1 197  ? 48.202 48.662  7.964   1.00 9.54  ? 197  PRO A N   1 
ATOM   1480 C  CA  . PRO A 1 197  ? 46.802 48.280  8.140   1.00 8.85  ? 197  PRO A CA  1 
ATOM   1481 C  C   . PRO A 1 197  ? 46.301 47.403  7.013   1.00 9.51  ? 197  PRO A C   1 
ATOM   1482 O  O   . PRO A 1 197  ? 46.673 47.628  5.835   1.00 9.15  ? 197  PRO A O   1 
ATOM   1483 C  CB  . PRO A 1 197  ? 46.077 49.633  8.104   1.00 9.67  ? 197  PRO A CB  1 
ATOM   1484 C  CG  . PRO A 1 197  ? 47.123 50.619  8.612   1.00 10.13 ? 197  PRO A CG  1 
ATOM   1485 C  CD  . PRO A 1 197  ? 48.402 50.117  8.062   1.00 10.05 ? 197  PRO A CD  1 
ATOM   1486 N  N   . THR A 1 198  ? 45.439 46.440  7.347   1.00 8.20  ? 198  THR A N   1 
ATOM   1487 C  CA  . THR A 1 198  ? 44.764 45.609  6.340   1.00 9.05  ? 198  THR A CA  1 
ATOM   1488 C  C   . THR A 1 198  ? 43.256 45.740  6.449   1.00 7.49  ? 198  THR A C   1 
ATOM   1489 O  O   . THR A 1 198  ? 42.536 45.028  5.724   1.00 7.75  ? 198  THR A O   1 
ATOM   1490 C  CB  . THR A 1 198  ? 45.140 44.117  6.475   1.00 10.22 ? 198  THR A CB  1 
ATOM   1491 O  OG1 . THR A 1 198  ? 44.750 43.698  7.789   1.00 11.88 ? 198  THR A OG1 1 
ATOM   1492 C  CG2 . THR A 1 198  ? 46.657 43.911  6.351   1.00 12.09 ? 198  THR A CG2 1 
ATOM   1493 N  N   . ALA A 1 199  ? 42.784 46.618  7.337   1.00 7.49  ? 199  ALA A N   1 
ATOM   1494 C  CA  . ALA A 1 199  ? 41.349 46.946  7.455   1.00 7.55  ? 199  ALA A CA  1 
ATOM   1495 C  C   . ALA A 1 199  ? 41.196 48.440  7.217   1.00 7.83  ? 199  ALA A C   1 
ATOM   1496 O  O   . ALA A 1 199  ? 41.965 49.236  7.770   1.00 7.55  ? 199  ALA A O   1 
ATOM   1497 C  CB  . ALA A 1 199  ? 40.843 46.590  8.882   1.00 8.57  ? 199  ALA A CB  1 
ATOM   1498 N  N   . SER A 1 200  ? 40.228 48.803  6.395   1.00 7.92  ? 200  SER A N   1 
ATOM   1499 C  CA  . SER A 1 200  ? 39.942 50.188  6.058   1.00 7.92  ? 200  SER A CA  1 
ATOM   1500 C  C   . SER A 1 200  ? 38.690 50.674  6.767   1.00 7.48  ? 200  SER A C   1 
ATOM   1501 O  O   . SER A 1 200  ? 37.720 49.901  6.923   1.00 8.23  ? 200  SER A O   1 
ATOM   1502 C  CB  . SER A 1 200  ? 39.788 50.315  4.542   1.00 8.98  ? 200  SER A CB  1 
ATOM   1503 O  OG  . SER A 1 200  ? 39.544 51.683  4.180   1.00 11.11 ? 200  SER A OG  1 
ATOM   1504 N  N   . TRP A 1 201  ? 38.686 51.943  7.150   1.00 7.58  ? 201  TRP A N   1 
ATOM   1505 C  CA  . TRP A 1 201  ? 37.581 52.617  7.857   1.00 7.37  ? 201  TRP A CA  1 
ATOM   1506 C  C   . TRP A 1 201  ? 37.227 53.903  7.103   1.00 7.39  ? 201  TRP A C   1 
ATOM   1507 O  O   . TRP A 1 201  ? 37.999 54.846  7.103   1.00 8.71  ? 201  TRP A O   1 
ATOM   1508 C  CB  . TRP A 1 201  ? 38.110 52.952  9.263   1.00 7.59  ? 201  TRP A CB  1 
ATOM   1509 C  CG  . TRP A 1 201  ? 37.300 53.753  10.243  1.00 7.80  ? 201  TRP A CG  1 
ATOM   1510 C  CD1 . TRP A 1 201  ? 37.455 55.065  10.535  1.00 8.46  ? 201  TRP A CD1 1 
ATOM   1511 C  CD2 . TRP A 1 201  ? 36.336 53.253  11.172  1.00 8.11  ? 201  TRP A CD2 1 
ATOM   1512 N  NE1 . TRP A 1 201  ? 36.627 55.428  11.549  1.00 8.63  ? 201  TRP A NE1 1 
ATOM   1513 C  CE2 . TRP A 1 201  ? 35.922 54.338  11.962  1.00 8.71  ? 201  TRP A CE2 1 
ATOM   1514 C  CE3 . TRP A 1 201  ? 35.776 52.000  11.403  1.00 8.89  ? 201  TRP A CE3 1 
ATOM   1515 C  CZ2 . TRP A 1 201  ? 34.966 54.216  12.958  1.00 8.65  ? 201  TRP A CZ2 1 
ATOM   1516 C  CZ3 . TRP A 1 201  ? 34.819 51.880  12.397  1.00 9.64  ? 201  TRP A CZ3 1 
ATOM   1517 C  CH2 . TRP A 1 201  ? 34.436 52.980  13.170  1.00 10.26 ? 201  TRP A CH2 1 
ATOM   1518 N  N   . ALA A 1 202  ? 36.059 53.914  6.467   1.00 7.29  ? 202  ALA A N   1 
ATOM   1519 C  CA  . ALA A 1 202  ? 35.619 55.090  5.690   1.00 7.50  ? 202  ALA A CA  1 
ATOM   1520 C  C   . ALA A 1 202  ? 34.203 55.463  6.124   1.00 7.53  ? 202  ALA A C   1 
ATOM   1521 O  O   . ALA A 1 202  ? 33.218 55.125  5.488   1.00 7.83  ? 202  ALA A O   1 
ATOM   1522 C  CB  . ALA A 1 202  ? 35.712 54.832  4.191   1.00 8.27  ? 202  ALA A CB  1 
ATOM   1523 N  N   . ILE A 1 203  ? 34.123 56.171  7.240   1.00 7.31  ? 203  ILE A N   1 
ATOM   1524 C  CA  . ILE A 1 203  ? 32.842 56.490  7.850   1.00 8.03  ? 203  ILE A CA  1 
ATOM   1525 C  C   . ILE A 1 203  ? 32.210 57.750  7.295   1.00 8.36  ? 203  ILE A C   1 
ATOM   1526 O  O   . ILE A 1 203  ? 31.053 58.006  7.540   1.00 8.72  ? 203  ILE A O   1 
ATOM   1527 C  CB  . ILE A 1 203  ? 32.936 56.551  9.392   1.00 8.07  ? 203  ILE A CB  1 
ATOM   1528 C  CG1 . ILE A 1 203  ? 34.042 57.517  9.847   1.00 8.73  ? 203  ILE A CG1 1 
ATOM   1529 C  CG2 . ILE A 1 203  ? 33.199 55.150  9.936   1.00 9.46  ? 203  ILE A CG2 1 
ATOM   1530 C  CD1 . ILE A 1 203  ? 33.997 57.897  11.325  1.00 8.92  ? 203  ILE A CD1 1 
ATOM   1531 N  N   . ALA A 1 204  ? 32.982 58.523  6.541   1.00 7.49  ? 204  ALA A N   1 
ATOM   1532 C  CA  . ALA A 1 204  ? 32.594 59.902  6.247   1.00 7.71  ? 204  ALA A CA  1 
ATOM   1533 C  C   . ALA A 1 204  ? 32.436 60.366  4.785   1.00 7.26  ? 204  ALA A C   1 
ATOM   1534 O  O   . ALA A 1 204  ? 31.748 61.338  4.563   1.00 8.79  ? 204  ALA A O   1 
ATOM   1535 C  CB  . ALA A 1 204  ? 33.453 60.879  7.016   1.00 9.13  ? 204  ALA A CB  1 
ATOM   1536 N  N   . PRO A 1 205  ? 33.067 59.719  3.804   1.00 7.22  ? 205  PRO A N   1 
ATOM   1537 C  CA  . PRO A 1 205  ? 32.885 60.206  2.424   1.00 8.14  ? 205  PRO A CA  1 
ATOM   1538 C  C   . PRO A 1 205  ? 31.431 60.158  1.980   1.00 8.09  ? 205  PRO A C   1 
ATOM   1539 O  O   . PRO A 1 205  ? 30.680 59.336  2.491   1.00 8.00  ? 205  PRO A O   1 
ATOM   1540 C  CB  . PRO A 1 205  ? 33.722 59.236  1.585   1.00 8.91  ? 205  PRO A CB  1 
ATOM   1541 C  CG  . PRO A 1 205  ? 34.757 58.725  2.531   1.00 12.05 ? 205  PRO A CG  1 
ATOM   1542 C  CD  . PRO A 1 205  ? 34.012 58.591  3.841   1.00 8.20  ? 205  PRO A CD  1 
ATOM   1543 N  N   . PHE A 1 206  ? 31.036 61.047  1.064   1.00 7.05  ? 206  PHE A N   1 
ATOM   1544 C  CA  . PHE A 1 206  ? 29.596 61.257  0.828   1.00 7.69  ? 206  PHE A CA  1 
ATOM   1545 C  C   . PHE A 1 206  ? 29.125 60.333  -0.306  1.00 7.54  ? 206  PHE A C   1 
ATOM   1546 O  O   . PHE A 1 206  ? 28.932 60.732  -1.471  1.00 7.69  ? 206  PHE A O   1 
ATOM   1547 C  CB  . PHE A 1 206  ? 29.300 62.726  0.529   1.00 7.59  ? 206  PHE A CB  1 
ATOM   1548 C  CG  . PHE A 1 206  ? 30.117 63.710  1.351   1.00 7.44  ? 206  PHE A CG  1 
ATOM   1549 C  CD1 . PHE A 1 206  ? 30.375 63.481  2.686   1.00 8.27  ? 206  PHE A CD1 1 
ATOM   1550 C  CD2 . PHE A 1 206  ? 30.647 64.860  0.745   1.00 7.19  ? 206  PHE A CD2 1 
ATOM   1551 C  CE1 . PHE A 1 206  ? 31.144 64.380  3.414   1.00 8.11  ? 206  PHE A CE1 1 
ATOM   1552 C  CE2 . PHE A 1 206  ? 31.422 65.756  1.475   1.00 7.55  ? 206  PHE A CE2 1 
ATOM   1553 C  CZ  . PHE A 1 206  ? 31.642 65.525  2.799   1.00 7.33  ? 206  PHE A CZ  1 
ATOM   1554 N  N   . GLY A 1 207  ? 28.970 59.064  0.040   1.00 7.16  ? 207  GLY A N   1 
ATOM   1555 C  CA  . GLY A 1 207  ? 28.811 57.997  -0.937  1.00 6.97  ? 207  GLY A CA  1 
ATOM   1556 C  C   . GLY A 1 207  ? 30.133 57.286  -1.175  1.00 6.99  ? 207  GLY A C   1 
ATOM   1557 O  O   . GLY A 1 207  ? 31.224 57.837  -0.847  1.00 7.42  ? 207  GLY A O   1 
ATOM   1558 N  N   . HIS A 1 208  ? 30.087 56.084  -1.751  1.00 6.69  ? 208  HIS A N   1 
ATOM   1559 C  CA  . HIS A 1 208  ? 31.262 55.211  -1.816  1.00 6.49  ? 208  HIS A CA  1 
ATOM   1560 C  C   . HIS A 1 208  ? 31.455 54.585  -3.175  1.00 6.55  ? 208  HIS A C   1 
ATOM   1561 O  O   . HIS A 1 208  ? 30.474 54.256  -3.884  1.00 7.36  ? 208  HIS A O   1 
ATOM   1562 C  CB  . HIS A 1 208  ? 31.152 54.101  -0.749  1.00 7.68  ? 208  HIS A CB  1 
ATOM   1563 C  CG  . HIS A 1 208  ? 31.200 54.604  0.666   1.00 6.59  ? 208  HIS A CG  1 
ATOM   1564 N  ND1 . HIS A 1 208  ? 32.384 54.895  1.307   1.00 9.06  ? 208  HIS A ND1 1 
ATOM   1565 C  CD2 . HIS A 1 208  ? 30.204 54.904  1.534   1.00 8.60  ? 208  HIS A CD2 1 
ATOM   1566 C  CE1 . HIS A 1 208  ? 32.098 55.334  2.529   1.00 9.00  ? 208  HIS A CE1 1 
ATOM   1567 N  NE2 . HIS A 1 208  ? 30.794 55.350  2.694   1.00 10.56 ? 208  HIS A NE2 1 
ATOM   1568 N  N   . SER A 1 209  ? 32.717 54.464  -3.569  1.00 6.77  ? 209  SER A N   1 
ATOM   1569 C  CA  . SER A 1 209  ? 33.103 53.988  -4.879  1.00 6.02  ? 209  SER A CA  1 
ATOM   1570 C  C   . SER A 1 209  ? 33.803 52.632  -4.816  1.00 6.62  ? 209  SER A C   1 
ATOM   1571 O  O   . SER A 1 209  ? 34.641 52.405  -3.939  1.00 6.94  ? 209  SER A O   1 
ATOM   1572 C  CB  . SER A 1 209  ? 34.110 54.979  -5.482  1.00 7.17  ? 209  SER A CB  1 
ATOM   1573 O  OG  . SER A 1 209  ? 34.597 54.471  -6.702  1.00 6.70  ? 209  SER A OG  1 
ATOM   1574 N  N   . PRO A 1 210  ? 33.570 51.739  -5.789  1.00 6.17  ? 210  PRO A N   1 
ATOM   1575 C  CA  . PRO A 1 210  ? 34.292 50.461  -5.866  1.00 6.82  ? 210  PRO A CA  1 
ATOM   1576 C  C   . PRO A 1 210  ? 35.756 50.650  -6.212  1.00 6.84  ? 210  PRO A C   1 
ATOM   1577 O  O   . PRO A 1 210  ? 36.536 49.676  -6.141  1.00 6.84  ? 210  PRO A O   1 
ATOM   1578 C  CB  . PRO A 1 210  ? 33.538 49.683  -6.963  1.00 7.56  ? 210  PRO A CB  1 
ATOM   1579 C  CG  . PRO A 1 210  ? 32.994 50.786  -7.838  1.00 7.84  ? 210  PRO A CG  1 
ATOM   1580 C  CD  . PRO A 1 210  ? 32.572 51.860  -6.869  1.00 6.56  ? 210  PRO A CD  1 
ATOM   1581 N  N   . THR A 1 211  ? 36.177 51.872  -6.573  1.00 6.57  ? 211  THR A N   1 
ATOM   1582 C  CA  . THR A 1 211  ? 37.605 52.093  -6.726  1.00 7.35  ? 211  THR A CA  1 
ATOM   1583 C  C   . THR A 1 211  ? 38.357 51.849  -5.440  1.00 6.86  ? 211  THR A C   1 
ATOM   1584 O  O   . THR A 1 211  ? 39.531 51.455  -5.492  1.00 7.35  ? 211  THR A O   1 
ATOM   1585 C  CB  . THR A 1 211  ? 37.815 53.530  -7.211  1.00 7.35  ? 211  THR A CB  1 
ATOM   1586 O  OG1 . THR A 1 211  ? 37.280 53.575  -8.536  1.00 7.99  ? 211  THR A OG1 1 
ATOM   1587 C  CG2 . THR A 1 211  ? 39.325 53.902  -7.293  1.00 8.99  ? 211  THR A CG2 1 
ATOM   1588 N  N   . MET A 1 212  ? 37.730 52.113  -4.305  1.00 5.92  ? 212  MET A N   1 
ATOM   1589 C  CA  . MET A 1 212  ? 38.367 51.852  -3.029  1.00 6.95  ? 212  MET A CA  1 
ATOM   1590 C  C   . MET A 1 212  ? 38.730 50.373  -2.807  1.00 7.45  ? 212  MET A C   1 
ATOM   1591 O  O   . MET A 1 212  ? 39.891 50.090  -2.608  1.00 7.07  ? 212  MET A O   1 
ATOM   1592 C  CB  . MET A 1 212  ? 37.540 52.425  -1.886  1.00 7.76  ? 212  MET A CB  1 
ATOM   1593 C  CG  . MET A 1 212  ? 37.304 53.927  -2.001  1.00 10.13 ? 212  MET A CG  1 
ATOM   1594 S  SD  . MET A 1 212  ? 38.823 54.911  -2.223  1.00 13.41 ? 212  MET A SD  1 
ATOM   1595 C  CE  . MET A 1 212  ? 39.580 54.785  -0.630  1.00 14.48 ? 212  MET A CE  1 
ATOM   1596 N  N   . PRO A 1 213  ? 37.782 49.433  -2.853  1.00 7.15  ? 213  PRO A N   1 
ATOM   1597 C  CA  . PRO A 1 213  ? 38.204 48.028  -2.701  1.00 7.04  ? 213  PRO A CA  1 
ATOM   1598 C  C   . PRO A 1 213  ? 39.162 47.631  -3.815  1.00 7.19  ? 213  PRO A C   1 
ATOM   1599 O  O   . PRO A 1 213  ? 40.043 46.790  -3.575  1.00 7.84  ? 213  PRO A O   1 
ATOM   1600 C  CB  . PRO A 1 213  ? 36.878 47.222  -2.770  1.00 8.38  ? 213  PRO A CB  1 
ATOM   1601 C  CG  . PRO A 1 213  ? 35.854 48.195  -3.382  1.00 7.62  ? 213  PRO A CG  1 
ATOM   1602 C  CD  . PRO A 1 213  ? 36.298 49.566  -2.884  1.00 7.25  ? 213  PRO A CD  1 
ATOM   1603 N  N   . TYR A 1 214  ? 39.050 48.186  -5.032  1.00 7.45  ? 214  TYR A N   1 
ATOM   1604 C  CA  . TYR A 1 214  ? 40.003 47.833  -6.095  1.00 7.49  ? 214  TYR A CA  1 
ATOM   1605 C  C   . TYR A 1 214  ? 41.436 48.117  -5.643  1.00 7.80  ? 214  TYR A C   1 
ATOM   1606 O  O   . TYR A 1 214  ? 42.314 47.241  -5.719  1.00 7.94  ? 214  TYR A O   1 
ATOM   1607 C  CB  . TYR A 1 214  ? 39.702 48.657  -7.336  1.00 8.19  ? 214  TYR A CB  1 
ATOM   1608 C  CG  . TYR A 1 214  ? 40.621 48.446  -8.518  1.00 8.72  ? 214  TYR A CG  1 
ATOM   1609 C  CD1 . TYR A 1 214  ? 40.334 47.451  -9.454  1.00 14.82 ? 214  TYR A CD1 1 
ATOM   1610 C  CD2 . TYR A 1 214  ? 41.722 49.261  -8.739  1.00 9.11  ? 214  TYR A CD2 1 
ATOM   1611 C  CE1 . TYR A 1 214  ? 41.158 47.265  -10.586 1.00 14.77 ? 214  TYR A CE1 1 
ATOM   1612 C  CE2 . TYR A 1 214  ? 42.535 49.082  -9.845  1.00 9.64  ? 214  TYR A CE2 1 
ATOM   1613 C  CZ  . TYR A 1 214  ? 42.221 48.113  -10.770 1.00 12.08 ? 214  TYR A CZ  1 
ATOM   1614 O  OH  . TYR A 1 214  ? 42.996 47.932  -11.895 1.00 13.11 ? 214  TYR A OH  1 
ATOM   1615 N  N   . ILE A 1 215  ? 41.686 49.344  -5.189  1.00 6.97  ? 215  ILE A N   1 
ATOM   1616 C  CA  . ILE A 1 215  ? 43.034 49.759  -4.781  1.00 6.64  ? 215  ILE A CA  1 
ATOM   1617 C  C   . ILE A 1 215  ? 43.436 49.029  -3.485  1.00 7.35  ? 215  ILE A C   1 
ATOM   1618 O  O   . ILE A 1 215  ? 44.562 48.538  -3.347  1.00 7.93  ? 215  ILE A O   1 
ATOM   1619 C  CB  . ILE A 1 215  ? 43.102 51.270  -4.578  1.00 7.72  ? 215  ILE A CB  1 
ATOM   1620 C  CG1 . ILE A 1 215  ? 42.932 52.011  -5.909  1.00 8.15  ? 215  ILE A CG1 1 
ATOM   1621 C  CG2 . ILE A 1 215  ? 44.422 51.666  -3.843  1.00 8.31  ? 215  ILE A CG2 1 
ATOM   1622 C  CD1 . ILE A 1 215  ? 42.789 53.520  -5.742  1.00 11.13 ? 215  ILE A CD1 1 
ATOM   1623 N  N   . LEU A 1 216  ? 42.512 48.951  -2.528  1.00 6.46  ? 216  LEU A N   1 
ATOM   1624 C  CA  . LEU A 1 216  ? 42.836 48.340  -1.240  1.00 6.68  ? 216  LEU A CA  1 
ATOM   1625 C  C   . LEU A 1 216  ? 43.170 46.862  -1.392  1.00 7.28  ? 216  LEU A C   1 
ATOM   1626 O  O   . LEU A 1 216  ? 44.172 46.423  -0.802  1.00 7.36  ? 216  LEU A O   1 
ATOM   1627 C  CB  . LEU A 1 216  ? 41.682 48.518  -0.270  1.00 6.42  ? 216  LEU A CB  1 
ATOM   1628 C  CG  . LEU A 1 216  ? 41.300 49.932  0.146   1.00 7.09  ? 216  LEU A CG  1 
ATOM   1629 C  CD1 . LEU A 1 216  ? 40.017 49.907  0.893   1.00 8.62  ? 216  LEU A CD1 1 
ATOM   1630 C  CD2 . LEU A 1 216  ? 42.427 50.580  0.991   1.00 9.15  ? 216  LEU A CD2 1 
ATOM   1631 N  N   . GLN A 1 217  ? 42.406 46.107  -2.170  1.00 7.69  ? 217  GLN A N   1 
ATOM   1632 C  CA  . GLN A 1 217  ? 42.687 44.688  -2.323  1.00 8.45  ? 217  GLN A CA  1 
ATOM   1633 C  C   . GLN A 1 217  ? 44.056 44.465  -3.005  1.00 8.98  ? 217  GLN A C   1 
ATOM   1634 O  O   . GLN A 1 217  ? 44.711 43.457  -2.724  1.00 11.07 ? 217  GLN A O   1 
ATOM   1635 C  CB  . GLN A 1 217  ? 41.506 44.065  -3.059  1.00 9.98  ? 217  GLN A CB  1 
ATOM   1636 C  CG  . GLN A 1 217  ? 41.549 42.539  -3.086  1.00 10.92 ? 217  GLN A CG  1 
ATOM   1637 C  CD  . GLN A 1 217  ? 42.376 41.971  -4.226  1.00 16.28 ? 217  GLN A CD  1 
ATOM   1638 O  OE1 . GLN A 1 217  ? 42.510 42.599  -5.279  1.00 16.27 ? 217  GLN A OE1 1 
ATOM   1639 N  NE2 . GLN A 1 217  ? 42.908 40.746  -4.034  1.00 16.95 ? 217  GLN A NE2 1 
ATOM   1640 N  N   . LYS A 1 218  ? 44.519 45.391  -3.847  1.00 7.93  ? 218  LYS A N   1 
ATOM   1641 C  CA  . LYS A 1 218  ? 45.834 45.287  -4.484  1.00 7.79  ? 218  LYS A CA  1 
ATOM   1642 C  C   . LYS A 1 218  ? 46.935 45.912  -3.623  1.00 7.61  ? 218  LYS A C   1 
ATOM   1643 O  O   . LYS A 1 218  ? 48.095 45.983  -4.044  1.00 7.92  ? 218  LYS A O   1 
ATOM   1644 C  CB  . LYS A 1 218  ? 45.746 46.006  -5.824  1.00 8.40  ? 218  LYS A CB  1 
ATOM   1645 C  CG  . LYS A 1 218  ? 44.940 45.204  -6.855  1.00 9.74  ? 218  LYS A CG  1 
ATOM   1646 C  CD  . LYS A 1 218  ? 44.705 46.042  -8.138  1.00 9.50  ? 218  LYS A CD  1 
ATOM   1647 C  CE  . LYS A 1 218  ? 44.264 45.226  -9.332  1.00 14.67 ? 218  LYS A CE  1 
ATOM   1648 N  NZ  . LYS A 1 218  ? 43.133 44.288  -9.124  1.00 14.95 ? 218  LYS A NZ  1 
ATOM   1649 N  N   . SER A 1 219  ? 46.574 46.372  -2.432  1.00 7.31  ? 219  SER A N   1 
ATOM   1650 C  CA  . SER A 1 219  ? 47.481 46.972  -1.457  1.00 7.58  ? 219  SER A CA  1 
ATOM   1651 C  C   . SER A 1 219  ? 47.489 46.188  -0.136  1.00 7.64  ? 219  SER A C   1 
ATOM   1652 O  O   . SER A 1 219  ? 47.853 46.729  0.895   1.00 8.78  ? 219  SER A O   1 
ATOM   1653 C  CB  . SER A 1 219  ? 47.136 48.449  -1.195  1.00 8.20  ? 219  SER A CB  1 
ATOM   1654 O  OG  . SER A 1 219  ? 47.132 49.160  -2.441  1.00 8.30  ? 219  SER A OG  1 
ATOM   1655 N  N   . GLY A 1 220  ? 47.132 44.904  -0.209  1.00 8.04  ? 220  GLY A N   1 
ATOM   1656 C  CA  . GLY A 1 220  ? 47.234 43.975  0.921   1.00 9.63  ? 220  GLY A CA  1 
ATOM   1657 C  C   . GLY A 1 220  ? 46.026 43.944  1.855   1.00 9.02  ? 220  GLY A C   1 
ATOM   1658 O  O   . GLY A 1 220  ? 46.030 43.205  2.846   1.00 10.40 ? 220  GLY A O   1 
ATOM   1659 N  N   . PHE A 1 221  ? 44.985 44.741  1.597   1.00 8.01  ? 221  PHE A N   1 
ATOM   1660 C  CA  . PHE A 1 221  ? 43.836 44.768  2.516   1.00 7.75  ? 221  PHE A CA  1 
ATOM   1661 C  C   . PHE A 1 221  ? 43.012 43.508  2.438   1.00 8.32  ? 221  PHE A C   1 
ATOM   1662 O  O   . PHE A 1 221  ? 42.909 42.873  1.377   1.00 9.05  ? 221  PHE A O   1 
ATOM   1663 C  CB  . PHE A 1 221  ? 42.933 45.998  2.281   1.00 7.66  ? 221  PHE A CB  1 
ATOM   1664 C  CG  . PHE A 1 221  ? 43.521 47.265  2.814   1.00 6.88  ? 221  PHE A CG  1 
ATOM   1665 C  CD1 . PHE A 1 221  ? 44.622 47.876  2.212   1.00 7.60  ? 221  PHE A CD1 1 
ATOM   1666 C  CD2 . PHE A 1 221  ? 42.937 47.869  3.927   1.00 7.15  ? 221  PHE A CD2 1 
ATOM   1667 C  CE1 . PHE A 1 221  ? 45.149 49.043  2.742   1.00 6.96  ? 221  PHE A CE1 1 
ATOM   1668 C  CE2 . PHE A 1 221  ? 43.442 49.020  4.444   1.00 7.11  ? 221  PHE A CE2 1 
ATOM   1669 C  CZ  . PHE A 1 221  ? 44.548 49.635  3.859   1.00 7.44  ? 221  PHE A CZ  1 
ATOM   1670 N  N   . LYS A 1 222  ? 42.350 43.233  3.553   1.00 8.56  ? 222  LYS A N   1 
ATOM   1671 C  CA  . LYS A 1 222  ? 41.475 42.081  3.665   1.00 9.29  ? 222  LYS A CA  1 
ATOM   1672 C  C   . LYS A 1 222  ? 40.062 42.484  4.041   1.00 9.05  ? 222  LYS A C   1 
ATOM   1673 O  O   . LYS A 1 222  ? 39.159 41.688  3.870   1.00 9.36  ? 222  LYS A O   1 
ATOM   1674 C  CB  . LYS A 1 222  ? 41.998 41.088  4.713   1.00 11.96 ? 222  LYS A CB  1 
ATOM   1675 C  CG  . LYS A 1 222  ? 43.419 40.625  4.502   1.00 14.81 ? 222  LYS A CG  1 
ATOM   1676 C  CD  . LYS A 1 222  ? 43.650 39.901  3.219   1.00 21.33 ? 222  LYS A CD  1 
ATOM   1677 C  CE  . LYS A 1 222  ? 45.030 39.251  3.277   1.00 26.17 ? 222  LYS A CE  1 
ATOM   1678 N  NZ  . LYS A 1 222  ? 45.284 38.364  2.123   1.00 30.30 ? 222  LYS A NZ  1 
ATOM   1679 N  N   . ASN A 1 223  ? 39.844 43.696  4.549   1.00 7.26  ? 223  ASN A N   1 
ATOM   1680 C  CA  . ASN A 1 223  ? 38.510 44.112  5.011   1.00 7.97  ? 223  ASN A CA  1 
ATOM   1681 C  C   . ASN A 1 223  ? 38.340 45.608  4.871   1.00 7.12  ? 223  ASN A C   1 
ATOM   1682 O  O   . ASN A 1 223  ? 39.292 46.347  4.982   1.00 7.26  ? 223  ASN A O   1 
ATOM   1683 C  CB  . ASN A 1 223  ? 38.300 43.747  6.486   1.00 8.56  ? 223  ASN A CB  1 
ATOM   1684 C  CG  . ASN A 1 223  ? 38.294 42.250  6.732   1.00 9.93  ? 223  ASN A CG  1 
ATOM   1685 O  OD1 . ASN A 1 223  ? 37.318 41.581  6.452   1.00 12.03 ? 223  ASN A OD1 1 
ATOM   1686 N  ND2 . ASN A 1 223  ? 39.388 41.736  7.250   1.00 8.37  ? 223  ASN A ND2 1 
ATOM   1687 N  N   . MET A 1 224  ? 37.106 46.040  4.679   1.00 6.99  ? 224  MET A N   1 
ATOM   1688 C  CA  . MET A 1 224  ? 36.812 47.476  4.695   1.00 7.25  ? 224  MET A CA  1 
ATOM   1689 C  C   . MET A 1 224  ? 35.428 47.777  5.239   1.00 7.44  ? 224  MET A C   1 
ATOM   1690 O  O   . MET A 1 224  ? 34.556 46.922  5.219   1.00 7.90  ? 224  MET A O   1 
ATOM   1691 C  CB  . MET A 1 224  ? 36.966 48.069  3.295   1.00 8.76  ? 224  MET A CB  1 
ATOM   1692 C  CG  . MET A 1 224  ? 35.958 47.533  2.283   1.00 8.71  ? 224  MET A CG  1 
ATOM   1693 S  SD  . MET A 1 224  ? 36.139 48.368  0.673   1.00 10.15 ? 224  MET A SD  1 
ATOM   1694 C  CE  . MET A 1 224  ? 35.666 50.019  1.099   1.00 13.95 ? 224  MET A CE  1 
ATOM   1695 N  N   . LEU A 1 225  ? 35.257 49.008  5.714   1.00 7.16  ? 225  LEU A N   1 
ATOM   1696 C  CA  . LEU A 1 225  ? 34.006 49.439  6.334   1.00 7.15  ? 225  LEU A CA  1 
ATOM   1697 C  C   . LEU A 1 225  ? 33.591 50.738  5.671   1.00 7.73  ? 225  LEU A C   1 
ATOM   1698 O  O   . LEU A 1 225  ? 34.438 51.650  5.464   1.00 7.32  ? 225  LEU A O   1 
ATOM   1699 C  CB  . LEU A 1 225  ? 34.188 49.632  7.838   1.00 7.86  ? 225  LEU A CB  1 
ATOM   1700 C  CG  . LEU A 1 225  ? 32.979 50.191  8.584   1.00 8.28  ? 225  LEU A CG  1 
ATOM   1701 C  CD1 . LEU A 1 225  ? 32.892 49.581  10.003  1.00 9.30  ? 225  LEU A CD1 1 
ATOM   1702 C  CD2 . LEU A 1 225  ? 33.033 51.727  8.605   1.00 8.48  ? 225  LEU A CD2 1 
ATOM   1703 N  N   . ILE A 1 226  ? 32.303 50.847  5.368   1.00 7.11  ? 226  ILE A N   1 
ATOM   1704 C  CA  . ILE A 1 226  ? 31.709 52.079  4.820   1.00 8.18  ? 226  ILE A CA  1 
ATOM   1705 C  C   . ILE A 1 226  ? 30.458 52.446  5.595   1.00 7.18  ? 226  ILE A C   1 
ATOM   1706 O  O   . ILE A 1 226  ? 29.903 51.623  6.337   1.00 8.21  ? 226  ILE A O   1 
ATOM   1707 C  CB  . ILE A 1 226  ? 31.395 51.882  3.296   1.00 7.98  ? 226  ILE A CB  1 
ATOM   1708 C  CG1 . ILE A 1 226  ? 30.338 50.792  3.100   1.00 8.20  ? 226  ILE A CG1 1 
ATOM   1709 C  CG2 . ILE A 1 226  ? 32.700 51.602  2.555   1.00 8.66  ? 226  ILE A CG2 1 
ATOM   1710 C  CD1 . ILE A 1 226  ? 29.907 50.607  1.606   1.00 9.64  ? 226  ILE A CD1 1 
ATOM   1711 N  N   . GLN A 1 227  ? 29.991 53.680  5.431   1.00 8.06  ? 227  GLN A N   1 
ATOM   1712 C  CA  . GLN A 1 227  ? 28.845 54.192  6.181   1.00 8.00  ? 227  GLN A CA  1 
ATOM   1713 C  C   . GLN A 1 227  ? 27.882 55.036  5.367   1.00 8.79  ? 227  GLN A C   1 
ATOM   1714 O  O   . GLN A 1 227  ? 26.674 54.910  5.586   1.00 9.08  ? 227  GLN A O   1 
ATOM   1715 C  CB  . GLN A 1 227  ? 29.376 55.039  7.356   1.00 8.92  ? 227  GLN A CB  1 
ATOM   1716 C  CG  . GLN A 1 227  ? 28.406 56.140  7.952   1.00 11.23 ? 227  GLN A CG  1 
ATOM   1717 C  CD  . GLN A 1 227  ? 27.067 55.631  8.493   1.00 10.19 ? 227  GLN A CD  1 
ATOM   1718 O  OE1 . GLN A 1 227  ? 26.931 54.462  8.864   1.00 12.19 ? 227  GLN A OE1 1 
ATOM   1719 N  NE2 . GLN A 1 227  ? 26.093 56.515  8.530   1.00 11.49 ? 227  GLN A NE2 1 
ATOM   1720 N  N   . ARG A 1 228  ? 28.334 55.955  4.532   1.00 8.64  ? 228  ARG A N   1 
ATOM   1721 C  CA  A ARG A 1 228  ? 27.411 56.928  3.966   0.50 8.93  ? 228  ARG A CA  1 
ATOM   1722 C  CA  B ARG A 1 228  ? 27.407 56.921  3.966   0.50 8.83  ? 228  ARG A CA  1 
ATOM   1723 C  C   . ARG A 1 228  ? 26.847 56.400  2.673   1.00 8.92  ? 228  ARG A C   1 
ATOM   1724 O  O   . ARG A 1 228  ? 27.354 56.671  1.590   1.00 9.10  ? 228  ARG A O   1 
ATOM   1725 C  CB  A ARG A 1 228  ? 28.086 58.291  3.773   0.50 9.54  ? 228  ARG A CB  1 
ATOM   1726 C  CB  B ARG A 1 228  ? 28.066 58.292  3.807   0.50 9.44  ? 228  ARG A CB  1 
ATOM   1727 C  CG  A ARG A 1 228  ? 28.195 59.105  5.032   0.50 10.44 ? 228  ARG A CG  1 
ATOM   1728 C  CG  B ARG A 1 228  ? 28.060 59.058  5.082   0.50 9.82  ? 228  ARG A CG  1 
ATOM   1729 C  CD  A ARG A 1 228  ? 28.426 60.582  4.728   0.50 11.14 ? 228  ARG A CD  1 
ATOM   1730 C  CD  B ARG A 1 228  ? 28.588 60.456  4.929   0.50 11.00 ? 228  ARG A CD  1 
ATOM   1731 N  NE  A ARG A 1 228  ? 28.749 61.387  5.911   0.50 13.70 ? 228  ARG A NE  1 
ATOM   1732 N  NE  B ARG A 1 228  ? 27.870 61.380  5.792   0.50 10.61 ? 228  ARG A NE  1 
ATOM   1733 C  CZ  A ARG A 1 228  ? 27.863 62.083  6.614   0.50 14.15 ? 228  ARG A CZ  1 
ATOM   1734 C  CZ  B ARG A 1 228  ? 28.434 62.394  6.418   0.50 10.63 ? 228  ARG A CZ  1 
ATOM   1735 N  NH1 A ARG A 1 228  ? 26.577 62.038  6.289   0.50 16.01 ? 228  ARG A NH1 1 
ATOM   1736 N  NH1 B ARG A 1 228  ? 29.736 62.599  6.301   0.50 9.30  ? 228  ARG A NH1 1 
ATOM   1737 N  NH2 A ARG A 1 228  ? 28.256 62.813  7.664   0.50 14.97 ? 228  ARG A NH2 1 
ATOM   1738 N  NH2 B ARG A 1 228  ? 27.690 63.201  7.174   0.50 10.03 ? 228  ARG A NH2 1 
ATOM   1739 N  N   . THR A 1 229  ? 25.799 55.597  2.806   1.00 8.86  ? 229  THR A N   1 
ATOM   1740 C  CA  . THR A 1 229  ? 25.047 55.103  1.681   1.00 8.46  ? 229  THR A CA  1 
ATOM   1741 C  C   . THR A 1 229  ? 23.591 55.512  1.885   1.00 7.71  ? 229  THR A C   1 
ATOM   1742 O  O   . THR A 1 229  ? 23.110 55.788  2.992   1.00 8.77  ? 229  THR A O   1 
ATOM   1743 C  CB  . THR A 1 229  ? 25.145 53.583  1.531   1.00 8.81  ? 229  THR A CB  1 
ATOM   1744 O  OG1 . THR A 1 229  ? 24.577 52.997  2.713   1.00 9.94  ? 229  THR A OG1 1 
ATOM   1745 C  CG2 . THR A 1 229  ? 26.629 53.151  1.492   1.00 9.35  ? 229  THR A CG2 1 
ATOM   1746 N  N   . HIS A 1 230  ? 22.907 55.575  0.756   1.00 8.26  ? 230  HIS A N   1 
ATOM   1747 C  CA  . HIS A 1 230  ? 21.501 56.019  0.735   1.00 8.80  ? 230  HIS A CA  1 
ATOM   1748 C  C   . HIS A 1 230  ? 20.675 55.272  1.771   1.00 8.72  ? 230  HIS A C   1 
ATOM   1749 O  O   . HIS A 1 230  ? 20.771 54.044  1.879   1.00 9.11  ? 230  HIS A O   1 
ATOM   1750 C  CB  . HIS A 1 230  ? 20.963 55.742  -0.665  1.00 8.69  ? 230  HIS A CB  1 
ATOM   1751 C  CG  . HIS A 1 230  ? 19.654 56.417  -1.005  1.00 9.61  ? 230  HIS A CG  1 
ATOM   1752 N  ND1 . HIS A 1 230  ? 18.474 56.161  -0.330  1.00 9.72  ? 230  HIS A ND1 1 
ATOM   1753 C  CD2 . HIS A 1 230  ? 19.344 57.307  -1.977  1.00 11.38 ? 230  HIS A CD2 1 
ATOM   1754 C  CE1 . HIS A 1 230  ? 17.507 56.900  -0.848  1.00 10.43 ? 230  HIS A CE1 1 
ATOM   1755 N  NE2 . HIS A 1 230  ? 17.997 57.585  -1.866  1.00 9.74  ? 230  HIS A NE2 1 
ATOM   1756 N  N   . TYR A 1 231  ? 19.845 56.006  2.518   1.00 8.91  ? 231  TYR A N   1 
ATOM   1757 C  CA  . TYR A 1 231  ? 19.026 55.375  3.552   1.00 9.33  ? 231  TYR A CA  1 
ATOM   1758 C  C   . TYR A 1 231  ? 18.146 54.234  3.024   1.00 9.71  ? 231  TYR A C   1 
ATOM   1759 O  O   . TYR A 1 231  ? 17.900 53.261  3.741   1.00 9.87  ? 231  TYR A O   1 
ATOM   1760 C  CB  . TYR A 1 231  ? 18.199 56.411  4.305   1.00 10.11 ? 231  TYR A CB  1 
ATOM   1761 C  CG  . TYR A 1 231  ? 17.213 57.188  3.454   1.00 9.94  ? 231  TYR A CG  1 
ATOM   1762 C  CD1 . TYR A 1 231  ? 15.907 56.705  3.259   1.00 11.35 ? 231  TYR A CD1 1 
ATOM   1763 C  CD2 . TYR A 1 231  ? 17.565 58.409  2.840   1.00 9.98  ? 231  TYR A CD2 1 
ATOM   1764 C  CE1 . TYR A 1 231  ? 14.995 57.417  2.481   1.00 11.94 ? 231  TYR A CE1 1 
ATOM   1765 C  CE2 . TYR A 1 231  ? 16.668 59.123  2.061   1.00 11.29 ? 231  TYR A CE2 1 
ATOM   1766 C  CZ  . TYR A 1 231  ? 15.366 58.621  1.883   1.00 10.73 ? 231  TYR A CZ  1 
ATOM   1767 O  OH  . TYR A 1 231  ? 14.435 59.317  1.128   1.00 12.68 ? 231  TYR A OH  1 
ATOM   1768 N  N   . SER A 1 232  ? 17.695 54.334  1.789   1.00 9.40  ? 232  SER A N   1 
ATOM   1769 C  CA  . SER A 1 232  ? 16.878 53.251  1.221   1.00 10.89 ? 232  SER A CA  1 
ATOM   1770 C  C   . SER A 1 232  ? 17.706 51.987  0.959   1.00 10.69 ? 232  SER A C   1 
ATOM   1771 O  O   . SER A 1 232  ? 17.200 50.858  1.061   1.00 11.16 ? 232  SER A O   1 
ATOM   1772 C  CB  . SER A 1 232  ? 16.200 53.691  -0.050  1.00 11.77 ? 232  SER A CB  1 
ATOM   1773 O  OG  . SER A 1 232  ? 15.304 54.745  0.173   1.00 14.40 ? 232  SER A OG  1 
ATOM   1774 N  N   . VAL A 1 233  ? 18.975 52.161  0.571   1.00 10.21 ? 233  VAL A N   1 
ATOM   1775 C  CA  . VAL A 1 233  ? 19.889 51.041  0.392   1.00 10.43 ? 233  VAL A CA  1 
ATOM   1776 C  C   . VAL A 1 233  ? 20.178 50.365  1.734   1.00 10.52 ? 233  VAL A C   1 
ATOM   1777 O  O   . VAL A 1 233  ? 20.136 49.129  1.837   1.00 10.67 ? 233  VAL A O   1 
ATOM   1778 C  CB  . VAL A 1 233  ? 21.202 51.514  -0.296  1.00 10.14 ? 233  VAL A CB  1 
ATOM   1779 C  CG1 . VAL A 1 233  ? 22.234 50.421  -0.283  1.00 10.56 ? 233  VAL A CG1 1 
ATOM   1780 C  CG2 . VAL A 1 233  ? 20.898 51.915  -1.737  1.00 11.40 ? 233  VAL A CG2 1 
ATOM   1781 N  N   . LYS A 1 234  ? 20.446 51.164  2.754   1.00 9.42  ? 234  LYS A N   1 
ATOM   1782 C  CA  . LYS A 1 234  ? 20.633 50.576  4.091   1.00 9.84  ? 234  LYS A CA  1 
ATOM   1783 C  C   . LYS A 1 234  ? 19.420 49.699  4.473   1.00 10.77 ? 234  LYS A C   1 
ATOM   1784 O  O   . LYS A 1 234  ? 19.586 48.574  4.949   1.00 10.64 ? 234  LYS A O   1 
ATOM   1785 C  CB  . LYS A 1 234  ? 20.840 51.666  5.132   1.00 9.09  ? 234  LYS A CB  1 
ATOM   1786 C  CG  . LYS A 1 234  ? 22.232 52.322  5.069   1.00 9.73  ? 234  LYS A CG  1 
ATOM   1787 C  CD  . LYS A 1 234  ? 22.265 53.600  5.850   1.00 10.66 ? 234  LYS A CD  1 
ATOM   1788 C  CE  . LYS A 1 234  ? 23.675 54.279  5.804   1.00 9.56  ? 234  LYS A CE  1 
ATOM   1789 N  NZ  . LYS A 1 234  ? 24.550 53.706  6.894   1.00 9.79  ? 234  LYS A NZ  1 
ATOM   1790 N  N   . LYS A 1 235  ? 18.211 50.229  4.289   1.00 10.24 ? 235  LYS A N   1 
ATOM   1791 C  CA  . LYS A 1 235  ? 17.000 49.457  4.653   1.00 11.65 ? 235  LYS A CA  1 
ATOM   1792 C  C   . LYS A 1 235  ? 16.904 48.173  3.851   1.00 11.08 ? 235  LYS A C   1 
ATOM   1793 O  O   . LYS A 1 235  ? 16.668 47.089  4.432   1.00 11.80 ? 235  LYS A O   1 
ATOM   1794 C  CB  . LYS A 1 235  ? 15.774 50.329  4.494   1.00 12.98 ? 235  LYS A CB  1 
ATOM   1795 C  CG  . LYS A 1 235  ? 14.475 49.622  4.968   1.00 12.70 ? 235  LYS A CG  1 
ATOM   1796 C  CD  . LYS A 1 235  ? 13.300 50.565  4.872   1.00 15.26 ? 235  LYS A CD  1 
ATOM   1797 C  CE  . LYS A 1 235  ? 11.972 49.917  5.340   1.00 15.62 ? 235  LYS A CE  1 
ATOM   1798 N  NZ  . LYS A 1 235  ? 10.838 50.877  5.186   1.00 23.60 ? 235  LYS A NZ  1 
ATOM   1799 N  N   . GLU A 1 236  ? 17.087 48.251  2.543   1.00 10.68 ? 236  GLU A N   1 
ATOM   1800 C  CA  . GLU A 1 236  ? 16.979 47.101  1.668   1.00 12.23 ? 236  GLU A CA  1 
ATOM   1801 C  C   . GLU A 1 236  ? 17.995 46.016  2.015   1.00 12.39 ? 236  GLU A C   1 
ATOM   1802 O  O   . GLU A 1 236  ? 17.674 44.834  2.121   1.00 13.05 ? 236  GLU A O   1 
ATOM   1803 C  CB  . GLU A 1 236  ? 17.156 47.564  0.213   1.00 13.77 ? 236  GLU A CB  1 
ATOM   1804 C  CG  . GLU A 1 236  ? 16.911 46.500  -0.860  1.00 18.66 ? 236  GLU A CG  1 
ATOM   1805 C  CD  . GLU A 1 236  ? 15.425 46.170  -1.051  1.00 24.85 ? 236  GLU A CD  1 
ATOM   1806 O  OE1 . GLU A 1 236  ? 14.542 46.980  -0.660  1.00 28.19 ? 236  GLU A OE1 1 
ATOM   1807 O  OE2 . GLU A 1 236  ? 15.146 45.092  -1.607  1.00 29.58 ? 236  GLU A OE2 1 
ATOM   1808 N  N   . LEU A 1 237  ? 19.256 46.398  2.171   1.00 11.12 ? 237  LEU A N   1 
ATOM   1809 C  CA  . LEU A 1 237  ? 20.286 45.428  2.480   1.00 10.72 ? 237  LEU A CA  1 
ATOM   1810 C  C   . LEU A 1 237  ? 20.094 44.906  3.906   1.00 10.27 ? 237  LEU A C   1 
ATOM   1811 O  O   . LEU A 1 237  ? 20.325 43.711  4.153   1.00 10.99 ? 237  LEU A O   1 
ATOM   1812 C  CB  . LEU A 1 237  ? 21.702 46.023  2.290   1.00 10.54 ? 237  LEU A CB  1 
ATOM   1813 C  CG  . LEU A 1 237  ? 22.057 46.445  0.848   1.00 10.86 ? 237  LEU A CG  1 
ATOM   1814 C  CD1 . LEU A 1 237  ? 23.505 46.996  0.818   1.00 12.73 ? 237  LEU A CD1 1 
ATOM   1815 C  CD2 . LEU A 1 237  ? 21.953 45.318  -0.194  1.00 14.09 ? 237  LEU A CD2 1 
ATOM   1816 N  N   . ALA A 1 238  ? 19.656 45.737  4.838   1.00 10.36 ? 238  ALA A N   1 
ATOM   1817 C  CA  . ALA A 1 238  ? 19.466 45.249  6.214   1.00 11.43 ? 238  ALA A CA  1 
ATOM   1818 C  C   . ALA A 1 238  ? 18.392 44.158  6.258   1.00 12.41 ? 238  ALA A C   1 
ATOM   1819 O  O   . ALA A 1 238  ? 18.567 43.146  6.956   1.00 12.32 ? 238  ALA A O   1 
ATOM   1820 C  CB  . ALA A 1 238  ? 19.077 46.381  7.111   1.00 11.21 ? 238  ALA A CB  1 
ATOM   1821 N  N   . GLN A 1 239  ? 17.326 44.365  5.495   1.00 12.24 ? 239  GLN A N   1 
ATOM   1822 C  CA  . GLN A 1 239  ? 16.221 43.399  5.464   1.00 14.77 ? 239  GLN A CA  1 
ATOM   1823 C  C   . GLN A 1 239  ? 16.702 42.029  5.017   1.00 15.09 ? 239  GLN A C   1 
ATOM   1824 O  O   . GLN A 1 239  ? 16.157 41.005  5.438   1.00 16.80 ? 239  GLN A O   1 
ATOM   1825 C  CB  . GLN A 1 239  ? 15.111 43.936  4.564   1.00 14.61 ? 239  GLN A CB  1 
ATOM   1826 C  CG  . GLN A 1 239  ? 14.286 45.005  5.240   1.00 17.67 ? 239  GLN A CG  1 
ATOM   1827 C  CD  . GLN A 1 239  ? 13.266 45.697  4.337   1.00 19.21 ? 239  GLN A CD  1 
ATOM   1828 O  OE1 . GLN A 1 239  ? 13.360 45.668  3.105   1.00 23.83 ? 239  GLN A OE1 1 
ATOM   1829 N  NE2 . GLN A 1 239  ? 12.292 46.353  4.967   1.00 24.03 ? 239  GLN A NE2 1 
ATOM   1830 N  N   . GLN A 1 240  ? 17.709 41.990  4.156   1.00 13.60 ? 240  GLN A N   1 
ATOM   1831 C  CA  . GLN A 1 240  ? 18.219 40.755  3.587   1.00 13.95 ? 240  GLN A CA  1 
ATOM   1832 C  C   . GLN A 1 240  ? 19.501 40.271  4.265   1.00 12.27 ? 240  GLN A C   1 
ATOM   1833 O  O   . GLN A 1 240  ? 20.100 39.300  3.829   1.00 11.58 ? 240  GLN A O   1 
ATOM   1834 C  CB  . GLN A 1 240  ? 18.462 40.927  2.074   1.00 15.01 ? 240  GLN A CB  1 
ATOM   1835 C  CG  . GLN A 1 240  ? 17.248 41.407  1.280   1.00 18.32 ? 240  GLN A CG  1 
ATOM   1836 C  CD  . GLN A 1 240  ? 16.094 40.445  1.399   1.00 21.33 ? 240  GLN A CD  1 
ATOM   1837 O  OE1 . GLN A 1 240  ? 16.291 39.227  1.356   1.00 24.90 ? 240  GLN A OE1 1 
ATOM   1838 N  NE2 . GLN A 1 240  ? 14.890 40.981  1.583   1.00 25.25 ? 240  GLN A NE2 1 
ATOM   1839 N  N   . ARG A 1 241  ? 19.895 40.955  5.346   1.00 11.77 ? 241  ARG A N   1 
ATOM   1840 C  CA  . ARG A 1 241  ? 21.204 40.729  5.967   1.00 11.22 ? 241  ARG A CA  1 
ATOM   1841 C  C   . ARG A 1 241  ? 22.323 40.710  4.930   1.00 10.65 ? 241  ARG A C   1 
ATOM   1842 O  O   . ARG A 1 241  ? 23.153 39.791  4.878   1.00 10.84 ? 241  ARG A O   1 
ATOM   1843 C  CB  . ARG A 1 241  ? 21.225 39.440  6.810   1.00 11.43 ? 241  ARG A CB  1 
ATOM   1844 C  CG  . ARG A 1 241  ? 20.226 39.513  7.918   1.00 14.26 ? 241  ARG A CG  1 
ATOM   1845 C  CD  . ARG A 1 241  ? 20.288 38.370  8.915   1.00 17.79 ? 241  ARG A CD  1 
ATOM   1846 N  NE  . ARG A 1 241  ? 20.309 37.071  8.274   1.00 23.64 ? 241  ARG A NE  1 
ATOM   1847 C  CZ  . ARG A 1 241  ? 20.684 35.958  8.892   1.00 25.97 ? 241  ARG A CZ  1 
ATOM   1848 N  NH1 . ARG A 1 241  ? 21.071 36.000  10.157  1.00 26.30 ? 241  ARG A NH1 1 
ATOM   1849 N  NH2 . ARG A 1 241  ? 20.693 34.808  8.238   1.00 27.03 ? 241  ARG A NH2 1 
ATOM   1850 N  N   . GLN A 1 242  ? 22.306 41.731  4.066   1.00 10.03 ? 242  GLN A N   1 
ATOM   1851 C  CA  . GLN A 1 242  ? 23.342 41.904  3.034   1.00 10.33 ? 242  GLN A CA  1 
ATOM   1852 C  C   . GLN A 1 242  ? 24.209 43.138  3.287   1.00 9.61  ? 242  GLN A C   1 
ATOM   1853 O  O   . GLN A 1 242  ? 24.758 43.698  2.338   1.00 10.40 ? 242  GLN A O   1 
ATOM   1854 C  CB  . GLN A 1 242  ? 22.706 41.949  1.647   1.00 9.90  ? 242  GLN A CB  1 
ATOM   1855 C  CG  . GLN A 1 242  ? 22.061 40.615  1.243   1.00 11.91 ? 242  GLN A CG  1 
ATOM   1856 C  CD  . GLN A 1 242  ? 21.213 40.742  -0.004  1.00 12.63 ? 242  GLN A CD  1 
ATOM   1857 O  OE1 . GLN A 1 242  ? 20.650 41.795  -0.282  1.00 13.14 ? 242  GLN A OE1 1 
ATOM   1858 N  NE2 . GLN A 1 242  ? 21.137 39.656  -0.759  1.00 14.51 ? 242  GLN A NE2 1 
ATOM   1859 N  N   . LEU A 1 243  ? 24.325 43.537  4.551   1.00 8.64  ? 243  LEU A N   1 
ATOM   1860 C  CA  . LEU A 1 243  ? 25.163 44.689  4.898   1.00 8.35  ? 243  LEU A CA  1 
ATOM   1861 C  C   . LEU A 1 243  ? 26.629 44.315  4.955   1.00 9.62  ? 243  LEU A C   1 
ATOM   1862 O  O   . LEU A 1 243  ? 27.486 45.208  4.936   1.00 9.58  ? 243  LEU A O   1 
ATOM   1863 C  CB  . LEU A 1 243  ? 24.722 45.252  6.234   1.00 9.53  ? 243  LEU A CB  1 
ATOM   1864 C  CG  . LEU A 1 243  ? 23.344 45.911  6.219   1.00 10.76 ? 243  LEU A CG  1 
ATOM   1865 C  CD1 . LEU A 1 243  ? 22.874 46.068  7.648   1.00 13.12 ? 243  LEU A CD1 1 
ATOM   1866 C  CD2 . LEU A 1 243  ? 23.336 47.295  5.516   1.00 12.80 ? 243  LEU A CD2 1 
ATOM   1867 N  N   . GLU A 1 244  ? 26.946 43.027  5.056   1.00 9.01  ? 244  GLU A N   1 
ATOM   1868 C  CA  . GLU A 1 244  ? 28.306 42.557  4.877   1.00 8.40  ? 244  GLU A CA  1 
ATOM   1869 C  C   . GLU A 1 244  ? 28.355 41.760  3.595   1.00 8.45  ? 244  GLU A C   1 
ATOM   1870 O  O   . GLU A 1 244  ? 27.503 40.875  3.379   1.00 9.23  ? 244  GLU A O   1 
ATOM   1871 C  CB  . GLU A 1 244  ? 28.812 41.733  6.067   1.00 8.33  ? 244  GLU A CB  1 
ATOM   1872 C  CG  . GLU A 1 244  ? 29.104 42.638  7.260   1.00 9.12  ? 244  GLU A CG  1 
ATOM   1873 C  CD  . GLU A 1 244  ? 29.411 41.940  8.571   1.00 9.56  ? 244  GLU A CD  1 
ATOM   1874 O  OE1 . GLU A 1 244  ? 28.839 40.853  8.854   1.00 9.72  ? 244  GLU A OE1 1 
ATOM   1875 O  OE2 . GLU A 1 244  ? 30.227 42.508  9.339   1.00 10.04 ? 244  GLU A OE2 1 
ATOM   1876 N  N   . PHE A 1 245  ? 29.336 42.034  2.749   1.00 8.06  ? 245  PHE A N   1 
ATOM   1877 C  CA  . PHE A 1 245  ? 29.352 41.460  1.406   1.00 8.26  ? 245  PHE A CA  1 
ATOM   1878 C  C   . PHE A 1 245  ? 30.754 41.419  0.853   1.00 7.91  ? 245  PHE A C   1 
ATOM   1879 O  O   . PHE A 1 245  ? 31.617 42.205  1.304   1.00 8.61  ? 245  PHE A O   1 
ATOM   1880 C  CB  . PHE A 1 245  ? 28.397 42.228  0.449   1.00 8.40  ? 245  PHE A CB  1 
ATOM   1881 C  CG  . PHE A 1 245  ? 28.559 43.739  0.500   1.00 7.69  ? 245  PHE A CG  1 
ATOM   1882 C  CD1 . PHE A 1 245  ? 29.504 44.382  -0.282  1.00 8.17  ? 245  PHE A CD1 1 
ATOM   1883 C  CD2 . PHE A 1 245  ? 27.739 44.491  1.337   1.00 8.45  ? 245  PHE A CD2 1 
ATOM   1884 C  CE1 . PHE A 1 245  ? 29.632 45.783  -0.240  1.00 8.40  ? 245  PHE A CE1 1 
ATOM   1885 C  CE2 . PHE A 1 245  ? 27.889 45.872  1.417   1.00 8.56  ? 245  PHE A CE2 1 
ATOM   1886 C  CZ  . PHE A 1 245  ? 28.830 46.515  0.595   1.00 8.19  ? 245  PHE A CZ  1 
ATOM   1887 N  N   . LEU A 1 246  ? 30.975 40.560  -0.127  1.00 8.10  ? 246  LEU A N   1 
ATOM   1888 C  CA  . LEU A 1 246  ? 32.226 40.499  -0.842  1.00 8.45  ? 246  LEU A CA  1 
ATOM   1889 C  C   . LEU A 1 246  ? 32.080 41.401  -2.044  1.00 7.96  ? 246  LEU A C   1 
ATOM   1890 O  O   . LEU A 1 246  ? 31.395 41.077  -3.023  1.00 8.16  ? 246  LEU A O   1 
ATOM   1891 C  CB  . LEU A 1 246  ? 32.511 39.045  -1.259  1.00 9.59  ? 246  LEU A CB  1 
ATOM   1892 C  CG  . LEU A 1 246  ? 32.882 38.149  -0.053  1.00 12.64 ? 246  LEU A CG  1 
ATOM   1893 C  CD1 . LEU A 1 246  ? 32.668 36.676  -0.424  1.00 16.45 ? 246  LEU A CD1 1 
ATOM   1894 C  CD2 . LEU A 1 246  ? 34.338 38.430  0.345   1.00 16.79 ? 246  LEU A CD2 1 
ATOM   1895 N  N   . TRP A 1 247  ? 32.720 42.560  -1.947  1.00 7.77  ? 247  TRP A N   1 
ATOM   1896 C  CA  . TRP A 1 247  ? 32.537 43.597  -2.965  1.00 7.25  ? 247  TRP A CA  1 
ATOM   1897 C  C   . TRP A 1 247  ? 33.560 43.404  -4.070  1.00 7.28  ? 247  TRP A C   1 
ATOM   1898 O  O   . TRP A 1 247  ? 34.768 43.591  -3.860  1.00 7.59  ? 247  TRP A O   1 
ATOM   1899 C  CB  . TRP A 1 247  ? 32.731 44.957  -2.313  1.00 7.29  ? 247  TRP A CB  1 
ATOM   1900 C  CG  . TRP A 1 247  ? 32.240 46.144  -3.155  1.00 7.10  ? 247  TRP A CG  1 
ATOM   1901 C  CD1 . TRP A 1 247  ? 31.734 46.140  -4.442  1.00 7.57  ? 247  TRP A CD1 1 
ATOM   1902 C  CD2 . TRP A 1 247  ? 32.261 47.514  -2.733  1.00 7.03  ? 247  TRP A CD2 1 
ATOM   1903 N  NE1 . TRP A 1 247  ? 31.404 47.432  -4.804  1.00 6.87  ? 247  TRP A NE1 1 
ATOM   1904 C  CE2 . TRP A 1 247  ? 31.720 48.290  -3.781  1.00 5.89  ? 247  TRP A CE2 1 
ATOM   1905 C  CE3 . TRP A 1 247  ? 32.679 48.166  -1.561  1.00 7.61  ? 247  TRP A CE3 1 
ATOM   1906 C  CZ2 . TRP A 1 247  ? 31.612 49.684  -3.696  1.00 8.43  ? 247  TRP A CZ2 1 
ATOM   1907 C  CZ3 . TRP A 1 247  ? 32.553 49.553  -1.480  1.00 6.99  ? 247  TRP A CZ3 1 
ATOM   1908 C  CH2 . TRP A 1 247  ? 32.035 50.293  -2.534  1.00 7.76  ? 247  TRP A CH2 1 
ATOM   1909 N  N   . ARG A 1 248  ? 33.081 42.987  -5.244  1.00 7.60  ? 248  ARG A N   1 
ATOM   1910 C  CA  . ARG A 1 248  ? 33.940 42.796  -6.409  1.00 8.16  ? 248  ARG A CA  1 
ATOM   1911 C  C   . ARG A 1 248  ? 33.677 43.886  -7.455  1.00 7.83  ? 248  ARG A C   1 
ATOM   1912 O  O   . ARG A 1 248  ? 32.645 44.548  -7.406  1.00 7.99  ? 248  ARG A O   1 
ATOM   1913 C  CB  . ARG A 1 248  ? 33.715 41.424  -7.047  1.00 9.03  ? 248  ARG A CB  1 
ATOM   1914 C  CG  . ARG A 1 248  ? 32.329 41.286  -7.702  1.00 8.79  ? 248  ARG A CG  1 
ATOM   1915 C  CD  . ARG A 1 248  ? 32.226 39.993  -8.530  1.00 11.41 ? 248  ARG A CD  1 
ATOM   1916 N  NE  . ARG A 1 248  ? 32.296 38.826  -7.641  1.00 13.12 ? 248  ARG A NE  1 
ATOM   1917 C  CZ  . ARG A 1 248  ? 32.219 37.572  -8.085  1.00 13.55 ? 248  ARG A CZ  1 
ATOM   1918 N  NH1 . ARG A 1 248  ? 32.128 37.328  -9.388  1.00 14.12 ? 248  ARG A NH1 1 
ATOM   1919 N  NH2 . ARG A 1 248  ? 32.260 36.563  -7.228  1.00 14.10 ? 248  ARG A NH2 1 
ATOM   1920 N  N   . GLN A 1 249  ? 34.607 44.025  -8.399  1.00 7.81  ? 249  GLN A N   1 
ATOM   1921 C  CA  . GLN A 1 249  ? 34.421 45.009  -9.482  1.00 7.46  ? 249  GLN A CA  1 
ATOM   1922 C  C   . GLN A 1 249  ? 33.326 44.569  -10.432 1.00 8.31  ? 249  GLN A C   1 
ATOM   1923 O  O   . GLN A 1 249  ? 33.057 43.357  -10.583 1.00 8.95  ? 249  GLN A O   1 
ATOM   1924 C  CB  . GLN A 1 249  ? 35.726 45.189  -10.239 1.00 8.56  ? 249  GLN A CB  1 
ATOM   1925 C  CG  . GLN A 1 249  ? 36.840 45.682  -9.299  1.00 8.15  ? 249  GLN A CG  1 
ATOM   1926 C  CD  . GLN A 1 249  ? 36.460 47.001  -8.627  1.00 8.74  ? 249  GLN A CD  1 
ATOM   1927 O  OE1 . GLN A 1 249  ? 36.150 47.990  -9.301  1.00 8.26  ? 249  GLN A OE1 1 
ATOM   1928 N  NE2 . GLN A 1 249  ? 36.457 47.030  -7.297  1.00 7.45  ? 249  GLN A NE2 1 
ATOM   1929 N  N   . ILE A 1 250  ? 32.696 45.533  -11.094 1.00 8.29  ? 250  ILE A N   1 
ATOM   1930 C  CA  . ILE A 1 250  ? 31.532 45.233  -11.918 1.00 9.24  ? 250  ILE A CA  1 
ATOM   1931 C  C   . ILE A 1 250  ? 31.815 44.302  -13.102 1.00 9.51  ? 250  ILE A C   1 
ATOM   1932 O  O   . ILE A 1 250  ? 30.883 43.675  -13.605 1.00 10.67 ? 250  ILE A O   1 
ATOM   1933 C  CB  . ILE A 1 250  ? 30.847 46.549  -12.417 1.00 9.70  ? 250  ILE A CB  1 
ATOM   1934 C  CG1 . ILE A 1 250  ? 31.834 47.457  -13.174 1.00 10.96 ? 250  ILE A CG1 1 
ATOM   1935 C  CG2 . ILE A 1 250  ? 30.149 47.260  -11.279 1.00 10.88 ? 250  ILE A CG2 1 
ATOM   1936 C  CD1 . ILE A 1 250  ? 31.216 48.809  -13.649 1.00 12.31 ? 250  ILE A CD1 1 
ATOM   1937 N  N   . TRP A 1 251  ? 33.066 44.241  -13.522 1.00 10.41 ? 251  TRP A N   1 
ATOM   1938 C  CA  . TRP A 1 251  ? 33.416 43.388  -14.665 1.00 12.12 ? 251  TRP A CA  1 
ATOM   1939 C  C   . TRP A 1 251  ? 33.999 42.052  -14.262 1.00 14.52 ? 251  TRP A C   1 
ATOM   1940 O  O   . TRP A 1 251  ? 34.328 41.239  -15.121 1.00 15.06 ? 251  TRP A O   1 
ATOM   1941 C  CB  . TRP A 1 251  ? 34.422 44.102  -15.564 1.00 13.45 ? 251  TRP A CB  1 
ATOM   1942 C  CG  . TRP A 1 251  ? 35.674 44.254  -14.848 1.00 15.30 ? 251  TRP A CG  1 
ATOM   1943 C  CD1 . TRP A 1 251  ? 36.654 43.297  -14.675 1.00 17.67 ? 251  TRP A CD1 1 
ATOM   1944 C  CD2 . TRP A 1 251  ? 36.105 45.404  -14.140 1.00 14.94 ? 251  TRP A CD2 1 
ATOM   1945 N  NE1 . TRP A 1 251  ? 37.664 43.802  -13.905 1.00 16.45 ? 251  TRP A NE1 1 
ATOM   1946 C  CE2 . TRP A 1 251  ? 37.361 45.099  -13.565 1.00 14.60 ? 251  TRP A CE2 1 
ATOM   1947 C  CE3 . TRP A 1 251  ? 35.549 46.668  -13.907 1.00 14.19 ? 251  TRP A CE3 1 
ATOM   1948 C  CZ2 . TRP A 1 251  ? 38.071 46.001  -12.786 1.00 15.43 ? 251  TRP A CZ2 1 
ATOM   1949 C  CZ3 . TRP A 1 251  ? 36.261 47.570  -13.157 1.00 15.84 ? 251  TRP A CZ3 1 
ATOM   1950 C  CH2 . TRP A 1 251  ? 37.518 47.237  -12.610 1.00 16.08 ? 251  TRP A CH2 1 
ATOM   1951 N  N   . ASP A 1 252  ? 34.163 41.833  -12.965 1.00 13.07 ? 252  ASP A N   1 
ATOM   1952 C  CA  . ASP A 1 252  ? 34.950 40.708  -12.465 1.00 14.37 ? 252  ASP A CA  1 
ATOM   1953 C  C   . ASP A 1 252  ? 34.127 39.434  -12.367 1.00 14.37 ? 252  ASP A C   1 
ATOM   1954 O  O   . ASP A 1 252  ? 33.364 39.216  -11.445 1.00 14.48 ? 252  ASP A O   1 
ATOM   1955 C  CB  . ASP A 1 252  ? 35.570 41.102  -11.115 1.00 13.91 ? 252  ASP A CB  1 
ATOM   1956 C  CG  . ASP A 1 252  ? 36.305 39.972  -10.452 1.00 16.48 ? 252  ASP A CG  1 
ATOM   1957 O  OD1 . ASP A 1 252  ? 36.569 38.921  -11.097 1.00 18.53 ? 252  ASP A OD1 1 
ATOM   1958 O  OD2 . ASP A 1 252  ? 36.616 40.061  -9.248  1.00 14.38 ? 252  ASP A OD2 1 
ATOM   1959 N  N   . ASN A 1 253  ? 34.279 38.575  -13.372 1.00 15.70 ? 253  ASN A N   1 
ATOM   1960 C  CA  . ASN A 1 253  ? 33.489 37.356  -13.420 1.00 17.17 ? 253  ASN A CA  1 
ATOM   1961 C  C   . ASN A 1 253  ? 33.905 36.316  -12.372 1.00 16.63 ? 253  ASN A C   1 
ATOM   1962 O  O   . ASN A 1 253  ? 33.053 35.659  -11.783 1.00 17.52 ? 253  ASN A O   1 
ATOM   1963 C  CB  . ASN A 1 253  ? 33.600 36.755  -14.814 1.00 18.10 ? 253  ASN A CB  1 
ATOM   1964 C  CG  . ASN A 1 253  ? 32.750 35.555  -14.986 1.00 22.93 ? 253  ASN A CG  1 
ATOM   1965 O  OD1 . ASN A 1 253  ? 31.553 35.570  -14.683 1.00 25.66 ? 253  ASN A OD1 1 
ATOM   1966 N  ND2 . ASN A 1 253  ? 33.359 34.481  -15.491 1.00 24.82 ? 253  ASN A ND2 1 
ATOM   1967 N  N   . LYS A 1 254  ? 35.202 36.233  -12.140 1.00 18.51 ? 254  LYS A N   1 
ATOM   1968 C  CA  . LYS A 1 254  ? 35.779 35.193  -11.282 1.00 19.81 ? 254  LYS A CA  1 
ATOM   1969 C  C   . LYS A 1 254  ? 35.682 35.548  -9.806  1.00 19.88 ? 254  LYS A C   1 
ATOM   1970 O  O   . LYS A 1 254  ? 35.426 34.677  -8.963  1.00 21.02 ? 254  LYS A O   1 
ATOM   1971 C  CB  . LYS A 1 254  ? 37.235 34.939  -11.675 1.00 21.67 ? 254  LYS A CB  1 
ATOM   1972 C  CG  . LYS A 1 254  ? 37.915 33.780  -10.976 1.00 25.86 ? 254  LYS A CG  1 
ATOM   1973 C  CD  . LYS A 1 254  ? 39.122 33.308  -11.801 1.00 29.72 ? 254  LYS A CD  1 
ATOM   1974 C  CE  . LYS A 1 254  ? 40.270 32.809  -10.913 1.00 31.29 ? 254  LYS A CE  1 
ATOM   1975 N  NZ  . LYS A 1 254  ? 39.832 31.999  -9.731  1.00 34.39 ? 254  LYS A NZ  1 
ATOM   1976 N  N   . GLY A 1 255  ? 35.874 36.825  -9.487  1.00 18.68 ? 255  GLY A N   1 
ATOM   1977 C  CA  . GLY A 1 255  ? 35.795 37.270  -8.103  1.00 16.96 ? 255  GLY A CA  1 
ATOM   1978 C  C   . GLY A 1 255  ? 37.138 37.563  -7.457  1.00 16.19 ? 255  GLY A C   1 
ATOM   1979 O  O   . GLY A 1 255  ? 37.181 37.824  -6.255  1.00 14.93 ? 255  GLY A O   1 
ATOM   1980 N  N   . ASP A 1 256  ? 38.226 37.566  -8.213  1.00 16.34 ? 256  ASP A N   1 
ATOM   1981 C  CA  . ASP A 1 256  ? 39.540 37.794  -7.597  1.00 17.57 ? 256  ASP A CA  1 
ATOM   1982 C  C   . ASP A 1 256  ? 39.752 39.206  -7.043  1.00 15.78 ? 256  ASP A C   1 
ATOM   1983 O  O   . ASP A 1 256  ? 40.638 39.428  -6.219  1.00 16.65 ? 256  ASP A O   1 
ATOM   1984 C  CB  . ASP A 1 256  ? 40.676 37.456  -8.555  1.00 20.04 ? 256  ASP A CB  1 
ATOM   1985 C  CG  . ASP A 1 256  ? 40.675 36.003  -8.984  1.00 25.42 ? 256  ASP A CG  1 
ATOM   1986 O  OD1 . ASP A 1 256  ? 40.126 35.144  -8.251  1.00 30.98 ? 256  ASP A OD1 1 
ATOM   1987 O  OD2 . ASP A 1 256  ? 41.225 35.647  -10.050 1.00 30.81 ? 256  ASP A OD2 1 
ATOM   1988 N  N   . THR A 1 257  ? 38.906 40.149  -7.461  1.00 13.19 ? 257  THR A N   1 
ATOM   1989 C  CA  . THR A 1 257  ? 38.993 41.513  -6.914  1.00 12.03 ? 257  THR A CA  1 
ATOM   1990 C  C   . THR A 1 257  ? 38.235 41.695  -5.592  1.00 11.09 ? 257  THR A C   1 
ATOM   1991 O  O   . THR A 1 257  ? 38.312 42.769  -4.975  1.00 11.30 ? 257  THR A O   1 
ATOM   1992 C  CB  . THR A 1 257  ? 38.456 42.594  -7.895  1.00 12.05 ? 257  THR A CB  1 
ATOM   1993 O  OG1 . THR A 1 257  ? 37.048 42.399  -8.116  1.00 10.59 ? 257  THR A OG1 1 
ATOM   1994 C  CG2 . THR A 1 257  ? 39.211 42.528  -9.249  1.00 14.30 ? 257  THR A CG2 1 
ATOM   1995 N  N   . ALA A 1 258  ? 37.504 40.668  -5.161  1.00 11.23 ? 258  ALA A N   1 
ATOM   1996 C  CA  . ALA A 1 258  ? 36.566 40.795  -4.034  1.00 10.65 ? 258  ALA A CA  1 
ATOM   1997 C  C   . ALA A 1 258  ? 37.256 41.220  -2.745  1.00 9.49  ? 258  ALA A C   1 
ATOM   1998 O  O   . ALA A 1 258  ? 38.351 40.724  -2.417  1.00 10.91 ? 258  ALA A O   1 
ATOM   1999 C  CB  . ALA A 1 258  ? 35.840 39.503  -3.784  1.00 11.84 ? 258  ALA A CB  1 
ATOM   2000 N  N   . LEU A 1 259  ? 36.627 42.129  -2.028  1.00 8.59  ? 259  LEU A N   1 
ATOM   2001 C  CA  . LEU A 1 259  ? 37.094 42.559  -0.704  1.00 8.31  ? 259  LEU A CA  1 
ATOM   2002 C  C   . LEU A 1 259  ? 35.920 42.560  0.241   1.00 8.10  ? 259  LEU A C   1 
ATOM   2003 O  O   . LEU A 1 259  ? 34.864 43.151  -0.034  1.00 7.88  ? 259  LEU A O   1 
ATOM   2004 C  CB  . LEU A 1 259  ? 37.694 43.959  -0.761  1.00 8.36  ? 259  LEU A CB  1 
ATOM   2005 C  CG  . LEU A 1 259  ? 38.468 44.365  0.503   1.00 8.15  ? 259  LEU A CG  1 
ATOM   2006 C  CD1 . LEU A 1 259  ? 39.699 43.490  0.743   1.00 9.93  ? 259  LEU A CD1 1 
ATOM   2007 C  CD2 . LEU A 1 259  ? 38.905 45.836  0.364   1.00 10.19 ? 259  LEU A CD2 1 
ATOM   2008 N  N   . PHE A 1 260  ? 36.076 41.880  1.392   1.00 7.89  ? 260  PHE A N   1 
ATOM   2009 C  CA  . PHE A 1 260  ? 34.995 41.849  2.373   1.00 8.03  ? 260  PHE A CA  1 
ATOM   2010 C  C   . PHE A 1 260  ? 34.692 43.244  2.868   1.00 7.14  ? 260  PHE A C   1 
ATOM   2011 O  O   . PHE A 1 260  ? 35.605 43.982  3.286   1.00 7.63  ? 260  PHE A O   1 
ATOM   2012 C  CB  . PHE A 1 260  ? 35.407 40.964  3.563   1.00 8.73  ? 260  PHE A CB  1 
ATOM   2013 C  CG  . PHE A 1 260  ? 34.309 40.804  4.574   1.00 8.14  ? 260  PHE A CG  1 
ATOM   2014 C  CD1 . PHE A 1 260  ? 33.322 39.824  4.399   1.00 10.23 ? 260  PHE A CD1 1 
ATOM   2015 C  CD2 . PHE A 1 260  ? 34.241 41.609  5.699   1.00 9.43  ? 260  PHE A CD2 1 
ATOM   2016 C  CE1 . PHE A 1 260  ? 32.294 39.670  5.343   1.00 12.17 ? 260  PHE A CE1 1 
ATOM   2017 C  CE2 . PHE A 1 260  ? 33.230 41.463  6.643   1.00 10.85 ? 260  PHE A CE2 1 
ATOM   2018 C  CZ  . PHE A 1 260  ? 32.263 40.505  6.467   1.00 11.73 ? 260  PHE A CZ  1 
ATOM   2019 N  N   . THR A 1 261  ? 33.411 43.617  2.847   1.00 6.89  ? 261  THR A N   1 
ATOM   2020 C  CA  . THR A 1 261  ? 33.005 44.977  3.169   1.00 7.05  ? 261  THR A CA  1 
ATOM   2021 C  C   . THR A 1 261  ? 31.883 44.931  4.198   1.00 7.24  ? 261  THR A C   1 
ATOM   2022 O  O   . THR A 1 261  ? 30.926 44.146  4.035   1.00 8.31  ? 261  THR A O   1 
ATOM   2023 C  CB  . THR A 1 261  ? 32.481 45.664  1.891   1.00 7.70  ? 261  THR A CB  1 
ATOM   2024 O  OG1 . THR A 1 261  ? 33.544 45.736  0.943   1.00 7.81  ? 261  THR A OG1 1 
ATOM   2025 C  CG2 . THR A 1 261  ? 32.042 47.093  2.178   1.00 8.81  ? 261  THR A CG2 1 
ATOM   2026 N  N   . HIS A 1 262  ? 31.984 45.792  5.216   1.00 7.03  ? 262  HIS A N   1 
ATOM   2027 C  CA  . HIS A 1 262  ? 30.926 45.981  6.199   1.00 7.10  ? 262  HIS A CA  1 
ATOM   2028 C  C   . HIS A 1 262  ? 30.305 47.358  5.999   1.00 7.27  ? 262  HIS A C   1 
ATOM   2029 O  O   . HIS A 1 262  ? 31.012 48.370  6.105   1.00 7.39  ? 262  HIS A O   1 
ATOM   2030 C  CB  . HIS A 1 262  ? 31.546 45.886  7.617   1.00 8.54  ? 262  HIS A CB  1 
ATOM   2031 C  CG  . HIS A 1 262  ? 30.601 46.257  8.719   1.00 7.63  ? 262  HIS A CG  1 
ATOM   2032 N  ND1 . HIS A 1 262  ? 29.985 45.321  9.519   1.00 8.68  ? 262  HIS A ND1 1 
ATOM   2033 C  CD2 . HIS A 1 262  ? 30.156 47.465  9.139   1.00 7.43  ? 262  HIS A CD2 1 
ATOM   2034 C  CE1 . HIS A 1 262  ? 29.234 45.947  10.420  1.00 9.33  ? 262  HIS A CE1 1 
ATOM   2035 N  NE2 . HIS A 1 262  ? 29.288 47.247  10.195  1.00 9.29  ? 262  HIS A NE2 1 
ATOM   2036 N  N   . MET A 1 263  ? 29.016 47.398  5.682   1.00 7.35  ? 263  MET A N   1 
ATOM   2037 C  CA  . MET A 1 263  ? 28.262 48.642  5.651   1.00 7.62  ? 263  MET A CA  1 
ATOM   2038 C  C   . MET A 1 263  ? 27.541 48.846  6.971   1.00 8.19  ? 263  MET A C   1 
ATOM   2039 O  O   . MET A 1 263  ? 26.783 47.953  7.405   1.00 8.81  ? 263  MET A O   1 
ATOM   2040 C  CB  . MET A 1 263  ? 27.233 48.621  4.508   1.00 8.26  ? 263  MET A CB  1 
ATOM   2041 C  CG  . MET A 1 263  ? 26.464 49.926  4.372   1.00 7.63  ? 263  MET A CG  1 
ATOM   2042 S  SD  . MET A 1 263  ? 25.120 49.806  3.163   1.00 9.12  ? 263  MET A SD  1 
ATOM   2043 C  CE  . MET A 1 263  ? 25.950 49.432  1.642   1.00 10.62 ? 263  MET A CE  1 
ATOM   2044 N  N   A MET A 1 264  ? 27.758 49.989  7.624   0.50 7.69  ? 264  MET A N   1 
ATOM   2045 N  N   B MET A 1 264  ? 27.753 49.983  7.630   0.50 7.97  ? 264  MET A N   1 
ATOM   2046 C  CA  A MET A 1 264  ? 27.032 50.341  8.852   0.50 8.25  ? 264  MET A CA  1 
ATOM   2047 C  CA  B MET A 1 264  ? 27.023 50.277  8.865   0.50 8.94  ? 264  MET A CA  1 
ATOM   2048 C  C   A MET A 1 264  ? 25.570 50.611  8.490   0.50 8.60  ? 264  MET A C   1 
ATOM   2049 C  C   B MET A 1 264  ? 25.577 50.622  8.506   0.50 8.94  ? 264  MET A C   1 
ATOM   2050 O  O   A MET A 1 264  ? 25.276 51.025  7.361   0.50 8.85  ? 264  MET A O   1 
ATOM   2051 O  O   B MET A 1 264  ? 25.302 51.094  7.401   0.50 9.30  ? 264  MET A O   1 
ATOM   2052 C  CB  A MET A 1 264  ? 27.684 51.554  9.519   0.50 7.98  ? 264  MET A CB  1 
ATOM   2053 C  CB  B MET A 1 264  ? 27.715 51.388  9.646   0.50 8.67  ? 264  MET A CB  1 
ATOM   2054 C  CG  A MET A 1 264  ? 29.145 51.298  9.969   0.50 8.11  ? 264  MET A CG  1 
ATOM   2055 C  CG  B MET A 1 264  ? 29.168 51.036  10.021  0.50 9.58  ? 264  MET A CG  1 
ATOM   2056 S  SD  A MET A 1 264  ? 30.137 52.727  10.477  0.50 9.36  ? 264  MET A SD  1 
ATOM   2057 S  SD  B MET A 1 264  ? 29.720 51.823  11.518  0.50 11.60 ? 264  MET A SD  1 
ATOM   2058 C  CE  A MET A 1 264  ? 29.035 53.582  11.641  0.50 10.74 ? 264  MET A CE  1 
ATOM   2059 C  CE  B MET A 1 264  ? 29.773 53.532  10.989  0.50 9.06  ? 264  MET A CE  1 
ATOM   2060 N  N   . PRO A 1 265  ? 24.640 50.316  9.409   1.00 8.81  ? 265  PRO A N   1 
ATOM   2061 C  CA  . PRO A 1 265  ? 23.215 50.319  9.040   1.00 9.73  ? 265  PRO A CA  1 
ATOM   2062 C  C   . PRO A 1 265  ? 22.435 51.600  9.233   1.00 9.68  ? 265  PRO A C   1 
ATOM   2063 O  O   . PRO A 1 265  ? 21.331 51.697  8.678   1.00 9.74  ? 265  PRO A O   1 
ATOM   2064 C  CB  . PRO A 1 265  ? 22.613 49.238  9.962   1.00 10.81 ? 265  PRO A CB  1 
ATOM   2065 C  CG  . PRO A 1 265  ? 23.471 49.191  11.152  1.00 10.91 ? 265  PRO A CG  1 
ATOM   2066 C  CD  . PRO A 1 265  ? 24.852 49.790  10.788  1.00 9.04  ? 265  PRO A CD  1 
ATOM   2067 N  N   . PHE A 1 266  ? 22.951 52.543  10.014  1.00 8.95  ? 266  PHE A N   1 
ATOM   2068 C  CA  . PHE A 1 266  ? 22.153 53.655  10.514  1.00 9.32  ? 266  PHE A CA  1 
ATOM   2069 C  C   . PHE A 1 266  ? 22.566 55.004  9.932   1.00 9.23  ? 266  PHE A C   1 
ATOM   2070 O  O   . PHE A 1 266  ? 23.446 55.089  9.072   1.00 9.31  ? 266  PHE A O   1 
ATOM   2071 C  CB  . PHE A 1 266  ? 22.118 53.653  12.042  1.00 9.80  ? 266  PHE A CB  1 
ATOM   2072 C  CG  . PHE A 1 266  ? 21.600 52.333  12.645  1.00 9.70  ? 266  PHE A CG  1 
ATOM   2073 C  CD1 . PHE A 1 266  ? 20.457 51.700  12.139  1.00 10.54 ? 266  PHE A CD1 1 
ATOM   2074 C  CD2 . PHE A 1 266  ? 22.275 51.745  13.686  1.00 9.81  ? 266  PHE A CD2 1 
ATOM   2075 C  CE1 . PHE A 1 266  ? 19.980 50.496  12.705  1.00 10.29 ? 266  PHE A CE1 1 
ATOM   2076 C  CE2 . PHE A 1 266  ? 21.798 50.563  14.282  1.00 10.69 ? 266  PHE A CE2 1 
ATOM   2077 C  CZ  . PHE A 1 266  ? 20.663 49.929  13.745  1.00 9.52  ? 266  PHE A CZ  1 
ATOM   2078 N  N   . TYR A 1 267  ? 21.912 56.055  10.385  1.00 9.51  ? 267  TYR A N   1 
ATOM   2079 C  CA  . TYR A 1 267  ? 21.955 57.342  9.743   1.00 9.59  ? 267  TYR A CA  1 
ATOM   2080 C  C   . TYR A 1 267  ? 23.302 58.042  9.913   1.00 9.62  ? 267  TYR A C   1 
ATOM   2081 O  O   . TYR A 1 267  ? 23.663 58.832  9.051   1.00 9.01  ? 267  TYR A O   1 
ATOM   2082 C  CB  . TYR A 1 267  ? 20.815 58.197  10.302  1.00 10.65 ? 267  TYR A CB  1 
ATOM   2083 C  CG  . TYR A 1 267  ? 20.930 59.693  10.132  1.00 11.03 ? 267  TYR A CG  1 
ATOM   2084 C  CD1 . TYR A 1 267  ? 20.611 60.327  8.927   1.00 13.12 ? 267  TYR A CD1 1 
ATOM   2085 C  CD2 . TYR A 1 267  ? 21.307 60.486  11.213  1.00 12.30 ? 267  TYR A CD2 1 
ATOM   2086 C  CE1 . TYR A 1 267  ? 20.696 61.728  8.814   1.00 12.89 ? 267  TYR A CE1 1 
ATOM   2087 C  CE2 . TYR A 1 267  ? 21.402 61.841  11.108  1.00 13.74 ? 267  TYR A CE2 1 
ATOM   2088 C  CZ  . TYR A 1 267  ? 21.097 62.453  9.924   1.00 13.39 ? 267  TYR A CZ  1 
ATOM   2089 O  OH  . TYR A 1 267  ? 21.200 63.846  9.872   1.00 17.92 ? 267  TYR A OH  1 
ATOM   2090 N  N   . SER A 1 268  ? 24.020 57.776  10.991  1.00 9.20  ? 268  SER A N   1 
ATOM   2091 C  CA  . SER A 1 268  ? 25.265 58.494  11.269  1.00 9.76  ? 268  SER A CA  1 
ATOM   2092 C  C   . SER A 1 268  ? 26.283 57.568  11.913  1.00 9.81  ? 268  SER A C   1 
ATOM   2093 O  O   . SER A 1 268  ? 25.960 56.453  12.382  1.00 10.09 ? 268  SER A O   1 
ATOM   2094 C  CB  . SER A 1 268  ? 24.963 59.720  12.152  1.00 9.99  ? 268  SER A CB  1 
ATOM   2095 O  OG  . SER A 1 268  ? 26.126 60.302  12.712  1.00 13.41 ? 268  SER A OG  1 
ATOM   2096 N  N   . TYR A 1 269  ? 27.540 58.039  11.946  1.00 9.68  ? 269  TYR A N   1 
ATOM   2097 C  CA  . TYR A 1 269  ? 28.565 57.330  12.693  1.00 9.20  ? 269  TYR A CA  1 
ATOM   2098 C  C   . TYR A 1 269  ? 28.704 57.814  14.147  1.00 9.18  ? 269  TYR A C   1 
ATOM   2099 O  O   . TYR A 1 269  ? 29.578 57.328  14.872  1.00 9.73  ? 269  TYR A O   1 
ATOM   2100 C  CB  . TYR A 1 269  ? 29.924 57.458  11.961  1.00 8.13  ? 269  TYR A CB  1 
ATOM   2101 C  CG  . TYR A 1 269  ? 30.399 58.876  11.713  1.00 9.25  ? 269  TYR A CG  1 
ATOM   2102 C  CD1 . TYR A 1 269  ? 30.875 59.689  12.758  1.00 10.08 ? 269  TYR A CD1 1 
ATOM   2103 C  CD2 . TYR A 1 269  ? 30.363 59.409  10.417  1.00 10.15 ? 269  TYR A CD2 1 
ATOM   2104 C  CE1 . TYR A 1 269  ? 31.337 61.012  12.504  1.00 11.11 ? 269  TYR A CE1 1 
ATOM   2105 C  CE2 . TYR A 1 269  ? 30.848 60.706  10.164  1.00 9.13  ? 269  TYR A CE2 1 
ATOM   2106 C  CZ  . TYR A 1 269  ? 31.330 61.499  11.198  1.00 9.71  ? 269  TYR A CZ  1 
ATOM   2107 O  OH  . TYR A 1 269  ? 31.784 62.782  10.927  1.00 10.53 ? 269  TYR A OH  1 
ATOM   2108 N  N   . ASP A 1 270  ? 27.857 58.749  14.559  1.00 9.89  ? 270  ASP A N   1 
ATOM   2109 C  CA  . ASP A 1 270  ? 27.887 59.197  15.956  1.00 10.36 ? 270  ASP A CA  1 
ATOM   2110 C  C   . ASP A 1 270  ? 27.298 58.171  16.933  1.00 9.24  ? 270  ASP A C   1 
ATOM   2111 O  O   . ASP A 1 270  ? 26.749 57.156  16.503  1.00 9.97  ? 270  ASP A O   1 
ATOM   2112 C  CB  . ASP A 1 270  ? 27.256 60.575  16.089  1.00 11.42 ? 270  ASP A CB  1 
ATOM   2113 C  CG  . ASP A 1 270  ? 25.765 60.594  15.855  1.00 12.63 ? 270  ASP A CG  1 
ATOM   2114 O  OD1 . ASP A 1 270  ? 25.103 59.528  15.725  1.00 13.38 ? 270  ASP A OD1 1 
ATOM   2115 O  OD2 . ASP A 1 270  ? 25.157 61.701  15.859  1.00 14.53 ? 270  ASP A OD2 1 
ATOM   2116 N  N   . ILE A 1 271  ? 27.502 58.395  18.228  1.00 9.55  ? 271  ILE A N   1 
ATOM   2117 C  CA  . ILE A 1 271  ? 27.101 57.377  19.223  1.00 9.95  ? 271  ILE A CA  1 
ATOM   2118 C  C   . ILE A 1 271  ? 25.579 57.103  19.194  1.00 9.32  ? 271  ILE A C   1 
ATOM   2119 O  O   . ILE A 1 271  ? 25.190 55.931  19.181  1.00 9.44  ? 271  ILE A O   1 
ATOM   2120 C  CB  . ILE A 1 271  ? 27.655 57.689  20.608  1.00 10.37 ? 271  ILE A CB  1 
ATOM   2121 C  CG1 . ILE A 1 271  ? 29.194 57.558  20.564  1.00 10.44 ? 271  ILE A CG1 1 
ATOM   2122 C  CG2 . ILE A 1 271  ? 27.056 56.713  21.656  1.00 10.42 ? 271  ILE A CG2 1 
ATOM   2123 C  CD1 . ILE A 1 271  ? 29.884 58.214  21.737  1.00 10.63 ? 271  ILE A CD1 1 
ATOM   2124 N  N   . PRO A 1 272  ? 24.731 58.128  19.092  1.00 9.41  ? 272  PRO A N   1 
ATOM   2125 C  CA  . PRO A 1 272  ? 23.286 57.848  18.985  1.00 10.19 ? 272  PRO A CA  1 
ATOM   2126 C  C   . PRO A 1 272  ? 22.920 56.923  17.845  1.00 11.20 ? 272  PRO A C   1 
ATOM   2127 O  O   . PRO A 1 272  ? 21.878 56.248  17.945  1.00 11.57 ? 272  PRO A O   1 
ATOM   2128 C  CB  . PRO A 1 272  ? 22.667 59.227  18.786  1.00 11.02 ? 272  PRO A CB  1 
ATOM   2129 C  CG  . PRO A 1 272  ? 23.598 60.149  19.536  1.00 11.06 ? 272  PRO A CG  1 
ATOM   2130 C  CD  . PRO A 1 272  ? 24.983 59.580  19.207  1.00 11.03 ? 272  PRO A CD  1 
ATOM   2131 N  N   . HIS A 1 273  ? 23.718 56.869  16.779  1.00 10.02 ? 273  HIS A N   1 
ATOM   2132 C  CA  . HIS A 1 273  ? 23.368 56.021  15.629  1.00 9.60  ? 273  HIS A CA  1 
ATOM   2133 C  C   . HIS A 1 273  ? 24.286 54.832  15.416  1.00 9.64  ? 273  HIS A C   1 
ATOM   2134 O  O   . HIS A 1 273  ? 24.318 54.260  14.313  1.00 10.36 ? 273  HIS A O   1 
ATOM   2135 C  CB  . HIS A 1 273  ? 23.221 56.859  14.337  1.00 9.60  ? 273  HIS A CB  1 
ATOM   2136 C  CG  . HIS A 1 273  ? 22.158 57.906  14.443  1.00 10.37 ? 273  HIS A CG  1 
ATOM   2137 N  ND1 . HIS A 1 273  ? 22.400 59.164  14.956  1.00 11.30 ? 273  HIS A ND1 1 
ATOM   2138 C  CD2 . HIS A 1 273  ? 20.828 57.862  14.160  1.00 10.56 ? 273  HIS A CD2 1 
ATOM   2139 C  CE1 . HIS A 1 273  ? 21.265 59.856  14.978  1.00 12.03 ? 273  HIS A CE1 1 
ATOM   2140 N  NE2 . HIS A 1 273  ? 20.303 59.088  14.493  1.00 11.11 ? 273  HIS A NE2 1 
ATOM   2141 N  N   . THR A 1 274  ? 25.001 54.434  16.470  1.00 9.68  ? 274  THR A N   1 
ATOM   2142 C  CA  . THR A 1 274  ? 25.874 53.273  16.347  1.00 10.24 ? 274  THR A CA  1 
ATOM   2143 C  C   . THR A 1 274  ? 25.639 52.206  17.422  1.00 10.34 ? 274  THR A C   1 
ATOM   2144 O  O   . THR A 1 274  ? 26.197 51.121  17.300  1.00 11.94 ? 274  THR A O   1 
ATOM   2145 C  CB  . THR A 1 274  ? 27.377 53.682  16.310  1.00 10.33 ? 274  THR A CB  1 
ATOM   2146 O  OG1 . THR A 1 274  ? 27.649 54.623  17.362  1.00 10.61 ? 274  THR A OG1 1 
ATOM   2147 C  CG2 . THR A 1 274  ? 27.717 54.360  14.971  1.00 11.97 ? 274  THR A CG2 1 
ATOM   2148 N  N   . CYS A 1 275  ? 24.847 52.473  18.466  1.00 11.51 ? 275  CYS A N   1 
ATOM   2149 C  CA  . CYS A 1 275  ? 24.651 51.384  19.450  1.00 11.96 ? 275  CYS A CA  1 
ATOM   2150 C  C   . CYS A 1 275  ? 23.519 50.403  19.052  1.00 11.72 ? 275  CYS A C   1 
ATOM   2151 O  O   . CYS A 1 275  ? 23.457 49.253  19.528  1.00 13.12 ? 275  CYS A O   1 
ATOM   2152 C  CB  . CYS A 1 275  ? 24.393 51.976  20.847  1.00 12.64 ? 275  CYS A CB  1 
ATOM   2153 S  SG  . CYS A 1 275  ? 22.674 52.036  21.416  1.00 15.30 ? 275  CYS A SG  1 
ATOM   2154 N  N   . GLY A 1 276  ? 22.633 50.872  18.204  1.00 11.29 ? 276  GLY A N   1 
ATOM   2155 C  CA  . GLY A 1 276  ? 21.375 50.182  17.921  1.00 12.22 ? 276  GLY A CA  1 
ATOM   2156 C  C   . GLY A 1 276  ? 20.427 51.107  17.209  1.00 11.50 ? 276  GLY A C   1 
ATOM   2157 O  O   . GLY A 1 276  ? 20.802 52.239  16.896  1.00 11.66 ? 276  GLY A O   1 
ATOM   2158 N  N   . PRO A 1 277  ? 19.195 50.647  16.917  1.00 11.59 ? 277  PRO A N   1 
ATOM   2159 C  CA  . PRO A 1 277  ? 18.256 51.392  16.079  1.00 11.71 ? 277  PRO A CA  1 
ATOM   2160 C  C   . PRO A 1 277  ? 17.564 52.593  16.698  1.00 11.35 ? 277  PRO A C   1 
ATOM   2161 O  O   . PRO A 1 277  ? 16.973 53.341  15.934  1.00 11.60 ? 277  PRO A O   1 
ATOM   2162 C  CB  . PRO A 1 277  ? 17.159 50.354  15.758  1.00 12.35 ? 277  PRO A CB  1 
ATOM   2163 C  CG  . PRO A 1 277  ? 17.234 49.338  16.902  1.00 11.05 ? 277  PRO A CG  1 
ATOM   2164 C  CD  . PRO A 1 277  ? 18.684 49.307  17.289  1.00 12.65 ? 277  PRO A CD  1 
ATOM   2165 N  N   . ASP A 1 278  ? 17.620 52.748  18.009  1.00 11.89 ? 278  ASP A N   1 
ATOM   2166 C  CA  . ASP A 1 278  ? 16.880 53.835  18.662  1.00 12.21 ? 278  ASP A CA  1 
ATOM   2167 C  C   . ASP A 1 278  ? 17.826 54.887  19.235  1.00 11.67 ? 278  ASP A C   1 
ATOM   2168 O  O   . ASP A 1 278  ? 18.423 54.670  20.283  1.00 12.32 ? 278  ASP A O   1 
ATOM   2169 C  CB  . ASP A 1 278  ? 16.020 53.277  19.799  1.00 12.70 ? 278  ASP A CB  1 
ATOM   2170 C  CG  . ASP A 1 278  ? 15.128 54.331  20.409  1.00 15.88 ? 278  ASP A CG  1 
ATOM   2171 O  OD1 . ASP A 1 278  ? 15.224 55.544  20.078  1.00 17.78 ? 278  ASP A OD1 1 
ATOM   2172 O  OD2 . ASP A 1 278  ? 14.253 54.015  21.252  1.00 17.60 ? 278  ASP A OD2 1 
ATOM   2173 N  N   . PRO A 1 279  ? 17.969 56.012  18.535  1.00 12.78 ? 279  PRO A N   1 
ATOM   2174 C  CA  . PRO A 1 279  ? 18.948 57.010  19.005  1.00 13.63 ? 279  PRO A CA  1 
ATOM   2175 C  C   . PRO A 1 279  ? 18.594 57.642  20.346  1.00 13.09 ? 279  PRO A C   1 
ATOM   2176 O  O   . PRO A 1 279  ? 19.497 58.083  21.072  1.00 13.21 ? 279  PRO A O   1 
ATOM   2177 C  CB  . PRO A 1 279  ? 18.948 58.065  17.893  1.00 13.96 ? 279  PRO A CB  1 
ATOM   2178 C  CG  . PRO A 1 279  ? 17.621 57.933  17.239  1.00 14.29 ? 279  PRO A CG  1 
ATOM   2179 C  CD  . PRO A 1 279  ? 17.246 56.453  17.330  1.00 13.14 ? 279  PRO A CD  1 
ATOM   2180 N  N   . LYS A 1 280  ? 17.300 57.632  20.709  1.00 13.65 ? 280  LYS A N   1 
ATOM   2181 C  CA  . LYS A 1 280  ? 16.906 58.148  22.023  1.00 14.71 ? 280  LYS A CA  1 
ATOM   2182 C  C   . LYS A 1 280  ? 17.525 57.325  23.130  1.00 13.65 ? 280  LYS A C   1 
ATOM   2183 O  O   . LYS A 1 280  ? 17.911 57.854  24.170  1.00 15.25 ? 280  LYS A O   1 
ATOM   2184 C  CB  . LYS A 1 280  ? 15.386 58.178  22.148  1.00 15.01 ? 280  LYS A CB  1 
ATOM   2185 C  CG  . LYS A 1 280  ? 14.883 58.637  23.500  1.00 18.31 ? 280  LYS A CG  1 
ATOM   2186 C  CD  . LYS A 1 280  ? 13.357 58.583  23.525  1.00 22.80 ? 280  LYS A CD  1 
ATOM   2187 C  CE  . LYS A 1 280  ? 12.846 58.738  24.950  1.00 28.77 ? 280  LYS A CE  1 
ATOM   2188 N  NZ  . LYS A 1 280  ? 13.367 57.650  25.842  1.00 32.62 ? 280  LYS A NZ  1 
ATOM   2189 N  N   . VAL A 1 281  ? 17.687 56.023  22.881  1.00 13.91 ? 281  VAL A N   1 
ATOM   2190 C  CA  . VAL A 1 281  ? 18.359 55.137  23.822  1.00 13.97 ? 281  VAL A CA  1 
ATOM   2191 C  C   . VAL A 1 281  ? 19.895 55.218  23.701  1.00 13.23 ? 281  VAL A C   1 
ATOM   2192 O  O   . VAL A 1 281  ? 20.591 55.372  24.707  1.00 12.59 ? 281  VAL A O   1 
ATOM   2193 C  CB  . VAL A 1 281  ? 17.886 53.655  23.664  1.00 13.98 ? 281  VAL A CB  1 
ATOM   2194 C  CG1 . VAL A 1 281  ? 18.677 52.741  24.589  1.00 14.25 ? 281  VAL A CG1 1 
ATOM   2195 C  CG2 . VAL A 1 281  ? 16.339 53.555  23.906  1.00 13.74 ? 281  VAL A CG2 1 
ATOM   2196 N  N   . CYS A 1 282  ? 20.417 55.101  22.470  1.00 12.75 ? 282  CYS A N   1 
ATOM   2197 C  CA  . CYS A 1 282  ? 21.872 55.114  22.272  1.00 13.09 ? 282  CYS A CA  1 
ATOM   2198 C  C   . CYS A 1 282  ? 22.510 56.408  22.787  1.00 11.35 ? 282  CYS A C   1 
ATOM   2199 O  O   . CYS A 1 282  ? 23.609 56.369  23.322  1.00 11.63 ? 282  CYS A O   1 
ATOM   2200 C  CB  . CYS A 1 282  ? 22.205 54.954  20.791  1.00 12.77 ? 282  CYS A CB  1 
ATOM   2201 S  SG  . CYS A 1 282  ? 21.777 53.347  20.157  1.00 14.69 ? 282  CYS A SG  1 
ATOM   2202 N  N   . CYS A 1 283  ? 21.810 57.529  22.642  1.00 11.96 ? 283  CYS A N   1 
ATOM   2203 C  CA  . CYS A 1 283  ? 22.341 58.792  23.141  1.00 11.99 ? 283  CYS A CA  1 
ATOM   2204 C  C   . CYS A 1 283  ? 22.638 58.771  24.636  1.00 12.08 ? 283  CYS A C   1 
ATOM   2205 O  O   . CYS A 1 283  ? 23.527 59.462  25.102  1.00 11.94 ? 283  CYS A O   1 
ATOM   2206 C  CB  . CYS A 1 283  ? 21.397 59.932  22.800  1.00 12.94 ? 283  CYS A CB  1 
ATOM   2207 S  SG  . CYS A 1 283  ? 22.170 61.557  22.880  1.00 15.33 ? 283  CYS A SG  1 
ATOM   2208 N  N   . GLN A 1 284  ? 21.899 57.935  25.391  1.00 11.82 ? 284  GLN A N   1 
ATOM   2209 C  CA  . GLN A 1 284  ? 22.131 57.808  26.827  1.00 12.40 ? 284  GLN A CA  1 
ATOM   2210 C  C   . GLN A 1 284  ? 23.385 57.068  27.164  1.00 12.41 ? 284  GLN A C   1 
ATOM   2211 O  O   . GLN A 1 284  ? 23.766 56.978  28.324  1.00 13.90 ? 284  GLN A O   1 
ATOM   2212 C  CB  . GLN A 1 284  ? 20.945 57.118  27.509  1.00 12.29 ? 284  GLN A CB  1 
ATOM   2213 C  CG  . GLN A 1 284  ? 19.654 57.871  27.331  1.00 14.83 ? 284  GLN A CG  1 
ATOM   2214 C  CD  . GLN A 1 284  ? 18.472 57.071  27.853  1.00 15.60 ? 284  GLN A CD  1 
ATOM   2215 O  OE1 . GLN A 1 284  ? 18.492 56.614  29.006  1.00 17.19 ? 284  GLN A OE1 1 
ATOM   2216 N  NE2 . GLN A 1 284  ? 17.488 56.863  27.004  1.00 17.05 ? 284  GLN A NE2 1 
ATOM   2217 N  N   . PHE A 1 285  ? 24.056 56.541  26.133  1.00 11.67 ? 285  PHE A N   1 
ATOM   2218 C  CA  . PHE A 1 285  ? 25.313 55.835  26.333  1.00 11.82 ? 285  PHE A CA  1 
ATOM   2219 C  C   . PHE A 1 285  ? 26.500 56.583  25.691  1.00 11.44 ? 285  PHE A C   1 
ATOM   2220 O  O   . PHE A 1 285  ? 27.586 56.012  25.489  1.00 11.68 ? 285  PHE A O   1 
ATOM   2221 C  CB  . PHE A 1 285  ? 25.188 54.371  25.904  1.00 12.86 ? 285  PHE A CB  1 
ATOM   2222 C  CG  . PHE A 1 285  ? 24.188 53.633  26.750  1.00 11.86 ? 285  PHE A CG  1 
ATOM   2223 C  CD1 . PHE A 1 285  ? 24.573 53.042  27.942  1.00 13.38 ? 285  PHE A CD1 1 
ATOM   2224 C  CD2 . PHE A 1 285  ? 22.858 53.594  26.364  1.00 14.13 ? 285  PHE A CD2 1 
ATOM   2225 C  CE1 . PHE A 1 285  ? 23.608 52.408  28.776  1.00 12.02 ? 285  PHE A CE1 1 
ATOM   2226 C  CE2 . PHE A 1 285  ? 21.902 52.961  27.192  1.00 14.29 ? 285  PHE A CE2 1 
ATOM   2227 C  CZ  . PHE A 1 285  ? 22.296 52.361  28.367  1.00 14.46 ? 285  PHE A CZ  1 
ATOM   2228 N  N   . ASP A 1 286  ? 26.256 57.868  25.415  1.00 11.10 ? 286  ASP A N   1 
ATOM   2229 C  CA  . ASP A 1 286  ? 27.336 58.806  25.067  1.00 10.74 ? 286  ASP A CA  1 
ATOM   2230 C  C   . ASP A 1 286  ? 27.591 59.637  26.319  1.00 10.45 ? 286  ASP A C   1 
ATOM   2231 O  O   . ASP A 1 286  ? 26.908 60.640  26.537  1.00 11.92 ? 286  ASP A O   1 
ATOM   2232 C  CB  . ASP A 1 286  ? 26.914 59.686  23.907  1.00 11.57 ? 286  ASP A CB  1 
ATOM   2233 C  CG  . ASP A 1 286  ? 28.046 60.563  23.398  1.00 9.10  ? 286  ASP A CG  1 
ATOM   2234 O  OD1 . ASP A 1 286  ? 29.089 60.639  24.083  1.00 10.18 ? 286  ASP A OD1 1 
ATOM   2235 O  OD2 . ASP A 1 286  ? 27.876 61.229  22.350  1.00 11.60 ? 286  ASP A OD2 1 
ATOM   2236 N  N   . PHE A 1 287  ? 28.582 59.236  27.103  1.00 10.38 ? 287  PHE A N   1 
ATOM   2237 C  CA  . PHE A 1 287  ? 28.747 59.838  28.425  1.00 11.02 ? 287  PHE A CA  1 
ATOM   2238 C  C   . PHE A 1 287  ? 29.343 61.232  28.376  1.00 12.57 ? 287  PHE A C   1 
ATOM   2239 O  O   . PHE A 1 287  ? 29.423 61.903  29.427  1.00 13.18 ? 287  PHE A O   1 
ATOM   2240 C  CB  . PHE A 1 287  ? 29.484 58.867  29.368  1.00 11.17 ? 287  PHE A CB  1 
ATOM   2241 C  CG  . PHE A 1 287  ? 28.677 57.609  29.634  1.00 12.12 ? 287  PHE A CG  1 
ATOM   2242 C  CD1 . PHE A 1 287  ? 27.675 57.587  30.644  1.00 13.46 ? 287  PHE A CD1 1 
ATOM   2243 C  CD2 . PHE A 1 287  ? 28.850 56.475  28.854  1.00 12.39 ? 287  PHE A CD2 1 
ATOM   2244 C  CE1 . PHE A 1 287  ? 26.892 56.433  30.851  1.00 13.20 ? 287  PHE A CE1 1 
ATOM   2245 C  CE2 . PHE A 1 287  ? 28.073 55.311  29.056  1.00 13.57 ? 287  PHE A CE2 1 
ATOM   2246 C  CZ  . PHE A 1 287  ? 27.083 55.297  30.058  1.00 12.31 ? 287  PHE A CZ  1 
ATOM   2247 N  N   . LYS A 1 288  ? 29.655 61.733  27.173  1.00 12.70 ? 288  LYS A N   1 
ATOM   2248 C  CA  . LYS A 1 288  ? 30.049 63.129  27.046  1.00 12.68 ? 288  LYS A CA  1 
ATOM   2249 C  C   . LYS A 1 288  ? 28.844 64.073  27.027  1.00 13.73 ? 288  LYS A C   1 
ATOM   2250 O  O   . LYS A 1 288  ? 29.023 65.312  27.039  1.00 13.70 ? 288  LYS A O   1 
ATOM   2251 C  CB  . LYS A 1 288  ? 30.920 63.316  25.782  1.00 13.33 ? 288  LYS A CB  1 
ATOM   2252 C  CG  . LYS A 1 288  ? 31.756 64.598  25.849  1.00 12.06 ? 288  LYS A CG  1 
ATOM   2253 C  CD  . LYS A 1 288  ? 32.581 64.788  24.564  1.00 11.49 ? 288  LYS A CD  1 
ATOM   2254 C  CE  . LYS A 1 288  ? 33.394 66.054  24.727  1.00 12.99 ? 288  LYS A CE  1 
ATOM   2255 N  NZ  . LYS A 1 288  ? 34.450 66.190  23.635  1.00 14.14 ? 288  LYS A NZ  1 
ATOM   2256 N  N   . ARG A 1 289  ? 27.622 63.543  27.030  1.00 14.21 ? 289  ARG A N   1 
ATOM   2257 C  CA  . ARG A 1 289  ? 26.444 64.393  26.875  1.00 15.45 ? 289  ARG A CA  1 
ATOM   2258 C  C   . ARG A 1 289  ? 25.656 64.735  28.174  1.00 17.41 ? 289  ARG A C   1 
ATOM   2259 O  O   . ARG A 1 289  ? 24.454 64.982  28.097  1.00 17.78 ? 289  ARG A O   1 
ATOM   2260 C  CB  . ARG A 1 289  ? 25.492 63.774  25.849  1.00 14.31 ? 289  ARG A CB  1 
ATOM   2261 C  CG  . ARG A 1 289  ? 26.093 63.663  24.462  1.00 14.55 ? 289  ARG A CG  1 
ATOM   2262 C  CD  . ARG A 1 289  ? 25.105 63.224  23.469  1.00 14.20 ? 289  ARG A CD  1 
ATOM   2263 N  NE  . ARG A 1 289  ? 25.633 62.911  22.146  1.00 13.19 ? 289  ARG A NE  1 
ATOM   2264 C  CZ  . ARG A 1 289  ? 25.183 63.438  21.014  1.00 13.48 ? 289  ARG A CZ  1 
ATOM   2265 N  NH1 . ARG A 1 289  ? 24.226 64.359  21.013  1.00 15.12 ? 289  ARG A NH1 1 
ATOM   2266 N  NH2 . ARG A 1 289  ? 25.687 63.006  19.868  1.00 13.64 ? 289  ARG A NH2 1 
ATOM   2267 N  N   . MET A 1 290  ? 26.308 64.742  29.336  1.00 20.00 ? 290  MET A N   1 
ATOM   2268 C  CA  . MET A 1 290  ? 25.559 65.003  30.590  1.00 22.16 ? 290  MET A CA  1 
ATOM   2269 C  C   . MET A 1 290  ? 25.483 66.494  31.020  1.00 23.18 ? 290  MET A C   1 
ATOM   2270 O  O   . MET A 1 290  ? 24.718 66.840  31.962  1.00 24.85 ? 290  MET A O   1 
ATOM   2271 C  CB  . MET A 1 290  ? 25.989 64.058  31.738  1.00 21.35 ? 290  MET A CB  1 
ATOM   2272 C  CG  . MET A 1 290  ? 25.898 62.604  31.386  1.00 22.64 ? 290  MET A CG  1 
ATOM   2273 S  SD  . MET A 1 290  ? 26.347 61.475  32.754  1.00 24.39 ? 290  MET A SD  1 
ATOM   2274 C  CE  . MET A 1 290  ? 28.161 61.439  32.619  1.00 26.21 ? 290  MET A CE  1 
ATOM   2275 N  N   . GLY A 1 291  ? 26.245 67.368  30.340  1.00 22.88 ? 291  GLY A N   1 
ATOM   2276 C  CA  . GLY A 1 291  ? 26.121 68.811  30.533  1.00 21.74 ? 291  GLY A CA  1 
ATOM   2277 C  C   . GLY A 1 291  ? 27.400 69.664  30.629  1.00 21.46 ? 291  GLY A C   1 
ATOM   2278 O  O   . GLY A 1 291  ? 27.478 70.757  30.034  1.00 22.39 ? 291  GLY A O   1 
ATOM   2279 N  N   . SER A 1 292  ? 28.403 69.186  31.368  1.00 19.90 ? 292  SER A N   1 
ATOM   2280 C  CA  . SER A 1 292  ? 29.624 69.967  31.615  1.00 17.88 ? 292  SER A CA  1 
ATOM   2281 C  C   . SER A 1 292  ? 30.495 70.148  30.357  1.00 16.81 ? 292  SER A C   1 
ATOM   2282 O  O   . SER A 1 292  ? 31.393 71.016  30.339  1.00 15.43 ? 292  SER A O   1 
ATOM   2283 C  CB  . SER A 1 292  ? 30.443 69.289  32.704  1.00 19.61 ? 292  SER A CB  1 
ATOM   2284 O  OG  . SER A 1 292  ? 30.889 68.019  32.240  1.00 20.04 ? 292  SER A OG  1 
ATOM   2285 N  N   . PHE A 1 293  ? 30.242 69.311  29.340  1.00 14.79 ? 293  PHE A N   1 
ATOM   2286 C  CA  . PHE A 1 293  ? 30.948 69.384  28.060  1.00 14.65 ? 293  PHE A CA  1 
ATOM   2287 C  C   . PHE A 1 293  ? 30.175 70.219  27.050  1.00 14.25 ? 293  PHE A C   1 
ATOM   2288 O  O   . PHE A 1 293  ? 30.610 70.333  25.906  1.00 14.86 ? 293  PHE A O   1 
ATOM   2289 C  CB  . PHE A 1 293  ? 31.174 67.973  27.491  1.00 15.06 ? 293  PHE A CB  1 
ATOM   2290 C  CG  . PHE A 1 293  ? 32.076 67.124  28.327  1.00 14.81 ? 293  PHE A CG  1 
ATOM   2291 C  CD1 . PHE A 1 293  ? 33.453 67.235  28.218  1.00 14.40 ? 293  PHE A CD1 1 
ATOM   2292 C  CD2 . PHE A 1 293  ? 31.539 66.210  29.206  1.00 15.91 ? 293  PHE A CD2 1 
ATOM   2293 C  CE1 . PHE A 1 293  ? 34.306 66.423  28.989  1.00 16.44 ? 293  PHE A CE1 1 
ATOM   2294 C  CE2 . PHE A 1 293  ? 32.378 65.398  29.986  1.00 16.22 ? 293  PHE A CE2 1 
ATOM   2295 C  CZ  . PHE A 1 293  ? 33.745 65.519  29.870  1.00 16.55 ? 293  PHE A CZ  1 
ATOM   2296 N  N   . GLY A 1 294  ? 29.037 70.784  27.450  1.00 14.28 ? 294  GLY A N   1 
ATOM   2297 C  CA  . GLY A 1 294  ? 28.279 71.602  26.523  1.00 15.61 ? 294  GLY A CA  1 
ATOM   2298 C  C   . GLY A 1 294  ? 27.582 70.799  25.437  1.00 15.89 ? 294  GLY A C   1 
ATOM   2299 O  O   . GLY A 1 294  ? 27.275 71.302  24.354  1.00 16.25 ? 294  GLY A O   1 
ATOM   2300 N  N   . LEU A 1 295  ? 27.347 69.527  25.732  1.00 14.99 ? 295  LEU A N   1 
ATOM   2301 C  CA  . LEU A 1 295  ? 26.608 68.658  24.835  1.00 15.19 ? 295  LEU A CA  1 
ATOM   2302 C  C   . LEU A 1 295  ? 25.378 68.122  25.550  1.00 16.28 ? 295  LEU A C   1 
ATOM   2303 O  O   . LEU A 1 295  ? 25.332 68.067  26.773  1.00 17.03 ? 295  LEU A O   1 
ATOM   2304 C  CB  . LEU A 1 295  ? 27.500 67.523  24.321  1.00 15.83 ? 295  LEU A CB  1 
ATOM   2305 C  CG  . LEU A 1 295  ? 28.794 67.916  23.607  1.00 15.29 ? 295  LEU A CG  1 
ATOM   2306 C  CD1 . LEU A 1 295  ? 29.600 66.633  23.351  1.00 17.95 ? 295  LEU A CD1 1 
ATOM   2307 C  CD2 . LEU A 1 295  ? 28.516 68.699  22.301  1.00 18.58 ? 295  LEU A CD2 1 
ATOM   2308 N  N   . SER A 1 296  ? 24.385 67.745  24.755  1.00 16.52 ? 296  SER A N   1 
ATOM   2309 C  CA  . SER A 1 296  ? 23.133 67.189  25.288  1.00 17.83 ? 296  SER A CA  1 
ATOM   2310 C  C   . SER A 1 296  ? 22.557 66.238  24.268  1.00 18.10 ? 296  SER A C   1 
ATOM   2311 O  O   . SER A 1 296  ? 23.085 66.110  23.165  1.00 16.95 ? 296  SER A O   1 
ATOM   2312 C  CB  . SER A 1 296  ? 22.135 68.311  25.656  1.00 18.01 ? 296  SER A CB  1 
ATOM   2313 O  OG  . SER A 1 296  ? 21.872 69.171  24.561  1.00 20.65 ? 296  SER A OG  1 
ATOM   2314 N  N   . CYS A 1 297  ? 21.486 65.540  24.661  1.00 17.07 ? 297  CYS A N   1 
ATOM   2315 C  CA  . CYS A 1 297  ? 20.774 64.594  23.801  1.00 18.01 ? 297  CYS A CA  1 
ATOM   2316 C  C   . CYS A 1 297  ? 19.516 65.251  23.239  1.00 18.24 ? 297  CYS A C   1 
ATOM   2317 O  O   . CYS A 1 297  ? 18.641 65.652  24.029  1.00 19.34 ? 297  CYS A O   1 
ATOM   2318 C  CB  . CYS A 1 297  ? 20.388 63.361  24.637  1.00 17.81 ? 297  CYS A CB  1 
ATOM   2319 S  SG  . CYS A 1 297  ? 21.776 62.200  24.836  1.00 19.58 ? 297  CYS A SG  1 
ATOM   2320 N  N   . PRO A 1 298  ? 19.416 65.418  21.919  1.00 18.87 ? 298  PRO A N   1 
ATOM   2321 C  CA  . PRO A 1 298  ? 18.230 66.058  21.318  1.00 19.32 ? 298  PRO A CA  1 
ATOM   2322 C  C   . PRO A 1 298  ? 16.936 65.262  21.515  1.00 19.00 ? 298  PRO A C   1 
ATOM   2323 O  O   . PRO A 1 298  ? 15.856 65.847  21.349  1.00 19.89 ? 298  PRO A O   1 
ATOM   2324 C  CB  . PRO A 1 298  ? 18.591 66.212  19.830  1.00 20.95 ? 298  PRO A CB  1 
ATOM   2325 C  CG  . PRO A 1 298  ? 19.814 65.398  19.594  1.00 20.11 ? 298  PRO A CG  1 
ATOM   2326 C  CD  . PRO A 1 298  ? 20.460 65.116  20.912  1.00 18.51 ? 298  PRO A CD  1 
ATOM   2327 N  N   . TRP A 1 299  ? 17.037 63.993  21.898  1.00 18.62 ? 299  TRP A N   1 
ATOM   2328 C  CA  . TRP A 1 299  ? 15.847 63.167  22.183  1.00 18.34 ? 299  TRP A CA  1 
ATOM   2329 C  C   . TRP A 1 299  ? 15.388 63.331  23.625  1.00 19.66 ? 299  TRP A C   1 
ATOM   2330 O  O   . TRP A 1 299  ? 14.450 62.652  24.073  1.00 19.48 ? 299  TRP A O   1 
ATOM   2331 C  CB  . TRP A 1 299  ? 16.121 61.685  21.850  1.00 17.28 ? 299  TRP A CB  1 
ATOM   2332 C  CG  . TRP A 1 299  ? 16.490 61.516  20.412  1.00 17.05 ? 299  TRP A CG  1 
ATOM   2333 C  CD1 . TRP A 1 299  ? 15.643 61.345  19.374  1.00 15.98 ? 299  TRP A CD1 1 
ATOM   2334 C  CD2 . TRP A 1 299  ? 17.809 61.609  19.848  1.00 15.87 ? 299  TRP A CD2 1 
ATOM   2335 N  NE1 . TRP A 1 299  ? 16.342 61.287  18.187  1.00 17.45 ? 299  TRP A NE1 1 
ATOM   2336 C  CE2 . TRP A 1 299  ? 17.678 61.427  18.461  1.00 17.07 ? 299  TRP A CE2 1 
ATOM   2337 C  CE3 . TRP A 1 299  ? 19.084 61.781  20.390  1.00 16.98 ? 299  TRP A CE3 1 
ATOM   2338 C  CZ2 . TRP A 1 299  ? 18.773 61.460  17.595  1.00 16.57 ? 299  TRP A CZ2 1 
ATOM   2339 C  CZ3 . TRP A 1 299  ? 20.173 61.787  19.534  1.00 17.16 ? 299  TRP A CZ3 1 
ATOM   2340 C  CH2 . TRP A 1 299  ? 20.004 61.637  18.153  1.00 16.15 ? 299  TRP A CH2 1 
ATOM   2341 N  N   . LYS A 1 300  ? 16.075 64.202  24.356  1.00 19.97 ? 300  LYS A N   1 
ATOM   2342 C  CA  . LYS A 1 300  ? 15.612 64.734  25.652  1.00 20.69 ? 300  LYS A CA  1 
ATOM   2343 C  C   . LYS A 1 300  ? 15.772 63.812  26.861  1.00 21.13 ? 300  LYS A C   1 
ATOM   2344 O  O   . LYS A 1 300  ? 15.285 64.111  27.962  1.00 21.70 ? 300  LYS A O   1 
ATOM   2345 C  CB  . LYS A 1 300  ? 14.168 65.219  25.551  1.00 21.37 ? 300  LYS A CB  1 
ATOM   2346 C  CG  . LYS A 1 300  ? 13.994 66.392  24.636  1.00 21.97 ? 300  LYS A CG  1 
ATOM   2347 C  CD  . LYS A 1 300  ? 12.506 66.721  24.517  1.00 28.20 ? 300  LYS A CD  1 
ATOM   2348 C  CE  . LYS A 1 300  ? 12.224 67.686  23.380  1.00 31.83 ? 300  LYS A CE  1 
ATOM   2349 N  NZ  . LYS A 1 300  ? 10.781 67.577  22.979  1.00 36.74 ? 300  LYS A NZ  1 
ATOM   2350 N  N   . VAL A 1 301  ? 16.446 62.684  26.683  1.00 20.36 ? 301  VAL A N   1 
ATOM   2351 C  CA  . VAL A 1 301  ? 16.773 61.823  27.802  1.00 19.75 ? 301  VAL A CA  1 
ATOM   2352 C  C   . VAL A 1 301  ? 18.296 61.807  27.904  1.00 19.12 ? 301  VAL A C   1 
ATOM   2353 O  O   . VAL A 1 301  ? 18.968 61.317  26.982  1.00 20.46 ? 301  VAL A O   1 
ATOM   2354 C  CB  . VAL A 1 301  ? 16.231 60.382  27.626  1.00 19.56 ? 301  VAL A CB  1 
ATOM   2355 C  CG1 . VAL A 1 301  ? 16.526 59.563  28.878  1.00 20.13 ? 301  VAL A CG1 1 
ATOM   2356 C  CG2 . VAL A 1 301  ? 14.726 60.400  27.351  1.00 21.51 ? 301  VAL A CG2 1 
ATOM   2357 N  N   . PRO A 1 302  ? 18.849 62.342  28.984  1.00 18.26 ? 302  PRO A N   1 
ATOM   2358 C  CA  . PRO A 1 302  ? 20.303 62.457  29.109  1.00 18.23 ? 302  PRO A CA  1 
ATOM   2359 C  C   . PRO A 1 302  ? 20.932 61.125  29.497  1.00 18.00 ? 302  PRO A C   1 
ATOM   2360 O  O   . PRO A 1 302  ? 20.265 60.226  30.010  1.00 18.23 ? 302  PRO A O   1 
ATOM   2361 C  CB  . PRO A 1 302  ? 20.484 63.503  30.221  1.00 19.15 ? 302  PRO A CB  1 
ATOM   2362 C  CG  . PRO A 1 302  ? 19.164 63.572  30.940  1.00 19.57 ? 302  PRO A CG  1 
ATOM   2363 C  CD  . PRO A 1 302  ? 18.126 62.884  30.155  1.00 18.26 ? 302  PRO A CD  1 
ATOM   2364 N  N   . PRO A 1 303  ? 22.238 60.987  29.304  1.00 16.56 ? 303  PRO A N   1 
ATOM   2365 C  CA  . PRO A 1 303  ? 22.944 59.838  29.862  1.00 16.77 ? 303  PRO A CA  1 
ATOM   2366 C  C   . PRO A 1 303  ? 22.908 59.967  31.367  1.00 18.54 ? 303  PRO A C   1 
ATOM   2367 O  O   . PRO A 1 303  ? 22.834 61.093  31.879  1.00 18.49 ? 303  PRO A O   1 
ATOM   2368 C  CB  . PRO A 1 303  ? 24.402 60.032  29.406  1.00 16.65 ? 303  PRO A CB  1 
ATOM   2369 C  CG  . PRO A 1 303  ? 24.398 61.186  28.485  1.00 17.64 ? 303  PRO A CG  1 
ATOM   2370 C  CD  . PRO A 1 303  ? 23.140 61.950  28.644  1.00 17.25 ? 303  PRO A CD  1 
ATOM   2371 N  N   . ARG A 1 304  ? 22.961 58.833  32.050  1.00 18.69 ? 304  ARG A N   1 
ATOM   2372 C  CA  . ARG A 1 304  ? 23.150 58.825  33.494  1.00 20.77 ? 304  ARG A CA  1 
ATOM   2373 C  C   . ARG A 1 304  ? 24.372 58.007  33.857  1.00 17.99 ? 304  ARG A C   1 
ATOM   2374 O  O   . ARG A 1 304  ? 24.607 56.930  33.261  1.00 17.74 ? 304  ARG A O   1 
ATOM   2375 C  CB  . ARG A 1 304  ? 21.913 58.230  34.171  1.00 21.23 ? 304  ARG A CB  1 
ATOM   2376 C  CG  . ARG A 1 304  ? 20.684 59.124  34.061  1.00 25.38 ? 304  ARG A CG  1 
ATOM   2377 C  CD  . ARG A 1 304  ? 19.444 58.524  34.682  1.00 25.80 ? 304  ARG A CD  1 
ATOM   2378 N  NE  . ARG A 1 304  ? 18.774 57.593  33.770  1.00 34.89 ? 304  ARG A NE  1 
ATOM   2379 C  CZ  . ARG A 1 304  ? 17.742 56.820  34.106  1.00 38.38 ? 304  ARG A CZ  1 
ATOM   2380 N  NH1 . ARG A 1 304  ? 17.241 56.858  35.337  1.00 40.66 ? 304  ARG A NH1 1 
ATOM   2381 N  NH2 . ARG A 1 304  ? 17.200 56.008  33.206  1.00 39.98 ? 304  ARG A NH2 1 
ATOM   2382 N  N   . THR A 1 305  ? 25.159 58.515  34.805  1.00 17.83 ? 305  THR A N   1 
ATOM   2383 C  CA  . THR A 1 305  ? 26.324 57.812  35.319  1.00 17.32 ? 305  THR A CA  1 
ATOM   2384 C  C   . THR A 1 305  ? 25.951 56.391  35.756  1.00 16.64 ? 305  THR A C   1 
ATOM   2385 O  O   . THR A 1 305  ? 24.913 56.197  36.429  1.00 17.05 ? 305  THR A O   1 
ATOM   2386 C  CB  . THR A 1 305  ? 26.951 58.609  36.491  1.00 17.70 ? 305  THR A CB  1 
ATOM   2387 O  OG1 . THR A 1 305  ? 27.517 59.827  35.972  1.00 21.41 ? 305  THR A OG1 1 
ATOM   2388 C  CG2 . THR A 1 305  ? 28.107 57.878  37.070  1.00 18.81 ? 305  THR A CG2 1 
ATOM   2389 N  N   . ILE A 1 306  ? 26.727 55.397  35.346  1.00 15.68 ? 306  ILE A N   1 
ATOM   2390 C  CA  . ILE A 1 306  ? 26.428 54.016  35.725  1.00 15.45 ? 306  ILE A CA  1 
ATOM   2391 C  C   . ILE A 1 306  ? 26.848 53.791  37.172  1.00 16.32 ? 306  ILE A C   1 
ATOM   2392 O  O   . ILE A 1 306  ? 27.948 54.153  37.581  1.00 16.92 ? 306  ILE A O   1 
ATOM   2393 C  CB  . ILE A 1 306  ? 27.095 53.015  34.744  1.00 15.11 ? 306  ILE A CB  1 
ATOM   2394 C  CG1 . ILE A 1 306  ? 26.724 53.336  33.279  1.00 13.79 ? 306  ILE A CG1 1 
ATOM   2395 C  CG2 . ILE A 1 306  ? 26.724 51.541  35.099  1.00 14.78 ? 306  ILE A CG2 1 
ATOM   2396 C  CD1 . ILE A 1 306  ? 25.239 53.280  32.931  1.00 14.56 ? 306  ILE A CD1 1 
ATOM   2397 N  N   . SER A 1 307  ? 25.919 53.207  37.942  1.00 18.30 ? 307  SER A N   1 
ATOM   2398 C  CA  . SER A 1 307  ? 26.114 52.912  39.365  1.00 18.86 ? 307  SER A CA  1 
ATOM   2399 C  C   . SER A 1 307  ? 25.627 51.488  39.601  1.00 19.90 ? 307  SER A C   1 
ATOM   2400 O  O   . SER A 1 307  ? 24.871 50.933  38.778  1.00 18.68 ? 307  SER A O   1 
ATOM   2401 C  CB  . SER A 1 307  ? 25.224 53.831  40.211  1.00 18.61 ? 307  SER A CB  1 
ATOM   2402 O  OG  . SER A 1 307  ? 23.849 53.520  40.031  1.00 18.08 ? 307  SER A OG  1 
ATOM   2403 N  N   . ASP A 1 308  ? 25.951 50.932  40.765  1.00 21.48 ? 308  ASP A N   1 
ATOM   2404 C  CA  . ASP A 1 308  ? 25.391 49.624  41.129  1.00 22.87 ? 308  ASP A CA  1 
ATOM   2405 C  C   . ASP A 1 308  ? 23.854 49.569  41.157  1.00 22.18 ? 308  ASP A C   1 
ATOM   2406 O  O   . ASP A 1 308  ? 23.275 48.516  40.880  1.00 21.16 ? 308  ASP A O   1 
ATOM   2407 C  CB  . ASP A 1 308  ? 25.951 49.163  42.465  1.00 24.59 ? 308  ASP A CB  1 
ATOM   2408 C  CG  . ASP A 1 308  ? 27.455 49.060  42.465  1.00 27.09 ? 308  ASP A CG  1 
ATOM   2409 O  OD1 . ASP A 1 308  ? 28.072 48.839  41.393  1.00 31.96 ? 308  ASP A OD1 1 
ATOM   2410 O  OD2 . ASP A 1 308  ? 28.122 49.190  43.513  1.00 34.20 ? 308  ASP A OD2 1 
ATOM   2411 N  N   . GLN A 1 309  ? 23.194 50.693  41.431  1.00 21.26 ? 309  GLN A N   1 
ATOM   2412 C  CA  A GLN A 1 309  ? 21.718 50.748  41.534  0.50 20.94 ? 309  GLN A CA  1 
ATOM   2413 C  CA  B GLN A 1 309  ? 21.748 50.732  41.547  0.50 21.45 ? 309  GLN A CA  1 
ATOM   2414 C  C   . GLN A 1 309  ? 21.008 50.899  40.209  1.00 21.13 ? 309  GLN A C   1 
ATOM   2415 O  O   . GLN A 1 309  ? 19.776 50.682  40.118  1.00 21.81 ? 309  GLN A O   1 
ATOM   2416 C  CB  A GLN A 1 309  ? 21.216 51.879  42.452  0.50 20.24 ? 309  GLN A CB  1 
ATOM   2417 C  CB  B GLN A 1 309  ? 21.405 51.802  42.581  0.50 21.46 ? 309  GLN A CB  1 
ATOM   2418 C  CG  A GLN A 1 309  ? 21.633 51.746  43.906  0.50 18.55 ? 309  GLN A CG  1 
ATOM   2419 C  CG  B GLN A 1 309  ? 20.266 52.713  42.322  0.50 21.17 ? 309  GLN A CG  1 
ATOM   2420 C  CD  A GLN A 1 309  ? 23.111 51.978  44.067  0.50 16.65 ? 309  GLN A CD  1 
ATOM   2421 C  CD  B GLN A 1 309  ? 20.242 53.836  43.334  0.50 19.16 ? 309  GLN A CD  1 
ATOM   2422 O  OE1 A GLN A 1 309  ? 23.653 52.928  43.485  0.50 15.11 ? 309  GLN A OE1 1 
ATOM   2423 O  OE1 B GLN A 1 309  ? 20.820 53.701  44.415  0.50 20.06 ? 309  GLN A OE1 1 
ATOM   2424 N  NE2 A GLN A 1 309  ? 23.778 51.102  44.813  0.50 17.08 ? 309  GLN A NE2 1 
ATOM   2425 N  NE2 B GLN A 1 309  ? 19.590 54.938  42.998  0.50 19.33 ? 309  GLN A NE2 1 
ATOM   2426 N  N   . ASN A 1 310  ? 21.753 51.284  39.169  1.00 19.96 ? 310  ASN A N   1 
ATOM   2427 C  CA  . ASN A 1 310  ? 21.123 51.409  37.868  1.00 18.16 ? 310  ASN A CA  1 
ATOM   2428 C  C   . ASN A 1 310  ? 21.722 50.466  36.811  1.00 17.07 ? 310  ASN A C   1 
ATOM   2429 O  O   . ASN A 1 310  ? 21.158 50.354  35.742  1.00 16.76 ? 310  ASN A O   1 
ATOM   2430 C  CB  . ASN A 1 310  ? 21.088 52.864  37.374  1.00 18.30 ? 310  ASN A CB  1 
ATOM   2431 C  CG  . ASN A 1 310  ? 22.478 53.412  37.037  1.00 17.33 ? 310  ASN A CG  1 
ATOM   2432 O  OD1 . ASN A 1 310  ? 23.442 52.665  36.855  1.00 18.12 ? 310  ASN A OD1 1 
ATOM   2433 N  ND2 . ASN A 1 310  ? 22.566 54.731  36.970  1.00 19.32 ? 310  ASN A ND2 1 
ATOM   2434 N  N   . VAL A 1 311  ? 22.820 49.806  37.132  1.00 16.06 ? 311  VAL A N   1 
ATOM   2435 C  CA  . VAL A 1 311  ? 23.563 49.087  36.058  1.00 16.51 ? 311  VAL A CA  1 
ATOM   2436 C  C   . VAL A 1 311  ? 22.701 47.980  35.432  1.00 17.75 ? 311  VAL A C   1 
ATOM   2437 O  O   . VAL A 1 311  ? 22.812 47.712  34.233  1.00 17.30 ? 311  VAL A O   1 
ATOM   2438 C  CB  . VAL A 1 311  ? 24.933 48.576  36.514  1.00 16.56 ? 311  VAL A CB  1 
ATOM   2439 C  CG1 . VAL A 1 311  ? 24.812 47.486  37.586  1.00 18.24 ? 311  VAL A CG1 1 
ATOM   2440 C  CG2 . VAL A 1 311  ? 25.784 48.066  35.292  1.00 16.93 ? 311  VAL A CG2 1 
ATOM   2441 N  N   . ALA A 1 312  ? 21.843 47.317  36.220  1.00 17.28 ? 312  ALA A N   1 
ATOM   2442 C  CA  . ALA A 1 312  ? 21.018 46.244  35.647  1.00 17.29 ? 312  ALA A CA  1 
ATOM   2443 C  C   . ALA A 1 312  ? 20.044 46.800  34.641  1.00 17.98 ? 312  ALA A C   1 
ATOM   2444 O  O   . ALA A 1 312  ? 19.911 46.238  33.549  1.00 18.43 ? 312  ALA A O   1 
ATOM   2445 C  CB  . ALA A 1 312  ? 20.279 45.447  36.751  1.00 17.86 ? 312  ALA A CB  1 
ATOM   2446 N  N   . ALA A 1 313  ? 19.364 47.895  34.973  1.00 16.66 ? 313  ALA A N   1 
ATOM   2447 C  CA  . ALA A 1 313  ? 18.398 48.522  34.091  1.00 17.99 ? 313  ALA A CA  1 
ATOM   2448 C  C   . ALA A 1 313  ? 19.102 49.115  32.869  1.00 17.57 ? 313  ALA A C   1 
ATOM   2449 O  O   . ALA A 1 313  ? 18.601 49.010  31.766  1.00 17.49 ? 313  ALA A O   1 
ATOM   2450 C  CB  . ALA A 1 313  ? 17.614 49.617  34.828  1.00 18.19 ? 313  ALA A CB  1 
ATOM   2451 N  N   . ARG A 1 314  ? 20.231 49.776  33.095  1.00 17.41 ? 314  ARG A N   1 
ATOM   2452 C  CA  . ARG A 1 314  ? 21.001 50.375  31.991  1.00 16.53 ? 314  ARG A CA  1 
ATOM   2453 C  C   . ARG A 1 314  ? 21.487 49.284  31.041  1.00 15.57 ? 314  ARG A C   1 
ATOM   2454 O  O   . ARG A 1 314  ? 21.365 49.454  29.821  1.00 15.66 ? 314  ARG A O   1 
ATOM   2455 C  CB  . ARG A 1 314  ? 22.174 51.166  32.559  1.00 15.65 ? 314  ARG A CB  1 
ATOM   2456 C  CG  . ARG A 1 314  ? 21.780 52.353  33.425  1.00 17.10 ? 314  ARG A CG  1 
ATOM   2457 C  CD  . ARG A 1 314  ? 21.540 53.615  32.658  1.00 21.05 ? 314  ARG A CD  1 
ATOM   2458 N  NE  . ARG A 1 314  ? 20.187 53.655  32.155  1.00 22.63 ? 314  ARG A NE  1 
ATOM   2459 C  CZ  . ARG A 1 314  ? 19.709 54.559  31.318  1.00 22.42 ? 314  ARG A CZ  1 
ATOM   2460 N  NH1 . ARG A 1 314  ? 20.497 55.530  30.837  1.00 24.30 ? 314  ARG A NH1 1 
ATOM   2461 N  NH2 . ARG A 1 314  ? 18.429 54.509  30.963  1.00 23.79 ? 314  ARG A NH2 1 
ATOM   2462 N  N   . SER A 1 315  ? 22.008 48.193  31.596  1.00 14.96 ? 315  SER A N   1 
ATOM   2463 C  CA  . SER A 1 315  ? 22.469 47.038  30.794  1.00 15.74 ? 315  SER A CA  1 
ATOM   2464 C  C   . SER A 1 315  ? 21.335 46.411  30.008  1.00 16.99 ? 315  SER A C   1 
ATOM   2465 O  O   . SER A 1 315  ? 21.521 46.017  28.854  1.00 17.82 ? 315  SER A O   1 
ATOM   2466 C  CB  . SER A 1 315  ? 23.124 45.991  31.673  1.00 15.91 ? 315  SER A CB  1 
ATOM   2467 O  OG  . SER A 1 315  ? 24.302 46.476  32.265  1.00 16.19 ? 315  SER A OG  1 
ATOM   2468 N  N   . ASP A 1 316  ? 20.161 46.268  30.623  1.00 17.01 ? 316  ASP A N   1 
ATOM   2469 C  CA  A ASP A 1 316  ? 19.051 45.722  29.886  0.50 17.30 ? 316  ASP A CA  1 
ATOM   2470 C  CA  B ASP A 1 316  ? 18.921 45.820  29.943  0.50 17.67 ? 316  ASP A CA  1 
ATOM   2471 C  C   . ASP A 1 316  ? 18.730 46.580  28.654  1.00 17.37 ? 316  ASP A C   1 
ATOM   2472 O  O   . ASP A 1 316  ? 18.528 46.014  27.569  1.00 16.91 ? 316  ASP A O   1 
ATOM   2473 C  CB  A ASP A 1 316  ? 17.861 45.587  30.814  0.50 17.14 ? 316  ASP A CB  1 
ATOM   2474 C  CB  B ASP A 1 316  ? 17.663 46.175  30.764  0.50 18.38 ? 316  ASP A CB  1 
ATOM   2475 C  CG  A ASP A 1 316  ? 16.989 44.414  30.474  0.50 18.12 ? 316  ASP A CG  1 
ATOM   2476 C  CG  B ASP A 1 316  ? 17.394 45.244  31.921  0.50 18.49 ? 316  ASP A CG  1 
ATOM   2477 O  OD1 A ASP A 1 316  ? 17.519 43.356  30.069  0.50 18.05 ? 316  ASP A OD1 1 
ATOM   2478 O  OD1 B ASP A 1 316  ? 18.042 44.191  32.009  0.50 19.69 ? 316  ASP A OD1 1 
ATOM   2479 O  OD2 A ASP A 1 316  ? 15.757 44.474  30.613  0.50 20.07 ? 316  ASP A OD2 1 
ATOM   2480 O  OD2 B ASP A 1 316  ? 16.520 45.507  32.790  0.50 20.06 ? 316  ASP A OD2 1 
ATOM   2481 N  N   . LEU A 1 317  ? 18.716 47.906  28.797  1.00 16.68 ? 317  LEU A N   1 
ATOM   2482 C  CA  . LEU A 1 317  ? 18.421 48.808  27.687  1.00 16.58 ? 317  LEU A CA  1 
ATOM   2483 C  C   . LEU A 1 317  ? 19.482 48.707  26.590  1.00 14.64 ? 317  LEU A C   1 
ATOM   2484 O  O   . LEU A 1 317  ? 19.136 48.643  25.419  1.00 15.22 ? 317  LEU A O   1 
ATOM   2485 C  CB  . LEU A 1 317  ? 18.348 50.270  28.157  1.00 17.61 ? 317  LEU A CB  1 
ATOM   2486 C  CG  . LEU A 1 317  ? 16.980 50.822  28.555  1.00 21.64 ? 317  LEU A CG  1 
ATOM   2487 C  CD1 . LEU A 1 317  ? 17.168 52.146  29.292  1.00 25.26 ? 317  LEU A CD1 1 
ATOM   2488 C  CD2 . LEU A 1 317  ? 16.046 50.984  27.358  1.00 24.95 ? 317  LEU A CD2 1 
ATOM   2489 N  N   . LEU A 1 318  ? 20.742 48.638  27.007  1.00 13.93 ? 318  LEU A N   1 
ATOM   2490 C  CA  . LEU A 1 318  ? 21.871 48.643  26.049  1.00 13.10 ? 318  LEU A CA  1 
ATOM   2491 C  C   . LEU A 1 318  ? 21.961 47.317  25.311  1.00 13.44 ? 318  LEU A C   1 
ATOM   2492 O  O   . LEU A 1 318  ? 22.087 47.292  24.066  1.00 13.47 ? 318  LEU A O   1 
ATOM   2493 C  CB  . LEU A 1 318  ? 23.175 48.965  26.757  1.00 13.30 ? 318  LEU A CB  1 
ATOM   2494 C  CG  . LEU A 1 318  ? 24.413 49.087  25.837  1.00 13.39 ? 318  LEU A CG  1 
ATOM   2495 C  CD1 . LEU A 1 318  ? 24.225 50.175  24.759  1.00 15.22 ? 318  LEU A CD1 1 
ATOM   2496 C  CD2 . LEU A 1 318  ? 25.641 49.364  26.686  1.00 14.76 ? 318  LEU A CD2 1 
ATOM   2497 N  N   . VAL A 1 319  ? 21.848 46.203  26.034  1.00 12.82 ? 319  VAL A N   1 
ATOM   2498 C  CA  . VAL A 1 319  ? 21.926 44.883  25.403  1.00 12.63 ? 319  VAL A CA  1 
ATOM   2499 C  C   . VAL A 1 319  ? 20.768 44.712  24.434  1.00 12.59 ? 319  VAL A C   1 
ATOM   2500 O  O   . VAL A 1 319  ? 20.940 44.117  23.374  1.00 12.86 ? 319  VAL A O   1 
ATOM   2501 C  CB  . VAL A 1 319  ? 21.957 43.733  26.448  1.00 13.56 ? 319  VAL A CB  1 
ATOM   2502 C  CG1 . VAL A 1 319  ? 21.808 42.361  25.769  1.00 13.48 ? 319  VAL A CG1 1 
ATOM   2503 C  CG2 . VAL A 1 319  ? 23.243 43.788  27.244  1.00 13.63 ? 319  VAL A CG2 1 
ATOM   2504 N  N   . ASP A 1 320  ? 19.604 45.232  24.811  1.00 13.46 ? 320  ASP A N   1 
ATOM   2505 C  CA  . ASP A 1 320  ? 18.448 45.272  23.926  1.00 13.59 ? 320  ASP A CA  1 
ATOM   2506 C  C   . ASP A 1 320  ? 18.796 45.909  22.586  1.00 13.01 ? 320  ASP A C   1 
ATOM   2507 O  O   . ASP A 1 320  ? 18.531 45.333  21.531  1.00 12.18 ? 320  ASP A O   1 
ATOM   2508 C  CB  . ASP A 1 320  ? 17.294 46.030  24.584  1.00 15.12 ? 320  ASP A CB  1 
ATOM   2509 C  CG  . ASP A 1 320  ? 16.009 45.945  23.784  1.00 15.09 ? 320  ASP A CG  1 
ATOM   2510 O  OD1 . ASP A 1 320  ? 15.551 44.815  23.512  1.00 18.93 ? 320  ASP A OD1 1 
ATOM   2511 O  OD2 . ASP A 1 320  ? 15.457 47.007  23.428  1.00 17.57 ? 320  ASP A OD2 1 
ATOM   2512 N  N   . GLN A 1 321  ? 19.390 47.098  22.629  1.00 12.31 ? 321  GLN A N   1 
ATOM   2513 C  CA  . GLN A 1 321  ? 19.834 47.768  21.379  1.00 11.77 ? 321  GLN A CA  1 
ATOM   2514 C  C   . GLN A 1 321  ? 20.834 46.914  20.586  1.00 10.14 ? 321  GLN A C   1 
ATOM   2515 O  O   . GLN A 1 321  ? 20.696 46.768  19.384  1.00 11.55 ? 321  GLN A O   1 
ATOM   2516 C  CB  . GLN A 1 321  ? 20.449 49.129  21.707  1.00 11.20 ? 321  GLN A CB  1 
ATOM   2517 C  CG  . GLN A 1 321  ? 19.453 50.154  22.170  1.00 13.33 ? 321  GLN A CG  1 
ATOM   2518 C  CD  . GLN A 1 321  ? 18.380 50.388  21.113  1.00 14.52 ? 321  GLN A CD  1 
ATOM   2519 O  OE1 . GLN A 1 321  ? 18.672 50.803  19.994  1.00 14.60 ? 321  GLN A OE1 1 
ATOM   2520 N  NE2 . GLN A 1 321  ? 17.112 50.133  21.468  1.00 14.79 ? 321  GLN A NE2 1 
ATOM   2521 N  N   . TRP A 1 322  ? 21.825 46.384  21.284  1.00 10.36 ? 322  TRP A N   1 
ATOM   2522 C  CA  . TRP A 1 322  ? 22.824 45.554  20.624  1.00 11.37 ? 322  TRP A CA  1 
ATOM   2523 C  C   . TRP A 1 322  ? 22.205 44.357  19.929  1.00 11.90 ? 322  TRP A C   1 
ATOM   2524 O  O   . TRP A 1 322  ? 22.565 44.014  18.794  1.00 11.83 ? 322  TRP A O   1 
ATOM   2525 C  CB  . TRP A 1 322  ? 23.837 45.070  21.628  1.00 11.48 ? 322  TRP A CB  1 
ATOM   2526 C  CG  . TRP A 1 322  ? 24.770 46.135  22.176  1.00 10.79 ? 322  TRP A CG  1 
ATOM   2527 C  CD1 . TRP A 1 322  ? 24.957 47.417  21.707  1.00 11.67 ? 322  TRP A CD1 1 
ATOM   2528 C  CD2 . TRP A 1 322  ? 25.660 45.976  23.282  1.00 11.23 ? 322  TRP A CD2 1 
ATOM   2529 N  NE1 . TRP A 1 322  ? 25.910 48.058  22.476  1.00 12.07 ? 322  TRP A NE1 1 
ATOM   2530 C  CE2 . TRP A 1 322  ? 26.389 47.190  23.426  1.00 10.94 ? 322  TRP A CE2 1 
ATOM   2531 C  CE3 . TRP A 1 322  ? 25.963 44.901  24.140  1.00 12.57 ? 322  TRP A CE3 1 
ATOM   2532 C  CZ2 . TRP A 1 322  ? 27.345 47.382  24.440  1.00 12.60 ? 322  TRP A CZ2 1 
ATOM   2533 C  CZ3 . TRP A 1 322  ? 26.935 45.085  25.141  1.00 12.21 ? 322  TRP A CZ3 1 
ATOM   2534 C  CH2 . TRP A 1 322  ? 27.606 46.310  25.277  1.00 13.45 ? 322  TRP A CH2 1 
ATOM   2535 N  N   . LYS A 1 323  ? 21.277 43.672  20.609  1.00 11.55 ? 323  LYS A N   1 
ATOM   2536 C  CA  . LYS A 1 323  ? 20.683 42.469  20.007  1.00 12.45 ? 323  LYS A CA  1 
ATOM   2537 C  C   . LYS A 1 323  ? 19.810 42.827  18.828  1.00 12.14 ? 323  LYS A C   1 
ATOM   2538 O  O   . LYS A 1 323  ? 19.717 42.071  17.872  1.00 12.38 ? 323  LYS A O   1 
ATOM   2539 C  CB  . LYS A 1 323  ? 19.922 41.635  21.068  1.00 13.20 ? 323  LYS A CB  1 
ATOM   2540 C  CG  . LYS A 1 323  ? 20.879 40.871  21.964  1.00 14.11 ? 323  LYS A CG  1 
ATOM   2541 C  CD  . LYS A 1 323  ? 20.163 40.084  23.051  1.00 14.06 ? 323  LYS A CD  1 
ATOM   2542 C  CE  . LYS A 1 323  ? 21.170 39.237  23.746  1.00 15.71 ? 323  LYS A CE  1 
ATOM   2543 N  NZ  . LYS A 1 323  ? 20.485 38.531  24.873  1.00 19.90 ? 323  LYS A NZ  1 
ATOM   2544 N  N   . LYS A 1 324  ? 19.188 43.987  18.856  1.00 10.93 ? 324  LYS A N   1 
ATOM   2545 C  CA  . LYS A 1 324  ? 18.472 44.473  17.666  1.00 11.17 ? 324  LYS A CA  1 
ATOM   2546 C  C   . LYS A 1 324  ? 19.417 44.743  16.492  1.00 11.75 ? 324  LYS A C   1 
ATOM   2547 O  O   . LYS A 1 324  ? 19.171 44.308  15.375  1.00 11.69 ? 324  LYS A O   1 
ATOM   2548 C  CB  . LYS A 1 324  ? 17.666 45.729  17.994  1.00 11.12 ? 324  LYS A CB  1 
ATOM   2549 C  CG  . LYS A 1 324  ? 16.424 45.387  18.815  1.00 11.66 ? 324  LYS A CG  1 
ATOM   2550 C  CD  . LYS A 1 324  ? 15.792 46.613  19.372  1.00 13.11 ? 324  LYS A CD  1 
ATOM   2551 C  CE  . LYS A 1 324  ? 14.512 46.200  20.135  1.00 14.26 ? 324  LYS A CE  1 
ATOM   2552 N  NZ  . LYS A 1 324  ? 13.919 47.337  20.892  1.00 16.40 ? 324  LYS A NZ  1 
ATOM   2553 N  N   . LYS A 1 325  ? 20.495 45.481  16.751  1.00 10.76 ? 325  LYS A N   1 
ATOM   2554 C  CA  . LYS A 1 325  ? 21.494 45.706  15.696  1.00 10.26 ? 325  LYS A CA  1 
ATOM   2555 C  C   . LYS A 1 325  ? 22.011 44.378  15.150  1.00 9.60  ? 325  LYS A C   1 
ATOM   2556 O  O   . LYS A 1 325  ? 22.183 44.213  13.941  1.00 9.70  ? 325  LYS A O   1 
ATOM   2557 C  CB  . LYS A 1 325  ? 22.651 46.540  16.226  1.00 10.18 ? 325  LYS A CB  1 
ATOM   2558 C  CG  . LYS A 1 325  ? 23.549 47.100  15.096  1.00 9.71  ? 325  LYS A CG  1 
ATOM   2559 C  CD  . LYS A 1 325  ? 24.655 47.969  15.678  1.00 11.39 ? 325  LYS A CD  1 
ATOM   2560 C  CE  . LYS A 1 325  ? 25.391 48.705  14.548  1.00 11.47 ? 325  LYS A CE  1 
ATOM   2561 N  NZ  . LYS A 1 325  ? 26.611 49.375  15.139  1.00 12.40 ? 325  LYS A NZ  1 
ATOM   2562 N  N   . ALA A 1 326  ? 22.257 43.405  16.038  1.00 10.02 ? 326  ALA A N   1 
ATOM   2563 C  CA  . ALA A 1 326  ? 22.822 42.108  15.625  1.00 10.73 ? 326  ALA A CA  1 
ATOM   2564 C  C   . ALA A 1 326  ? 21.891 41.347  14.681  1.00 10.83 ? 326  ALA A C   1 
ATOM   2565 O  O   . ALA A 1 326  ? 22.331 40.491  13.912  1.00 11.59 ? 326  ALA A O   1 
ATOM   2566 C  CB  . ALA A 1 326  ? 23.131 41.258  16.834  1.00 10.82 ? 326  ALA A CB  1 
ATOM   2567 N  N   . GLU A 1 327  ? 20.600 41.659  14.751  1.00 11.35 ? 327  GLU A N   1 
ATOM   2568 C  CA  . GLU A 1 327  ? 19.627 41.009  13.850  1.00 13.48 ? 327  GLU A CA  1 
ATOM   2569 C  C   . GLU A 1 327  ? 19.872 41.335  12.386  1.00 12.78 ? 327  GLU A C   1 
ATOM   2570 O  O   . GLU A 1 327  ? 19.405 40.619  11.478  1.00 13.70 ? 327  GLU A O   1 
ATOM   2571 C  CB  . GLU A 1 327  ? 18.204 41.423  14.203  1.00 14.57 ? 327  GLU A CB  1 
ATOM   2572 C  CG  . GLU A 1 327  ? 17.604 40.629  15.332  1.00 18.18 ? 327  GLU A CG  1 
ATOM   2573 C  CD  . GLU A 1 327  ? 17.585 39.118  15.064  1.00 17.98 ? 327  GLU A CD  1 
ATOM   2574 O  OE1 . GLU A 1 327  ? 16.911 38.658  14.124  1.00 23.00 ? 327  GLU A OE1 1 
ATOM   2575 O  OE2 . GLU A 1 327  ? 18.269 38.401  15.781  1.00 21.64 ? 327  GLU A OE2 1 
ATOM   2576 N  N   . LEU A 1 328  ? 20.586 42.438  12.141  1.00 11.75 ? 328  LEU A N   1 
ATOM   2577 C  CA  . LEU A 1 328  ? 20.819 42.920  10.777  1.00 11.06 ? 328  LEU A CA  1 
ATOM   2578 C  C   . LEU A 1 328  ? 22.010 42.248  10.114  1.00 11.11 ? 328  LEU A C   1 
ATOM   2579 O  O   . LEU A 1 328  ? 22.290 42.515  8.947   1.00 11.48 ? 328  LEU A O   1 
ATOM   2580 C  CB  . LEU A 1 328  ? 20.997 44.445  10.787  1.00 11.08 ? 328  LEU A CB  1 
ATOM   2581 C  CG  . LEU A 1 328  ? 19.907 45.234  11.487  1.00 10.50 ? 328  LEU A CG  1 
ATOM   2582 C  CD1 . LEU A 1 328  ? 20.149 46.726  11.327  1.00 12.13 ? 328  LEU A CD1 1 
ATOM   2583 C  CD2 . LEU A 1 328  ? 18.501 44.871  10.990  1.00 12.54 ? 328  LEU A CD2 1 
ATOM   2584 N  N   . TYR A 1 329  ? 22.740 41.420  10.853  1.00 10.06 ? 329  TYR A N   1 
ATOM   2585 C  CA  . TYR A 1 329  ? 23.991 40.823  10.393  1.00 9.71  ? 329  TYR A CA  1 
ATOM   2586 C  C   . TYR A 1 329  ? 23.967 39.307  10.601  1.00 11.18 ? 329  TYR A C   1 
ATOM   2587 O  O   . TYR A 1 329  ? 23.118 38.784  11.345  1.00 13.03 ? 329  TYR A O   1 
ATOM   2588 C  CB  . TYR A 1 329  ? 25.191 41.437  11.160  1.00 10.99 ? 329  TYR A CB  1 
ATOM   2589 C  CG  . TYR A 1 329  ? 25.378 42.902  10.808  1.00 10.25 ? 329  TYR A CG  1 
ATOM   2590 C  CD1 . TYR A 1 329  ? 26.119 43.256  9.699   1.00 11.27 ? 329  TYR A CD1 1 
ATOM   2591 C  CD2 . TYR A 1 329  ? 24.803 43.913  11.579  1.00 11.87 ? 329  TYR A CD2 1 
ATOM   2592 C  CE1 . TYR A 1 329  ? 26.274 44.594  9.326   1.00 11.12 ? 329  TYR A CE1 1 
ATOM   2593 C  CE2 . TYR A 1 329  ? 24.953 45.251  11.241  1.00 12.01 ? 329  TYR A CE2 1 
ATOM   2594 C  CZ  . TYR A 1 329  ? 25.679 45.568  10.098  1.00 10.38 ? 329  TYR A CZ  1 
ATOM   2595 O  OH  . TYR A 1 329  ? 25.783 46.917  9.763   1.00 11.39 ? 329  TYR A OH  1 
ATOM   2596 N  N   . ARG A 1 330  ? 24.886 38.599  9.967   1.00 10.76 ? 330  ARG A N   1 
ATOM   2597 C  CA  . ARG A 1 330  ? 24.824 37.137  9.870   1.00 11.85 ? 330  ARG A CA  1 
ATOM   2598 C  C   . ARG A 1 330  ? 25.607 36.381  10.915  1.00 13.05 ? 330  ARG A C   1 
ATOM   2599 O  O   . ARG A 1 330  ? 25.408 35.160  11.049  1.00 14.95 ? 330  ARG A O   1 
ATOM   2600 C  CB  . ARG A 1 330  ? 25.265 36.680  8.478   1.00 12.08 ? 330  ARG A CB  1 
ATOM   2601 C  CG  . ARG A 1 330  ? 24.290 37.093  7.399   1.00 12.07 ? 330  ARG A CG  1 
ATOM   2602 C  CD  . ARG A 1 330  ? 24.633 36.553  6.034   1.00 13.13 ? 330  ARG A CD  1 
ATOM   2603 N  NE  . ARG A 1 330  ? 23.676 37.108  5.095   1.00 14.95 ? 330  ARG A NE  1 
ATOM   2604 C  CZ  . ARG A 1 330  ? 23.347 36.584  3.922   1.00 17.95 ? 330  ARG A CZ  1 
ATOM   2605 N  NH1 . ARG A 1 330  ? 23.923 35.464  3.484   1.00 18.86 ? 330  ARG A NH1 1 
ATOM   2606 N  NH2 . ARG A 1 330  ? 22.439 37.217  3.185   1.00 17.58 ? 330  ARG A NH2 1 
ATOM   2607 N  N   . THR A 1 331  ? 26.531 37.029  11.610  1.00 12.52 ? 331  THR A N   1 
ATOM   2608 C  CA  . THR A 1 331  ? 27.304 36.303  12.630  1.00 11.86 ? 331  THR A CA  1 
ATOM   2609 C  C   . THR A 1 331  ? 26.894 36.699  14.037  1.00 12.52 ? 331  THR A C   1 
ATOM   2610 O  O   . THR A 1 331  ? 26.085 37.587  14.213  1.00 13.51 ? 331  THR A O   1 
ATOM   2611 C  CB  . THR A 1 331  ? 28.821 36.492  12.483  1.00 12.38 ? 331  THR A CB  1 
ATOM   2612 O  OG1 . THR A 1 331  ? 29.223 37.790  12.980  1.00 12.40 ? 331  THR A OG1 1 
ATOM   2613 C  CG2 . THR A 1 331  ? 29.289 36.361  10.998  1.00 13.39 ? 331  THR A CG2 1 
ATOM   2614 N  N   . ASN A 1 332  ? 27.535 36.077  15.030  1.00 12.52 ? 332  ASN A N   1 
ATOM   2615 C  CA  . ASN A 1 332  ? 27.330 36.428  16.439  1.00 12.74 ? 332  ASN A CA  1 
ATOM   2616 C  C   . ASN A 1 332  ? 28.403 37.390  16.950  1.00 11.84 ? 332  ASN A C   1 
ATOM   2617 O  O   . ASN A 1 332  ? 28.673 37.453  18.150  1.00 12.75 ? 332  ASN A O   1 
ATOM   2618 C  CB  . ASN A 1 332  ? 27.281 35.149  17.319  1.00 14.14 ? 332  ASN A CB  1 
ATOM   2619 C  CG  . ASN A 1 332  ? 28.626 34.454  17.446  1.00 17.48 ? 332  ASN A CG  1 
ATOM   2620 O  OD1 . ASN A 1 332  ? 29.437 34.455  16.528  1.00 18.36 ? 332  ASN A OD1 1 
ATOM   2621 N  ND2 . ASN A 1 332  ? 28.868 33.833  18.612  1.00 21.54 ? 332  ASN A ND2 1 
ATOM   2622 N  N   . VAL A 1 333  ? 29.004 38.150  16.022  1.00 11.35 ? 333  VAL A N   1 
ATOM   2623 C  CA  . VAL A 1 333  ? 30.061 39.098  16.364  1.00 11.17 ? 333  VAL A CA  1 
ATOM   2624 C  C   . VAL A 1 333  ? 29.529 40.453  15.938  1.00 10.46 ? 333  VAL A C   1 
ATOM   2625 O  O   . VAL A 1 333  ? 29.184 40.624  14.772  1.00 11.59 ? 333  VAL A O   1 
ATOM   2626 C  CB  . VAL A 1 333  ? 31.361 38.791  15.596  1.00 11.72 ? 333  VAL A CB  1 
ATOM   2627 C  CG1 . VAL A 1 333  ? 32.472 39.787  16.011  1.00 11.68 ? 333  VAL A CG1 1 
ATOM   2628 C  CG2 . VAL A 1 333  ? 31.797 37.343  15.817  1.00 13.61 ? 333  VAL A CG2 1 
ATOM   2629 N  N   . LEU A 1 334  ? 29.440 41.421  16.855  1.00 9.57  ? 334  LEU A N   1 
ATOM   2630 C  CA  . LEU A 1 334  ? 28.805 42.693  16.608  1.00 9.71  ? 334  LEU A CA  1 
ATOM   2631 C  C   . LEU A 1 334  ? 29.800 43.846  16.766  1.00 9.45  ? 334  LEU A C   1 
ATOM   2632 O  O   . LEU A 1 334  ? 30.519 43.945  17.759  1.00 10.06 ? 334  LEU A O   1 
ATOM   2633 C  CB  . LEU A 1 334  ? 27.673 42.895  17.622  1.00 9.63  ? 334  LEU A CB  1 
ATOM   2634 C  CG  . LEU A 1 334  ? 26.820 44.149  17.417  1.00 10.58 ? 334  LEU A CG  1 
ATOM   2635 C  CD1 . LEU A 1 334  ? 26.020 44.075  16.100  1.00 11.90 ? 334  LEU A CD1 1 
ATOM   2636 C  CD2 . LEU A 1 334  ? 25.872 44.344  18.613  1.00 11.04 ? 334  LEU A CD2 1 
ATOM   2637 N  N   . LEU A 1 335  ? 29.780 44.757  15.796  1.00 8.36  ? 335  LEU A N   1 
ATOM   2638 C  CA  . LEU A 1 335  ? 30.620 45.959  15.820  1.00 8.90  ? 335  LEU A CA  1 
ATOM   2639 C  C   . LEU A 1 335  ? 29.831 47.152  16.359  1.00 8.18  ? 335  LEU A C   1 
ATOM   2640 O  O   . LEU A 1 335  ? 28.786 47.507  15.799  1.00 9.31  ? 335  LEU A O   1 
ATOM   2641 C  CB  . LEU A 1 335  ? 31.068 46.296  14.385  1.00 9.52  ? 335  LEU A CB  1 
ATOM   2642 C  CG  . LEU A 1 335  ? 31.946 47.556  14.289  1.00 8.78  ? 335  LEU A CG  1 
ATOM   2643 C  CD1 . LEU A 1 335  ? 33.242 47.442  15.050  1.00 11.17 ? 335  LEU A CD1 1 
ATOM   2644 C  CD2 . LEU A 1 335  ? 32.197 47.861  12.828  1.00 12.52 ? 335  LEU A CD2 1 
ATOM   2645 N  N   . ILE A 1 336  ? 30.329 47.767  17.433  1.00 8.68  ? 336  ILE A N   1 
ATOM   2646 C  CA  . ILE A 1 336  ? 29.738 48.960  18.023  1.00 8.96  ? 336  ILE A CA  1 
ATOM   2647 C  C   . ILE A 1 336  ? 30.796 50.076  18.038  1.00 7.79  ? 336  ILE A C   1 
ATOM   2648 O  O   . ILE A 1 336  ? 31.575 50.204  18.977  1.00 9.13  ? 336  ILE A O   1 
ATOM   2649 C  CB  . ILE A 1 336  ? 29.194 48.685  19.454  1.00 9.91  ? 336  ILE A CB  1 
ATOM   2650 C  CG1 . ILE A 1 336  ? 28.157 47.535  19.446  1.00 9.68  ? 336  ILE A CG1 1 
ATOM   2651 C  CG2 . ILE A 1 336  ? 28.638 49.993  20.044  1.00 9.98  ? 336  ILE A CG2 1 
ATOM   2652 C  CD1 . ILE A 1 336  ? 26.870 47.866  18.722  1.00 10.71 ? 336  ILE A CD1 1 
ATOM   2653 N  N   . PRO A 1 337  ? 30.834 50.906  17.004  1.00 7.83  ? 337  PRO A N   1 
ATOM   2654 C  CA  . PRO A 1 337  ? 31.705 52.096  17.066  1.00 7.94  ? 337  PRO A CA  1 
ATOM   2655 C  C   . PRO A 1 337  ? 31.315 53.012  18.224  1.00 8.71  ? 337  PRO A C   1 
ATOM   2656 O  O   . PRO A 1 337  ? 30.121 53.127  18.508  1.00 9.54  ? 337  PRO A O   1 
ATOM   2657 C  CB  . PRO A 1 337  ? 31.456 52.776  15.705  1.00 8.58  ? 337  PRO A CB  1 
ATOM   2658 C  CG  . PRO A 1 337  ? 30.974 51.626  14.800  1.00 8.72  ? 337  PRO A CG  1 
ATOM   2659 C  CD  . PRO A 1 337  ? 30.078 50.847  15.736  1.00 8.79  ? 337  PRO A CD  1 
ATOM   2660 N  N   . LEU A 1 338  ? 32.295 53.633  18.871  1.00 8.72  ? 338  LEU A N   1 
ATOM   2661 C  CA  . LEU A 1 338  ? 32.046 54.558  19.979  1.00 8.56  ? 338  LEU A CA  1 
ATOM   2662 C  C   . LEU A 1 338  ? 32.852 55.844  19.743  1.00 8.58  ? 338  LEU A C   1 
ATOM   2663 O  O   . LEU A 1 338  ? 34.004 55.947  20.181  1.00 8.99  ? 338  LEU A O   1 
ATOM   2664 C  CB  . LEU A 1 338  ? 32.388 53.891  21.319  1.00 9.86  ? 338  LEU A CB  1 
ATOM   2665 C  CG  . LEU A 1 338  ? 32.009 54.764  22.518  1.00 10.53 ? 338  LEU A CG  1 
ATOM   2666 C  CD1 . LEU A 1 338  ? 30.509 54.644  22.832  1.00 12.78 ? 338  LEU A CD1 1 
ATOM   2667 C  CD2 . LEU A 1 338  ? 32.774 54.293  23.728  1.00 12.49 ? 338  LEU A CD2 1 
ATOM   2668 N  N   . GLY A 1 339  ? 32.237 56.811  19.084  1.00 8.38  ? 339  GLY A N   1 
ATOM   2669 C  CA  . GLY A 1 339  ? 32.968 58.041  18.784  1.00 9.44  ? 339  GLY A CA  1 
ATOM   2670 C  C   . GLY A 1 339  ? 32.150 59.014  17.976  1.00 9.65  ? 339  GLY A C   1 
ATOM   2671 O  O   . GLY A 1 339  ? 30.970 58.776  17.696  1.00 9.95  ? 339  GLY A O   1 
ATOM   2672 N  N   . ASP A 1 340  ? 32.791 60.135  17.599  1.00 8.80  ? 340  ASP A N   1 
ATOM   2673 C  CA  . ASP A 1 340  ? 32.165 61.233  16.892  1.00 9.10  ? 340  ASP A CA  1 
ATOM   2674 C  C   . ASP A 1 340  ? 33.320 62.185  16.525  1.00 8.76  ? 340  ASP A C   1 
ATOM   2675 O  O   . ASP A 1 340  ? 34.489 61.865  16.705  1.00 8.79  ? 340  ASP A O   1 
ATOM   2676 C  CB  . ASP A 1 340  ? 31.128 61.905  17.833  1.00 10.24 ? 340  ASP A CB  1 
ATOM   2677 C  CG  . ASP A 1 340  ? 30.033 62.682  17.133  1.00 11.05 ? 340  ASP A CG  1 
ATOM   2678 O  OD1 . ASP A 1 340  ? 30.188 63.067  15.935  1.00 13.55 ? 340  ASP A OD1 1 
ATOM   2679 O  OD2 . ASP A 1 340  ? 28.980 62.976  17.759  1.00 12.87 ? 340  ASP A OD2 1 
ATOM   2680 N  N   . ASP A 1 341  ? 32.957 63.350  16.017  1.00 9.50  ? 341  ASP A N   1 
ATOM   2681 C  CA  . ASP A 1 341  ? 33.941 64.291  15.469  1.00 9.22  ? 341  ASP A CA  1 
ATOM   2682 C  C   . ASP A 1 341  ? 34.802 64.833  16.595  1.00 9.68  ? 341  ASP A C   1 
ATOM   2683 O  O   . ASP A 1 341  ? 34.292 65.308  17.586  1.00 10.22 ? 341  ASP A O   1 
ATOM   2684 C  CB  . ASP A 1 341  ? 33.240 65.438  14.749  1.00 11.40 ? 341  ASP A CB  1 
ATOM   2685 C  CG  . ASP A 1 341  ? 32.694 65.033  13.403  1.00 12.89 ? 341  ASP A CG  1 
ATOM   2686 O  OD1 . ASP A 1 341  ? 32.759 63.869  13.051  1.00 12.10 ? 341  ASP A OD1 1 
ATOM   2687 O  OD2 . ASP A 1 341  ? 32.241 65.915  12.700  1.00 18.20 ? 341  ASP A OD2 1 
ATOM   2688 N  N   . PHE A 1 342  ? 36.109 64.760  16.405  1.00 8.53  ? 342  PHE A N   1 
ATOM   2689 C  CA  . PHE A 1 342  ? 37.086 65.316  17.348  1.00 9.06  ? 342  PHE A CA  1 
ATOM   2690 C  C   . PHE A 1 342  ? 36.780 64.914  18.805  1.00 9.46  ? 342  PHE A C   1 
ATOM   2691 O  O   . PHE A 1 342  ? 37.028 65.688  19.759  1.00 11.21 ? 342  PHE A O   1 
ATOM   2692 C  CB  . PHE A 1 342  ? 37.235 66.839  17.161  1.00 9.96  ? 342  PHE A CB  1 
ATOM   2693 C  CG  . PHE A 1 342  ? 37.793 67.229  15.824  1.00 9.89  ? 342  PHE A CG  1 
ATOM   2694 C  CD1 . PHE A 1 342  ? 39.169 67.198  15.596  1.00 8.49  ? 342  PHE A CD1 1 
ATOM   2695 C  CD2 . PHE A 1 342  ? 36.948 67.647  14.779  1.00 10.01 ? 342  PHE A CD2 1 
ATOM   2696 C  CE1 . PHE A 1 342  ? 39.690 67.590  14.376  1.00 8.13  ? 342  PHE A CE1 1 
ATOM   2697 C  CE2 . PHE A 1 342  ? 37.498 68.015  13.529  1.00 10.74 ? 342  PHE A CE2 1 
ATOM   2698 C  CZ  . PHE A 1 342  ? 38.862 67.998  13.360  1.00 9.79  ? 342  PHE A CZ  1 
ATOM   2699 N  N   . ARG A 1 343  ? 36.360 63.657  18.975  1.00 8.77  ? 343  ARG A N   1 
ATOM   2700 C  CA  . ARG A 1 343  ? 36.161 63.115  20.321  1.00 8.79  ? 343  ARG A CA  1 
ATOM   2701 C  C   . ARG A 1 343  ? 37.464 62.678  20.968  1.00 10.09 ? 343  ARG A C   1 
ATOM   2702 O  O   . ARG A 1 343  ? 38.532 62.612  20.355  1.00 9.38  ? 343  ARG A O   1 
ATOM   2703 C  CB  . ARG A 1 343  ? 35.145 61.968  20.305  1.00 9.29  ? 343  ARG A CB  1 
ATOM   2704 C  CG  . ARG A 1 343  ? 33.723 62.435  20.072  1.00 10.76 ? 343  ARG A CG  1 
ATOM   2705 C  CD  . ARG A 1 343  ? 33.240 63.383  21.159  1.00 11.08 ? 343  ARG A CD  1 
ATOM   2706 N  NE  . ARG A 1 343  ? 31.805 63.646  21.093  1.00 10.85 ? 343  ARG A NE  1 
ATOM   2707 C  CZ  . ARG A 1 343  ? 30.876 62.930  21.733  1.00 10.27 ? 343  ARG A CZ  1 
ATOM   2708 N  NH1 . ARG A 1 343  ? 31.243 61.896  22.472  1.00 10.41 ? 343  ARG A NH1 1 
ATOM   2709 N  NH2 . ARG A 1 343  ? 29.607 63.294  21.654  1.00 11.02 ? 343  ARG A NH2 1 
ATOM   2710 N  N   . PHE A 1 344  ? 37.332 62.363  22.253  1.00 10.30 ? 344  PHE A N   1 
ATOM   2711 C  CA  . PHE A 1 344  ? 38.452 61.888  23.071  1.00 10.67 ? 344  PHE A CA  1 
ATOM   2712 C  C   . PHE A 1 344  ? 39.550 62.925  23.215  1.00 11.68 ? 344  PHE A C   1 
ATOM   2713 O  O   . PHE A 1 344  ? 40.737 62.616  23.155  1.00 13.03 ? 344  PHE A O   1 
ATOM   2714 C  CB  . PHE A 1 344  ? 38.900 60.513  22.568  1.00 11.27 ? 344  PHE A CB  1 
ATOM   2715 C  CG  . PHE A 1 344  ? 37.863 59.470  22.781  1.00 10.91 ? 344  PHE A CG  1 
ATOM   2716 C  CD1 . PHE A 1 344  ? 37.657 58.943  24.068  1.00 12.87 ? 344  PHE A CD1 1 
ATOM   2717 C  CD2 . PHE A 1 344  ? 37.040 59.046  21.737  1.00 11.43 ? 344  PHE A CD2 1 
ATOM   2718 C  CE1 . PHE A 1 344  ? 36.669 57.976  24.275  1.00 13.05 ? 344  PHE A CE1 1 
ATOM   2719 C  CE2 . PHE A 1 344  ? 36.040 58.092  21.941  1.00 11.58 ? 344  PHE A CE2 1 
ATOM   2720 C  CZ  . PHE A 1 344  ? 35.879 57.553  23.229  1.00 12.12 ? 344  PHE A CZ  1 
ATOM   2721 N  N   . LYS A 1 345  ? 39.127 64.170  23.426  1.00 12.53 ? 345  LYS A N   1 
ATOM   2722 C  CA  . LYS A 1 345  ? 40.045 65.287  23.620  1.00 14.77 ? 345  LYS A CA  1 
ATOM   2723 C  C   . LYS A 1 345  ? 40.393 65.355  25.121  1.00 16.27 ? 345  LYS A C   1 
ATOM   2724 O  O   . LYS A 1 345  ? 41.474 64.942  25.532  1.00 19.63 ? 345  LYS A O   1 
ATOM   2725 C  CB  . LYS A 1 345  ? 39.367 66.562  23.099  1.00 15.35 ? 345  LYS A CB  1 
ATOM   2726 C  CG  . LYS A 1 345  ? 40.204 67.806  23.116  1.00 17.40 ? 345  LYS A CG  1 
ATOM   2727 C  CD  . LYS A 1 345  ? 39.436 68.957  22.508  1.00 21.04 ? 345  LYS A CD  1 
ATOM   2728 C  CE  . LYS A 1 345  ? 40.139 70.268  22.750  1.00 23.12 ? 345  LYS A CE  1 
ATOM   2729 N  NZ  . LYS A 1 345  ? 39.331 71.367  22.135  1.00 24.83 ? 345  LYS A NZ  1 
ATOM   2730 N  N   . GLN A 1 346  ? 39.429 65.745  25.932  1.00 15.93 ? 346  GLN A N   1 
ATOM   2731 C  CA  . GLN A 1 346  ? 39.661 66.022  27.348  1.00 17.01 ? 346  GLN A CA  1 
ATOM   2732 C  C   . GLN A 1 346  ? 39.968 64.732  28.138  1.00 16.21 ? 346  GLN A C   1 
ATOM   2733 O  O   . GLN A 1 346  ? 39.346 63.679  27.909  1.00 14.25 ? 346  GLN A O   1 
ATOM   2734 C  CB  . GLN A 1 346  ? 38.426 66.722  27.945  1.00 17.40 ? 346  GLN A CB  1 
ATOM   2735 C  CG  . GLN A 1 346  ? 37.999 68.074  27.300  1.00 21.96 ? 346  GLN A CG  1 
ATOM   2736 C  CD  . GLN A 1 346  ? 36.797 67.953  26.338  1.00 25.50 ? 346  GLN A CD  1 
ATOM   2737 O  OE1 . GLN A 1 346  ? 36.686 66.986  25.572  1.00 22.26 ? 346  GLN A OE1 1 
ATOM   2738 N  NE2 . GLN A 1 346  ? 35.898 68.939  26.382  1.00 27.79 ? 346  GLN A NE2 1 
ATOM   2739 N  N   . ASN A 1 347  ? 40.883 64.808  29.104  1.00 16.31 ? 347  ASN A N   1 
ATOM   2740 C  CA  . ASN A 1 347  ? 41.079 63.690  30.044  1.00 16.21 ? 347  ASN A CA  1 
ATOM   2741 C  C   . ASN A 1 347  ? 39.806 63.263  30.743  1.00 14.87 ? 347  ASN A C   1 
ATOM   2742 O  O   . ASN A 1 347  ? 39.533 62.062  30.826  1.00 15.21 ? 347  ASN A O   1 
ATOM   2743 C  CB  . ASN A 1 347  ? 42.121 64.051  31.108  1.00 17.08 ? 347  ASN A CB  1 
ATOM   2744 C  CG  . ASN A 1 347  ? 43.442 64.338  30.501  1.00 21.46 ? 347  ASN A CG  1 
ATOM   2745 O  OD1 . ASN A 1 347  ? 43.951 65.476  30.561  1.00 28.59 ? 347  ASN A OD1 1 
ATOM   2746 N  ND2 . ASN A 1 347  ? 44.009 63.339  29.873  1.00 23.24 ? 347  ASN A ND2 1 
ATOM   2747 N  N   . THR A 1 348  ? 38.980 64.236  31.122  1.00 14.56 ? 348  THR A N   1 
ATOM   2748 C  CA  . THR A 1 348  ? 37.704 63.933  31.766  1.00 15.39 ? 348  THR A CA  1 
ATOM   2749 C  C   . THR A 1 348  ? 36.787 63.156  30.833  1.00 15.11 ? 348  THR A C   1 
ATOM   2750 O  O   . THR A 1 348  ? 35.975 62.343  31.292  1.00 14.70 ? 348  THR A O   1 
ATOM   2751 C  CB  . THR A 1 348  ? 36.983 65.213  32.258  1.00 15.67 ? 348  THR A CB  1 
ATOM   2752 O  OG1 . THR A 1 348  ? 36.854 66.165  31.186  1.00 19.00 ? 348  THR A OG1 1 
ATOM   2753 C  CG2 . THR A 1 348  ? 37.792 65.938  33.350  1.00 16.87 ? 348  THR A CG2 1 
ATOM   2754 N  N   . GLU A 1 349  ? 36.904 63.383  29.519  1.00 12.88 ? 349  GLU A N   1 
ATOM   2755 C  CA  . GLU A 1 349  ? 36.087 62.655  28.555  1.00 12.68 ? 349  GLU A CA  1 
ATOM   2756 C  C   . GLU A 1 349  ? 36.541 61.196  28.389  1.00 11.45 ? 349  GLU A C   1 
ATOM   2757 O  O   . GLU A 1 349  ? 35.734 60.279  28.367  1.00 11.70 ? 349  GLU A O   1 
ATOM   2758 C  CB  . GLU A 1 349  ? 36.145 63.379  27.202  1.00 12.19 ? 349  GLU A CB  1 
ATOM   2759 C  CG  . GLU A 1 349  ? 35.418 62.628  26.118  1.00 12.20 ? 349  GLU A CG  1 
ATOM   2760 C  CD  . GLU A 1 349  ? 35.640 63.205  24.714  1.00 11.73 ? 349  GLU A CD  1 
ATOM   2761 O  OE1 . GLU A 1 349  ? 36.339 64.216  24.553  1.00 13.97 ? 349  GLU A OE1 1 
ATOM   2762 O  OE2 . GLU A 1 349  ? 35.115 62.595  23.795  1.00 13.40 ? 349  GLU A OE2 1 
ATOM   2763 N  N   . TRP A 1 350  ? 37.850 60.988  28.326  1.00 10.99 ? 350  TRP A N   1 
ATOM   2764 C  CA  . TRP A 1 350  ? 38.381 59.631  28.344  1.00 11.13 ? 350  TRP A CA  1 
ATOM   2765 C  C   . TRP A 1 350  ? 37.828 58.871  29.559  1.00 11.89 ? 350  TRP A C   1 
ATOM   2766 O  O   . TRP A 1 350  ? 37.349 57.747  29.441  1.00 12.67 ? 350  TRP A O   1 
ATOM   2767 C  CB  . TRP A 1 350  ? 39.908 59.611  28.374  1.00 11.15 ? 350  TRP A CB  1 
ATOM   2768 C  CG  . TRP A 1 350  ? 40.516 59.820  27.014  1.00 11.42 ? 350  TRP A CG  1 
ATOM   2769 C  CD1 . TRP A 1 350  ? 40.844 61.007  26.437  1.00 11.84 ? 350  TRP A CD1 1 
ATOM   2770 C  CD2 . TRP A 1 350  ? 40.829 58.798  26.060  1.00 11.59 ? 350  TRP A CD2 1 
ATOM   2771 N  NE1 . TRP A 1 350  ? 41.387 60.789  25.184  1.00 10.76 ? 350  TRP A NE1 1 
ATOM   2772 C  CE2 . TRP A 1 350  ? 41.354 59.447  24.915  1.00 11.04 ? 350  TRP A CE2 1 
ATOM   2773 C  CE3 . TRP A 1 350  ? 40.716 57.402  26.045  1.00 13.59 ? 350  TRP A CE3 1 
ATOM   2774 C  CZ2 . TRP A 1 350  ? 41.756 58.749  23.783  1.00 13.10 ? 350  TRP A CZ2 1 
ATOM   2775 C  CZ3 . TRP A 1 350  ? 41.140 56.714  24.906  1.00 14.18 ? 350  TRP A CZ3 1 
ATOM   2776 C  CH2 . TRP A 1 350  ? 41.636 57.397  23.802  1.00 12.85 ? 350  TRP A CH2 1 
ATOM   2777 N  N   . ASP A 1 351  ? 37.889 59.507  30.734  1.00 13.38 ? 351  ASP A N   1 
ATOM   2778 C  CA  . ASP A 1 351  ? 37.455 58.870  31.987  1.00 14.28 ? 351  ASP A CA  1 
ATOM   2779 C  C   . ASP A 1 351  ? 35.984 58.555  31.968  1.00 13.35 ? 351  ASP A C   1 
ATOM   2780 O  O   . ASP A 1 351  ? 35.587 57.424  32.326  1.00 13.70 ? 351  ASP A O   1 
ATOM   2781 C  CB  . ASP A 1 351  ? 37.725 59.791  33.179  1.00 16.00 ? 351  ASP A CB  1 
ATOM   2782 C  CG  . ASP A 1 351  ? 39.176 59.889  33.539  1.00 20.12 ? 351  ASP A CG  1 
ATOM   2783 O  OD1 . ASP A 1 351  ? 39.961 58.967  33.222  1.00 23.60 ? 351  ASP A OD1 1 
ATOM   2784 O  OD2 . ASP A 1 351  ? 39.618 60.857  34.210  1.00 26.36 ? 351  ASP A OD2 1 
ATOM   2785 N  N   . VAL A 1 352  ? 35.174 59.515  31.542  1.00 13.13 ? 352  VAL A N   1 
ATOM   2786 C  CA  . VAL A 1 352  ? 33.734 59.360  31.625  1.00 13.66 ? 352  VAL A CA  1 
ATOM   2787 C  C   . VAL A 1 352  ? 33.257 58.235  30.684  1.00 13.49 ? 352  VAL A C   1 
ATOM   2788 O  O   . VAL A 1 352  ? 32.383 57.431  31.044  1.00 15.04 ? 352  VAL A O   1 
ATOM   2789 C  CB  . VAL A 1 352  ? 32.995 60.715  31.444  1.00 15.28 ? 352  VAL A CB  1 
ATOM   2790 C  CG1 . VAL A 1 352  ? 32.795 61.086  29.986  1.00 15.61 ? 352  VAL A CG1 1 
ATOM   2791 C  CG2 . VAL A 1 352  ? 31.690 60.728  32.206  1.00 17.34 ? 352  VAL A CG2 1 
ATOM   2792 N  N   . GLN A 1 353  ? 33.837 58.136  29.481  1.00 12.25 ? 353  GLN A N   1 
ATOM   2793 C  CA  . GLN A 1 353  ? 33.443 57.063  28.575  1.00 11.45 ? 353  GLN A CA  1 
ATOM   2794 C  C   . GLN A 1 353  ? 33.977 55.723  29.071  1.00 11.56 ? 353  GLN A C   1 
ATOM   2795 O  O   . GLN A 1 353  ? 33.216 54.754  29.206  1.00 12.50 ? 353  GLN A O   1 
ATOM   2796 C  CB  . GLN A 1 353  ? 33.936 57.345  27.141  1.00 11.36 ? 353  GLN A CB  1 
ATOM   2797 C  CG  . GLN A 1 353  ? 33.400 58.637  26.498  1.00 11.85 ? 353  GLN A CG  1 
ATOM   2798 C  CD  . GLN A 1 353  ? 31.954 58.551  26.027  1.00 10.80 ? 353  GLN A CD  1 
ATOM   2799 O  OE1 . GLN A 1 353  ? 31.121 57.812  26.601  1.00 12.60 ? 353  GLN A OE1 1 
ATOM   2800 N  NE2 . GLN A 1 353  ? 31.610 59.330  25.020  1.00 11.38 ? 353  GLN A NE2 1 
ATOM   2801 N  N   . ARG A 1 354  ? 35.266 55.659  29.400  1.00 11.12 ? 354  ARG A N   1 
ATOM   2802 C  CA  . ARG A 1 354  ? 35.878 54.405  29.822  1.00 11.71 ? 354  ARG A CA  1 
ATOM   2803 C  C   . ARG A 1 354  ? 35.234 53.816  31.094  1.00 13.07 ? 354  ARG A C   1 
ATOM   2804 O  O   . ARG A 1 354  ? 34.901 52.636  31.131  1.00 13.15 ? 354  ARG A O   1 
ATOM   2805 C  CB  . ARG A 1 354  ? 37.379 54.544  30.023  1.00 11.44 ? 354  ARG A CB  1 
ATOM   2806 C  CG  . ARG A 1 354  ? 38.045 53.266  30.450  1.00 11.82 ? 354  ARG A CG  1 
ATOM   2807 C  CD  . ARG A 1 354  ? 39.536 53.420  30.768  1.00 13.97 ? 354  ARG A CD  1 
ATOM   2808 N  NE  . ARG A 1 354  ? 39.763 54.493  31.744  1.00 16.06 ? 354  ARG A NE  1 
ATOM   2809 C  CZ  . ARG A 1 354  ? 39.646 54.371  33.060  1.00 17.93 ? 354  ARG A CZ  1 
ATOM   2810 N  NH1 . ARG A 1 354  ? 39.286 53.207  33.600  1.00 17.76 ? 354  ARG A NH1 1 
ATOM   2811 N  NH2 . ARG A 1 354  ? 39.911 55.413  33.830  1.00 20.54 ? 354  ARG A NH2 1 
ATOM   2812 N  N   . VAL A 1 355  ? 35.077 54.633  32.127  1.00 12.91 ? 355  VAL A N   1 
ATOM   2813 C  CA  . VAL A 1 355  ? 34.665 54.070  33.422  1.00 14.31 ? 355  VAL A CA  1 
ATOM   2814 C  C   . VAL A 1 355  ? 33.223 53.580  33.329  1.00 13.50 ? 355  VAL A C   1 
ATOM   2815 O  O   . VAL A 1 355  ? 32.887 52.485  33.864  1.00 15.25 ? 355  VAL A O   1 
ATOM   2816 C  CB  . VAL A 1 355  ? 34.824 55.091  34.568  1.00 15.01 ? 355  VAL A CB  1 
ATOM   2817 C  CG1 . VAL A 1 355  ? 34.343 54.516  35.879  1.00 19.57 ? 355  VAL A CG1 1 
ATOM   2818 C  CG2 . VAL A 1 355  ? 36.282 55.486  34.765  1.00 17.76 ? 355  VAL A CG2 1 
ATOM   2819 N  N   . ASN A 1 356  ? 32.358 54.354  32.686  1.00 13.09 ? 356  ASN A N   1 
ATOM   2820 C  CA  . ASN A 1 356  ? 30.969 53.942  32.499  1.00 12.59 ? 356  ASN A CA  1 
ATOM   2821 C  C   . ASN A 1 356  ? 30.830 52.640  31.680  1.00 13.37 ? 356  ASN A C   1 
ATOM   2822 O  O   . ASN A 1 356  ? 30.081 51.721  32.077  1.00 13.44 ? 356  ASN A O   1 
ATOM   2823 C  CB  . ASN A 1 356  ? 30.120 55.097  32.026  1.00 13.28 ? 356  ASN A CB  1 
ATOM   2824 C  CG  . ASN A 1 356  ? 29.871 56.095  33.129  1.00 14.06 ? 356  ASN A CG  1 
ATOM   2825 O  OD1 . ASN A 1 356  ? 29.152 55.775  34.093  1.00 15.43 ? 356  ASN A OD1 1 
ATOM   2826 N  ND2 . ASN A 1 356  ? 30.479 57.275  33.058  1.00 13.26 ? 356  ASN A ND2 1 
ATOM   2827 N  N   . TYR A 1 357  ? 31.566 52.525  30.572  1.00 12.32 ? 357  TYR A N   1 
ATOM   2828 C  CA  . TYR A 1 357  ? 31.545 51.292  29.795  1.00 12.19 ? 357  TYR A CA  1 
ATOM   2829 C  C   . TYR A 1 357  ? 32.150 50.138  30.560  1.00 12.07 ? 357  TYR A C   1 
ATOM   2830 O  O   . TYR A 1 357  ? 31.612 49.023  30.493  1.00 12.57 ? 357  TYR A O   1 
ATOM   2831 C  CB  . TYR A 1 357  ? 32.185 51.482  28.377  1.00 11.87 ? 357  TYR A CB  1 
ATOM   2832 C  CG  . TYR A 1 357  ? 31.178 51.998  27.402  1.00 10.74 ? 357  TYR A CG  1 
ATOM   2833 C  CD1 . TYR A 1 357  ? 30.310 51.118  26.722  1.00 11.40 ? 357  TYR A CD1 1 
ATOM   2834 C  CD2 . TYR A 1 357  ? 31.013 53.365  27.229  1.00 11.14 ? 357  TYR A CD2 1 
ATOM   2835 C  CE1 . TYR A 1 357  ? 29.330 51.602  25.856  1.00 11.15 ? 357  TYR A CE1 1 
ATOM   2836 C  CE2 . TYR A 1 357  ? 30.024 53.875  26.381  1.00 11.01 ? 357  TYR A CE2 1 
ATOM   2837 C  CZ  . TYR A 1 357  ? 29.187 52.987  25.678  1.00 11.71 ? 357  TYR A CZ  1 
ATOM   2838 O  OH  . TYR A 1 357  ? 28.196 53.429  24.826  1.00 12.62 ? 357  TYR A OH  1 
ATOM   2839 N  N   . GLU A 1 358  ? 33.248 50.357  31.280  1.00 12.47 ? 358  GLU A N   1 
ATOM   2840 C  CA  . GLU A 1 358  ? 33.779 49.262  32.111  1.00 13.39 ? 358  GLU A CA  1 
ATOM   2841 C  C   . GLU A 1 358  ? 32.726 48.714  33.108  1.00 13.35 ? 358  GLU A C   1 
ATOM   2842 O  O   . GLU A 1 358  ? 32.619 47.498  33.283  1.00 12.86 ? 358  GLU A O   1 
ATOM   2843 C  CB  . GLU A 1 358  ? 35.006 49.703  32.895  1.00 13.56 ? 358  GLU A CB  1 
ATOM   2844 C  CG  . GLU A 1 358  ? 36.294 49.848  32.082  1.00 16.03 ? 358  GLU A CG  1 
ATOM   2845 C  CD  . GLU A 1 358  ? 37.469 50.343  32.929  1.00 17.05 ? 358  GLU A CD  1 
ATOM   2846 O  OE1 . GLU A 1 358  ? 37.316 50.423  34.172  1.00 25.13 ? 358  GLU A OE1 1 
ATOM   2847 O  OE2 . GLU A 1 358  ? 38.555 50.631  32.397  1.00 19.86 ? 358  GLU A OE2 1 
ATOM   2848 N  N   . ARG A 1 359  ? 31.924 49.585  33.703  1.00 13.32 ? 359  ARG A N   1 
ATOM   2849 C  CA  . ARG A 1 359  ? 30.906 49.107  34.652  1.00 14.54 ? 359  ARG A CA  1 
ATOM   2850 C  C   . ARG A 1 359  ? 29.835 48.310  33.917  1.00 14.87 ? 359  ARG A C   1 
ATOM   2851 O  O   . ARG A 1 359  ? 29.368 47.253  34.391  1.00 14.85 ? 359  ARG A O   1 
ATOM   2852 C  CB  . ARG A 1 359  ? 30.264 50.263  35.391  1.00 15.58 ? 359  ARG A CB  1 
ATOM   2853 C  CG  . ARG A 1 359  ? 31.135 50.949  36.410  1.00 17.41 ? 359  ARG A CG  1 
ATOM   2854 C  CD  . ARG A 1 359  ? 30.454 52.201  36.868  1.00 22.47 ? 359  ARG A CD  1 
ATOM   2855 N  NE  . ARG A 1 359  ? 31.337 53.055  37.644  1.00 26.26 ? 359  ARG A NE  1 
ATOM   2856 C  CZ  . ARG A 1 359  ? 31.379 54.382  37.535  1.00 28.25 ? 359  ARG A CZ  1 
ATOM   2857 N  NH1 . ARG A 1 359  ? 30.586 55.035  36.666  1.00 24.36 ? 359  ARG A NH1 1 
ATOM   2858 N  NH2 . ARG A 1 359  ? 32.226 55.057  38.306  1.00 32.25 ? 359  ARG A NH2 1 
ATOM   2859 N  N   . LEU A 1 360  ? 29.432 48.790  32.742  1.00 13.78 ? 360  LEU A N   1 
ATOM   2860 C  CA  . LEU A 1 360  ? 28.521 48.015  31.915  1.00 13.53 ? 360  LEU A CA  1 
ATOM   2861 C  C   . LEU A 1 360  ? 29.076 46.654  31.532  1.00 13.47 ? 360  LEU A C   1 
ATOM   2862 O  O   . LEU A 1 360  ? 28.369 45.628  31.680  1.00 14.13 ? 360  LEU A O   1 
ATOM   2863 C  CB  . LEU A 1 360  ? 28.114 48.823  30.685  1.00 13.39 ? 360  LEU A CB  1 
ATOM   2864 C  CG  . LEU A 1 360  ? 27.231 50.012  31.030  1.00 13.54 ? 360  LEU A CG  1 
ATOM   2865 C  CD1 . LEU A 1 360  ? 27.386 51.059  29.948  1.00 15.31 ? 360  LEU A CD1 1 
ATOM   2866 C  CD2 . LEU A 1 360  ? 25.744 49.666  31.221  1.00 16.06 ? 360  LEU A CD2 1 
ATOM   2867 N  N   . PHE A 1 361  ? 30.308 46.580  31.053  1.00 12.56 ? 361  PHE A N   1 
ATOM   2868 C  CA  . PHE A 1 361  ? 30.868 45.308  30.658  1.00 13.42 ? 361  PHE A CA  1 
ATOM   2869 C  C   . PHE A 1 361  ? 30.937 44.327  31.828  1.00 14.70 ? 361  PHE A C   1 
ATOM   2870 O  O   . PHE A 1 361  ? 30.676 43.128  31.657  1.00 13.83 ? 361  PHE A O   1 
ATOM   2871 C  CB  . PHE A 1 361  ? 32.286 45.470  30.111  1.00 13.13 ? 361  PHE A CB  1 
ATOM   2872 C  CG  . PHE A 1 361  ? 32.392 46.307  28.850  1.00 11.94 ? 361  PHE A CG  1 
ATOM   2873 C  CD1 . PHE A 1 361  ? 31.327 46.443  27.973  1.00 11.80 ? 361  PHE A CD1 1 
ATOM   2874 C  CD2 . PHE A 1 361  ? 33.599 46.946  28.558  1.00 11.53 ? 361  PHE A CD2 1 
ATOM   2875 C  CE1 . PHE A 1 361  ? 31.466 47.223  26.785  1.00 12.26 ? 361  PHE A CE1 1 
ATOM   2876 C  CE2 . PHE A 1 361  ? 33.750 47.725  27.371  1.00 11.88 ? 361  PHE A CE2 1 
ATOM   2877 C  CZ  . PHE A 1 361  ? 32.688 47.867  26.511  1.00 12.29 ? 361  PHE A CZ  1 
ATOM   2878 N  N   . GLU A 1 362  ? 31.371 44.805  32.994  1.00 14.15 ? 362  GLU A N   1 
ATOM   2879 C  CA  . GLU A 1 362  ? 31.504 43.902  34.142  1.00 14.47 ? 362  GLU A CA  1 
ATOM   2880 C  C   . GLU A 1 362  ? 30.121 43.289  34.473  1.00 14.39 ? 362  GLU A C   1 
ATOM   2881 O  O   . GLU A 1 362  ? 30.005 42.064  34.655  1.00 15.44 ? 362  GLU A O   1 
ATOM   2882 C  CB  . GLU A 1 362  ? 32.131 44.600  35.350  1.00 16.34 ? 362  GLU A CB  1 
ATOM   2883 C  CG  . GLU A 1 362  ? 32.291 43.575  36.479  1.00 18.73 ? 362  GLU A CG  1 
ATOM   2884 C  CD  . GLU A 1 362  ? 32.747 44.158  37.809  1.00 25.50 ? 362  GLU A CD  1 
ATOM   2885 O  OE1 . GLU A 1 362  ? 33.226 45.313  37.835  1.00 28.88 ? 362  GLU A OE1 1 
ATOM   2886 O  OE2 . GLU A 1 362  ? 32.624 43.436  38.832  1.00 26.82 ? 362  GLU A OE2 1 
ATOM   2887 N  N   . HIS A 1 363  ? 29.089 44.109  34.490  1.00 14.04 ? 363  HIS A N   1 
ATOM   2888 C  CA  . HIS A 1 363  ? 27.752 43.593  34.755  1.00 15.65 ? 363  HIS A CA  1 
ATOM   2889 C  C   . HIS A 1 363  ? 27.262 42.641  33.670  1.00 15.39 ? 363  HIS A C   1 
ATOM   2890 O  O   . HIS A 1 363  ? 26.845 41.523  33.948  1.00 16.30 ? 363  HIS A O   1 
ATOM   2891 C  CB  . HIS A 1 363  ? 26.766 44.718  34.976  1.00 15.97 ? 363  HIS A CB  1 
ATOM   2892 C  CG  . HIS A 1 363  ? 25.372 44.238  35.276  1.00 17.19 ? 363  HIS A CG  1 
ATOM   2893 N  ND1 . HIS A 1 363  ? 25.002 43.742  36.517  1.00 22.83 ? 363  HIS A ND1 1 
ATOM   2894 C  CD2 . HIS A 1 363  ? 24.266 44.178  34.500  1.00 19.33 ? 363  HIS A CD2 1 
ATOM   2895 C  CE1 . HIS A 1 363  ? 23.729 43.381  36.471  1.00 21.07 ? 363  HIS A CE1 1 
ATOM   2896 N  NE2 . HIS A 1 363  ? 23.255 43.644  35.266  1.00 23.21 ? 363  HIS A NE2 1 
ATOM   2897 N  N   . ILE A 1 364  ? 27.308 43.090  32.418  1.00 15.12 ? 364  ILE A N   1 
ATOM   2898 C  CA  . ILE A 1 364  ? 26.749 42.320  31.324  1.00 14.30 ? 364  ILE A CA  1 
ATOM   2899 C  C   . ILE A 1 364  ? 27.457 40.992  31.215  1.00 14.43 ? 364  ILE A C   1 
ATOM   2900 O  O   . ILE A 1 364  ? 26.800 39.934  31.041  1.00 14.96 ? 364  ILE A O   1 
ATOM   2901 C  CB  . ILE A 1 364  ? 26.855 43.134  29.987  1.00 14.54 ? 364  ILE A CB  1 
ATOM   2902 C  CG1 . ILE A 1 364  ? 25.871 44.296  30.048  1.00 14.95 ? 364  ILE A CG1 1 
ATOM   2903 C  CG2 . ILE A 1 364  ? 26.637 42.205  28.788  1.00 13.95 ? 364  ILE A CG2 1 
ATOM   2904 C  CD1 . ILE A 1 364  ? 26.133 45.409  29.032  1.00 14.62 ? 364  ILE A CD1 1 
ATOM   2905 N  N   . ASN A 1 365  ? 28.768 40.997  31.311  1.00 14.02 ? 365  ASN A N   1 
ATOM   2906 C  CA  . ASN A 1 365  ? 29.551 39.793  31.054  1.00 14.80 ? 365  ASN A CA  1 
ATOM   2907 C  C   . ASN A 1 365  ? 29.389 38.754  32.169  1.00 16.83 ? 365  ASN A C   1 
ATOM   2908 O  O   . ASN A 1 365  ? 29.685 37.582  31.973  1.00 16.52 ? 365  ASN A O   1 
ATOM   2909 C  CB  . ASN A 1 365  ? 31.028 40.116  30.850  1.00 14.19 ? 365  ASN A CB  1 
ATOM   2910 C  CG  . ASN A 1 365  ? 31.277 40.931  29.580  1.00 13.27 ? 365  ASN A CG  1 
ATOM   2911 O  OD1 . ASN A 1 365  ? 30.358 41.095  28.760  1.00 13.70 ? 365  ASN A OD1 1 
ATOM   2912 N  ND2 . ASN A 1 365  ? 32.518 41.426  29.423  1.00 12.67 ? 365  ASN A ND2 1 
ATOM   2913 N  N   . SER A 1 366  ? 28.933 39.223  33.332  1.00 18.56 ? 366  SER A N   1 
ATOM   2914 C  CA  . SER A 1 366  ? 28.785 38.374  34.535  1.00 21.58 ? 366  SER A CA  1 
ATOM   2915 C  C   . SER A 1 366  ? 27.376 37.827  34.671  1.00 22.62 ? 366  SER A C   1 
ATOM   2916 O  O   . SER A 1 366  ? 27.137 36.938  35.504  1.00 23.52 ? 366  SER A O   1 
ATOM   2917 C  CB  . SER A 1 366  ? 29.152 39.166  35.801  1.00 21.91 ? 366  SER A CB  1 
ATOM   2918 O  OG  . SER A 1 366  ? 28.107 40.070  36.096  1.00 25.08 ? 366  SER A OG  1 
ATOM   2919 N  N   . GLN A 1 367  ? 26.435 38.372  33.911  1.00 22.92 ? 367  GLN A N   1 
ATOM   2920 C  CA  . GLN A 1 367  ? 25.034 37.986  33.979  1.00 24.33 ? 367  GLN A CA  1 
ATOM   2921 C  C   . GLN A 1 367  ? 24.719 37.029  32.848  1.00 24.15 ? 367  GLN A C   1 
ATOM   2922 O  O   . GLN A 1 367  ? 24.388 37.447  31.725  1.00 23.52 ? 367  GLN A O   1 
ATOM   2923 C  CB  . GLN A 1 367  ? 24.118 39.206  33.901  1.00 25.05 ? 367  GLN A CB  1 
ATOM   2924 C  CG  . GLN A 1 367  ? 24.186 40.115  35.115  1.00 28.85 ? 367  GLN A CG  1 
ATOM   2925 C  CD  . GLN A 1 367  ? 23.411 39.566  36.292  1.00 32.99 ? 367  GLN A CD  1 
ATOM   2926 O  OE1 . GLN A 1 367  ? 22.200 39.344  36.200  1.00 34.41 ? 367  GLN A OE1 1 
ATOM   2927 N  NE2 . GLN A 1 367  ? 24.104 39.358  37.408  1.00 35.15 ? 367  GLN A NE2 1 
ATOM   2928 N  N   . ALA A 1 368  ? 24.781 35.734  33.163  1.00 24.03 ? 368  ALA A N   1 
ATOM   2929 C  CA  . ALA A 1 368  ? 24.578 34.685  32.161  1.00 23.11 ? 368  ALA A CA  1 
ATOM   2930 C  C   . ALA A 1 368  ? 23.352 34.883  31.277  1.00 22.75 ? 368  ALA A C   1 
ATOM   2931 O  O   . ALA A 1 368  ? 23.414 34.593  30.074  1.00 22.20 ? 368  ALA A O   1 
ATOM   2932 C  CB  . ALA A 1 368  ? 24.518 33.321  32.842  1.00 23.70 ? 368  ALA A CB  1 
ATOM   2933 N  N   . HIS A 1 369  ? 22.249 35.370  31.849  1.00 21.39 ? 369  HIS A N   1 
ATOM   2934 C  CA  . HIS A 1 369  ? 20.992 35.528  31.124  1.00 21.89 ? 369  HIS A CA  1 
ATOM   2935 C  C   . HIS A 1 369  ? 21.107 36.423  29.872  1.00 20.72 ? 369  HIS A C   1 
ATOM   2936 O  O   . HIS A 1 369  ? 20.290 36.319  28.954  1.00 21.61 ? 369  HIS A O   1 
ATOM   2937 C  CB  . HIS A 1 369  ? 19.883 36.054  32.051  1.00 22.81 ? 369  HIS A CB  1 
ATOM   2938 C  CG  . HIS A 1 369  ? 20.098 37.460  32.518  1.00 24.67 ? 369  HIS A CG  1 
ATOM   2939 N  ND1 . HIS A 1 369  ? 19.613 38.551  31.828  1.00 28.45 ? 369  HIS A ND1 1 
ATOM   2940 C  CD2 . HIS A 1 369  ? 20.737 37.955  33.602  1.00 27.79 ? 369  HIS A CD2 1 
ATOM   2941 C  CE1 . HIS A 1 369  ? 19.947 39.658  32.463  1.00 26.70 ? 369  HIS A CE1 1 
ATOM   2942 N  NE2 . HIS A 1 369  ? 20.636 39.325  33.541  1.00 28.40 ? 369  HIS A NE2 1 
ATOM   2943 N  N   . PHE A 1 370  ? 22.101 37.315  29.850  1.00 20.73 ? 370  PHE A N   1 
ATOM   2944 C  CA  . PHE A 1 370  ? 22.304 38.148  28.656  1.00 18.61 ? 370  PHE A CA  1 
ATOM   2945 C  C   . PHE A 1 370  ? 22.926 37.356  27.503  1.00 17.15 ? 370  PHE A C   1 
ATOM   2946 O  O   . PHE A 1 370  ? 22.681 37.673  26.339  1.00 16.36 ? 370  PHE A O   1 
ATOM   2947 C  CB  . PHE A 1 370  ? 23.248 39.322  28.934  1.00 19.41 ? 370  PHE A CB  1 
ATOM   2948 C  CG  . PHE A 1 370  ? 22.681 40.415  29.800  1.00 20.00 ? 370  PHE A CG  1 
ATOM   2949 C  CD1 . PHE A 1 370  ? 21.536 41.112  29.427  1.00 20.69 ? 370  PHE A CD1 1 
ATOM   2950 C  CD2 . PHE A 1 370  ? 23.363 40.794  30.940  1.00 21.34 ? 370  PHE A CD2 1 
ATOM   2951 C  CE1 . PHE A 1 370  ? 21.048 42.171  30.234  1.00 22.79 ? 370  PHE A CE1 1 
ATOM   2952 C  CE2 . PHE A 1 370  ? 22.897 41.824  31.742  1.00 23.07 ? 370  PHE A CE2 1 
ATOM   2953 C  CZ  . PHE A 1 370  ? 21.746 42.518  31.380  1.00 21.01 ? 370  PHE A CZ  1 
ATOM   2954 N  N   . ASN A 1 371  ? 23.765 36.379  27.839  1.00 15.09 ? 371  ASN A N   1 
ATOM   2955 C  CA  . ASN A 1 371  ? 24.541 35.619  26.879  1.00 14.81 ? 371  ASN A CA  1 
ATOM   2956 C  C   . ASN A 1 371  ? 25.336 36.531  25.944  1.00 13.47 ? 371  ASN A C   1 
ATOM   2957 O  O   . ASN A 1 371  ? 25.321 36.365  24.728  1.00 13.89 ? 371  ASN A O   1 
ATOM   2958 C  CB  . ASN A 1 371  ? 23.654 34.635  26.097  1.00 15.42 ? 371  ASN A CB  1 
ATOM   2959 C  CG  . ASN A 1 371  ? 22.981 33.604  27.015  1.00 16.40 ? 371  ASN A CG  1 
ATOM   2960 O  OD1 . ASN A 1 371  ? 23.660 32.803  27.644  1.00 18.85 ? 371  ASN A OD1 1 
ATOM   2961 N  ND2 . ASN A 1 371  ? 21.667 33.677  27.113  1.00 19.26 ? 371  ASN A ND2 1 
ATOM   2962 N  N   . VAL A 1 372  ? 26.019 37.486  26.550  1.00 12.76 ? 372  VAL A N   1 
ATOM   2963 C  CA  . VAL A 1 372  ? 26.829 38.472  25.817  1.00 13.06 ? 372  VAL A CA  1 
ATOM   2964 C  C   . VAL A 1 372  ? 28.216 38.497  26.424  1.00 13.42 ? 372  VAL A C   1 
ATOM   2965 O  O   . VAL A 1 372  ? 28.375 38.424  27.664  1.00 14.02 ? 372  VAL A O   1 
ATOM   2966 C  CB  . VAL A 1 372  ? 26.184 39.883  25.906  1.00 13.18 ? 372  VAL A CB  1 
ATOM   2967 C  CG1 . VAL A 1 372  ? 27.169 40.987  25.390  1.00 13.38 ? 372  VAL A CG1 1 
ATOM   2968 C  CG2 . VAL A 1 372  ? 24.884 39.947  25.132  1.00 13.99 ? 372  VAL A CG2 1 
ATOM   2969 N  N   . GLN A 1 373  ? 29.244 38.625  25.584  1.00 12.60 ? 373  GLN A N   1 
ATOM   2970 C  CA  . GLN A 1 373  ? 30.600 38.952  26.036  1.00 12.13 ? 373  GLN A CA  1 
ATOM   2971 C  C   . GLN A 1 373  ? 30.981 40.262  25.319  1.00 11.68 ? 373  GLN A C   1 
ATOM   2972 O  O   . GLN A 1 373  ? 31.173 40.244  24.091  1.00 11.84 ? 373  GLN A O   1 
ATOM   2973 C  CB  . GLN A 1 373  ? 31.592 37.820  25.713  1.00 13.23 ? 373  GLN A CB  1 
ATOM   2974 C  CG  . GLN A 1 373  ? 33.073 38.137  26.036  1.00 15.26 ? 373  GLN A CG  1 
ATOM   2975 C  CD  . GLN A 1 373  ? 33.303 38.473  27.518  1.00 19.16 ? 373  GLN A CD  1 
ATOM   2976 O  OE1 . GLN A 1 373  ? 32.594 37.958  28.409  1.00 19.45 ? 373  GLN A OE1 1 
ATOM   2977 N  NE2 . GLN A 1 373  ? 34.293 39.324  27.785  1.00 19.83 ? 373  GLN A NE2 1 
ATOM   2978 N  N   . ALA A 1 374  ? 31.072 41.379  26.043  1.00 10.75 ? 374  ALA A N   1 
ATOM   2979 C  CA  . ALA A 1 374  ? 31.342 42.701  25.455  1.00 11.40 ? 374  ALA A CA  1 
ATOM   2980 C  C   . ALA A 1 374  ? 32.675 43.233  25.934  1.00 11.41 ? 374  ALA A C   1 
ATOM   2981 O  O   . ALA A 1 374  ? 33.036 43.055  27.127  1.00 11.49 ? 374  ALA A O   1 
ATOM   2982 C  CB  . ALA A 1 374  ? 30.245 43.647  25.840  1.00 11.03 ? 374  ALA A CB  1 
ATOM   2983 N  N   . GLN A 1 375  ? 33.399 43.925  25.055  1.00 10.95 ? 375  GLN A N   1 
ATOM   2984 C  CA  A GLN A 1 375  ? 34.709 44.470  25.408  0.50 11.10 ? 375  GLN A CA  1 
ATOM   2985 C  CA  B GLN A 1 375  ? 34.712 44.464  25.407  0.50 11.42 ? 375  GLN A CA  1 
ATOM   2986 C  C   . GLN A 1 375  ? 35.070 45.594  24.466  1.00 10.80 ? 375  GLN A C   1 
ATOM   2987 O  O   . GLN A 1 375  ? 34.511 45.683  23.367  1.00 11.06 ? 375  GLN A O   1 
ATOM   2988 C  CB  A GLN A 1 375  ? 35.781 43.399  25.291  0.50 11.38 ? 375  GLN A CB  1 
ATOM   2989 C  CB  B GLN A 1 375  ? 35.777 43.376  25.309  0.50 12.03 ? 375  GLN A CB  1 
ATOM   2990 C  CG  A GLN A 1 375  ? 35.717 42.600  23.993  0.50 12.94 ? 375  GLN A CG  1 
ATOM   2991 C  CG  B GLN A 1 375  ? 35.895 42.724  23.929  0.50 14.82 ? 375  GLN A CG  1 
ATOM   2992 C  CD  A GLN A 1 375  ? 34.885 41.324  24.123  0.50 13.06 ? 375  GLN A CD  1 
ATOM   2993 C  CD  B GLN A 1 375  ? 36.390 41.282  23.987  0.50 18.51 ? 375  GLN A CD  1 
ATOM   2994 O  OE1 A GLN A 1 375  ? 35.118 40.505  25.025  0.50 14.76 ? 375  GLN A OE1 1 
ATOM   2995 O  OE1 B GLN A 1 375  ? 35.803 40.439  24.669  0.50 20.88 ? 375  GLN A OE1 1 
ATOM   2996 N  NE2 A GLN A 1 375  ? 33.900 41.158  23.239  0.50 12.20 ? 375  GLN A NE2 1 
ATOM   2997 N  NE2 B GLN A 1 375  ? 37.473 41.001  23.283  0.50 19.17 ? 375  GLN A NE2 1 
ATOM   2998 N  N   . PHE A 1 376  ? 35.993 46.444  24.904  1.00 10.20 ? 376  PHE A N   1 
ATOM   2999 C  CA  . PHE A 1 376  ? 36.608 47.354  23.937  1.00 10.73 ? 376  PHE A CA  1 
ATOM   3000 C  C   . PHE A 1 376  ? 37.398 46.533  22.962  1.00 11.25 ? 376  PHE A C   1 
ATOM   3001 O  O   . PHE A 1 376  ? 38.037 45.551  23.314  1.00 12.01 ? 376  PHE A O   1 
ATOM   3002 C  CB  . PHE A 1 376  ? 37.554 48.320  24.624  1.00 11.43 ? 376  PHE A CB  1 
ATOM   3003 C  CG  . PHE A 1 376  ? 36.883 49.248  25.558  1.00 10.43 ? 376  PHE A CG  1 
ATOM   3004 C  CD1 . PHE A 1 376  ? 35.877 50.096  25.119  1.00 11.68 ? 376  PHE A CD1 1 
ATOM   3005 C  CD2 . PHE A 1 376  ? 37.277 49.301  26.910  1.00 12.03 ? 376  PHE A CD2 1 
ATOM   3006 C  CE1 . PHE A 1 376  ? 35.250 50.990  26.029  1.00 13.84 ? 376  PHE A CE1 1 
ATOM   3007 C  CE2 . PHE A 1 376  ? 36.618 50.177  27.803  1.00 13.67 ? 376  PHE A CE2 1 
ATOM   3008 C  CZ  . PHE A 1 376  ? 35.640 51.007  27.353  1.00 13.80 ? 376  PHE A CZ  1 
ATOM   3009 N  N   . GLY A 1 377  ? 37.364 46.959  21.701  1.00 10.27 ? 377  GLY A N   1 
ATOM   3010 C  CA  . GLY A 1 377  ? 38.083 46.263  20.659  1.00 10.88 ? 377  GLY A CA  1 
ATOM   3011 C  C   . GLY A 1 377  ? 38.564 47.250  19.610  1.00 9.34  ? 377  GLY A C   1 
ATOM   3012 O  O   . GLY A 1 377  ? 38.262 48.421  19.638  1.00 10.20 ? 377  GLY A O   1 
ATOM   3013 N  N   . THR A 1 378  ? 39.307 46.688  18.664  1.00 10.92 ? 378  THR A N   1 
ATOM   3014 C  CA  . THR A 1 378  ? 39.709 47.411  17.466  1.00 11.13 ? 378  THR A CA  1 
ATOM   3015 C  C   . THR A 1 378  ? 38.948 46.874  16.265  1.00 10.66 ? 378  THR A C   1 
ATOM   3016 O  O   . THR A 1 378  ? 38.240 45.840  16.303  1.00 10.67 ? 378  THR A O   1 
ATOM   3017 C  CB  . THR A 1 378  ? 41.218 47.319  17.202  1.00 11.54 ? 378  THR A CB  1 
ATOM   3018 O  OG1 . THR A 1 378  ? 41.546 45.976  16.851  1.00 12.86 ? 378  THR A OG1 1 
ATOM   3019 C  CG2 . THR A 1 378  ? 42.062 47.668  18.460  1.00 13.74 ? 378  THR A CG2 1 
ATOM   3020 N  N   . LEU A 1 379  ? 39.115 47.592  15.159  1.00 9.93  ? 379  LEU A N   1 
ATOM   3021 C  CA  . LEU A 1 379  ? 38.465 47.183  13.927  1.00 9.74  ? 379  LEU A CA  1 
ATOM   3022 C  C   . LEU A 1 379  ? 38.956 45.817  13.433  1.00 9.34  ? 379  LEU A C   1 
ATOM   3023 O  O   . LEU A 1 379  ? 38.169 44.951  13.038  1.00 9.09  ? 379  LEU A O   1 
ATOM   3024 C  CB  . LEU A 1 379  ? 38.650 48.275  12.872  1.00 9.61  ? 379  LEU A CB  1 
ATOM   3025 C  CG  . LEU A 1 379  ? 37.873 48.027  11.578  1.00 10.03 ? 379  LEU A CG  1 
ATOM   3026 C  CD1 . LEU A 1 379  ? 36.355 48.061  11.819  1.00 11.13 ? 379  LEU A CD1 1 
ATOM   3027 C  CD2 . LEU A 1 379  ? 38.286 49.101  10.527  1.00 10.53 ? 379  LEU A CD2 1 
ATOM   3028 N  N   . GLN A 1 380  ? 40.270 45.617  13.430  1.00 9.08  ? 380  GLN A N   1 
ATOM   3029 C  CA  . GLN A 1 380  ? 40.815 44.334  13.004  1.00 10.28 ? 380  GLN A CA  1 
ATOM   3030 C  C   . GLN A 1 380  ? 40.307 43.187  13.883  1.00 10.29 ? 380  GLN A C   1 
ATOM   3031 O  O   . GLN A 1 380  ? 40.057 42.079  13.380  1.00 10.32 ? 380  GLN A O   1 
ATOM   3032 C  CB  . GLN A 1 380  ? 42.346 44.374  12.971  1.00 11.37 ? 380  GLN A CB  1 
ATOM   3033 C  CG  . GLN A 1 380  ? 42.978 43.079  12.427  1.00 13.33 ? 380  GLN A CG  1 
ATOM   3034 C  CD  . GLN A 1 380  ? 42.703 42.923  10.962  1.00 14.86 ? 380  GLN A CD  1 
ATOM   3035 O  OE1 . GLN A 1 380  ? 42.794 43.896  10.208  1.00 15.69 ? 380  GLN A OE1 1 
ATOM   3036 N  NE2 . GLN A 1 380  ? 42.337 41.704  10.543  1.00 18.87 ? 380  GLN A NE2 1 
ATOM   3037 N  N   . GLU A 1 381  ? 40.168 43.424  15.181  1.00 10.47 ? 381  GLU A N   1 
ATOM   3038 C  CA  . GLU A 1 381  ? 39.674 42.359  16.064  1.00 11.05 ? 381  GLU A CA  1 
ATOM   3039 C  C   . GLU A 1 381  ? 38.244 41.975  15.673  1.00 10.42 ? 381  GLU A C   1 
ATOM   3040 O  O   . GLU A 1 381  ? 37.914 40.789  15.654  1.00 11.95 ? 381  GLU A O   1 
ATOM   3041 C  CB  . GLU A 1 381  ? 39.657 42.841  17.512  1.00 12.04 ? 381  GLU A CB  1 
ATOM   3042 C  CG  . GLU A 1 381  ? 40.973 42.860  18.278  1.00 16.36 ? 381  GLU A CG  1 
ATOM   3043 C  CD  . GLU A 1 381  ? 40.662 43.185  19.728  1.00 22.27 ? 381  GLU A CD  1 
ATOM   3044 O  OE1 . GLU A 1 381  ? 40.485 44.352  20.008  1.00 20.97 ? 381  GLU A OE1 1 
ATOM   3045 O  OE2 . GLU A 1 381  ? 40.534 42.262  20.595  1.00 27.81 ? 381  GLU A OE2 1 
ATOM   3046 N  N   . TYR A 1 382  ? 37.411 42.964  15.360  1.00 9.78  ? 382  TYR A N   1 
ATOM   3047 C  CA  . TYR A 1 382  ? 36.076 42.666  14.862  1.00 9.12  ? 382  TYR A CA  1 
ATOM   3048 C  C   . TYR A 1 382  ? 36.120 41.773  13.613  1.00 8.98  ? 382  TYR A C   1 
ATOM   3049 O  O   . TYR A 1 382  ? 35.479 40.723  13.541  1.00 9.35  ? 382  TYR A O   1 
ATOM   3050 C  CB  . TYR A 1 382  ? 35.303 43.961  14.550  1.00 9.68  ? 382  TYR A CB  1 
ATOM   3051 C  CG  . TYR A 1 382  ? 33.999 43.671  13.842  1.00 8.75  ? 382  TYR A CG  1 
ATOM   3052 C  CD1 . TYR A 1 382  ? 32.926 43.089  14.527  1.00 9.18  ? 382  TYR A CD1 1 
ATOM   3053 C  CD2 . TYR A 1 382  ? 33.857 43.889  12.455  1.00 9.56  ? 382  TYR A CD2 1 
ATOM   3054 C  CE1 . TYR A 1 382  ? 31.742 42.750  13.864  1.00 10.65 ? 382  TYR A CE1 1 
ATOM   3055 C  CE2 . TYR A 1 382  ? 32.671 43.590  11.798  1.00 10.58 ? 382  TYR A CE2 1 
ATOM   3056 C  CZ  . TYR A 1 382  ? 31.621 42.996  12.523  1.00 9.98  ? 382  TYR A CZ  1 
ATOM   3057 O  OH  . TYR A 1 382  ? 30.414 42.654  11.914  1.00 10.54 ? 382  TYR A OH  1 
ATOM   3058 N  N   . PHE A 1 383  ? 36.869 42.203  12.601  1.00 8.79  ? 383  PHE A N   1 
ATOM   3059 C  CA  . PHE A 1 383  ? 36.901 41.428  11.366  1.00 8.63  ? 383  PHE A CA  1 
ATOM   3060 C  C   . PHE A 1 383  ? 37.480 40.026  11.586  1.00 9.11  ? 383  PHE A C   1 
ATOM   3061 O  O   . PHE A 1 383  ? 36.994 39.060  11.001  1.00 10.27 ? 383  PHE A O   1 
ATOM   3062 C  CB  . PHE A 1 383  ? 37.668 42.163  10.265  1.00 8.81  ? 383  PHE A CB  1 
ATOM   3063 C  CG  . PHE A 1 383  ? 36.910 43.333  9.655   1.00 9.11  ? 383  PHE A CG  1 
ATOM   3064 C  CD1 . PHE A 1 383  ? 35.697 43.130  8.996   1.00 10.03 ? 383  PHE A CD1 1 
ATOM   3065 C  CD2 . PHE A 1 383  ? 37.439 44.633  9.695   1.00 9.42  ? 383  PHE A CD2 1 
ATOM   3066 C  CE1 . PHE A 1 383  ? 34.997 44.183  8.419   1.00 10.48 ? 383  PHE A CE1 1 
ATOM   3067 C  CE2 . PHE A 1 383  ? 36.742 45.694  9.090   1.00 9.24  ? 383  PHE A CE2 1 
ATOM   3068 C  CZ  . PHE A 1 383  ? 35.534 45.468  8.467   1.00 9.11  ? 383  PHE A CZ  1 
ATOM   3069 N  N   . ASP A 1 384  ? 38.533 39.926  12.399  1.00 10.38 ? 384  ASP A N   1 
ATOM   3070 C  CA  . ASP A 1 384  ? 39.106 38.587  12.665  1.00 12.05 ? 384  ASP A CA  1 
ATOM   3071 C  C   . ASP A 1 384  ? 38.053 37.656  13.260  1.00 11.20 ? 384  ASP A C   1 
ATOM   3072 O  O   . ASP A 1 384  ? 37.942 36.468  12.867  1.00 12.06 ? 384  ASP A O   1 
ATOM   3073 C  CB  . ASP A 1 384  ? 40.253 38.700  13.659  1.00 12.52 ? 384  ASP A CB  1 
ATOM   3074 C  CG  . ASP A 1 384  ? 41.479 39.297  13.073  1.00 15.19 ? 384  ASP A CG  1 
ATOM   3075 O  OD1 . ASP A 1 384  ? 41.608 39.449  11.838  1.00 17.45 ? 384  ASP A OD1 1 
ATOM   3076 O  OD2 . ASP A 1 384  ? 42.390 39.647  13.845  1.00 18.05 ? 384  ASP A OD2 1 
ATOM   3077 N  N   . ALA A 1 385  ? 37.268 38.176  14.190  1.00 10.55 ? 385  ALA A N   1 
ATOM   3078 C  CA  . ALA A 1 385  ? 36.233 37.370  14.824  1.00 11.36 ? 385  ALA A CA  1 
ATOM   3079 C  C   . ALA A 1 385  ? 35.110 37.028  13.849  1.00 11.96 ? 385  ALA A C   1 
ATOM   3080 O  O   . ALA A 1 385  ? 34.622 35.899  13.841  1.00 12.24 ? 385  ALA A O   1 
ATOM   3081 C  CB  . ALA A 1 385  ? 35.708 38.082  16.061  1.00 11.54 ? 385  ALA A CB  1 
ATOM   3082 N  N   . VAL A 1 386  ? 34.715 37.969  12.974  1.00 11.11 ? 386  VAL A N   1 
ATOM   3083 C  CA  . VAL A 1 386  ? 33.720 37.643  11.951  1.00 11.70 ? 386  VAL A CA  1 
ATOM   3084 C  C   . VAL A 1 386  ? 34.183 36.502  11.063  1.00 11.87 ? 386  VAL A C   1 
ATOM   3085 O  O   . VAL A 1 386  ? 33.417 35.569  10.761  1.00 11.98 ? 386  VAL A O   1 
ATOM   3086 C  CB  . VAL A 1 386  ? 33.384 38.891  11.063  1.00 11.09 ? 386  VAL A CB  1 
ATOM   3087 C  CG1 . VAL A 1 386  ? 32.583 38.507  9.817   1.00 13.41 ? 386  VAL A CG1 1 
ATOM   3088 C  CG2 . VAL A 1 386  ? 32.634 39.900  11.893  1.00 12.59 ? 386  VAL A CG2 1 
ATOM   3089 N  N   . HIS A 1 387  ? 35.435 36.568  10.635  1.00 11.53 ? 387  HIS A N   1 
ATOM   3090 C  CA  . HIS A 1 387  ? 35.944 35.529  9.725   1.00 12.40 ? 387  HIS A CA  1 
ATOM   3091 C  C   . HIS A 1 387  ? 36.161 34.184  10.421  1.00 12.75 ? 387  HIS A C   1 
ATOM   3092 O  O   . HIS A 1 387  ? 36.029 33.127  9.779   1.00 13.50 ? 387  HIS A O   1 
ATOM   3093 C  CB  . HIS A 1 387  ? 37.173 35.994  8.953   1.00 13.19 ? 387  HIS A CB  1 
ATOM   3094 C  CG  . HIS A 1 387  ? 36.866 37.122  8.022   1.00 11.72 ? 387  HIS A CG  1 
ATOM   3095 N  ND1 . HIS A 1 387  ? 35.922 37.011  7.026   1.00 15.88 ? 387  HIS A ND1 1 
ATOM   3096 C  CD2 . HIS A 1 387  ? 37.328 38.394  7.966   1.00 12.68 ? 387  HIS A CD2 1 
ATOM   3097 C  CE1 . HIS A 1 387  ? 35.838 38.159  6.372   1.00 16.69 ? 387  HIS A CE1 1 
ATOM   3098 N  NE2 . HIS A 1 387  ? 36.681 39.011  6.926   1.00 14.44 ? 387  HIS A NE2 1 
ATOM   3099 N  N   . GLN A 1 388  ? 36.424 34.225  11.718  1.00 13.73 ? 388  GLN A N   1 
ATOM   3100 C  CA  . GLN A 1 388  ? 36.485 32.981  12.511  1.00 15.33 ? 388  GLN A CA  1 
ATOM   3101 C  C   . GLN A 1 388  ? 35.114 32.320  12.511  1.00 16.40 ? 388  GLN A C   1 
ATOM   3102 O  O   . GLN A 1 388  ? 35.007 31.097  12.299  1.00 16.57 ? 388  GLN A O   1 
ATOM   3103 C  CB  . GLN A 1 388  ? 36.996 33.290  13.904  1.00 15.62 ? 388  GLN A CB  1 
ATOM   3104 C  CG  . GLN A 1 388  ? 38.508 33.516  13.945  1.00 19.94 ? 388  GLN A CG  1 
ATOM   3105 C  CD  . GLN A 1 388  ? 38.972 34.254  15.200  1.00 27.00 ? 388  GLN A CD  1 
ATOM   3106 O  OE1 . GLN A 1 388  ? 38.177 34.509  16.119  1.00 30.72 ? 388  GLN A OE1 1 
ATOM   3107 N  NE2 . GLN A 1 388  ? 40.259 34.611  15.239  1.00 29.80 ? 388  GLN A NE2 1 
ATOM   3108 N  N   . ALA A 1 389  ? 34.064 33.117  12.667  1.00 16.62 ? 389  ALA A N   1 
ATOM   3109 C  CA  . ALA A 1 389  ? 32.673 32.637  12.629  1.00 18.15 ? 389  ALA A CA  1 
ATOM   3110 C  C   . ALA A 1 389  ? 32.313 32.059  11.267  1.00 19.34 ? 389  ALA A C   1 
ATOM   3111 O  O   . ALA A 1 389  ? 31.664 31.009  11.193  1.00 20.63 ? 389  ALA A O   1 
ATOM   3112 C  CB  . ALA A 1 389  ? 31.727 33.771  12.997  1.00 17.33 ? 389  ALA A CB  1 
ATOM   3113 N  N   . GLU A 1 390  ? 32.738 32.743  10.199  1.00 19.52 ? 390  GLU A N   1 
ATOM   3114 C  CA  . GLU A 1 390  ? 32.556 32.312  8.815   1.00 21.29 ? 390  GLU A CA  1 
ATOM   3115 C  C   . GLU A 1 390  ? 33.221 30.968  8.566   1.00 22.07 ? 390  GLU A C   1 
ATOM   3116 O  O   . GLU A 1 390  ? 32.601 30.067  7.986   1.00 22.81 ? 390  GLU A O   1 
ATOM   3117 C  CB  . GLU A 1 390  ? 33.136 33.373  7.862   1.00 20.60 ? 390  GLU A CB  1 
ATOM   3118 C  CG  . GLU A 1 390  ? 32.985 33.087  6.369   1.00 22.00 ? 390  GLU A CG  1 
ATOM   3119 C  CD  . GLU A 1 390  ? 33.751 34.082  5.512   1.00 23.63 ? 390  GLU A CD  1 
ATOM   3120 O  OE1 . GLU A 1 390  ? 34.575 34.847  6.070   1.00 23.94 ? 390  GLU A OE1 1 
ATOM   3121 O  OE2 . GLU A 1 390  ? 33.536 34.103  4.272   1.00 27.90 ? 390  GLU A OE2 1 
ATOM   3122 N  N   . ARG A 1 391  ? 34.471 30.826  9.009   1.00 22.79 ? 391  ARG A N   1 
ATOM   3123 C  CA  . ARG A 1 391  ? 35.199 29.564  8.848   1.00 24.65 ? 391  ARG A CA  1 
ATOM   3124 C  C   . ARG A 1 391  ? 34.559 28.435  9.672   1.00 24.13 ? 391  ARG A C   1 
ATOM   3125 O  O   . ARG A 1 391  ? 34.629 27.257  9.279   1.00 25.82 ? 391  ARG A O   1 
ATOM   3126 C  CB  . ARG A 1 391  ? 36.667 29.725  9.228   1.00 24.37 ? 391  ARG A CB  1 
ATOM   3127 C  CG  . ARG A 1 391  ? 37.463 30.591  8.278   1.00 26.82 ? 391  ARG A CG  1 
ATOM   3128 C  CD  . ARG A 1 391  ? 38.973 30.497  8.452   1.00 26.94 ? 391  ARG A CD  1 
ATOM   3129 N  NE  . ARG A 1 391  ? 39.450 30.924  9.767   1.00 31.65 ? 391  ARG A NE  1 
ATOM   3130 C  CZ  . ARG A 1 391  ? 39.664 32.192  10.131  1.00 32.65 ? 391  ARG A CZ  1 
ATOM   3131 N  NH1 . ARG A 1 391  ? 39.420 33.195  9.297   1.00 33.05 ? 391  ARG A NH1 1 
ATOM   3132 N  NH2 . ARG A 1 391  ? 40.108 32.456  11.350  1.00 34.09 ? 391  ARG A NH2 1 
ATOM   3133 N  N   . ALA A 1 392  ? 33.929 28.781  10.791  1.00 24.24 ? 392  ALA A N   1 
ATOM   3134 C  CA  . ALA A 1 392  ? 33.216 27.793  11.610  1.00 24.80 ? 392  ALA A CA  1 
ATOM   3135 C  C   . ALA A 1 392  ? 31.896 27.363  10.949  1.00 25.30 ? 392  ALA A C   1 
ATOM   3136 O  O   . ALA A 1 392  ? 31.139 26.552  11.521  1.00 26.48 ? 392  ALA A O   1 
ATOM   3137 C  CB  . ALA A 1 392  ? 32.967 28.330  13.000  1.00 24.78 ? 392  ALA A CB  1 
ATOM   3138 N  N   . GLY A 1 393  ? 31.634 27.888  9.748   1.00 24.95 ? 393  GLY A N   1 
ATOM   3139 C  CA  . GLY A 1 393  ? 30.424 27.582  9.005   1.00 24.89 ? 393  GLY A CA  1 
ATOM   3140 C  C   . GLY A 1 393  ? 29.194 28.268  9.540   1.00 24.30 ? 393  GLY A C   1 
ATOM   3141 O  O   . GLY A 1 393  ? 28.077 27.851  9.246   1.00 24.97 ? 393  GLY A O   1 
ATOM   3142 N  N   . GLN A 1 394  ? 29.366 29.344  10.304  1.00 24.08 ? 394  GLN A N   1 
ATOM   3143 C  CA  . GLN A 1 394  ? 28.200 29.957  10.916  1.00 24.57 ? 394  GLN A CA  1 
ATOM   3144 C  C   . GLN A 1 394  ? 27.520 30.991  10.000  1.00 23.64 ? 394  GLN A C   1 
ATOM   3145 O  O   . GLN A 1 394  ? 26.368 31.379  10.237  1.00 24.68 ? 394  GLN A O   1 
ATOM   3146 C  CB  . GLN A 1 394  ? 28.517 30.474  12.325  1.00 25.67 ? 394  GLN A CB  1 
ATOM   3147 C  CG  . GLN A 1 394  ? 28.777 31.934  12.427  1.00 28.77 ? 394  GLN A CG  1 
ATOM   3148 C  CD  . GLN A 1 394  ? 28.617 32.441  13.852  1.00 29.34 ? 394  GLN A CD  1 
ATOM   3149 O  OE1 . GLN A 1 394  ? 28.005 33.469  14.052  1.00 25.98 ? 394  GLN A OE1 1 
ATOM   3150 N  NE2 . GLN A 1 394  ? 29.165 31.713  14.838  1.00 29.52 ? 394  GLN A NE2 1 
ATOM   3151 N  N   . ALA A 1 395  ? 28.213 31.381  8.923   1.00 22.32 ? 395  ALA A N   1 
ATOM   3152 C  CA  . ALA A 1 395  ? 27.684 32.365  7.977   1.00 21.34 ? 395  ALA A CA  1 
ATOM   3153 C  C   . ALA A 1 395  ? 28.312 32.220  6.587   1.00 20.98 ? 395  ALA A C   1 
ATOM   3154 O  O   . ALA A 1 395  ? 29.470 31.824  6.456   1.00 20.75 ? 395  ALA A O   1 
ATOM   3155 C  CB  . ALA A 1 395  ? 27.909 33.802  8.533   1.00 21.90 ? 395  ALA A CB  1 
ATOM   3156 N  N   . GLU A 1 396  ? 27.532 32.521  5.554   1.00 20.61 ? 396  GLU A N   1 
ATOM   3157 C  CA  . GLU A 1 396  ? 28.066 32.718  4.210   1.00 21.18 ? 396  GLU A CA  1 
ATOM   3158 C  C   . GLU A 1 396  ? 27.684 34.140  3.814   1.00 18.47 ? 396  GLU A C   1 
ATOM   3159 O  O   . GLU A 1 396  ? 26.610 34.624  4.202   1.00 18.37 ? 396  GLU A O   1 
ATOM   3160 C  CB  . GLU A 1 396  ? 27.518 31.687  3.206   1.00 21.57 ? 396  GLU A CB  1 
ATOM   3161 C  CG  . GLU A 1 396  ? 26.002 31.592  3.134   1.00 26.77 ? 396  GLU A CG  1 
ATOM   3162 C  CD  . GLU A 1 396  ? 25.518 30.288  2.517   1.00 26.96 ? 396  GLU A CD  1 
ATOM   3163 O  OE1 . GLU A 1 396  ? 25.985 29.924  1.415   1.00 35.08 ? 396  GLU A OE1 1 
ATOM   3164 O  OE2 . GLU A 1 396  ? 24.652 29.615  3.134   1.00 35.26 ? 396  GLU A OE2 1 
ATOM   3165 N  N   . PHE A 1 397  ? 28.570 34.805  3.092   1.00 15.69 ? 397  PHE A N   1 
ATOM   3166 C  CA  . PHE A 1 397  ? 28.326 36.194  2.743   1.00 13.15 ? 397  PHE A CA  1 
ATOM   3167 C  C   . PHE A 1 397  ? 27.974 36.372  1.266   1.00 12.25 ? 397  PHE A C   1 
ATOM   3168 O  O   . PHE A 1 397  ? 28.535 35.689  0.426   1.00 13.48 ? 397  PHE A O   1 
ATOM   3169 C  CB  . PHE A 1 397  ? 29.552 37.032  3.106   1.00 13.51 ? 397  PHE A CB  1 
ATOM   3170 C  CG  . PHE A 1 397  ? 29.831 37.063  4.586   1.00 11.69 ? 397  PHE A CG  1 
ATOM   3171 C  CD1 . PHE A 1 397  ? 29.011 37.777  5.426   1.00 10.87 ? 397  PHE A CD1 1 
ATOM   3172 C  CD2 . PHE A 1 397  ? 30.911 36.369  5.113   1.00 13.60 ? 397  PHE A CD2 1 
ATOM   3173 C  CE1 . PHE A 1 397  ? 29.231 37.804  6.793   1.00 11.56 ? 397  PHE A CE1 1 
ATOM   3174 C  CE2 . PHE A 1 397  ? 31.149 36.399  6.515   1.00 14.91 ? 397  PHE A CE2 1 
ATOM   3175 C  CZ  . PHE A 1 397  ? 30.306 37.102  7.328   1.00 13.25 ? 397  PHE A CZ  1 
ATOM   3176 N  N   . PRO A 1 398  ? 27.064 37.283  0.979   1.00 10.69 ? 398  PRO A N   1 
ATOM   3177 C  CA  . PRO A 1 398  ? 26.696 37.572  -0.416  1.00 10.82 ? 398  PRO A CA  1 
ATOM   3178 C  C   . PRO A 1 398  ? 27.788 38.314  -1.162  1.00 10.73 ? 398  PRO A C   1 
ATOM   3179 O  O   . PRO A 1 398  ? 28.630 38.985  -0.554  1.00 10.37 ? 398  PRO A O   1 
ATOM   3180 C  CB  . PRO A 1 398  ? 25.455 38.431  -0.266  1.00 12.33 ? 398  PRO A CB  1 
ATOM   3181 C  CG  . PRO A 1 398  ? 25.683 39.181  1.032   1.00 11.56 ? 398  PRO A CG  1 
ATOM   3182 C  CD  . PRO A 1 398  ? 26.310 38.134  1.911   1.00 11.77 ? 398  PRO A CD  1 
ATOM   3183 N  N   . THR A 1 399  ? 27.741 38.187  -2.472  1.00 9.86  ? 399  THR A N   1 
ATOM   3184 C  CA  . THR A 1 399  ? 28.628 38.928  -3.360  1.00 9.02  ? 399  THR A CA  1 
ATOM   3185 C  C   . THR A 1 399  ? 27.888 40.152  -3.885  1.00 9.45  ? 399  THR A C   1 
ATOM   3186 O  O   . THR A 1 399  ? 26.669 40.143  -4.030  1.00 10.00 ? 399  THR A O   1 
ATOM   3187 C  CB  . THR A 1 399  ? 29.053 38.050  -4.525  1.00 10.16 ? 399  THR A CB  1 
ATOM   3188 O  OG1 . THR A 1 399  ? 27.871 37.592  -5.210  1.00 11.96 ? 399  THR A OG1 1 
ATOM   3189 C  CG2 . THR A 1 399  ? 29.831 36.806  -4.035  1.00 11.28 ? 399  THR A CG2 1 
ATOM   3190 N  N   . LEU A 1 400  ? 28.652 41.220  -4.139  1.00 8.67  ? 400  LEU A N   1 
ATOM   3191 C  CA  . LEU A 1 400  ? 28.042 42.481  -4.564  1.00 8.25  ? 400  LEU A CA  1 
ATOM   3192 C  C   . LEU A 1 400  ? 28.957 43.172  -5.556  1.00 8.19  ? 400  LEU A C   1 
ATOM   3193 O  O   . LEU A 1 400  ? 30.179 43.141  -5.426  1.00 7.86  ? 400  LEU A O   1 
ATOM   3194 C  CB  . LEU A 1 400  ? 27.756 43.353  -3.338  1.00 8.35  ? 400  LEU A CB  1 
ATOM   3195 C  CG  . LEU A 1 400  ? 27.101 44.739  -3.559  1.00 8.41  ? 400  LEU A CG  1 
ATOM   3196 C  CD1 . LEU A 1 400  ? 26.267 45.155  -2.339  1.00 10.43 ? 400  LEU A CD1 1 
ATOM   3197 C  CD2 . LEU A 1 400  ? 28.105 45.843  -3.901  1.00 9.28  ? 400  LEU A CD2 1 
ATOM   3198 N  N   . SER A 1 401  ? 28.333 43.802  -6.558  1.00 7.59  ? 401  SER A N   1 
ATOM   3199 C  CA  . SER A 1 401  ? 29.070 44.760  -7.403  1.00 7.53  ? 401  SER A CA  1 
ATOM   3200 C  C   . SER A 1 401  ? 28.230 46.008  -7.592  1.00 7.18  ? 401  SER A C   1 
ATOM   3201 O  O   . SER A 1 401  ? 27.001 45.990  -7.396  1.00 7.68  ? 401  SER A O   1 
ATOM   3202 C  CB  . SER A 1 401  ? 29.478 44.165  -8.745  1.00 8.21  ? 401  SER A CB  1 
ATOM   3203 O  OG  . SER A 1 401  ? 28.369 44.126  -9.621  1.00 8.81  ? 401  SER A OG  1 
ATOM   3204 N  N   . GLY A 1 402  ? 28.924 47.103  -7.926  1.00 7.42  ? 402  GLY A N   1 
ATOM   3205 C  CA  . GLY A 1 402  ? 28.276 48.387  -8.177  1.00 8.20  ? 402  GLY A CA  1 
ATOM   3206 C  C   . GLY A 1 402  ? 28.877 49.462  -7.298  1.00 7.97  ? 402  GLY A C   1 
ATOM   3207 O  O   . GLY A 1 402  ? 29.934 49.254  -6.665  1.00 8.90  ? 402  GLY A O   1 
ATOM   3208 N  N   . ASP A 1 403  ? 28.249 50.623  -7.277  1.00 6.95  ? 403  ASP A N   1 
ATOM   3209 C  CA  . ASP A 1 403  ? 28.716 51.732  -6.438  1.00 7.63  ? 403  ASP A CA  1 
ATOM   3210 C  C   . ASP A 1 403  ? 27.596 52.193  -5.523  1.00 7.71  ? 403  ASP A C   1 
ATOM   3211 O  O   . ASP A 1 403  ? 26.479 51.617  -5.505  1.00 8.47  ? 403  ASP A O   1 
ATOM   3212 C  CB  . ASP A 1 403  ? 29.262 52.872  -7.295  1.00 7.76  ? 403  ASP A CB  1 
ATOM   3213 C  CG  . ASP A 1 403  ? 28.189 53.640  -8.006  1.00 9.94  ? 403  ASP A CG  1 
ATOM   3214 O  OD1 . ASP A 1 403  ? 27.026 53.195  -8.034  1.00 13.02 ? 403  ASP A OD1 1 
ATOM   3215 O  OD2 . ASP A 1 403  ? 28.481 54.731  -8.516  1.00 13.22 ? 403  ASP A OD2 1 
ATOM   3216 N  N   . PHE A 1 404  ? 27.892 53.202  -4.716  1.00 6.78  ? 404  PHE A N   1 
ATOM   3217 C  CA  . PHE A 1 404  ? 26.965 53.773  -3.746  1.00 7.21  ? 404  PHE A CA  1 
ATOM   3218 C  C   . PHE A 1 404  ? 26.874 55.290  -3.907  1.00 6.90  ? 404  PHE A C   1 
ATOM   3219 O  O   . PHE A 1 404  ? 26.984 56.050  -2.945  1.00 8.30  ? 404  PHE A O   1 
ATOM   3220 C  CB  . PHE A 1 404  ? 27.359 53.365  -2.301  1.00 7.64  ? 404  PHE A CB  1 
ATOM   3221 C  CG  . PHE A 1 404  ? 27.316 51.872  -2.082  1.00 7.12  ? 404  PHE A CG  1 
ATOM   3222 C  CD1 . PHE A 1 404  ? 26.069 51.245  -1.939  1.00 7.08  ? 404  PHE A CD1 1 
ATOM   3223 C  CD2 . PHE A 1 404  ? 28.459 51.103  -2.093  1.00 6.99  ? 404  PHE A CD2 1 
ATOM   3224 C  CE1 . PHE A 1 404  ? 25.982 49.830  -1.802  1.00 8.15  ? 404  PHE A CE1 1 
ATOM   3225 C  CE2 . PHE A 1 404  ? 28.383 49.685  -1.921  1.00 7.85  ? 404  PHE A CE2 1 
ATOM   3226 C  CZ  . PHE A 1 404  ? 27.130 49.065  -1.785  1.00 7.68  ? 404  PHE A CZ  1 
ATOM   3227 N  N   . PHE A 1 405  ? 26.621 55.682  -5.163  1.00 7.44  ? 405  PHE A N   1 
ATOM   3228 C  CA  . PHE A 1 405  ? 26.257 57.072  -5.495  1.00 6.98  ? 405  PHE A CA  1 
ATOM   3229 C  C   . PHE A 1 405  ? 24.877 57.038  -6.140  1.00 7.54  ? 405  PHE A C   1 
ATOM   3230 O  O   . PHE A 1 405  ? 24.567 56.051  -6.828  1.00 8.77  ? 405  PHE A O   1 
ATOM   3231 C  CB  . PHE A 1 405  ? 27.245 57.693  -6.476  1.00 8.08  ? 405  PHE A CB  1 
ATOM   3232 C  CG  . PHE A 1 405  ? 28.654 57.775  -5.948  1.00 7.69  ? 405  PHE A CG  1 
ATOM   3233 C  CD1 . PHE A 1 405  ? 28.915 58.578  -4.862  1.00 7.86  ? 405  PHE A CD1 1 
ATOM   3234 C  CD2 . PHE A 1 405  ? 29.692 57.074  -6.541  1.00 8.68  ? 405  PHE A CD2 1 
ATOM   3235 C  CE1 . PHE A 1 405  ? 30.225 58.682  -4.315  1.00 7.50  ? 405  PHE A CE1 1 
ATOM   3236 C  CE2 . PHE A 1 405  ? 30.999 57.160  -6.016  1.00 8.53  ? 405  PHE A CE2 1 
ATOM   3237 C  CZ  . PHE A 1 405  ? 31.256 57.974  -4.889  1.00 8.25  ? 405  PHE A CZ  1 
ATOM   3238 N  N   . THR A 1 406  ? 24.065 58.086  -6.017  1.00 8.04  ? 406  THR A N   1 
ATOM   3239 C  CA  . THR A 1 406  ? 24.304 59.283  -5.229  1.00 7.66  ? 406  THR A CA  1 
ATOM   3240 C  C   . THR A 1 406  ? 23.678 59.172  -3.850  1.00 8.24  ? 406  THR A C   1 
ATOM   3241 O  O   . THR A 1 406  ? 22.514 58.744  -3.696  1.00 8.68  ? 406  THR A O   1 
ATOM   3242 C  CB  . THR A 1 406  ? 23.745 60.501  -6.014  1.00 7.94  ? 406  THR A CB  1 
ATOM   3243 O  OG1 . THR A 1 406  ? 24.669 60.728  -7.082  1.00 8.23  ? 406  THR A OG1 1 
ATOM   3244 C  CG2 . THR A 1 406  ? 23.676 61.770  -5.184  1.00 9.09  ? 406  THR A CG2 1 
ATOM   3245 N  N   . TYR A 1 407  ? 24.459 59.527  -2.846  1.00 7.93  ? 407  TYR A N   1 
ATOM   3246 C  CA  . TYR A 1 407  ? 24.051 59.431  -1.458  1.00 7.32  ? 407  TYR A CA  1 
ATOM   3247 C  C   . TYR A 1 407  ? 22.911 60.389  -1.159  1.00 7.92  ? 407  TYR A C   1 
ATOM   3248 O  O   . TYR A 1 407  ? 22.909 61.510  -1.606  1.00 8.07  ? 407  TYR A O   1 
ATOM   3249 C  CB  . TYR A 1 407  ? 25.259 59.778  -0.605  1.00 7.78  ? 407  TYR A CB  1 
ATOM   3250 C  CG  . TYR A 1 407  ? 25.071 59.910  0.891   1.00 7.71  ? 407  TYR A CG  1 
ATOM   3251 C  CD1 . TYR A 1 407  ? 24.605 58.861  1.676   1.00 8.78  ? 407  TYR A CD1 1 
ATOM   3252 C  CD2 . TYR A 1 407  ? 25.476 61.053  1.527   1.00 8.07  ? 407  TYR A CD2 1 
ATOM   3253 C  CE1 . TYR A 1 407  ? 24.512 59.003  3.047   1.00 9.40  ? 407  TYR A CE1 1 
ATOM   3254 C  CE2 . TYR A 1 407  ? 25.388 61.200  2.873   1.00 9.71  ? 407  TYR A CE2 1 
ATOM   3255 C  CZ  . TYR A 1 407  ? 24.911 60.178  3.638   1.00 9.11  ? 407  TYR A CZ  1 
ATOM   3256 O  OH  . TYR A 1 407  ? 24.867 60.356  5.000   1.00 10.28 ? 407  TYR A OH  1 
ATOM   3257 N  N   . ALA A 1 408  ? 21.953 59.911  -0.379  1.00 8.81  ? 408  ALA A N   1 
ATOM   3258 C  CA  . ALA A 1 408  ? 20.983 60.785  0.302   1.00 9.41  ? 408  ALA A CA  1 
ATOM   3259 C  C   . ALA A 1 408  ? 20.900 60.335  1.736   1.00 9.27  ? 408  ALA A C   1 
ATOM   3260 O  O   . ALA A 1 408  ? 20.793 59.114  1.989   1.00 9.40  ? 408  ALA A O   1 
ATOM   3261 C  CB  . ALA A 1 408  ? 19.568 60.699  -0.362  1.00 10.06 ? 408  ALA A CB  1 
ATOM   3262 N  N   . ASP A 1 409  ? 20.980 61.270  2.676   1.00 8.79  ? 409  ASP A N   1 
ATOM   3263 C  CA  . ASP A 1 409  ? 20.914 60.912  4.100   1.00 9.94  ? 409  ASP A CA  1 
ATOM   3264 C  C   . ASP A 1 409  ? 19.482 60.995  4.658   1.00 10.41 ? 409  ASP A C   1 
ATOM   3265 O  O   . ASP A 1 409  ? 19.213 60.409  5.715   1.00 11.13 ? 409  ASP A O   1 
ATOM   3266 C  CB  . ASP A 1 409  ? 21.891 61.730  4.969   1.00 10.08 ? 409  ASP A CB  1 
ATOM   3267 C  CG  . ASP A 1 409  ? 21.698 63.238  4.888   1.00 9.60  ? 409  ASP A CG  1 
ATOM   3268 O  OD1 . ASP A 1 409  ? 21.045 63.766  3.965   1.00 10.11 ? 409  ASP A OD1 1 
ATOM   3269 O  OD2 . ASP A 1 409  ? 22.254 63.956  5.755   1.00 11.95 ? 409  ASP A OD2 1 
ATOM   3270 N  N   . ARG A 1 410  ? 18.589 61.680  3.935   1.00 10.18 ? 410  ARG A N   1 
ATOM   3271 C  CA  . ARG A 1 410  ? 17.186 61.813  4.379   1.00 11.55 ? 410  ARG A CA  1 
ATOM   3272 C  C   . ARG A 1 410  ? 16.384 62.445  3.249   1.00 12.11 ? 410  ARG A C   1 
ATOM   3273 O  O   . ARG A 1 410  ? 16.919 63.189  2.398   1.00 12.33 ? 410  ARG A O   1 
ATOM   3274 C  CB  . ARG A 1 410  ? 17.067 62.606  5.679   1.00 11.64 ? 410  ARG A CB  1 
ATOM   3275 C  CG  . ARG A 1 410  ? 17.553 64.063  5.630   1.00 13.42 ? 410  ARG A CG  1 
ATOM   3276 C  CD  . ARG A 1 410  ? 17.560 64.680  7.014   1.00 13.52 ? 410  ARG A CD  1 
ATOM   3277 N  NE  . ARG A 1 410  ? 18.283 65.950  7.142   1.00 15.16 ? 410  ARG A NE  1 
ATOM   3278 C  CZ  . ARG A 1 410  ? 17.747 67.152  6.959   1.00 17.20 ? 410  ARG A CZ  1 
ATOM   3279 N  NH1 . ARG A 1 410  ? 16.469 67.271  6.566   1.00 18.30 ? 410  ARG A NH1 1 
ATOM   3280 N  NH2 . ARG A 1 410  ? 18.488 68.240  7.114   1.00 17.91 ? 410  ARG A NH2 1 
ATOM   3281 N  N   . SER A 1 411  ? 15.088 62.091  3.223   1.00 12.79 ? 411  SER A N   1 
ATOM   3282 C  CA  A SER A 1 411  ? 14.099 62.616  2.279   0.50 13.58 ? 411  SER A CA  1 
ATOM   3283 C  CA  B SER A 1 411  ? 14.131 62.698  2.308   0.50 13.60 ? 411  SER A CA  1 
ATOM   3284 C  C   . SER A 1 411  ? 14.663 62.717  0.866   1.00 12.98 ? 411  SER A C   1 
ATOM   3285 O  O   . SER A 1 411  ? 15.144 61.704  0.333   1.00 13.33 ? 411  SER A O   1 
ATOM   3286 C  CB  A SER A 1 411  ? 13.462 63.910  2.784   0.50 14.60 ? 411  SER A CB  1 
ATOM   3287 C  CB  B SER A 1 411  ? 13.782 64.103  2.802   0.50 14.77 ? 411  SER A CB  1 
ATOM   3288 O  OG  A SER A 1 411  ? 14.434 64.881  3.093   0.50 15.99 ? 411  SER A OG  1 
ATOM   3289 O  OG  B SER A 1 411  ? 12.697 64.633  2.078   0.50 16.75 ? 411  SER A OG  1 
ATOM   3290 N  N   . ASP A 1 412  ? 14.583 63.895  0.230   1.00 12.31 ? 412  ASP A N   1 
ATOM   3291 C  CA  . ASP A 1 412  ? 15.103 64.097  -1.116  1.00 11.09 ? 412  ASP A CA  1 
ATOM   3292 C  C   . ASP A 1 412  ? 16.450 64.845  -1.112  1.00 10.00 ? 412  ASP A C   1 
ATOM   3293 O  O   . ASP A 1 412  ? 16.825 65.425  -2.143  1.00 10.30 ? 412  ASP A O   1 
ATOM   3294 C  CB  . ASP A 1 412  ? 14.108 64.910  -1.959  1.00 12.12 ? 412  ASP A CB  1 
ATOM   3295 C  CG  . ASP A 1 412  ? 13.916 66.331  -1.441  1.00 11.56 ? 412  ASP A CG  1 
ATOM   3296 O  OD1 . ASP A 1 412  ? 14.387 66.673  -0.339  1.00 12.30 ? 412  ASP A OD1 1 
ATOM   3297 O  OD2 . ASP A 1 412  ? 13.268 67.186  -2.116  1.00 15.16 ? 412  ASP A OD2 1 
ATOM   3298 N  N   . ASN A 1 413  ? 17.148 64.813  0.018   1.00 10.01 ? 413  ASN A N   1 
ATOM   3299 C  CA  . ASN A 1 413  ? 18.420 65.557  0.161   1.00 9.37  ? 413  ASN A CA  1 
ATOM   3300 C  C   . ASN A 1 413  ? 19.580 64.686  -0.393  1.00 8.82  ? 413  ASN A C   1 
ATOM   3301 O  O   . ASN A 1 413  ? 20.258 63.997  0.370   1.00 9.43  ? 413  ASN A O   1 
ATOM   3302 C  CB  . ASN A 1 413  ? 18.671 65.873  1.624   1.00 10.73 ? 413  ASN A CB  1 
ATOM   3303 C  CG  . ASN A 1 413  ? 17.720 66.936  2.230   1.00 9.97  ? 413  ASN A CG  1 
ATOM   3304 O  OD1 . ASN A 1 413  ? 17.990 67.397  3.321   1.00 12.62 ? 413  ASN A OD1 1 
ATOM   3305 N  ND2 . ASN A 1 413  ? 16.637 67.327  1.519   1.00 11.03 ? 413  ASN A ND2 1 
ATOM   3306 N  N   . TYR A 1 414  ? 19.732 64.728  -1.707  1.00 8.46  ? 414  TYR A N   1 
ATOM   3307 C  CA  . TYR A 1 414  ? 20.810 64.047  -2.446  1.00 8.91  ? 414  TYR A CA  1 
ATOM   3308 C  C   . TYR A 1 414  ? 22.045 64.932  -2.504  1.00 8.87  ? 414  TYR A C   1 
ATOM   3309 O  O   . TYR A 1 414  ? 21.966 66.119  -2.837  1.00 8.44  ? 414  TYR A O   1 
ATOM   3310 C  CB  . TYR A 1 414  ? 20.351 63.705  -3.862  1.00 9.49  ? 414  TYR A CB  1 
ATOM   3311 C  CG  . TYR A 1 414  ? 19.345 62.550  -3.862  1.00 9.21  ? 414  TYR A CG  1 
ATOM   3312 C  CD1 . TYR A 1 414  ? 17.975 62.770  -3.632  1.00 10.27 ? 414  TYR A CD1 1 
ATOM   3313 C  CD2 . TYR A 1 414  ? 19.785 61.240  -4.033  1.00 9.68  ? 414  TYR A CD2 1 
ATOM   3314 C  CE1 . TYR A 1 414  ? 17.076 61.687  -3.591  1.00 10.09 ? 414  TYR A CE1 1 
ATOM   3315 C  CE2 . TYR A 1 414  ? 18.888 60.158  -4.004  1.00 10.04 ? 414  TYR A CE2 1 
ATOM   3316 C  CZ  . TYR A 1 414  ? 17.548 60.412  -3.785  1.00 10.24 ? 414  TYR A CZ  1 
ATOM   3317 O  OH  . TYR A 1 414  ? 16.682 59.311  -3.763  1.00 10.39 ? 414  TYR A OH  1 
ATOM   3318 N  N   . TRP A 1 415  ? 23.183 64.320  -2.199  1.00 8.77  ? 415  TRP A N   1 
ATOM   3319 C  CA  . TRP A 1 415  ? 24.429 65.052  -2.077  1.00 7.76  ? 415  TRP A CA  1 
ATOM   3320 C  C   . TRP A 1 415  ? 25.142 65.083  -3.423  1.00 9.00  ? 415  TRP A C   1 
ATOM   3321 O  O   . TRP A 1 415  ? 26.277 64.601  -3.561  1.00 10.33 ? 415  TRP A O   1 
ATOM   3322 C  CB  . TRP A 1 415  ? 25.292 64.370  -1.030  1.00 7.61  ? 415  TRP A CB  1 
ATOM   3323 C  CG  . TRP A 1 415  ? 24.746 64.415  0.368   1.00 7.82  ? 415  TRP A CG  1 
ATOM   3324 C  CD1 . TRP A 1 415  ? 23.421 64.172  0.796   1.00 8.37  ? 415  TRP A CD1 1 
ATOM   3325 C  CD2 . TRP A 1 415  ? 25.508 64.663  1.554   1.00 7.72  ? 415  TRP A CD2 1 
ATOM   3326 N  NE1 . TRP A 1 415  ? 23.376 64.285  2.161   1.00 9.17  ? 415  TRP A NE1 1 
ATOM   3327 C  CE2 . TRP A 1 415  ? 24.636 64.555  2.660   1.00 8.50  ? 415  TRP A CE2 1 
ATOM   3328 C  CE3 . TRP A 1 415  ? 26.877 64.943  1.802   1.00 8.73  ? 415  TRP A CE3 1 
ATOM   3329 C  CZ2 . TRP A 1 415  ? 25.066 64.746  3.974   1.00 9.32  ? 415  TRP A CZ2 1 
ATOM   3330 C  CZ3 . TRP A 1 415  ? 27.301 65.141  3.079   1.00 9.36  ? 415  TRP A CZ3 1 
ATOM   3331 C  CH2 . TRP A 1 415  ? 26.410 65.015  4.174   1.00 9.16  ? 415  TRP A CH2 1 
ATOM   3332 N  N   . SER A 1 416  ? 24.512 65.659  -4.434  1.00 7.60  ? 416  SER A N   1 
ATOM   3333 C  CA  . SER A 1 416  ? 25.149 65.780  -5.729  1.00 8.24  ? 416  SER A CA  1 
ATOM   3334 C  C   . SER A 1 416  ? 25.737 67.177  -5.944  1.00 7.29  ? 416  SER A C   1 
ATOM   3335 O  O   . SER A 1 416  ? 26.407 67.387  -6.941  1.00 7.85  ? 416  SER A O   1 
ATOM   3336 C  CB  . SER A 1 416  ? 24.211 65.363  -6.865  1.00 7.59  ? 416  SER A CB  1 
ATOM   3337 O  OG  . SER A 1 416  ? 22.916 65.929  -6.670  1.00 8.93  ? 416  SER A OG  1 
ATOM   3338 N  N   . GLY A 1 417  ? 25.532 68.103  -5.010  1.00 6.83  ? 417  GLY A N   1 
ATOM   3339 C  CA  . GLY A 1 417  ? 26.100 69.448  -5.169  1.00 8.01  ? 417  GLY A CA  1 
ATOM   3340 C  C   . GLY A 1 417  ? 27.625 69.422  -5.106  1.00 5.99  ? 417  GLY A C   1 
ATOM   3341 O  O   . GLY A 1 417  ? 28.283 70.141  -5.861  1.00 7.05  ? 417  GLY A O   1 
ATOM   3342 N  N   . TYR A 1 418  ? 28.185 68.596  -4.220  1.00 6.06  ? 418  TYR A N   1 
ATOM   3343 C  CA  . TYR A 1 418  ? 29.644 68.624  -4.040  1.00 5.91  ? 418  TYR A CA  1 
ATOM   3344 C  C   . TYR A 1 418  ? 30.386 67.988  -5.199  1.00 6.35  ? 418  TYR A C   1 
ATOM   3345 O  O   . TYR A 1 418  ? 31.635 68.038  -5.251  1.00 6.57  ? 418  TYR A O   1 
ATOM   3346 C  CB  . TYR A 1 418  ? 30.025 67.963  -2.728  1.00 6.56  ? 418  TYR A CB  1 
ATOM   3347 C  CG  . TYR A 1 418  ? 30.143 66.445  -2.775  1.00 6.95  ? 418  TYR A CG  1 
ATOM   3348 C  CD1 . TYR A 1 418  ? 29.025 65.620  -2.623  1.00 8.02  ? 418  TYR A CD1 1 
ATOM   3349 C  CD2 . TYR A 1 418  ? 31.383 65.838  -2.956  1.00 6.64  ? 418  TYR A CD2 1 
ATOM   3350 C  CE1 . TYR A 1 418  ? 29.142 64.217  -2.644  1.00 6.92  ? 418  TYR A CE1 1 
ATOM   3351 C  CE2 . TYR A 1 418  ? 31.524 64.466  -2.989  1.00 6.45  ? 418  TYR A CE2 1 
ATOM   3352 C  CZ  . TYR A 1 418  ? 30.396 63.669  -2.821  1.00 5.99  ? 418  TYR A CZ  1 
ATOM   3353 O  OH  . TYR A 1 418  ? 30.570 62.301  -2.824  1.00 7.34  ? 418  TYR A OH  1 
ATOM   3354 N  N   . TYR A 1 419  ? 29.673 67.416  -6.169  1.00 5.58  ? 419  TYR A N   1 
ATOM   3355 C  CA  . TYR A 1 419  ? 30.337 66.978  -7.393  1.00 5.66  ? 419  TYR A CA  1 
ATOM   3356 C  C   . TYR A 1 419  ? 30.867 68.192  -8.193  1.00 5.84  ? 419  TYR A C   1 
ATOM   3357 O  O   . TYR A 1 419  ? 31.698 68.027  -9.072  1.00 6.51  ? 419  TYR A O   1 
ATOM   3358 C  CB  . TYR A 1 419  ? 29.416 66.180  -8.297  1.00 6.43  ? 419  TYR A CB  1 
ATOM   3359 C  CG  . TYR A 1 419  ? 28.770 64.976  -7.666  1.00 5.16  ? 419  TYR A CG  1 
ATOM   3360 C  CD1 . TYR A 1 419  ? 29.345 64.298  -6.572  1.00 6.77  ? 419  TYR A CD1 1 
ATOM   3361 C  CD2 . TYR A 1 419  ? 27.589 64.445  -8.221  1.00 6.82  ? 419  TYR A CD2 1 
ATOM   3362 C  CE1 . TYR A 1 419  ? 28.760 63.145  -6.016  1.00 6.89  ? 419  TYR A CE1 1 
ATOM   3363 C  CE2 . TYR A 1 419  ? 26.986 63.331  -7.659  1.00 7.07  ? 419  TYR A CE2 1 
ATOM   3364 C  CZ  . TYR A 1 419  ? 27.590 62.683  -6.579  1.00 6.53  ? 419  TYR A CZ  1 
ATOM   3365 O  OH  . TYR A 1 419  ? 27.028 61.545  -6.025  1.00 7.13  ? 419  TYR A OH  1 
ATOM   3366 N  N   . THR A 1 420  ? 30.389 69.400  -7.851  1.00 6.01  ? 420  THR A N   1 
ATOM   3367 C  CA  . THR A 1 420  ? 30.775 70.629  -8.557  1.00 7.21  ? 420  THR A CA  1 
ATOM   3368 C  C   . THR A 1 420  ? 31.328 71.723  -7.660  1.00 7.11  ? 420  THR A C   1 
ATOM   3369 O  O   . THR A 1 420  ? 32.083 72.557  -8.153  1.00 7.74  ? 420  THR A O   1 
ATOM   3370 C  CB  . THR A 1 420  ? 29.533 71.138  -9.351  1.00 7.85  ? 420  THR A CB  1 
ATOM   3371 O  OG1 . THR A 1 420  ? 29.094 70.096  -10.233 1.00 8.35  ? 420  THR A OG1 1 
ATOM   3372 C  CG2 . THR A 1 420  ? 29.837 72.344  -10.232 1.00 8.94  ? 420  THR A CG2 1 
ATOM   3373 N  N   . SER A 1 421  ? 30.968 71.744  -6.385  1.00 6.46  ? 421  SER A N   1 
ATOM   3374 C  CA  . SER A 1 421  ? 31.330 72.873  -5.544  1.00 7.20  ? 421  SER A CA  1 
ATOM   3375 C  C   . SER A 1 421  ? 32.814 73.191  -5.589  1.00 7.59  ? 421  SER A C   1 
ATOM   3376 O  O   . SER A 1 421  ? 33.673 72.306  -5.521  1.00 6.92  ? 421  SER A O   1 
ATOM   3377 C  CB  . SER A 1 421  ? 30.961 72.568  -4.110  1.00 6.74  ? 421  SER A CB  1 
ATOM   3378 O  OG  . SER A 1 421  ? 29.544 72.405  -4.013  1.00 8.00  ? 421  SER A OG  1 
ATOM   3379 N  N   . ARG A 1 422  ? 33.111 74.489  -5.639  1.00 6.25  ? 422  ARG A N   1 
ATOM   3380 C  CA  . ARG A 1 422  ? 34.511 74.992  -5.694  1.00 6.80  ? 422  ARG A CA  1 
ATOM   3381 C  C   . ARG A 1 422  ? 35.262 74.370  -6.875  1.00 7.12  ? 422  ARG A C   1 
ATOM   3382 O  O   . ARG A 1 422  ? 36.278 73.663  -6.720  1.00 6.97  ? 422  ARG A O   1 
ATOM   3383 C  CB  . ARG A 1 422  ? 35.263 74.786  -4.370  1.00 7.53  ? 422  ARG A CB  1 
ATOM   3384 C  CG  . ARG A 1 422  ? 34.984 75.871  -3.293  1.00 8.58  ? 422  ARG A CG  1 
ATOM   3385 C  CD  . ARG A 1 422  ? 33.518 75.981  -2.829  1.00 9.08  ? 422  ARG A CD  1 
ATOM   3386 N  NE  . ARG A 1 422  ? 33.502 76.957  -1.733  1.00 9.15  ? 422  ARG A NE  1 
ATOM   3387 C  CZ  . ARG A 1 422  ? 33.626 76.665  -0.446  1.00 9.98  ? 422  ARG A CZ  1 
ATOM   3388 N  NH1 . ARG A 1 422  ? 33.573 75.420  -0.007  1.00 8.87  ? 422  ARG A NH1 1 
ATOM   3389 N  NH2 . ARG A 1 422  ? 33.770 77.665  0.432   1.00 9.87  ? 422  ARG A NH2 1 
ATOM   3390 N  N   . PRO A 1 423  ? 34.761 74.575  -8.079  1.00 6.80  ? 423  PRO A N   1 
ATOM   3391 C  CA  . PRO A 1 423  ? 35.345 73.920  -9.247  1.00 6.56  ? 423  PRO A CA  1 
ATOM   3392 C  C   . PRO A 1 423  ? 36.751 74.419  -9.593  1.00 6.57  ? 423  PRO A C   1 
ATOM   3393 O  O   . PRO A 1 423  ? 37.475 73.673  -10.265 1.00 7.00  ? 423  PRO A O   1 
ATOM   3394 C  CB  . PRO A 1 423  ? 34.320 74.220  -10.363 1.00 7.05  ? 423  PRO A CB  1 
ATOM   3395 C  CG  . PRO A 1 423  ? 33.758 75.539  -9.957  1.00 8.15  ? 423  PRO A CG  1 
ATOM   3396 C  CD  . PRO A 1 423  ? 33.600 75.421  -8.444  1.00 7.35  ? 423  PRO A CD  1 
ATOM   3397 N  N   . TYR A 1 424  ? 37.155 75.623  -9.167  1.00 7.09  ? 424  TYR A N   1 
ATOM   3398 C  CA  . TYR A 1 424  ? 38.522 76.061  -9.431  1.00 6.63  ? 424  TYR A CA  1 
ATOM   3399 C  C   . TYR A 1 424  ? 39.473 75.046  -8.822  1.00 6.13  ? 424  TYR A C   1 
ATOM   3400 O  O   . TYR A 1 424  ? 40.467 74.656  -9.456  1.00 6.62  ? 424  TYR A O   1 
ATOM   3401 C  CB  . TYR A 1 424  ? 38.744 77.436  -8.820  1.00 7.46  ? 424  TYR A CB  1 
ATOM   3402 C  CG  . TYR A 1 424  ? 40.134 77.991  -9.057  1.00 7.86  ? 424  TYR A CG  1 
ATOM   3403 C  CD1 . TYR A 1 424  ? 41.170 77.735  -8.161  1.00 8.55  ? 424  TYR A CD1 1 
ATOM   3404 C  CD2 . TYR A 1 424  ? 40.392 78.777  -10.183 1.00 10.12 ? 424  TYR A CD2 1 
ATOM   3405 C  CE1 . TYR A 1 424  ? 42.471 78.255  -8.417  1.00 10.47 ? 424  TYR A CE1 1 
ATOM   3406 C  CE2 . TYR A 1 424  ? 41.635 79.288  -10.414 1.00 11.46 ? 424  TYR A CE2 1 
ATOM   3407 C  CZ  . TYR A 1 424  ? 42.663 79.038  -9.542  1.00 9.63  ? 424  TYR A CZ  1 
ATOM   3408 O  OH  . TYR A 1 424  ? 43.911 79.589  -9.860  1.00 13.28 ? 424  TYR A OH  1 
ATOM   3409 N  N   . HIS A 1 425  ? 39.201 74.616  -7.591  1.00 6.28  ? 425  HIS A N   1 
ATOM   3410 C  CA  . HIS A 1 425  ? 40.144 73.727  -6.880  1.00 6.31  ? 425  HIS A CA  1 
ATOM   3411 C  C   . HIS A 1 425  ? 40.044 72.300  -7.350  1.00 6.72  ? 425  HIS A C   1 
ATOM   3412 O  O   . HIS A 1 425  ? 41.019 71.551  -7.322  1.00 6.32  ? 425  HIS A O   1 
ATOM   3413 C  CB  . HIS A 1 425  ? 39.920 73.870  -5.368  1.00 7.39  ? 425  HIS A CB  1 
ATOM   3414 C  CG  . HIS A 1 425  ? 40.004 75.294  -4.961  1.00 8.03  ? 425  HIS A CG  1 
ATOM   3415 N  ND1 . HIS A 1 425  ? 38.919 76.143  -5.022  1.00 9.30  ? 425  HIS A ND1 1 
ATOM   3416 C  CD2 . HIS A 1 425  ? 41.082 76.064  -4.668  1.00 9.15  ? 425  HIS A CD2 1 
ATOM   3417 C  CE1 . HIS A 1 425  ? 39.309 77.369  -4.707  1.00 9.41  ? 425  HIS A CE1 1 
ATOM   3418 N  NE2 . HIS A 1 425  ? 40.613 77.350  -4.482  1.00 9.73  ? 425  HIS A NE2 1 
ATOM   3419 N  N   . LYS A 1 426  ? 38.864 71.894  -7.821  1.00 6.36  ? 426  LYS A N   1 
ATOM   3420 C  CA  . LYS A 1 426  ? 38.717 70.601  -8.497  1.00 6.19  ? 426  LYS A CA  1 
ATOM   3421 C  C   . LYS A 1 426  ? 39.607 70.538  -9.729  1.00 6.23  ? 426  LYS A C   1 
ATOM   3422 O  O   . LYS A 1 426  ? 40.223 69.506  -10.012 1.00 6.41  ? 426  LYS A O   1 
ATOM   3423 C  CB  . LYS A 1 426  ? 37.238 70.382  -8.877  1.00 6.81  ? 426  LYS A CB  1 
ATOM   3424 C  CG  . LYS A 1 426  ? 36.344 69.983  -7.695  1.00 6.89  ? 426  LYS A CG  1 
ATOM   3425 C  CD  . LYS A 1 426  ? 34.850 70.035  -8.074  1.00 7.38  ? 426  LYS A CD  1 
ATOM   3426 C  CE  . LYS A 1 426  ? 33.971 69.171  -7.161  1.00 7.87  ? 426  LYS A CE  1 
ATOM   3427 N  NZ  . LYS A 1 426  ? 33.928 69.595  -5.726  1.00 7.32  ? 426  LYS A NZ  1 
ATOM   3428 N  N   . ARG A 1 427  ? 39.642 71.621  -10.507 1.00 6.08  ? 427  ARG A N   1 
ATOM   3429 C  CA  . ARG A 1 427  ? 40.494 71.647  -11.661 1.00 6.75  ? 427  ARG A CA  1 
ATOM   3430 C  C   . ARG A 1 427  ? 41.977 71.652  -11.242 1.00 6.94  ? 427  ARG A C   1 
ATOM   3431 O  O   . ARG A 1 427  ? 42.795 70.957  -11.816 1.00 5.68  ? 427  ARG A O   1 
ATOM   3432 C  CB  . ARG A 1 427  ? 40.137 72.870  -12.542 1.00 6.65  ? 427  ARG A CB  1 
ATOM   3433 C  CG  . ARG A 1 427  ? 41.103 73.108  -13.669 1.00 7.79  ? 427  ARG A CG  1 
ATOM   3434 C  CD  . ARG A 1 427  ? 41.182 72.026  -14.723 1.00 10.38 ? 427  ARG A CD  1 
ATOM   3435 N  NE  . ARG A 1 427  ? 42.219 72.402  -15.701 1.00 10.22 ? 427  ARG A NE  1 
ATOM   3436 C  CZ  . ARG A 1 427  ? 43.040 71.580  -16.266 1.00 10.16 ? 427  ARG A CZ  1 
ATOM   3437 N  NH1 . ARG A 1 427  ? 42.973 70.273  -16.067 1.00 10.92 ? 427  ARG A NH1 1 
ATOM   3438 N  NH2 . ARG A 1 427  ? 43.989 72.089  -17.079 1.00 11.30 ? 427  ARG A NH2 1 
ATOM   3439 N  N   . MET A 1 428  ? 42.296 72.455  -10.230 1.00 6.29  ? 428  MET A N   1 
ATOM   3440 C  CA  . MET A 1 428  ? 43.669 72.506  -9.728  1.00 6.48  ? 428  MET A CA  1 
ATOM   3441 C  C   . MET A 1 428  ? 44.173 71.126  -9.283  1.00 6.23  ? 428  MET A C   1 
ATOM   3442 O  O   . MET A 1 428  ? 45.334 70.776  -9.517  1.00 6.58  ? 428  MET A O   1 
ATOM   3443 C  CB  . MET A 1 428  ? 43.723 73.492  -8.574  1.00 7.57  ? 428  MET A CB  1 
ATOM   3444 C  CG  . MET A 1 428  ? 45.169 73.880  -8.180  1.00 7.57  ? 428  MET A CG  1 
ATOM   3445 S  SD  . MET A 1 428  ? 45.085 75.189  -6.905  1.00 9.25  ? 428  MET A SD  1 
ATOM   3446 C  CE  . MET A 1 428  ? 46.808 75.707  -6.844  1.00 9.77  ? 428  MET A CE  1 
ATOM   3447 N  N   . ASP A 1 429  ? 43.293 70.308  -8.688  1.00 6.50  ? 429  ASP A N   1 
ATOM   3448 C  CA  . ASP A 1 429  ? 43.636 68.947  -8.290  1.00 6.09  ? 429  ASP A CA  1 
ATOM   3449 C  C   . ASP A 1 429  ? 44.214 68.172  -9.468  1.00 6.30  ? 429  ASP A C   1 
ATOM   3450 O  O   . ASP A 1 429  ? 45.204 67.454  -9.328  1.00 6.30  ? 429  ASP A O   1 
ATOM   3451 C  CB  . ASP A 1 429  ? 42.373 68.240  -7.786  1.00 7.36  ? 429  ASP A CB  1 
ATOM   3452 C  CG  . ASP A 1 429  ? 42.634 66.789  -7.486  1.00 6.42  ? 429  ASP A CG  1 
ATOM   3453 O  OD1 . ASP A 1 429  ? 43.151 66.524  -6.355  1.00 7.80  ? 429  ASP A OD1 1 
ATOM   3454 O  OD2 . ASP A 1 429  ? 42.342 65.883  -8.300  1.00 7.24  ? 429  ASP A OD2 1 
ATOM   3455 N  N   . ARG A 1 430  ? 43.540 68.272  -10.625 1.00 5.86  ? 430  ARG A N   1 
ATOM   3456 C  CA  . ARG A 1 430  ? 43.981 67.489  -11.787 1.00 5.98  ? 430  ARG A CA  1 
ATOM   3457 C  C   . ARG A 1 430  ? 45.301 68.017  -12.364 1.00 5.72  ? 430  ARG A C   1 
ATOM   3458 O  O   . ARG A 1 430  ? 46.133 67.226  -12.837 1.00 6.76  ? 430  ARG A O   1 
ATOM   3459 C  CB  . ARG A 1 430  ? 42.899 67.508  -12.868 1.00 6.21  ? 430  ARG A CB  1 
ATOM   3460 C  CG  . ARG A 1 430  ? 41.656 66.763  -12.455 1.00 7.15  ? 430  ARG A CG  1 
ATOM   3461 C  CD  . ARG A 1 430  ? 41.911 65.317  -12.004 1.00 6.74  ? 430  ARG A CD  1 
ATOM   3462 N  NE  . ARG A 1 430  ? 40.656 64.549  -12.039 1.00 6.69  ? 430  ARG A NE  1 
ATOM   3463 C  CZ  . ARG A 1 430  ? 39.960 64.212  -10.971 1.00 6.20  ? 430  ARG A CZ  1 
ATOM   3464 N  NH1 . ARG A 1 430  ? 40.361 64.547  -9.751  1.00 6.65  ? 430  ARG A NH1 1 
ATOM   3465 N  NH2 . ARG A 1 430  ? 38.837 63.515  -11.097 1.00 6.63  ? 430  ARG A NH2 1 
ATOM   3466 N  N   . VAL A 1 431  ? 45.494 69.334  -12.311 1.00 5.82  ? 431  VAL A N   1 
ATOM   3467 C  CA  . VAL A 1 431  ? 46.775 69.916  -12.753 1.00 6.66  ? 431  VAL A CA  1 
ATOM   3468 C  C   . VAL A 1 431  ? 47.903 69.407  -11.849 1.00 6.84  ? 431  VAL A C   1 
ATOM   3469 O  O   . VAL A 1 431  ? 48.944 68.925  -12.326 1.00 6.75  ? 431  VAL A O   1 
ATOM   3470 C  CB  . VAL A 1 431  ? 46.654 71.439  -12.747 1.00 6.77  ? 431  VAL A CB  1 
ATOM   3471 C  CG1 . VAL A 1 431  ? 48.008 72.079  -13.061 1.00 8.62  ? 431  VAL A CG1 1 
ATOM   3472 C  CG2 . VAL A 1 431  ? 45.552 71.878  -13.765 1.00 7.94  ? 431  VAL A CG2 1 
ATOM   3473 N  N   . LEU A 1 432  ? 47.707 69.507  -10.543 1.00 6.07  ? 432  LEU A N   1 
ATOM   3474 C  CA  . LEU A 1 432  ? 48.752 69.085  -9.607  1.00 6.19  ? 432  LEU A CA  1 
ATOM   3475 C  C   . LEU A 1 432  ? 48.962 67.569  -9.699  1.00 5.91  ? 432  LEU A C   1 
ATOM   3476 O  O   . LEU A 1 432  ? 50.102 67.096  -9.596  1.00 6.68  ? 432  LEU A O   1 
ATOM   3477 C  CB  . LEU A 1 432  ? 48.427 69.553  -8.193  1.00 7.32  ? 432  LEU A CB  1 
ATOM   3478 C  CG  . LEU A 1 432  ? 49.402 69.169  -7.104  1.00 7.90  ? 432  LEU A CG  1 
ATOM   3479 C  CD1 . LEU A 1 432  ? 50.835 69.644  -7.382  1.00 7.47  ? 432  LEU A CD1 1 
ATOM   3480 C  CD2 . LEU A 1 432  ? 48.945 69.771  -5.785  1.00 7.78  ? 432  LEU A CD2 1 
ATOM   3481 N  N   . MET A 1 433  ? 47.894 66.792  -9.929  1.00 5.39  ? 433  MET A N   1 
ATOM   3482 C  CA  . MET A 1 433  ? 48.048 65.353  -10.122 1.00 6.14  ? 433  MET A CA  1 
ATOM   3483 C  C   . MET A 1 433  ? 49.104 65.048  -11.173 1.00 6.15  ? 433  MET A C   1 
ATOM   3484 O  O   . MET A 1 433  ? 49.987 64.194  -10.986 1.00 6.25  ? 433  MET A O   1 
ATOM   3485 C  CB  . MET A 1 433  ? 46.716 64.760  -10.605 1.00 6.57  ? 433  MET A CB  1 
ATOM   3486 C  CG  . MET A 1 433  ? 46.793 63.256  -10.871 1.00 7.03  ? 433  MET A CG  1 
ATOM   3487 S  SD  . MET A 1 433  ? 45.229 62.579  -11.531 1.00 9.43  ? 433  MET A SD  1 
ATOM   3488 C  CE  . MET A 1 433  ? 45.254 63.282  -13.184 1.00 10.95 ? 433  MET A CE  1 
ATOM   3489 N  N   . HIS A 1 434  ? 48.992 65.733  -12.305 1.00 5.90  ? 434  HIS A N   1 
ATOM   3490 C  CA  . HIS A 1 434  ? 49.907 65.504  -13.409 1.00 5.46  ? 434  HIS A CA  1 
ATOM   3491 C  C   . HIS A 1 434  ? 51.317 66.007  -13.099 1.00 5.98  ? 434  HIS A C   1 
ATOM   3492 O  O   . HIS A 1 434  ? 52.300 65.332  -13.440 1.00 6.91  ? 434  HIS A O   1 
ATOM   3493 C  CB  . HIS A 1 434  ? 49.356 66.203  -14.668 1.00 7.19  ? 434  HIS A CB  1 
ATOM   3494 C  CG  . HIS A 1 434  ? 50.368 66.235  -15.767 1.00 6.69  ? 434  HIS A CG  1 
ATOM   3495 N  ND1 . HIS A 1 434  ? 50.748 65.109  -16.466 1.00 7.95  ? 434  HIS A ND1 1 
ATOM   3496 C  CD2 . HIS A 1 434  ? 51.204 67.231  -16.146 1.00 8.05  ? 434  HIS A CD2 1 
ATOM   3497 C  CE1 . HIS A 1 434  ? 51.746 65.432  -17.283 1.00 8.71  ? 434  HIS A CE1 1 
ATOM   3498 N  NE2 . HIS A 1 434  ? 52.037 66.711  -17.116 1.00 9.13  ? 434  HIS A NE2 1 
ATOM   3499 N  N   A TYR A 1 435  ? 51.408 67.172  -12.466 0.50 6.76  ? 435  TYR A N   1 
ATOM   3500 N  N   B TYR A 1 435  ? 51.427 67.170  -12.478 0.50 5.63  ? 435  TYR A N   1 
ATOM   3501 C  CA  A TYR A 1 435  ? 52.693 67.748  -12.094 0.50 7.06  ? 435  TYR A CA  1 
ATOM   3502 C  CA  B TYR A 1 435  ? 52.750 67.687  -12.161 0.50 4.76  ? 435  TYR A CA  1 
ATOM   3503 C  C   A TYR A 1 435  ? 53.463 66.819  -11.163 0.50 7.23  ? 435  TYR A C   1 
ATOM   3504 C  C   B TYR A 1 435  ? 53.502 66.857  -11.113 0.50 5.78  ? 435  TYR A C   1 
ATOM   3505 O  O   A TYR A 1 435  ? 54.666 66.618  -11.330 0.50 7.25  ? 435  TYR A O   1 
ATOM   3506 O  O   B TYR A 1 435  ? 54.714 66.727  -11.177 0.50 5.52  ? 435  TYR A O   1 
ATOM   3507 C  CB  A TYR A 1 435  ? 52.496 69.112  -11.428 0.50 8.59  ? 435  TYR A CB  1 
ATOM   3508 C  CB  B TYR A 1 435  ? 52.698 69.176  -11.832 0.50 5.19  ? 435  TYR A CB  1 
ATOM   3509 C  CG  A TYR A 1 435  ? 52.394 70.261  -12.405 0.50 10.80 ? 435  TYR A CG  1 
ATOM   3510 C  CG  B TYR A 1 435  ? 52.571 70.029  -13.088 0.50 3.83  ? 435  TYR A CG  1 
ATOM   3511 C  CD1 A TYR A 1 435  ? 51.514 70.210  -13.478 0.50 10.43 ? 435  TYR A CD1 1 
ATOM   3512 C  CD1 B TYR A 1 435  ? 53.531 69.984  -14.100 0.50 6.01  ? 435  TYR A CD1 1 
ATOM   3513 C  CD2 A TYR A 1 435  ? 53.177 71.398  -12.255 0.50 12.81 ? 435  TYR A CD2 1 
ATOM   3514 C  CD2 B TYR A 1 435  ? 51.462 70.817  -13.296 0.50 4.13  ? 435  TYR A CD2 1 
ATOM   3515 C  CE1 A TYR A 1 435  ? 51.417 71.258  -14.374 0.50 11.93 ? 435  TYR A CE1 1 
ATOM   3516 C  CE1 B TYR A 1 435  ? 53.397 70.766  -15.260 0.50 8.46  ? 435  TYR A CE1 1 
ATOM   3517 C  CE2 A TYR A 1 435  ? 53.087 72.451  -13.145 0.50 14.73 ? 435  TYR A CE2 1 
ATOM   3518 C  CE2 B TYR A 1 435  ? 51.326 71.598  -14.430 0.50 6.33  ? 435  TYR A CE2 1 
ATOM   3519 C  CZ  A TYR A 1 435  ? 52.205 72.376  -14.202 0.50 12.98 ? 435  TYR A CZ  1 
ATOM   3520 C  CZ  B TYR A 1 435  ? 52.293 71.574  -15.413 0.50 6.54  ? 435  TYR A CZ  1 
ATOM   3521 O  OH  A TYR A 1 435  ? 52.112 73.422  -15.091 0.50 16.38 ? 435  TYR A OH  1 
ATOM   3522 O  OH  B TYR A 1 435  ? 52.166 72.341  -16.564 0.50 7.86  ? 435  TYR A OH  1 
ATOM   3523 N  N   . VAL A 1 436  ? 52.765 66.253  -10.184 1.00 5.92  ? 436  VAL A N   1 
ATOM   3524 C  CA  . VAL A 1 436  ? 53.399 65.318  -9.233  1.00 6.51  ? 436  VAL A CA  1 
ATOM   3525 C  C   . VAL A 1 436  ? 53.934 64.118  -10.031 1.00 6.71  ? 436  VAL A C   1 
ATOM   3526 O  O   . VAL A 1 436  ? 55.093 63.690  -9.850  1.00 6.48  ? 436  VAL A O   1 
ATOM   3527 C  CB  . VAL A 1 436  ? 52.422 64.897  -8.124  1.00 6.31  ? 436  VAL A CB  1 
ATOM   3528 C  CG1 . VAL A 1 436  ? 52.961 63.685  -7.339  1.00 7.53  ? 436  VAL A CG1 1 
ATOM   3529 C  CG2 . VAL A 1 436  ? 52.224 66.061  -7.173  1.00 7.28  ? 436  VAL A CG2 1 
ATOM   3530 N  N   . ARG A 1 437  ? 53.111 63.525  -10.888 1.00 5.84  ? 437  ARG A N   1 
ATOM   3531 C  CA  . ARG A 1 437  ? 53.578 62.381  -11.682 1.00 6.58  ? 437  ARG A CA  1 
ATOM   3532 C  C   . ARG A 1 437  ? 54.819 62.764  -12.495 1.00 7.10  ? 437  ARG A C   1 
ATOM   3533 O  O   . ARG A 1 437  ? 55.817 62.013  -12.542 1.00 6.79  ? 437  ARG A O   1 
ATOM   3534 C  CB  . ARG A 1 437  ? 52.482 61.924  -12.626 1.00 6.96  ? 437  ARG A CB  1 
ATOM   3535 C  CG  . ARG A 1 437  ? 52.957 60.918  -13.661 1.00 8.32  ? 437  ARG A CG  1 
ATOM   3536 C  CD  . ARG A 1 437  ? 51.829 60.442  -14.534 1.00 8.32  ? 437  ARG A CD  1 
ATOM   3537 N  NE  . ARG A 1 437  ? 52.355 59.701  -15.693 1.00 8.00  ? 437  ARG A NE  1 
ATOM   3538 C  CZ  . ARG A 1 437  ? 51.621 58.898  -16.442 1.00 8.38  ? 437  ARG A CZ  1 
ATOM   3539 N  NH1 . ARG A 1 437  ? 50.360 58.636  -16.128 1.00 9.11  ? 437  ARG A NH1 1 
ATOM   3540 N  NH2 . ARG A 1 437  ? 52.172 58.345  -17.511 1.00 8.69  ? 437  ARG A NH2 1 
ATOM   3541 N  N   . ALA A 1 438  ? 54.767 63.919  -13.176 1.00 6.19  ? 438  ALA A N   1 
ATOM   3542 C  CA  . ALA A 1 438  ? 55.862 64.310  -14.068 1.00 6.69  ? 438  ALA A CA  1 
ATOM   3543 C  C   . ALA A 1 438  ? 57.124 64.606  -13.250 1.00 6.80  ? 438  ALA A C   1 
ATOM   3544 O  O   . ALA A 1 438  ? 58.225 64.257  -13.699 1.00 7.56  ? 438  ALA A O   1 
ATOM   3545 C  CB  . ALA A 1 438  ? 55.443 65.494  -14.887 1.00 7.72  ? 438  ALA A CB  1 
ATOM   3546 N  N   . ALA A 1 439  ? 57.000 65.240  -12.085 1.00 7.50  ? 439  ALA A N   1 
ATOM   3547 C  CA  . ALA A 1 439  ? 58.173 65.564  -11.273 1.00 6.79  ? 439  ALA A CA  1 
ATOM   3548 C  C   . ALA A 1 439  ? 58.796 64.277  -10.742 1.00 7.04  ? 439  ALA A C   1 
ATOM   3549 O  O   . ALA A 1 439  ? 60.047 64.137  -10.729 1.00 7.62  ? 439  ALA A O   1 
ATOM   3550 C  CB  . ALA A 1 439  ? 57.807 66.491  -10.150 1.00 7.46  ? 439  ALA A CB  1 
ATOM   3551 N  N   . GLU A 1 440  ? 57.985 63.344  -10.264 1.00 6.62  ? 440  GLU A N   1 
ATOM   3552 C  CA  . GLU A 1 440  ? 58.533 62.109  -9.755  1.00 6.95  ? 440  GLU A CA  1 
ATOM   3553 C  C   . GLU A 1 440  ? 59.202 61.306  -10.866 1.00 7.23  ? 440  GLU A C   1 
ATOM   3554 O  O   . GLU A 1 440  ? 60.259 60.680  -10.662 1.00 7.94  ? 440  GLU A O   1 
ATOM   3555 C  CB  . GLU A 1 440  ? 57.450 61.261  -9.054  1.00 7.26  ? 440  GLU A CB  1 
ATOM   3556 C  CG  . GLU A 1 440  ? 56.910 61.907  -7.790  1.00 8.33  ? 440  GLU A CG  1 
ATOM   3557 C  CD  . GLU A 1 440  ? 56.243 60.923  -6.845  1.00 11.42 ? 440  GLU A CD  1 
ATOM   3558 O  OE1 . GLU A 1 440  ? 55.136 60.442  -7.123  1.00 11.28 ? 440  GLU A OE1 1 
ATOM   3559 O  OE2 . GLU A 1 440  ? 56.861 60.573  -5.822  1.00 11.41 ? 440  GLU A OE2 1 
ATOM   3560 N  N   . MET A 1 441  ? 58.580 61.275  -12.038 1.00 6.10  ? 441  MET A N   1 
ATOM   3561 C  CA  . MET A 1 441  ? 59.130 60.518  -13.145 1.00 6.99  ? 441  MET A CA  1 
ATOM   3562 C  C   . MET A 1 441  ? 60.430 61.138  -13.690 1.00 7.38  ? 441  MET A C   1 
ATOM   3563 O  O   . MET A 1 441  ? 61.459 60.437  -13.822 1.00 7.94  ? 441  MET A O   1 
ATOM   3564 C  CB  . MET A 1 441  ? 58.090 60.376  -14.267 1.00 7.17  ? 441  MET A CB  1 
ATOM   3565 C  CG  . MET A 1 441  ? 58.600 59.647  -15.498 1.00 7.31  ? 441  MET A CG  1 
ATOM   3566 S  SD  . MET A 1 441  ? 57.348 59.405  -16.772 1.00 8.40  ? 441  MET A SD  1 
ATOM   3567 C  CE  . MET A 1 441  ? 56.240 58.226  -15.961 1.00 10.43 ? 441  MET A CE  1 
ATOM   3568 N  N   . LEU A 1 442  ? 60.428 62.444  -13.959 1.00 6.99  ? 442  LEU A N   1 
ATOM   3569 C  CA  . LEU A 1 442  ? 61.614 63.102  -14.514 1.00 7.80  ? 442  LEU A CA  1 
ATOM   3570 C  C   . LEU A 1 442  ? 62.798 62.969  -13.583 1.00 8.25  ? 442  LEU A C   1 
ATOM   3571 O  O   . LEU A 1 442  ? 63.952 62.808  -14.055 1.00 9.42  ? 442  LEU A O   1 
ATOM   3572 C  CB  . LEU A 1 442  ? 61.326 64.575  -14.792 1.00 7.76  ? 442  LEU A CB  1 
ATOM   3573 C  CG  . LEU A 1 442  ? 60.715 64.829  -16.155 1.00 7.64  ? 442  LEU A CG  1 
ATOM   3574 C  CD1 . LEU A 1 442  ? 60.111 66.204  -16.180 1.00 9.90  ? 442  LEU A CD1 1 
ATOM   3575 C  CD2 . LEU A 1 442  ? 61.827 64.693  -17.212 1.00 9.47  ? 442  LEU A CD2 1 
ATOM   3576 N  N   . SER A 1 443  ? 62.569 63.072  -12.270 1.00 7.79  ? 443  SER A N   1 
ATOM   3577 C  CA  . SER A 1 443  ? 63.689 63.021  -11.327 1.00 8.57  ? 443  SER A CA  1 
ATOM   3578 C  C   . SER A 1 443  ? 64.086 61.604  -10.985 1.00 8.90  ? 443  SER A C   1 
ATOM   3579 O  O   . SER A 1 443  ? 65.200 61.406  -10.446 1.00 9.92  ? 443  SER A O   1 
ATOM   3580 C  CB  . SER A 1 443  ? 63.418 63.829  -10.081 1.00 8.48  ? 443  SER A CB  1 
ATOM   3581 O  OG  . SER A 1 443  ? 62.339 63.286  -9.320  1.00 7.96  ? 443  SER A OG  1 
ATOM   3582 N  N   . ALA A 1 444  ? 63.276 60.612  -11.316 1.00 7.46  ? 444  ALA A N   1 
ATOM   3583 C  CA  . ALA A 1 444  ? 63.573 59.201  -11.003 1.00 8.86  ? 444  ALA A CA  1 
ATOM   3584 C  C   . ALA A 1 444  ? 64.752 58.665  -11.777 1.00 9.40  ? 444  ALA A C   1 
ATOM   3585 O  O   . ALA A 1 444  ? 65.374 57.662  -11.357 1.00 10.52 ? 444  ALA A O   1 
ATOM   3586 C  CB  . ALA A 1 444  ? 62.379 58.304  -11.266 1.00 8.54  ? 444  ALA A CB  1 
ATOM   3587 N  N   . TRP A 1 445  ? 65.020 59.241  -12.944 1.00 10.06 ? 445  TRP A N   1 
ATOM   3588 C  CA  . TRP A 1 445  ? 66.062 58.713  -13.825 1.00 10.67 ? 445  TRP A CA  1 
ATOM   3589 C  C   . TRP A 1 445  ? 67.458 58.783  -13.187 1.00 11.30 ? 445  TRP A C   1 
ATOM   3590 O  O   . TRP A 1 445  ? 68.324 57.983  -13.578 1.00 12.92 ? 445  TRP A O   1 
ATOM   3591 C  CB  . TRP A 1 445  ? 66.075 59.446  -15.164 1.00 10.38 ? 445  TRP A CB  1 
ATOM   3592 C  CG  . TRP A 1 445  ? 64.801 59.274  -15.915 1.00 8.96  ? 445  TRP A CG  1 
ATOM   3593 C  CD1 . TRP A 1 445  ? 63.790 60.212  -16.039 1.00 9.58  ? 445  TRP A CD1 1 
ATOM   3594 C  CD2 . TRP A 1 445  ? 64.343 58.101  -16.585 1.00 9.27  ? 445  TRP A CD2 1 
ATOM   3595 N  NE1 . TRP A 1 445  ? 62.764 59.689  -16.787 1.00 9.38  ? 445  TRP A NE1 1 
ATOM   3596 C  CE2 . TRP A 1 445  ? 63.063 58.399  -17.130 1.00 8.61  ? 445  TRP A CE2 1 
ATOM   3597 C  CE3 . TRP A 1 445  ? 64.894 56.822  -16.817 1.00 10.54 ? 445  TRP A CE3 1 
ATOM   3598 C  CZ2 . TRP A 1 445  ? 62.349 57.487  -17.875 1.00 9.05  ? 445  TRP A CZ2 1 
ATOM   3599 C  CZ3 . TRP A 1 445  ? 64.165 55.922  -17.567 1.00 10.36 ? 445  TRP A CZ3 1 
ATOM   3600 C  CH2 . TRP A 1 445  ? 62.898 56.245  -18.072 1.00 10.28 ? 445  TRP A CH2 1 
ATOM   3601 N  N   . HIS A 1 446  ? 67.689 59.724  -12.279 1.00 11.14 ? 446  HIS A N   1 
ATOM   3602 C  CA  . HIS A 1 446  ? 68.980 59.837  -11.625 1.00 12.86 ? 446  HIS A CA  1 
ATOM   3603 C  C   . HIS A 1 446  ? 68.826 59.727  -10.121 1.00 12.14 ? 446  HIS A C   1 
ATOM   3604 O  O   . HIS A 1 446  ? 67.764 59.965  -9.551  1.00 11.50 ? 446  HIS A O   1 
ATOM   3605 C  CB  . HIS A 1 446  ? 69.576 61.206  -11.872 1.00 13.39 ? 446  HIS A CB  1 
ATOM   3606 C  CG  . HIS A 1 446  ? 69.964 61.460  -13.285 1.00 15.52 ? 446  HIS A CG  1 
ATOM   3607 N  ND1 . HIS A 1 446  ? 69.195 62.212  -14.150 1.00 17.79 ? 446  HIS A ND1 1 
ATOM   3608 C  CD2 . HIS A 1 446  ? 71.077 61.110  -13.977 1.00 20.40 ? 446  HIS A CD2 1 
ATOM   3609 C  CE1 . HIS A 1 446  ? 69.798 62.291  -15.320 1.00 21.47 ? 446  HIS A CE1 1 
ATOM   3610 N  NE2 . HIS A 1 446  ? 70.941 61.638  -15.243 1.00 20.01 ? 446  HIS A NE2 1 
ATOM   3611 N  N   . SER A 1 447  ? 69.951 59.406  -9.485  1.00 12.93 ? 447  SER A N   1 
ATOM   3612 C  CA  A SER A 1 447  ? 70.164 59.614  -8.076  0.50 12.62 ? 447  SER A CA  1 
ATOM   3613 C  CA  B SER A 1 447  ? 70.146 59.637  -8.056  0.50 13.07 ? 447  SER A CA  1 
ATOM   3614 C  C   . SER A 1 447  ? 70.598 61.072  -7.852  1.00 13.07 ? 447  SER A C   1 
ATOM   3615 O  O   . SER A 1 447  ? 71.407 61.606  -8.639  1.00 14.70 ? 447  SER A O   1 
ATOM   3616 C  CB  A SER A 1 447  ? 71.261 58.656  -7.633  0.50 14.34 ? 447  SER A CB  1 
ATOM   3617 C  CB  B SER A 1 447  ? 71.199 58.686  -7.479  0.50 14.87 ? 447  SER A CB  1 
ATOM   3618 O  OG  A SER A 1 447  ? 71.225 58.526  -6.241  0.50 12.74 ? 447  SER A OG  1 
ATOM   3619 O  OG  B SER A 1 447  ? 70.605 57.499  -7.001  0.50 15.64 ? 447  SER A OG  1 
ATOM   3620 N  N   . TRP A 1 448  ? 70.078 61.743  -6.831  1.00 10.96 ? 448  TRP A N   1 
ATOM   3621 C  CA  . TRP A 1 448  ? 70.405 63.127  -6.591  1.00 12.66 ? 448  TRP A CA  1 
ATOM   3622 C  C   . TRP A 1 448  ? 71.105 63.307  -5.275  1.00 14.30 ? 448  TRP A C   1 
ATOM   3623 O  O   . TRP A 1 448  ? 70.731 62.709  -4.285  1.00 15.04 ? 448  TRP A O   1 
ATOM   3624 C  CB  . TRP A 1 448  ? 69.133 63.997  -6.593  1.00 11.72 ? 448  TRP A CB  1 
ATOM   3625 C  CG  . TRP A 1 448  ? 68.477 64.025  -7.960  1.00 10.40 ? 448  TRP A CG  1 
ATOM   3626 C  CD1 . TRP A 1 448  ? 67.636 63.084  -8.481  1.00 11.30 ? 448  TRP A CD1 1 
ATOM   3627 C  CD2 . TRP A 1 448  ? 68.640 65.021  -8.966  1.00 10.42 ? 448  TRP A CD2 1 
ATOM   3628 N  NE1 . TRP A 1 448  ? 67.233 63.449  -9.744  1.00 10.82 ? 448  TRP A NE1 1 
ATOM   3629 C  CE2 . TRP A 1 448  ? 67.848 64.628  -10.070 1.00 9.89  ? 448  TRP A CE2 1 
ATOM   3630 C  CE3 . TRP A 1 448  ? 69.379 66.212  -9.046  1.00 11.73 ? 448  TRP A CE3 1 
ATOM   3631 C  CZ2 . TRP A 1 448  ? 67.755 65.382  -11.224 1.00 11.54 ? 448  TRP A CZ2 1 
ATOM   3632 C  CZ3 . TRP A 1 448  ? 69.282 66.973  -10.211 1.00 11.30 ? 448  TRP A CZ3 1 
ATOM   3633 C  CH2 . TRP A 1 448  ? 68.481 66.523  -11.292 1.00 10.93 ? 448  TRP A CH2 1 
ATOM   3634 N  N   . ASP A 1 449  ? 72.100 64.191  -5.262  1.00 16.66 ? 449  ASP A N   1 
ATOM   3635 C  CA  . ASP A 1 449  ? 72.716 64.636  -4.016  1.00 18.02 ? 449  ASP A CA  1 
ATOM   3636 C  C   . ASP A 1 449  ? 71.692 65.238  -3.074  1.00 17.69 ? 449  ASP A C   1 
ATOM   3637 O  O   . ASP A 1 449  ? 70.787 65.932  -3.526  1.00 16.78 ? 449  ASP A O   1 
ATOM   3638 C  CB  . ASP A 1 449  ? 73.764 65.706  -4.299  1.00 19.94 ? 449  ASP A CB  1 
ATOM   3639 C  CG  . ASP A 1 449  ? 74.608 66.004  -3.090  1.00 22.38 ? 449  ASP A CG  1 
ATOM   3640 O  OD1 . ASP A 1 449  ? 75.499 65.179  -2.780  1.00 31.09 ? 449  ASP A OD1 1 
ATOM   3641 O  OD2 . ASP A 1 449  ? 74.443 67.002  -2.374  1.00 26.48 ? 449  ASP A OD2 1 
ATOM   3642 N  N   . GLY A 1 450  ? 71.848 65.023  -1.768  1.00 17.88 ? 450  GLY A N   1 
ATOM   3643 C  CA  . GLY A 1 450  ? 70.982 65.661  -0.794  1.00 18.30 ? 450  GLY A CA  1 
ATOM   3644 C  C   . GLY A 1 450  ? 70.837 67.164  -0.937  1.00 18.94 ? 450  GLY A C   1 
ATOM   3645 O  O   . GLY A 1 450  ? 69.775 67.731  -0.644  1.00 19.26 ? 450  GLY A O   1 
ATOM   3646 N  N   . MET A 1 451  ? 71.904 67.831  -1.388  1.00 18.40 ? 451  MET A N   1 
ATOM   3647 C  CA  . MET A 1 451  ? 71.885 69.272  -1.532  1.00 19.30 ? 451  MET A CA  1 
ATOM   3648 C  C   . MET A 1 451  ? 70.902 69.746  -2.593  1.00 17.15 ? 451  MET A C   1 
ATOM   3649 O  O   . MET A 1 451  ? 70.523 70.916  -2.600  1.00 18.22 ? 451  MET A O   1 
ATOM   3650 C  CB  . MET A 1 451  ? 73.289 69.795  -1.881  1.00 20.88 ? 451  MET A CB  1 
ATOM   3651 C  CG  . MET A 1 451  ? 74.298 69.712  -0.735  1.00 26.34 ? 451  MET A CG  1 
ATOM   3652 S  SD  . MET A 1 451  ? 73.712 70.519  0.780   1.00 38.37 ? 451  MET A SD  1 
ATOM   3653 C  CE  . MET A 1 451  ? 73.582 72.262  0.215   1.00 37.37 ? 451  MET A CE  1 
ATOM   3654 N  N   . ALA A 1 452  ? 70.492 68.839  -3.487  1.00 15.54 ? 452  ALA A N   1 
ATOM   3655 C  CA  . ALA A 1 452  ? 69.555 69.195  -4.553  1.00 15.11 ? 452  ALA A CA  1 
ATOM   3656 C  C   . ALA A 1 452  ? 68.122 69.325  -4.013  1.00 14.15 ? 452  ALA A C   1 
ATOM   3657 O  O   . ALA A 1 452  ? 67.272 69.906  -4.699  1.00 14.95 ? 452  ALA A O   1 
ATOM   3658 C  CB  . ALA A 1 452  ? 69.613 68.183  -5.690  1.00 14.94 ? 452  ALA A CB  1 
ATOM   3659 N  N   . ARG A 1 453  ? 67.859 68.793  -2.813  1.00 13.40 ? 453  ARG A N   1 
ATOM   3660 C  CA  . ARG A 1 453  ? 66.535 68.950  -2.157  1.00 14.13 ? 453  ARG A CA  1 
ATOM   3661 C  C   . ARG A 1 453  ? 65.423 68.331  -3.013  1.00 13.13 ? 453  ARG A C   1 
ATOM   3662 O  O   . ARG A 1 453  ? 64.274 68.809  -2.947  1.00 14.41 ? 453  ARG A O   1 
ATOM   3663 C  CB  . ARG A 1 453  ? 66.249 70.422  -1.853  1.00 13.68 ? 453  ARG A CB  1 
ATOM   3664 C  CG  . ARG A 1 453  ? 67.289 71.056  -0.917  1.00 15.79 ? 453  ARG A CG  1 
ATOM   3665 C  CD  . ARG A 1 453  ? 67.075 72.552  -0.713  1.00 17.99 ? 453  ARG A CD  1 
ATOM   3666 N  NE  . ARG A 1 453  ? 65.886 72.808  0.097   1.00 21.58 ? 453  ARG A NE  1 
ATOM   3667 C  CZ  . ARG A 1 453  ? 65.382 74.014  0.315   1.00 23.37 ? 453  ARG A CZ  1 
ATOM   3668 N  NH1 . ARG A 1 453  ? 65.951 75.101  -0.226  1.00 24.90 ? 453  ARG A NH1 1 
ATOM   3669 N  NH2 . ARG A 1 453  ? 64.293 74.133  1.058   1.00 25.62 ? 453  ARG A NH2 1 
ATOM   3670 N  N   . ILE A 1 454  ? 65.743 67.305  -3.795  1.00 11.57 ? 454  ILE A N   1 
ATOM   3671 C  CA  . ILE A 1 454  ? 64.723 66.702  -4.662  1.00 11.20 ? 454  ILE A CA  1 
ATOM   3672 C  C   . ILE A 1 454  ? 63.710 65.947  -3.796  1.00 11.22 ? 454  ILE A C   1 
ATOM   3673 O  O   . ILE A 1 454  ? 62.497 66.169  -3.935  1.00 10.47 ? 454  ILE A O   1 
ATOM   3674 C  CB  . ILE A 1 454  ? 65.388 65.748  -5.655  1.00 10.83 ? 454  ILE A CB  1 
ATOM   3675 C  CG1 . ILE A 1 454  ? 66.324 66.518  -6.608  1.00 13.28 ? 454  ILE A CG1 1 
ATOM   3676 C  CG2 . ILE A 1 454  ? 64.351 64.924  -6.436  1.00 11.43 ? 454  ILE A CG2 1 
ATOM   3677 C  CD1 . ILE A 1 454  ? 65.682 67.585  -7.477  1.00 14.18 ? 454  ILE A CD1 1 
ATOM   3678 N  N   . GLU A 1 455  ? 64.165 65.078  -2.906  1.00 10.81 ? 455  GLU A N   1 
ATOM   3679 C  CA  . GLU A 1 455  ? 63.242 64.296  -2.073  1.00 11.32 ? 455  GLU A CA  1 
ATOM   3680 C  C   . GLU A 1 455  ? 62.410 65.219  -1.211  1.00 11.87 ? 455  GLU A C   1 
ATOM   3681 O  O   . GLU A 1 455  ? 61.214 64.973  -1.028  1.00 11.26 ? 455  GLU A O   1 
ATOM   3682 C  CB  . GLU A 1 455  ? 64.021 63.325  -1.176  1.00 13.24 ? 455  GLU A CB  1 
ATOM   3683 C  CG  . GLU A 1 455  ? 64.626 62.134  -1.916  1.00 13.86 ? 455  GLU A CG  1 
ATOM   3684 C  CD  . GLU A 1 455  ? 66.019 62.405  -2.534  1.00 13.62 ? 455  GLU A CD  1 
ATOM   3685 O  OE1 . GLU A 1 455  ? 66.508 63.563  -2.416  1.00 15.16 ? 455  GLU A OE1 1 
ATOM   3686 O  OE2 . GLU A 1 455  ? 66.563 61.451  -3.102  1.00 14.12 ? 455  GLU A OE2 1 
ATOM   3687 N  N   . GLU A 1 456  ? 62.990 66.280  -0.694  1.00 12.30 ? 456  GLU A N   1 
ATOM   3688 C  CA  . GLU A 1 456  ? 62.279 67.232  0.122   1.00 11.91 ? 456  GLU A CA  1 
ATOM   3689 C  C   . GLU A 1 456  ? 61.106 67.862  -0.655  1.00 11.09 ? 456  GLU A C   1 
ATOM   3690 O  O   . GLU A 1 456  ? 59.970 67.931  -0.160  1.00 10.57 ? 456  GLU A O   1 
ATOM   3691 C  CB  . GLU A 1 456  ? 63.257 68.329  0.593   1.00 13.30 ? 456  GLU A CB  1 
ATOM   3692 C  CG  . GLU A 1 456  ? 62.619 69.455  1.370   1.00 16.04 ? 456  GLU A CG  1 
ATOM   3693 C  CD  . GLU A 1 456  ? 63.560 70.636  1.602   1.00 17.48 ? 456  GLU A CD  1 
ATOM   3694 O  OE1 . GLU A 1 456  ? 64.789 70.496  1.421   1.00 22.39 ? 456  GLU A OE1 1 
ATOM   3695 O  OE2 . GLU A 1 456  ? 63.064 71.722  1.970   1.00 21.94 ? 456  GLU A OE2 1 
ATOM   3696 N  N   . ARG A 1 457  ? 61.389 68.380  -1.841  1.00 9.91  ? 457  ARG A N   1 
ATOM   3697 C  CA  . ARG A 1 457  ? 60.349 69.024  -2.667  1.00 9.72  ? 457  ARG A CA  1 
ATOM   3698 C  C   . ARG A 1 457  ? 59.269 68.032  -3.094  1.00 8.81  ? 457  ARG A C   1 
ATOM   3699 O  O   . ARG A 1 457  ? 58.078 68.364  -3.056  1.00 8.82  ? 457  ARG A O   1 
ATOM   3700 C  CB  . ARG A 1 457  ? 60.986 69.763  -3.864  1.00 10.09 ? 457  ARG A CB  1 
ATOM   3701 C  CG  . ARG A 1 457  ? 61.305 71.223  -3.624  1.00 13.56 ? 457  ARG A CG  1 
ATOM   3702 C  CD  . ARG A 1 457  ? 62.287 71.465  -2.496  1.00 14.50 ? 457  ARG A CD  1 
ATOM   3703 N  NE  . ARG A 1 457  ? 62.496 72.893  -2.198  1.00 16.23 ? 457  ARG A NE  1 
ATOM   3704 C  CZ  . ARG A 1 457  ? 63.392 73.667  -2.806  1.00 20.48 ? 457  ARG A CZ  1 
ATOM   3705 N  NH1 . ARG A 1 457  ? 64.178 73.186  -3.780  1.00 18.58 ? 457  ARG A NH1 1 
ATOM   3706 N  NH2 . ARG A 1 457  ? 63.489 74.940  -2.442  1.00 22.51 ? 457  ARG A NH2 1 
ATOM   3707 N  N   . LEU A 1 458  ? 59.655 66.815  -3.413  1.00 7.78  ? 458  LEU A N   1 
ATOM   3708 C  CA  . LEU A 1 458  ? 58.655 65.823  -3.864  1.00 8.35  ? 458  LEU A CA  1 
ATOM   3709 C  C   . LEU A 1 458  ? 57.789 65.373  -2.704  1.00 9.04  ? 458  LEU A C   1 
ATOM   3710 O  O   . LEU A 1 458  ? 56.568 65.167  -2.875  1.00 9.21  ? 458  LEU A O   1 
ATOM   3711 C  CB  . LEU A 1 458  ? 59.380 64.630  -4.459  1.00 8.72  ? 458  LEU A CB  1 
ATOM   3712 C  CG  . LEU A 1 458  ? 60.033 64.923  -5.823  1.00 8.55  ? 458  LEU A CG  1 
ATOM   3713 C  CD1 . LEU A 1 458  ? 60.791 63.702  -6.231  1.00 11.19 ? 458  LEU A CD1 1 
ATOM   3714 C  CD2 . LEU A 1 458  ? 58.979 65.309  -6.890  1.00 9.99  ? 458  LEU A CD2 1 
ATOM   3715 N  N   . GLU A 1 459  ? 58.370 65.261  -1.504  1.00 8.71  ? 459  GLU A N   1 
ATOM   3716 C  CA  . GLU A 1 459  ? 57.545 64.870  -0.346  1.00 9.49  ? 459  GLU A CA  1 
ATOM   3717 C  C   . GLU A 1 459  ? 56.539 65.965  -0.043  1.00 9.45  ? 459  GLU A C   1 
ATOM   3718 O  O   . GLU A 1 459  ? 55.353 65.698  0.235   1.00 9.06  ? 459  GLU A O   1 
ATOM   3719 C  CB  . GLU A 1 459  ? 58.438 64.638  0.860   1.00 10.14 ? 459  GLU A CB  1 
ATOM   3720 C  CG  . GLU A 1 459  ? 57.661 64.263  2.111   1.00 12.56 ? 459  GLU A CG  1 
ATOM   3721 C  CD  . GLU A 1 459  ? 58.561 63.628  3.172   1.00 17.35 ? 459  GLU A CD  1 
ATOM   3722 O  OE1 . GLU A 1 459  ? 59.212 64.401  3.894   1.00 22.08 ? 459  GLU A OE1 1 
ATOM   3723 O  OE2 . GLU A 1 459  ? 58.633 62.381  3.266   1.00 19.63 ? 459  GLU A OE2 1 
ATOM   3724 N  N   . GLN A 1 460  ? 56.951 67.218  -0.117  1.00 8.75  ? 460  GLN A N   1 
ATOM   3725 C  CA  . GLN A 1 460  ? 56.020 68.345  0.101   1.00 10.56 ? 460  GLN A CA  1 
ATOM   3726 C  C   . GLN A 1 460  ? 54.880 68.267  -0.936  1.00 9.38  ? 460  GLN A C   1 
ATOM   3727 O  O   . GLN A 1 460  ? 53.687 68.361  -0.594  1.00 9.45  ? 460  GLN A O   1 
ATOM   3728 C  CB  . GLN A 1 460  ? 56.751 69.691  -0.025  1.00 11.85 ? 460  GLN A CB  1 
ATOM   3729 C  CG  . GLN A 1 460  ? 55.864 70.932  0.020   1.00 16.92 ? 460  GLN A CG  1 
ATOM   3730 C  CD  . GLN A 1 460  ? 56.661 72.215  -0.258  1.00 16.79 ? 460  GLN A CD  1 
ATOM   3731 O  OE1 . GLN A 1 460  ? 57.731 72.164  -0.879  1.00 25.27 ? 460  GLN A OE1 1 
ATOM   3732 N  NE2 . GLN A 1 460  ? 56.117 73.343  0.141   1.00 24.45 ? 460  GLN A NE2 1 
ATOM   3733 N  N   . ALA A 1 461  ? 55.234 68.098  -2.208  1.00 7.96  ? 461  ALA A N   1 
ATOM   3734 C  CA  . ALA A 1 461  ? 54.209 68.084  -3.247  1.00 8.03  ? 461  ALA A CA  1 
ATOM   3735 C  C   . ALA A 1 461  ? 53.254 66.903  -3.061  1.00 7.97  ? 461  ALA A C   1 
ATOM   3736 O  O   . ALA A 1 461  ? 52.031 67.076  -3.157  1.00 8.29  ? 461  ALA A O   1 
ATOM   3737 C  CB  . ALA A 1 461  ? 54.880 68.043  -4.613  1.00 8.82  ? 461  ALA A CB  1 
ATOM   3738 N  N   . ARG A 1 462  ? 53.776 65.726  -2.765  1.00 7.62  ? 462  ARG A N   1 
ATOM   3739 C  CA  . ARG A 1 462  ? 52.904 64.572  -2.570  1.00 7.15  ? 462  ARG A CA  1 
ATOM   3740 C  C   . ARG A 1 462  ? 51.966 64.809  -1.390  1.00 7.37  ? 462  ARG A C   1 
ATOM   3741 O  O   . ARG A 1 462  ? 50.775 64.423  -1.425  1.00 7.72  ? 462  ARG A O   1 
ATOM   3742 C  CB  . ARG A 1 462  ? 53.665 63.285  -2.305  1.00 7.65  ? 462  ARG A CB  1 
ATOM   3743 C  CG  . ARG A 1 462  ? 54.392 62.692  -3.519  1.00 7.70  ? 462  ARG A CG  1 
ATOM   3744 C  CD  . ARG A 1 462  ? 54.885 61.278  -3.269  1.00 8.54  ? 462  ARG A CD  1 
ATOM   3745 N  NE  . ARG A 1 462  ? 55.791 61.230  -2.109  1.00 9.10  ? 462  ARG A NE  1 
ATOM   3746 C  CZ  . ARG A 1 462  ? 57.104 61.405  -2.183  1.00 10.14 ? 462  ARG A CZ  1 
ATOM   3747 N  NH1 . ARG A 1 462  ? 57.713 61.541  -3.356  1.00 11.41 ? 462  ARG A NH1 1 
ATOM   3748 N  NH2 . ARG A 1 462  ? 57.842 61.395  -1.076  1.00 12.48 ? 462  ARG A NH2 1 
ATOM   3749 N  N   . ARG A 1 463  ? 52.482 65.425  -0.326  1.00 7.39  ? 463  ARG A N   1 
ATOM   3750 C  CA  . ARG A 1 463  ? 51.670 65.562  0.877   1.00 6.94  ? 463  ARG A CA  1 
ATOM   3751 C  C   . ARG A 1 463  ? 50.603 66.634  0.714   1.00 7.54  ? 463  ARG A C   1 
ATOM   3752 O  O   . ARG A 1 463  ? 49.502 66.463  1.274   1.00 8.26  ? 463  ARG A O   1 
ATOM   3753 C  CB  . ARG A 1 463  ? 52.552 65.852  2.107   1.00 7.33  ? 463  ARG A CB  1 
ATOM   3754 C  CG  . ARG A 1 463  ? 53.278 64.628  2.521   1.00 8.45  ? 463  ARG A CG  1 
ATOM   3755 C  CD  . ARG A 1 463  ? 54.307 64.809  3.639   1.00 10.40 ? 463  ARG A CD  1 
ATOM   3756 N  NE  . ARG A 1 463  ? 54.797 63.479  3.971   1.00 11.76 ? 463  ARG A NE  1 
ATOM   3757 C  CZ  . ARG A 1 463  ? 55.537 63.179  5.041   1.00 15.11 ? 463  ARG A CZ  1 
ATOM   3758 N  NH1 . ARG A 1 463  ? 55.933 64.140  5.839   1.00 15.31 ? 463  ARG A NH1 1 
ATOM   3759 N  NH2 . ARG A 1 463  ? 55.906 61.925  5.257   1.00 15.03 ? 463  ARG A NH2 1 
ATOM   3760 N  N   . GLU A 1 464  ? 50.860 67.720  -0.006  1.00 7.43  ? 464  GLU A N   1 
ATOM   3761 C  CA  . GLU A 1 464  ? 49.832 68.726  -0.180  1.00 8.14  ? 464  GLU A CA  1 
ATOM   3762 C  C   . GLU A 1 464  ? 48.745 68.197  -1.106  1.00 8.49  ? 464  GLU A C   1 
ATOM   3763 O  O   . GLU A 1 464  ? 47.564 68.455  -0.857  1.00 8.12  ? 464  GLU A O   1 
ATOM   3764 C  CB  . GLU A 1 464  ? 50.385 70.028  -0.736  1.00 9.82  ? 464  GLU A CB  1 
ATOM   3765 C  CG  . GLU A 1 464  ? 51.547 70.677  0.047   1.00 12.73 ? 464  GLU A CG  1 
ATOM   3766 C  CD  . GLU A 1 464  ? 51.265 71.132  1.467   1.00 19.33 ? 464  GLU A CD  1 
ATOM   3767 O  OE1 . GLU A 1 464  ? 50.270 70.743  2.077   1.00 17.17 ? 464  GLU A OE1 1 
ATOM   3768 O  OE2 . GLU A 1 464  ? 52.121 71.905  1.974   1.00 22.11 ? 464  GLU A OE2 1 
ATOM   3769 N  N   . LEU A 1 465  ? 49.110 67.475  -2.159  1.00 6.51  ? 465  LEU A N   1 
ATOM   3770 C  CA  . LEU A 1 465  ? 48.073 66.909  -3.041  1.00 7.04  ? 465  LEU A CA  1 
ATOM   3771 C  C   . LEU A 1 465  ? 47.294 65.836  -2.266  1.00 6.51  ? 465  LEU A C   1 
ATOM   3772 O  O   . LEU A 1 465  ? 46.063 65.732  -2.374  1.00 6.90  ? 465  LEU A O   1 
ATOM   3773 C  CB  . LEU A 1 465  ? 48.719 66.302  -4.291  1.00 7.40  ? 465  LEU A CB  1 
ATOM   3774 C  CG  . LEU A 1 465  ? 47.726 65.651  -5.272  1.00 7.64  ? 465  LEU A CG  1 
ATOM   3775 C  CD1 . LEU A 1 465  ? 46.639 66.610  -5.760  1.00 8.38  ? 465  LEU A CD1 1 
ATOM   3776 C  CD2 . LEU A 1 465  ? 48.542 65.101  -6.430  1.00 8.55  ? 465  LEU A CD2 1 
ATOM   3777 N  N   . SER A 1 466  ? 47.988 65.033  -1.481  1.00 6.22  ? 466  SER A N   1 
ATOM   3778 C  CA  . SER A 1 466  ? 47.329 64.023  -0.666  1.00 6.07  ? 466  SER A CA  1 
ATOM   3779 C  C   . SER A 1 466  ? 46.332 64.612  0.322   1.00 6.54  ? 466  SER A C   1 
ATOM   3780 O  O   . SER A 1 466  ? 45.199 64.099  0.464   1.00 6.79  ? 466  SER A O   1 
ATOM   3781 C  CB  . SER A 1 466  ? 48.355 63.161  0.082   1.00 6.40  ? 466  SER A CB  1 
ATOM   3782 O  OG  . SER A 1 466  ? 49.089 62.343  -0.778  1.00 7.12  ? 466  SER A OG  1 
ATOM   3783 N  N   . LEU A 1 467  ? 46.700 65.701  0.961   1.00 6.08  ? 467  LEU A N   1 
ATOM   3784 C  CA  . LEU A 1 467  ? 45.836 66.348  1.926   1.00 6.83  ? 467  LEU A CA  1 
ATOM   3785 C  C   . LEU A 1 467  ? 44.538 66.764  1.228   1.00 6.19  ? 467  LEU A C   1 
ATOM   3786 O  O   . LEU A 1 467  ? 43.446 66.650  1.785   1.00 6.63  ? 467  LEU A O   1 
ATOM   3787 C  CB  . LEU A 1 467  ? 46.568 67.567  2.508   1.00 7.85  ? 467  LEU A CB  1 
ATOM   3788 C  CG  . LEU A 1 467  ? 45.805 68.210  3.654   1.00 10.67 ? 467  LEU A CG  1 
ATOM   3789 C  CD1 . LEU A 1 467  ? 45.968 67.337  4.933   1.00 15.54 ? 467  LEU A CD1 1 
ATOM   3790 C  CD2 . LEU A 1 467  ? 46.360 69.644  3.873   1.00 12.06 ? 467  LEU A CD2 1 
ATOM   3791 N  N   . PHE A 1 468  ? 44.650 67.281  0.014   1.00 5.96  ? 468  PHE A N   1 
ATOM   3792 C  CA  . PHE A 1 468  ? 43.464 67.803  -0.668  1.00 6.12  ? 468  PHE A CA  1 
ATOM   3793 C  C   . PHE A 1 468  ? 42.486 66.704  -1.084  1.00 5.50  ? 468  PHE A C   1 
ATOM   3794 O  O   . PHE A 1 468  ? 41.319 67.000  -1.397  1.00 6.43  ? 468  PHE A O   1 
ATOM   3795 C  CB  . PHE A 1 468  ? 43.895 68.622  -1.890  1.00 6.79  ? 468  PHE A CB  1 
ATOM   3796 C  CG  . PHE A 1 468  ? 42.783 69.450  -2.471  1.00 5.33  ? 468  PHE A CG  1 
ATOM   3797 C  CD1 . PHE A 1 468  ? 42.154 70.390  -1.703  1.00 7.24  ? 468  PHE A CD1 1 
ATOM   3798 C  CD2 . PHE A 1 468  ? 42.349 69.259  -3.804  1.00 6.73  ? 468  PHE A CD2 1 
ATOM   3799 C  CE1 . PHE A 1 468  ? 41.089 71.131  -2.215  1.00 7.36  ? 468  PHE A CE1 1 
ATOM   3800 C  CE2 . PHE A 1 468  ? 41.265 70.019  -4.309  1.00 5.78  ? 468  PHE A CE2 1 
ATOM   3801 C  CZ  . PHE A 1 468  ? 40.662 70.941  -3.513  1.00 6.90  ? 468  PHE A CZ  1 
ATOM   3802 N  N   . GLN A 1 469  ? 42.916 65.448  -1.076  1.00 5.13  ? 469  GLN A N   1 
ATOM   3803 C  CA  . GLN A 1 469  ? 41.967 64.370  -1.328  1.00 5.23  ? 469  GLN A CA  1 
ATOM   3804 C  C   . GLN A 1 469  ? 40.941 64.194  -0.212  1.00 5.95  ? 469  GLN A C   1 
ATOM   3805 O  O   . GLN A 1 469  ? 39.981 63.431  -0.368  1.00 5.90  ? 469  GLN A O   1 
ATOM   3806 C  CB  . GLN A 1 469  ? 42.686 63.034  -1.537  1.00 5.36  ? 469  GLN A CB  1 
ATOM   3807 C  CG  . GLN A 1 469  ? 43.780 63.115  -2.618  1.00 5.79  ? 469  GLN A CG  1 
ATOM   3808 C  CD  . GLN A 1 469  ? 43.275 63.734  -3.887  1.00 5.97  ? 469  GLN A CD  1 
ATOM   3809 O  OE1 . GLN A 1 469  ? 42.279 63.281  -4.464  1.00 6.99  ? 469  GLN A OE1 1 
ATOM   3810 N  NE2 . GLN A 1 469  ? 43.930 64.806  -4.312  1.00 6.91  ? 469  GLN A NE2 1 
ATOM   3811 N  N   . HIS A 1 470  ? 41.156 64.845  0.925   1.00 5.57  ? 470  HIS A N   1 
ATOM   3812 C  CA  . HIS A 1 470  ? 40.226 64.781  2.025   1.00 5.75  ? 470  HIS A CA  1 
ATOM   3813 C  C   . HIS A 1 470  ? 38.795 65.030  1.558   1.00 5.92  ? 470  HIS A C   1 
ATOM   3814 O  O   . HIS A 1 470  ? 38.553 65.802  0.627   1.00 6.43  ? 470  HIS A O   1 
ATOM   3815 C  CB  . HIS A 1 470  ? 40.658 65.834  3.073   1.00 6.67  ? 470  HIS A CB  1 
ATOM   3816 C  CG  . HIS A 1 470  ? 39.669 66.050  4.169   1.00 6.40  ? 470  HIS A CG  1 
ATOM   3817 N  ND1 . HIS A 1 470  ? 39.065 65.004  4.851   1.00 8.06  ? 470  HIS A ND1 1 
ATOM   3818 C  CD2 . HIS A 1 470  ? 39.170 67.200  4.682   1.00 6.81  ? 470  HIS A CD2 1 
ATOM   3819 C  CE1 . HIS A 1 470  ? 38.233 65.520  5.738   1.00 8.26  ? 470  HIS A CE1 1 
ATOM   3820 N  NE2 . HIS A 1 470  ? 38.277 66.839  5.662   1.00 7.74  ? 470  HIS A NE2 1 
ATOM   3821 N  N   . HIS A 1 471  ? 37.830 64.403  2.247   1.00 6.04  ? 471  HIS A N   1 
ATOM   3822 C  CA  . HIS A 1 471  ? 36.410 64.557  1.913   1.00 6.64  ? 471  HIS A CA  1 
ATOM   3823 C  C   . HIS A 1 471  ? 35.805 65.926  2.250   1.00 6.92  ? 471  HIS A C   1 
ATOM   3824 O  O   . HIS A 1 471  ? 34.605 66.108  1.988   1.00 7.91  ? 471  HIS A O   1 
ATOM   3825 C  CB  . HIS A 1 471  ? 35.598 63.401  2.518   1.00 6.42  ? 471  HIS A CB  1 
ATOM   3826 C  CG  . HIS A 1 471  ? 35.664 63.342  4.019   1.00 5.77  ? 471  HIS A CG  1 
ATOM   3827 N  ND1 . HIS A 1 471  ? 36.600 62.587  4.703   1.00 6.73  ? 471  HIS A ND1 1 
ATOM   3828 C  CD2 . HIS A 1 471  ? 34.903 63.962  4.970   1.00 5.91  ? 471  HIS A CD2 1 
ATOM   3829 C  CE1 . HIS A 1 471  ? 36.413 62.751  6.010   1.00 6.72  ? 471  HIS A CE1 1 
ATOM   3830 N  NE2 . HIS A 1 471  ? 35.406 63.593  6.198   1.00 6.64  ? 471  HIS A NE2 1 
ATOM   3831 N  N   . ASP A 1 472  ? 36.602 66.884  2.744   1.00 6.97  ? 472  ASP A N   1 
ATOM   3832 C  CA  . ASP A 1 472  ? 36.198 68.299  2.700   1.00 7.46  ? 472  ASP A CA  1 
ATOM   3833 C  C   . ASP A 1 472  ? 37.155 69.154  1.867   1.00 7.80  ? 472  ASP A C   1 
ATOM   3834 O  O   . ASP A 1 472  ? 37.016 70.384  1.896   1.00 8.20  ? 472  ASP A O   1 
ATOM   3835 C  CB  . ASP A 1 472  ? 36.050 68.920  4.112   1.00 8.07  ? 472  ASP A CB  1 
ATOM   3836 C  CG  . ASP A 1 472  ? 35.022 68.185  4.957   1.00 7.24  ? 472  ASP A CG  1 
ATOM   3837 O  OD1 . ASP A 1 472  ? 33.845 68.130  4.503   1.00 8.20  ? 472  ASP A OD1 1 
ATOM   3838 O  OD2 . ASP A 1 472  ? 35.364 67.637  6.007   1.00 8.41  ? 472  ASP A OD2 1 
ATOM   3839 N  N   . GLY A 1 473  ? 38.094 68.545  1.142   1.00 6.53  ? 473  GLY A N   1 
ATOM   3840 C  CA  . GLY A 1 473  ? 39.068 69.266  0.346   1.00 6.83  ? 473  GLY A CA  1 
ATOM   3841 C  C   . GLY A 1 473  ? 38.529 69.358  -1.072  1.00 6.18  ? 473  GLY A C   1 
ATOM   3842 O  O   . GLY A 1 473  ? 37.812 70.301  -1.430  1.00 6.65  ? 473  GLY A O   1 
ATOM   3843 N  N   . ILE A 1 474  ? 38.861 68.360  -1.901  1.00 6.00  ? 474  ILE A N   1 
ATOM   3844 C  CA  . ILE A 1 474  ? 38.427 68.336  -3.306  1.00 6.50  ? 474  ILE A CA  1 
ATOM   3845 C  C   . ILE A 1 474  ? 36.903 68.461  -3.458  1.00 6.51  ? 474  ILE A C   1 
ATOM   3846 O  O   . ILE A 1 474  ? 36.415 68.952  -4.491  1.00 6.96  ? 474  ILE A O   1 
ATOM   3847 C  CB  . ILE A 1 474  ? 39.007 67.088  -3.974  1.00 5.62  ? 474  ILE A CB  1 
ATOM   3848 C  CG1 . ILE A 1 474  ? 38.759 67.124  -5.492  1.00 7.53  ? 474  ILE A CG1 1 
ATOM   3849 C  CG2 . ILE A 1 474  ? 38.473 65.785  -3.355  1.00 6.89  ? 474  ILE A CG2 1 
ATOM   3850 C  CD1 . ILE A 1 474  ? 39.494 65.973  -6.225  1.00 8.67  ? 474  ILE A CD1 1 
ATOM   3851 N  N   . THR A 1 475  ? 36.162 68.040  -2.435  1.00 5.81  ? 475  THR A N   1 
ATOM   3852 C  CA  . THR A 1 475  ? 34.690 68.115  -2.461  1.00 6.58  ? 475  THR A CA  1 
ATOM   3853 C  C   . THR A 1 475  ? 34.153 69.538  -2.460  1.00 6.24  ? 475  THR A C   1 
ATOM   3854 O  O   . THR A 1 475  ? 32.989 69.742  -2.817  1.00 6.94  ? 475  THR A O   1 
ATOM   3855 C  CB  . THR A 1 475  ? 34.117 67.460  -1.226  1.00 6.46  ? 475  THR A CB  1 
ATOM   3856 O  OG1 . THR A 1 475  ? 34.652 68.158  -0.093  1.00 7.59  ? 475  THR A OG1 1 
ATOM   3857 C  CG2 . THR A 1 475  ? 34.498 65.976  -1.120  1.00 8.27  ? 475  THR A CG2 1 
ATOM   3858 N  N   . GLY A 1 476  ? 34.965 70.529  -2.081  1.00 6.38  ? 476  GLY A N   1 
ATOM   3859 C  CA  . GLY A 1 476  ? 34.465 71.899  -2.061  1.00 7.14  ? 476  GLY A CA  1 
ATOM   3860 C  C   . GLY A 1 476  ? 33.490 72.169  -0.913  1.00 7.23  ? 476  GLY A C   1 
ATOM   3861 O  O   . GLY A 1 476  ? 32.605 73.015  -1.046  1.00 7.77  ? 476  GLY A O   1 
ATOM   3862 N  N   . THR A 1 477  ? 33.641 71.454  0.202   1.00 6.94  ? 477  THR A N   1 
ATOM   3863 C  CA  . THR A 1 477  ? 32.735 71.583  1.331   1.00 7.59  ? 477  THR A CA  1 
ATOM   3864 C  C   . THR A 1 477  ? 33.393 72.196  2.553   1.00 7.41  ? 477  THR A C   1 
ATOM   3865 O  O   . THR A 1 477  ? 32.839 72.065  3.656   1.00 10.06 ? 477  THR A O   1 
ATOM   3866 C  CB  . THR A 1 477  ? 32.089 70.240  1.688   1.00 7.85  ? 477  THR A CB  1 
ATOM   3867 O  OG1 . THR A 1 477  ? 33.110 69.253  1.936   1.00 8.30  ? 477  THR A OG1 1 
ATOM   3868 C  CG2 . THR A 1 477  ? 31.261 69.727  0.505   1.00 8.24  ? 477  THR A CG2 1 
ATOM   3869 N  N   . ALA A 1 478  ? 34.499 72.936  2.383   1.00 7.84  ? 478  ALA A N   1 
ATOM   3870 C  CA  . ALA A 1 478  ? 35.146 73.584  3.521   1.00 7.69  ? 478  ALA A CA  1 
ATOM   3871 C  C   . ALA A 1 478  ? 34.838 75.079  3.576   1.00 7.64  ? 478  ALA A C   1 
ATOM   3872 O  O   . ALA A 1 478  ? 34.347 75.690  2.632   1.00 8.13  ? 478  ALA A O   1 
ATOM   3873 C  CB  . ALA A 1 478  ? 36.690 73.344  3.474   1.00 8.22  ? 478  ALA A CB  1 
ATOM   3874 N  N   . LYS A 1 479  ? 35.110 75.670  4.736   1.00 8.18  ? 479  LYS A N   1 
ATOM   3875 C  CA  . LYS A 1 479  ? 34.929 77.125  4.860   1.00 9.40  ? 479  LYS A CA  1 
ATOM   3876 C  C   . LYS A 1 479  ? 35.900 77.854  3.945   1.00 8.91  ? 479  LYS A C   1 
ATOM   3877 O  O   . LYS A 1 479  ? 36.968 77.350  3.591   1.00 8.19  ? 479  LYS A O   1 
ATOM   3878 C  CB  . LYS A 1 479  ? 35.186 77.566  6.307   1.00 10.88 ? 479  LYS A CB  1 
ATOM   3879 C  CG  . LYS A 1 479  ? 33.990 77.236  7.213   1.00 14.37 ? 479  LYS A CG  1 
ATOM   3880 C  CD  . LYS A 1 479  ? 33.961 78.091  8.468   1.00 18.49 ? 479  LYS A CD  1 
ATOM   3881 C  CE  . LYS A 1 479  ? 32.666 77.894  9.288   1.00 17.99 ? 479  LYS A CE  1 
ATOM   3882 N  NZ  . LYS A 1 479  ? 31.469 78.563  8.696   1.00 19.76 ? 479  LYS A NZ  1 
ATOM   3883 N  N   . THR A 1 480  ? 35.530 79.078  3.580   1.00 9.86  ? 480  THR A N   1 
ATOM   3884 C  CA  . THR A 1 480  ? 36.330 79.873  2.666   1.00 10.17 ? 480  THR A CA  1 
ATOM   3885 C  C   . THR A 1 480  ? 37.803 79.949  3.024   1.00 9.79  ? 480  THR A C   1 
ATOM   3886 O  O   . THR A 1 480  ? 38.657 79.741  2.159   1.00 10.23 ? 480  THR A O   1 
ATOM   3887 C  CB  . THR A 1 480  ? 35.734 81.294  2.578   1.00 12.43 ? 480  THR A CB  1 
ATOM   3888 O  OG1 . THR A 1 480  ? 34.428 81.147  2.020   1.00 14.65 ? 480  THR A OG1 1 
ATOM   3889 C  CG2 . THR A 1 480  ? 36.487 82.155  1.583   1.00 15.83 ? 480  THR A CG2 1 
ATOM   3890 N  N   . HIS A 1 481  ? 38.140 80.236  4.287   1.00 9.73  ? 481  HIS A N   1 
ATOM   3891 C  CA  . HIS A 1 481  ? 39.559 80.378  4.620   1.00 9.25  ? 481  HIS A CA  1 
ATOM   3892 C  C   . HIS A 1 481  ? 40.296 79.053  4.579   1.00 9.70  ? 481  HIS A C   1 
ATOM   3893 O  O   . HIS A 1 481  ? 41.503 79.016  4.413   1.00 9.60  ? 481  HIS A O   1 
ATOM   3894 C  CB  . HIS A 1 481  ? 39.793 81.084  5.990   1.00 11.15 ? 481  HIS A CB  1 
ATOM   3895 C  CG  . HIS A 1 481  ? 39.606 80.209  7.193   1.00 11.60 ? 481  HIS A CG  1 
ATOM   3896 N  ND1 . HIS A 1 481  ? 38.367 79.795  7.636   1.00 13.38 ? 481  HIS A ND1 1 
ATOM   3897 C  CD2 . HIS A 1 481  ? 40.511 79.692  8.060   1.00 12.10 ? 481  HIS A CD2 1 
ATOM   3898 C  CE1 . HIS A 1 481  ? 38.525 79.057  8.725   1.00 12.62 ? 481  HIS A CE1 1 
ATOM   3899 N  NE2 . HIS A 1 481  ? 39.814 78.979  9.002   1.00 13.43 ? 481  HIS A NE2 1 
ATOM   3900 N  N   . VAL A 1 482  ? 39.556 77.956  4.712   1.00 8.76  ? 482  VAL A N   1 
ATOM   3901 C  CA  . VAL A 1 482  ? 40.159 76.640  4.633   1.00 8.73  ? 482  VAL A CA  1 
ATOM   3902 C  C   . VAL A 1 482  ? 40.425 76.290  3.146   1.00 7.49  ? 482  VAL A C   1 
ATOM   3903 O  O   . VAL A 1 482  ? 41.486 75.764  2.815   1.00 8.22  ? 482  VAL A O   1 
ATOM   3904 C  CB  . VAL A 1 482  ? 39.246 75.608  5.293   1.00 8.08  ? 482  VAL A CB  1 
ATOM   3905 C  CG1 . VAL A 1 482  ? 39.883 74.215  5.185   1.00 8.76  ? 482  VAL A CG1 1 
ATOM   3906 C  CG2 . VAL A 1 482  ? 39.016 75.957  6.791   1.00 9.69  ? 482  VAL A CG2 1 
ATOM   3907 N  N   . VAL A 1 483  ? 39.493 76.619  2.252   1.00 7.50  ? 483  VAL A N   1 
ATOM   3908 C  CA  . VAL A 1 483  ? 39.751 76.470  0.826   1.00 8.10  ? 483  VAL A CA  1 
ATOM   3909 C  C   . VAL A 1 483  ? 41.004 77.252  0.425   1.00 8.06  ? 483  VAL A C   1 
ATOM   3910 O  O   . VAL A 1 483  ? 41.841 76.762  -0.338  1.00 8.69  ? 483  VAL A O   1 
ATOM   3911 C  CB  . VAL A 1 483  ? 38.527 76.959  0.020   1.00 7.81  ? 483  VAL A CB  1 
ATOM   3912 C  CG1 . VAL A 1 483  ? 38.781 76.909  -1.491  1.00 10.60 ? 483  VAL A CG1 1 
ATOM   3913 C  CG2 . VAL A 1 483  ? 37.300 76.086  0.367   1.00 9.30  ? 483  VAL A CG2 1 
ATOM   3914 N  N   . VAL A 1 484  ? 41.129 78.471  0.941   1.00 9.03  ? 484  VAL A N   1 
ATOM   3915 C  CA  . VAL A 1 484  ? 42.322 79.278  0.707   1.00 9.87  ? 484  VAL A CA  1 
ATOM   3916 C  C   . VAL A 1 484  ? 43.594 78.581  1.166   1.00 8.85  ? 484  VAL A C   1 
ATOM   3917 O  O   . VAL A 1 484  ? 44.566 78.550  0.437   1.00 9.50  ? 484  VAL A O   1 
ATOM   3918 C  CB  . VAL A 1 484  ? 42.210 80.685  1.316   1.00 10.10 ? 484  VAL A CB  1 
ATOM   3919 C  CG1 . VAL A 1 484  ? 43.559 81.410  1.244   1.00 11.99 ? 484  VAL A CG1 1 
ATOM   3920 C  CG2 . VAL A 1 484  ? 41.133 81.480  0.591   1.00 12.99 ? 484  VAL A CG2 1 
ATOM   3921 N  N   . ASP A 1 485  ? 43.566 77.994  2.352   1.00 8.74  ? 485  ASP A N   1 
ATOM   3922 C  CA  . ASP A 1 485  ? 44.684 77.187  2.827   1.00 8.50  ? 485  ASP A CA  1 
ATOM   3923 C  C   . ASP A 1 485  ? 45.035 76.042  1.882   1.00 9.12  ? 485  ASP A C   1 
ATOM   3924 O  O   . ASP A 1 485  ? 46.189 75.859  1.567   1.00 8.85  ? 485  ASP A O   1 
ATOM   3925 C  CB  . ASP A 1 485  ? 44.440 76.671  4.251   1.00 9.33  ? 485  ASP A CB  1 
ATOM   3926 C  CG  . ASP A 1 485  ? 45.686 76.061  4.870   1.00 11.06 ? 485  ASP A CG  1 
ATOM   3927 O  OD1 . ASP A 1 485  ? 46.678 76.786  5.019   1.00 15.37 ? 485  ASP A OD1 1 
ATOM   3928 O  OD2 . ASP A 1 485  ? 45.683 74.884  5.215   1.00 10.48 ? 485  ASP A OD2 1 
ATOM   3929 N  N   . TYR A 1 486  ? 44.045 75.280  1.434   1.00 7.37  ? 486  TYR A N   1 
ATOM   3930 C  CA  . TYR A 1 486  ? 44.312 74.186  0.497   1.00 7.52  ? 486  TYR A CA  1 
ATOM   3931 C  C   . TYR A 1 486  ? 44.931 74.723  -0.789  1.00 7.34  ? 486  TYR A C   1 
ATOM   3932 O  O   . TYR A 1 486  ? 45.840 74.141  -1.314  1.00 7.61  ? 486  TYR A O   1 
ATOM   3933 C  CB  . TYR A 1 486  ? 43.027 73.416  0.158   1.00 8.43  ? 486  TYR A CB  1 
ATOM   3934 C  CG  . TYR A 1 486  ? 42.434 72.545  1.274   1.00 7.91  ? 486  TYR A CG  1 
ATOM   3935 C  CD1 . TYR A 1 486  ? 43.227 71.686  2.043   1.00 9.84  ? 486  TYR A CD1 1 
ATOM   3936 C  CD2 . TYR A 1 486  ? 41.066 72.548  1.512   1.00 8.42  ? 486  TYR A CD2 1 
ATOM   3937 C  CE1 . TYR A 1 486  ? 42.654 70.876  3.033   1.00 10.37 ? 486  TYR A CE1 1 
ATOM   3938 C  CE2 . TYR A 1 486  ? 40.503 71.750  2.491   1.00 8.24  ? 486  TYR A CE2 1 
ATOM   3939 C  CZ  . TYR A 1 486  ? 41.288 70.920  3.237   1.00 8.53  ? 486  TYR A CZ  1 
ATOM   3940 O  OH  . TYR A 1 486  ? 40.667 70.145  4.194   1.00 10.50 ? 486  TYR A OH  1 
ATOM   3941 N  N   . GLU A 1 487  ? 44.412 75.834  -1.282  1.00 8.42  ? 487  GLU A N   1 
ATOM   3942 C  CA  . GLU A 1 487  ? 44.904 76.428  -2.528  1.00 8.55  ? 487  GLU A CA  1 
ATOM   3943 C  C   . GLU A 1 487  ? 46.362 76.859  -2.371  1.00 9.13  ? 487  GLU A C   1 
ATOM   3944 O  O   . GLU A 1 487  ? 47.224 76.587  -3.240  1.00 9.15  ? 487  GLU A O   1 
ATOM   3945 C  CB  . GLU A 1 487  ? 44.045 77.623  -2.931  1.00 8.97  ? 487  GLU A CB  1 
ATOM   3946 C  CG  . GLU A 1 487  ? 44.467 78.186  -4.277  1.00 11.39 ? 487  GLU A CG  1 
ATOM   3947 C  CD  . GLU A 1 487  ? 43.626 79.331  -4.744  1.00 15.67 ? 487  GLU A CD  1 
ATOM   3948 O  OE1 . GLU A 1 487  ? 42.483 79.511  -4.277  1.00 16.13 ? 487  GLU A OE1 1 
ATOM   3949 O  OE2 . GLU A 1 487  ? 44.131 80.044  -5.645  1.00 19.98 ? 487  GLU A OE2 1 
ATOM   3950 N  N   . GLN A 1 488  ? 46.677 77.529  -1.268  1.00 9.27  ? 488  GLN A N   1 
ATOM   3951 C  CA  . GLN A 1 488  ? 48.070 77.971  -1.006  1.00 10.48 ? 488  GLN A CA  1 
ATOM   3952 C  C   . GLN A 1 488  ? 48.993 76.780  -0.908  1.00 9.90  ? 488  GLN A C   1 
ATOM   3953 O  O   . GLN A 1 488  ? 50.121 76.803  -1.461  1.00 9.68  ? 488  GLN A O   1 
ATOM   3954 C  CB  . GLN A 1 488  ? 48.158 78.776  0.309   1.00 12.69 ? 488  GLN A CB  1 
ATOM   3955 C  CG  . GLN A 1 488  ? 47.419 80.065  0.260   1.00 17.89 ? 488  GLN A CG  1 
ATOM   3956 C  CD  . GLN A 1 488  ? 47.390 80.764  1.616   1.00 23.72 ? 488  GLN A CD  1 
ATOM   3957 O  OE1 . GLN A 1 488  ? 47.628 80.151  2.674   1.00 27.40 ? 488  GLN A OE1 1 
ATOM   3958 N  NE2 . GLN A 1 488  ? 47.081 82.035  1.590   1.00 26.94 ? 488  GLN A NE2 1 
ATOM   3959 N  N   . ARG A 1 489  ? 48.557 75.719  -0.242  1.00 8.63  ? 489  ARG A N   1 
ATOM   3960 C  CA  . ARG A 1 489  ? 49.359 74.501  -0.142  1.00 8.99  ? 489  ARG A CA  1 
ATOM   3961 C  C   . ARG A 1 489  ? 49.591 73.899  -1.525  1.00 8.50  ? 489  ARG A C   1 
ATOM   3962 O  O   . ARG A 1 489  ? 50.704 73.534  -1.873  1.00 8.12  ? 489  ARG A O   1 
ATOM   3963 C  CB  . ARG A 1 489  ? 48.682 73.497  0.764   1.00 8.25  ? 489  ARG A CB  1 
ATOM   3964 C  CG  . ARG A 1 489  ? 48.764 73.840  2.215   1.00 8.72  ? 489  ARG A CG  1 
ATOM   3965 C  CD  . ARG A 1 489  ? 47.768 72.956  3.028   1.00 10.90 ? 489  ARG A CD  1 
ATOM   3966 N  NE  . ARG A 1 489  ? 47.881 73.106  4.487   1.00 10.78 ? 489  ARG A NE  1 
ATOM   3967 C  CZ  . ARG A 1 489  ? 48.735 72.443  5.262   1.00 11.98 ? 489  ARG A CZ  1 
ATOM   3968 N  NH1 . ARG A 1 489  ? 49.587 71.557  4.774   1.00 13.06 ? 489  ARG A NH1 1 
ATOM   3969 N  NH2 . ARG A 1 489  ? 48.726 72.697  6.570   1.00 13.60 ? 489  ARG A NH2 1 
ATOM   3970 N  N   . MET A 1 490  ? 48.557 73.835  -2.361  1.00 7.41  ? 490  MET A N   1 
ATOM   3971 C  CA  . MET A 1 490  ? 48.722 73.279  -3.700  1.00 7.88  ? 490  MET A CA  1 
ATOM   3972 C  C   . MET A 1 490  ? 49.599 74.170  -4.576  1.00 8.17  ? 490  MET A C   1 
ATOM   3973 O  O   . MET A 1 490  ? 50.330 73.667  -5.441  1.00 8.45  ? 490  MET A O   1 
ATOM   3974 C  CB  . MET A 1 490  ? 47.362 73.042  -4.365  1.00 7.53  ? 490  MET A CB  1 
ATOM   3975 C  CG  . MET A 1 490  ? 46.612 71.860  -3.726  1.00 9.01  ? 490  MET A CG  1 
ATOM   3976 S  SD  . MET A 1 490  ? 45.310 71.131  -4.810  1.00 10.91 ? 490  MET A SD  1 
ATOM   3977 C  CE  . MET A 1 490  ? 44.037 72.314  -4.455  1.00 13.16 ? 490  MET A CE  1 
ATOM   3978 N  N   . GLN A 1 491  ? 49.516 75.484  -4.377  1.00 8.03  ? 491  GLN A N   1 
ATOM   3979 C  CA  . GLN A 1 491  ? 50.410 76.381  -5.136  1.00 9.77  ? 491  GLN A CA  1 
ATOM   3980 C  C   . GLN A 1 491  ? 51.878 76.145  -4.799  1.00 9.33  ? 491  GLN A C   1 
ATOM   3981 O  O   . GLN A 1 491  ? 52.751 76.079  -5.694  1.00 9.89  ? 491  GLN A O   1 
ATOM   3982 C  CB  . GLN A 1 491  ? 50.077 77.842  -4.859  1.00 11.09 ? 491  GLN A CB  1 
ATOM   3983 C  CG  . GLN A 1 491  ? 50.889 78.753  -5.794  1.00 15.89 ? 491  GLN A CG  1 
ATOM   3984 C  CD  . GLN A 1 491  ? 50.766 78.354  -7.256  1.00 24.02 ? 491  GLN A CD  1 
ATOM   3985 O  OE1 . GLN A 1 491  ? 49.673 78.141  -7.738  1.00 28.85 ? 491  GLN A OE1 1 
ATOM   3986 N  NE2 . GLN A 1 491  ? 51.900 78.210  -7.946  1.00 25.78 ? 491  GLN A NE2 1 
ATOM   3987 N  N   . GLU A 1 492  ? 52.162 75.936  -3.516  1.00 9.54  ? 492  GLU A N   1 
ATOM   3988 C  CA  . GLU A 1 492  ? 53.511 75.612  -3.095  1.00 10.79 ? 492  GLU A CA  1 
ATOM   3989 C  C   . GLU A 1 492  ? 53.932 74.281  -3.702  1.00 9.79  ? 492  GLU A C   1 
ATOM   3990 O  O   . GLU A 1 492  ? 55.077 74.105  -4.154  1.00 10.06 ? 492  GLU A O   1 
ATOM   3991 C  CB  . GLU A 1 492  ? 53.589 75.560  -1.563  1.00 12.37 ? 492  GLU A CB  1 
ATOM   3992 C  CG  . GLU A 1 492  ? 53.523 76.916  -0.871  1.00 19.03 ? 492  GLU A CG  1 
ATOM   3993 C  CD  . GLU A 1 492  ? 54.482 77.941  -1.461  1.00 24.97 ? 492  GLU A CD  1 
ATOM   3994 O  OE1 . GLU A 1 492  ? 55.704 77.662  -1.559  1.00 29.92 ? 492  GLU A OE1 1 
ATOM   3995 O  OE2 . GLU A 1 492  ? 54.014 79.043  -1.824  1.00 30.27 ? 492  GLU A OE2 1 
ATOM   3996 N  N   . ALA A 1 493  ? 53.011 73.319  -3.745  1.00 8.52  ? 493  ALA A N   1 
ATOM   3997 C  CA  . ALA A 1 493  ? 53.307 72.007  -4.336  1.00 7.44  ? 493  ALA A CA  1 
ATOM   3998 C  C   . ALA A 1 493  ? 53.624 72.140  -5.853  1.00 7.89  ? 493  ALA A C   1 
ATOM   3999 O  O   . ALA A 1 493  ? 54.526 71.467  -6.358  1.00 7.66  ? 493  ALA A O   1 
ATOM   4000 C  CB  . ALA A 1 493  ? 52.116 71.045  -4.090  1.00 8.05  ? 493  ALA A CB  1 
ATOM   4001 N  N   . LEU A 1 494  ? 52.880 72.982  -6.572  1.00 7.47  ? 494  LEU A N   1 
ATOM   4002 C  CA  . LEU A 1 494  ? 53.158 73.211  -7.995  1.00 7.80  ? 494  LEU A CA  1 
ATOM   4003 C  C   . LEU A 1 494  ? 54.551 73.798  -8.169  1.00 8.11  ? 494  LEU A C   1 
ATOM   4004 O  O   . LEU A 1 494  ? 55.280 73.377  -9.073  1.00 8.18  ? 494  LEU A O   1 
ATOM   4005 C  CB  . LEU A 1 494  ? 52.110 74.143  -8.606  1.00 8.15  ? 494  LEU A CB  1 
ATOM   4006 C  CG  . LEU A 1 494  ? 50.742 73.482  -8.830  1.00 8.30  ? 494  LEU A CG  1 
ATOM   4007 C  CD1 . LEU A 1 494  ? 49.693 74.552  -9.154  1.00 10.55 ? 494  LEU A CD1 1 
ATOM   4008 C  CD2 . LEU A 1 494  ? 50.795 72.448  -9.935  1.00 9.47  ? 494  LEU A CD2 1 
ATOM   4009 N  N   . LYS A 1 495  ? 54.938 74.739  -7.315  1.00 8.73  ? 495  LYS A N   1 
ATOM   4010 C  CA  . LYS A 1 495  ? 56.284 75.330  -7.410  1.00 9.11  ? 495  LYS A CA  1 
ATOM   4011 C  C   . LYS A 1 495  ? 57.335 74.289  -7.125  1.00 8.75  ? 495  LYS A C   1 
ATOM   4012 O  O   . LYS A 1 495  ? 58.377 74.257  -7.805  1.00 9.22  ? 495  LYS A O   1 
ATOM   4013 C  CB  . LYS A 1 495  ? 56.404 76.494  -6.449  1.00 11.25 ? 495  LYS A CB  1 
ATOM   4014 C  CG  . LYS A 1 495  ? 55.551 77.662  -6.875  1.00 14.80 ? 495  LYS A CG  1 
ATOM   4015 C  CD  . LYS A 1 495  ? 55.767 78.898  -6.014  1.00 22.95 ? 495  LYS A CD  1 
ATOM   4016 C  CE  . LYS A 1 495  ? 55.056 78.804  -4.700  1.00 27.19 ? 495  LYS A CE  1 
ATOM   4017 N  NZ  . LYS A 1 495  ? 55.247 80.061  -3.901  1.00 31.22 ? 495  LYS A NZ  1 
ATOM   4018 N  N   . ALA A 1 496  ? 57.080 73.406  -6.160  1.00 7.78  ? 496  ALA A N   1 
ATOM   4019 C  CA  . ALA A 1 496  ? 58.011 72.342  -5.856  1.00 8.08  ? 496  ALA A CA  1 
ATOM   4020 C  C   . ALA A 1 496  ? 58.187 71.423  -7.079  1.00 8.31  ? 496  ALA A C   1 
ATOM   4021 O  O   . ALA A 1 496  ? 59.302 71.023  -7.436  1.00 8.77  ? 496  ALA A O   1 
ATOM   4022 C  CB  . ALA A 1 496  ? 57.509 71.528  -4.619  1.00 8.91  ? 496  ALA A CB  1 
ATOM   4023 N  N   . CYS A 1 497  ? 57.078 71.039  -7.713  1.00 7.67  ? 497  CYS A N   1 
ATOM   4024 C  CA  . CYS A 1 497  ? 57.133 70.185  -8.903  1.00 7.23  ? 497  CYS A CA  1 
ATOM   4025 C  C   . CYS A 1 497  ? 57.893 70.871  -10.022 1.00 8.10  ? 497  CYS A C   1 
ATOM   4026 O  O   . CYS A 1 497  ? 58.719 70.238  -10.663 1.00 7.72  ? 497  CYS A O   1 
ATOM   4027 C  CB  . CYS A 1 497  ? 55.713 69.846  -9.378  1.00 7.72  ? 497  CYS A CB  1 
ATOM   4028 S  SG  . CYS A 1 497  ? 54.824 68.698  -8.317  1.00 8.86  ? 497  CYS A SG  1 
ATOM   4029 N  N   . GLN A 1 498  ? 57.632 72.148  -10.229 1.00 8.04  ? 498  GLN A N   1 
ATOM   4030 C  CA  . GLN A 1 498  ? 58.344 72.872  -11.283 1.00 8.92  ? 498  GLN A CA  1 
ATOM   4031 C  C   . GLN A 1 498  ? 59.829 72.837  -11.016 1.00 8.60  ? 498  GLN A C   1 
ATOM   4032 O  O   . GLN A 1 498  ? 60.618 72.605  -11.958 1.00 8.41  ? 498  GLN A O   1 
ATOM   4033 C  CB  . GLN A 1 498  ? 57.885 74.316  -11.346 1.00 8.89  ? 498  GLN A CB  1 
ATOM   4034 C  CG  . GLN A 1 498  ? 58.733 75.130  -12.317 1.00 12.76 ? 498  GLN A CG  1 
ATOM   4035 C  CD  . GLN A 1 498  ? 58.220 76.544  -12.526 1.00 13.68 ? 498  GLN A CD  1 
ATOM   4036 O  OE1 . GLN A 1 498  ? 57.937 76.948  -13.660 1.00 14.55 ? 498  GLN A OE1 1 
ATOM   4037 N  NE2 . GLN A 1 498  ? 58.130 77.320  -11.429 1.00 16.11 ? 498  GLN A NE2 1 
ATOM   4038 N  N   . MET A 1 499  ? 60.252 73.074  -9.785  1.00 7.89  ? 499  MET A N   1 
ATOM   4039 C  CA  . MET A 1 499  ? 61.676 73.102  -9.459  1.00 8.88  ? 499  MET A CA  1 
ATOM   4040 C  C   . MET A 1 499  ? 62.326 71.756  -9.778  1.00 9.11  ? 499  MET A C   1 
ATOM   4041 O  O   . MET A 1 499  ? 63.364 71.694  -10.404 1.00 9.64  ? 499  MET A O   1 
ATOM   4042 C  CB  . MET A 1 499  ? 61.864 73.474  -7.987  1.00 9.77  ? 499  MET A CB  1 
ATOM   4043 C  CG  . MET A 1 499  ? 63.300 73.302  -7.458  1.00 11.50 ? 499  MET A CG  1 
ATOM   4044 S  SD  . MET A 1 499  ? 64.592 74.300  -8.253  1.00 16.76 ? 499  MET A SD  1 
ATOM   4045 C  CE  . MET A 1 499  ? 64.009 75.915  -7.809  1.00 17.90 ? 499  MET A CE  1 
ATOM   4046 N  N   . VAL A 1 500  ? 61.681 70.678  -9.354  1.00 8.29  ? 500  VAL A N   1 
ATOM   4047 C  CA  . VAL A 1 500  ? 62.240 69.361  -9.543  1.00 7.88  ? 500  VAL A CA  1 
ATOM   4048 C  C   . VAL A 1 500  ? 62.265 69.040  -11.045 1.00 8.02  ? 500  VAL A C   1 
ATOM   4049 O  O   . VAL A 1 500  ? 63.255 68.498  -11.555 1.00 8.18  ? 500  VAL A O   1 
ATOM   4050 C  CB  . VAL A 1 500  ? 61.441 68.294  -8.769  1.00 8.30  ? 500  VAL A CB  1 
ATOM   4051 C  CG1 . VAL A 1 500  ? 61.871 66.920  -9.166  1.00 8.34  ? 500  VAL A CG1 1 
ATOM   4052 C  CG2 . VAL A 1 500  ? 61.688 68.500  -7.270  1.00 9.96  ? 500  VAL A CG2 1 
ATOM   4053 N  N   . MET A 1 501  ? 61.192 69.354  -11.749 1.00 7.71  ? 501  MET A N   1 
ATOM   4054 C  CA  . MET A 1 501  ? 61.107 69.062  -13.176 1.00 8.31  ? 501  MET A CA  1 
ATOM   4055 C  C   . MET A 1 501  ? 62.201 69.776  -13.948 1.00 7.84  ? 501  MET A C   1 
ATOM   4056 O  O   . MET A 1 501  ? 62.874 69.168  -14.768 1.00 8.35  ? 501  MET A O   1 
ATOM   4057 C  CB  . MET A 1 501  ? 59.732 69.440  -13.715 1.00 8.28  ? 501  MET A CB  1 
ATOM   4058 C  CG  . MET A 1 501  ? 58.632 68.490  -13.248 1.00 8.65  ? 501  MET A CG  1 
ATOM   4059 S  SD  . MET A 1 501  ? 56.965 69.112  -13.571 1.00 12.34 ? 501  MET A SD  1 
ATOM   4060 C  CE  . MET A 1 501  ? 56.869 68.825  -15.319 1.00 13.84 ? 501  MET A CE  1 
ATOM   4061 N  N   . GLN A 1 502  ? 62.391 71.059  -13.673 1.00 7.98  ? 502  GLN A N   1 
ATOM   4062 C  CA  . GLN A 1 502  ? 63.314 71.835  -14.521 1.00 8.37  ? 502  GLN A CA  1 
ATOM   4063 C  C   . GLN A 1 502  ? 64.774 71.466  -14.191 1.00 9.71  ? 502  GLN A C   1 
ATOM   4064 O  O   . GLN A 1 502  ? 65.601 71.399  -15.121 1.00 10.05 ? 502  GLN A O   1 
ATOM   4065 C  CB  . GLN A 1 502  ? 63.024 73.319  -14.411 1.00 9.94  ? 502  GLN A CB  1 
ATOM   4066 C  CG  . GLN A 1 502  ? 63.224 73.945  -13.053 1.00 10.36 ? 502  GLN A CG  1 
ATOM   4067 C  CD  . GLN A 1 502  ? 64.637 74.485  -12.839 1.00 12.27 ? 502  GLN A CD  1 
ATOM   4068 O  OE1 . GLN A 1 502  ? 65.432 74.619  -13.786 1.00 12.44 ? 502  GLN A OE1 1 
ATOM   4069 N  NE2 . GLN A 1 502  ? 64.964 74.789  -11.594 1.00 13.40 ? 502  GLN A NE2 1 
ATOM   4070 N  N   . GLN A 1 503  ? 65.085 71.154  -12.938 1.00 8.80  ? 503  GLN A N   1 
ATOM   4071 C  CA  . GLN A 1 503  ? 66.433 70.623  -12.639 1.00 9.47  ? 503  GLN A CA  1 
ATOM   4072 C  C   . GLN A 1 503  ? 66.657 69.317  -13.365 1.00 9.71  ? 503  GLN A C   1 
ATOM   4073 O  O   . GLN A 1 503  ? 67.755 69.022  -13.886 1.00 9.64  ? 503  GLN A O   1 
ATOM   4074 C  CB  . GLN A 1 503  ? 66.621 70.381  -11.138 1.00 10.12 ? 503  GLN A CB  1 
ATOM   4075 C  CG  . GLN A 1 503  ? 66.754 71.643  -10.296 1.00 11.32 ? 503  GLN A CG  1 
ATOM   4076 C  CD  . GLN A 1 503  ? 68.106 72.348  -10.453 1.00 13.46 ? 503  GLN A CD  1 
ATOM   4077 O  OE1 . GLN A 1 503  ? 69.110 71.707  -10.745 1.00 14.68 ? 503  GLN A OE1 1 
ATOM   4078 N  NE2 . GLN A 1 503  ? 68.117 73.655  -10.251 1.00 14.37 ? 503  GLN A NE2 1 
ATOM   4079 N  N   . SER A 1 504  ? 65.630 68.469  -13.410 1.00 7.75  ? 504  SER A N   1 
ATOM   4080 C  CA  . SER A 1 504  ? 65.753 67.172  -14.065 1.00 9.03  ? 504  SER A CA  1 
ATOM   4081 C  C   . SER A 1 504  ? 65.976 67.296  -15.584 1.00 8.76  ? 504  SER A C   1 
ATOM   4082 O  O   . SER A 1 504  ? 66.841 66.610  -16.158 1.00 9.20  ? 504  SER A O   1 
ATOM   4083 C  CB  . SER A 1 504  ? 64.513 66.297  -13.812 1.00 9.31  ? 504  SER A CB  1 
ATOM   4084 O  OG  . SER A 1 504  ? 64.387 66.006  -12.407 1.00 9.91  ? 504  SER A OG  1 
ATOM   4085 N  N   . VAL A 1 505  ? 65.217 68.182  -16.214 1.00 8.33  ? 505  VAL A N   1 
ATOM   4086 C  CA  . VAL A 1 505  ? 65.357 68.408  -17.656 1.00 8.80  ? 505  VAL A CA  1 
ATOM   4087 C  C   . VAL A 1 505  ? 66.797 68.902  -17.954 1.00 9.31  ? 505  VAL A C   1 
ATOM   4088 O  O   . VAL A 1 505  ? 67.456 68.430  -18.900 1.00 10.44 ? 505  VAL A O   1 
ATOM   4089 C  CB  . VAL A 1 505  ? 64.301 69.416  -18.145 1.00 9.77  ? 505  VAL A CB  1 
ATOM   4090 C  CG1 . VAL A 1 505  ? 64.591 69.847  -19.602 1.00 10.72 ? 505  VAL A CG1 1 
ATOM   4091 C  CG2 . VAL A 1 505  ? 62.894 68.811  -18.034 1.00 10.57 ? 505  VAL A CG2 1 
ATOM   4092 N  N   . TYR A 1 506  ? 67.271 69.842  -17.169 1.00 9.50  ? 506  TYR A N   1 
ATOM   4093 C  CA  . TYR A 1 506  ? 68.609 70.347  -17.408 1.00 10.79 ? 506  TYR A CA  1 
ATOM   4094 C  C   . TYR A 1 506  ? 69.643 69.212  -17.308 1.00 11.30 ? 506  TYR A C   1 
ATOM   4095 O  O   . TYR A 1 506  ? 70.556 69.075  -18.146 1.00 12.17 ? 506  TYR A O   1 
ATOM   4096 C  CB  . TYR A 1 506  ? 68.890 71.480  -16.437 1.00 12.34 ? 506  TYR A CB  1 
ATOM   4097 C  CG  . TYR A 1 506  ? 70.179 72.193  -16.723 1.00 15.81 ? 506  TYR A CG  1 
ATOM   4098 C  CD1 . TYR A 1 506  ? 70.338 72.898  -17.936 1.00 18.02 ? 506  TYR A CD1 1 
ATOM   4099 C  CD2 . TYR A 1 506  ? 71.210 72.193  -15.797 1.00 15.99 ? 506  TYR A CD2 1 
ATOM   4100 C  CE1 . TYR A 1 506  ? 71.510 73.577  -18.227 1.00 19.73 ? 506  TYR A CE1 1 
ATOM   4101 C  CE2 . TYR A 1 506  ? 72.429 72.874  -16.087 1.00 19.79 ? 506  TYR A CE2 1 
ATOM   4102 C  CZ  . TYR A 1 506  ? 72.545 73.538  -17.308 1.00 18.97 ? 506  TYR A CZ  1 
ATOM   4103 O  OH  . TYR A 1 506  ? 73.690 74.244  -17.622 1.00 19.36 ? 506  TYR A OH  1 
ATOM   4104 N  N   . ARG A 1 507  ? 69.511 68.349  -16.309 1.00 10.65 ? 507  ARG A N   1 
ATOM   4105 C  CA  . ARG A 1 507  ? 70.445 67.232  -16.183 1.00 10.83 ? 507  ARG A CA  1 
ATOM   4106 C  C   . ARG A 1 507  ? 70.315 66.225  -17.326 1.00 11.31 ? 507  ARG A C   1 
ATOM   4107 O  O   . ARG A 1 507  ? 71.312 65.682  -17.813 1.00 11.06 ? 507  ARG A O   1 
ATOM   4108 C  CB  . ARG A 1 507  ? 70.229 66.554  -14.832 1.00 11.16 ? 507  ARG A CB  1 
ATOM   4109 C  CG  . ARG A 1 507  ? 71.297 65.499  -14.473 1.00 13.58 ? 507  ARG A CG  1 
ATOM   4110 C  CD  . ARG A 1 507  ? 71.214 65.127  -13.012 1.00 14.29 ? 507  ARG A CD  1 
ATOM   4111 N  NE  . ARG A 1 507  ? 72.206 64.100  -12.655 1.00 16.90 ? 507  ARG A NE  1 
ATOM   4112 C  CZ  . ARG A 1 507  ? 72.245 63.472  -11.472 1.00 17.52 ? 507  ARG A CZ  1 
ATOM   4113 N  NH1 . ARG A 1 507  ? 71.364 63.772  -10.526 1.00 18.56 ? 507  ARG A NH1 1 
ATOM   4114 N  NH2 . ARG A 1 507  ? 73.147 62.514  -11.253 1.00 19.36 ? 507  ARG A NH2 1 
ATOM   4115 N  N   . LEU A 1 508  ? 69.102 65.930  -17.752 1.00 9.27  ? 508  LEU A N   1 
ATOM   4116 C  CA  . LEU A 1 508  ? 68.891 64.897  -18.740 1.00 9.26  ? 508  LEU A CA  1 
ATOM   4117 C  C   . LEU A 1 508  ? 69.327 65.306  -20.136 1.00 10.15 ? 508  LEU A C   1 
ATOM   4118 O  O   . LEU A 1 508  ? 69.550 64.444  -20.979 1.00 11.95 ? 508  LEU A O   1 
ATOM   4119 C  CB  . LEU A 1 508  ? 67.410 64.511  -18.771 1.00 9.32  ? 508  LEU A CB  1 
ATOM   4120 C  CG  . LEU A 1 508  ? 66.969 63.684  -17.541 1.00 8.91  ? 508  LEU A CG  1 
ATOM   4121 C  CD1 . LEU A 1 508  ? 65.427 63.745  -17.424 1.00 11.27 ? 508  LEU A CD1 1 
ATOM   4122 C  CD2 . LEU A 1 508  ? 67.432 62.234  -17.665 1.00 12.53 ? 508  LEU A CD2 1 
ATOM   4123 N  N   . LEU A 1 509  ? 69.383 66.612  -20.376 1.00 10.45 ? 509  LEU A N   1 
ATOM   4124 C  CA  . LEU A 1 509  ? 69.633 67.140  -21.716 1.00 10.48 ? 509  LEU A CA  1 
ATOM   4125 C  C   . LEU A 1 509  ? 70.915 67.970  -21.809 1.00 11.63 ? 509  LEU A C   1 
ATOM   4126 O  O   . LEU A 1 509  ? 71.077 68.685  -22.802 1.00 11.89 ? 509  LEU A O   1 
ATOM   4127 C  CB  . LEU A 1 509  ? 68.409 67.938  -22.210 1.00 10.57 ? 509  LEU A CB  1 
ATOM   4128 C  CG  . LEU A 1 509  ? 67.185 67.083  -22.553 1.00 10.30 ? 509  LEU A CG  1 
ATOM   4129 C  CD1 . LEU A 1 509  ? 66.030 68.026  -22.966 1.00 10.07 ? 509  LEU A CD1 1 
ATOM   4130 C  CD2 . LEU A 1 509  ? 67.437 66.094  -23.700 1.00 12.25 ? 509  LEU A CD2 1 
ATOM   4131 N  N   . THR A 1 510  ? 71.829 67.862  -20.842 1.00 11.33 ? 510  THR A N   1 
ATOM   4132 C  CA  . THR A 1 510  ? 73.108 68.576  -20.945 1.00 12.64 ? 510  THR A CA  1 
ATOM   4133 C  C   . THR A 1 510  ? 74.246 67.562  -20.954 1.00 13.59 ? 510  THR A C   1 
ATOM   4134 O  O   . THR A 1 510  ? 74.243 66.581  -20.197 1.00 13.34 ? 510  THR A O   1 
ATOM   4135 C  CB  . THR A 1 510  ? 73.244 69.537  -19.767 1.00 11.93 ? 510  THR A CB  1 
ATOM   4136 O  OG1 . THR A 1 510  ? 72.172 70.492  -19.811 1.00 12.34 ? 510  THR A OG1 1 
ATOM   4137 C  CG2 . THR A 1 510  ? 74.560 70.403  -19.831 1.00 12.71 ? 510  THR A CG2 1 
ATOM   4138 N  N   . LYS A 1 511  ? 75.215 67.789  -21.845 1.00 15.19 ? 511  LYS A N   1 
ATOM   4139 C  CA  . LYS A 1 511  ? 76.387 66.911  -21.938 1.00 15.66 ? 511  LYS A CA  1 
ATOM   4140 C  C   . LYS A 1 511  ? 76.967 66.730  -20.553 1.00 15.20 ? 511  LYS A C   1 
ATOM   4141 O  O   . LYS A 1 511  ? 77.207 67.686  -19.852 1.00 14.31 ? 511  LYS A O   1 
ATOM   4142 C  CB  . LYS A 1 511  ? 77.437 67.565  -22.829 1.00 16.59 ? 511  LYS A CB  1 
ATOM   4143 C  CG  . LYS A 1 511  ? 78.678 66.703  -23.061 1.00 20.38 ? 511  LYS A CG  1 
ATOM   4144 C  CD  . LYS A 1 511  ? 79.543 67.339  -24.117 1.00 25.56 ? 511  LYS A CD  1 
ATOM   4145 C  CE  . LYS A 1 511  ? 80.749 66.470  -24.413 1.00 30.35 ? 511  LYS A CE  1 
ATOM   4146 N  NZ  . LYS A 1 511  ? 81.627 67.150  -25.403 1.00 33.44 ? 511  LYS A NZ  1 
ATOM   4147 N  N   . PRO A 1 512  ? 77.160 65.481  -20.138 1.00 16.61 ? 512  PRO A N   1 
ATOM   4148 C  CA  . PRO A 1 512  ? 77.559 65.206  -18.755 1.00 17.30 ? 512  PRO A CA  1 
ATOM   4149 C  C   . PRO A 1 512  ? 78.832 65.928  -18.270 1.00 16.38 ? 512  PRO A C   1 
ATOM   4150 O  O   . PRO A 1 512  ? 78.863 66.407  -17.149 1.00 16.65 ? 512  PRO A O   1 
ATOM   4151 C  CB  . PRO A 1 512  ? 77.757 63.690  -18.752 1.00 18.44 ? 512  PRO A CB  1 
ATOM   4152 C  CG  . PRO A 1 512  ? 76.855 63.214  -19.829 1.00 19.31 ? 512  PRO A CG  1 
ATOM   4153 C  CD  . PRO A 1 512  ? 76.893 64.245  -20.907 1.00 18.03 ? 512  PRO A CD  1 
ATOM   4154 N  N   . SER A 1 513  ? 79.848 66.059  -19.131 1.00 16.66 ? 513  SER A N   1 
ATOM   4155 C  CA  . SER A 1 513  ? 81.091 66.736  -18.701 1.00 17.20 ? 513  SER A CA  1 
ATOM   4156 C  C   . SER A 1 513  ? 80.960 68.259  -18.643 1.00 16.92 ? 513  SER A C   1 
ATOM   4157 O  O   . SER A 1 513  ? 81.908 68.936  -18.245 1.00 17.61 ? 513  SER A O   1 
ATOM   4158 C  CB  . SER A 1 513  ? 82.240 66.351  -19.632 1.00 17.92 ? 513  SER A CB  1 
ATOM   4159 O  OG  . SER A 1 513  ? 81.908 66.681  -20.946 1.00 18.63 ? 513  SER A OG  1 
ATOM   4160 N  N   . ILE A 1 514  ? 79.801 68.794  -19.054 1.00 16.13 ? 514  ILE A N   1 
ATOM   4161 C  CA  . ILE A 1 514  ? 79.516 70.234  -19.029 1.00 17.25 ? 514  ILE A CA  1 
ATOM   4162 C  C   . ILE A 1 514  ? 78.538 70.584  -17.880 1.00 15.14 ? 514  ILE A C   1 
ATOM   4163 O  O   . ILE A 1 514  ? 78.562 71.666  -17.307 1.00 15.49 ? 514  ILE A O   1 
ATOM   4164 C  CB  . ILE A 1 514  ? 78.911 70.687  -20.400 1.00 17.35 ? 514  ILE A CB  1 
ATOM   4165 C  CG1 . ILE A 1 514  ? 79.954 70.558  -21.514 1.00 20.35 ? 514  ILE A CG1 1 
ATOM   4166 C  CG2 . ILE A 1 514  ? 78.344 72.122  -20.315 1.00 19.05 ? 514  ILE A CG2 1 
ATOM   4167 C  CD1 . ILE A 1 514  ? 79.448 70.858  -22.910 1.00 20.47 ? 514  ILE A CD1 1 
ATOM   4168 N  N   . TYR A 1 515  ? 77.663 69.635  -17.559 1.00 14.73 ? 515  TYR A N   1 
ATOM   4169 C  CA  . TYR A 1 515  ? 76.626 69.845  -16.543 1.00 14.40 ? 515  TYR A CA  1 
ATOM   4170 C  C   . TYR A 1 515  ? 77.198 70.403  -15.234 1.00 13.90 ? 515  TYR A C   1 
ATOM   4171 O  O   . TYR A 1 515  ? 78.085 69.773  -14.591 1.00 13.99 ? 515  TYR A O   1 
ATOM   4172 C  CB  . TYR A 1 515  ? 75.939 68.513  -16.346 1.00 14.88 ? 515  TYR A CB  1 
ATOM   4173 C  CG  . TYR A 1 515  ? 74.919 68.479  -15.265 1.00 14.08 ? 515  TYR A CG  1 
ATOM   4174 C  CD1 . TYR A 1 515  ? 73.747 69.222  -15.346 1.00 12.55 ? 515  TYR A CD1 1 
ATOM   4175 C  CD2 . TYR A 1 515  ? 75.127 67.684  -14.158 1.00 14.77 ? 515  TYR A CD2 1 
ATOM   4176 C  CE1 . TYR A 1 515  ? 72.787 69.165  -14.336 1.00 13.25 ? 515  TYR A CE1 1 
ATOM   4177 C  CE2 . TYR A 1 515  ? 74.184 67.609  -13.146 1.00 13.28 ? 515  TYR A CE2 1 
ATOM   4178 C  CZ  . TYR A 1 515  ? 73.027 68.364  -13.246 1.00 14.44 ? 515  TYR A CZ  1 
ATOM   4179 O  OH  . TYR A 1 515  ? 72.103 68.282  -12.250 1.00 13.94 ? 515  TYR A OH  1 
ATOM   4180 N  N   . SER A 1 516  ? 76.729 71.587  -14.832 1.00 14.64 ? 516  SER A N   1 
ATOM   4181 C  CA  . SER A 1 516  ? 77.259 72.290  -13.659 1.00 15.26 ? 516  SER A CA  1 
ATOM   4182 C  C   . SER A 1 516  ? 76.121 72.943  -12.842 1.00 15.66 ? 516  SER A C   1 
ATOM   4183 O  O   . SER A 1 516  ? 75.937 74.169  -12.864 1.00 16.16 ? 516  SER A O   1 
ATOM   4184 C  CB  . SER A 1 516  ? 78.317 73.323  -14.101 1.00 16.20 ? 516  SER A CB  1 
ATOM   4185 O  OG  . SER A 1 516  ? 78.993 73.818  -12.956 1.00 19.51 ? 516  SER A OG  1 
ATOM   4186 N  N   . PRO A 1 517  ? 75.332 72.120  -12.150 1.00 16.38 ? 517  PRO A N   1 
ATOM   4187 C  CA  . PRO A 1 517  ? 74.084 72.621  -11.580 1.00 16.68 ? 517  PRO A CA  1 
ATOM   4188 C  C   . PRO A 1 517  ? 74.227 73.502  -10.356 1.00 16.63 ? 517  PRO A C   1 
ATOM   4189 O  O   . PRO A 1 517  ? 75.081 73.232  -9.489  1.00 19.36 ? 517  PRO A O   1 
ATOM   4190 C  CB  . PRO A 1 517  ? 73.319 71.339  -11.211 1.00 17.19 ? 517  PRO A CB  1 
ATOM   4191 C  CG  . PRO A 1 517  ? 74.399 70.363  -10.903 1.00 16.50 ? 517  PRO A CG  1 
ATOM   4192 C  CD  . PRO A 1 517  ? 75.514 70.685  -11.901 1.00 16.54 ? 517  PRO A CD  1 
ATOM   4193 N  N   . ASP A 1 518  ? 73.440 74.567  -10.318 1.00 17.30 ? 518  ASP A N   1 
ATOM   4194 C  CA  . ASP A 1 518  ? 73.136 75.300  -9.112  1.00 17.36 ? 518  ASP A CA  1 
ATOM   4195 C  C   . ASP A 1 518  ? 71.715 74.843  -8.773  1.00 16.26 ? 518  ASP A C   1 
ATOM   4196 O  O   . ASP A 1 518  ? 70.774 75.128  -9.513  1.00 15.76 ? 518  ASP A O   1 
ATOM   4197 C  CB  . ASP A 1 518  ? 73.188 76.790  -9.424  1.00 18.56 ? 518  ASP A CB  1 
ATOM   4198 C  CG  . ASP A 1 518  ? 72.667 77.661  -8.305  1.00 21.30 ? 518  ASP A CG  1 
ATOM   4199 O  OD1 . ASP A 1 518  ? 72.082 77.154  -7.314  1.00 20.58 ? 518  ASP A OD1 1 
ATOM   4200 O  OD2 . ASP A 1 518  ? 72.768 78.906  -8.375  1.00 23.71 ? 518  ASP A OD2 1 
ATOM   4201 N  N   . PHE A 1 519  ? 71.575 74.149  -7.653  1.00 16.01 ? 519  PHE A N   1 
ATOM   4202 C  CA  . PHE A 1 519  ? 70.292 73.509  -7.333  1.00 15.85 ? 519  PHE A CA  1 
ATOM   4203 C  C   . PHE A 1 519  ? 69.193 74.485  -6.930  1.00 16.77 ? 519  PHE A C   1 
ATOM   4204 O  O   . PHE A 1 519  ? 68.041 74.074  -6.764  1.00 17.91 ? 519  PHE A O   1 
ATOM   4205 C  CB  . PHE A 1 519  ? 70.492 72.429  -6.281  1.00 15.76 ? 519  PHE A CB  1 
ATOM   4206 C  CG  . PHE A 1 519  ? 71.358 71.283  -6.728  1.00 15.52 ? 519  PHE A CG  1 
ATOM   4207 C  CD1 . PHE A 1 519  ? 71.081 70.578  -7.911  1.00 16.02 ? 519  PHE A CD1 1 
ATOM   4208 C  CD2 . PHE A 1 519  ? 72.438 70.890  -5.951  1.00 17.81 ? 519  PHE A CD2 1 
ATOM   4209 C  CE1 . PHE A 1 519  ? 71.871 69.527  -8.317  1.00 16.75 ? 519  PHE A CE1 1 
ATOM   4210 C  CE2 . PHE A 1 519  ? 73.238 69.841  -6.346  1.00 17.28 ? 519  PHE A CE2 1 
ATOM   4211 C  CZ  . PHE A 1 519  ? 72.951 69.133  -7.527  1.00 17.90 ? 519  PHE A CZ  1 
ATOM   4212 N  N   . SER A 1 520  ? 69.528 75.763  -6.785  1.00 16.57 ? 520  SER A N   1 
ATOM   4213 C  CA  . SER A 1 520  ? 68.561 76.811  -6.487  1.00 18.26 ? 520  SER A CA  1 
ATOM   4214 C  C   . SER A 1 520  ? 68.131 77.602  -7.747  1.00 17.52 ? 520  SER A C   1 
ATOM   4215 O  O   . SER A 1 520  ? 67.168 78.369  -7.700  1.00 18.43 ? 520  SER A O   1 
ATOM   4216 C  CB  . SER A 1 520  ? 69.145 77.773  -5.438  1.00 18.79 ? 520  SER A CB  1 
ATOM   4217 O  OG  . SER A 1 520  ? 70.061 78.689  -6.017  1.00 23.20 ? 520  SER A OG  1 
ATOM   4218 N  N   . PHE A 1 521  ? 68.829 77.387  -8.870  1.00 16.81 ? 521  PHE A N   1 
ATOM   4219 C  CA  . PHE A 1 521  ? 68.637 78.195  -10.079 1.00 16.66 ? 521  PHE A CA  1 
ATOM   4220 C  C   . PHE A 1 521  ? 67.512 77.661  -10.979 1.00 15.82 ? 521  PHE A C   1 
ATOM   4221 O  O   . PHE A 1 521  ? 67.305 76.445  -11.043 1.00 15.98 ? 521  PHE A O   1 
ATOM   4222 C  CB  . PHE A 1 521  ? 69.950 78.202  -10.865 1.00 17.86 ? 521  PHE A CB  1 
ATOM   4223 C  CG  . PHE A 1 521  ? 69.951 79.152  -12.025 1.00 18.83 ? 521  PHE A CG  1 
ATOM   4224 C  CD1 . PHE A 1 521  ? 70.094 80.526  -11.823 1.00 22.78 ? 521  PHE A CD1 1 
ATOM   4225 C  CD2 . PHE A 1 521  ? 69.818 78.680  -13.328 1.00 19.91 ? 521  PHE A CD2 1 
ATOM   4226 C  CE1 . PHE A 1 521  ? 70.083 81.414  -12.913 1.00 25.14 ? 521  PHE A CE1 1 
ATOM   4227 C  CE2 . PHE A 1 521  ? 69.800 79.558  -14.417 1.00 21.41 ? 521  PHE A CE2 1 
ATOM   4228 C  CZ  . PHE A 1 521  ? 69.944 80.923  -14.209 1.00 22.69 ? 521  PHE A CZ  1 
ATOM   4229 N  N   . SER A 1 522  ? 66.824 78.567  -11.674 1.00 15.93 ? 522  SER A N   1 
ATOM   4230 C  CA  . SER A 1 522  ? 65.796 78.209  -12.643 1.00 16.45 ? 522  SER A CA  1 
ATOM   4231 C  C   . SER A 1 522  ? 66.398 78.134  -14.043 1.00 14.60 ? 522  SER A C   1 
ATOM   4232 O  O   . SER A 1 522  ? 66.510 79.153  -14.721 1.00 16.40 ? 522  SER A O   1 
ATOM   4233 C  CB  . SER A 1 522  ? 64.676 79.252  -12.637 1.00 18.26 ? 522  SER A CB  1 
ATOM   4234 O  OG  . SER A 1 522  ? 63.949 79.149  -11.422 1.00 25.05 ? 522  SER A OG  1 
ATOM   4235 N  N   . TYR A 1 523  ? 66.777 76.938  -14.465 1.00 12.29 ? 523  TYR A N   1 
ATOM   4236 C  CA  . TYR A 1 523  ? 67.248 76.714  -15.840 1.00 11.54 ? 523  TYR A CA  1 
ATOM   4237 C  C   . TYR A 1 523  ? 66.122 76.803  -16.861 1.00 11.31 ? 523  TYR A C   1 
ATOM   4238 O  O   . TYR A 1 523  ? 66.337 77.230  -18.003 1.00 10.85 ? 523  TYR A O   1 
ATOM   4239 C  CB  . TYR A 1 523  ? 67.937 75.350  -15.955 1.00 11.94 ? 523  TYR A CB  1 
ATOM   4240 C  CG  . TYR A 1 523  ? 69.214 75.335  -15.158 1.00 12.87 ? 523  TYR A CG  1 
ATOM   4241 C  CD1 . TYR A 1 523  ? 70.388 75.926  -15.670 1.00 14.51 ? 523  TYR A CD1 1 
ATOM   4242 C  CD2 . TYR A 1 523  ? 69.244 74.789  -13.878 1.00 13.88 ? 523  TYR A CD2 1 
ATOM   4243 C  CE1 . TYR A 1 523  ? 71.559 75.948  -14.910 1.00 16.15 ? 523  TYR A CE1 1 
ATOM   4244 C  CE2 . TYR A 1 523  ? 70.416 74.792  -13.126 1.00 15.02 ? 523  TYR A CE2 1 
ATOM   4245 C  CZ  . TYR A 1 523  ? 71.545 75.392  -13.642 1.00 16.22 ? 523  TYR A CZ  1 
ATOM   4246 O  OH  . TYR A 1 523  ? 72.688 75.399  -12.881 1.00 17.05 ? 523  TYR A OH  1 
ATOM   4247 N  N   . PHE A 1 524  ? 64.918 76.391  -16.449 1.00 10.63 ? 524  PHE A N   1 
ATOM   4248 C  CA  . PHE A 1 524  ? 63.726 76.437  -17.289 1.00 9.96  ? 524  PHE A CA  1 
ATOM   4249 C  C   . PHE A 1 524  ? 62.583 76.923  -16.456 1.00 11.48 ? 524  PHE A C   1 
ATOM   4250 O  O   . PHE A 1 524  ? 62.547 76.684  -15.245 1.00 11.90 ? 524  PHE A O   1 
ATOM   4251 C  CB  . PHE A 1 524  ? 63.352 75.049  -17.832 1.00 9.96  ? 524  PHE A CB  1 
ATOM   4252 C  CG  . PHE A 1 524  ? 64.397 74.427  -18.712 1.00 9.40  ? 524  PHE A CG  1 
ATOM   4253 C  CD1 . PHE A 1 524  ? 65.402 73.654  -18.125 1.00 10.75 ? 524  PHE A CD1 1 
ATOM   4254 C  CD2 . PHE A 1 524  ? 64.351 74.542  -20.109 1.00 10.68 ? 524  PHE A CD2 1 
ATOM   4255 C  CE1 . PHE A 1 524  ? 66.361 73.056  -18.892 1.00 11.04 ? 524  PHE A CE1 1 
ATOM   4256 C  CE2 . PHE A 1 524  ? 65.303 73.922  -20.901 1.00 10.35 ? 524  PHE A CE2 1 
ATOM   4257 C  CZ  . PHE A 1 524  ? 66.323 73.181  -20.275 1.00 11.20 ? 524  PHE A CZ  1 
ATOM   4258 N  N   . THR A 1 525  ? 61.648 77.567  -17.120 1.00 11.91 ? 525  THR A N   1 
ATOM   4259 C  CA  . THR A 1 525  ? 60.343 77.764  -16.492 1.00 13.30 ? 525  THR A CA  1 
ATOM   4260 C  C   . THR A 1 525  ? 59.294 76.966  -17.252 1.00 12.64 ? 525  THR A C   1 
ATOM   4261 O  O   . THR A 1 525  ? 59.361 76.821  -18.486 1.00 13.01 ? 525  THR A O   1 
ATOM   4262 C  CB  . THR A 1 525  ? 59.946 79.227  -16.476 1.00 15.54 ? 525  THR A CB  1 
ATOM   4263 O  OG1 . THR A 1 525  ? 59.855 79.687  -17.805 1.00 18.28 ? 525  THR A OG1 1 
ATOM   4264 C  CG2 . THR A 1 525  ? 61.051 80.141  -15.865 1.00 17.76 ? 525  THR A CG2 1 
ATOM   4265 N  N   . LEU A 1 526  ? 58.313 76.464  -16.521 1.00 11.65 ? 526  LEU A N   1 
ATOM   4266 C  CA  . LEU A 1 526  ? 57.207 75.762  -17.154 1.00 13.03 ? 526  LEU A CA  1 
ATOM   4267 C  C   . LEU A 1 526  ? 56.277 76.765  -17.819 1.00 12.87 ? 526  LEU A C   1 
ATOM   4268 O  O   . LEU A 1 526  ? 56.008 77.848  -17.282 1.00 15.21 ? 526  LEU A O   1 
ATOM   4269 C  CB  . LEU A 1 526  ? 56.400 74.938  -16.141 1.00 14.52 ? 526  LEU A CB  1 
ATOM   4270 C  CG  . LEU A 1 526  ? 56.944 73.578  -15.725 1.00 17.03 ? 526  LEU A CG  1 
ATOM   4271 C  CD1 . LEU A 1 526  ? 56.137 73.114  -14.501 1.00 19.00 ? 526  LEU A CD1 1 
ATOM   4272 C  CD2 . LEU A 1 526  ? 56.815 72.590  -16.873 1.00 18.08 ? 526  LEU A CD2 1 
ATOM   4273 N  N   . ASP A 1 527  ? 55.720 76.369  -18.949 1.00 10.34 ? 527  ASP A N   1 
ATOM   4274 C  CA  . ASP A 1 527  ? 54.715 77.149  -19.647 1.00 12.58 ? 527  ASP A CA  1 
ATOM   4275 C  C   . ASP A 1 527  ? 53.487 76.267  -19.700 1.00 11.71 ? 527  ASP A C   1 
ATOM   4276 O  O   . ASP A 1 527  ? 53.541 75.167  -20.212 1.00 14.12 ? 527  ASP A O   1 
ATOM   4277 C  CB  . ASP A 1 527  ? 55.189 77.525  -21.069 1.00 12.09 ? 527  ASP A CB  1 
ATOM   4278 C  CG  . ASP A 1 527  ? 54.161 78.350  -21.814 1.00 15.43 ? 527  ASP A CG  1 
ATOM   4279 O  OD1 . ASP A 1 527  ? 53.885 79.484  -21.386 1.00 17.57 ? 527  ASP A OD1 1 
ATOM   4280 O  OD2 . ASP A 1 527  ? 53.562 77.926  -22.829 1.00 19.28 ? 527  ASP A OD2 1 
ATOM   4281 N  N   . ASP A 1 528  ? 52.389 76.737  -19.124 1.00 11.49 ? 528  ASP A N   1 
ATOM   4282 C  CA  . ASP A 1 528  ? 51.177 75.930  -19.128 1.00 12.13 ? 528  ASP A CA  1 
ATOM   4283 C  C   . ASP A 1 528  ? 50.065 76.772  -19.745 1.00 12.27 ? 528  ASP A C   1 
ATOM   4284 O  O   . ASP A 1 528  ? 49.711 77.811  -19.204 1.00 12.75 ? 528  ASP A O   1 
ATOM   4285 C  CB  . ASP A 1 528  ? 50.844 75.524  -17.692 1.00 11.94 ? 528  ASP A CB  1 
ATOM   4286 C  CG  . ASP A 1 528  ? 49.785 74.470  -17.621 1.00 12.65 ? 528  ASP A CG  1 
ATOM   4287 O  OD1 . ASP A 1 528  ? 48.763 74.542  -18.331 1.00 12.38 ? 528  ASP A OD1 1 
ATOM   4288 O  OD2 . ASP A 1 528  ? 49.936 73.494  -16.852 1.00 13.37 ? 528  ASP A OD2 1 
ATOM   4289 N  N   . SER A 1 529  ? 49.517 76.301  -20.857 1.00 13.28 ? 529  SER A N   1 
ATOM   4290 C  CA  . SER A 1 529  ? 48.487 77.030  -21.600 1.00 14.30 ? 529  SER A CA  1 
ATOM   4291 C  C   . SER A 1 529  ? 47.107 76.893  -21.019 1.00 14.31 ? 529  SER A C   1 
ATOM   4292 O  O   . SER A 1 529  ? 46.203 77.596  -21.454 1.00 16.64 ? 529  SER A O   1 
ATOM   4293 C  CB  . SER A 1 529  ? 48.375 76.542  -23.051 1.00 16.23 ? 529  SER A CB  1 
ATOM   4294 O  OG  . SER A 1 529  ? 49.604 76.564  -23.713 1.00 21.14 ? 529  SER A OG  1 
ATOM   4295 N  N   . ARG A 1 530  ? 46.901 75.976  -20.080 1.00 12.63 ? 530  ARG A N   1 
ATOM   4296 C  CA  . ARG A 1 530  ? 45.546 75.704  -19.602 1.00 13.06 ? 530  ARG A CA  1 
ATOM   4297 C  C   . ARG A 1 530  ? 45.392 75.781  -18.120 1.00 13.25 ? 530  ARG A C   1 
ATOM   4298 O  O   . ARG A 1 530  ? 44.354 75.358  -17.591 1.00 15.97 ? 530  ARG A O   1 
ATOM   4299 C  CB  . ARG A 1 530  ? 45.072 74.322  -20.077 1.00 13.04 ? 530  ARG A CB  1 
ATOM   4300 C  CG  . ARG A 1 530  ? 45.014 74.248  -21.612 1.00 14.06 ? 530  ARG A CG  1 
ATOM   4301 C  CD  . ARG A 1 530  ? 44.348 73.016  -22.199 1.00 13.18 ? 530  ARG A CD  1 
ATOM   4302 N  NE  . ARG A 1 530  ? 45.028 71.821  -21.713 1.00 14.36 ? 530  ARG A NE  1 
ATOM   4303 C  CZ  . ARG A 1 530  ? 44.849 70.610  -22.222 1.00 15.81 ? 530  ARG A CZ  1 
ATOM   4304 N  NH1 . ARG A 1 530  ? 44.006 70.408  -23.236 1.00 19.76 ? 530  ARG A NH1 1 
ATOM   4305 N  NH2 . ARG A 1 530  ? 45.509 69.609  -21.701 1.00 15.37 ? 530  ARG A NH2 1 
ATOM   4306 N  N   . TRP A 1 531  ? 46.410 76.259  -17.422 1.00 10.68 ? 531  TRP A N   1 
ATOM   4307 C  CA  . TRP A 1 531  ? 46.267 76.484  -15.983 1.00 11.08 ? 531  TRP A CA  1 
ATOM   4308 C  C   . TRP A 1 531  ? 47.192 77.620  -15.550 1.00 11.63 ? 531  TRP A C   1 
ATOM   4309 O  O   . TRP A 1 531  ? 48.392 77.534  -15.811 1.00 12.42 ? 531  TRP A O   1 
ATOM   4310 C  CB  . TRP A 1 531  ? 46.619 75.230  -15.141 1.00 12.54 ? 531  TRP A CB  1 
ATOM   4311 C  CG  . TRP A 1 531  ? 46.515 75.590  -13.686 1.00 13.38 ? 531  TRP A CG  1 
ATOM   4312 C  CD1 . TRP A 1 531  ? 47.551 76.026  -12.859 1.00 15.37 ? 531  TRP A CD1 1 
ATOM   4313 C  CD2 . TRP A 1 531  ? 45.332 75.689  -12.936 1.00 14.49 ? 531  TRP A CD2 1 
ATOM   4314 N  NE1 . TRP A 1 531  ? 47.049 76.335  -11.621 1.00 18.06 ? 531  TRP A NE1 1 
ATOM   4315 C  CE2 . TRP A 1 531  ? 45.692 76.148  -11.631 1.00 12.91 ? 531  TRP A CE2 1 
ATOM   4316 C  CE3 . TRP A 1 531  ? 44.011 75.413  -13.209 1.00 14.21 ? 531  TRP A CE3 1 
ATOM   4317 C  CZ2 . TRP A 1 531  ? 44.738 76.338  -10.598 1.00 15.67 ? 531  TRP A CZ2 1 
ATOM   4318 C  CZ3 . TRP A 1 531  ? 43.067 75.608  -12.204 1.00 15.03 ? 531  TRP A CZ3 1 
ATOM   4319 C  CH2 . TRP A 1 531  ? 43.440 76.061  -10.908 1.00 15.29 ? 531  TRP A CH2 1 
ATOM   4320 N  N   . PRO A 1 532  ? 46.690 78.608  -14.809 1.00 12.01 ? 532  PRO A N   1 
ATOM   4321 C  CA  . PRO A 1 532  ? 45.266 78.796  -14.455 1.00 12.61 ? 532  PRO A CA  1 
ATOM   4322 C  C   . PRO A 1 532  ? 44.389 79.105  -15.654 1.00 13.28 ? 532  PRO A C   1 
ATOM   4323 O  O   . PRO A 1 532  ? 43.165 78.969  -15.581 1.00 14.44 ? 532  PRO A O   1 
ATOM   4324 C  CB  . PRO A 1 532  ? 45.324 80.013  -13.498 1.00 12.98 ? 532  PRO A CB  1 
ATOM   4325 C  CG  . PRO A 1 532  ? 46.708 79.910  -12.901 1.00 15.61 ? 532  PRO A CG  1 
ATOM   4326 C  CD  . PRO A 1 532  ? 47.557 79.597  -14.124 1.00 12.68 ? 532  PRO A CD  1 
ATOM   4327 N  N   . GLY A 1 533  ? 45.005 79.484  -16.764 1.00 14.38 ? 533  GLY A N   1 
ATOM   4328 C  CA  . GLY A 1 533  ? 44.260 79.714  -17.981 1.00 17.36 ? 533  GLY A CA  1 
ATOM   4329 C  C   . GLY A 1 533  ? 44.146 81.154  -18.376 1.00 20.01 ? 533  GLY A C   1 
ATOM   4330 O  O   . GLY A 1 533  ? 44.227 82.071  -17.534 1.00 19.15 ? 533  GLY A O   1 
ATOM   4331 N  N   . SER A 1 534  ? 43.975 81.315  -19.691 1.00 22.36 ? 534  SER A N   1 
ATOM   4332 C  CA  . SER A 1 534  ? 43.713 82.601  -20.313 1.00 24.61 ? 534  SER A CA  1 
ATOM   4333 C  C   . SER A 1 534  ? 42.445 83.156  -19.704 1.00 24.44 ? 534  SER A C   1 
ATOM   4334 O  O   . SER A 1 534  ? 41.398 82.474  -19.659 1.00 24.64 ? 534  SER A O   1 
ATOM   4335 C  CB  . SER A 1 534  ? 43.542 82.443  -21.827 1.00 25.81 ? 534  SER A CB  1 
ATOM   4336 O  OG  . SER A 1 534  ? 43.372 83.705  -22.448 1.00 30.37 ? 534  SER A OG  1 
ATOM   4337 N  N   . GLY A 1 535  ? 42.536 84.384  -19.218 1.00 24.37 ? 535  GLY A N   1 
ATOM   4338 C  CA  . GLY A 1 535  ? 41.390 85.016  -18.599 1.00 23.88 ? 535  GLY A CA  1 
ATOM   4339 C  C   . GLY A 1 535  ? 41.243 84.705  -17.125 1.00 23.85 ? 535  GLY A C   1 
ATOM   4340 O  O   . GLY A 1 535  ? 40.362 85.247  -16.450 1.00 24.50 ? 535  GLY A O   1 
ATOM   4341 N  N   . VAL A 1 536  ? 42.087 83.811  -16.609 1.00 23.02 ? 536  VAL A N   1 
ATOM   4342 C  CA  . VAL A 1 536  ? 42.059 83.501  -15.184 1.00 23.26 ? 536  VAL A CA  1 
ATOM   4343 C  C   . VAL A 1 536  ? 43.222 84.206  -14.493 1.00 24.71 ? 536  VAL A C   1 
ATOM   4344 O  O   . VAL A 1 536  ? 43.020 84.958  -13.538 1.00 24.03 ? 536  VAL A O   1 
ATOM   4345 C  CB  . VAL A 1 536  ? 42.088 81.977  -14.917 1.00 22.84 ? 536  VAL A CB  1 
ATOM   4346 C  CG1 . VAL A 1 536  ? 41.951 81.688  -13.422 1.00 22.73 ? 536  VAL A CG1 1 
ATOM   4347 C  CG2 . VAL A 1 536  ? 40.949 81.285  -15.673 1.00 23.06 ? 536  VAL A CG2 1 
ATOM   4348 N  N   . GLU A 1 537  ? 44.433 83.966  -14.985 1.00 25.48 ? 537  GLU A N   1 
ATOM   4349 C  CA  . GLU A 1 537  ? 45.631 84.633  -14.480 1.00 27.47 ? 537  GLU A CA  1 
ATOM   4350 C  C   . GLU A 1 537  ? 46.547 84.923  -15.656 1.00 28.16 ? 537  GLU A C   1 
ATOM   4351 O  O   . GLU A 1 537  ? 46.735 84.069  -16.531 1.00 28.21 ? 537  GLU A O   1 
ATOM   4352 C  CB  . GLU A 1 537  ? 46.345 83.729  -13.485 1.00 27.83 ? 537  GLU A CB  1 
ATOM   4353 C  CG  . GLU A 1 537  ? 47.639 84.272  -12.899 1.00 31.47 ? 537  GLU A CG  1 
ATOM   4354 C  CD  . GLU A 1 537  ? 48.141 83.407  -11.762 1.00 35.11 ? 537  GLU A CD  1 
ATOM   4355 O  OE1 . GLU A 1 537  ? 47.433 83.316  -10.729 1.00 36.79 ? 537  GLU A OE1 1 
ATOM   4356 O  OE2 . GLU A 1 537  ? 49.237 82.808  -11.895 1.00 37.46 ? 537  GLU A OE2 1 
ATOM   4357 N  N   . ASP A 1 538  ? 47.117 86.124  -15.675 1.00 29.16 ? 538  ASP A N   1 
ATOM   4358 C  CA  . ASP A 1 538  ? 48.161 86.434  -16.645 1.00 30.72 ? 538  ASP A CA  1 
ATOM   4359 C  C   . ASP A 1 538  ? 49.462 85.889  -16.049 1.00 30.25 ? 538  ASP A C   1 
ATOM   4360 O  O   . ASP A 1 538  ? 50.145 86.566  -15.278 1.00 31.17 ? 538  ASP A O   1 
ATOM   4361 C  CB  . ASP A 1 538  ? 48.227 87.952  -16.883 1.00 31.67 ? 538  ASP A CB  1 
ATOM   4362 C  CG  . ASP A 1 538  ? 48.735 88.302  -18.265 1.00 34.74 ? 538  ASP A CG  1 
ATOM   4363 O  OD1 . ASP A 1 538  ? 49.826 87.812  -18.637 1.00 37.89 ? 538  ASP A OD1 1 
ATOM   4364 O  OD2 . ASP A 1 538  ? 48.120 89.064  -19.056 1.00 38.87 ? 538  ASP A OD2 1 
ATOM   4365 N  N   . SER A 1 539  ? 49.781 84.637  -16.361 1.00 29.01 ? 539  SER A N   1 
ATOM   4366 C  CA  . SER A 1 539  ? 50.914 83.974  -15.709 1.00 28.47 ? 539  SER A CA  1 
ATOM   4367 C  C   . SER A 1 539  ? 52.004 83.559  -16.694 1.00 27.25 ? 539  SER A C   1 
ATOM   4368 O  O   . SER A 1 539  ? 53.153 83.356  -16.293 1.00 28.32 ? 539  SER A O   1 
ATOM   4369 C  CB  . SER A 1 539  ? 50.452 82.759  -14.889 1.00 28.40 ? 539  SER A CB  1 
ATOM   4370 O  OG  . SER A 1 539  ? 49.902 81.750  -15.726 1.00 30.73 ? 539  SER A OG  1 
ATOM   4371 N  N   . ARG A 1 540  ? 51.635 83.431  -17.970 1.00 25.14 ? 540  ARG A N   1 
ATOM   4372 C  CA  . ARG A 1 540  ? 52.539 82.899  -18.987 1.00 23.18 ? 540  ARG A CA  1 
ATOM   4373 C  C   . ARG A 1 540  ? 53.622 83.886  -19.333 1.00 22.41 ? 540  ARG A C   1 
ATOM   4374 O  O   . ARG A 1 540  ? 53.354 85.076  -19.455 1.00 22.99 ? 540  ARG A O   1 
ATOM   4375 C  CB  . ARG A 1 540  ? 51.755 82.516  -20.229 1.00 22.62 ? 540  ARG A CB  1 
ATOM   4376 C  CG  . ARG A 1 540  ? 50.946 81.242  -19.987 1.00 20.28 ? 540  ARG A CG  1 
ATOM   4377 C  CD  . ARG A 1 540  ? 50.195 80.786  -21.177 1.00 17.81 ? 540  ARG A CD  1 
ATOM   4378 N  NE  . ARG A 1 540  ? 51.084 80.136  -22.132 1.00 15.97 ? 540  ARG A NE  1 
ATOM   4379 C  CZ  . ARG A 1 540  ? 50.684 79.733  -23.326 1.00 17.72 ? 540  ARG A CZ  1 
ATOM   4380 N  NH1 . ARG A 1 540  ? 49.425 79.917  -23.719 1.00 16.96 ? 540  ARG A NH1 1 
ATOM   4381 N  NH2 . ARG A 1 540  ? 51.536 79.138  -24.125 1.00 17.38 ? 540  ARG A NH2 1 
ATOM   4382 N  N   . THR A 1 541  ? 54.847 83.390  -19.469 1.00 21.65 ? 541  THR A N   1 
ATOM   4383 C  CA  . THR A 1 541  ? 55.919 84.263  -19.903 1.00 21.20 ? 541  THR A CA  1 
ATOM   4384 C  C   . THR A 1 541  ? 55.953 84.300  -21.422 1.00 19.51 ? 541  THR A C   1 
ATOM   4385 O  O   . THR A 1 541  ? 55.711 83.301  -22.102 1.00 21.54 ? 541  THR A O   1 
ATOM   4386 C  CB  . THR A 1 541  ? 57.277 83.819  -19.367 1.00 22.35 ? 541  THR A CB  1 
ATOM   4387 O  OG1 . THR A 1 541  ? 57.675 82.641  -20.051 1.00 24.85 ? 541  THR A OG1 1 
ATOM   4388 C  CG2 . THR A 1 541  ? 57.197 83.381  -17.907 1.00 21.68 ? 541  THR A CG2 1 
ATOM   4389 N  N   . THR A 1 542  ? 56.240 85.481  -21.938 1.00 17.05 ? 542  THR A N   1 
ATOM   4390 C  CA  . THR A 1 542  ? 56.495 85.661  -23.355 1.00 15.47 ? 542  THR A CA  1 
ATOM   4391 C  C   . THR A 1 542  ? 57.967 85.393  -23.635 1.00 14.08 ? 542  THR A C   1 
ATOM   4392 O  O   . THR A 1 542  ? 58.861 85.862  -22.893 1.00 14.90 ? 542  THR A O   1 
ATOM   4393 C  CB  . THR A 1 542  ? 56.193 87.099  -23.708 1.00 15.90 ? 542  THR A CB  1 
ATOM   4394 O  OG1 . THR A 1 542  ? 54.827 87.373  -23.381 1.00 17.81 ? 542  THR A OG1 1 
ATOM   4395 C  CG2 . THR A 1 542  ? 56.314 87.350  -25.206 1.00 16.40 ? 542  THR A CG2 1 
ATOM   4396 N  N   . ILE A 1 543  ? 58.229 84.650  -24.700 1.00 12.75 ? 543  ILE A N   1 
ATOM   4397 C  CA  . ILE A 1 543  ? 59.584 84.469  -25.185 1.00 12.49 ? 543  ILE A CA  1 
ATOM   4398 C  C   . ILE A 1 543  ? 59.943 85.736  -25.965 1.00 12.82 ? 543  ILE A C   1 
ATOM   4399 O  O   . ILE A 1 543  ? 59.317 86.058  -26.987 1.00 12.79 ? 543  ILE A O   1 
ATOM   4400 C  CB  . ILE A 1 543  ? 59.677 83.221  -26.056 1.00 12.06 ? 543  ILE A CB  1 
ATOM   4401 C  CG1 . ILE A 1 543  ? 59.360 81.952  -25.199 1.00 12.27 ? 543  ILE A CG1 1 
ATOM   4402 C  CG2 . ILE A 1 543  ? 61.055 83.171  -26.750 1.00 12.61 ? 543  ILE A CG2 1 
ATOM   4403 C  CD1 . ILE A 1 543  ? 59.313 80.666  -25.966 1.00 12.77 ? 543  ILE A CD1 1 
ATOM   4404 N  N   . ILE A 1 544  ? 60.897 86.471  -25.407 1.00 13.30 ? 544  ILE A N   1 
ATOM   4405 C  CA  . ILE A 1 544  ? 61.278 87.775  -25.963 1.00 14.67 ? 544  ILE A CA  1 
ATOM   4406 C  C   . ILE A 1 544  ? 62.505 87.613  -26.847 1.00 14.09 ? 544  ILE A C   1 
ATOM   4407 O  O   . ILE A 1 544  ? 63.607 87.273  -26.389 1.00 14.15 ? 544  ILE A O   1 
ATOM   4408 C  CB  . ILE A 1 544  ? 61.501 88.784  -24.830 1.00 15.25 ? 544  ILE A CB  1 
ATOM   4409 C  CG1 . ILE A 1 544  ? 60.185 89.004  -24.068 1.00 18.03 ? 544  ILE A CG1 1 
ATOM   4410 C  CG2 . ILE A 1 544  ? 62.014 90.112  -25.378 1.00 17.72 ? 544  ILE A CG2 1 
ATOM   4411 C  CD1 . ILE A 1 544  ? 60.271 90.004  -22.906 1.00 19.30 ? 544  ILE A CD1 1 
ATOM   4412 N  N   . LEU A 1 545  ? 62.244 87.777  -28.134 1.00 13.87 ? 545  LEU A N   1 
ATOM   4413 C  CA  . LEU A 1 545  ? 63.265 87.677  -29.164 1.00 14.05 ? 545  LEU A CA  1 
ATOM   4414 C  C   . LEU A 1 545  ? 63.401 89.028  -29.858 1.00 15.11 ? 545  LEU A C   1 
ATOM   4415 O  O   . LEU A 1 545  ? 62.458 89.816  -29.902 1.00 16.00 ? 545  LEU A O   1 
ATOM   4416 C  CB  . LEU A 1 545  ? 62.886 86.595  -30.194 1.00 14.03 ? 545  LEU A CB  1 
ATOM   4417 C  CG  . LEU A 1 545  ? 62.700 85.162  -29.659 1.00 14.94 ? 545  LEU A CG  1 
ATOM   4418 C  CD1 . LEU A 1 545  ? 62.291 84.199  -30.758 1.00 16.29 ? 545  LEU A CD1 1 
ATOM   4419 C  CD2 . LEU A 1 545  ? 63.957 84.652  -28.993 1.00 14.54 ? 545  LEU A CD2 1 
ATOM   4420 N  N   . GLY A 1 546  ? 64.563 89.276  -30.438 1.00 15.65 ? 546  GLY A N   1 
ATOM   4421 C  CA  . GLY A 1 546  ? 64.786 90.534  -31.125 1.00 16.47 ? 546  GLY A CA  1 
ATOM   4422 C  C   . GLY A 1 546  ? 66.208 90.590  -31.604 1.00 16.27 ? 546  GLY A C   1 
ATOM   4423 O  O   . GLY A 1 546  ? 67.125 90.086  -30.939 1.00 14.58 ? 546  GLY A O   1 
ATOM   4424 N  N   . GLU A 1 547  ? 66.398 91.251  -32.738 1.00 17.82 ? 547  GLU A N   1 
ATOM   4425 C  CA  . GLU A 1 547  ? 67.724 91.367  -33.348 1.00 20.28 ? 547  GLU A CA  1 
ATOM   4426 C  C   . GLU A 1 547  ? 68.749 92.009  -32.413 1.00 20.19 ? 547  GLU A C   1 
ATOM   4427 O  O   . GLU A 1 547  ? 69.931 91.668  -32.446 1.00 21.66 ? 547  GLU A O   1 
ATOM   4428 C  CB  . GLU A 1 547  ? 67.623 92.189  -34.627 1.00 21.74 ? 547  GLU A CB  1 
ATOM   4429 C  CG  . GLU A 1 547  ? 68.931 92.272  -35.404 1.00 27.98 ? 547  GLU A CG  1 
ATOM   4430 C  CD  . GLU A 1 547  ? 68.849 93.216  -36.589 1.00 33.45 ? 547  GLU A CD  1 
ATOM   4431 O  OE1 . GLU A 1 547  ? 67.717 93.522  -37.035 1.00 37.29 ? 547  GLU A OE1 1 
ATOM   4432 O  OE2 . GLU A 1 547  ? 69.918 93.655  -37.078 1.00 37.10 ? 547  GLU A OE2 1 
ATOM   4433 N  N   . ASP A 1 548  ? 68.284 92.936  -31.579 1.00 19.46 ? 548  ASP A N   1 
ATOM   4434 C  CA  . ASP A 1 548  ? 69.174 93.650  -30.662 1.00 20.04 ? 548  ASP A CA  1 
ATOM   4435 C  C   . ASP A 1 548  ? 69.154 93.082  -29.249 1.00 20.25 ? 548  ASP A C   1 
ATOM   4436 O  O   . ASP A 1 548  ? 69.651 93.719  -28.309 1.00 21.61 ? 548  ASP A O   1 
ATOM   4437 C  CB  . ASP A 1 548  ? 68.810 95.134  -30.624 1.00 20.39 ? 548  ASP A CB  1 
ATOM   4438 C  CG  . ASP A 1 548  ? 69.016 95.817  -31.949 1.00 22.09 ? 548  ASP A CG  1 
ATOM   4439 O  OD1 . ASP A 1 548  ? 70.179 95.934  -32.383 1.00 26.71 ? 548  ASP A OD1 1 
ATOM   4440 O  OD2 . ASP A 1 548  ? 68.076 96.282  -32.618 1.00 26.01 ? 548  ASP A OD2 1 
ATOM   4441 N  N   . ILE A 1 549  ? 68.612 91.874  -29.085 1.00 18.84 ? 549  ILE A N   1 
ATOM   4442 C  CA  . ILE A 1 549  ? 68.592 91.262  -27.748 1.00 19.01 ? 549  ILE A CA  1 
ATOM   4443 C  C   . ILE A 1 549  ? 68.871 89.762  -27.746 1.00 17.84 ? 549  ILE A C   1 
ATOM   4444 O  O   . ILE A 1 549  ? 69.702 89.304  -26.964 1.00 18.39 ? 549  ILE A O   1 
ATOM   4445 C  CB  . ILE A 1 549  ? 67.297 91.608  -26.942 1.00 18.42 ? 549  ILE A CB  1 
ATOM   4446 C  CG1 . ILE A 1 549  ? 67.425 91.113  -25.480 1.00 20.41 ? 549  ILE A CG1 1 
ATOM   4447 C  CG2 . ILE A 1 549  ? 66.012 91.145  -27.663 1.00 18.00 ? 549  ILE A CG2 1 
ATOM   4448 C  CD1 . ILE A 1 549  ? 66.263 91.444  -24.561 1.00 21.51 ? 549  ILE A CD1 1 
ATOM   4449 N  N   . LEU A 1 550  ? 68.192 89.021  -28.605 1.00 16.55 ? 550  LEU A N   1 
ATOM   4450 C  CA  . LEU A 1 550  ? 68.263 87.570  -28.542 1.00 15.46 ? 550  LEU A CA  1 
ATOM   4451 C  C   . LEU A 1 550  ? 67.585 86.966  -29.745 1.00 14.99 ? 550  LEU A C   1 
ATOM   4452 O  O   . LEU A 1 550  ? 66.404 87.141  -29.933 1.00 15.16 ? 550  LEU A O   1 
ATOM   4453 C  CB  . LEU A 1 550  ? 67.586 87.067  -27.264 1.00 16.30 ? 550  LEU A CB  1 
ATOM   4454 C  CG  . LEU A 1 550  ? 67.621 85.557  -27.024 1.00 16.22 ? 550  LEU A CG  1 
ATOM   4455 C  CD1 . LEU A 1 550  ? 69.043 85.094  -26.874 1.00 18.11 ? 550  LEU A CD1 1 
ATOM   4456 C  CD2 . LEU A 1 550  ? 66.793 85.193  -25.810 1.00 16.94 ? 550  LEU A CD2 1 
ATOM   4457 N  N   . PRO A 1 551  ? 68.330 86.248  -30.563 1.00 14.89 ? 551  PRO A N   1 
ATOM   4458 C  CA  . PRO A 1 551  ? 67.756 85.790  -31.824 1.00 15.21 ? 551  PRO A CA  1 
ATOM   4459 C  C   . PRO A 1 551  ? 66.905 84.531  -31.687 1.00 14.06 ? 551  PRO A C   1 
ATOM   4460 O  O   . PRO A 1 551  ? 66.034 84.319  -32.503 1.00 14.51 ? 551  PRO A O   1 
ATOM   4461 C  CB  . PRO A 1 551  ? 68.977 85.513  -32.710 1.00 15.90 ? 551  PRO A CB  1 
ATOM   4462 C  CG  . PRO A 1 551  ? 70.115 85.554  -31.871 1.00 18.29 ? 551  PRO A CG  1 
ATOM   4463 C  CD  . PRO A 1 551  ? 69.800 86.290  -30.615 1.00 16.01 ? 551  PRO A CD  1 
ATOM   4464 N  N   . SER A 1 552  ? 67.187 83.702  -30.689 1.00 13.26 ? 552  SER A N   1 
ATOM   4465 C  CA  . SER A 1 552  ? 66.541 82.403  -30.602 1.00 12.55 ? 552  SER A CA  1 
ATOM   4466 C  C   . SER A 1 552  ? 66.402 81.913  -29.166 1.00 11.69 ? 552  SER A C   1 
ATOM   4467 O  O   . SER A 1 552  ? 67.056 82.408  -28.275 1.00 11.69 ? 552  SER A O   1 
ATOM   4468 C  CB  . SER A 1 552  ? 67.297 81.373  -31.431 1.00 14.44 ? 552  SER A CB  1 
ATOM   4469 O  OG  . SER A 1 552  ? 68.528 81.040  -30.839 1.00 16.41 ? 552  SER A OG  1 
ATOM   4470 N  N   . LYS A 1 553  ? 65.528 80.929  -28.986 1.00 10.85 ? 553  LYS A N   1 
ATOM   4471 C  CA  . LYS A 1 553  ? 65.241 80.334  -27.676 1.00 10.52 ? 553  LYS A CA  1 
ATOM   4472 C  C   . LYS A 1 553  ? 64.983 78.820  -27.823 1.00 9.51  ? 553  LYS A C   1 
ATOM   4473 O  O   . LYS A 1 553  ? 64.192 78.391  -28.662 1.00 10.51 ? 553  LYS A O   1 
ATOM   4474 C  CB  . LYS A 1 553  ? 63.968 80.988  -27.106 1.00 11.09 ? 553  LYS A CB  1 
ATOM   4475 C  CG  . LYS A 1 553  ? 63.475 80.392  -25.768 1.00 12.86 ? 553  LYS A CG  1 
ATOM   4476 C  CD  . LYS A 1 553  ? 64.505 80.534  -24.690 1.00 13.44 ? 553  LYS A CD  1 
ATOM   4477 C  CE  . LYS A 1 553  ? 64.725 82.004  -24.260 1.00 15.63 ? 553  LYS A CE  1 
ATOM   4478 N  NZ  . LYS A 1 553  ? 65.926 82.121  -23.337 1.00 15.04 ? 553  LYS A NZ  1 
ATOM   4479 N  N   . HIS A 1 554  ? 65.642 78.040  -26.965 1.00 10.37 ? 554  HIS A N   1 
ATOM   4480 C  CA  . HIS A 1 554  ? 65.330 76.619  -26.812 1.00 9.88  ? 554  HIS A CA  1 
ATOM   4481 C  C   . HIS A 1 554  ? 64.117 76.391  -25.895 1.00 9.26  ? 554  HIS A C   1 
ATOM   4482 O  O   . HIS A 1 554  ? 63.978 77.029  -24.833 1.00 10.10 ? 554  HIS A O   1 
ATOM   4483 C  CB  . HIS A 1 554  ? 66.540 75.936  -26.181 1.00 12.04 ? 554  HIS A CB  1 
ATOM   4484 C  CG  . HIS A 1 554  ? 67.689 75.709  -27.120 1.00 14.02 ? 554  HIS A CG  1 
ATOM   4485 N  ND1 . HIS A 1 554  ? 68.230 76.712  -27.908 1.00 19.90 ? 554  HIS A ND1 1 
ATOM   4486 C  CD2 . HIS A 1 554  ? 68.387 74.591  -27.414 1.00 17.94 ? 554  HIS A CD2 1 
ATOM   4487 C  CE1 . HIS A 1 554  ? 69.238 76.222  -28.608 1.00 21.37 ? 554  HIS A CE1 1 
ATOM   4488 N  NE2 . HIS A 1 554  ? 69.361 74.941  -28.316 1.00 17.61 ? 554  HIS A NE2 1 
ATOM   4489 N  N   . VAL A 1 555  ? 63.265 75.473  -26.346 1.00 9.03  ? 555  VAL A N   1 
ATOM   4490 C  CA  . VAL A 1 555  ? 62.137 74.970  -25.552 1.00 9.26  ? 555  VAL A CA  1 
ATOM   4491 C  C   . VAL A 1 555  ? 62.247 73.446  -25.548 1.00 9.03  ? 555  VAL A C   1 
ATOM   4492 O  O   . VAL A 1 555  ? 62.756 72.838  -26.489 1.00 9.24  ? 555  VAL A O   1 
ATOM   4493 C  CB  . VAL A 1 555  ? 60.782 75.464  -26.081 1.00 9.47  ? 555  VAL A CB  1 
ATOM   4494 C  CG1 . VAL A 1 555  ? 60.700 76.990  -26.028 1.00 9.95  ? 555  VAL A CG1 1 
ATOM   4495 C  CG2 . VAL A 1 555  ? 60.525 74.985  -27.481 1.00 10.08 ? 555  VAL A CG2 1 
ATOM   4496 N  N   . VAL A 1 556  ? 61.732 72.820  -24.481 1.00 8.70  ? 556  VAL A N   1 
ATOM   4497 C  CA  . VAL A 1 556  ? 61.780 71.365  -24.308 1.00 7.74  ? 556  VAL A CA  1 
ATOM   4498 C  C   . VAL A 1 556  ? 60.378 70.890  -23.927 1.00 7.51  ? 556  VAL A C   1 
ATOM   4499 O  O   . VAL A 1 556  ? 59.738 71.490  -23.045 1.00 7.83  ? 556  VAL A O   1 
ATOM   4500 C  CB  . VAL A 1 556  ? 62.778 70.970  -23.216 1.00 8.17  ? 556  VAL A CB  1 
ATOM   4501 C  CG1 . VAL A 1 556  ? 62.710 69.475  -22.972 1.00 8.88  ? 556  VAL A CG1 1 
ATOM   4502 C  CG2 . VAL A 1 556  ? 64.188 71.411  -23.607 1.00 9.30  ? 556  VAL A CG2 1 
ATOM   4503 N  N   . MET A 1 557  ? 59.947 69.814  -24.561 1.00 7.62  ? 557  MET A N   1 
ATOM   4504 C  CA  . MET A 1 557  ? 58.709 69.130  -24.182 1.00 7.22  ? 557  MET A CA  1 
ATOM   4505 C  C   . MET A 1 557  ? 58.991 67.807  -23.511 1.00 8.11  ? 557  MET A C   1 
ATOM   4506 O  O   . MET A 1 557  ? 59.877 67.053  -23.928 1.00 8.43  ? 557  MET A O   1 
ATOM   4507 C  CB  . MET A 1 557  ? 57.822 68.868  -25.415 1.00 8.00  ? 557  MET A CB  1 
ATOM   4508 C  CG  . MET A 1 557  ? 56.811 69.991  -25.692 1.00 9.30  ? 557  MET A CG  1 
ATOM   4509 S  SD  . MET A 1 557  ? 57.487 71.622  -25.930 1.00 10.69 ? 557  MET A SD  1 
ATOM   4510 C  CE  . MET A 1 557  ? 58.536 71.359  -27.384 1.00 13.64 ? 557  MET A CE  1 
ATOM   4511 N  N   . HIS A 1 558  ? 58.213 67.511  -22.458 1.00 7.85  ? 558  HIS A N   1 
ATOM   4512 C  CA  . HIS A 1 558  ? 58.237 66.209  -21.789 1.00 7.02  ? 558  HIS A CA  1 
ATOM   4513 C  C   . HIS A 1 558  ? 56.961 65.453  -22.024 1.00 7.52  ? 558  HIS A C   1 
ATOM   4514 O  O   . HIS A 1 558  ? 55.881 66.037  -21.984 1.00 7.92  ? 558  HIS A O   1 
ATOM   4515 C  CB  . HIS A 1 558  ? 58.423 66.394  -20.279 1.00 8.46  ? 558  HIS A CB  1 
ATOM   4516 C  CG  . HIS A 1 558  ? 58.341 65.130  -19.497 1.00 7.66  ? 558  HIS A CG  1 
ATOM   4517 N  ND1 . HIS A 1 558  ? 57.418 64.945  -18.489 1.00 8.30  ? 558  HIS A ND1 1 
ATOM   4518 C  CD2 . HIS A 1 558  ? 59.104 64.014  -19.519 1.00 7.89  ? 558  HIS A CD2 1 
ATOM   4519 C  CE1 . HIS A 1 558  ? 57.605 63.750  -17.946 1.00 8.22  ? 558  HIS A CE1 1 
ATOM   4520 N  NE2 . HIS A 1 558  ? 58.625 63.164  -18.540 1.00 7.79  ? 558  HIS A NE2 1 
ATOM   4521 N  N   . ASN A 1 559  ? 57.093 64.139  -22.242 1.00 7.13  ? 559  ASN A N   1 
ATOM   4522 C  CA  . ASN A 1 559  ? 55.953 63.276  -22.426 1.00 6.85  ? 559  ASN A CA  1 
ATOM   4523 C  C   . ASN A 1 559  ? 55.959 62.195  -21.356 1.00 7.33  ? 559  ASN A C   1 
ATOM   4524 O  O   . ASN A 1 559  ? 56.747 61.257  -21.452 1.00 7.92  ? 559  ASN A O   1 
ATOM   4525 C  CB  . ASN A 1 559  ? 56.067 62.625  -23.797 1.00 7.68  ? 559  ASN A CB  1 
ATOM   4526 C  CG  . ASN A 1 559  ? 55.044 61.551  -24.019 1.00 7.92  ? 559  ASN A CG  1 
ATOM   4527 O  OD1 . ASN A 1 559  ? 53.958 61.544  -23.435 1.00 8.20  ? 559  ASN A OD1 1 
ATOM   4528 N  ND2 . ASN A 1 559  ? 55.375 60.614  -24.902 1.00 9.83  ? 559  ASN A ND2 1 
ATOM   4529 N  N   . THR A 1 560  ? 55.083 62.300  -20.365 1.00 6.78  ? 560  THR A N   1 
ATOM   4530 C  CA  . THR A 1 560  ? 55.103 61.322  -19.281 1.00 7.21  ? 560  THR A CA  1 
ATOM   4531 C  C   . THR A 1 560  ? 54.519 59.967  -19.682 1.00 7.45  ? 560  THR A C   1 
ATOM   4532 O  O   . THR A 1 560  ? 54.691 58.980  -18.955 1.00 8.38  ? 560  THR A O   1 
ATOM   4533 C  CB  . THR A 1 560  ? 54.344 61.930  -18.091 1.00 6.91  ? 560  THR A CB  1 
ATOM   4534 O  OG1 . THR A 1 560  ? 54.617 61.170  -16.881 1.00 8.26  ? 560  THR A OG1 1 
ATOM   4535 C  CG2 . THR A 1 560  ? 52.840 61.953  -18.300 1.00 8.86  ? 560  THR A CG2 1 
ATOM   4536 N  N   . LEU A 1 561  ? 53.801 59.888  -20.804 1.00 7.61  ? 561  LEU A N   1 
ATOM   4537 C  CA  . LEU A 1 561  ? 53.180 58.635  -21.234 1.00 7.97  ? 561  LEU A CA  1 
ATOM   4538 C  C   . LEU A 1 561  ? 54.185 57.716  -21.909 1.00 7.58  ? 561  LEU A C   1 
ATOM   4539 O  O   . LEU A 1 561  ? 55.086 58.179  -22.594 1.00 8.08  ? 561  LEU A O   1 
ATOM   4540 C  CB  . LEU A 1 561  ? 52.031 58.927  -22.216 1.00 8.52  ? 561  LEU A CB  1 
ATOM   4541 C  CG  . LEU A 1 561  ? 50.897 59.821  -21.664 1.00 9.00  ? 561  LEU A CG  1 
ATOM   4542 C  CD1 . LEU A 1 561  ? 49.845 59.979  -22.764 1.00 12.26 ? 561  LEU A CD1 1 
ATOM   4543 C  CD2 . LEU A 1 561  ? 50.219 59.213  -20.428 1.00 9.72  ? 561  LEU A CD2 1 
ATOM   4544 N  N   . PRO A 1 562  ? 54.019 56.404  -21.750 1.00 8.47  ? 562  PRO A N   1 
ATOM   4545 C  CA  . PRO A 1 562  ? 54.992 55.449  -22.318 1.00 8.73  ? 562  PRO A CA  1 
ATOM   4546 C  C   . PRO A 1 562  ? 54.759 55.080  -23.774 1.00 9.47  ? 562  PRO A C   1 
ATOM   4547 O  O   . PRO A 1 562  ? 54.940 53.915  -24.137 1.00 10.85 ? 562  PRO A O   1 
ATOM   4548 C  CB  . PRO A 1 562  ? 54.815 54.239  -21.401 1.00 9.27  ? 562  PRO A CB  1 
ATOM   4549 C  CG  . PRO A 1 562  ? 53.337 54.249  -21.078 1.00 8.63  ? 562  PRO A CG  1 
ATOM   4550 C  CD  . PRO A 1 562  ? 52.992 55.736  -20.912 1.00 9.13  ? 562  PRO A CD  1 
ATOM   4551 N  N   . HIS A 1 563  ? 54.393 56.050  -24.596 1.00 9.47  ? 563  HIS A N   1 
ATOM   4552 C  CA  . HIS A 1 563  ? 54.337 55.819  -26.038 1.00 9.93  ? 563  HIS A CA  1 
ATOM   4553 C  C   . HIS A 1 563  ? 54.755 57.113  -26.695 1.00 10.49 ? 563  HIS A C   1 
ATOM   4554 O  O   . HIS A 1 563  ? 54.596 58.193  -26.095 1.00 10.15 ? 563  HIS A O   1 
ATOM   4555 C  CB  . HIS A 1 563  ? 52.938 55.340  -26.481 1.00 10.76 ? 563  HIS A CB  1 
ATOM   4556 C  CG  . HIS A 1 563  ? 51.800 56.207  -26.026 1.00 11.35 ? 563  HIS A CG  1 
ATOM   4557 N  ND1 . HIS A 1 563  ? 51.001 55.877  -24.950 1.00 11.62 ? 563  HIS A ND1 1 
ATOM   4558 C  CD2 . HIS A 1 563  ? 51.294 57.363  -26.528 1.00 12.58 ? 563  HIS A CD2 1 
ATOM   4559 C  CE1 . HIS A 1 563  ? 50.056 56.797  -24.806 1.00 13.40 ? 563  HIS A CE1 1 
ATOM   4560 N  NE2 . HIS A 1 563  ? 50.219 57.718  -25.742 1.00 13.19 ? 563  HIS A NE2 1 
ATOM   4561 N  N   . TRP A 1 564  ? 55.302 57.041  -27.914 1.00 10.86 ? 564  TRP A N   1 
ATOM   4562 C  CA  . TRP A 1 564  ? 55.595 58.256  -28.704 1.00 10.74 ? 564  TRP A CA  1 
ATOM   4563 C  C   . TRP A 1 564  ? 54.330 59.069  -28.822 1.00 11.73 ? 564  TRP A C   1 
ATOM   4564 O  O   . TRP A 1 564  ? 53.222 58.550  -29.014 1.00 11.51 ? 564  TRP A O   1 
ATOM   4565 C  CB  . TRP A 1 564  ? 56.057 57.916  -30.146 1.00 12.36 ? 564  TRP A CB  1 
ATOM   4566 C  CG  . TRP A 1 564  ? 57.444 57.465  -30.199 1.00 10.95 ? 564  TRP A CG  1 
ATOM   4567 C  CD1 . TRP A 1 564  ? 57.892 56.169  -30.051 1.00 13.39 ? 564  TRP A CD1 1 
ATOM   4568 C  CD2 . TRP A 1 564  ? 58.619 58.282  -30.337 1.00 11.08 ? 564  TRP A CD2 1 
ATOM   4569 N  NE1 . TRP A 1 564  ? 59.264 56.144  -30.096 1.00 14.40 ? 564  TRP A NE1 1 
ATOM   4570 C  CE2 . TRP A 1 564  ? 59.741 57.420  -30.270 1.00 12.81 ? 564  TRP A CE2 1 
ATOM   4571 C  CE3 . TRP A 1 564  ? 58.843 59.660  -30.497 1.00 12.84 ? 564  TRP A CE3 1 
ATOM   4572 C  CZ2 . TRP A 1 564  ? 61.058 57.887  -30.380 1.00 13.89 ? 564  TRP A CZ2 1 
ATOM   4573 C  CZ3 . TRP A 1 564  ? 60.165 60.117  -30.604 1.00 13.95 ? 564  TRP A CZ3 1 
ATOM   4574 C  CH2 . TRP A 1 564  ? 61.240 59.237  -30.537 1.00 15.05 ? 564  TRP A CH2 1 
ATOM   4575 N  N   . ARG A 1 565  ? 54.494 60.380  -28.674 1.00 11.78 ? 565  ARG A N   1 
ATOM   4576 C  CA  . ARG A 1 565  ? 53.351 61.247  -28.788 1.00 13.21 ? 565  ARG A CA  1 
ATOM   4577 C  C   . ARG A 1 565  ? 53.703 62.448  -29.644 1.00 12.56 ? 565  ARG A C   1 
ATOM   4578 O  O   . ARG A 1 565  ? 54.770 63.031  -29.494 1.00 13.27 ? 565  ARG A O   1 
ATOM   4579 C  CB  . ARG A 1 565  ? 52.916 61.704  -27.392 1.00 14.96 ? 565  ARG A CB  1 
ATOM   4580 C  CG  . ARG A 1 565  ? 51.528 62.267  -27.347 1.00 18.60 ? 565  ARG A CG  1 
ATOM   4581 C  CD  . ARG A 1 565  ? 50.749 61.915  -26.054 1.00 17.46 ? 565  ARG A CD  1 
ATOM   4582 N  NE  . ARG A 1 565  ? 51.471 62.308  -24.842 1.00 16.72 ? 565  ARG A NE  1 
ATOM   4583 C  CZ  . ARG A 1 565  ? 50.930 62.977  -23.810 1.00 12.84 ? 565  ARG A CZ  1 
ATOM   4584 N  NH1 . ARG A 1 565  ? 49.641 63.360  -23.810 1.00 13.48 ? 565  ARG A NH1 1 
ATOM   4585 N  NH2 . ARG A 1 565  ? 51.713 63.246  -22.779 1.00 12.11 ? 565  ARG A NH2 1 
ATOM   4586 N  N   . GLU A 1 566  ? 52.793 62.774  -30.546 1.00 13.33 ? 566  GLU A N   1 
ATOM   4587 C  CA  . GLU A 1 566  ? 52.772 64.065  -31.180 1.00 15.54 ? 566  GLU A CA  1 
ATOM   4588 C  C   . GLU A 1 566  ? 51.596 64.855  -30.615 1.00 16.17 ? 566  GLU A C   1 
ATOM   4589 O  O   . GLU A 1 566  ? 50.518 64.303  -30.334 1.00 17.30 ? 566  GLU A O   1 
ATOM   4590 C  CB  . GLU A 1 566  ? 52.602 63.928  -32.673 1.00 17.49 ? 566  GLU A CB  1 
ATOM   4591 C  CG  . GLU A 1 566  ? 53.769 63.298  -33.345 1.00 19.36 ? 566  GLU A CG  1 
ATOM   4592 C  CD  . GLU A 1 566  ? 53.573 63.225  -34.848 1.00 26.42 ? 566  GLU A CD  1 
ATOM   4593 O  OE1 . GLU A 1 566  ? 52.434 62.955  -35.305 1.00 30.29 ? 566  GLU A OE1 1 
ATOM   4594 O  OE2 . GLU A 1 566  ? 54.560 63.458  -35.564 1.00 28.86 ? 566  GLU A OE2 1 
ATOM   4595 N  N   . GLN A 1 567  ? 51.798 66.158  -30.453 1.00 14.16 ? 567  GLN A N   1 
ATOM   4596 C  CA  . GLN A 1 567  ? 50.773 67.018  -29.885 1.00 14.10 ? 567  GLN A CA  1 
ATOM   4597 C  C   . GLN A 1 567  ? 51.168 68.437  -30.308 1.00 12.45 ? 567  GLN A C   1 
ATOM   4598 O  O   . GLN A 1 567  ? 52.343 68.810  -30.265 1.00 11.16 ? 567  GLN A O   1 
ATOM   4599 C  CB  . GLN A 1 567  ? 50.719 66.908  -28.332 1.00 14.55 ? 567  GLN A CB  1 
ATOM   4600 C  CG  . GLN A 1 567  ? 49.600 67.754  -27.640 1.00 15.17 ? 567  GLN A CG  1 
ATOM   4601 C  CD  . GLN A 1 567  ? 49.957 68.233  -26.207 1.00 17.10 ? 567  GLN A CD  1 
ATOM   4602 O  OE1 . GLN A 1 567  ? 49.954 67.426  -25.235 1.00 13.34 ? 567  GLN A OE1 1 
ATOM   4603 N  NE2 . GLN A 1 567  ? 50.228 69.549  -26.061 1.00 17.98 ? 567  GLN A NE2 1 
ATOM   4604 N  N   . LEU A 1 568  ? 50.176 69.221  -30.706 1.00 11.17 ? 568  LEU A N   1 
ATOM   4605 C  CA  . LEU A 1 568  ? 50.437 70.663  -30.860 1.00 10.51 ? 568  LEU A CA  1 
ATOM   4606 C  C   . LEU A 1 568  ? 50.750 71.299  -29.528 1.00 10.02 ? 568  LEU A C   1 
ATOM   4607 O  O   . LEU A 1 568  ? 50.073 71.014  -28.508 1.00 11.19 ? 568  LEU A O   1 
ATOM   4608 C  CB  . LEU A 1 568  ? 49.226 71.389  -31.479 1.00 11.86 ? 568  LEU A CB  1 
ATOM   4609 C  CG  . LEU A 1 568  ? 48.885 71.022  -32.925 1.00 12.90 ? 568  LEU A CG  1 
ATOM   4610 C  CD1 . LEU A 1 568  ? 47.829 71.977  -33.451 1.00 15.54 ? 568  LEU A CD1 1 
ATOM   4611 C  CD2 . LEU A 1 568  ? 50.076 71.168  -33.827 1.00 15.59 ? 568  LEU A CD2 1 
ATOM   4612 N  N   . VAL A 1 569  ? 51.740 72.159  -29.521 1.00 9.45  ? 569  VAL A N   1 
ATOM   4613 C  CA  . VAL A 1 569  ? 52.125 72.945  -28.350 1.00 9.30  ? 569  VAL A CA  1 
ATOM   4614 C  C   . VAL A 1 569  ? 52.179 74.406  -28.761 1.00 10.66 ? 569  VAL A C   1 
ATOM   4615 O  O   . VAL A 1 569  ? 52.437 74.715  -29.934 1.00 11.99 ? 569  VAL A O   1 
ATOM   4616 C  CB  . VAL A 1 569  ? 53.491 72.509  -27.766 1.00 9.77  ? 569  VAL A CB  1 
ATOM   4617 C  CG1 . VAL A 1 569  ? 53.385 71.100  -27.173 1.00 10.84 ? 569  VAL A CG1 1 
ATOM   4618 C  CG2 . VAL A 1 569  ? 54.604 72.569  -28.790 1.00 10.10 ? 569  VAL A CG2 1 
ATOM   4619 N  N   . ASP A 1 570  ? 51.925 75.294  -27.816 1.00 9.82  ? 570  ASP A N   1 
ATOM   4620 C  CA  . ASP A 1 570  ? 51.956 76.724  -28.125 1.00 11.33 ? 570  ASP A CA  1 
ATOM   4621 C  C   . ASP A 1 570  ? 52.757 77.488  -27.109 1.00 11.15 ? 570  ASP A C   1 
ATOM   4622 O  O   . ASP A 1 570  ? 52.834 77.102  -25.921 1.00 12.43 ? 570  ASP A O   1 
ATOM   4623 C  CB  . ASP A 1 570  ? 50.548 77.305  -28.278 1.00 12.76 ? 570  ASP A CB  1 
ATOM   4624 C  CG  . ASP A 1 570  ? 49.821 77.434  -26.970 1.00 18.24 ? 570  ASP A CG  1 
ATOM   4625 O  OD1 . ASP A 1 570  ? 49.563 76.397  -26.333 1.00 26.35 ? 570  ASP A OD1 1 
ATOM   4626 O  OD2 . ASP A 1 570  ? 49.446 78.532  -26.495 1.00 23.80 ? 570  ASP A OD2 1 
ATOM   4627 N  N   . PHE A 1 571  ? 53.395 78.556  -27.577 1.00 10.22 ? 571  PHE A N   1 
ATOM   4628 C  CA  . PHE A 1 571  ? 54.149 79.470  -26.725 1.00 10.08 ? 571  PHE A CA  1 
ATOM   4629 C  C   . PHE A 1 571  ? 53.776 80.906  -27.097 1.00 9.38  ? 571  PHE A C   1 
ATOM   4630 O  O   . PHE A 1 571  ? 53.399 81.169  -28.242 1.00 11.45 ? 571  PHE A O   1 
ATOM   4631 C  CB  . PHE A 1 571  ? 55.658 79.300  -26.956 1.00 10.10 ? 571  PHE A CB  1 
ATOM   4632 C  CG  . PHE A 1 571  ? 56.184 77.956  -26.526 1.00 9.33  ? 571  PHE A CG  1 
ATOM   4633 C  CD1 . PHE A 1 571  ? 56.159 76.887  -27.396 1.00 9.32  ? 571  PHE A CD1 1 
ATOM   4634 C  CD2 . PHE A 1 571  ? 56.657 77.776  -25.246 1.00 9.69  ? 571  PHE A CD2 1 
ATOM   4635 C  CE1 . PHE A 1 571  ? 56.591 75.624  -27.001 1.00 8.96  ? 571  PHE A CE1 1 
ATOM   4636 C  CE2 . PHE A 1 571  ? 57.095 76.523  -24.830 1.00 9.51  ? 571  PHE A CE2 1 
ATOM   4637 C  CZ  . PHE A 1 571  ? 57.072 75.460  -25.709 1.00 10.10 ? 571  PHE A CZ  1 
ATOM   4638 N  N   . TYR A 1 572  ? 53.921 81.824  -26.161 1.00 9.34  ? 572  TYR A N   1 
ATOM   4639 C  CA  . TYR A 1 572  ? 53.800 83.247  -26.469 1.00 10.65 ? 572  TYR A CA  1 
ATOM   4640 C  C   . TYR A 1 572  ? 55.172 83.748  -26.875 1.00 10.79 ? 572  TYR A C   1 
ATOM   4641 O  O   . TYR A 1 572  ? 56.183 83.427  -26.220 1.00 10.39 ? 572  TYR A O   1 
ATOM   4642 C  CB  . TYR A 1 572  ? 53.350 84.022  -25.231 1.00 11.85 ? 572  TYR A CB  1 
ATOM   4643 C  CG  . TYR A 1 572  ? 51.888 83.879  -24.839 1.00 13.71 ? 572  TYR A CG  1 
ATOM   4644 C  CD1 . TYR A 1 572  ? 50.981 83.186  -25.628 1.00 14.85 ? 572  TYR A CD1 1 
ATOM   4645 C  CD2 . TYR A 1 572  ? 51.421 84.494  -23.673 1.00 18.25 ? 572  TYR A CD2 1 
ATOM   4646 C  CE1 . TYR A 1 572  ? 49.629 83.073  -25.240 1.00 16.44 ? 572  TYR A CE1 1 
ATOM   4647 C  CE2 . TYR A 1 572  ? 50.077 84.399  -23.301 1.00 19.14 ? 572  TYR A CE2 1 
ATOM   4648 C  CZ  . TYR A 1 572  ? 49.209 83.703  -24.096 1.00 17.12 ? 572  TYR A CZ  1 
ATOM   4649 O  OH  . TYR A 1 572  ? 47.873 83.597  -23.729 1.00 20.57 ? 572  TYR A OH  1 
ATOM   4650 N  N   . VAL A 1 573  ? 55.205 84.556  -27.940 1.00 11.02 ? 573  VAL A N   1 
ATOM   4651 C  CA  . VAL A 1 573  ? 56.450 85.131  -28.470 1.00 11.60 ? 573  VAL A CA  1 
ATOM   4652 C  C   . VAL A 1 573  ? 56.233 86.615  -28.765 1.00 10.99 ? 573  VAL A C   1 
ATOM   4653 O  O   . VAL A 1 573  ? 55.110 87.053  -29.028 1.00 12.18 ? 573  VAL A O   1 
ATOM   4654 C  CB  . VAL A 1 573  ? 56.926 84.411  -29.746 1.00 12.15 ? 573  VAL A CB  1 
ATOM   4655 C  CG1 . VAL A 1 573  ? 57.521 83.043  -29.409 1.00 13.93 ? 573  VAL A CG1 1 
ATOM   4656 C  CG2 . VAL A 1 573  ? 55.812 84.272  -30.794 1.00 13.18 ? 573  VAL A CG2 1 
ATOM   4657 N  N   . SER A 1 574  ? 57.317 87.382  -28.730 1.00 12.14 ? 574  SER A N   1 
ATOM   4658 C  CA  . SER A 1 574  ? 57.222 88.846  -28.855 1.00 12.94 ? 574  SER A CA  1 
ATOM   4659 C  C   . SER A 1 574  ? 57.188 89.328  -30.293 1.00 14.11 ? 574  SER A C   1 
ATOM   4660 O  O   . SER A 1 574  ? 57.093 90.551  -30.529 1.00 16.27 ? 574  SER A O   1 
ATOM   4661 C  CB  . SER A 1 574  ? 58.378 89.495  -28.121 1.00 13.33 ? 574  SER A CB  1 
ATOM   4662 O  OG  . SER A 1 574  ? 59.616 89.135  -28.729 1.00 13.57 ? 574  SER A OG  1 
ATOM   4663 N  N   . SER A 1 575  ? 57.238 88.413  -31.253 1.00 13.97 ? 575  SER A N   1 
ATOM   4664 C  CA  . SER A 1 575  ? 57.142 88.759  -32.673 1.00 15.48 ? 575  SER A CA  1 
ATOM   4665 C  C   . SER A 1 575  ? 56.356 87.697  -33.430 1.00 15.42 ? 575  SER A C   1 
ATOM   4666 O  O   . SER A 1 575  ? 56.402 86.512  -33.065 1.00 14.63 ? 575  SER A O   1 
ATOM   4667 C  CB  . SER A 1 575  ? 58.544 88.843  -33.272 1.00 16.18 ? 575  SER A CB  1 
ATOM   4668 O  OG  . SER A 1 575  ? 58.541 88.859  -34.697 1.00 17.34 ? 575  SER A OG  1 
ATOM   4669 N  N   . PRO A 1 576  ? 55.648 88.076  -34.485 1.00 15.33 ? 576  PRO A N   1 
ATOM   4670 C  CA  . PRO A 1 576  ? 54.975 87.080  -35.313 1.00 15.51 ? 576  PRO A CA  1 
ATOM   4671 C  C   . PRO A 1 576  ? 55.919 86.358  -36.280 1.00 14.87 ? 576  PRO A C   1 
ATOM   4672 O  O   . PRO A 1 576  ? 55.546 85.362  -36.874 1.00 15.09 ? 576  PRO A O   1 
ATOM   4673 C  CB  . PRO A 1 576  ? 53.908 87.892  -36.058 1.00 15.99 ? 576  PRO A CB  1 
ATOM   4674 C  CG  . PRO A 1 576  ? 54.381 89.299  -36.026 1.00 17.71 ? 576  PRO A CG  1 
ATOM   4675 C  CD  . PRO A 1 576  ? 55.395 89.465  -34.940 1.00 15.70 ? 576  PRO A CD  1 
ATOM   4676 N  N   . PHE A 1 577  ? 57.133 86.878  -36.457 1.00 14.50 ? 577  PHE A N   1 
ATOM   4677 C  CA  . PHE A 1 577  ? 58.045 86.348  -37.458 1.00 14.92 ? 577  PHE A CA  1 
ATOM   4678 C  C   . PHE A 1 577  ? 59.017 85.385  -36.793 1.00 14.81 ? 577  PHE A C   1 
ATOM   4679 O  O   . PHE A 1 577  ? 60.178 85.697  -36.531 1.00 15.65 ? 577  PHE A O   1 
ATOM   4680 C  CB  . PHE A 1 577  ? 58.768 87.497  -38.184 1.00 16.01 ? 577  PHE A CB  1 
ATOM   4681 C  CG  . PHE A 1 577  ? 57.820 88.515  -38.779 1.00 18.36 ? 577  PHE A CG  1 
ATOM   4682 C  CD1 . PHE A 1 577  ? 56.782 88.109  -39.595 1.00 18.17 ? 577  PHE A CD1 1 
ATOM   4683 C  CD2 . PHE A 1 577  ? 57.985 89.880  -38.521 1.00 21.74 ? 577  PHE A CD2 1 
ATOM   4684 C  CE1 . PHE A 1 577  ? 55.901 89.049  -40.175 1.00 20.62 ? 577  PHE A CE1 1 
ATOM   4685 C  CE2 . PHE A 1 577  ? 57.116 90.828  -39.085 1.00 23.20 ? 577  PHE A CE2 1 
ATOM   4686 C  CZ  . PHE A 1 577  ? 56.080 90.406  -39.911 1.00 21.63 ? 577  PHE A CZ  1 
ATOM   4687 N  N   . VAL A 1 578  ? 58.478 84.201  -36.481 1.00 13.74 ? 578  VAL A N   1 
ATOM   4688 C  CA  . VAL A 1 578  ? 59.218 83.197  -35.725 1.00 13.93 ? 578  VAL A CA  1 
ATOM   4689 C  C   . VAL A 1 578  ? 59.108 81.872  -36.445 1.00 14.01 ? 578  VAL A C   1 
ATOM   4690 O  O   . VAL A 1 578  ? 58.050 81.500  -36.926 1.00 14.60 ? 578  VAL A O   1 
ATOM   4691 C  CB  . VAL A 1 578  ? 58.689 83.095  -34.258 1.00 13.57 ? 578  VAL A CB  1 
ATOM   4692 C  CG1 . VAL A 1 578  ? 59.431 81.976  -33.493 1.00 14.47 ? 578  VAL A CG1 1 
ATOM   4693 C  CG2 . VAL A 1 578  ? 58.928 84.376  -33.533 1.00 13.82 ? 578  VAL A CG2 1 
ATOM   4694 N  N   . SER A 1 579  ? 60.223 81.167  -36.517 1.00 14.42 ? 579  SER A N   1 
ATOM   4695 C  CA  . SER A 1 579  ? 60.186 79.841  -37.090 1.00 15.24 ? 579  SER A CA  1 
ATOM   4696 C  C   . SER A 1 579  ? 60.729 78.822  -36.104 1.00 13.34 ? 579  SER A C   1 
ATOM   4697 O  O   . SER A 1 579  ? 61.474 79.155  -35.196 1.00 14.20 ? 579  SER A O   1 
ATOM   4698 C  CB  . SER A 1 579  ? 60.902 79.776  -38.440 1.00 17.98 ? 579  SER A CB  1 
ATOM   4699 O  OG  . SER A 1 579  ? 62.199 80.246  -38.289 1.00 21.67 ? 579  SER A OG  1 
ATOM   4700 N  N   . VAL A 1 580  ? 60.357 77.576  -36.334 1.00 12.06 ? 580  VAL A N   1 
ATOM   4701 C  CA  . VAL A 1 580  ? 60.683 76.492  -35.417 1.00 11.75 ? 580  VAL A CA  1 
ATOM   4702 C  C   . VAL A 1 580  ? 61.564 75.472  -36.142 1.00 12.95 ? 580  VAL A C   1 
ATOM   4703 O  O   . VAL A 1 580  ? 61.290 75.104  -37.307 1.00 13.50 ? 580  VAL A O   1 
ATOM   4704 C  CB  . VAL A 1 580  ? 59.398 75.806  -34.910 1.00 11.52 ? 580  VAL A CB  1 
ATOM   4705 C  CG1 . VAL A 1 580  ? 59.738 74.736  -33.882 1.00 12.21 ? 580  VAL A CG1 1 
ATOM   4706 C  CG2 . VAL A 1 580  ? 58.454 76.843  -34.302 1.00 13.08 ? 580  VAL A CG2 1 
ATOM   4707 N  N   . THR A 1 581  ? 62.585 74.998  -35.432 1.00 12.97 ? 581  THR A N   1 
ATOM   4708 C  CA  . THR A 1 581  ? 63.413 73.871  -35.873 1.00 13.43 ? 581  THR A CA  1 
ATOM   4709 C  C   . THR A 1 581  ? 63.543 72.848  -34.746 1.00 12.58 ? 581  THR A C   1 
ATOM   4710 O  O   . THR A 1 581  ? 63.382 73.199  -33.555 1.00 12.97 ? 581  THR A O   1 
ATOM   4711 C  CB  . THR A 1 581  ? 64.820 74.346  -36.282 1.00 14.37 ? 581  THR A CB  1 
ATOM   4712 O  OG1 . THR A 1 581  ? 65.327 75.293  -35.331 1.00 16.68 ? 581  THR A OG1 1 
ATOM   4713 C  CG2 . THR A 1 581  ? 64.759 75.179  -37.595 1.00 13.98 ? 581  THR A CG2 1 
ATOM   4714 N  N   . ASP A 1 582  ? 63.822 71.599  -35.100 1.00 13.90 ? 582  ASP A N   1 
ATOM   4715 C  CA  . ASP A 1 582  ? 64.254 70.617  -34.098 1.00 15.02 ? 582  ASP A CA  1 
ATOM   4716 C  C   . ASP A 1 582  ? 65.764 70.755  -33.850 1.00 16.36 ? 582  ASP A C   1 
ATOM   4717 O  O   . ASP A 1 582  ? 66.395 71.660  -34.382 1.00 16.50 ? 582  ASP A O   1 
ATOM   4718 C  CB  . ASP A 1 582  ? 63.809 69.200  -34.451 1.00 16.71 ? 582  ASP A CB  1 
ATOM   4719 C  CG  . ASP A 1 582  ? 64.470 68.644  -35.721 1.00 16.51 ? 582  ASP A CG  1 
ATOM   4720 O  OD1 . ASP A 1 582  ? 65.527 69.159  -36.159 1.00 15.99 ? 582  ASP A OD1 1 
ATOM   4721 O  OD2 . ASP A 1 582  ? 63.981 67.657  -36.312 1.00 19.71 ? 582  ASP A OD2 1 
ATOM   4722 N  N   . LEU A 1 583  ? 66.365 69.917  -32.997 1.00 19.77 ? 583  LEU A N   1 
ATOM   4723 C  CA  . LEU A 1 583  ? 67.777 70.204  -32.731 1.00 21.01 ? 583  LEU A CA  1 
ATOM   4724 C  C   . LEU A 1 583  ? 68.715 69.690  -33.838 1.00 21.38 ? 583  LEU A C   1 
ATOM   4725 O  O   . LEU A 1 583  ? 69.922 69.963  -33.787 1.00 23.61 ? 583  LEU A O   1 
ATOM   4726 C  CB  . LEU A 1 583  ? 68.252 69.796  -31.318 1.00 21.57 ? 583  LEU A CB  1 
ATOM   4727 C  CG  . LEU A 1 583  ? 69.194 70.817  -30.652 1.00 21.09 ? 583  LEU A CG  1 
ATOM   4728 C  CD1 . LEU A 1 583  ? 68.580 72.221  -30.621 1.00 24.93 ? 583  LEU A CD1 1 
ATOM   4729 C  CD2 . LEU A 1 583  ? 69.567 70.423  -29.225 1.00 22.12 ? 583  LEU A CD2 1 
ATOM   4730 N  N   . ALA A 1 584  ? 68.158 69.001  -34.849 1.00 19.62 ? 584  ALA A N   1 
ATOM   4731 C  CA  . ALA A 1 584  ? 68.948 68.716  -36.062 1.00 17.65 ? 584  ALA A CA  1 
ATOM   4732 C  C   . ALA A 1 584  ? 68.740 69.809  -37.098 1.00 16.71 ? 584  ALA A C   1 
ATOM   4733 O  O   . ALA A 1 584  ? 69.151 69.678  -38.265 1.00 15.56 ? 584  ALA A O   1 
ATOM   4734 C  CB  . ALA A 1 584  ? 68.611 67.358  -36.646 1.00 17.33 ? 584  ALA A CB  1 
ATOM   4735 N  N   . ASN A 1 585  ? 68.091 70.891  -36.688 1.00 15.30 ? 585  ASN A N   1 
ATOM   4736 C  CA  . ASN A 1 585  ? 67.892 72.061  -37.540 1.00 16.19 ? 585  ASN A CA  1 
ATOM   4737 C  C   . ASN A 1 585  ? 66.904 71.777  -38.686 1.00 16.48 ? 585  ASN A C   1 
ATOM   4738 O  O   . ASN A 1 585  ? 66.854 72.516  -39.685 1.00 18.99 ? 585  ASN A O   1 
ATOM   4739 C  CB  . ASN A 1 585  ? 69.253 72.635  -38.027 1.00 17.21 ? 585  ASN A CB  1 
ATOM   4740 C  CG  . ASN A 1 585  ? 69.180 74.097  -38.413 1.00 21.22 ? 585  ASN A CG  1 
ATOM   4741 O  OD1 . ASN A 1 585  ? 68.483 74.912  -37.787 1.00 23.87 ? 585  ASN A OD1 1 
ATOM   4742 N  ND2 . ASN A 1 585  ? 69.924 74.450  -39.463 1.00 23.98 ? 585  ASN A ND2 1 
ATOM   4743 N  N   . ASN A 1 586  ? 66.109 70.724  -38.556 1.00 15.50 ? 586  ASN A N   1 
ATOM   4744 C  CA  . ASN A 1 586  ? 65.029 70.451  -39.517 1.00 16.61 ? 586  ASN A CA  1 
ATOM   4745 C  C   . ASN A 1 586  ? 63.896 71.440  -39.263 1.00 16.65 ? 586  ASN A C   1 
ATOM   4746 O  O   . ASN A 1 586  ? 63.452 71.585  -38.114 1.00 15.42 ? 586  ASN A O   1 
ATOM   4747 C  CB  . ASN A 1 586  ? 64.444 69.049  -39.352 1.00 17.28 ? 586  ASN A CB  1 
ATOM   4748 C  CG  . ASN A 1 586  ? 65.476 67.959  -39.463 1.00 17.89 ? 586  ASN A CG  1 
ATOM   4749 O  OD1 . ASN A 1 586  ? 66.343 67.996  -40.341 1.00 18.47 ? 586  ASN A OD1 1 
ATOM   4750 N  ND2 . ASN A 1 586  ? 65.385 66.965  -38.573 1.00 16.20 ? 586  ASN A ND2 1 
ATOM   4751 N  N   . PRO A 1 587  ? 63.396 72.130  -40.287 1.00 16.64 ? 587  PRO A N   1 
ATOM   4752 C  CA  . PRO A 1 587  ? 62.267 73.047  -40.072 1.00 16.56 ? 587  PRO A CA  1 
ATOM   4753 C  C   . PRO A 1 587  ? 61.034 72.283  -39.602 1.00 15.58 ? 587  PRO A C   1 
ATOM   4754 O  O   . PRO A 1 587  ? 60.839 71.119  -39.987 1.00 16.53 ? 587  PRO A O   1 
ATOM   4755 C  CB  . PRO A 1 587  ? 62.013 73.655  -41.461 1.00 17.34 ? 587  PRO A CB  1 
ATOM   4756 C  CG  . PRO A 1 587  ? 63.205 73.315  -42.291 1.00 19.64 ? 587  PRO A CG  1 
ATOM   4757 C  CD  . PRO A 1 587  ? 63.820 72.072  -41.704 1.00 17.37 ? 587  PRO A CD  1 
ATOM   4758 N  N   . VAL A 1 588  ? 60.213 72.941  -38.775 1.00 14.33 ? 588  VAL A N   1 
ATOM   4759 C  CA  . VAL A 1 588  ? 58.986 72.353  -38.271 1.00 13.62 ? 588  VAL A CA  1 
ATOM   4760 C  C   . VAL A 1 588  ? 57.880 73.320  -38.659 1.00 12.96 ? 588  VAL A C   1 
ATOM   4761 O  O   . VAL A 1 588  ? 58.020 74.519  -38.408 1.00 14.17 ? 588  VAL A O   1 
ATOM   4762 C  CB  . VAL A 1 588  ? 59.043 72.181  -36.719 1.00 14.25 ? 588  VAL A CB  1 
ATOM   4763 C  CG1 . VAL A 1 588  ? 57.704 71.725  -36.149 1.00 14.61 ? 588  VAL A CG1 1 
ATOM   4764 C  CG2 . VAL A 1 588  ? 60.156 71.174  -36.329 1.00 13.80 ? 588  VAL A CG2 1 
ATOM   4765 N  N   . GLU A 1 589  ? 56.806 72.820  -39.260 1.00 12.87 ? 589  GLU A N   1 
ATOM   4766 C  CA  . GLU A 1 589  ? 55.701 73.670  -39.666 1.00 14.03 ? 589  GLU A CA  1 
ATOM   4767 C  C   . GLU A 1 589  ? 55.071 74.303  -38.437 1.00 13.53 ? 589  GLU A C   1 
ATOM   4768 O  O   . GLU A 1 589  ? 54.863 73.621  -37.429 1.00 14.48 ? 589  GLU A O   1 
ATOM   4769 C  CB  . GLU A 1 589  ? 54.645 72.847  -40.383 1.00 15.16 ? 589  GLU A CB  1 
ATOM   4770 C  CG  . GLU A 1 589  ? 53.503 73.717  -40.851 1.00 21.46 ? 589  GLU A CG  1 
ATOM   4771 C  CD  . GLU A 1 589  ? 52.452 72.996  -41.656 1.00 27.40 ? 589  GLU A CD  1 
ATOM   4772 O  OE1 . GLU A 1 589  ? 52.657 71.807  -41.972 1.00 31.22 ? 589  GLU A OE1 1 
ATOM   4773 O  OE2 . GLU A 1 589  ? 51.407 73.633  -41.964 1.00 30.43 ? 589  GLU A OE2 1 
ATOM   4774 N  N   . ALA A 1 590  ? 54.781 75.595  -38.504 1.00 12.34 ? 590  ALA A N   1 
ATOM   4775 C  CA  . ALA A 1 590  ? 54.249 76.317  -37.364 1.00 11.98 ? 590  ALA A CA  1 
ATOM   4776 C  C   . ALA A 1 590  ? 53.125 77.232  -37.821 1.00 11.85 ? 590  ALA A C   1 
ATOM   4777 O  O   . ALA A 1 590  ? 53.022 77.577  -39.025 1.00 12.45 ? 590  ALA A O   1 
ATOM   4778 C  CB  . ALA A 1 590  ? 55.312 77.092  -36.656 1.00 12.54 ? 590  ALA A CB  1 
ATOM   4779 N  N   . GLN A 1 591  ? 52.283 77.623  -36.890 1.00 11.68 ? 591  GLN A N   1 
ATOM   4780 C  CA  . GLN A 1 591  ? 51.190 78.565  -37.134 1.00 10.97 ? 591  GLN A CA  1 
ATOM   4781 C  C   . GLN A 1 591  ? 51.271 79.645  -36.092 1.00 11.93 ? 591  GLN A C   1 
ATOM   4782 O  O   . GLN A 1 591  ? 51.448 79.345  -34.905 1.00 12.63 ? 591  GLN A O   1 
ATOM   4783 C  CB  . GLN A 1 591  ? 49.814 77.867  -37.090 1.00 12.10 ? 591  GLN A CB  1 
ATOM   4784 C  CG  . GLN A 1 591  ? 48.636 78.857  -37.042 1.00 11.94 ? 591  GLN A CG  1 
ATOM   4785 C  CD  . GLN A 1 591  ? 47.320 78.145  -36.834 1.00 11.56 ? 591  GLN A CD  1 
ATOM   4786 O  OE1 . GLN A 1 591  ? 47.107 77.058  -37.402 1.00 13.13 ? 591  GLN A OE1 1 
ATOM   4787 N  NE2 . GLN A 1 591  ? 46.448 78.715  -36.034 1.00 12.29 ? 591  GLN A NE2 1 
ATOM   4788 N  N   . VAL A 1 592  ? 51.140 80.906  -36.507 1.00 11.09 ? 592  VAL A N   1 
ATOM   4789 C  CA  . VAL A 1 592  ? 51.075 82.011  -35.573 1.00 11.09 ? 592  VAL A CA  1 
ATOM   4790 C  C   . VAL A 1 592  ? 49.664 82.571  -35.575 1.00 11.62 ? 592  VAL A C   1 
ATOM   4791 O  O   . VAL A 1 592  ? 49.030 82.679  -36.635 1.00 11.80 ? 592  VAL A O   1 
ATOM   4792 C  CB  . VAL A 1 592  ? 52.138 83.076  -35.913 1.00 11.42 ? 592  VAL A CB  1 
ATOM   4793 C  CG1 . VAL A 1 592  ? 51.907 84.353  -35.103 1.00 12.51 ? 592  VAL A CG1 1 
ATOM   4794 C  CG2 . VAL A 1 592  ? 53.520 82.516  -35.589 1.00 11.64 ? 592  VAL A CG2 1 
ATOM   4795 N  N   . SER A 1 593  ? 49.153 82.842  -34.378 1.00 12.78 ? 593  SER A N   1 
ATOM   4796 C  CA  . SER A 1 593  ? 47.820 83.405  -34.153 1.00 13.58 ? 593  SER A CA  1 
ATOM   4797 C  C   . SER A 1 593  ? 47.966 84.562  -33.187 1.00 13.41 ? 593  SER A C   1 
ATOM   4798 O  O   . SER A 1 593  ? 48.951 84.649  -32.438 1.00 14.77 ? 593  SER A O   1 
ATOM   4799 C  CB  . SER A 1 593  ? 46.826 82.361  -33.550 1.00 14.53 ? 593  SER A CB  1 
ATOM   4800 O  OG  . SER A 1 593  ? 46.638 81.198  -34.366 1.00 15.49 ? 593  SER A OG  1 
ATOM   4801 N  N   . PRO A 1 594  ? 46.987 85.445  -33.147 1.00 12.51 ? 594  PRO A N   1 
ATOM   4802 C  CA  . PRO A 1 594  ? 47.027 86.501  -32.131 1.00 12.25 ? 594  PRO A CA  1 
ATOM   4803 C  C   . PRO A 1 594  ? 46.815 85.979  -30.713 1.00 12.63 ? 594  PRO A C   1 
ATOM   4804 O  O   . PRO A 1 594  ? 46.379 84.834  -30.524 1.00 12.43 ? 594  PRO A O   1 
ATOM   4805 C  CB  . PRO A 1 594  ? 45.864 87.431  -32.527 1.00 13.40 ? 594  PRO A CB  1 
ATOM   4806 C  CG  . PRO A 1 594  ? 45.517 87.025  -33.956 1.00 12.65 ? 594  PRO A CG  1 
ATOM   4807 C  CD  . PRO A 1 594  ? 45.793 85.559  -34.014 1.00 12.47 ? 594  PRO A CD  1 
ATOM   4808 N  N   . VAL A 1 595  ? 47.120 86.811  -29.712 1.00 12.37 ? 595  VAL A N   1 
ATOM   4809 C  CA  . VAL A 1 595  ? 46.736 86.518  -28.347 1.00 12.69 ? 595  VAL A CA  1 
ATOM   4810 C  C   . VAL A 1 595  ? 45.469 87.300  -28.075 1.00 12.77 ? 595  VAL A C   1 
ATOM   4811 O  O   . VAL A 1 595  ? 45.491 88.545  -28.035 1.00 13.67 ? 595  VAL A O   1 
ATOM   4812 C  CB  . VAL A 1 595  ? 47.848 86.872  -27.318 1.00 13.34 ? 595  VAL A CB  1 
ATOM   4813 C  CG1 . VAL A 1 595  ? 47.315 86.657  -25.917 1.00 13.74 ? 595  VAL A CG1 1 
ATOM   4814 C  CG2 . VAL A 1 595  ? 49.114 86.043  -27.564 1.00 14.41 ? 595  VAL A CG2 1 
ATOM   4815 N  N   . TRP A 1 596  ? 44.357 86.593  -27.888 1.00 13.20 ? 596  TRP A N   1 
ATOM   4816 C  CA  . TRP A 1 596  ? 43.055 87.197  -27.696 1.00 14.25 ? 596  TRP A CA  1 
ATOM   4817 C  C   . TRP A 1 596  ? 42.672 87.079  -26.241 1.00 15.97 ? 596  TRP A C   1 
ATOM   4818 O  O   . TRP A 1 596  ? 42.815 86.012  -25.637 1.00 16.50 ? 596  TRP A O   1 
ATOM   4819 C  CB  . TRP A 1 596  ? 42.026 86.438  -28.548 1.00 14.26 ? 596  TRP A CB  1 
ATOM   4820 C  CG  . TRP A 1 596  ? 42.152 86.630  -30.009 1.00 12.94 ? 596  TRP A CG  1 
ATOM   4821 C  CD1 . TRP A 1 596  ? 42.529 85.694  -30.945 1.00 12.78 ? 596  TRP A CD1 1 
ATOM   4822 C  CD2 . TRP A 1 596  ? 41.852 87.817  -30.739 1.00 11.88 ? 596  TRP A CD2 1 
ATOM   4823 N  NE1 . TRP A 1 596  ? 42.490 86.246  -32.205 1.00 13.30 ? 596  TRP A NE1 1 
ATOM   4824 C  CE2 . TRP A 1 596  ? 42.069 87.546  -32.102 1.00 13.72 ? 596  TRP A CE2 1 
ATOM   4825 C  CE3 . TRP A 1 596  ? 41.401 89.102  -30.372 1.00 12.92 ? 596  TRP A CE3 1 
ATOM   4826 C  CZ2 . TRP A 1 596  ? 41.866 88.514  -33.102 1.00 14.41 ? 596  TRP A CZ2 1 
ATOM   4827 C  CZ3 . TRP A 1 596  ? 41.202 90.060  -31.369 1.00 14.54 ? 596  TRP A CZ3 1 
ATOM   4828 C  CH2 . TRP A 1 596  ? 41.438 89.762  -32.703 1.00 14.42 ? 596  TRP A CH2 1 
ATOM   4829 N  N   . SER A 1 597  ? 42.202 88.174  -25.665 1.00 15.99 ? 597  SER A N   1 
ATOM   4830 C  CA  . SER A 1 597  ? 41.622 88.136  -24.332 1.00 17.31 ? 597  SER A CA  1 
ATOM   4831 C  C   . SER A 1 597  ? 40.240 88.752  -24.375 1.00 16.65 ? 597  SER A C   1 
ATOM   4832 O  O   . SER A 1 597  ? 39.962 89.645  -25.174 1.00 18.36 ? 597  SER A O   1 
ATOM   4833 C  CB  . SER A 1 597  ? 42.486 88.885  -23.333 1.00 18.90 ? 597  SER A CB  1 
ATOM   4834 O  OG  . SER A 1 597  ? 42.653 90.193  -23.796 1.00 21.79 ? 597  SER A OG  1 
ATOM   4835 N  N   . TRP A 1 598  ? 39.392 88.286  -23.483 1.00 16.18 ? 598  TRP A N   1 
ATOM   4836 C  CA  . TRP A 1 598  ? 38.011 88.728  -23.459 1.00 16.26 ? 598  TRP A CA  1 
ATOM   4837 C  C   . TRP A 1 598  ? 37.764 89.655  -22.282 1.00 18.05 ? 598  TRP A C   1 
ATOM   4838 O  O   . TRP A 1 598  ? 38.249 89.422  -21.183 1.00 19.46 ? 598  TRP A O   1 
ATOM   4839 C  CB  . TRP A 1 598  ? 37.082 87.513  -23.386 1.00 15.61 ? 598  TRP A CB  1 
ATOM   4840 C  CG  . TRP A 1 598  ? 37.033 86.761  -24.692 1.00 12.35 ? 598  TRP A CG  1 
ATOM   4841 C  CD1 . TRP A 1 598  ? 37.955 85.865  -25.168 1.00 12.64 ? 598  TRP A CD1 1 
ATOM   4842 C  CD2 . TRP A 1 598  ? 36.008 86.838  -25.691 1.00 12.24 ? 598  TRP A CD2 1 
ATOM   4843 N  NE1 . TRP A 1 598  ? 37.566 85.386  -26.392 1.00 12.02 ? 598  TRP A NE1 1 
ATOM   4844 C  CE2 . TRP A 1 598  ? 36.370 85.957  -26.736 1.00 11.09 ? 598  TRP A CE2 1 
ATOM   4845 C  CE3 . TRP A 1 598  ? 34.814 87.558  -25.805 1.00 12.93 ? 598  TRP A CE3 1 
ATOM   4846 C  CZ2 . TRP A 1 598  ? 35.584 85.788  -27.881 1.00 12.35 ? 598  TRP A CZ2 1 
ATOM   4847 C  CZ3 . TRP A 1 598  ? 34.028 87.380  -26.939 1.00 11.63 ? 598  TRP A CZ3 1 
ATOM   4848 C  CH2 . TRP A 1 598  ? 34.413 86.495  -27.955 1.00 13.33 ? 598  TRP A CH2 1 
ATOM   4849 N  N   . HIS A 1 599  ? 36.970 90.677  -22.524 1.00 20.81 ? 599  HIS A N   1 
ATOM   4850 C  CA  . HIS A 1 599  ? 36.773 91.752  -21.574 1.00 23.73 ? 599  HIS A CA  1 
ATOM   4851 C  C   . HIS A 1 599  ? 35.290 92.016  -21.455 1.00 24.94 ? 599  HIS A C   1 
ATOM   4852 O  O   . HIS A 1 599  ? 34.612 92.132  -22.458 1.00 23.80 ? 599  HIS A O   1 
ATOM   4853 C  CB  . HIS A 1 599  ? 37.501 93.000  -22.061 1.00 25.24 ? 599  HIS A CB  1 
ATOM   4854 C  CG  . HIS A 1 599  ? 38.983 92.830  -22.084 1.00 29.05 ? 599  HIS A CG  1 
ATOM   4855 N  ND1 . HIS A 1 599  ? 39.706 92.527  -20.954 1.00 33.47 ? 599  HIS A ND1 1 
ATOM   4856 C  CD2 . HIS A 1 599  ? 39.870 92.863  -23.102 1.00 32.37 ? 599  HIS A CD2 1 
ATOM   4857 C  CE1 . HIS A 1 599  ? 40.978 92.395  -21.273 1.00 32.88 ? 599  HIS A CE1 1 
ATOM   4858 N  NE2 . HIS A 1 599  ? 41.104 92.594  -22.570 1.00 34.61 ? 599  HIS A NE2 1 
ATOM   4859 N  N   . HIS A 1 600  ? 34.783 92.102  -20.230 1.00 27.55 ? 600  HIS A N   1 
ATOM   4860 C  CA  . HIS A 1 600  ? 33.442 92.630  -20.066 1.00 30.27 ? 600  HIS A CA  1 
ATOM   4861 C  C   . HIS A 1 600  ? 33.605 94.123  -20.050 1.00 30.91 ? 600  HIS A C   1 
ATOM   4862 O  O   . HIS A 1 600  ? 34.128 94.699  -19.087 1.00 31.85 ? 600  HIS A O   1 
ATOM   4863 C  CB  . HIS A 1 600  ? 32.713 92.163  -18.806 1.00 30.92 ? 600  HIS A CB  1 
ATOM   4864 C  CG  . HIS A 1 600  ? 31.421 92.892  -18.586 1.00 34.66 ? 600  HIS A CG  1 
ATOM   4865 N  ND1 . HIS A 1 600  ? 30.360 92.803  -19.464 1.00 37.14 ? 600  HIS A ND1 1 
ATOM   4866 C  CD2 . HIS A 1 600  ? 31.038 93.768  -17.626 1.00 37.26 ? 600  HIS A CD2 1 
ATOM   4867 C  CE1 . HIS A 1 600  ? 29.368 93.563  -19.038 1.00 38.22 ? 600  HIS A CE1 1 
ATOM   4868 N  NE2 . HIS A 1 600  ? 29.752 94.161  -17.923 1.00 38.74 ? 600  HIS A NE2 1 
ATOM   4869 N  N   . ASP A 1 601  ? 33.183 94.733  -21.147 1.00 31.74 ? 601  ASP A N   1 
ATOM   4870 C  CA  . ASP A 1 601  ? 33.298 96.156  -21.342 1.00 32.85 ? 601  ASP A CA  1 
ATOM   4871 C  C   . ASP A 1 601  ? 32.153 96.836  -20.580 1.00 33.35 ? 601  ASP A C   1 
ATOM   4872 O  O   . ASP A 1 601  ? 31.006 96.775  -21.016 1.00 33.10 ? 601  ASP A O   1 
ATOM   4873 C  CB  . ASP A 1 601  ? 33.199 96.440  -22.835 1.00 33.06 ? 601  ASP A CB  1 
ATOM   4874 C  CG  . ASP A 1 601  ? 33.563 97.859  -23.187 1.00 35.11 ? 601  ASP A CG  1 
ATOM   4875 O  OD1 . ASP A 1 601  ? 33.548 98.730  -22.282 1.00 35.17 ? 601  ASP A OD1 1 
ATOM   4876 O  OD2 . ASP A 1 601  ? 33.865 98.198  -24.356 1.00 37.44 ? 601  ASP A OD2 1 
ATOM   4877 N  N   . THR A 1 602  ? 32.466 97.459  -19.442 1.00 34.21 ? 602  THR A N   1 
ATOM   4878 C  CA  . THR A 1 602  ? 31.436 98.127  -18.628 1.00 35.46 ? 602  THR A CA  1 
ATOM   4879 C  C   . THR A 1 602  ? 30.906 99.414  -19.258 1.00 35.19 ? 602  THR A C   1 
ATOM   4880 O  O   . THR A 1 602  ? 29.892 99.952  -18.799 1.00 36.20 ? 602  THR A O   1 
ATOM   4881 C  CB  . THR A 1 602  ? 31.905 98.381  -17.159 1.00 35.59 ? 602  THR A CB  1 
ATOM   4882 O  OG1 . THR A 1 602  ? 33.191 99.020  -17.150 1.00 37.91 ? 602  THR A OG1 1 
ATOM   4883 C  CG2 . THR A 1 602  ? 32.136 97.060  -16.422 1.00 36.54 ? 602  THR A CG2 1 
ATOM   4884 N  N   . LEU A 1 603  ? 31.576 99.897  -20.306 1.00 34.35 ? 603  LEU A N   1 
ATOM   4885 C  CA  . LEU A 1 603  ? 31.089 101.023 -21.095 1.00 33.60 ? 603  LEU A CA  1 
ATOM   4886 C  C   . LEU A 1 603  ? 29.936 100.605 -22.000 1.00 32.35 ? 603  LEU A C   1 
ATOM   4887 O  O   . LEU A 1 603  ? 28.813 101.087 -21.827 1.00 32.38 ? 603  LEU A O   1 
ATOM   4888 C  CB  . LEU A 1 603  ? 32.219 101.662 -21.926 1.00 34.42 ? 603  LEU A CB  1 
ATOM   4889 C  CG  . LEU A 1 603  ? 33.251 102.589 -21.255 1.00 35.60 ? 603  LEU A CG  1 
ATOM   4890 C  CD1 . LEU A 1 603  ? 32.563 103.719 -20.478 1.00 37.65 ? 603  LEU A CD1 1 
ATOM   4891 C  CD2 . LEU A 1 603  ? 34.238 101.832 -20.363 1.00 36.98 ? 603  LEU A CD2 1 
ATOM   4892 N  N   . THR A 1 604  ? 30.217 99.690  -22.933 1.00 29.68 ? 604  THR A N   1 
ATOM   4893 C  CA  . THR A 1 604  ? 29.263 99.242  -23.955 1.00 28.08 ? 604  THR A CA  1 
ATOM   4894 C  C   . THR A 1 604  ? 28.330 98.118  -23.469 1.00 26.10 ? 604  THR A C   1 
ATOM   4895 O  O   . THR A 1 604  ? 27.385 97.763  -24.167 1.00 25.17 ? 604  THR A O   1 
ATOM   4896 C  CB  . THR A 1 604  ? 30.002 98.729  -25.211 1.00 28.39 ? 604  THR A CB  1 
ATOM   4897 O  OG1 . THR A 1 604  ? 30.874 97.640  -24.848 1.00 29.06 ? 604  THR A OG1 1 
ATOM   4898 C  CG2 . THR A 1 604  ? 30.951 99.791  -25.789 1.00 29.31 ? 604  THR A CG2 1 
ATOM   4899 N  N   . LYS A 1 605  ? 28.623 97.554  -22.300 1.00 25.16 ? 605  LYS A N   1 
ATOM   4900 C  CA  . LYS A 1 605  ? 27.858 96.431  -21.740 1.00 24.39 ? 605  LYS A CA  1 
ATOM   4901 C  C   . LYS A 1 605  ? 27.889 95.223  -22.668 1.00 23.84 ? 605  LYS A C   1 
ATOM   4902 O  O   . LYS A 1 605  ? 26.869 94.571  -22.895 1.00 24.24 ? 605  LYS A O   1 
ATOM   4903 C  CB  . LYS A 1 605  ? 26.402 96.824  -21.432 1.00 24.82 ? 605  LYS A CB  1 
ATOM   4904 C  CG  . LYS A 1 605  ? 26.272 97.965  -20.463 1.00 25.56 ? 605  LYS A CG  1 
ATOM   4905 C  CD  . LYS A 1 605  ? 26.707 97.550  -19.069 1.00 27.01 ? 605  LYS A CD  1 
ATOM   4906 C  CE  . LYS A 1 605  ? 26.617 98.747  -18.113 1.00 28.47 ? 605  LYS A CE  1 
ATOM   4907 N  NZ  . LYS A 1 605  ? 26.895 98.346  -16.716 1.00 32.71 ? 605  LYS A NZ  1 
ATOM   4908 N  N   . THR A 1 606  ? 29.061 94.946  -23.229 1.00 22.02 ? 606  THR A N   1 
ATOM   4909 C  CA  . THR A 1 606  ? 29.231 93.746  -24.055 1.00 21.52 ? 606  THR A CA  1 
ATOM   4910 C  C   . THR A 1 606  ? 30.463 93.030  -23.572 1.00 20.22 ? 606  THR A C   1 
ATOM   4911 O  O   . THR A 1 606  ? 31.319 93.609  -22.883 1.00 20.49 ? 606  THR A O   1 
ATOM   4912 C  CB  . THR A 1 606  ? 29.448 94.093  -25.533 1.00 21.92 ? 606  THR A CB  1 
ATOM   4913 O  OG1 . THR A 1 606  ? 30.607 94.933  -25.652 1.00 24.56 ? 606  THR A OG1 1 
ATOM   4914 C  CG2 . THR A 1 606  ? 28.275 94.898  -26.131 1.00 22.50 ? 606  THR A CG2 1 
ATOM   4915 N  N   . ILE A 1 607  ? 30.559 91.758  -23.963 1.00 18.64 ? 607  ILE A N   1 
ATOM   4916 C  CA  . ILE A 1 607  ? 31.745 90.946  -23.707 1.00 17.27 ? 607  ILE A CA  1 
ATOM   4917 C  C   . ILE A 1 607  ? 32.430 90.709  -25.058 1.00 16.32 ? 607  ILE A C   1 
ATOM   4918 O  O   . ILE A 1 607  ? 31.843 90.127  -25.972 1.00 15.60 ? 607  ILE A O   1 
ATOM   4919 C  CB  . ILE A 1 607  ? 31.329 89.618  -23.089 1.00 17.28 ? 607  ILE A CB  1 
ATOM   4920 C  CG1 . ILE A 1 607  ? 30.512 89.850  -21.817 1.00 18.49 ? 607  ILE A CG1 1 
ATOM   4921 C  CG2 . ILE A 1 607  ? 32.576 88.767  -22.780 1.00 17.35 ? 607  ILE A CG2 1 
ATOM   4922 C  CD1 . ILE A 1 607  ? 29.743 88.622  -21.370 1.00 21.94 ? 607  ILE A CD1 1 
ATOM   4923 N  N   . HIS A 1 608  ? 33.669 91.170  -25.213 1.00 16.42 ? 608  HIS A N   1 
ATOM   4924 C  CA  . HIS A 1 608  ? 34.268 91.136  -26.542 1.00 16.74 ? 608  HIS A CA  1 
ATOM   4925 C  C   . HIS A 1 608  ? 35.765 90.979  -26.416 1.00 15.26 ? 608  HIS A C   1 
ATOM   4926 O  O   . HIS A 1 608  ? 36.328 91.288  -25.363 1.00 16.90 ? 608  HIS A O   1 
ATOM   4927 C  CB  . HIS A 1 608  ? 33.913 92.387  -27.363 1.00 18.17 ? 608  HIS A CB  1 
ATOM   4928 C  CG  . HIS A 1 608  ? 34.452 93.659  -26.792 1.00 21.21 ? 608  HIS A CG  1 
ATOM   4929 N  ND1 . HIS A 1 608  ? 35.409 94.417  -27.434 1.00 27.51 ? 608  HIS A ND1 1 
ATOM   4930 C  CD2 . HIS A 1 608  ? 34.168 94.306  -25.636 1.00 25.65 ? 608  HIS A CD2 1 
ATOM   4931 C  CE1 . HIS A 1 608  ? 35.688 95.482  -26.696 1.00 27.85 ? 608  HIS A CE1 1 
ATOM   4932 N  NE2 . HIS A 1 608  ? 34.943 95.441  -25.604 1.00 27.85 ? 608  HIS A NE2 1 
ATOM   4933 N  N   . PRO A 1 609  ? 36.405 90.484  -27.466 1.00 14.98 ? 609  PRO A N   1 
ATOM   4934 C  CA  . PRO A 1 609  ? 37.836 90.211  -27.411 1.00 15.28 ? 609  PRO A CA  1 
ATOM   4935 C  C   . PRO A 1 609  ? 38.702 91.371  -27.853 1.00 16.19 ? 609  PRO A C   1 
ATOM   4936 O  O   . PRO A 1 609  ? 38.335 92.158  -28.735 1.00 18.13 ? 609  PRO A O   1 
ATOM   4937 C  CB  . PRO A 1 609  ? 37.986 89.051  -28.402 1.00 15.23 ? 609  PRO A CB  1 
ATOM   4938 C  CG  . PRO A 1 609  ? 36.968 89.304  -29.456 1.00 15.15 ? 609  PRO A CG  1 
ATOM   4939 C  CD  . PRO A 1 609  ? 35.829 90.046  -28.752 1.00 14.00 ? 609  PRO A CD  1 
ATOM   4940 N  N   . GLN A 1 610  ? 39.880 91.416  -27.244 1.00 15.76 ? 610  GLN A N   1 
ATOM   4941 C  CA  . GLN A 1 610  ? 40.918 92.362  -27.602 1.00 17.79 ? 610  GLN A CA  1 
ATOM   4942 C  C   . GLN A 1 610  ? 42.169 91.568  -27.938 1.00 16.32 ? 610  GLN A C   1 
ATOM   4943 O  O   . GLN A 1 610  ? 42.480 90.577  -27.265 1.00 15.98 ? 610  GLN A O   1 
ATOM   4944 C  CB  . GLN A 1 610  ? 41.162 93.339  -26.452 1.00 18.97 ? 610  GLN A CB  1 
ATOM   4945 C  CG  . GLN A 1 610  ? 39.923 94.249  -26.216 1.00 24.23 ? 610  GLN A CG  1 
ATOM   4946 C  CD  . GLN A 1 610  ? 39.630 95.238  -27.374 1.00 29.09 ? 610  GLN A CD  1 
ATOM   4947 O  OE1 . GLN A 1 610  ? 38.646 95.081  -28.128 1.00 30.84 ? 610  GLN A OE1 1 
ATOM   4948 N  NE2 . GLN A 1 610  ? 40.468 96.261  -27.499 1.00 31.77 ? 610  GLN A NE2 1 
ATOM   4949 N  N   . GLY A 1 611  ? 42.852 91.978  -28.987 1.00 16.16 ? 611  GLY A N   1 
ATOM   4950 C  CA  . GLY A 1 611  ? 44.063 91.293  -29.418 1.00 16.11 ? 611  GLY A CA  1 
ATOM   4951 C  C   . GLY A 1 611  ? 45.289 92.024  -28.915 1.00 16.61 ? 611  GLY A C   1 
ATOM   4952 O  O   . GLY A 1 611  ? 45.311 93.267  -28.805 1.00 16.60 ? 611  GLY A O   1 
ATOM   4953 N  N   . SER A 1 612  ? 46.321 91.262  -28.582 1.00 16.84 ? 612  SER A N   1 
ATOM   4954 C  CA  . SER A 1 612  ? 47.581 91.881  -28.178 1.00 17.44 ? 612  SER A CA  1 
ATOM   4955 C  C   . SER A 1 612  ? 48.275 92.494  -29.379 1.00 17.32 ? 612  SER A C   1 
ATOM   4956 O  O   . SER A 1 612  ? 48.237 91.961  -30.488 1.00 17.80 ? 612  SER A O   1 
ATOM   4957 C  CB  . SER A 1 612  ? 48.504 90.842  -27.538 1.00 16.59 ? 612  SER A CB  1 
ATOM   4958 O  OG  . SER A 1 612  ? 49.727 91.465  -27.157 1.00 17.86 ? 612  SER A OG  1 
ATOM   4959 N  N   . THR A 1 613  ? 48.951 93.621  -29.145 1.00 20.79 ? 613  THR A N   1 
ATOM   4960 C  CA  . THR A 1 613  ? 49.763 94.189  -30.208 1.00 21.41 ? 613  THR A CA  1 
ATOM   4961 C  C   . THR A 1 613  ? 51.256 93.935  -29.940 1.00 22.44 ? 613  THR A C   1 
ATOM   4962 O  O   . THR A 1 613  ? 52.104 94.407  -30.711 1.00 23.71 ? 613  THR A O   1 
ATOM   4963 C  CB  . THR A 1 613  ? 49.496 95.695  -30.374 1.00 22.51 ? 613  THR A CB  1 
ATOM   4964 O  OG1 . THR A 1 613  ? 49.794 96.350  -29.143 1.00 23.97 ? 613  THR A OG1 1 
ATOM   4965 C  CG2 . THR A 1 613  ? 47.992 95.973  -30.582 1.00 21.98 ? 613  THR A CG2 1 
ATOM   4966 N  N   . THR A 1 614  ? 51.560 93.186  -28.876 1.00 22.19 ? 614  THR A N   1 
ATOM   4967 C  CA  . THR A 1 614  ? 52.951 92.979  -28.454 1.00 22.92 ? 614  THR A CA  1 
ATOM   4968 C  C   . THR A 1 614  ? 53.375 91.523  -28.342 1.00 21.94 ? 614  THR A C   1 
ATOM   4969 O  O   . THR A 1 614  ? 54.573 91.222  -28.323 1.00 22.46 ? 614  THR A O   1 
ATOM   4970 C  CB  . THR A 1 614  ? 53.234 93.677  -27.118 1.00 22.28 ? 614  THR A CB  1 
ATOM   4971 O  OG1 . THR A 1 614  ? 52.276 93.299  -26.121 1.00 26.40 ? 614  THR A OG1 1 
ATOM   4972 C  CG2 . THR A 1 614  ? 53.102 95.211  -27.237 1.00 25.36 ? 614  THR A CG2 1 
ATOM   4973 N  N   . LYS A 1 615  ? 52.404 90.624  -28.236 1.00 19.38 ? 615  LYS A N   1 
ATOM   4974 C  CA  . LYS A 1 615  ? 52.732 89.207  -28.153 1.00 18.17 ? 615  LYS A CA  1 
ATOM   4975 C  C   . LYS A 1 615  ? 51.791 88.401  -29.032 1.00 16.76 ? 615  LYS A C   1 
ATOM   4976 O  O   . LYS A 1 615  ? 50.672 88.833  -29.330 1.00 16.38 ? 615  LYS A O   1 
ATOM   4977 C  CB  . LYS A 1 615  ? 52.799 88.685  -26.714 1.00 19.45 ? 615  LYS A CB  1 
ATOM   4978 C  CG  . LYS A 1 615  ? 51.520 88.704  -25.928 1.00 20.36 ? 615  LYS A CG  1 
ATOM   4979 C  CD  . LYS A 1 615  ? 51.750 88.198  -24.493 1.00 20.79 ? 615  LYS A CD  1 
ATOM   4980 C  CE  . LYS A 1 615  ? 50.451 88.141  -23.721 1.00 22.18 ? 615  LYS A CE  1 
ATOM   4981 N  NZ  . LYS A 1 615  ? 50.688 88.141  -22.230 1.00 25.46 ? 615  LYS A NZ  1 
ATOM   4982 N  N   . TYR A 1 616  ? 52.271 87.232  -29.442 1.00 14.49 ? 616  TYR A N   1 
ATOM   4983 C  CA  . TYR A 1 616  ? 51.617 86.380  -30.428 1.00 14.07 ? 616  TYR A CA  1 
ATOM   4984 C  C   . TYR A 1 616  ? 51.768 84.956  -29.971 1.00 13.14 ? 616  TYR A C   1 
ATOM   4985 O  O   . TYR A 1 616  ? 52.672 84.644  -29.184 1.00 13.48 ? 616  TYR A O   1 
ATOM   4986 C  CB  . TYR A 1 616  ? 52.288 86.556  -31.803 1.00 14.80 ? 616  TYR A CB  1 
ATOM   4987 C  CG  . TYR A 1 616  ? 52.294 88.017  -32.157 1.00 16.53 ? 616  TYR A CG  1 
ATOM   4988 C  CD1 . TYR A 1 616  ? 51.158 88.611  -32.722 1.00 16.19 ? 616  TYR A CD1 1 
ATOM   4989 C  CD2 . TYR A 1 616  ? 53.374 88.829  -31.803 1.00 16.89 ? 616  TYR A CD2 1 
ATOM   4990 C  CE1 . TYR A 1 616  ? 51.119 89.980  -32.969 1.00 19.94 ? 616  TYR A CE1 1 
ATOM   4991 C  CE2 . TYR A 1 616  ? 53.353 90.201  -32.064 1.00 19.09 ? 616  TYR A CE2 1 
ATOM   4992 C  CZ  . TYR A 1 616  ? 52.216 90.751  -32.648 1.00 18.38 ? 616  TYR A CZ  1 
ATOM   4993 O  OH  . TYR A 1 616  ? 52.175 92.109  -32.912 1.00 23.34 ? 616  TYR A OH  1 
ATOM   4994 N  N   . ARG A 1 617  ? 50.907 84.078  -30.465 1.00 12.57 ? 617  ARG A N   1 
ATOM   4995 C  CA  . ARG A 1 617  ? 50.986 82.655  -30.122 1.00 13.97 ? 617  ARG A CA  1 
ATOM   4996 C  C   . ARG A 1 617  ? 51.614 81.917  -31.273 1.00 13.57 ? 617  ARG A C   1 
ATOM   4997 O  O   . ARG A 1 617  ? 51.137 82.053  -32.414 1.00 14.62 ? 617  ARG A O   1 
ATOM   4998 C  CB  . ARG A 1 617  ? 49.584 82.072  -29.936 1.00 14.95 ? 617  ARG A CB  1 
ATOM   4999 C  CG  . ARG A 1 617  ? 48.881 82.402  -28.665 1.00 19.19 ? 617  ARG A CG  1 
ATOM   5000 C  CD  . ARG A 1 617  ? 47.499 81.748  -28.585 1.00 18.94 ? 617  ARG A CD  1 
ATOM   5001 N  NE  . ARG A 1 617  ? 47.545 80.288  -28.627 1.00 20.25 ? 617  ARG A NE  1 
ATOM   5002 C  CZ  . ARG A 1 617  ? 46.855 79.513  -29.473 1.00 22.28 ? 617  ARG A CZ  1 
ATOM   5003 N  NH1 . ARG A 1 617  ? 46.039 80.037  -30.387 1.00 21.10 ? 617  ARG A NH1 1 
ATOM   5004 N  NH2 . ARG A 1 617  ? 46.984 78.198  -29.413 1.00 20.11 ? 617  ARG A NH2 1 
ATOM   5005 N  N   . ILE A 1 618  ? 52.647 81.120  -31.019 1.00 12.34 ? 618  ILE A N   1 
ATOM   5006 C  CA  . ILE A 1 618  ? 53.152 80.220  -32.040 1.00 12.52 ? 618  ILE A CA  1 
ATOM   5007 C  C   . ILE A 1 618  ? 52.805 78.796  -31.662 1.00 11.32 ? 618  ILE A C   1 
ATOM   5008 O  O   . ILE A 1 618  ? 52.965 78.404  -30.508 1.00 12.03 ? 618  ILE A O   1 
ATOM   5009 C  CB  . ILE A 1 618  ? 54.646 80.406  -32.300 1.00 12.19 ? 618  ILE A CB  1 
ATOM   5010 C  CG1 . ILE A 1 618  ? 55.050 79.551  -33.499 1.00 14.65 ? 618  ILE A CG1 1 
ATOM   5011 C  CG2 . ILE A 1 618  ? 55.518 80.113  -31.041 1.00 13.76 ? 618  ILE A CG2 1 
ATOM   5012 C  CD1 . ILE A 1 618  ? 56.335 79.960  -34.159 1.00 13.94 ? 618  ILE A CD1 1 
ATOM   5013 N  N   . ILE A 1 619  ? 52.344 78.025  -32.630 1.00 11.50 ? 619  ILE A N   1 
ATOM   5014 C  CA  . ILE A 1 619  ? 51.855 76.660  -32.431 1.00 11.31 ? 619  ILE A CA  1 
ATOM   5015 C  C   . ILE A 1 619  ? 52.566 75.721  -33.371 1.00 11.35 ? 619  ILE A C   1 
ATOM   5016 O  O   . ILE A 1 619  ? 52.755 76.051  -34.565 1.00 11.05 ? 619  ILE A O   1 
ATOM   5017 C  CB  . ILE A 1 619  ? 50.343 76.641  -32.798 1.00 13.92 ? 619  ILE A CB  1 
ATOM   5018 C  CG1 . ILE A 1 619  ? 49.597 77.683  -31.974 1.00 16.36 ? 619  ILE A CG1 1 
ATOM   5019 C  CG2 . ILE A 1 619  ? 49.722 75.283  -32.653 1.00 17.29 ? 619  ILE A CG2 1 
ATOM   5020 C  CD1 . ILE A 1 619  ? 48.519 78.401  -32.778 1.00 17.85 ? 619  ILE A CD1 1 
ATOM   5021 N  N   . PHE A 1 620  ? 52.988 74.554  -32.908 1.00 9.95  ? 620  PHE A N   1 
ATOM   5022 C  CA  . PHE A 1 620  ? 53.641 73.594  -33.784 1.00 9.82  ? 620  PHE A CA  1 
ATOM   5023 C  C   . PHE A 1 620  ? 53.510 72.208  -33.158 1.00 10.15 ? 620  PHE A C   1 
ATOM   5024 O  O   . PHE A 1 620  ? 53.219 72.070  -31.959 1.00 10.47 ? 620  PHE A O   1 
ATOM   5025 C  CB  . PHE A 1 620  ? 55.117 73.964  -33.998 1.00 9.39  ? 620  PHE A CB  1 
ATOM   5026 C  CG  . PHE A 1 620  ? 55.982 73.891  -32.740 1.00 9.42  ? 620  PHE A CG  1 
ATOM   5027 C  CD1 . PHE A 1 620  ? 56.165 75.009  -31.945 1.00 10.72 ? 620  PHE A CD1 1 
ATOM   5028 C  CD2 . PHE A 1 620  ? 56.679 72.715  -32.414 1.00 11.72 ? 620  PHE A CD2 1 
ATOM   5029 C  CE1 . PHE A 1 620  ? 56.976 74.941  -30.794 1.00 10.50 ? 620  PHE A CE1 1 
ATOM   5030 C  CE2 . PHE A 1 620  ? 57.500 72.655  -31.289 1.00 11.19 ? 620  PHE A CE2 1 
ATOM   5031 C  CZ  . PHE A 1 620  ? 57.640 73.763  -30.491 1.00 11.62 ? 620  PHE A CZ  1 
ATOM   5032 N  N   . LYS A 1 621  ? 53.714 71.189  -33.968 1.00 10.14 ? 621  LYS A N   1 
ATOM   5033 C  CA  . LYS A 1 621  ? 53.639 69.829  -33.488 1.00 11.26 ? 621  LYS A CA  1 
ATOM   5034 C  C   . LYS A 1 621  ? 54.948 69.380  -32.886 1.00 11.19 ? 621  LYS A C   1 
ATOM   5035 O  O   . LYS A 1 621  ? 55.982 69.393  -33.545 1.00 12.68 ? 621  LYS A O   1 
ATOM   5036 C  CB  . LYS A 1 621  ? 53.226 68.919  -34.640 1.00 12.22 ? 621  LYS A CB  1 
ATOM   5037 C  CG  . LYS A 1 621  ? 52.831 67.526  -34.185 1.00 14.87 ? 621  LYS A CG  1 
ATOM   5038 C  CD  . LYS A 1 621  ? 51.906 66.855  -35.189 1.00 21.98 ? 621  LYS A CD  1 
ATOM   5039 C  CE  . LYS A 1 621  ? 52.574 66.695  -36.530 1.00 23.54 ? 621  LYS A CE  1 
ATOM   5040 N  NZ  . LYS A 1 621  ? 51.686 66.006  -37.528 1.00 28.43 ? 621  LYS A NZ  1 
ATOM   5041 N  N   . ALA A 1 622  ? 54.909 69.012  -31.611 1.00 11.17 ? 622  ALA A N   1 
ATOM   5042 C  CA  . ALA A 1 622  ? 56.070 68.419  -30.970 1.00 11.06 ? 622  ALA A CA  1 
ATOM   5043 C  C   . ALA A 1 622  ? 55.960 66.905  -30.998 1.00 11.41 ? 622  ALA A C   1 
ATOM   5044 O  O   . ALA A 1 622  ? 54.891 66.374  -30.759 1.00 12.70 ? 622  ALA A O   1 
ATOM   5045 C  CB  . ALA A 1 622  ? 56.186 68.898  -29.503 1.00 11.32 ? 622  ALA A CB  1 
ATOM   5046 N  N   . ARG A 1 623  ? 57.064 66.228  -31.279 1.00 10.52 ? 623  ARG A N   1 
ATOM   5047 C  CA  . ARG A 1 623  ? 57.091 64.766  -31.295 1.00 11.07 ? 623  ARG A CA  1 
ATOM   5048 C  C   . ARG A 1 623  ? 58.069 64.340  -30.232 1.00 10.00 ? 623  ARG A C   1 
ATOM   5049 O  O   . ARG A 1 623  ? 59.229 64.732  -30.249 1.00 11.00 ? 623  ARG A O   1 
ATOM   5050 C  CB  . ARG A 1 623  ? 57.539 64.253  -32.669 1.00 12.20 ? 623  ARG A CB  1 
ATOM   5051 C  CG  . ARG A 1 623  ? 57.622 62.741  -32.739 1.00 14.44 ? 623  ARG A CG  1 
ATOM   5052 C  CD  . ARG A 1 623  ? 57.862 62.194  -34.188 1.00 15.90 ? 623  ARG A CD  1 
ATOM   5053 N  NE  . ARG A 1 623  ? 57.874 60.729  -34.150 1.00 20.29 ? 623  ARG A NE  1 
ATOM   5054 C  CZ  . ARG A 1 623  ? 58.981 60.020  -34.031 1.00 23.34 ? 623  ARG A CZ  1 
ATOM   5055 N  NH1 . ARG A 1 623  ? 60.158 60.630  -33.970 1.00 25.84 ? 623  ARG A NH1 1 
ATOM   5056 N  NH2 . ARG A 1 623  ? 58.916 58.701  -33.953 1.00 23.63 ? 623  ARG A NH2 1 
ATOM   5057 N  N   . VAL A 1 624  ? 57.568 63.591  -29.259 1.00 9.32  ? 624  VAL A N   1 
ATOM   5058 C  CA  . VAL A 1 624  ? 58.307 63.336  -28.017 1.00 8.93  ? 624  VAL A CA  1 
ATOM   5059 C  C   . VAL A 1 624  ? 58.348 61.833  -27.699 1.00 8.53  ? 624  VAL A C   1 
ATOM   5060 O  O   . VAL A 1 624  ? 57.335 61.155  -27.810 1.00 9.09  ? 624  VAL A O   1 
ATOM   5061 C  CB  . VAL A 1 624  ? 57.664 64.115  -26.839 1.00 9.01  ? 624  VAL A CB  1 
ATOM   5062 C  CG1 . VAL A 1 624  ? 58.614 64.111  -25.636 1.00 10.65 ? 624  VAL A CG1 1 
ATOM   5063 C  CG2 . VAL A 1 624  ? 57.358 65.566  -27.255 1.00 10.33 ? 624  VAL A CG2 1 
ATOM   5064 N  N   . PRO A 1 625  ? 59.543 61.328  -27.343 1.00 9.27  ? 625  PRO A N   1 
ATOM   5065 C  CA  . PRO A 1 625  ? 59.672 59.889  -27.060 1.00 9.11  ? 625  PRO A CA  1 
ATOM   5066 C  C   . PRO A 1 625  ? 58.806 59.439  -25.867 1.00 9.24  ? 625  PRO A C   1 
ATOM   5067 O  O   . PRO A 1 625  ? 58.395 60.264  -25.018 1.00 8.99  ? 625  PRO A O   1 
ATOM   5068 C  CB  . PRO A 1 625  ? 61.166 59.722  -26.720 1.00 10.45 ? 625  PRO A CB  1 
ATOM   5069 C  CG  . PRO A 1 625  ? 61.858 60.884  -27.377 1.00 11.07 ? 625  PRO A CG  1 
ATOM   5070 C  CD  . PRO A 1 625  ? 60.844 62.023  -27.234 1.00 9.72  ? 625  PRO A CD  1 
ATOM   5071 N  N   . PRO A 1 626  ? 58.595 58.140  -25.740 1.00 9.09  ? 626  PRO A N   1 
ATOM   5072 C  CA  . PRO A 1 626  ? 57.917 57.595  -24.542 1.00 8.51  ? 626  PRO A CA  1 
ATOM   5073 C  C   . PRO A 1 626  ? 58.693 58.024  -23.302 1.00 8.61  ? 626  PRO A C   1 
ATOM   5074 O  O   . PRO A 1 626  ? 59.920 57.857  -23.231 1.00 8.72  ? 626  PRO A O   1 
ATOM   5075 C  CB  . PRO A 1 626  ? 58.060 56.073  -24.723 1.00 8.79  ? 626  PRO A CB  1 
ATOM   5076 C  CG  . PRO A 1 626  ? 58.317 55.890  -26.242 1.00 10.20 ? 626  PRO A CG  1 
ATOM   5077 C  CD  . PRO A 1 626  ? 59.107 57.076  -26.637 1.00 10.53 ? 626  PRO A CD  1 
ATOM   5078 N  N   . MET A 1 627  ? 57.982 58.582  -22.317 1.00 7.45  ? 627  MET A N   1 
ATOM   5079 C  CA  . MET A 1 627  ? 58.626 58.959  -21.029 1.00 7.76  ? 627  MET A CA  1 
ATOM   5080 C  C   . MET A 1 627  ? 59.893 59.773  -21.279 1.00 8.03  ? 627  MET A C   1 
ATOM   5081 O  O   . MET A 1 627  ? 60.915 59.608  -20.616 1.00 9.06  ? 627  MET A O   1 
ATOM   5082 C  CB  . MET A 1 627  ? 58.905 57.727  -20.173 1.00 8.74  ? 627  MET A CB  1 
ATOM   5083 C  CG  . MET A 1 627  ? 57.612 57.018  -19.823 1.00 8.43  ? 627  MET A CG  1 
ATOM   5084 S  SD  . MET A 1 627  ? 57.805 55.346  -19.136 1.00 11.27 ? 627  MET A SD  1 
ATOM   5085 C  CE  . MET A 1 627  ? 58.710 55.663  -17.690 1.00 12.34 ? 627  MET A CE  1 
ATOM   5086 N  N   . GLY A 1 628  ? 59.819 60.660  -22.273 1.00 7.91  ? 628  GLY A N   1 
ATOM   5087 C  CA  . GLY A 1 628  ? 61.028 61.300  -22.781 1.00 8.96  ? 628  GLY A CA  1 
ATOM   5088 C  C   . GLY A 1 628  ? 60.915 62.789  -23.004 1.00 8.47  ? 628  GLY A C   1 
ATOM   5089 O  O   . GLY A 1 628  ? 59.922 63.425  -22.594 1.00 8.30  ? 628  GLY A O   1 
ATOM   5090 N  N   . LEU A 1 629  ? 61.950 63.346  -23.636 1.00 8.21  ? 629  LEU A N   1 
ATOM   5091 C  CA  . LEU A 1 629  ? 62.093 64.803  -23.836 1.00 8.65  ? 629  LEU A CA  1 
ATOM   5092 C  C   . LEU A 1 629  ? 62.509 65.078  -25.273 1.00 8.92  ? 629  LEU A C   1 
ATOM   5093 O  O   . LEU A 1 629  ? 63.282 64.295  -25.882 1.00 9.54  ? 629  LEU A O   1 
ATOM   5094 C  CB  . LEU A 1 629  ? 63.180 65.408  -22.935 1.00 8.53  ? 629  LEU A CB  1 
ATOM   5095 C  CG  . LEU A 1 629  ? 62.956 65.264  -21.435 1.00 8.84  ? 629  LEU A CG  1 
ATOM   5096 C  CD1 . LEU A 1 629  ? 64.227 65.468  -20.653 1.00 9.64  ? 629  LEU A CD1 1 
ATOM   5097 C  CD2 . LEU A 1 629  ? 61.878 66.254  -20.990 1.00 9.25  ? 629  LEU A CD2 1 
ATOM   5098 N  N   . ALA A 1 630  ? 62.060 66.217  -25.788 1.00 8.63  ? 630  ALA A N   1 
ATOM   5099 C  CA  . ALA A 1 630  ? 62.436 66.667  -27.140 1.00 9.39  ? 630  ALA A CA  1 
ATOM   5100 C  C   . ALA A 1 630  ? 62.660 68.157  -27.117 1.00 9.53  ? 630  ALA A C   1 
ATOM   5101 O  O   . ALA A 1 630  ? 61.841 68.910  -26.583 1.00 9.81  ? 630  ALA A O   1 
ATOM   5102 C  CB  . ALA A 1 630  ? 61.393 66.307  -28.160 1.00 10.33 ? 630  ALA A CB  1 
ATOM   5103 N  N   . THR A 1 631  ? 63.762 68.596  -27.717 1.00 9.45  ? 631  THR A N   1 
ATOM   5104 C  CA  . THR A 1 631  ? 64.152 70.025  -27.752 1.00 10.74 ? 631  THR A CA  1 
ATOM   5105 C  C   . THR A 1 631  ? 63.849 70.670  -29.106 1.00 10.90 ? 631  THR A C   1 
ATOM   5106 O  O   . THR A 1 631  ? 64.097 70.055  -30.161 1.00 11.07 ? 631  THR A O   1 
ATOM   5107 C  CB  . THR A 1 631  ? 65.661 70.104  -27.482 1.00 11.47 ? 631  THR A CB  1 
ATOM   5108 O  OG1 . THR A 1 631  ? 65.931 69.420  -26.246 1.00 10.55 ? 631  THR A OG1 1 
ATOM   5109 C  CG2 . THR A 1 631  ? 66.163 71.566  -27.271 1.00 13.21 ? 631  THR A CG2 1 
ATOM   5110 N  N   . TYR A 1 632  ? 63.325 71.888  -29.080 1.00 10.16 ? 632  TYR A N   1 
ATOM   5111 C  CA  . TYR A 1 632  ? 63.099 72.673  -30.292 1.00 10.17 ? 632  TYR A CA  1 
ATOM   5112 C  C   . TYR A 1 632  ? 63.666 74.058  -30.090 1.00 10.39 ? 632  TYR A C   1 
ATOM   5113 O  O   . TYR A 1 632  ? 63.990 74.478  -28.981 1.00 10.57 ? 632  TYR A O   1 
ATOM   5114 C  CB  . TYR A 1 632  ? 61.602 72.761  -30.619 1.00 11.21 ? 632  TYR A CB  1 
ATOM   5115 C  CG  . TYR A 1 632  ? 61.014 71.435  -31.019 1.00 10.92 ? 632  TYR A CG  1 
ATOM   5116 C  CD1 . TYR A 1 632  ? 60.601 70.500  -30.048 1.00 11.47 ? 632  TYR A CD1 1 
ATOM   5117 C  CD2 . TYR A 1 632  ? 60.813 71.110  -32.367 1.00 11.37 ? 632  TYR A CD2 1 
ATOM   5118 C  CE1 . TYR A 1 632  ? 60.071 69.268  -30.434 1.00 12.14 ? 632  TYR A CE1 1 
ATOM   5119 C  CE2 . TYR A 1 632  ? 60.285 69.890  -32.750 1.00 12.37 ? 632  TYR A CE2 1 
ATOM   5120 C  CZ  . TYR A 1 632  ? 59.915 68.977  -31.783 1.00 12.01 ? 632  TYR A CZ  1 
ATOM   5121 O  OH  . TYR A 1 632  ? 59.405 67.756  -32.169 1.00 13.60 ? 632  TYR A OH  1 
ATOM   5122 N  N   . VAL A 1 633  ? 63.829 74.772  -31.208 1.00 10.52 ? 633  VAL A N   1 
ATOM   5123 C  CA  . VAL A 1 633  ? 64.377 76.117  -31.199 1.00 11.38 ? 633  VAL A CA  1 
ATOM   5124 C  C   . VAL A 1 633  ? 63.432 77.054  -31.934 1.00 10.38 ? 633  VAL A C   1 
ATOM   5125 O  O   . VAL A 1 633  ? 62.960 76.732  -33.011 1.00 10.78 ? 633  VAL A O   1 
ATOM   5126 C  CB  . VAL A 1 633  ? 65.776 76.158  -31.876 1.00 11.34 ? 633  VAL A CB  1 
ATOM   5127 C  CG1 . VAL A 1 633  ? 66.359 77.567  -31.834 1.00 13.39 ? 633  VAL A CG1 1 
ATOM   5128 C  CG2 . VAL A 1 633  ? 66.719 75.188  -31.169 1.00 13.63 ? 633  VAL A CG2 1 
ATOM   5129 N  N   . LEU A 1 634  ? 63.136 78.185  -31.310 1.00 10.15 ? 634  LEU A N   1 
ATOM   5130 C  CA  . LEU A 1 634  ? 62.328 79.250  -31.908 1.00 10.82 ? 634  LEU A CA  1 
ATOM   5131 C  C   . LEU A 1 634  ? 63.266 80.387  -32.288 1.00 11.66 ? 634  LEU A C   1 
ATOM   5132 O  O   . LEU A 1 634  ? 64.034 80.847  -31.448 1.00 11.65 ? 634  LEU A O   1 
ATOM   5133 C  CB  . LEU A 1 634  ? 61.303 79.779  -30.903 1.00 11.38 ? 634  LEU A CB  1 
ATOM   5134 C  CG  . LEU A 1 634  ? 60.354 78.790  -30.226 1.00 17.36 ? 634  LEU A CG  1 
ATOM   5135 C  CD1 . LEU A 1 634  ? 59.219 79.554  -29.576 1.00 16.97 ? 634  LEU A CD1 1 
ATOM   5136 C  CD2 . LEU A 1 634  ? 59.817 77.760  -31.138 1.00 20.45 ? 634  LEU A CD2 1 
ATOM   5137 N  N   . THR A 1 635  ? 63.189 80.814  -33.566 1.00 12.00 ? 635  THR A N   1 
ATOM   5138 C  CA  . THR A 1 635  ? 64.126 81.821  -34.090 1.00 12.55 ? 635  THR A CA  1 
ATOM   5139 C  C   . THR A 1 635  ? 63.354 82.960  -34.742 1.00 13.64 ? 635  THR A C   1 
ATOM   5140 O  O   . THR A 1 635  ? 62.437 82.728  -35.530 1.00 13.88 ? 635  THR A O   1 
ATOM   5141 C  CB  . THR A 1 635  ? 65.072 81.164  -35.130 1.00 13.76 ? 635  THR A CB  1 
ATOM   5142 O  OG1 . THR A 1 635  ? 65.782 80.080  -34.498 1.00 13.89 ? 635  THR A OG1 1 
ATOM   5143 C  CG2 . THR A 1 635  ? 66.190 82.161  -35.564 1.00 14.33 ? 635  THR A CG2 1 
ATOM   5144 N  N   . ILE A 1 636  ? 63.750 84.191  -34.428 1.00 14.66 ? 636  ILE A N   1 
ATOM   5145 C  CA  . ILE A 1 636  ? 63.092 85.352  -35.038 1.00 16.17 ? 636  ILE A CA  1 
ATOM   5146 C  C   . ILE A 1 636  ? 63.707 85.629  -36.415 1.00 18.15 ? 636  ILE A C   1 
ATOM   5147 O  O   . ILE A 1 636  ? 64.888 85.340  -36.656 1.00 17.63 ? 636  ILE A O   1 
ATOM   5148 C  CB  . ILE A 1 636  ? 63.191 86.594  -34.112 1.00 15.95 ? 636  ILE A CB  1 
ATOM   5149 C  CG1 . ILE A 1 636  ? 62.195 87.684  -34.538 1.00 16.16 ? 636  ILE A CG1 1 
ATOM   5150 C  CG2 . ILE A 1 636  ? 64.647 87.123  -34.021 1.00 16.84 ? 636  ILE A CG2 1 
ATOM   5151 C  CD1 . ILE A 1 636  ? 62.140 88.879  -33.567 1.00 18.24 ? 636  ILE A CD1 1 
ATOM   5152 N  N   . SER A 1 637  ? 62.884 86.167  -37.314 1.00 19.54 ? 637  SER A N   1 
ATOM   5153 C  CA  . SER A 1 637  ? 63.392 86.723  -38.574 1.00 22.09 ? 637  SER A CA  1 
ATOM   5154 C  C   . SER A 1 637  ? 62.765 88.093  -38.835 1.00 23.37 ? 637  SER A C   1 
ATOM   5155 O  O   . SER A 1 637  ? 61.876 88.520  -38.103 1.00 22.37 ? 637  SER A O   1 
ATOM   5156 C  CB  . SER A 1 637  ? 63.148 85.751  -39.729 1.00 23.72 ? 637  SER A CB  1 
ATOM   5157 O  OG  . SER A 1 637  ? 61.762 85.530  -39.907 1.00 26.61 ? 637  SER A OG  1 
ATOM   5158 N  N   . ASP A 1 638  ? 63.252 88.801  -39.863 1.00 25.58 ? 638  ASP A N   1 
ATOM   5159 C  CA  . ASP A 1 638  ? 62.726 90.143  -40.145 1.00 27.73 ? 638  ASP A CA  1 
ATOM   5160 C  C   . ASP A 1 638  ? 61.374 90.123  -40.864 1.00 27.64 ? 638  ASP A C   1 
ATOM   5161 O  O   . ASP A 1 638  ? 60.626 91.114  -40.831 1.00 29.11 ? 638  ASP A O   1 
ATOM   5162 C  CB  . ASP A 1 638  ? 63.750 91.035  -40.877 1.00 28.45 ? 638  ASP A CB  1 
ATOM   5163 C  CG  . ASP A 1 638  ? 64.160 90.492  -42.241 1.00 31.87 ? 638  ASP A CG  1 
ATOM   5164 O  OD1 . ASP A 1 638  ? 63.986 89.282  -42.524 1.00 35.36 ? 638  ASP A OD1 1 
ATOM   5165 O  OD2 . ASP A 1 638  ? 64.688 91.230  -43.107 1.00 37.05 ? 638  ASP A OD2 1 
ATOM   5166 N  N   . SER A 1 639  ? 61.052 88.992  -41.485 1.00 27.19 ? 639  SER A N   1 
ATOM   5167 C  CA  . SER A 1 639  ? 59.809 88.851  -42.231 1.00 27.12 ? 639  SER A CA  1 
ATOM   5168 C  C   . SER A 1 639  ? 59.241 87.439  -42.126 1.00 26.74 ? 639  SER A C   1 
ATOM   5169 O  O   . SER A 1 639  ? 59.859 86.562  -41.507 1.00 25.30 ? 639  SER A O   1 
ATOM   5170 C  CB  . SER A 1 639  ? 60.039 89.226  -43.703 1.00 27.35 ? 639  SER A CB  1 
ATOM   5171 O  OG  . SER A 1 639  ? 61.029 88.391  -44.284 1.00 29.08 ? 639  SER A OG  1 
ATOM   5172 N  N   . LYS A 1 640  ? 58.076 87.227  -42.741 1.00 25.63 ? 640  LYS A N   1 
ATOM   5173 C  CA  . LYS A 1 640  ? 57.393 85.933  -42.717 1.00 25.14 ? 640  LYS A CA  1 
ATOM   5174 C  C   . LYS A 1 640  ? 58.356 84.798  -43.053 1.00 24.24 ? 640  LYS A C   1 
ATOM   5175 O  O   . LYS A 1 640  ? 58.931 84.767  -44.142 1.00 24.45 ? 640  LYS A O   1 
ATOM   5176 C  CB  . LYS A 1 640  ? 56.220 85.901  -43.702 1.00 25.32 ? 640  LYS A CB  1 
ATOM   5177 C  CG  . LYS A 1 640  ? 54.991 86.747  -43.375 1.00 27.87 ? 640  LYS A CG  1 
ATOM   5178 C  CD  . LYS A 1 640  ? 53.817 86.236  -44.233 1.00 29.87 ? 640  LYS A CD  1 
ATOM   5179 C  CE  . LYS A 1 640  ? 52.700 87.246  -44.372 1.00 31.22 ? 640  LYS A CE  1 
ATOM   5180 N  NZ  . LYS A 1 640  ? 51.374 86.575  -44.567 1.00 34.12 ? 640  LYS A NZ  1 
ATOM   5181 N  N   . PRO A 1 641  ? 58.549 83.876  -42.109 1.00 22.86 ? 641  PRO A N   1 
ATOM   5182 C  CA  . PRO A 1 641  ? 59.352 82.672  -42.335 1.00 22.17 ? 641  PRO A CA  1 
ATOM   5183 C  C   . PRO A 1 641  ? 58.691 81.709  -43.315 1.00 21.16 ? 641  PRO A C   1 
ATOM   5184 O  O   . PRO A 1 641  ? 57.468 81.624  -43.360 1.00 20.51 ? 641  PRO A O   1 
ATOM   5185 C  CB  . PRO A 1 641  ? 59.365 82.010  -40.948 1.00 22.44 ? 641  PRO A CB  1 
ATOM   5186 C  CG  . PRO A 1 641  ? 59.032 83.087  -40.026 1.00 22.70 ? 641  PRO A CG  1 
ATOM   5187 C  CD  . PRO A 1 641  ? 58.046 83.940  -40.724 1.00 22.77 ? 641  PRO A CD  1 
ATOM   5188 N  N   . GLU A 1 642  ? 59.492 80.943  -44.040 1.00 21.57 ? 642  GLU A N   1 
ATOM   5189 C  CA  . GLU A 1 642  ? 58.971 79.980  -44.998 1.00 21.97 ? 642  GLU A CA  1 
ATOM   5190 C  C   . GLU A 1 642  ? 58.014 78.927  -44.416 1.00 21.49 ? 642  GLU A C   1 
ATOM   5191 O  O   . GLU A 1 642  ? 57.042 78.536  -45.057 1.00 21.79 ? 642  GLU A O   1 
ATOM   5192 C  CB  . GLU A 1 642  ? 60.140 79.278  -45.694 1.00 22.67 ? 642  GLU A CB  1 
ATOM   5193 C  CG  . GLU A 1 642  ? 59.726 78.245  -46.716 1.00 26.24 ? 642  GLU A CG  1 
ATOM   5194 C  CD  . GLU A 1 642  ? 60.907 77.684  -47.488 1.00 30.78 ? 642  GLU A CD  1 
ATOM   5195 O  OE1 . GLU A 1 642  ? 61.990 78.318  -47.474 1.00 34.81 ? 642  GLU A OE1 1 
ATOM   5196 O  OE2 . GLU A 1 642  ? 60.748 76.603  -48.107 1.00 35.09 ? 642  GLU A OE2 1 
ATOM   5197 N  N   . HIS A 1 643  ? 58.280 78.465  -43.201 1.00 20.14 ? 643  HIS A N   1 
ATOM   5198 C  CA  . HIS A 1 643  ? 57.518 77.339  -42.661 1.00 18.70 ? 643  HIS A CA  1 
ATOM   5199 C  C   . HIS A 1 643  ? 56.535 77.728  -41.557 1.00 17.64 ? 643  HIS A C   1 
ATOM   5200 O  O   . HIS A 1 643  ? 56.094 76.881  -40.796 1.00 16.55 ? 643  HIS A O   1 
ATOM   5201 C  CB  . HIS A 1 643  ? 58.448 76.246  -42.158 1.00 19.37 ? 643  HIS A CB  1 
ATOM   5202 C  CG  . HIS A 1 643  ? 59.350 75.696  -43.214 1.00 19.99 ? 643  HIS A CG  1 
ATOM   5203 N  ND1 . HIS A 1 643  ? 58.970 74.689  -44.065 1.00 23.07 ? 643  HIS A ND1 1 
ATOM   5204 C  CD2 . HIS A 1 643  ? 60.608 76.032  -43.566 1.00 23.37 ? 643  HIS A CD2 1 
ATOM   5205 C  CE1 . HIS A 1 643  ? 59.963 74.417  -44.891 1.00 22.16 ? 643  HIS A CE1 1 
ATOM   5206 N  NE2 . HIS A 1 643  ? 60.969 75.217  -44.606 1.00 23.04 ? 643  HIS A NE2 1 
ATOM   5207 N  N   . THR A 1 644  ? 56.200 79.006  -41.496 1.00 15.57 ? 644  THR A N   1 
ATOM   5208 C  CA  . THR A 1 644  ? 55.226 79.511  -40.537 1.00 15.07 ? 644  THR A CA  1 
ATOM   5209 C  C   . THR A 1 644  ? 54.074 80.135  -41.307 1.00 15.68 ? 644  THR A C   1 
ATOM   5210 O  O   . THR A 1 644  ? 54.323 80.948  -42.217 1.00 16.39 ? 644  THR A O   1 
ATOM   5211 C  CB  . THR A 1 644  ? 55.890 80.531  -39.609 1.00 14.84 ? 644  THR A CB  1 
ATOM   5212 O  OG1 . THR A 1 644  ? 56.929 79.860  -38.864 1.00 15.47 ? 644  THR A OG1 1 
ATOM   5213 C  CG2 . THR A 1 644  ? 54.893 81.093  -38.537 1.00 15.14 ? 644  THR A CG2 1 
ATOM   5214 N  N   . SER A 1 645  ? 52.845 79.743  -40.980 1.00 14.05 ? 645  SER A N   1 
ATOM   5215 C  CA  . SER A 1 645  ? 51.641 80.354  -41.543 1.00 14.06 ? 645  SER A CA  1 
ATOM   5216 C  C   . SER A 1 645  ? 50.921 81.173  -40.498 1.00 13.42 ? 645  SER A C   1 
ATOM   5217 O  O   . SER A 1 645  ? 51.255 81.086  -39.325 1.00 13.28 ? 645  SER A O   1 
ATOM   5218 C  CB  . SER A 1 645  ? 50.699 79.284  -42.058 1.00 14.09 ? 645  SER A CB  1 
ATOM   5219 O  OG  . SER A 1 645  ? 50.221 78.493  -40.958 1.00 15.86 ? 645  SER A OG  1 
ATOM   5220 N  N   . TYR A 1 646  ? 49.953 81.993  -40.914 1.00 13.00 ? 646  TYR A N   1 
ATOM   5221 C  CA  . TYR A 1 646  ? 49.272 82.936  -40.027 1.00 13.33 ? 646  TYR A CA  1 
ATOM   5222 C  C   . TYR A 1 646  ? 47.798 82.691  -40.131 1.00 13.56 ? 646  TYR A C   1 
ATOM   5223 O  O   . TYR A 1 646  ? 47.258 82.582  -41.237 1.00 15.41 ? 646  TYR A O   1 
ATOM   5224 C  CB  . TYR A 1 646  ? 49.601 84.387  -40.437 1.00 15.43 ? 646  TYR A CB  1 
ATOM   5225 C  CG  . TYR A 1 646  ? 51.076 84.612  -40.237 1.00 14.26 ? 646  TYR A CG  1 
ATOM   5226 C  CD1 . TYR A 1 646  ? 51.559 84.995  -38.987 1.00 13.31 ? 646  TYR A CD1 1 
ATOM   5227 C  CD2 . TYR A 1 646  ? 52.005 84.304  -41.246 1.00 14.75 ? 646  TYR A CD2 1 
ATOM   5228 C  CE1 . TYR A 1 646  ? 52.913 85.120  -38.756 1.00 14.17 ? 646  TYR A CE1 1 
ATOM   5229 C  CE2 . TYR A 1 646  ? 53.367 84.430  -41.014 1.00 16.72 ? 646  TYR A CE2 1 
ATOM   5230 C  CZ  . TYR A 1 646  ? 53.803 84.853  -39.770 1.00 15.77 ? 646  TYR A CZ  1 
ATOM   5231 O  OH  . TYR A 1 646  ? 55.145 84.977  -39.479 1.00 17.33 ? 646  TYR A OH  1 
ATOM   5232 N  N   . ALA A 1 647  ? 47.137 82.585  -38.978 1.00 12.30 ? 647  ALA A N   1 
ATOM   5233 C  CA  . ALA A 1 647  ? 45.709 82.368  -38.945 1.00 12.15 ? 647  ALA A CA  1 
ATOM   5234 C  C   . ALA A 1 647  ? 44.960 83.593  -39.458 1.00 12.38 ? 647  ALA A C   1 
ATOM   5235 O  O   . ALA A 1 647  ? 45.365 84.738  -39.261 1.00 12.51 ? 647  ALA A O   1 
ATOM   5236 C  CB  . ALA A 1 647  ? 45.265 82.078  -37.503 1.00 13.17 ? 647  ALA A CB  1 
ATOM   5237 N  N   . SER A 1 648  ? 43.816 83.349  -40.057 1.00 11.81 ? 648  SER A N   1 
ATOM   5238 C  CA  . SER A 1 648  ? 42.876 84.446  -40.280 1.00 12.84 ? 648  SER A CA  1 
ATOM   5239 C  C   . SER A 1 648  ? 41.979 84.607  -39.046 1.00 12.23 ? 648  SER A C   1 
ATOM   5240 O  O   . SER A 1 648  ? 41.788 83.651  -38.257 1.00 12.00 ? 648  SER A O   1 
ATOM   5241 C  CB  . SER A 1 648  ? 42.039 84.185  -41.520 1.00 14.26 ? 648  SER A CB  1 
ATOM   5242 O  OG  . SER A 1 648  ? 41.322 82.999  -41.401 1.00 18.63 ? 648  SER A OG  1 
ATOM   5243 N  N   . ASN A 1 649  ? 41.383 85.778  -38.880 1.00 11.29 ? 649  ASN A N   1 
ATOM   5244 C  CA  . ASN A 1 649  ? 40.515 86.058  -37.751 1.00 11.48 ? 649  ASN A CA  1 
ATOM   5245 C  C   . ASN A 1 649  ? 39.281 86.798  -38.223 1.00 11.16 ? 649  ASN A C   1 
ATOM   5246 O  O   . ASN A 1 649  ? 39.418 87.776  -39.004 1.00 12.33 ? 649  ASN A O   1 
ATOM   5247 C  CB  . ASN A 1 649  ? 41.242 86.868  -36.678 1.00 11.03 ? 649  ASN A CB  1 
ATOM   5248 C  CG  . ASN A 1 649  ? 42.440 86.133  -36.108 1.00 12.56 ? 649  ASN A CG  1 
ATOM   5249 O  OD1 . ASN A 1 649  ? 42.303 85.373  -35.125 1.00 12.64 ? 649  ASN A OD1 1 
ATOM   5250 N  ND2 . ASN A 1 649  ? 43.592 86.292  -36.730 1.00 12.45 ? 649  ASN A ND2 1 
ATOM   5251 N  N   . LEU A 1 650  ? 38.117 86.378  -37.763 1.00 10.98 ? 650  LEU A N   1 
ATOM   5252 C  CA  . LEU A 1 650  ? 36.841 86.961  -38.170 1.00 11.49 ? 650  LEU A CA  1 
ATOM   5253 C  C   . LEU A 1 650  ? 36.030 87.236  -36.935 1.00 12.31 ? 650  LEU A C   1 
ATOM   5254 O  O   . LEU A 1 650  ? 35.771 86.320  -36.151 1.00 12.61 ? 650  LEU A O   1 
ATOM   5255 C  CB  . LEU A 1 650  ? 36.098 85.996  -39.084 1.00 11.88 ? 650  LEU A CB  1 
ATOM   5256 C  CG  . LEU A 1 650  ? 34.648 86.324  -39.433 1.00 12.81 ? 650  LEU A CG  1 
ATOM   5257 C  CD1 . LEU A 1 650  ? 34.560 87.581  -40.308 1.00 14.12 ? 650  LEU A CD1 1 
ATOM   5258 C  CD2 . LEU A 1 650  ? 34.041 85.162  -40.201 1.00 16.03 ? 650  LEU A CD2 1 
ATOM   5259 N  N   . LEU A 1 651  ? 35.665 88.488  -36.703 1.00 12.65 ? 651  LEU A N   1 
ATOM   5260 C  CA  . LEU A 1 651  ? 34.877 88.894  -35.566 1.00 13.82 ? 651  LEU A CA  1 
ATOM   5261 C  C   . LEU A 1 651  ? 33.442 89.112  -36.022 1.00 14.18 ? 651  LEU A C   1 
ATOM   5262 O  O   . LEU A 1 651  ? 33.179 89.966  -36.890 1.00 15.24 ? 651  LEU A O   1 
ATOM   5263 C  CB  . LEU A 1 651  ? 35.470 90.176  -35.002 1.00 15.34 ? 651  LEU A CB  1 
ATOM   5264 C  CG  . LEU A 1 651  ? 35.228 90.567  -33.538 1.00 20.22 ? 651  LEU A CG  1 
ATOM   5265 C  CD1 . LEU A 1 651  ? 33.987 91.381  -33.351 1.00 25.96 ? 651  LEU A CD1 1 
ATOM   5266 C  CD2 . LEU A 1 651  ? 35.288 89.416  -32.545 1.00 19.97 ? 651  LEU A CD2 1 
ATOM   5267 N  N   . LEU A 1 652  ? 32.507 88.342  -35.487 1.00 14.71 ? 652  LEU A N   1 
ATOM   5268 C  CA  . LEU A 1 652  ? 31.108 88.415  -35.863 1.00 14.72 ? 652  LEU A CA  1 
ATOM   5269 C  C   . LEU A 1 652  ? 30.338 89.144  -34.785 1.00 15.89 ? 652  LEU A C   1 
ATOM   5270 O  O   . LEU A 1 652  ? 30.225 88.685  -33.636 1.00 15.60 ? 652  LEU A O   1 
ATOM   5271 C  CB  . LEU A 1 652  ? 30.545 87.026  -36.140 1.00 14.77 ? 652  LEU A CB  1 
ATOM   5272 C  CG  . LEU A 1 652  ? 31.281 86.296  -37.255 1.00 14.37 ? 652  LEU A CG  1 
ATOM   5273 C  CD1 . LEU A 1 652  ? 30.786 84.850  -37.353 1.00 16.81 ? 652  LEU A CD1 1 
ATOM   5274 C  CD2 . LEU A 1 652  ? 31.124 87.030  -38.623 1.00 15.63 ? 652  LEU A CD2 1 
ATOM   5275 N  N   . ARG A 1 653  ? 29.840 90.330  -35.141 1.00 17.43 ? 653  ARG A N   1 
ATOM   5276 C  CA  . ARG A 1 653  ? 29.064 91.174  -34.252 1.00 19.68 ? 653  ARG A CA  1 
ATOM   5277 C  C   . ARG A 1 653  ? 28.551 92.343  -35.095 1.00 20.01 ? 653  ARG A C   1 
ATOM   5278 O  O   . ARG A 1 653  ? 29.204 92.778  -36.032 1.00 20.55 ? 653  ARG A O   1 
ATOM   5279 C  CB  . ARG A 1 653  ? 29.887 91.702  -33.070 1.00 20.65 ? 653  ARG A CB  1 
ATOM   5280 C  CG  . ARG A 1 653  ? 31.043 92.588  -33.439 1.00 23.03 ? 653  ARG A CG  1 
ATOM   5281 C  CD  . ARG A 1 653  ? 31.131 93.873  -32.626 1.00 30.58 ? 653  ARG A CD  1 
ATOM   5282 N  NE  . ARG A 1 653  ? 31.271 93.717  -31.183 1.00 32.98 ? 653  ARG A NE  1 
ATOM   5283 C  CZ  . ARG A 1 653  ? 30.902 94.631  -30.284 1.00 35.03 ? 653  ARG A CZ  1 
ATOM   5284 N  NH1 . ARG A 1 653  ? 30.333 95.769  -30.665 1.00 38.06 ? 653  ARG A NH1 1 
ATOM   5285 N  NH2 . ARG A 1 653  ? 31.070 94.408  -28.989 1.00 37.37 ? 653  ARG A NH2 1 
ATOM   5286 N  N   . LYS A 1 654  ? 27.380 92.832  -34.747 1.00 22.33 ? 654  LYS A N   1 
ATOM   5287 C  CA  . LYS A 1 654  ? 26.926 94.087  -35.322 1.00 24.76 ? 654  LYS A CA  1 
ATOM   5288 C  C   . LYS A 1 654  ? 27.694 95.229  -34.639 1.00 25.49 ? 654  LYS A C   1 
ATOM   5289 O  O   . LYS A 1 654  ? 28.118 95.090  -33.501 1.00 26.61 ? 654  LYS A O   1 
ATOM   5290 C  CB  . LYS A 1 654  ? 25.418 94.209  -35.146 1.00 25.43 ? 654  LYS A CB  1 
ATOM   5291 C  CG  . LYS A 1 654  ? 24.641 93.246  -36.046 1.00 28.20 ? 654  LYS A CG  1 
ATOM   5292 C  CD  . LYS A 1 654  ? 23.496 93.939  -36.780 1.00 33.94 ? 654  LYS A CD  1 
ATOM   5293 C  CE  . LYS A 1 654  ? 24.025 94.893  -37.860 1.00 36.55 ? 654  LYS A CE  1 
ATOM   5294 N  NZ  . LYS A 1 654  ? 22.985 95.244  -38.875 1.00 38.80 ? 654  LYS A NZ  1 
ATOM   5295 N  N   . ASN A 1 655  ? 27.911 96.329  -35.336 1.00 26.76 ? 655  ASN A N   1 
ATOM   5296 C  CA  . ASN A 1 655  ? 28.558 97.476  -34.712 1.00 26.93 ? 655  ASN A CA  1 
ATOM   5297 C  C   . ASN A 1 655  ? 29.992 97.172  -34.282 1.00 25.38 ? 655  ASN A C   1 
ATOM   5298 O  O   . ASN A 1 655  ? 30.374 97.436  -33.154 1.00 26.49 ? 655  ASN A O   1 
ATOM   5299 C  CB  . ASN A 1 655  ? 27.747 97.929  -33.495 1.00 28.09 ? 655  ASN A CB  1 
ATOM   5300 C  CG  . ASN A 1 655  ? 28.182 99.280  -32.964 1.00 32.19 ? 655  ASN A CG  1 
ATOM   5301 O  OD1 . ASN A 1 655  ? 28.461 100.209 -33.729 1.00 35.93 ? 655  ASN A OD1 1 
ATOM   5302 N  ND2 . ASN A 1 655  ? 28.231 99.402  -31.645 1.00 35.96 ? 655  ASN A ND2 1 
ATOM   5303 N  N   . PRO A 1 656  ? 30.786 96.612  -35.182 1.00 23.08 ? 656  PRO A N   1 
ATOM   5304 C  CA  . PRO A 1 656  ? 32.164 96.279  -34.812 1.00 21.72 ? 656  PRO A CA  1 
ATOM   5305 C  C   . PRO A 1 656  ? 32.998 97.543  -34.751 1.00 20.68 ? 656  PRO A C   1 
ATOM   5306 O  O   . PRO A 1 656  ? 32.657 98.564  -35.371 1.00 19.57 ? 656  PRO A O   1 
ATOM   5307 C  CB  . PRO A 1 656  ? 32.633 95.401  -35.964 1.00 21.60 ? 656  PRO A CB  1 
ATOM   5308 C  CG  . PRO A 1 656  ? 31.852 95.889  -37.129 1.00 21.54 ? 656  PRO A CG  1 
ATOM   5309 C  CD  . PRO A 1 656  ? 30.491 96.251  -36.584 1.00 22.84 ? 656  PRO A CD  1 
ATOM   5310 N  N   . THR A 1 657  ? 34.074 97.471  -33.991 1.00 19.91 ? 657  THR A N   1 
ATOM   5311 C  CA  . THR A 1 657  ? 35.119 98.473  -34.058 1.00 19.93 ? 657  THR A CA  1 
ATOM   5312 C  C   . THR A 1 657  ? 36.406 97.736  -34.405 1.00 18.94 ? 657  THR A C   1 
ATOM   5313 O  O   . THR A 1 657  ? 36.488 96.494  -34.284 1.00 19.31 ? 657  THR A O   1 
ATOM   5314 C  CB  . THR A 1 657  ? 35.275 99.197  -32.715 1.00 20.44 ? 657  THR A CB  1 
ATOM   5315 O  OG1 . THR A 1 657  ? 35.254 98.233  -31.653 1.00 23.22 ? 657  THR A OG1 1 
ATOM   5316 C  CG2 . THR A 1 657  ? 34.065 100.084 -32.430 1.00 21.44 ? 657  THR A CG2 1 
ATOM   5317 N  N   . SER A 1 658  ? 37.419 98.491  -34.796 1.00 18.05 ? 658  SER A N   1 
ATOM   5318 C  CA  . SER A 1 658  ? 38.662 97.922  -35.292 1.00 18.44 ? 658  SER A CA  1 
ATOM   5319 C  C   . SER A 1 658  ? 39.402 97.093  -34.229 1.00 18.81 ? 658  SER A C   1 
ATOM   5320 O  O   . SER A 1 658  ? 39.168 97.251  -33.020 1.00 19.00 ? 658  SER A O   1 
ATOM   5321 C  CB  . SER A 1 658  ? 39.574 99.049  -35.714 1.00 18.89 ? 658  SER A CB  1 
ATOM   5322 O  OG  . SER A 1 658  ? 39.903 99.797  -34.552 1.00 20.25 ? 658  SER A OG  1 
ATOM   5323 N  N   . LEU A 1 659  ? 40.291 96.223  -34.700 1.00 18.52 ? 659  LEU A N   1 
ATOM   5324 C  CA  . LEU A 1 659  ? 41.076 95.357  -33.818 1.00 18.76 ? 659  LEU A CA  1 
ATOM   5325 C  C   . LEU A 1 659  ? 42.487 95.276  -34.368 1.00 19.38 ? 659  LEU A C   1 
ATOM   5326 O  O   . LEU A 1 659  ? 42.823 94.339  -35.091 1.00 18.46 ? 659  LEU A O   1 
ATOM   5327 C  CB  . LEU A 1 659  ? 40.451 93.952  -33.753 1.00 19.74 ? 659  LEU A CB  1 
ATOM   5328 C  CG  . LEU A 1 659  ? 39.118 93.778  -33.019 1.00 20.34 ? 659  LEU A CG  1 
ATOM   5329 C  CD1 . LEU A 1 659  ? 38.535 92.385  -33.297 1.00 21.62 ? 659  LEU A CD1 1 
ATOM   5330 C  CD2 . LEU A 1 659  ? 39.255 94.039  -31.526 1.00 22.82 ? 659  LEU A CD2 1 
ATOM   5331 N  N   . PRO A 1 660  ? 43.304 96.288  -34.071 1.00 19.93 ? 660  PRO A N   1 
ATOM   5332 C  CA  . PRO A 1 660  ? 44.687 96.298  -34.546 1.00 19.76 ? 660  PRO A CA  1 
ATOM   5333 C  C   . PRO A 1 660  ? 45.503 95.194  -33.862 1.00 19.39 ? 660  PRO A C   1 
ATOM   5334 O  O   . PRO A 1 660  ? 45.210 94.845  -32.723 1.00 19.35 ? 660  PRO A O   1 
ATOM   5335 C  CB  . PRO A 1 660  ? 45.199 97.683  -34.119 1.00 20.63 ? 660  PRO A CB  1 
ATOM   5336 C  CG  . PRO A 1 660  ? 44.318 98.128  -33.023 1.00 21.17 ? 660  PRO A CG  1 
ATOM   5337 C  CD  . PRO A 1 660  ? 42.978 97.482  -33.268 1.00 20.40 ? 660  PRO A CD  1 
ATOM   5338 N  N   . LEU A 1 661  ? 46.512 94.686  -34.547 1.00 20.06 ? 661  LEU A N   1 
ATOM   5339 C  CA  . LEU A 1 661  ? 47.254 93.536  -34.016 1.00 19.78 ? 661  LEU A CA  1 
ATOM   5340 C  C   . LEU A 1 661  ? 48.788 93.679  -34.071 1.00 21.13 ? 661  LEU A C   1 
ATOM   5341 O  O   . LEU A 1 661  ? 49.509 92.690  -34.260 1.00 19.86 ? 661  LEU A O   1 
ATOM   5342 C  CB  . LEU A 1 661  ? 46.802 92.264  -34.739 1.00 19.63 ? 661  LEU A CB  1 
ATOM   5343 C  CG  . LEU A 1 661  ? 45.381 91.775  -34.445 1.00 17.18 ? 661  LEU A CG  1 
ATOM   5344 C  CD1 . LEU A 1 661  ? 45.122 90.528  -35.300 1.00 17.03 ? 661  LEU A CD1 1 
ATOM   5345 C  CD2 . LEU A 1 661  ? 45.245 91.467  -32.962 1.00 17.73 ? 661  LEU A CD2 1 
ATOM   5346 N  N   . GLY A 1 662  ? 49.290 94.908  -33.935 1.00 22.64 ? 662  GLY A N   1 
ATOM   5347 C  CA  . GLY A 1 662  ? 50.724 95.160  -34.078 1.00 22.88 ? 662  GLY A CA  1 
ATOM   5348 C  C   . GLY A 1 662  ? 51.287 94.680  -35.404 1.00 23.31 ? 662  GLY A C   1 
ATOM   5349 O  O   . GLY A 1 662  ? 50.744 94.981  -36.467 1.00 23.98 ? 662  GLY A O   1 
ATOM   5350 N  N   . GLN A 1 663  ? 52.352 93.877  -35.344 1.00 23.40 ? 663  GLN A N   1 
ATOM   5351 C  CA  . GLN A 1 663  ? 53.001 93.380  -36.562 1.00 23.72 ? 663  GLN A CA  1 
ATOM   5352 C  C   . GLN A 1 663  ? 52.310 92.199  -37.232 1.00 22.32 ? 663  GLN A C   1 
ATOM   5353 O  O   . GLN A 1 663  ? 52.756 91.732  -38.278 1.00 23.58 ? 663  GLN A O   1 
ATOM   5354 C  CB  . GLN A 1 663  ? 54.441 92.937  -36.298 1.00 24.82 ? 663  GLN A CB  1 
ATOM   5355 C  CG  . GLN A 1 663  ? 55.305 93.854  -35.460 1.00 28.09 ? 663  GLN A CG  1 
ATOM   5356 C  CD  . GLN A 1 663  ? 56.555 93.119  -35.025 1.00 30.35 ? 663  GLN A CD  1 
ATOM   5357 O  OE1 . GLN A 1 663  ? 57.450 92.898  -35.846 1.00 30.76 ? 663  GLN A OE1 1 
ATOM   5358 N  NE2 . GLN A 1 663  ? 56.602 92.691  -33.754 1.00 31.81 ? 663  GLN A NE2 1 
ATOM   5359 N  N   . TYR A 1 664  ? 51.236 91.697  -36.628 1.00 22.09 ? 664  TYR A N   1 
ATOM   5360 C  CA  . TYR A 1 664  ? 50.575 90.509  -37.168 1.00 20.61 ? 664  TYR A CA  1 
ATOM   5361 C  C   . TYR A 1 664  ? 50.184 90.745  -38.634 1.00 20.86 ? 664  TYR A C   1 
ATOM   5362 O  O   . TYR A 1 664  ? 49.538 91.751  -38.933 1.00 22.05 ? 664  TYR A O   1 
ATOM   5363 C  CB  . TYR A 1 664  ? 49.369 90.191  -36.291 1.00 18.88 ? 664  TYR A CB  1 
ATOM   5364 C  CG  . TYR A 1 664  ? 48.765 88.849  -36.579 1.00 17.24 ? 664  TYR A CG  1 
ATOM   5365 C  CD1 . TYR A 1 664  ? 49.313 87.689  -36.018 1.00 14.59 ? 664  TYR A CD1 1 
ATOM   5366 C  CD2 . TYR A 1 664  ? 47.629 88.739  -37.379 1.00 15.02 ? 664  TYR A CD2 1 
ATOM   5367 C  CE1 . TYR A 1 664  ? 48.755 86.454  -36.285 1.00 14.53 ? 664  TYR A CE1 1 
ATOM   5368 C  CE2 . TYR A 1 664  ? 47.060 87.504  -37.649 1.00 17.08 ? 664  TYR A CE2 1 
ATOM   5369 C  CZ  . TYR A 1 664  ? 47.637 86.360  -37.091 1.00 14.42 ? 664  TYR A CZ  1 
ATOM   5370 O  OH  . TYR A 1 664  ? 47.066 85.135  -37.329 1.00 14.94 ? 664  TYR A OH  1 
ATOM   5371 N  N   . PRO A 1 665  ? 50.622 89.884  -39.549 1.00 21.44 ? 665  PRO A N   1 
ATOM   5372 C  CA  . PRO A 1 665  ? 50.499 90.165  -40.991 1.00 21.62 ? 665  PRO A CA  1 
ATOM   5373 C  C   . PRO A 1 665  ? 49.122 90.072  -41.671 1.00 22.03 ? 665  PRO A C   1 
ATOM   5374 O  O   . PRO A 1 665  ? 49.032 90.408  -42.855 1.00 23.60 ? 665  PRO A O   1 
ATOM   5375 C  CB  . PRO A 1 665  ? 51.468 89.161  -41.632 1.00 21.99 ? 665  PRO A CB  1 
ATOM   5376 C  CG  . PRO A 1 665  ? 51.552 88.051  -40.639 1.00 21.71 ? 665  PRO A CG  1 
ATOM   5377 C  CD  . PRO A 1 665  ? 51.398 88.658  -39.295 1.00 21.14 ? 665  PRO A CD  1 
ATOM   5378 N  N   A GLU A 1 666  ? 48.088 89.644  -40.954 0.50 21.26 ? 666  GLU A N   1 
ATOM   5379 N  N   B GLU A 1 666  ? 48.098 89.592  -40.965 0.50 21.26 ? 666  GLU A N   1 
ATOM   5380 C  CA  A GLU A 1 666  ? 46.770 89.425  -41.553 0.50 20.60 ? 666  GLU A CA  1 
ATOM   5381 C  CA  B GLU A 1 666  ? 46.757 89.444  -41.541 0.50 20.63 ? 666  GLU A CA  1 
ATOM   5382 C  C   A GLU A 1 666  ? 45.750 90.285  -40.812 0.50 19.75 ? 666  GLU A C   1 
ATOM   5383 C  C   B GLU A 1 666  ? 45.801 90.351  -40.796 0.50 19.81 ? 666  GLU A C   1 
ATOM   5384 O  O   A GLU A 1 666  ? 45.624 90.188  -39.592 0.50 18.72 ? 666  GLU A O   1 
ATOM   5385 O  O   B GLU A 1 666  ? 45.757 90.337  -39.563 0.50 18.82 ? 666  GLU A O   1 
ATOM   5386 C  CB  A GLU A 1 666  ? 46.438 87.933  -41.468 0.50 21.09 ? 666  GLU A CB  1 
ATOM   5387 C  CB  B GLU A 1 666  ? 46.281 87.995  -41.438 0.50 21.16 ? 666  GLU A CB  1 
ATOM   5388 C  CG  A GLU A 1 666  ? 44.980 87.560  -41.650 0.50 22.53 ? 666  GLU A CG  1 
ATOM   5389 C  CG  B GLU A 1 666  ? 47.131 86.998  -42.210 0.50 22.53 ? 666  GLU A CG  1 
ATOM   5390 C  CD  A GLU A 1 666  ? 44.596 87.229  -43.081 0.50 23.95 ? 666  GLU A CD  1 
ATOM   5391 C  CD  B GLU A 1 666  ? 46.958 87.132  -43.711 0.50 24.83 ? 666  GLU A CD  1 
ATOM   5392 O  OE1 A GLU A 1 666  ? 45.350 87.588  -44.019 0.50 26.29 ? 666  GLU A OE1 1 
ATOM   5393 O  OE1 B GLU A 1 666  ? 45.912 86.697  -44.230 0.50 27.02 ? 666  GLU A OE1 1 
ATOM   5394 O  OE2 A GLU A 1 666  ? 43.521 86.618  -43.267 0.50 22.05 ? 666  GLU A OE2 1 
ATOM   5395 O  OE2 B GLU A 1 666  ? 47.871 87.669  -44.370 0.50 27.49 ? 666  GLU A OE2 1 
ATOM   5396 N  N   . ASP A 1 667  ? 45.043 91.155  -41.539 1.00 18.73 ? 667  ASP A N   1 
ATOM   5397 C  CA  . ASP A 1 667  ? 44.071 92.060  -40.914 1.00 17.89 ? 667  ASP A CA  1 
ATOM   5398 C  C   . ASP A 1 667  ? 42.836 91.269  -40.436 1.00 14.71 ? 667  ASP A C   1 
ATOM   5399 O  O   . ASP A 1 667  ? 42.354 90.421  -41.164 1.00 14.91 ? 667  ASP A O   1 
ATOM   5400 C  CB  . ASP A 1 667  ? 43.570 93.111  -41.936 1.00 18.96 ? 667  ASP A CB  1 
ATOM   5401 C  CG  . ASP A 1 667  ? 44.650 94.103  -42.355 1.00 23.10 ? 667  ASP A CG  1 
ATOM   5402 O  OD1 . ASP A 1 667  ? 45.691 94.229  -41.658 1.00 28.21 ? 667  ASP A OD1 1 
ATOM   5403 O  OD2 . ASP A 1 667  ? 44.520 94.837  -43.367 1.00 27.36 ? 667  ASP A OD2 1 
ATOM   5404 N  N   . VAL A 1 668  ? 42.315 91.607  -39.271 1.00 14.40 ? 668  VAL A N   1 
ATOM   5405 C  CA  . VAL A 1 668  ? 41.045 91.032  -38.774 1.00 15.05 ? 668  VAL A CA  1 
ATOM   5406 C  C   . VAL A 1 668  ? 39.911 91.419  -39.709 1.00 14.56 ? 668  VAL A C   1 
ATOM   5407 O  O   . VAL A 1 668  ? 39.877 92.587  -40.171 1.00 15.62 ? 668  VAL A O   1 
ATOM   5408 C  CB  . VAL A 1 668  ? 40.691 91.497  -37.340 1.00 15.15 ? 668  VAL A CB  1 
ATOM   5409 C  CG1 . VAL A 1 668  ? 39.349 90.973  -36.891 1.00 15.37 ? 668  VAL A CG1 1 
ATOM   5410 C  CG2 . VAL A 1 668  ? 41.767 91.079  -36.357 1.00 15.57 ? 668  VAL A CG2 1 
ATOM   5411 N  N   . LYS A 1 669  ? 39.034 90.466  -40.001 1.00 13.11 ? 669  LYS A N   1 
ATOM   5412 C  CA  . LYS A 1 669  ? 37.806 90.643  -40.801 1.00 14.38 ? 669  LYS A CA  1 
ATOM   5413 C  C   . LYS A 1 669  ? 36.593 90.728  -39.876 1.00 13.61 ? 669  LYS A C   1 
ATOM   5414 O  O   . LYS A 1 669  ? 36.600 90.168  -38.756 1.00 13.23 ? 669  LYS A O   1 
ATOM   5415 C  CB  . LYS A 1 669  ? 37.640 89.462  -41.753 1.00 16.49 ? 669  LYS A CB  1 
ATOM   5416 C  CG  . LYS A 1 669  ? 38.388 89.580  -43.075 1.00 22.90 ? 669  LYS A CG  1 
ATOM   5417 C  CD  . LYS A 1 669  ? 39.889 89.360  -42.959 1.00 28.24 ? 669  LYS A CD  1 
ATOM   5418 C  CE  . LYS A 1 669  ? 40.621 89.946  -44.187 1.00 29.89 ? 669  LYS A CE  1 
ATOM   5419 N  NZ  . LYS A 1 669  ? 42.075 90.159  -43.933 1.00 30.53 ? 669  LYS A NZ  1 
ATOM   5420 N  N   . PHE A 1 670  ? 35.538 91.402  -40.337 1.00 13.42 ? 670  PHE A N   1 
ATOM   5421 C  CA  . PHE A 1 670  ? 34.334 91.641  -39.547 1.00 13.78 ? 670  PHE A CA  1 
ATOM   5422 C  C   . PHE A 1 670  ? 33.100 91.180  -40.314 1.00 14.65 ? 670  PHE A C   1 
ATOM   5423 O  O   . PHE A 1 670  ? 33.101 91.184  -41.537 1.00 15.41 ? 670  PHE A O   1 
ATOM   5424 C  CB  . PHE A 1 670  ? 34.226 93.135  -39.135 1.00 14.76 ? 670  PHE A CB  1 
ATOM   5425 C  CG  . PHE A 1 670  ? 35.386 93.591  -38.323 1.00 14.62 ? 670  PHE A CG  1 
ATOM   5426 C  CD1 . PHE A 1 670  ? 36.528 94.068  -38.962 1.00 16.40 ? 670  PHE A CD1 1 
ATOM   5427 C  CD2 . PHE A 1 670  ? 35.384 93.466  -36.937 1.00 17.15 ? 670  PHE A CD2 1 
ATOM   5428 C  CE1 . PHE A 1 670  ? 37.636 94.458  -38.230 1.00 16.87 ? 670  PHE A CE1 1 
ATOM   5429 C  CE2 . PHE A 1 670  ? 36.492 93.853  -36.201 1.00 18.27 ? 670  PHE A CE2 1 
ATOM   5430 C  CZ  . PHE A 1 670  ? 37.620 94.361  -36.865 1.00 17.79 ? 670  PHE A CZ  1 
ATOM   5431 N  N   . GLY A 1 671  ? 32.048 90.780  -39.606 1.00 15.21 ? 671  GLY A N   1 
ATOM   5432 C  CA  . GLY A 1 671  ? 30.789 90.444  -40.242 1.00 15.19 ? 671  GLY A CA  1 
ATOM   5433 C  C   . GLY A 1 671  ? 29.668 90.444  -39.243 1.00 15.77 ? 671  GLY A C   1 
ATOM   5434 O  O   . GLY A 1 671  ? 29.886 90.451  -38.029 1.00 14.68 ? 671  GLY A O   1 
ATOM   5435 N  N   . ASP A 1 672  ? 28.439 90.445  -39.757 1.00 15.77 ? 672  ASP A N   1 
ATOM   5436 C  CA  . ASP A 1 672  ? 27.280 90.267  -38.885 1.00 17.54 ? 672  ASP A CA  1 
ATOM   5437 C  C   . ASP A 1 672  ? 27.270 88.800  -38.418 1.00 16.85 ? 672  ASP A C   1 
ATOM   5438 O  O   . ASP A 1 672  ? 27.749 87.931  -39.149 1.00 16.28 ? 672  ASP A O   1 
ATOM   5439 C  CB  . ASP A 1 672  ? 25.961 90.508  -39.629 1.00 18.43 ? 672  ASP A CB  1 
ATOM   5440 C  CG  . ASP A 1 672  ? 25.670 91.972  -39.869 1.00 22.94 ? 672  ASP A CG  1 
ATOM   5441 O  OD1 . ASP A 1 672  ? 26.281 92.848  -39.219 1.00 24.77 ? 672  ASP A OD1 1 
ATOM   5442 O  OD2 . ASP A 1 672  ? 24.791 92.320  -40.694 1.00 28.52 ? 672  ASP A OD2 1 
ATOM   5443 N  N   . PRO A 1 673  ? 26.702 88.528  -37.232 1.00 17.63 ? 673  PRO A N   1 
ATOM   5444 C  CA  . PRO A 1 673  ? 26.551 87.129  -36.785 1.00 18.36 ? 673  PRO A CA  1 
ATOM   5445 C  C   . PRO A 1 673  ? 25.940 86.257  -37.877 1.00 18.29 ? 673  PRO A C   1 
ATOM   5446 O  O   . PRO A 1 673  ? 25.011 86.688  -38.585 1.00 19.11 ? 673  PRO A O   1 
ATOM   5447 C  CB  . PRO A 1 673  ? 25.632 87.243  -35.578 1.00 18.90 ? 673  PRO A CB  1 
ATOM   5448 C  CG  . PRO A 1 673  ? 25.936 88.600  -35.005 1.00 19.87 ? 673  PRO A CG  1 
ATOM   5449 C  CD  . PRO A 1 673  ? 26.218 89.480  -36.211 1.00 18.46 ? 673  PRO A CD  1 
ATOM   5450 N  N   . ARG A 1 674  ? 26.464 85.050  -38.019 1.00 17.53 ? 674  ARG A N   1 
ATOM   5451 C  CA  . ARG A 1 674  ? 26.011 84.113  -39.046 1.00 18.18 ? 674  ARG A CA  1 
ATOM   5452 C  C   . ARG A 1 674  ? 26.475 82.710  -38.682 1.00 18.25 ? 674  ARG A C   1 
ATOM   5453 O  O   . ARG A 1 674  ? 27.451 82.553  -37.955 1.00 17.91 ? 674  ARG A O   1 
ATOM   5454 C  CB  . ARG A 1 674  ? 26.554 84.502  -40.429 1.00 18.04 ? 674  ARG A CB  1 
ATOM   5455 C  CG  . ARG A 1 674  ? 28.071 84.421  -40.627 1.00 19.04 ? 674  ARG A CG  1 
ATOM   5456 C  CD  . ARG A 1 674  ? 28.443 84.585  -42.094 1.00 20.20 ? 674  ARG A CD  1 
ATOM   5457 N  NE  . ARG A 1 674  ? 29.818 84.239  -42.433 1.00 23.65 ? 674  ARG A NE  1 
ATOM   5458 C  CZ  . ARG A 1 674  ? 30.805 85.111  -42.571 1.00 24.62 ? 674  ARG A CZ  1 
ATOM   5459 N  NH1 . ARG A 1 674  ? 30.592 86.414  -42.383 1.00 26.12 ? 674  ARG A NH1 1 
ATOM   5460 N  NH2 . ARG A 1 674  ? 32.016 84.678  -42.900 1.00 25.43 ? 674  ARG A NH2 1 
ATOM   5461 N  N   . GLU A 1 675  ? 25.789 81.693  -39.183 1.00 18.08 ? 675  GLU A N   1 
ATOM   5462 C  CA  . GLU A 1 675  ? 26.295 80.340  -39.043 1.00 18.48 ? 675  GLU A CA  1 
ATOM   5463 C  C   . GLU A 1 675  ? 27.617 80.147  -39.775 1.00 19.17 ? 675  GLU A C   1 
ATOM   5464 O  O   . GLU A 1 675  ? 27.866 80.737  -40.843 1.00 20.38 ? 675  GLU A O   1 
ATOM   5465 C  CB  . GLU A 1 675  ? 25.234 79.352  -39.513 1.00 19.82 ? 675  GLU A CB  1 
ATOM   5466 C  CG  . GLU A 1 675  ? 23.979 79.532  -38.703 1.00 22.64 ? 675  GLU A CG  1 
ATOM   5467 C  CD  . GLU A 1 675  ? 23.096 78.310  -38.726 1.00 28.92 ? 675  GLU A CD  1 
ATOM   5468 O  OE1 . GLU A 1 675  ? 23.244 77.513  -39.683 1.00 31.75 ? 675  GLU A OE1 1 
ATOM   5469 O  OE2 . GLU A 1 675  ? 22.276 78.145  -37.778 1.00 31.53 ? 675  GLU A OE2 1 
ATOM   5470 N  N   . ILE A 1 676  ? 28.507 79.346  -39.200 1.00 18.64 ? 676  ILE A N   1 
ATOM   5471 C  CA  . ILE A 1 676  ? 29.760 79.067  -39.874 1.00 19.35 ? 676  ILE A CA  1 
ATOM   5472 C  C   . ILE A 1 676  ? 30.130 77.592  -39.734 1.00 17.98 ? 676  ILE A C   1 
ATOM   5473 O  O   . ILE A 1 676  ? 29.624 76.908  -38.831 1.00 17.79 ? 676  ILE A O   1 
ATOM   5474 C  CB  . ILE A 1 676  ? 30.904 79.936  -39.350 1.00 20.91 ? 676  ILE A CB  1 
ATOM   5475 C  CG1 . ILE A 1 676  ? 31.106 79.718  -37.871 1.00 20.50 ? 676  ILE A CG1 1 
ATOM   5476 C  CG2 . ILE A 1 676  ? 30.751 81.449  -39.710 1.00 23.81 ? 676  ILE A CG2 1 
ATOM   5477 C  CD1 . ILE A 1 676  ? 32.565 79.526  -37.558 1.00 25.77 ? 676  ILE A CD1 1 
ATOM   5478 N  N   . SER A 1 677  ? 31.005 77.138  -40.619 1.00 17.12 ? 677  SER A N   1 
ATOM   5479 C  CA  A SER A 1 677  ? 31.522 75.766  -40.656 0.50 17.51 ? 677  SER A CA  1 
ATOM   5480 C  CA  B SER A 1 677  ? 31.548 75.780  -40.535 0.50 17.43 ? 677  SER A CA  1 
ATOM   5481 C  C   . SER A 1 677  ? 33.056 75.800  -40.669 1.00 17.64 ? 677  SER A C   1 
ATOM   5482 O  O   . SER A 1 677  ? 33.643 76.658  -41.342 1.00 18.12 ? 677  SER A O   1 
ATOM   5483 C  CB  A SER A 1 677  ? 30.989 75.072  -41.931 0.50 17.88 ? 677  SER A CB  1 
ATOM   5484 C  CB  B SER A 1 677  ? 30.919 74.847  -41.583 0.50 17.74 ? 677  SER A CB  1 
ATOM   5485 O  OG  A SER A 1 677  ? 31.647 73.856  -42.203 0.50 19.37 ? 677  SER A OG  1 
ATOM   5486 O  OG  B SER A 1 677  ? 29.530 74.752  -41.376 0.50 19.72 ? 677  SER A OG  1 
ATOM   5487 N  N   . LEU A 1 678  ? 33.708 74.861  -39.985 1.00 16.26 ? 678  LEU A N   1 
ATOM   5488 C  CA  . LEU A 1 678  ? 35.156 74.783  -39.972 1.00 16.19 ? 678  LEU A CA  1 
ATOM   5489 C  C   . LEU A 1 678  ? 35.600 73.343  -40.099 1.00 16.04 ? 678  LEU A C   1 
ATOM   5490 O  O   . LEU A 1 678  ? 34.898 72.446  -39.612 1.00 15.90 ? 678  LEU A O   1 
ATOM   5491 C  CB  . LEU A 1 678  ? 35.713 75.328  -38.658 1.00 16.65 ? 678  LEU A CB  1 
ATOM   5492 C  CG  . LEU A 1 678  ? 35.827 76.828  -38.477 1.00 17.40 ? 678  LEU A CG  1 
ATOM   5493 C  CD1 . LEU A 1 678  ? 36.168 77.065  -37.022 1.00 20.69 ? 678  LEU A CD1 1 
ATOM   5494 C  CD2 . LEU A 1 678  ? 36.942 77.382  -39.332 1.00 20.17 ? 678  LEU A CD2 1 
ATOM   5495 N  N   . ARG A 1 679  ? 36.734 73.140  -40.736 1.00 15.78 ? 679  ARG A N   1 
ATOM   5496 C  CA  . ARG A 1 679  ? 37.375 71.829  -40.808 1.00 18.07 ? 679  ARG A CA  1 
ATOM   5497 C  C   . ARG A 1 679  ? 38.882 72.046  -40.775 1.00 18.11 ? 679  ARG A C   1 
ATOM   5498 O  O   . ARG A 1 679  ? 39.421 72.844  -41.560 1.00 18.99 ? 679  ARG A O   1 
ATOM   5499 C  CB  . ARG A 1 679  ? 36.973 71.109  -42.099 1.00 19.20 ? 679  ARG A CB  1 
ATOM   5500 C  CG  . ARG A 1 679  ? 37.467 69.685  -42.164 1.00 21.41 ? 679  ARG A CG  1 
ATOM   5501 C  CD  . ARG A 1 679  ? 37.251 69.047  -43.525 1.00 25.68 ? 679  ARG A CD  1 
ATOM   5502 N  NE  . ARG A 1 679  ? 37.649 67.647  -43.488 1.00 30.94 ? 679  ARG A NE  1 
ATOM   5503 C  CZ  . ARG A 1 679  ? 37.781 66.865  -44.553 1.00 33.73 ? 679  ARG A CZ  1 
ATOM   5504 N  NH1 . ARG A 1 679  ? 37.553 67.334  -45.775 1.00 35.66 ? 679  ARG A NH1 1 
ATOM   5505 N  NH2 . ARG A 1 679  ? 38.146 65.604  -44.387 1.00 36.55 ? 679  ARG A NH2 1 
ATOM   5506 N  N   . VAL A 1 680  ? 39.560 71.374  -39.852 1.00 17.23 ? 680  VAL A N   1 
ATOM   5507 C  CA  . VAL A 1 680  ? 40.999 71.353  -39.812 1.00 17.76 ? 680  VAL A CA  1 
ATOM   5508 C  C   . VAL A 1 680  ? 41.530 70.001  -40.282 1.00 19.55 ? 680  VAL A C   1 
ATOM   5509 O  O   . VAL A 1 680  ? 40.999 68.950  -39.887 1.00 19.22 ? 680  VAL A O   1 
ATOM   5510 C  CB  . VAL A 1 680  ? 41.520 71.642  -38.382 1.00 17.09 ? 680  VAL A CB  1 
ATOM   5511 C  CG1 . VAL A 1 680  ? 43.013 71.404  -38.304 1.00 17.11 ? 680  VAL A CG1 1 
ATOM   5512 C  CG2 . VAL A 1 680  ? 41.142 73.085  -37.948 1.00 15.80 ? 680  VAL A CG2 1 
ATOM   5513 N  N   . GLY A 1 681  ? 42.554 70.046  -41.136 1.00 20.78 ? 681  GLY A N   1 
ATOM   5514 C  CA  . GLY A 1 681  ? 43.125 68.839  -41.731 1.00 23.61 ? 681  GLY A CA  1 
ATOM   5515 C  C   . GLY A 1 681  ? 42.063 67.979  -42.406 1.00 24.78 ? 681  GLY A C   1 
ATOM   5516 O  O   . GLY A 1 681  ? 41.137 68.498  -43.046 1.00 25.77 ? 681  GLY A O   1 
ATOM   5517 N  N   . ASN A 1 682  ? 42.189 66.661  -42.254 1.00 27.23 ? 682  ASN A N   1 
ATOM   5518 C  CA  . ASN A 1 682  ? 41.176 65.738  -42.784 1.00 28.36 ? 682  ASN A CA  1 
ATOM   5519 C  C   . ASN A 1 682  ? 40.199 65.311  -41.687 1.00 28.08 ? 682  ASN A C   1 
ATOM   5520 O  O   . ASN A 1 682  ? 39.514 64.291  -41.788 1.00 29.18 ? 682  ASN A O   1 
ATOM   5521 C  CB  . ASN A 1 682  ? 41.815 64.533  -43.495 1.00 29.67 ? 682  ASN A CB  1 
ATOM   5522 C  CG  . ASN A 1 682  ? 42.834 63.802  -42.629 1.00 32.72 ? 682  ASN A CG  1 
ATOM   5523 O  OD1 . ASN A 1 682  ? 42.679 63.686  -41.403 1.00 37.46 ? 682  ASN A OD1 1 
ATOM   5524 N  ND2 . ASN A 1 682  ? 43.882 63.291  -43.268 1.00 35.90 ? 682  ASN A ND2 1 
ATOM   5525 N  N   . GLY A 1 683  ? 40.111 66.137  -40.651 1.00 26.72 ? 683  GLY A N   1 
ATOM   5526 C  CA  . GLY A 1 683  ? 39.305 65.834  -39.494 1.00 24.35 ? 683  GLY A CA  1 
ATOM   5527 C  C   . GLY A 1 683  ? 37.838 66.146  -39.697 1.00 22.45 ? 683  GLY A C   1 
ATOM   5528 O  O   . GLY A 1 683  ? 37.391 66.352  -40.827 1.00 22.77 ? 683  GLY A O   1 
ATOM   5529 N  N   . PRO A 1 684  ? 37.076 66.205  -38.607 1.00 20.31 ? 684  PRO A N   1 
ATOM   5530 C  CA  . PRO A 1 684  ? 35.636 66.446  -38.735 1.00 19.45 ? 684  PRO A CA  1 
ATOM   5531 C  C   . PRO A 1 684  ? 35.323 67.892  -39.156 1.00 18.15 ? 684  PRO A C   1 
ATOM   5532 O  O   . PRO A 1 684  ? 36.158 68.774  -38.974 1.00 17.63 ? 684  PRO A O   1 
ATOM   5533 C  CB  . PRO A 1 684  ? 35.093 66.170  -37.325 1.00 19.20 ? 684  PRO A CB  1 
ATOM   5534 C  CG  . PRO A 1 684  ? 36.286 66.385  -36.399 1.00 20.05 ? 684  PRO A CG  1 
ATOM   5535 C  CD  . PRO A 1 684  ? 37.504 66.072  -37.203 1.00 20.94 ? 684  PRO A CD  1 
ATOM   5536 N  N   . THR A 1 685  ? 34.145 68.094  -39.718 1.00 17.30 ? 685  THR A N   1 
ATOM   5537 C  CA  . THR A 1 685  ? 33.651 69.418  -40.069 1.00 16.53 ? 685  THR A CA  1 
ATOM   5538 C  C   . THR A 1 685  ? 32.620 69.771  -39.023 1.00 16.43 ? 685  THR A C   1 
ATOM   5539 O  O   . THR A 1 685  ? 31.677 69.018  -38.797 1.00 16.47 ? 685  THR A O   1 
ATOM   5540 C  CB  . THR A 1 685  ? 33.032 69.411  -41.495 1.00 17.65 ? 685  THR A CB  1 
ATOM   5541 O  OG1 . THR A 1 685  ? 34.060 69.113  -42.433 1.00 18.94 ? 685  THR A OG1 1 
ATOM   5542 C  CG2 . THR A 1 685  ? 32.548 70.802  -41.888 1.00 18.88 ? 685  THR A CG2 1 
ATOM   5543 N  N   . LEU A 1 686  ? 32.801 70.919  -38.362 1.00 13.84 ? 686  LEU A N   1 
ATOM   5544 C  CA  . LEU A 1 686  ? 31.906 71.350  -37.308 1.00 14.20 ? 686  LEU A CA  1 
ATOM   5545 C  C   . LEU A 1 686  ? 31.111 72.556  -37.787 1.00 13.31 ? 686  LEU A C   1 
ATOM   5546 O  O   . LEU A 1 686  ? 31.701 73.503  -38.337 1.00 13.63 ? 686  LEU A O   1 
ATOM   5547 C  CB  . LEU A 1 686  ? 32.687 71.746  -36.036 1.00 13.20 ? 686  LEU A CB  1 
ATOM   5548 C  CG  . LEU A 1 686  ? 33.681 70.784  -35.366 1.00 19.37 ? 686  LEU A CG  1 
ATOM   5549 C  CD1 . LEU A 1 686  ? 33.819 71.133  -33.888 1.00 18.82 ? 686  LEU A CD1 1 
ATOM   5550 C  CD2 . LEU A 1 686  ? 33.446 69.320  -35.551 1.00 17.86 ? 686  LEU A CD2 1 
ATOM   5551 N  N   . ALA A 1 687  ? 29.822 72.548  -37.542 1.00 13.04 ? 687  ALA A N   1 
ATOM   5552 C  CA  . ALA A 1 687  ? 28.983 73.701  -37.847 1.00 13.13 ? 687  ALA A CA  1 
ATOM   5553 C  C   . ALA A 1 687  ? 28.531 74.369  -36.563 1.00 13.90 ? 687  ALA A C   1 
ATOM   5554 O  O   . ALA A 1 687  ? 28.207 73.677  -35.570 1.00 13.99 ? 687  ALA A O   1 
ATOM   5555 C  CB  . ALA A 1 687  ? 27.754 73.258  -38.672 1.00 14.09 ? 687  ALA A CB  1 
ATOM   5556 N  N   . PHE A 1 688  ? 28.464 75.705  -36.567 1.00 13.40 ? 688  PHE A N   1 
ATOM   5557 C  CA  . PHE A 1 688  ? 28.135 76.510  -35.405 1.00 12.84 ? 688  PHE A CA  1 
ATOM   5558 C  C   . PHE A 1 688  ? 26.964 77.417  -35.680 1.00 13.70 ? 688  PHE A C   1 
ATOM   5559 O  O   . PHE A 1 688  ? 26.823 77.937  -36.825 1.00 14.50 ? 688  PHE A O   1 
ATOM   5560 C  CB  . PHE A 1 688  ? 29.333 77.380  -35.000 1.00 13.11 ? 688  PHE A CB  1 
ATOM   5561 C  CG  . PHE A 1 688  ? 30.553 76.571  -34.659 1.00 10.82 ? 688  PHE A CG  1 
ATOM   5562 C  CD1 . PHE A 1 688  ? 31.406 76.108  -35.632 1.00 12.30 ? 688  PHE A CD1 1 
ATOM   5563 C  CD2 . PHE A 1 688  ? 30.837 76.295  -33.319 1.00 12.03 ? 688  PHE A CD2 1 
ATOM   5564 C  CE1 . PHE A 1 688  ? 32.522 75.350  -35.313 1.00 11.50 ? 688  PHE A CE1 1 
ATOM   5565 C  CE2 . PHE A 1 688  ? 31.948 75.557  -32.995 1.00 12.07 ? 688  PHE A CE2 1 
ATOM   5566 C  CZ  . PHE A 1 688  ? 32.787 75.080  -33.965 1.00 10.99 ? 688  PHE A CZ  1 
ATOM   5567 N  N   . SER A 1 689  ? 26.143 77.632  -34.676 1.00 14.21 ? 689  SER A N   1 
ATOM   5568 C  CA  . SER A 1 689  ? 25.042 78.608  -34.738 1.00 14.57 ? 689  SER A CA  1 
ATOM   5569 C  C   . SER A 1 689  ? 25.592 80.039  -34.828 1.00 14.87 ? 689  SER A C   1 
ATOM   5570 O  O   . SER A 1 689  ? 26.774 80.305  -34.582 1.00 13.94 ? 689  SER A O   1 
ATOM   5571 C  CB  . SER A 1 689  ? 24.169 78.520  -33.491 1.00 15.45 ? 689  SER A CB  1 
ATOM   5572 O  OG  . SER A 1 689  ? 24.831 79.075  -32.375 1.00 14.94 ? 689  SER A OG  1 
ATOM   5573 N  N   . GLU A 1 690  ? 24.713 80.988  -35.127 1.00 15.49 ? 690  GLU A N   1 
ATOM   5574 C  CA  . GLU A 1 690  ? 25.105 82.393  -35.106 1.00 15.89 ? 690  GLU A CA  1 
ATOM   5575 C  C   . GLU A 1 690  ? 25.476 82.900  -33.696 1.00 15.55 ? 690  GLU A C   1 
ATOM   5576 O  O   . GLU A 1 690  ? 26.079 83.974  -33.549 1.00 15.53 ? 690  GLU A O   1 
ATOM   5577 C  CB  . GLU A 1 690  ? 23.977 83.215  -35.753 1.00 17.57 ? 690  GLU A CB  1 
ATOM   5578 C  CG  . GLU A 1 690  ? 22.861 83.644  -34.846 1.00 21.55 ? 690  GLU A CG  1 
ATOM   5579 C  CD  . GLU A 1 690  ? 22.000 84.698  -35.528 1.00 26.84 ? 690  GLU A CD  1 
ATOM   5580 O  OE1 . GLU A 1 690  ? 21.404 84.374  -36.588 1.00 30.55 ? 690  GLU A OE1 1 
ATOM   5581 O  OE2 . GLU A 1 690  ? 21.948 85.850  -35.029 1.00 30.77 ? 690  GLU A OE2 1 
ATOM   5582 N  N   . GLN A 1 691  ? 25.144 82.119  -32.657 1.00 15.55 ? 691  GLN A N   1 
ATOM   5583 C  CA  . GLN A 1 691  ? 25.614 82.436  -31.305 1.00 15.21 ? 691  GLN A CA  1 
ATOM   5584 C  C   . GLN A 1 691  ? 26.944 81.761  -30.946 1.00 13.60 ? 691  GLN A C   1 
ATOM   5585 O  O   . GLN A 1 691  ? 27.375 81.861  -29.791 1.00 15.45 ? 691  GLN A O   1 
ATOM   5586 C  CB  . GLN A 1 691  ? 24.588 82.113  -30.218 1.00 16.65 ? 691  GLN A CB  1 
ATOM   5587 C  CG  . GLN A 1 691  ? 23.280 82.864  -30.331 1.00 20.34 ? 691  GLN A CG  1 
ATOM   5588 C  CD  . GLN A 1 691  ? 22.190 81.893  -30.565 1.00 28.87 ? 691  GLN A CD  1 
ATOM   5589 O  OE1 . GLN A 1 691  ? 21.550 81.442  -29.606 1.00 30.87 ? 691  GLN A OE1 1 
ATOM   5590 N  NE2 . GLN A 1 691  ? 22.010 81.495  -31.820 1.00 29.04 ? 691  GLN A NE2 1 
ATOM   5591 N  N   . GLY A 1 692  ? 27.589 81.123  -31.906 1.00 12.55 ? 692  GLY A N   1 
ATOM   5592 C  CA  . GLY A 1 692  ? 28.933 80.565  -31.709 1.00 12.82 ? 692  GLY A CA  1 
ATOM   5593 C  C   . GLY A 1 692  ? 28.956 79.220  -31.009 1.00 12.82 ? 692  GLY A C   1 
ATOM   5594 O  O   . GLY A 1 692  ? 30.021 78.813  -30.518 1.00 13.41 ? 692  GLY A O   1 
ATOM   5595 N  N   . LEU A 1 693  ? 27.823 78.514  -31.002 1.00 12.32 ? 693  LEU A N   1 
ATOM   5596 C  CA  . LEU A 1 693  ? 27.703 77.216  -30.316 1.00 12.96 ? 693  LEU A CA  1 
ATOM   5597 C  C   . LEU A 1 693  ? 27.559 76.111  -31.331 1.00 13.06 ? 693  LEU A C   1 
ATOM   5598 O  O   . LEU A 1 693  ? 26.832 76.252  -32.332 1.00 12.95 ? 693  LEU A O   1 
ATOM   5599 C  CB  . LEU A 1 693  ? 26.511 77.247  -29.356 1.00 14.03 ? 693  LEU A CB  1 
ATOM   5600 C  CG  . LEU A 1 693  ? 26.719 78.191  -28.166 1.00 16.76 ? 693  LEU A CG  1 
ATOM   5601 C  CD1 . LEU A 1 693  ? 25.443 78.942  -27.831 1.00 22.59 ? 693  LEU A CD1 1 
ATOM   5602 C  CD2 . LEU A 1 693  ? 27.213 77.450  -26.940 1.00 18.61 ? 693  LEU A CD2 1 
ATOM   5603 N  N   . LEU A 1 694  ? 28.253 75.001  -31.099 1.00 11.91 ? 694  LEU A N   1 
ATOM   5604 C  CA  . LEU A 1 694  ? 28.176 73.851  -31.963 1.00 11.94 ? 694  LEU A CA  1 
ATOM   5605 C  C   . LEU A 1 694  ? 26.730 73.448  -32.232 1.00 11.64 ? 694  LEU A C   1 
ATOM   5606 O  O   . LEU A 1 694  ? 25.895 73.463  -31.337 1.00 11.84 ? 694  LEU A O   1 
ATOM   5607 C  CB  . LEU A 1 694  ? 28.924 72.667  -31.306 1.00 12.18 ? 694  LEU A CB  1 
ATOM   5608 C  CG  . LEU A 1 694  ? 29.081 71.396  -32.131 1.00 12.15 ? 694  LEU A CG  1 
ATOM   5609 C  CD1 . LEU A 1 694  ? 29.985 71.621  -33.300 1.00 13.09 ? 694  LEU A CD1 1 
ATOM   5610 C  CD2 . LEU A 1 694  ? 29.628 70.276  -31.240 1.00 12.87 ? 694  LEU A CD2 1 
ATOM   5611 N  N   . LYS A 1 695  ? 26.447 73.159  -33.502 1.00 12.80 ? 695  LYS A N   1 
ATOM   5612 C  CA  . LYS A 1 695  ? 25.156 72.595  -33.863 1.00 15.33 ? 695  LYS A CA  1 
ATOM   5613 C  C   . LYS A 1 695  ? 25.255 71.243  -34.552 1.00 14.07 ? 695  LYS A C   1 
ATOM   5614 O  O   . LYS A 1 695  ? 24.275 70.478  -34.493 1.00 15.31 ? 695  LYS A O   1 
ATOM   5615 C  CB  . LYS A 1 695  ? 24.291 73.591  -34.673 1.00 16.39 ? 695  LYS A CB  1 
ATOM   5616 C  CG  . LYS A 1 695  ? 24.908 74.090  -35.941 1.00 19.43 ? 695  LYS A CG  1 
ATOM   5617 C  CD  . LYS A 1 695  ? 23.964 75.105  -36.635 1.00 19.87 ? 695  LYS A CD  1 
ATOM   5618 C  CE  . LYS A 1 695  ? 22.786 74.392  -37.284 1.00 27.24 ? 695  LYS A CE  1 
ATOM   5619 N  NZ  . LYS A 1 695  ? 21.965 75.346  -38.099 1.00 29.30 ? 695  LYS A NZ  1 
ATOM   5620 N  N   . SER A 1 696  ? 26.367 70.912  -35.190 1.00 13.77 ? 696  SER A N   1 
ATOM   5621 C  CA  . SER A 1 696  ? 26.501 69.600  -35.859 1.00 13.98 ? 696  SER A CA  1 
ATOM   5622 C  C   . SER A 1 696  ? 27.946 69.212  -36.091 1.00 14.58 ? 696  SER A C   1 
ATOM   5623 O  O   . SER A 1 696  ? 28.823 70.085  -36.141 1.00 14.33 ? 696  SER A O   1 
ATOM   5624 C  CB  . SER A 1 696  ? 25.706 69.576  -37.189 1.00 15.96 ? 696  SER A CB  1 
ATOM   5625 O  OG  . SER A 1 696  ? 26.392 70.300  -38.194 1.00 18.87 ? 696  SER A OG  1 
ATOM   5626 N  N   . ILE A 1 697  ? 28.211 67.899  -36.227 1.00 14.86 ? 697  ILE A N   1 
ATOM   5627 C  CA  . ILE A 1 697  ? 29.513 67.347  -36.555 1.00 15.01 ? 697  ILE A CA  1 
ATOM   5628 C  C   . ILE A 1 697  ? 29.392 66.403  -37.746 1.00 16.62 ? 697  ILE A C   1 
ATOM   5629 O  O   . ILE A 1 697  ? 28.524 65.522  -37.745 1.00 17.12 ? 697  ILE A O   1 
ATOM   5630 C  CB  . ILE A 1 697  ? 30.135 66.547  -35.338 1.00 15.63 ? 697  ILE A CB  1 
ATOM   5631 C  CG1 . ILE A 1 697  ? 30.244 67.455  -34.109 1.00 14.09 ? 697  ILE A CG1 1 
ATOM   5632 C  CG2 . ILE A 1 697  ? 31.494 65.904  -35.705 1.00 15.54 ? 697  ILE A CG2 1 
ATOM   5633 C  CD1 . ILE A 1 697  ? 30.671 66.714  -32.824 1.00 15.40 ? 697  ILE A CD1 1 
ATOM   5634 N  N   . GLN A 1 698  ? 30.293 66.562  -38.704 1.00 17.17 ? 698  GLN A N   1 
ATOM   5635 C  CA  . GLN A 1 698  ? 30.380 65.673  -39.857 1.00 19.02 ? 698  GLN A CA  1 
ATOM   5636 C  C   . GLN A 1 698  ? 31.735 65.003  -39.833 1.00 19.20 ? 698  GLN A C   1 
ATOM   5637 O  O   . GLN A 1 698  ? 32.754 65.643  -40.013 1.00 17.83 ? 698  GLN A O   1 
ATOM   5638 C  CB  . GLN A 1 698  ? 30.170 66.474  -41.158 1.00 19.49 ? 698  GLN A CB  1 
ATOM   5639 C  CG  . GLN A 1 698  ? 30.040 65.583  -42.397 1.00 21.83 ? 698  GLN A CG  1 
ATOM   5640 C  CD  . GLN A 1 698  ? 30.252 66.362  -43.693 1.00 22.24 ? 698  GLN A CD  1 
ATOM   5641 O  OE1 . GLN A 1 698  ? 31.143 67.209  -43.784 1.00 25.32 ? 698  GLN A OE1 1 
ATOM   5642 N  NE2 . GLN A 1 698  ? 29.433 66.070  -44.694 1.00 26.46 ? 698  GLN A NE2 1 
ATOM   5643 N  N   . LEU A 1 699  ? 31.754 63.691  -39.602 1.00 20.86 ? 699  LEU A N   1 
ATOM   5644 C  CA  . LEU A 1 699  ? 33.002 62.976  -39.392 1.00 23.62 ? 699  LEU A CA  1 
ATOM   5645 C  C   . LEU A 1 699  ? 33.892 62.929  -40.633 1.00 25.68 ? 699  LEU A C   1 
ATOM   5646 O  O   . LEU A 1 699  ? 35.102 63.122  -40.538 1.00 26.31 ? 699  LEU A O   1 
ATOM   5647 C  CB  . LEU A 1 699  ? 32.738 61.566  -38.815 1.00 23.29 ? 699  LEU A CB  1 
ATOM   5648 C  CG  . LEU A 1 699  ? 31.994 61.554  -37.474 1.00 23.58 ? 699  LEU A CG  1 
ATOM   5649 C  CD1 . LEU A 1 699  ? 31.644 60.111  -37.051 1.00 23.99 ? 699  LEU A CD1 1 
ATOM   5650 C  CD2 . LEU A 1 699  ? 32.843 62.262  -36.432 1.00 23.64 ? 699  LEU A CD2 1 
ATOM   5651 N  N   . THR A 1 700  ? 33.279 62.710  -41.797 1.00 28.47 ? 700  THR A N   1 
ATOM   5652 C  CA  . THR A 1 700  ? 34.017 62.552  -43.056 1.00 31.23 ? 700  THR A CA  1 
ATOM   5653 C  C   . THR A 1 700  ? 33.304 63.292  -44.187 1.00 32.45 ? 700  THR A C   1 
ATOM   5654 O  O   . THR A 1 700  ? 32.135 63.624  -44.062 1.00 32.59 ? 700  THR A O   1 
ATOM   5655 C  CB  . THR A 1 700  ? 34.181 61.044  -43.425 1.00 31.00 ? 700  THR A CB  1 
ATOM   5656 O  OG1 . THR A 1 700  ? 32.889 60.423  -43.518 1.00 32.21 ? 700  THR A OG1 1 
ATOM   5657 C  CG2 . THR A 1 700  ? 34.875 60.260  -42.307 1.00 31.75 ? 700  THR A CG2 1 
ATOM   5658 N  N   . GLN A 1 701  ? 34.024 63.537  -45.284 1.00 34.93 ? 701  GLN A N   1 
ATOM   5659 C  CA  . GLN A 1 701  ? 33.503 64.243  -46.468 1.00 37.18 ? 701  GLN A CA  1 
ATOM   5660 C  C   . GLN A 1 701  ? 32.084 63.842  -46.899 1.00 37.72 ? 701  GLN A C   1 
ATOM   5661 O  O   . GLN A 1 701  ? 31.226 64.705  -47.127 1.00 38.45 ? 701  GLN A O   1 
ATOM   5662 C  CB  . GLN A 1 701  ? 34.464 64.072  -47.654 1.00 37.73 ? 701  GLN A CB  1 
ATOM   5663 C  CG  . GLN A 1 701  ? 35.663 65.017  -47.648 1.00 39.92 ? 701  GLN A CG  1 
ATOM   5664 C  CD  . GLN A 1 701  ? 35.361 66.383  -48.265 1.00 42.73 ? 701  GLN A CD  1 
ATOM   5665 O  OE1 . GLN A 1 701  ? 36.070 67.359  -47.999 1.00 43.79 ? 701  GLN A OE1 1 
ATOM   5666 N  NE2 . GLN A 1 701  ? 34.316 66.454  -49.088 1.00 44.21 ? 701  GLN A NE2 1 
ATOM   5667 N  N   . ASP A 1 702  ? 31.840 62.540  -47.000 1.00 38.24 ? 702  ASP A N   1 
ATOM   5668 C  CA  . ASP A 1 702  ? 30.556 62.030  -47.483 1.00 39.04 ? 702  ASP A CA  1 
ATOM   5669 C  C   . ASP A 1 702  ? 29.482 61.946  -46.394 1.00 38.67 ? 702  ASP A C   1 
ATOM   5670 O  O   . ASP A 1 702  ? 28.281 62.067  -46.681 1.00 39.08 ? 702  ASP A O   1 
ATOM   5671 C  CB  . ASP A 1 702  ? 30.755 60.648  -48.108 1.00 39.63 ? 702  ASP A CB  1 
ATOM   5672 C  CG  . ASP A 1 702  ? 31.195 59.611  -47.089 1.00 41.58 ? 702  ASP A CG  1 
ATOM   5673 O  OD1 . ASP A 1 702  ? 32.266 59.799  -46.460 1.00 43.82 ? 702  ASP A OD1 1 
ATOM   5674 O  OD2 . ASP A 1 702  ? 30.530 58.582  -46.847 1.00 43.79 ? 702  ASP A OD2 1 
ATOM   5675 N  N   . SER A 1 703  ? 29.929 61.761  -45.150 1.00 37.51 ? 703  SER A N   1 
ATOM   5676 C  CA  . SER A 1 703  ? 29.054 61.418  -44.030 1.00 35.94 ? 703  SER A CA  1 
ATOM   5677 C  C   . SER A 1 703  ? 28.034 62.502  -43.658 1.00 34.53 ? 703  SER A C   1 
ATOM   5678 O  O   . SER A 1 703  ? 28.156 63.648  -44.094 1.00 35.08 ? 703  SER A O   1 
ATOM   5679 C  CB  . SER A 1 703  ? 29.895 60.992  -42.816 1.00 36.28 ? 703  SER A CB  1 
ATOM   5680 O  OG  . SER A 1 703  ? 30.550 62.096  -42.216 1.00 35.83 ? 703  SER A OG  1 
ATOM   5681 N  N   . PRO A 1 704  ? 27.023 62.137  -42.866 1.00 33.06 ? 704  PRO A N   1 
ATOM   5682 C  CA  . PRO A 1 704  ? 25.973 63.076  -42.451 1.00 31.31 ? 704  PRO A CA  1 
ATOM   5683 C  C   . PRO A 1 704  ? 26.437 64.147  -41.453 1.00 29.87 ? 704  PRO A C   1 
ATOM   5684 O  O   . PRO A 1 704  ? 27.394 63.935  -40.699 1.00 29.53 ? 704  PRO A O   1 
ATOM   5685 C  CB  . PRO A 1 704  ? 24.938 62.173  -41.772 1.00 31.92 ? 704  PRO A CB  1 
ATOM   5686 C  CG  . PRO A 1 704  ? 25.326 60.790  -42.122 1.00 31.96 ? 704  PRO A CG  1 
ATOM   5687 C  CD  . PRO A 1 704  ? 26.802 60.788  -42.314 1.00 32.93 ? 704  PRO A CD  1 
ATOM   5688 N  N   . HIS A 1 705  ? 25.756 65.291  -41.469 1.00 27.87 ? 705  HIS A N   1 
ATOM   5689 C  CA  . HIS A 1 705  ? 25.937 66.324  -40.442 1.00 26.07 ? 705  HIS A CA  1 
ATOM   5690 C  C   . HIS A 1 705  ? 25.081 65.950  -39.234 1.00 24.42 ? 705  HIS A C   1 
ATOM   5691 O  O   . HIS A 1 705  ? 23.889 66.216  -39.191 1.00 24.23 ? 705  HIS A O   1 
ATOM   5692 C  CB  . HIS A 1 705  ? 25.575 67.712  -41.004 1.00 26.75 ? 705  HIS A CB  1 
ATOM   5693 C  CG  . HIS A 1 705  ? 26.464 68.148  -42.130 1.00 27.93 ? 705  HIS A CG  1 
ATOM   5694 N  ND1 . HIS A 1 705  ? 27.598 68.908  -41.935 1.00 28.00 ? 705  HIS A ND1 1 
ATOM   5695 C  CD2 . HIS A 1 705  ? 26.400 67.905  -43.462 1.00 29.87 ? 705  HIS A CD2 1 
ATOM   5696 C  CE1 . HIS A 1 705  ? 28.194 69.115  -43.097 1.00 30.54 ? 705  HIS A CE1 1 
ATOM   5697 N  NE2 . HIS A 1 705  ? 27.485 68.519  -44.041 1.00 30.98 ? 705  HIS A NE2 1 
ATOM   5698 N  N   . VAL A 1 706  ? 25.718 65.339  -38.229 1.00 21.46 ? 706  VAL A N   1 
ATOM   5699 C  CA  . VAL A 1 706  ? 25.005 64.825  -37.058 1.00 19.68 ? 706  VAL A CA  1 
ATOM   5700 C  C   . VAL A 1 706  ? 24.662 65.929  -36.054 1.00 18.41 ? 706  VAL A C   1 
ATOM   5701 O  O   . VAL A 1 706  ? 25.581 66.625  -35.589 1.00 16.97 ? 706  VAL A O   1 
ATOM   5702 C  CB  . VAL A 1 706  ? 25.888 63.749  -36.342 1.00 19.24 ? 706  VAL A CB  1 
ATOM   5703 C  CG1 . VAL A 1 706  ? 25.167 63.169  -35.130 1.00 19.36 ? 706  VAL A CG1 1 
ATOM   5704 C  CG2 . VAL A 1 706  ? 26.328 62.652  -37.321 1.00 19.91 ? 706  VAL A CG2 1 
ATOM   5705 N  N   . PRO A 1 707  ? 23.396 66.116  -35.685 1.00 17.39 ? 707  PRO A N   1 
ATOM   5706 C  CA  . PRO A 1 707  ? 23.044 67.133  -34.688 1.00 17.44 ? 707  PRO A CA  1 
ATOM   5707 C  C   . PRO A 1 707  ? 23.696 66.882  -33.330 1.00 16.66 ? 707  PRO A C   1 
ATOM   5708 O  O   . PRO A 1 707  ? 23.550 65.823  -32.710 1.00 17.24 ? 707  PRO A O   1 
ATOM   5709 C  CB  . PRO A 1 707  ? 21.513 67.043  -34.593 1.00 17.47 ? 707  PRO A CB  1 
ATOM   5710 C  CG  . PRO A 1 707  ? 21.098 66.344  -35.843 1.00 20.18 ? 707  PRO A CG  1 
ATOM   5711 C  CD  . PRO A 1 707  ? 22.191 65.417  -36.203 1.00 18.43 ? 707  PRO A CD  1 
ATOM   5712 N  N   . VAL A 1 708  ? 24.483 67.863  -32.925 1.00 15.18 ? 708  VAL A N   1 
ATOM   5713 C  CA  . VAL A 1 708  ? 25.143 67.875  -31.632 1.00 14.02 ? 708  VAL A CA  1 
ATOM   5714 C  C   . VAL A 1 708  ? 25.146 69.333  -31.221 1.00 13.07 ? 708  VAL A C   1 
ATOM   5715 O  O   . VAL A 1 708  ? 25.896 70.137  -31.762 1.00 14.63 ? 708  VAL A O   1 
ATOM   5716 C  CB  . VAL A 1 708  ? 26.599 67.383  -31.721 1.00 13.99 ? 708  VAL A CB  1 
ATOM   5717 C  CG1 . VAL A 1 708  ? 27.237 67.407  -30.342 1.00 14.17 ? 708  VAL A CG1 1 
ATOM   5718 C  CG2 . VAL A 1 708  ? 26.659 65.983  -32.287 1.00 15.95 ? 708  VAL A CG2 1 
ATOM   5719 N  N   A HIS A 1 709  ? 24.251 69.685  -30.309 0.50 12.65 ? 709  HIS A N   1 
ATOM   5720 N  N   B HIS A 1 709  ? 24.240 69.698  -30.338 0.50 12.47 ? 709  HIS A N   1 
ATOM   5721 C  CA  A HIS A 1 709  ? 23.980 71.088  -29.978 0.50 13.45 ? 709  HIS A CA  1 
ATOM   5722 C  CA  B HIS A 1 709  ? 24.061 71.106  -30.017 0.50 13.10 ? 709  HIS A CA  1 
ATOM   5723 C  C   A HIS A 1 709  ? 24.386 71.463  -28.542 0.50 13.10 ? 709  HIS A C   1 
ATOM   5724 C  C   B HIS A 1 709  ? 24.499 71.374  -28.585 0.50 13.00 ? 709  HIS A C   1 
ATOM   5725 O  O   A HIS A 1 709  ? 23.826 70.928  -27.569 0.50 12.75 ? 709  HIS A O   1 
ATOM   5726 O  O   B HIS A 1 709  ? 24.099 70.662  -27.673 0.50 12.74 ? 709  HIS A O   1 
ATOM   5727 C  CB  A HIS A 1 709  ? 22.490 71.397  -30.177 0.50 14.12 ? 709  HIS A CB  1 
ATOM   5728 C  CB  B HIS A 1 709  ? 22.601 71.512  -30.225 0.50 13.57 ? 709  HIS A CB  1 
ATOM   5729 C  CG  A HIS A 1 709  ? 22.046 71.369  -31.607 0.50 16.24 ? 709  HIS A CG  1 
ATOM   5730 C  CG  B HIS A 1 709  ? 22.314 72.957  -29.937 0.50 15.23 ? 709  HIS A CG  1 
ATOM   5731 N  ND1 A HIS A 1 709  ? 21.632 72.498  -32.281 0.50 21.38 ? 709  HIS A ND1 1 
ATOM   5732 N  ND1 B HIS A 1 709  ? 23.104 73.988  -30.407 0.50 17.48 ? 709  HIS A ND1 1 
ATOM   5733 C  CD2 A HIS A 1 709  ? 21.964 70.348  -32.492 0.50 18.30 ? 709  HIS A CD2 1 
ATOM   5734 C  CD2 B HIS A 1 709  ? 21.283 73.540  -29.282 0.50 17.20 ? 709  HIS A CD2 1 
ATOM   5735 C  CE1 A HIS A 1 709  ? 21.299 72.168  -33.517 0.50 20.02 ? 709  HIS A CE1 1 
ATOM   5736 C  CE1 B HIS A 1 709  ? 22.591 75.143  -30.016 0.50 17.82 ? 709  HIS A CE1 1 
ATOM   5737 N  NE2 A HIS A 1 709  ? 21.509 70.873  -33.675 0.50 16.55 ? 709  HIS A NE2 1 
ATOM   5738 N  NE2 B HIS A 1 709  ? 21.486 74.899  -29.334 0.50 18.48 ? 709  HIS A NE2 1 
ATOM   5739 N  N   . PHE A 1 710  ? 25.344 72.391  -28.409 1.00 12.57 ? 710  PHE A N   1 
ATOM   5740 C  CA  . PHE A 1 710  ? 25.706 72.885  -27.082 1.00 12.21 ? 710  PHE A CA  1 
ATOM   5741 C  C   . PHE A 1 710  ? 24.717 73.967  -26.643 1.00 12.59 ? 710  PHE A C   1 
ATOM   5742 O  O   . PHE A 1 710  ? 24.311 74.834  -27.465 1.00 12.70 ? 710  PHE A O   1 
ATOM   5743 C  CB  . PHE A 1 710  ? 27.133 73.469  -27.036 1.00 12.84 ? 710  PHE A CB  1 
ATOM   5744 C  CG  . PHE A 1 710  ? 28.218 72.480  -26.629 1.00 13.08 ? 710  PHE A CG  1 
ATOM   5745 C  CD1 . PHE A 1 710  ? 28.167 71.839  -25.396 1.00 15.63 ? 710  PHE A CD1 1 
ATOM   5746 C  CD2 . PHE A 1 710  ? 29.330 72.267  -27.433 1.00 16.29 ? 710  PHE A CD2 1 
ATOM   5747 C  CE1 . PHE A 1 710  ? 29.185 70.943  -25.006 1.00 16.97 ? 710  PHE A CE1 1 
ATOM   5748 C  CE2 . PHE A 1 710  ? 30.361 71.379  -27.019 1.00 15.04 ? 710  PHE A CE2 1 
ATOM   5749 C  CZ  . PHE A 1 710  ? 30.268 70.731  -25.823 1.00 15.79 ? 710  PHE A CZ  1 
ATOM   5750 N  N   . LYS A 1 711  ? 24.335 73.957  -25.379 1.00 11.62 ? 711  LYS A N   1 
ATOM   5751 C  CA  . LYS A 1 711  ? 23.416 74.922  -24.811 1.00 14.34 ? 711  LYS A CA  1 
ATOM   5752 C  C   . LYS A 1 711  ? 23.834 75.147  -23.371 1.00 13.40 ? 711  LYS A C   1 
ATOM   5753 O  O   . LYS A 1 711  ? 24.253 74.171  -22.698 1.00 14.32 ? 711  LYS A O   1 
ATOM   5754 C  CB  . LYS A 1 711  ? 21.989 74.347  -24.848 1.00 15.50 ? 711  LYS A CB  1 
ATOM   5755 C  CG  . LYS A 1 711  ? 20.903 75.281  -24.339 1.00 18.52 ? 711  LYS A CG  1 
ATOM   5756 C  CD  . LYS A 1 711  ? 19.501 74.640  -24.491 1.00 20.16 ? 711  LYS A CD  1 
ATOM   5757 C  CE  . LYS A 1 711  ? 19.048 74.635  -25.957 1.00 23.41 ? 711  LYS A CE  1 
ATOM   5758 N  NZ  . LYS A 1 711  ? 17.753 73.891  -26.125 1.00 25.24 ? 711  LYS A NZ  1 
ATOM   5759 N  N   . PHE A 1 712  ? 23.735 76.375  -22.876 1.00 11.03 ? 712  PHE A N   1 
ATOM   5760 C  CA  . PHE A 1 712  ? 23.917 76.712  -21.480 1.00 11.48 ? 712  PHE A CA  1 
ATOM   5761 C  C   . PHE A 1 712  ? 22.604 77.017  -20.803 1.00 10.80 ? 712  PHE A C   1 
ATOM   5762 O  O   . PHE A 1 712  ? 21.768 77.749  -21.360 1.00 11.78 ? 712  PHE A O   1 
ATOM   5763 C  CB  . PHE A 1 712  ? 24.934 77.863  -21.292 1.00 11.87 ? 712  PHE A CB  1 
ATOM   5764 C  CG  . PHE A 1 712  ? 26.349 77.450  -21.603 1.00 11.19 ? 712  PHE A CG  1 
ATOM   5765 C  CD1 . PHE A 1 712  ? 26.822 77.485  -22.911 1.00 12.05 ? 712  PHE A CD1 1 
ATOM   5766 C  CD2 . PHE A 1 712  ? 27.185 76.965  -20.598 1.00 11.30 ? 712  PHE A CD2 1 
ATOM   5767 C  CE1 . PHE A 1 712  ? 28.127 77.084  -23.232 1.00 10.75 ? 712  PHE A CE1 1 
ATOM   5768 C  CE2 . PHE A 1 712  ? 28.468 76.564  -20.901 1.00 11.06 ? 712  PHE A CE2 1 
ATOM   5769 C  CZ  . PHE A 1 712  ? 28.944 76.602  -22.197 1.00 11.14 ? 712  PHE A CZ  1 
ATOM   5770 N  N   . LEU A 1 713  ? 22.382 76.438  -19.637 1.00 10.08 ? 713  LEU A N   1 
ATOM   5771 C  CA  . LEU A 1 713  ? 21.160 76.654  -18.864 1.00 10.48 ? 713  LEU A CA  1 
ATOM   5772 C  C   . LEU A 1 713  ? 21.470 76.951  -17.411 1.00 10.56 ? 713  LEU A C   1 
ATOM   5773 O  O   . LEU A 1 713  ? 22.667 76.838  -16.973 1.00 10.68 ? 713  LEU A O   1 
ATOM   5774 C  CB  . LEU A 1 713  ? 20.231 75.432  -18.970 1.00 10.71 ? 713  LEU A CB  1 
ATOM   5775 C  CG  . LEU A 1 713  ? 19.889 74.989  -20.380 1.00 11.31 ? 713  LEU A CG  1 
ATOM   5776 C  CD1 . LEU A 1 713  ? 20.765 73.823  -20.836 1.00 13.88 ? 713  LEU A CD1 1 
ATOM   5777 C  CD2 . LEU A 1 713  ? 18.401 74.530  -20.495 1.00 13.27 ? 713  LEU A CD2 1 
ATOM   5778 N  N   . LYS A 1 714  ? 20.466 77.305  -16.633 1.00 11.55 ? 714  LYS A N   1 
ATOM   5779 C  CA  . LYS A 1 714  ? 20.653 77.591  -15.236 1.00 13.32 ? 714  LYS A CA  1 
ATOM   5780 C  C   . LYS A 1 714  ? 19.627 76.906  -14.385 1.00 13.11 ? 714  LYS A C   1 
ATOM   5781 O  O   . LYS A 1 714  ? 18.424 76.866  -14.709 1.00 14.20 ? 714  LYS A O   1 
ATOM   5782 C  CB  . LYS A 1 714  ? 20.637 79.093  -14.941 1.00 16.34 ? 714  LYS A CB  1 
ATOM   5783 C  CG  . LYS A 1 714  ? 19.561 79.861  -15.632 1.00 21.28 ? 714  LYS A CG  1 
ATOM   5784 C  CD  . LYS A 1 714  ? 19.618 81.348  -15.248 1.00 26.87 ? 714  LYS A CD  1 
ATOM   5785 C  CE  . LYS A 1 714  ? 20.968 81.992  -15.532 1.00 30.16 ? 714  LYS A CE  1 
ATOM   5786 N  NZ  . LYS A 1 714  ? 20.957 83.460  -15.211 1.00 33.96 ? 714  LYS A NZ  1 
ATOM   5787 N  N   . TYR A 1 715  ? 20.089 76.362  -13.265 1.00 10.92 ? 715  TYR A N   1 
ATOM   5788 C  CA  . TYR A 1 715  ? 19.221 75.886  -12.219 1.00 10.76 ? 715  TYR A CA  1 
ATOM   5789 C  C   . TYR A 1 715  ? 19.177 76.934  -11.122 1.00 12.13 ? 715  TYR A C   1 
ATOM   5790 O  O   . TYR A 1 715  ? 20.150 77.675  -10.874 1.00 12.25 ? 715  TYR A O   1 
ATOM   5791 C  CB  . TYR A 1 715  ? 19.784 74.599  -11.591 1.00 11.10 ? 715  TYR A CB  1 
ATOM   5792 C  CG  . TYR A 1 715  ? 19.721 73.387  -12.446 1.00 9.55  ? 715  TYR A CG  1 
ATOM   5793 C  CD1 . TYR A 1 715  ? 18.548 72.641  -12.510 1.00 10.86 ? 715  TYR A CD1 1 
ATOM   5794 C  CD2 . TYR A 1 715  ? 20.829 72.950  -13.191 1.00 11.20 ? 715  TYR A CD2 1 
ATOM   5795 C  CE1 . TYR A 1 715  ? 18.465 71.500  -13.280 1.00 10.35 ? 715  TYR A CE1 1 
ATOM   5796 C  CE2 . TYR A 1 715  ? 20.758 71.803  -13.987 1.00 9.58  ? 715  TYR A CE2 1 
ATOM   5797 C  CZ  . TYR A 1 715  ? 19.565 71.058  -14.029 1.00 9.13  ? 715  TYR A CZ  1 
ATOM   5798 O  OH  . TYR A 1 715  ? 19.467 69.922  -14.781 1.00 10.60 ? 715  TYR A OH  1 
ATOM   5799 N  N   . GLY A 1 716  ? 18.058 76.995  -10.411 1.00 12.23 ? 716  GLY A N   1 
ATOM   5800 C  CA  . GLY A 1 716  ? 17.893 77.911  -9.311  1.00 12.31 ? 716  GLY A CA  1 
ATOM   5801 C  C   . GLY A 1 716  ? 17.759 77.130  -8.012  1.00 12.99 ? 716  GLY A C   1 
ATOM   5802 O  O   . GLY A 1 716  ? 18.100 75.907  -7.953  1.00 13.53 ? 716  GLY A O   1 
ATOM   5803 N  N   . VAL A 1 717  ? 17.289 77.802  -6.972  1.00 13.39 ? 717  VAL A N   1 
ATOM   5804 C  CA  . VAL A 1 717  ? 17.174 77.254  -5.631  1.00 14.80 ? 717  VAL A CA  1 
ATOM   5805 C  C   . VAL A 1 717  ? 15.705 77.411  -5.197  1.00 15.44 ? 717  VAL A C   1 
ATOM   5806 O  O   . VAL A 1 717  ? 15.020 78.339  -5.647  1.00 16.64 ? 717  VAL A O   1 
ATOM   5807 C  CB  . VAL A 1 717  ? 18.128 78.000  -4.663  1.00 15.07 ? 717  VAL A CB  1 
ATOM   5808 C  CG1 . VAL A 1 717  ? 17.893 77.650  -3.198  1.00 18.40 ? 717  VAL A CG1 1 
ATOM   5809 C  CG2 . VAL A 1 717  ? 19.584 77.736  -5.055  1.00 14.94 ? 717  VAL A CG2 1 
ATOM   5810 N  N   . ARG A 1 718  ? 15.230 76.520  -4.337  1.00 15.01 ? 718  ARG A N   1 
ATOM   5811 C  CA  . ARG A 1 718  ? 13.844 76.562  -3.846  1.00 16.52 ? 718  ARG A CA  1 
ATOM   5812 C  C   . ARG A 1 718  ? 13.616 77.731  -2.922  1.00 18.66 ? 718  ARG A C   1 
ATOM   5813 O  O   . ARG A 1 718  ? 14.461 78.068  -2.114  1.00 19.48 ? 718  ARG A O   1 
ATOM   5814 C  CB  . ARG A 1 718  ? 13.503 75.252  -3.129  1.00 15.71 ? 718  ARG A CB  1 
ATOM   5815 C  CG  . ARG A 1 718  ? 13.587 74.098  -4.082  1.00 16.25 ? 718  ARG A CG  1 
ATOM   5816 C  CD  . ARG A 1 718  ? 13.549 72.738  -3.412  1.00 16.72 ? 718  ARG A CD  1 
ATOM   5817 N  NE  . ARG A 1 718  ? 13.821 71.718  -4.409  1.00 15.71 ? 718  ARG A NE  1 
ATOM   5818 C  CZ  . ARG A 1 718  ? 13.799 70.405  -4.174  1.00 16.63 ? 718  ARG A CZ  1 
ATOM   5819 N  NH1 . ARG A 1 718  ? 13.484 69.953  -2.963  1.00 15.24 ? 718  ARG A NH1 1 
ATOM   5820 N  NH2 . ARG A 1 718  ? 14.089 69.571  -5.160  1.00 16.82 ? 718  ARG A NH2 1 
ATOM   5821 N  N   . SER A 1 719  ? 12.445 78.348  -3.058  1.00 20.30 ? 719  SER A N   1 
ATOM   5822 C  CA  . SER A 1 719  ? 12.062 79.458  -2.200  1.00 22.45 ? 719  SER A CA  1 
ATOM   5823 C  C   . SER A 1 719  ? 11.306 78.949  -0.965  1.00 23.22 ? 719  SER A C   1 
ATOM   5824 O  O   . SER A 1 719  ? 11.041 79.715  -0.048  1.00 24.68 ? 719  SER A O   1 
ATOM   5825 C  CB  . SER A 1 719  ? 11.196 80.445  -2.995  1.00 22.33 ? 719  SER A CB  1 
ATOM   5826 O  OG  . SER A 1 719  ? 10.010 79.821  -3.412  1.00 25.41 ? 719  SER A OG  1 
ATOM   5827 N  N   . HIS A 1 720  ? 10.920 77.672  -0.967  1.00 23.95 ? 720  HIS A N   1 
ATOM   5828 C  CA  . HIS A 1 720  ? 10.334 77.015  0.196   1.00 24.38 ? 720  HIS A CA  1 
ATOM   5829 C  C   . HIS A 1 720  ? 11.002 75.660  0.376   1.00 23.52 ? 720  HIS A C   1 
ATOM   5830 O  O   . HIS A 1 720  ? 11.357 75.016  -0.608  1.00 23.87 ? 720  HIS A O   1 
ATOM   5831 C  CB  . HIS A 1 720  ? 8.833  76.787  -0.005  1.00 25.75 ? 720  HIS A CB  1 
ATOM   5832 C  CG  . HIS A 1 720  ? 8.099  78.004  -0.460  1.00 27.94 ? 720  HIS A CG  1 
ATOM   5833 N  ND1 . HIS A 1 720  ? 7.791  79.046  0.389   1.00 32.59 ? 720  HIS A ND1 1 
ATOM   5834 C  CD2 . HIS A 1 720  ? 7.631  78.356  -1.681  1.00 30.78 ? 720  HIS A CD2 1 
ATOM   5835 C  CE1 . HIS A 1 720  ? 7.149  79.981  -0.289  1.00 31.85 ? 720  HIS A CE1 1 
ATOM   5836 N  NE2 . HIS A 1 720  ? 7.044  79.590  -1.547  1.00 31.13 ? 720  HIS A NE2 1 
ATOM   5837 N  N   . GLY A 1 721  ? 11.127 75.229  1.624   1.00 22.74 ? 721  GLY A N   1 
ATOM   5838 C  CA  . GLY A 1 721  ? 11.721 73.939  1.933   1.00 22.03 ? 721  GLY A CA  1 
ATOM   5839 C  C   . GLY A 1 721  ? 13.236 74.025  1.918   1.00 21.23 ? 721  GLY A C   1 
ATOM   5840 O  O   . GLY A 1 721  ? 13.822 75.071  2.239   1.00 21.77 ? 721  GLY A O   1 
ATOM   5841 N  N   . ASP A 1 722  ? 13.877 72.930  1.528   1.00 19.37 ? 722  ASP A N   1 
ATOM   5842 C  CA  . ASP A 1 722  ? 15.322 72.822  1.743   1.00 17.42 ? 722  ASP A CA  1 
ATOM   5843 C  C   . ASP A 1 722  ? 16.100 73.518  0.647   1.00 16.49 ? 722  ASP A C   1 
ATOM   5844 O  O   . ASP A 1 722  ? 15.759 73.428  -0.511  1.00 16.05 ? 722  ASP A O   1 
ATOM   5845 C  CB  . ASP A 1 722  ? 15.762 71.359  1.843   1.00 17.05 ? 722  ASP A CB  1 
ATOM   5846 C  CG  . ASP A 1 722  ? 15.183 70.634  3.057   1.00 18.03 ? 722  ASP A CG  1 
ATOM   5847 O  OD1 . ASP A 1 722  ? 14.959 71.238  4.148   1.00 19.04 ? 722  ASP A OD1 1 
ATOM   5848 O  OD2 . ASP A 1 722  ? 14.940 69.412  2.986   1.00 18.47 ? 722  ASP A OD2 1 
ATOM   5849 N  N   . ARG A 1 723  ? 17.177 74.195  1.049   1.00 15.43 ? 723  ARG A N   1 
ATOM   5850 C  CA  . ARG A 1 723  ? 17.992 74.972  0.124   1.00 15.31 ? 723  ARG A CA  1 
ATOM   5851 C  C   . ARG A 1 723  ? 19.271 74.216  -0.292  1.00 13.44 ? 723  ARG A C   1 
ATOM   5852 O  O   . ARG A 1 723  ? 19.924 73.572  0.543   1.00 13.06 ? 723  ARG A O   1 
ATOM   5853 C  CB  . ARG A 1 723  ? 18.391 76.295  0.790   1.00 17.22 ? 723  ARG A CB  1 
ATOM   5854 C  CG  . ARG A 1 723  ? 17.358 77.475  0.775   1.00 21.97 ? 723  ARG A CG  1 
ATOM   5855 C  CD  . ARG A 1 723  ? 15.866 77.153  0.838   1.00 28.66 ? 723  ARG A CD  1 
ATOM   5856 N  NE  . ARG A 1 723  ? 15.081 78.391  0.977   1.00 29.64 ? 723  ARG A NE  1 
ATOM   5857 C  CZ  . ARG A 1 723  ? 14.117 78.596  1.877   1.00 34.23 ? 723  ARG A CZ  1 
ATOM   5858 N  NH1 . ARG A 1 723  ? 13.753 77.640  2.726   1.00 35.68 ? 723  ARG A NH1 1 
ATOM   5859 N  NH2 . ARG A 1 723  ? 13.489 79.765  1.915   1.00 35.84 ? 723  ARG A NH2 1 
ATOM   5860 N  N   . SER A 1 724  ? 19.617 74.321  -1.576  1.00 12.21 ? 724  SER A N   1 
ATOM   5861 C  CA  . SER A 1 724  ? 20.922 73.863  -2.069  1.00 11.70 ? 724  SER A CA  1 
ATOM   5862 C  C   . SER A 1 724  ? 22.025 74.566  -1.305  1.00 11.52 ? 724  SER A C   1 
ATOM   5863 O  O   . SER A 1 724  ? 21.918 75.750  -0.974  1.00 13.19 ? 724  SER A O   1 
ATOM   5864 C  CB  . SER A 1 724  ? 21.078 74.194  -3.539  1.00 11.48 ? 724  SER A CB  1 
ATOM   5865 O  OG  . SER A 1 724  ? 20.018 73.576  -4.249  1.00 11.58 ? 724  SER A OG  1 
ATOM   5866 N  N   . GLY A 1 725  ? 23.143 73.855  -1.123  1.00 10.75 ? 725  GLY A N   1 
ATOM   5867 C  CA  . GLY A 1 725  ? 24.347 74.431  -0.522  1.00 9.78  ? 725  GLY A CA  1 
ATOM   5868 C  C   . GLY A 1 725  ? 25.551 73.678  -1.062  1.00 9.07  ? 725  GLY A C   1 
ATOM   5869 O  O   . GLY A 1 725  ? 25.476 73.040  -2.111  1.00 9.52  ? 725  GLY A O   1 
ATOM   5870 N  N   . ALA A 1 726  ? 26.671 73.755  -0.350  1.00 8.49  ? 726  ALA A N   1 
ATOM   5871 C  CA  . ALA A 1 726  ? 27.911 73.109  -0.818  1.00 8.40  ? 726  ALA A CA  1 
ATOM   5872 C  C   . ALA A 1 726  ? 27.761 71.606  -1.060  1.00 8.07  ? 726  ALA A C   1 
ATOM   5873 O  O   . ALA A 1 726  ? 28.437 71.061  -1.935  1.00 8.15  ? 726  ALA A O   1 
ATOM   5874 C  CB  . ALA A 1 726  ? 29.063 73.345  0.126   1.00 9.82  ? 726  ALA A CB  1 
ATOM   5875 N  N   . TYR A 1 727  ? 26.920 70.939  -0.270  1.00 7.99  ? 727  TYR A N   1 
ATOM   5876 C  CA  . TYR A 1 727  ? 26.758 69.481  -0.367  1.00 7.66  ? 727  TYR A CA  1 
ATOM   5877 C  C   . TYR A 1 727  ? 25.580 69.097  -1.268  1.00 7.58  ? 727  TYR A C   1 
ATOM   5878 O  O   . TYR A 1 727  ? 25.692 68.232  -2.133  1.00 8.08  ? 727  TYR A O   1 
ATOM   5879 C  CB  . TYR A 1 727  ? 26.500 68.878  1.008   1.00 8.20  ? 727  TYR A CB  1 
ATOM   5880 C  CG  . TYR A 1 727  ? 27.557 69.158  2.057   1.00 8.51  ? 727  TYR A CG  1 
ATOM   5881 C  CD1 . TYR A 1 727  ? 27.526 70.329  2.800   1.00 8.62  ? 727  TYR A CD1 1 
ATOM   5882 C  CD2 . TYR A 1 727  ? 28.569 68.224  2.340   1.00 8.76  ? 727  TYR A CD2 1 
ATOM   5883 C  CE1 . TYR A 1 727  ? 28.466 70.562  3.797   1.00 8.32  ? 727  TYR A CE1 1 
ATOM   5884 C  CE2 . TYR A 1 727  ? 29.507 68.452  3.337   1.00 8.42  ? 727  TYR A CE2 1 
ATOM   5885 C  CZ  . TYR A 1 727  ? 29.453 69.615  4.059   1.00 7.52  ? 727  TYR A CZ  1 
ATOM   5886 O  OH  . TYR A 1 727  ? 30.351 69.837  5.088   1.00 8.95  ? 727  TYR A OH  1 
ATOM   5887 N  N   . LEU A 1 728  ? 24.420 69.716  -0.985  1.00 8.95  ? 728  LEU A N   1 
ATOM   5888 C  CA  . LEU A 1 728  ? 23.133 69.313  -1.590  1.00 9.05  ? 728  LEU A CA  1 
ATOM   5889 C  C   . LEU A 1 728  ? 22.787 70.065  -2.855  1.00 9.07  ? 728  LEU A C   1 
ATOM   5890 O  O   . LEU A 1 728  ? 22.978 71.289  -2.936  1.00 9.82  ? 728  LEU A O   1 
ATOM   5891 C  CB  . LEU A 1 728  ? 21.984 69.575  -0.606  1.00 10.43 ? 728  LEU A CB  1 
ATOM   5892 C  CG  . LEU A 1 728  ? 22.130 68.937  0.772   1.00 9.18  ? 728  LEU A CG  1 
ATOM   5893 C  CD1 . LEU A 1 728  ? 20.817 69.191  1.585   1.00 10.52 ? 728  LEU A CD1 1 
ATOM   5894 C  CD2 . LEU A 1 728  ? 22.455 67.443  0.702   1.00 11.17 ? 728  LEU A CD2 1 
ATOM   5895 N  N   . PHE A 1 729  ? 22.229 69.355  -3.832  1.00 9.46  ? 729  PHE A N   1 
ATOM   5896 C  CA  . PHE A 1 729  ? 21.661 69.945  -5.030  1.00 9.97  ? 729  PHE A CA  1 
ATOM   5897 C  C   . PHE A 1 729  ? 20.148 69.751  -4.936  1.00 10.36 ? 729  PHE A C   1 
ATOM   5898 O  O   . PHE A 1 729  ? 19.661 68.632  -5.021  1.00 9.94  ? 729  PHE A O   1 
ATOM   5899 C  CB  . PHE A 1 729  ? 22.236 69.229  -6.234  1.00 9.82  ? 729  PHE A CB  1 
ATOM   5900 C  CG  . PHE A 1 729  ? 21.721 69.713  -7.586  1.00 8.94  ? 729  PHE A CG  1 
ATOM   5901 C  CD1 . PHE A 1 729  ? 21.406 71.060  -7.839  1.00 10.02 ? 729  PHE A CD1 1 
ATOM   5902 C  CD2 . PHE A 1 729  ? 21.638 68.793  -8.626  1.00 8.91  ? 729  PHE A CD2 1 
ATOM   5903 C  CE1 . PHE A 1 729  ? 20.988 71.444  -9.118  1.00 9.56  ? 729  PHE A CE1 1 
ATOM   5904 C  CE2 . PHE A 1 729  ? 21.214 69.173  -9.894  1.00 8.66  ? 729  PHE A CE2 1 
ATOM   5905 C  CZ  . PHE A 1 729  ? 20.893 70.502  -10.129 1.00 9.85  ? 729  PHE A CZ  1 
ATOM   5906 N  N   . LEU A 1 730  ? 19.447 70.870  -4.748  1.00 9.98  ? 730  LEU A N   1 
ATOM   5907 C  CA  . LEU A 1 730  ? 17.986 70.838  -4.572  1.00 11.19 ? 730  LEU A CA  1 
ATOM   5908 C  C   . LEU A 1 730  ? 17.363 71.846  -5.544  1.00 10.72 ? 730  LEU A C   1 
ATOM   5909 O  O   . LEU A 1 730  ? 16.934 72.935  -5.113  1.00 11.49 ? 730  LEU A O   1 
ATOM   5910 C  CB  . LEU A 1 730  ? 17.651 71.171  -3.123  1.00 11.29 ? 730  LEU A CB  1 
ATOM   5911 C  CG  . LEU A 1 730  ? 18.016 70.085  -2.107  1.00 11.26 ? 730  LEU A CG  1 
ATOM   5912 C  CD1 . LEU A 1 730  ? 17.988 70.602  -0.711  1.00 13.38 ? 730  LEU A CD1 1 
ATOM   5913 C  CD2 . LEU A 1 730  ? 17.050 68.892  -2.286  1.00 14.56 ? 730  LEU A CD2 1 
ATOM   5914 N  N   . PRO A 1 731  ? 17.378 71.532  -6.831  1.00 10.57 ? 731  PRO A N   1 
ATOM   5915 C  CA  . PRO A 1 731  ? 16.930 72.504  -7.845  1.00 11.97 ? 731  PRO A CA  1 
ATOM   5916 C  C   . PRO A 1 731  ? 15.440 72.804  -7.711  1.00 12.61 ? 731  PRO A C   1 
ATOM   5917 O  O   . PRO A 1 731  ? 14.647 71.965  -7.254  1.00 13.28 ? 731  PRO A O   1 
ATOM   5918 C  CB  . PRO A 1 731  ? 17.193 71.783  -9.166  1.00 12.02 ? 731  PRO A CB  1 
ATOM   5919 C  CG  . PRO A 1 731  ? 17.187 70.302  -8.829  1.00 12.45 ? 731  PRO A CG  1 
ATOM   5920 C  CD  . PRO A 1 731  ? 17.771 70.254  -7.448  1.00 10.88 ? 731  PRO A CD  1 
ATOM   5921 N  N   . ASN A 1 732  ? 15.073 74.012  -8.136  1.00 13.67 ? 732  ASN A N   1 
ATOM   5922 C  CA  . ASN A 1 732  ? 13.652 74.403  -8.194  1.00 15.56 ? 732  ASN A CA  1 
ATOM   5923 C  C   . ASN A 1 732  ? 13.140 74.073  -9.587  1.00 15.29 ? 732  ASN A C   1 
ATOM   5924 O  O   . ASN A 1 732  ? 12.663 74.967  -10.324 1.00 18.04 ? 732  ASN A O   1 
ATOM   5925 C  CB  . ASN A 1 732  ? 13.471 75.900  -7.888  1.00 16.76 ? 732  ASN A CB  1 
ATOM   5926 C  CG  . ASN A 1 732  ? 14.180 76.794  -8.884  1.00 19.83 ? 732  ASN A CG  1 
ATOM   5927 O  OD1 . ASN A 1 732  ? 15.171 76.408  -9.492  1.00 21.12 ? 732  ASN A OD1 1 
ATOM   5928 N  ND2 . ASN A 1 732  ? 13.651 78.010  -9.073  1.00 22.49 ? 732  ASN A ND2 1 
ATOM   5929 N  N   . GLY A 1 733  ? 13.247 72.817  -9.994  1.00 14.24 ? 733  GLY A N   1 
ATOM   5930 C  CA  . GLY A 1 733  ? 12.778 72.373  -11.293 1.00 14.64 ? 733  GLY A CA  1 
ATOM   5931 C  C   . GLY A 1 733  ? 13.881 72.215  -12.336 1.00 13.63 ? 733  GLY A C   1 
ATOM   5932 O  O   . GLY A 1 733  ? 15.039 72.582  -12.058 1.00 13.48 ? 733  GLY A O   1 
ATOM   5933 N  N   . PRO A 1 734  ? 13.550 71.719  -13.516 1.00 12.75 ? 734  PRO A N   1 
ATOM   5934 C  CA  . PRO A 1 734  ? 14.504 71.635  -14.621 1.00 14.05 ? 734  PRO A CA  1 
ATOM   5935 C  C   . PRO A 1 734  ? 15.118 72.994  -14.938 1.00 14.04 ? 734  PRO A C   1 
ATOM   5936 O  O   . PRO A 1 734  ? 14.545 74.053  -14.671 1.00 13.30 ? 734  PRO A O   1 
ATOM   5937 C  CB  . PRO A 1 734  ? 13.648 71.169  -15.804 1.00 15.06 ? 734  PRO A CB  1 
ATOM   5938 C  CG  . PRO A 1 734  ? 12.480 70.494  -15.161 1.00 16.95 ? 734  PRO A CG  1 
ATOM   5939 C  CD  . PRO A 1 734  ? 12.216 71.185  -13.880 1.00 14.08 ? 734  PRO A CD  1 
ATOM   5940 N  N   . ALA A 1 735  ? 16.325 72.941  -15.499 1.00 12.73 ? 735  ALA A N   1 
ATOM   5941 C  CA  . ALA A 1 735  ? 17.056 74.151  -15.855 1.00 13.65 ? 735  ALA A CA  1 
ATOM   5942 C  C   . ALA A 1 735  ? 16.340 74.980  -16.928 1.00 13.47 ? 735  ALA A C   1 
ATOM   5943 O  O   . ALA A 1 735  ? 15.631 74.427  -17.756 1.00 14.71 ? 735  ALA A O   1 
ATOM   5944 C  CB  . ALA A 1 735  ? 18.451 73.770  -16.307 1.00 12.99 ? 735  ALA A CB  1 
ATOM   5945 N  N   . SER A 1 736  ? 16.580 76.292  -16.883 1.00 14.11 ? 736  SER A N   1 
ATOM   5946 C  CA  . SER A 1 736  ? 16.014 77.251  -17.850 1.00 15.92 ? 736  SER A CA  1 
ATOM   5947 C  C   . SER A 1 736  ? 17.155 77.785  -18.714 1.00 16.11 ? 736  SER A C   1 
ATOM   5948 O  O   . SER A 1 736  ? 18.242 78.021  -18.192 1.00 15.27 ? 736  SER A O   1 
ATOM   5949 C  CB  . SER A 1 736  ? 15.367 78.420  -17.113 1.00 17.34 ? 736  SER A CB  1 
ATOM   5950 O  OG  . SER A 1 736  ? 14.504 77.976  -16.087 1.00 23.91 ? 736  SER A OG  1 
ATOM   5951 N  N   . PRO A 1 737  ? 16.954 77.972  -20.022 1.00 17.32 ? 737  PRO A N   1 
ATOM   5952 C  CA  . PRO A 1 737  ? 18.062 78.434  -20.886 1.00 18.44 ? 737  PRO A CA  1 
ATOM   5953 C  C   . PRO A 1 737  ? 18.635 79.785  -20.448 1.00 18.34 ? 737  PRO A C   1 
ATOM   5954 O  O   . PRO A 1 737  ? 17.887 80.667  -20.048 1.00 19.38 ? 737  PRO A O   1 
ATOM   5955 C  CB  . PRO A 1 737  ? 17.424 78.551  -22.279 1.00 19.38 ? 737  PRO A CB  1 
ATOM   5956 C  CG  . PRO A 1 737  ? 16.187 77.686  -22.210 1.00 19.86 ? 737  PRO A CG  1 
ATOM   5957 C  CD  . PRO A 1 737  ? 15.707 77.734  -20.784 1.00 18.57 ? 737  PRO A CD  1 
ATOM   5958 N  N   . VAL A 1 738  ? 19.960 79.938  -20.496 1.00 18.30 ? 738  VAL A N   1 
ATOM   5959 C  CA  . VAL A 1 738  ? 20.570 81.251  -20.238 1.00 18.72 ? 738  VAL A CA  1 
ATOM   5960 C  C   . VAL A 1 738  ? 20.178 82.155  -21.417 1.00 19.01 ? 738  VAL A C   1 
ATOM   5961 O  O   . VAL A 1 738  ? 20.260 81.739  -22.574 1.00 18.60 ? 738  VAL A O   1 
ATOM   5962 C  CB  . VAL A 1 738  ? 22.103 81.140  -20.129 1.00 18.17 ? 738  VAL A CB  1 
ATOM   5963 C  CG1 . VAL A 1 738  ? 22.786 82.540  -20.105 1.00 19.23 ? 738  VAL A CG1 1 
ATOM   5964 C  CG2 . VAL A 1 738  ? 22.506 80.293  -18.889 1.00 18.27 ? 738  VAL A CG2 1 
ATOM   5965 N  N   . GLU A 1 739  ? 19.741 83.377  -21.118 1.00 19.86 ? 739  GLU A N   1 
ATOM   5966 C  CA  . GLU A 1 739  ? 19.416 84.331  -22.185 1.00 20.92 ? 739  GLU A CA  1 
ATOM   5967 C  C   . GLU A 1 739  ? 20.721 84.882  -22.735 1.00 19.87 ? 739  GLU A C   1 
ATOM   5968 O  O   . GLU A 1 739  ? 21.499 85.485  -21.999 1.00 20.31 ? 739  GLU A O   1 
ATOM   5969 C  CB  . GLU A 1 739  ? 18.597 85.486  -21.644 1.00 21.59 ? 739  GLU A CB  1 
ATOM   5970 C  CG  . GLU A 1 739  ? 17.170 85.134  -21.301 1.00 27.02 ? 739  GLU A CG  1 
ATOM   5971 C  CD  . GLU A 1 739  ? 16.399 86.362  -20.863 1.00 33.75 ? 739  GLU A CD  1 
ATOM   5972 O  OE1 . GLU A 1 739  ? 16.367 87.341  -21.640 1.00 36.29 ? 739  GLU A OE1 1 
ATOM   5973 O  OE2 . GLU A 1 739  ? 15.834 86.350  -19.744 1.00 37.42 ? 739  GLU A OE2 1 
ATOM   5974 N  N   . LEU A 1 740  ? 20.951 84.643  -24.015 1.00 19.86 ? 740  LEU A N   1 
ATOM   5975 C  CA  . LEU A 1 740  ? 22.258 84.924  -24.611 1.00 20.06 ? 740  LEU A CA  1 
ATOM   5976 C  C   . LEU A 1 740  ? 22.416 86.316  -25.210 1.00 20.50 ? 740  LEU A C   1 
ATOM   5977 O  O   . LEU A 1 740  ? 23.532 86.751  -25.417 1.00 20.62 ? 740  LEU A O   1 
ATOM   5978 C  CB  . LEU A 1 740  ? 22.594 83.876  -25.664 1.00 20.33 ? 740  LEU A CB  1 
ATOM   5979 C  CG  . LEU A 1 740  ? 22.557 82.418  -25.209 1.00 19.69 ? 740  LEU A CG  1 
ATOM   5980 C  CD1 . LEU A 1 740  ? 23.042 81.570  -26.346 1.00 20.21 ? 740  LEU A CD1 1 
ATOM   5981 C  CD2 . LEU A 1 740  ? 23.407 82.187  -23.924 1.00 19.05 ? 740  LEU A CD2 1 
ATOM   5982 N  N   . GLY A 1 741  ? 21.309 87.012  -25.477 1.00 21.07 ? 741  GLY A N   1 
ATOM   5983 C  CA  . GLY A 1 741  ? 21.387 88.267  -26.214 1.00 21.05 ? 741  GLY A CA  1 
ATOM   5984 C  C   . GLY A 1 741  ? 21.958 88.029  -27.613 1.00 20.64 ? 741  GLY A C   1 
ATOM   5985 O  O   . GLY A 1 741  ? 21.645 87.036  -28.263 1.00 21.63 ? 741  GLY A O   1 
ATOM   5986 N  N   A GLN A 1 742  ? 22.809 88.944  -28.079 0.50 20.59 ? 742  GLN A N   1 
ATOM   5987 N  N   B GLN A 1 742  ? 22.780 88.966  -28.071 0.50 20.50 ? 742  GLN A N   1 
ATOM   5988 C  CA  A GLN A 1 742  ? 23.484 88.776  -29.372 0.50 19.95 ? 742  GLN A CA  1 
ATOM   5989 C  CA  B GLN A 1 742  ? 23.491 88.820  -29.334 0.50 19.67 ? 742  GLN A CA  1 
ATOM   5990 C  C   A GLN A 1 742  ? 25.018 88.746  -29.192 0.50 18.42 ? 742  GLN A C   1 
ATOM   5991 C  C   B GLN A 1 742  ? 24.982 88.806  -28.973 0.50 18.35 ? 742  GLN A C   1 
ATOM   5992 O  O   A GLN A 1 742  ? 25.719 89.712  -29.492 0.50 18.42 ? 742  GLN A O   1 
ATOM   5993 O  O   B GLN A 1 742  ? 25.600 89.868  -28.826 0.50 17.88 ? 742  GLN A O   1 
ATOM   5994 C  CB  A GLN A 1 742  ? 23.055 89.859  -30.374 0.50 20.26 ? 742  GLN A CB  1 
ATOM   5995 C  CB  B GLN A 1 742  ? 23.160 89.984  -30.282 0.50 20.08 ? 742  GLN A CB  1 
ATOM   5996 C  CG  A GLN A 1 742  ? 23.523 89.588  -31.799 0.50 21.91 ? 742  GLN A CG  1 
ATOM   5997 C  CG  B GLN A 1 742  ? 21.687 90.077  -30.729 0.50 20.93 ? 742  GLN A CG  1 
ATOM   5998 C  CD  A GLN A 1 742  ? 23.107 90.649  -32.817 0.50 22.10 ? 742  GLN A CD  1 
ATOM   5999 C  CD  B GLN A 1 742  ? 21.461 91.182  -31.750 0.50 21.44 ? 742  GLN A CD  1 
ATOM   6000 O  OE1 A GLN A 1 742  ? 22.881 90.325  -33.982 0.50 24.90 ? 742  GLN A OE1 1 
ATOM   6001 O  OE1 B GLN A 1 742  ? 21.332 90.913  -32.945 0.50 25.38 ? 742  GLN A OE1 1 
ATOM   6002 N  NE2 A GLN A 1 742  ? 23.028 91.911  -32.390 0.50 24.63 ? 742  GLN A NE2 1 
ATOM   6003 N  NE2 B GLN A 1 742  ? 21.417 92.420  -31.284 0.50 24.77 ? 742  GLN A NE2 1 
ATOM   6004 N  N   . PRO A 1 743  ? 25.543 87.618  -28.723 1.00 17.15 ? 743  PRO A N   1 
ATOM   6005 C  CA  . PRO A 1 743  ? 26.937 87.559  -28.271 1.00 16.00 ? 743  PRO A CA  1 
ATOM   6006 C  C   . PRO A 1 743  ? 27.938 87.752  -29.406 1.00 14.87 ? 743  PRO A C   1 
ATOM   6007 O  O   . PRO A 1 743  ? 27.668 87.511  -30.597 1.00 16.74 ? 743  PRO A O   1 
ATOM   6008 C  CB  . PRO A 1 743  ? 27.045 86.157  -27.651 1.00 15.75 ? 743  PRO A CB  1 
ATOM   6009 C  CG  . PRO A 1 743  ? 26.021 85.369  -28.288 1.00 16.16 ? 743  PRO A CG  1 
ATOM   6010 C  CD  . PRO A 1 743  ? 24.898 86.286  -28.701 1.00 16.40 ? 743  PRO A CD  1 
ATOM   6011 N  N   . VAL A 1 744  ? 29.111 88.234  -29.011 1.00 13.06 ? 744  VAL A N   1 
ATOM   6012 C  CA  . VAL A 1 744  ? 30.230 88.414  -29.938 1.00 12.47 ? 744  VAL A CA  1 
ATOM   6013 C  C   . VAL A 1 744  ? 30.953 87.090  -30.163 1.00 11.55 ? 744  VAL A C   1 
ATOM   6014 O  O   . VAL A 1 744  ? 31.293 86.389  -29.186 1.00 12.08 ? 744  VAL A O   1 
ATOM   6015 C  CB  . VAL A 1 744  ? 31.214 89.455  -29.404 1.00 11.82 ? 744  VAL A CB  1 
ATOM   6016 C  CG1 . VAL A 1 744  ? 32.379 89.614  -30.325 1.00 13.41 ? 744  VAL A CG1 1 
ATOM   6017 C  CG2 . VAL A 1 744  ? 30.477 90.812  -29.167 1.00 15.13 ? 744  VAL A CG2 1 
ATOM   6018 N  N   . VAL A 1 745  ? 31.141 86.728  -31.419 1.00 10.86 ? 745  VAL A N   1 
ATOM   6019 C  CA  . VAL A 1 745  ? 31.760 85.463  -31.816 1.00 10.76 ? 745  VAL A CA  1 
ATOM   6020 C  C   . VAL A 1 745  ? 33.069 85.736  -32.540 1.00 11.31 ? 745  VAL A C   1 
ATOM   6021 O  O   . VAL A 1 745  ? 33.117 86.571  -33.473 1.00 11.43 ? 745  VAL A O   1 
ATOM   6022 C  CB  . VAL A 1 745  ? 30.803 84.635  -32.711 1.00 11.23 ? 745  VAL A CB  1 
ATOM   6023 C  CG1 . VAL A 1 745  ? 31.458 83.321  -33.177 1.00 12.93 ? 745  VAL A CG1 1 
ATOM   6024 C  CG2 . VAL A 1 745  ? 29.521 84.376  -31.979 1.00 11.59 ? 745  VAL A CG2 1 
ATOM   6025 N  N   . LEU A 1 746  ? 34.149 85.074  -32.139 1.00 10.22 ? 746  LEU A N   1 
ATOM   6026 C  CA  . LEU A 1 746  ? 35.441 85.206  -32.786 1.00 10.09 ? 746  LEU A CA  1 
ATOM   6027 C  C   . LEU A 1 746  ? 35.854 83.903  -33.430 1.00 10.47 ? 746  LEU A C   1 
ATOM   6028 O  O   . LEU A 1 746  ? 35.936 82.859  -32.732 1.00 10.18 ? 746  LEU A O   1 
ATOM   6029 C  CB  . LEU A 1 746  ? 36.486 85.609  -31.741 1.00 11.32 ? 746  LEU A CB  1 
ATOM   6030 C  CG  . LEU A 1 746  ? 37.950 85.606  -32.189 1.00 12.63 ? 746  LEU A CG  1 
ATOM   6031 C  CD1 . LEU A 1 746  ? 38.191 86.686  -33.238 1.00 14.57 ? 746  LEU A CD1 1 
ATOM   6032 C  CD2 . LEU A 1 746  ? 38.835 85.842  -30.994 1.00 15.82 ? 746  LEU A CD2 1 
ATOM   6033 N  N   . VAL A 1 747  ? 36.152 83.923  -34.708 1.00 9.64  ? 747  VAL A N   1 
ATOM   6034 C  CA  . VAL A 1 747  ? 36.553 82.740  -35.445 1.00 10.69 ? 747  VAL A CA  1 
ATOM   6035 C  C   . VAL A 1 747  ? 37.995 82.892  -35.850 1.00 11.60 ? 747  VAL A C   1 
ATOM   6036 O  O   . VAL A 1 747  ? 38.356 83.843  -36.557 1.00 12.46 ? 747  VAL A O   1 
ATOM   6037 C  CB  . VAL A 1 747  ? 35.674 82.561  -36.699 1.00 10.85 ? 747  VAL A CB  1 
ATOM   6038 C  CG1 . VAL A 1 747  ? 36.034 81.273  -37.398 1.00 12.38 ? 747  VAL A CG1 1 
ATOM   6039 C  CG2 . VAL A 1 747  ? 34.236 82.557  -36.319 1.00 12.48 ? 747  VAL A CG2 1 
ATOM   6040 N  N   . THR A 1 748  ? 38.857 81.970  -35.457 1.00 11.26 ? 748  THR A N   1 
ATOM   6041 C  CA  . THR A 1 748  ? 40.228 81.970  -35.894 1.00 12.40 ? 748  THR A CA  1 
ATOM   6042 C  C   . THR A 1 748  ? 40.444 80.748  -36.755 1.00 12.61 ? 748  THR A C   1 
ATOM   6043 O  O   . THR A 1 748  ? 40.125 79.629  -36.308 1.00 13.36 ? 748  THR A O   1 
ATOM   6044 C  CB  . THR A 1 748  ? 41.145 81.995  -34.654 1.00 13.18 ? 748  THR A CB  1 
ATOM   6045 O  OG1 . THR A 1 748  ? 40.936 83.218  -33.934 1.00 14.28 ? 748  THR A OG1 1 
ATOM   6046 C  CG2 . THR A 1 748  ? 42.614 82.019  -35.060 1.00 14.56 ? 748  THR A CG2 1 
ATOM   6047 N  N   . LYS A 1 749  ? 40.974 80.905  -37.972 1.00 12.43 ? 749  LYS A N   1 
ATOM   6048 C  CA  . LYS A 1 749  ? 41.109 79.782  -38.895 1.00 13.79 ? 749  LYS A CA  1 
ATOM   6049 C  C   . LYS A 1 749  ? 42.542 79.641  -39.288 1.00 13.25 ? 749  LYS A C   1 
ATOM   6050 O  O   . LYS A 1 749  ? 43.156 80.574  -39.856 1.00 12.88 ? 749  LYS A O   1 
ATOM   6051 C  CB  . LYS A 1 749  ? 40.269 79.974  -40.154 1.00 13.63 ? 749  LYS A CB  1 
ATOM   6052 C  CG  . LYS A 1 749  ? 40.321 78.777  -41.112 1.00 16.06 ? 749  LYS A CG  1 
ATOM   6053 C  CD  . LYS A 1 749  ? 39.479 79.051  -42.365 1.00 18.34 ? 749  LYS A CD  1 
ATOM   6054 C  CE  . LYS A 1 749  ? 39.879 78.082  -43.466 1.00 23.97 ? 749  LYS A CE  1 
ATOM   6055 N  NZ  . LYS A 1 749  ? 39.551 78.630  -44.814 1.00 29.70 ? 749  LYS A NZ  1 
ATOM   6056 N  N   . GLY A 1 750  ? 43.119 78.492  -38.964 1.00 12.79 ? 750  GLY A N   1 
ATOM   6057 C  CA  . GLY A 1 750  ? 44.505 78.241  -39.267 1.00 13.16 ? 750  GLY A CA  1 
ATOM   6058 C  C   . GLY A 1 750  ? 44.703 76.855  -39.827 1.00 12.70 ? 750  GLY A C   1 
ATOM   6059 O  O   . GLY A 1 750  ? 43.817 75.998  -39.729 1.00 13.86 ? 750  GLY A O   1 
ATOM   6060 N  N   . LYS A 1 751  ? 45.879 76.639  -40.410 1.00 13.67 ? 751  LYS A N   1 
ATOM   6061 C  CA  . LYS A 1 751  ? 46.217 75.354  -41.008 1.00 15.17 ? 751  LYS A CA  1 
ATOM   6062 C  C   . LYS A 1 751  ? 46.329 74.264  -39.946 1.00 13.83 ? 751  LYS A C   1 
ATOM   6063 O  O   . LYS A 1 751  ? 45.947 73.118  -40.211 1.00 14.20 ? 751  LYS A O   1 
ATOM   6064 C  CB  . LYS A 1 751  ? 47.535 75.471  -41.768 1.00 16.68 ? 751  LYS A CB  1 
ATOM   6065 C  CG  . LYS A 1 751  ? 47.956 74.204  -42.484 1.00 23.55 ? 751  LYS A CG  1 
ATOM   6066 C  CD  . LYS A 1 751  ? 47.883 74.344  -44.006 1.00 31.25 ? 751  LYS A CD  1 
ATOM   6067 C  CE  . LYS A 1 751  ? 48.379 73.067  -44.674 1.00 33.34 ? 751  LYS A CE  1 
ATOM   6068 N  NZ  . LYS A 1 751  ? 49.645 72.568  -44.053 1.00 37.28 ? 751  LYS A NZ  1 
ATOM   6069 N  N   . LEU A 1 752  ? 46.861 74.621  -38.772 1.00 13.31 ? 752  LEU A N   1 
ATOM   6070 C  CA  . LEU A 1 752  ? 47.112 73.639  -37.689 1.00 12.39 ? 752  LEU A CA  1 
ATOM   6071 C  C   . LEU A 1 752  ? 46.019 73.657  -36.624 1.00 13.00 ? 752  LEU A C   1 
ATOM   6072 O  O   . LEU A 1 752  ? 45.713 72.636  -36.012 1.00 12.19 ? 752  LEU A O   1 
ATOM   6073 C  CB  . LEU A 1 752  ? 48.473 73.894  -37.029 1.00 12.83 ? 752  LEU A CB  1 
ATOM   6074 C  CG  . LEU A 1 752  ? 49.707 73.794  -37.938 1.00 15.11 ? 752  LEU A CG  1 
ATOM   6075 C  CD1 . LEU A 1 752  ? 51.005 73.935  -37.157 1.00 16.19 ? 752  LEU A CD1 1 
ATOM   6076 C  CD2 . LEU A 1 752  ? 49.730 72.541  -38.788 1.00 18.71 ? 752  LEU A CD2 1 
ATOM   6077 N  N   . GLU A 1 753  ? 45.405 74.817  -36.394 1.00 12.31 ? 753  GLU A N   1 
ATOM   6078 C  CA  . GLU A 1 753  ? 44.467 74.968  -35.290 1.00 12.62 ? 753  GLU A CA  1 
ATOM   6079 C  C   . GLU A 1 753  ? 43.469 76.064  -35.640 1.00 11.96 ? 753  GLU A C   1 
ATOM   6080 O  O   . GLU A 1 753  ? 43.877 77.175  -36.045 1.00 12.33 ? 753  GLU A O   1 
ATOM   6081 C  CB  . GLU A 1 753  ? 45.220 75.336  -33.993 1.00 12.56 ? 753  GLU A CB  1 
ATOM   6082 C  CG  . GLU A 1 753  ? 44.307 75.517  -32.780 1.00 14.65 ? 753  GLU A CG  1 
ATOM   6083 C  CD  . GLU A 1 753  ? 45.021 76.169  -31.595 1.00 17.72 ? 753  GLU A CD  1 
ATOM   6084 O  OE1 . GLU A 1 753  ? 45.298 77.395  -31.645 1.00 25.79 ? 753  GLU A OE1 1 
ATOM   6085 O  OE2 . GLU A 1 753  ? 45.304 75.436  -30.642 1.00 24.39 ? 753  GLU A OE2 1 
ATOM   6086 N  N   . SER A 1 754  ? 42.193 75.767  -35.495 1.00 10.33 ? 754  SER A N   1 
ATOM   6087 C  CA  . SER A 1 754  ? 41.136 76.757  -35.662 1.00 10.14 ? 754  SER A CA  1 
ATOM   6088 C  C   . SER A 1 754  ? 40.248 76.766  -34.436 1.00 9.84  ? 754  SER A C   1 
ATOM   6089 O  O   . SER A 1 754  ? 40.240 75.796  -33.633 1.00 11.01 ? 754  SER A O   1 
ATOM   6090 C  CB  . SER A 1 754  ? 40.302 76.422  -36.901 1.00 10.96 ? 754  SER A CB  1 
ATOM   6091 O  OG  . SER A 1 754  ? 41.076 76.500  -38.064 1.00 11.54 ? 754  SER A OG  1 
ATOM   6092 N  N   . SER A 1 755  ? 39.479 77.812  -34.223 1.00 9.80  ? 755  SER A N   1 
ATOM   6093 C  CA  A SER A 1 755  ? 38.609 77.890  -33.069 0.50 10.38 ? 755  SER A CA  1 
ATOM   6094 C  CA  B SER A 1 755  ? 38.591 77.866  -33.080 0.50 10.73 ? 755  SER A CA  1 
ATOM   6095 C  C   . SER A 1 755  ? 37.440 78.833  -33.271 1.00 9.97  ? 755  SER A C   1 
ATOM   6096 O  O   . SER A 1 755  ? 37.526 79.786  -34.096 1.00 10.74 ? 755  SER A O   1 
ATOM   6097 C  CB  A SER A 1 755  ? 39.412 78.367  -31.862 0.50 11.68 ? 755  SER A CB  1 
ATOM   6098 C  CB  B SER A 1 755  ? 39.369 78.228  -31.805 0.50 12.36 ? 755  SER A CB  1 
ATOM   6099 O  OG  A SER A 1 755  ? 40.113 79.547  -32.172 0.50 10.82 ? 755  SER A OG  1 
ATOM   6100 O  OG  B SER A 1 755  ? 39.619 79.615  -31.701 0.50 12.94 ? 755  SER A OG  1 
ATOM   6101 N  N   . VAL A 1 756  ? 36.385 78.620  -32.514 1.00 9.36  ? 756  VAL A N   1 
ATOM   6102 C  CA  . VAL A 1 756  ? 35.268 79.534  -32.435 1.00 9.77  ? 756  VAL A CA  1 
ATOM   6103 C  C   . VAL A 1 756  ? 35.121 79.848  -30.965 1.00 9.86  ? 756  VAL A C   1 
ATOM   6104 O  O   . VAL A 1 756  ? 34.924 78.913  -30.141 1.00 10.96 ? 756  VAL A O   1 
ATOM   6105 C  CB  . VAL A 1 756  ? 33.984 78.916  -33.000 1.00 10.37 ? 756  VAL A CB  1 
ATOM   6106 C  CG1 . VAL A 1 756  ? 32.774 79.855  -32.777 1.00 12.20 ? 756  VAL A CG1 1 
ATOM   6107 C  CG2 . VAL A 1 756  ? 34.217 78.553  -34.472 1.00 11.99 ? 756  VAL A CG2 1 
ATOM   6108 N  N   . SER A 1 757  ? 35.129 81.118  -30.600 1.00 9.69  ? 757  SER A N   1 
ATOM   6109 C  CA  . SER A 1 757  ? 35.003 81.534  -29.194 1.00 9.93  ? 757  SER A CA  1 
ATOM   6110 C  C   . SER A 1 757  ? 33.849 82.509  -29.087 1.00 10.21 ? 757  SER A C   1 
ATOM   6111 O  O   . SER A 1 757  ? 33.703 83.366  -29.983 1.00 11.51 ? 757  SER A O   1 
ATOM   6112 C  CB  . SER A 1 757  ? 36.285 82.260  -28.746 1.00 11.10 ? 757  SER A CB  1 
ATOM   6113 O  OG  . SER A 1 757  ? 37.398 81.379  -28.876 1.00 13.65 ? 757  SER A OG  1 
ATOM   6114 N  N   . VAL A 1 758  ? 33.042 82.444  -28.044 1.00 9.61  ? 758  VAL A N   1 
ATOM   6115 C  CA  . VAL A 1 758  ? 31.917 83.363  -27.884 1.00 10.34 ? 758  VAL A CA  1 
ATOM   6116 C  C   . VAL A 1 758  ? 31.805 83.818  -26.445 1.00 10.81 ? 758  VAL A C   1 
ATOM   6117 O  O   . VAL A 1 758  ? 31.963 83.011  -25.509 1.00 10.08 ? 758  VAL A O   1 
ATOM   6118 C  CB  . VAL A 1 758  ? 30.605 82.719  -28.392 1.00 10.60 ? 758  VAL A CB  1 
ATOM   6119 C  CG1 . VAL A 1 758  ? 30.316 81.365  -27.706 1.00 11.52 ? 758  VAL A CG1 1 
ATOM   6120 C  CG2 . VAL A 1 758  ? 29.435 83.676  -28.191 1.00 12.83 ? 758  VAL A CG2 1 
ATOM   6121 N  N   . GLY A 1 759  ? 31.512 85.104  -26.236 1.00 11.04 ? 759  GLY A N   1 
ATOM   6122 C  CA  . GLY A 1 759  ? 31.399 85.675  -24.903 1.00 12.55 ? 759  GLY A CA  1 
ATOM   6123 C  C   . GLY A 1 759  ? 29.954 85.608  -24.464 1.00 12.74 ? 759  GLY A C   1 
ATOM   6124 O  O   . GLY A 1 759  ? 29.138 86.485  -24.791 1.00 13.03 ? 759  GLY A O   1 
ATOM   6125 N  N   . LEU A 1 760  ? 29.589 84.569  -23.734 1.00 12.95 ? 760  LEU A N   1 
ATOM   6126 C  CA  . LEU A 1 760  ? 28.237 84.409  -23.215 1.00 13.86 ? 760  LEU A CA  1 
ATOM   6127 C  C   . LEU A 1 760  ? 28.165 84.956  -21.815 1.00 13.33 ? 760  LEU A C   1 
ATOM   6128 O  O   . LEU A 1 760  ? 29.205 85.116  -21.151 1.00 14.00 ? 760  LEU A O   1 
ATOM   6129 C  CB  . LEU A 1 760  ? 27.878 82.928  -23.178 1.00 13.96 ? 760  LEU A CB  1 
ATOM   6130 C  CG  . LEU A 1 760  ? 28.000 82.223  -24.514 1.00 13.86 ? 760  LEU A CG  1 
ATOM   6131 C  CD1 . LEU A 1 760  ? 27.777 80.720  -24.366 1.00 15.84 ? 760  LEU A CD1 1 
ATOM   6132 C  CD2 . LEU A 1 760  ? 27.059 82.787  -25.609 1.00 17.24 ? 760  LEU A CD2 1 
ATOM   6133 N  N   . PRO A 1 761  ? 26.970 85.229  -21.296 1.00 14.59 ? 761  PRO A N   1 
ATOM   6134 C  CA  . PRO A 1 761  ? 26.862 85.611  -19.886 1.00 14.99 ? 761  PRO A CA  1 
ATOM   6135 C  C   . PRO A 1 761  ? 27.450 84.496  -19.013 1.00 14.56 ? 761  PRO A C   1 
ATOM   6136 O  O   . PRO A 1 761  ? 27.003 83.350  -19.048 1.00 15.33 ? 761  PRO A O   1 
ATOM   6137 C  CB  . PRO A 1 761  ? 25.343 85.768  -19.667 1.00 16.25 ? 761  PRO A CB  1 
ATOM   6138 C  CG  . PRO A 1 761  ? 24.826 86.103  -21.037 1.00 16.43 ? 761  PRO A CG  1 
ATOM   6139 C  CD  . PRO A 1 761  ? 25.662 85.269  -21.975 1.00 14.55 ? 761  PRO A CD  1 
ATOM   6140 N  N   . SER A 1 762  ? 28.444 84.895  -18.228 1.00 14.22 ? 762  SER A N   1 
ATOM   6141 C  CA  . SER A 1 762  ? 29.171 84.051  -17.281 1.00 13.72 ? 762  SER A CA  1 
ATOM   6142 C  C   . SER A 1 762  ? 30.124 83.042  -17.886 1.00 12.25 ? 762  SER A C   1 
ATOM   6143 O  O   . SER A 1 762  ? 30.796 82.343  -17.122 1.00 12.20 ? 762  SER A O   1 
ATOM   6144 C  CB  . SER A 1 762  ? 28.247 83.258  -16.368 1.00 13.94 ? 762  SER A CB  1 
ATOM   6145 O  OG  . SER A 1 762  ? 27.295 84.058  -15.689 1.00 17.86 ? 762  SER A OG  1 
ATOM   6146 N  N   . VAL A 1 763  ? 30.188 82.921  -19.197 1.00 11.02 ? 763  VAL A N   1 
ATOM   6147 C  CA  . VAL A 1 763  ? 31.058 81.917  -19.805 1.00 11.04 ? 763  VAL A CA  1 
ATOM   6148 C  C   . VAL A 1 763  ? 31.660 82.382  -21.104 1.00 10.49 ? 763  VAL A C   1 
ATOM   6149 O  O   . VAL A 1 763  ? 30.915 82.741  -22.011 1.00 11.09 ? 763  VAL A O   1 
ATOM   6150 C  CB  . VAL A 1 763  ? 30.284 80.603  -20.104 1.00 12.74 ? 763  VAL A CB  1 
ATOM   6151 C  CG1 . VAL A 1 763  ? 31.221 79.546  -20.641 1.00 12.26 ? 763  VAL A CG1 1 
ATOM   6152 C  CG2 . VAL A 1 763  ? 29.567 80.033  -18.894 1.00 14.94 ? 763  VAL A CG2 1 
ATOM   6153 N  N   . VAL A 1 764  ? 32.980 82.390  -21.230 1.00 8.93  ? 764  VAL A N   1 
ATOM   6154 C  CA  . VAL A 1 764  ? 33.580 82.475  -22.545 1.00 9.15  ? 764  VAL A CA  1 
ATOM   6155 C  C   . VAL A 1 764  ? 33.759 81.030  -23.010 1.00 9.53  ? 764  VAL A C   1 
ATOM   6156 O  O   . VAL A 1 764  ? 34.541 80.277  -22.401 1.00 8.91  ? 764  VAL A O   1 
ATOM   6157 C  CB  . VAL A 1 764  ? 34.935 83.237  -22.561 1.00 9.91  ? 764  VAL A CB  1 
ATOM   6158 C  CG1 . VAL A 1 764  ? 35.463 83.270  -23.988 1.00 11.24 ? 764  VAL A CG1 1 
ATOM   6159 C  CG2 . VAL A 1 764  ? 34.758 84.671  -22.025 1.00 11.53 ? 764  VAL A CG2 1 
ATOM   6160 N  N   . HIS A 1 765  ? 33.031 80.646  -24.045 1.00 9.43  ? 765  HIS A N   1 
ATOM   6161 C  CA  . HIS A 1 765  ? 32.952 79.252  -24.506 1.00 9.39  ? 765  HIS A CA  1 
ATOM   6162 C  C   . HIS A 1 765  ? 33.768 79.138  -25.781 1.00 10.00 ? 765  HIS A C   1 
ATOM   6163 O  O   . HIS A 1 765  ? 33.602 79.977  -26.704 1.00 10.39 ? 765  HIS A O   1 
ATOM   6164 C  CB  . HIS A 1 765  ? 31.476 78.925  -24.738 1.00 9.86  ? 765  HIS A CB  1 
ATOM   6165 C  CG  . HIS A 1 765  ? 31.223 77.637  -25.428 1.00 9.19  ? 765  HIS A CG  1 
ATOM   6166 N  ND1 . HIS A 1 765  ? 31.435 76.409  -24.821 1.00 9.41  ? 765  HIS A ND1 1 
ATOM   6167 C  CD2 . HIS A 1 765  ? 30.727 77.378  -26.661 1.00 10.95 ? 765  HIS A CD2 1 
ATOM   6168 C  CE1 . HIS A 1 765  ? 31.075 75.454  -25.664 1.00 11.13 ? 765  HIS A CE1 1 
ATOM   6169 N  NE2 . HIS A 1 765  ? 30.644 76.017  -26.793 1.00 11.57 ? 765  HIS A NE2 1 
ATOM   6170 N  N   . GLN A 1 766  ? 34.670 78.172  -25.857 1.00 8.95  ? 766  GLN A N   1 
ATOM   6171 C  CA  A GLN A 1 766  ? 35.590 78.034  -26.971 0.50 9.55  ? 766  GLN A CA  1 
ATOM   6172 C  CA  B GLN A 1 766  ? 35.560 78.031  -26.984 0.50 9.52  ? 766  GLN A CA  1 
ATOM   6173 C  C   . GLN A 1 766  ? 35.575 76.605  -27.485 1.00 9.58  ? 766  GLN A C   1 
ATOM   6174 O  O   . GLN A 1 766  ? 35.669 75.651  -26.685 1.00 9.80  ? 766  GLN A O   1 
ATOM   6175 C  CB  A GLN A 1 766  ? 37.015 78.400  -26.545 0.50 9.88  ? 766  GLN A CB  1 
ATOM   6176 C  CB  B GLN A 1 766  ? 36.974 78.448  -26.607 0.50 9.65  ? 766  GLN A CB  1 
ATOM   6177 C  CG  A GLN A 1 766  ? 37.129 79.730  -25.792 0.50 10.29 ? 766  GLN A CG  1 
ATOM   6178 C  CG  B GLN A 1 766  ? 37.931 78.463  -27.773 0.50 10.19 ? 766  GLN A CG  1 
ATOM   6179 C  CD  A GLN A 1 766  ? 38.116 79.692  -24.596 0.50 15.56 ? 766  GLN A CD  1 
ATOM   6180 C  CD  B GLN A 1 766  ? 39.353 78.838  -27.381 0.50 13.08 ? 766  GLN A CD  1 
ATOM   6181 O  OE1 A GLN A 1 766  ? 39.293 79.417  -24.805 0.50 14.05 ? 766  GLN A OE1 1 
ATOM   6182 O  OE1 B GLN A 1 766  ? 39.743 78.708  -26.215 0.50 16.36 ? 766  GLN A OE1 1 
ATOM   6183 N  NE2 A GLN A 1 766  ? 37.631 79.962  -23.352 0.50 13.46 ? 766  GLN A NE2 1 
ATOM   6184 N  NE2 B GLN A 1 766  ? 40.131 79.307  -28.356 0.50 13.23 ? 766  GLN A NE2 1 
ATOM   6185 N  N   . THR A 1 767  ? 35.454 76.440  -28.790 1.00 8.60  ? 767  THR A N   1 
ATOM   6186 C  CA  . THR A 1 767  ? 35.604 75.144  -29.457 1.00 9.69  ? 767  THR A CA  1 
ATOM   6187 C  C   . THR A 1 767  ? 36.838 75.183  -30.302 1.00 9.43  ? 767  THR A C   1 
ATOM   6188 O  O   . THR A 1 767  ? 36.946 76.069  -31.167 1.00 10.21 ? 767  THR A O   1 
ATOM   6189 C  CB  . THR A 1 767  ? 34.401 74.867  -30.340 1.00 9.94  ? 767  THR A CB  1 
ATOM   6190 O  OG1 . THR A 1 767  ? 33.215 74.936  -29.547 1.00 12.29 ? 767  THR A OG1 1 
ATOM   6191 C  CG2 . THR A 1 767  ? 34.463 73.430  -30.915 1.00 10.78 ? 767  THR A CG2 1 
ATOM   6192 N  N   . ILE A 1 768  ? 37.808 74.312  -30.045 1.00 9.75  ? 768  ILE A N   1 
ATOM   6193 C  CA  . ILE A 1 768  ? 39.097 74.309  -30.701 1.00 9.99  ? 768  ILE A CA  1 
ATOM   6194 C  C   . ILE A 1 768  ? 39.264 73.034  -31.520 1.00 10.61 ? 768  ILE A C   1 
ATOM   6195 O  O   . ILE A 1 768  ? 38.926 71.930  -31.037 1.00 11.33 ? 768  ILE A O   1 
ATOM   6196 C  CB  . ILE A 1 768  ? 40.238 74.400  -29.668 1.00 9.88  ? 768  ILE A CB  1 
ATOM   6197 C  CG1 . ILE A 1 768  ? 40.049 75.636  -28.805 1.00 11.86 ? 768  ILE A CG1 1 
ATOM   6198 C  CG2 . ILE A 1 768  ? 41.589 74.443  -30.333 1.00 12.33 ? 768  ILE A CG2 1 
ATOM   6199 C  CD1 . ILE A 1 768  ? 40.838 75.641  -27.480 1.00 14.36 ? 768  ILE A CD1 1 
ATOM   6200 N  N   . MET A 1 769  ? 39.765 73.190  -32.735 1.00 10.45 ? 769  MET A N   1 
ATOM   6201 C  CA  A MET A 1 769  ? 39.903 72.091  -33.683 0.50 11.07 ? 769  MET A CA  1 
ATOM   6202 C  CA  B MET A 1 769  ? 39.903 72.094  -33.687 0.50 11.42 ? 769  MET A CA  1 
ATOM   6203 C  C   . MET A 1 769  ? 41.346 71.973  -34.097 1.00 11.90 ? 769  MET A C   1 
ATOM   6204 O  O   . MET A 1 769  ? 41.942 72.929  -34.551 1.00 11.16 ? 769  MET A O   1 
ATOM   6205 C  CB  A MET A 1 769  ? 39.045 72.351  -34.911 0.50 12.14 ? 769  MET A CB  1 
ATOM   6206 C  CB  B MET A 1 769  ? 39.056 72.357  -34.923 0.50 12.48 ? 769  MET A CB  1 
ATOM   6207 C  CG  A MET A 1 769  ? 37.590 72.365  -34.566 0.50 10.21 ? 769  MET A CG  1 
ATOM   6208 C  CG  B MET A 1 769  ? 37.594 72.227  -34.637 0.50 11.73 ? 769  MET A CG  1 
ATOM   6209 S  SD  A MET A 1 769  ? 36.605 73.000  -35.900 0.50 13.82 ? 769  MET A SD  1 
ATOM   6210 S  SD  B MET A 1 769  ? 36.603 73.014  -35.890 0.50 14.80 ? 769  MET A SD  1 
ATOM   6211 C  CE  A MET A 1 769  ? 36.844 71.656  -37.066 0.50 11.57 ? 769  MET A CE  1 
ATOM   6212 C  CE  B MET A 1 769  ? 36.473 74.636  -35.139 0.50 18.41 ? 769  MET A CE  1 
ATOM   6213 N  N   . ARG A 1 770  ? 41.891 70.777  -33.949 1.00 12.46 ? 770  ARG A N   1 
ATOM   6214 C  CA  A ARG A 1 770  ? 43.258 70.553  -34.355 0.50 13.92 ? 770  ARG A CA  1 
ATOM   6215 C  CA  B ARG A 1 770  ? 43.252 70.524  -34.380 0.50 13.53 ? 770  ARG A CA  1 
ATOM   6216 C  C   . ARG A 1 770  ? 43.365 69.373  -35.343 1.00 15.03 ? 770  ARG A C   1 
ATOM   6217 O  O   . ARG A 1 770  ? 44.484 68.895  -35.589 1.00 16.98 ? 770  ARG A O   1 
ATOM   6218 C  CB  A ARG A 1 770  ? 44.180 70.394  -33.123 0.50 14.13 ? 770  ARG A CB  1 
ATOM   6219 C  CB  B ARG A 1 770  ? 44.126 70.171  -33.210 0.50 13.64 ? 770  ARG A CB  1 
ATOM   6220 C  CG  A ARG A 1 770  ? 44.015 71.483  -32.029 0.50 14.76 ? 770  ARG A CG  1 
ATOM   6221 C  CG  B ARG A 1 770  ? 44.494 71.297  -32.344 0.50 13.00 ? 770  ARG A CG  1 
ATOM   6222 C  CD  A ARG A 1 770  ? 45.016 71.408  -30.853 0.50 14.48 ? 770  ARG A CD  1 
ATOM   6223 C  CD  B ARG A 1 770  ? 45.343 70.828  -31.175 0.50 11.17 ? 770  ARG A CD  1 
ATOM   6224 N  NE  A ARG A 1 770  ? 44.824 72.468  -29.863 0.50 16.79 ? 770  ARG A NE  1 
ATOM   6225 N  NE  B ARG A 1 770  ? 44.645 69.849  -30.343 0.50 13.41 ? 770  ARG A NE  1 
ATOM   6226 C  CZ  A ARG A 1 770  ? 44.200 72.324  -28.690 0.50 16.00 ? 770  ARG A CZ  1 
ATOM   6227 C  CZ  B ARG A 1 770  ? 43.814 70.163  -29.368 0.50 13.60 ? 770  ARG A CZ  1 
ATOM   6228 N  NH1 A ARG A 1 770  ? 43.694 71.147  -28.316 0.50 15.50 ? 770  ARG A NH1 1 
ATOM   6229 N  NH1 B ARG A 1 770  ? 43.535 71.437  -29.106 0.50 14.75 ? 770  ARG A NH1 1 
ATOM   6230 N  NH2 A ARG A 1 770  ? 44.093 73.364  -27.873 0.50 16.72 ? 770  ARG A NH2 1 
ATOM   6231 N  NH2 B ARG A 1 770  ? 43.241 69.189  -28.673 0.50 13.73 ? 770  ARG A NH2 1 
ATOM   6232 N  N   . GLY A 1 771  ? 42.225 68.921  -35.865 1.00 15.01 ? 771  GLY A N   1 
ATOM   6233 C  CA  . GLY A 1 771  ? 42.222 67.857  -36.854 1.00 17.28 ? 771  GLY A CA  1 
ATOM   6234 C  C   . GLY A 1 771  ? 41.611 66.553  -36.388 1.00 17.91 ? 771  GLY A C   1 
ATOM   6235 O  O   . GLY A 1 771  ? 41.434 65.640  -37.193 1.00 19.60 ? 771  GLY A O   1 
ATOM   6236 N  N   . GLY A 1 772  ? 41.272 66.461  -35.102 1.00 17.60 ? 772  GLY A N   1 
ATOM   6237 C  CA  . GLY A 1 772  ? 40.634 65.282  -34.502 1.00 17.47 ? 772  GLY A CA  1 
ATOM   6238 C  C   . GLY A 1 772  ? 39.446 65.728  -33.657 1.00 16.59 ? 772  GLY A C   1 
ATOM   6239 O  O   . GLY A 1 772  ? 38.752 66.680  -34.000 1.00 16.69 ? 772  GLY A O   1 
ATOM   6240 N  N   . ALA A 1 773  ? 39.176 65.028  -32.546 1.00 15.06 ? 773  ALA A N   1 
ATOM   6241 C  CA  . ALA A 1 773  ? 38.088 65.413  -31.652 1.00 13.70 ? 773  ALA A CA  1 
ATOM   6242 C  C   . ALA A 1 773  ? 38.278 66.862  -31.188 1.00 12.03 ? 773  ALA A C   1 
ATOM   6243 O  O   . ALA A 1 773  ? 39.378 67.214  -30.784 1.00 11.38 ? 773  ALA A O   1 
ATOM   6244 C  CB  . ALA A 1 773  ? 38.055 64.508  -30.437 1.00 14.77 ? 773  ALA A CB  1 
ATOM   6245 N  N   . PRO A 1 774  ? 37.235 67.681  -31.215 1.00 11.22 ? 774  PRO A N   1 
ATOM   6246 C  CA  . PRO A 1 774  ? 37.413 69.057  -30.713 1.00 10.59 ? 774  PRO A CA  1 
ATOM   6247 C  C   . PRO A 1 774  ? 37.725 69.109  -29.219 1.00 9.86  ? 774  PRO A C   1 
ATOM   6248 O  O   . PRO A 1 774  ? 37.449 68.143  -28.467 1.00 9.61  ? 774  PRO A O   1 
ATOM   6249 C  CB  . PRO A 1 774  ? 36.049 69.733  -30.967 1.00 12.19 ? 774  PRO A CB  1 
ATOM   6250 C  CG  . PRO A 1 774  ? 35.096 68.667  -31.237 1.00 15.37 ? 774  PRO A CG  1 
ATOM   6251 C  CD  . PRO A 1 774  ? 35.879 67.439  -31.746 1.00 11.87 ? 774  PRO A CD  1 
ATOM   6252 N  N   . GLU A 1 775  ? 38.308 70.215  -28.824 1.00 9.61  ? 775  GLU A N   1 
ATOM   6253 C  CA  . GLU A 1 775  ? 38.547 70.541  -27.436 1.00 9.20  ? 775  GLU A CA  1 
ATOM   6254 C  C   . GLU A 1 775  ? 37.597 71.678  -27.095 1.00 8.54  ? 775  GLU A C   1 
ATOM   6255 O  O   . GLU A 1 775  ? 37.396 72.618  -27.939 1.00 10.59 ? 775  GLU A O   1 
ATOM   6256 C  CB  . GLU A 1 775  ? 39.995 70.945  -27.228 1.00 9.21  ? 775  GLU A CB  1 
ATOM   6257 C  CG  . GLU A 1 775  ? 40.299 71.399  -25.799 1.00 11.32 ? 775  GLU A CG  1 
ATOM   6258 C  CD  . GLU A 1 775  ? 41.770 71.626  -25.545 1.00 17.73 ? 775  GLU A CD  1 
ATOM   6259 O  OE1 . GLU A 1 775  ? 42.614 70.880  -26.088 1.00 21.50 ? 775  GLU A OE1 1 
ATOM   6260 O  OE2 . GLU A 1 775  ? 42.102 72.518  -24.759 1.00 20.44 ? 775  GLU A OE2 1 
ATOM   6261 N  N   . ILE A 1 776  ? 36.929 71.623  -25.960 1.00 7.91  ? 776  ILE A N   1 
ATOM   6262 C  CA  . ILE A 1 776  ? 36.076 72.686  -25.489 1.00 8.69  ? 776  ILE A CA  1 
ATOM   6263 C  C   . ILE A 1 776  ? 36.748 73.306  -24.295 1.00 8.36  ? 776  ILE A C   1 
ATOM   6264 O  O   . ILE A 1 776  ? 37.207 72.590  -23.392 1.00 8.34  ? 776  ILE A O   1 
ATOM   6265 C  CB  . ILE A 1 776  ? 34.681 72.152  -25.069 1.00 9.41  ? 776  ILE A CB  1 
ATOM   6266 C  CG1 . ILE A 1 776  ? 34.070 71.236  -26.155 1.00 13.74 ? 776  ILE A CG1 1 
ATOM   6267 C  CG2 . ILE A 1 776  ? 33.784 73.328  -24.596 1.00 11.14 ? 776  ILE A CG2 1 
ATOM   6268 C  CD1 . ILE A 1 776  ? 33.921 71.865  -27.531 1.00 16.97 ? 776  ILE A CD1 1 
ATOM   6269 N  N   . ARG A 1 777  ? 36.795 74.630  -24.230 1.00 8.32  ? 777  ARG A N   1 
ATOM   6270 C  CA  . ARG A 1 777  ? 37.256 75.324  -23.030 1.00 8.72  ? 777  ARG A CA  1 
ATOM   6271 C  C   . ARG A 1 777  ? 36.207 76.318  -22.598 1.00 8.94  ? 777  ARG A C   1 
ATOM   6272 O  O   . ARG A 1 777  ? 35.722 77.118  -23.456 1.00 9.66  ? 777  ARG A O   1 
ATOM   6273 C  CB  . ARG A 1 777  ? 38.562 76.082  -23.272 1.00 10.12 ? 777  ARG A CB  1 
ATOM   6274 C  CG  . ARG A 1 777  ? 39.721 75.224  -23.618 1.00 10.34 ? 777  ARG A CG  1 
ATOM   6275 C  CD  . ARG A 1 777  ? 40.988 76.021  -23.772 1.00 11.01 ? 777  ARG A CD  1 
ATOM   6276 N  NE  . ARG A 1 777  ? 42.085 75.185  -24.240 1.00 13.77 ? 777  ARG A NE  1 
ATOM   6277 C  CZ  . ARG A 1 777  ? 43.274 75.651  -24.579 1.00 18.49 ? 777  ARG A CZ  1 
ATOM   6278 N  NH1 . ARG A 1 777  ? 43.541 76.958  -24.439 1.00 20.22 ? 777  ARG A NH1 1 
ATOM   6279 N  NH2 . ARG A 1 777  ? 44.212 74.825  -25.040 1.00 21.03 ? 777  ARG A NH2 1 
ATOM   6280 N  N   . ASN A 1 778  ? 35.843 76.335  -21.339 1.00 8.05  ? 778  ASN A N   1 
ATOM   6281 C  CA  . ASN A 1 778  ? 34.908 77.304  -20.811 1.00 7.88  ? 778  ASN A CA  1 
ATOM   6282 C  C   . ASN A 1 778  ? 35.614 78.112  -19.749 1.00 8.17  ? 778  ASN A C   1 
ATOM   6283 O  O   . ASN A 1 778  ? 36.029 77.545  -18.711 1.00 8.61  ? 778  ASN A O   1 
ATOM   6284 C  CB  . ASN A 1 778  ? 33.698 76.625  -20.145 1.00 8.25  ? 778  ASN A CB  1 
ATOM   6285 C  CG  . ASN A 1 778  ? 32.758 75.966  -21.129 1.00 9.34  ? 778  ASN A CG  1 
ATOM   6286 O  OD1 . ASN A 1 778  ? 32.704 76.333  -22.307 1.00 10.45 ? 778  ASN A OD1 1 
ATOM   6287 N  ND2 . ASN A 1 778  ? 31.976 74.992  -20.623 1.00 8.88  ? 778  ASN A ND2 1 
ATOM   6288 N  N   . LEU A 1 779  ? 35.686 79.439  -19.949 1.00 8.45  ? 779  LEU A N   1 
ATOM   6289 C  CA  . LEU A 1 779  ? 36.139 80.320  -18.863 1.00 9.08  ? 779  LEU A CA  1 
ATOM   6290 C  C   . LEU A 1 779  ? 34.897 80.758  -18.119 1.00 8.76  ? 779  LEU A C   1 
ATOM   6291 O  O   . LEU A 1 779  ? 34.086 81.542  -18.657 1.00 9.61  ? 779  LEU A O   1 
ATOM   6292 C  CB  . LEU A 1 779  ? 36.923 81.513  -19.439 1.00 10.02 ? 779  LEU A CB  1 
ATOM   6293 C  CG  . LEU A 1 779  ? 37.479 82.512  -18.413 1.00 13.38 ? 779  LEU A CG  1 
ATOM   6294 C  CD1 . LEU A 1 779  ? 38.469 81.844  -17.518 1.00 16.34 ? 779  LEU A CD1 1 
ATOM   6295 C  CD2 . LEU A 1 779  ? 38.080 83.736  -19.140 1.00 15.45 ? 779  LEU A CD2 1 
ATOM   6296 N  N   . VAL A 1 780  ? 34.682 80.186  -16.945 1.00 8.61  ? 780  VAL A N   1 
ATOM   6297 C  CA  . VAL A 1 780  ? 33.425 80.320  -16.214 1.00 9.77  ? 780  VAL A CA  1 
ATOM   6298 C  C   . VAL A 1 780  ? 33.581 81.318  -15.070 1.00 10.22 ? 780  VAL A C   1 
ATOM   6299 O  O   . VAL A 1 780  ? 34.392 81.117  -14.164 1.00 10.08 ? 780  VAL A O   1 
ATOM   6300 C  CB  . VAL A 1 780  ? 32.948 78.937  -15.663 1.00 9.53  ? 780  VAL A CB  1 
ATOM   6301 C  CG1 . VAL A 1 780  ? 31.622 79.069  -14.933 1.00 10.48 ? 780  VAL A CG1 1 
ATOM   6302 C  CG2 . VAL A 1 780  ? 32.891 77.904  -16.780 1.00 10.38 ? 780  VAL A CG2 1 
ATOM   6303 N  N   . ASP A 1 781  ? 32.815 82.406  -15.146 1.00 10.12 ? 781  ASP A N   1 
ATOM   6304 C  CA  . ASP A 1 781  ? 32.811 83.405  -14.092 1.00 10.63 ? 781  ASP A CA  1 
ATOM   6305 C  C   . ASP A 1 781  ? 31.392 83.736  -13.725 1.00 11.51 ? 781  ASP A C   1 
ATOM   6306 O  O   . ASP A 1 781  ? 30.729 84.585  -14.382 1.00 12.02 ? 781  ASP A O   1 
ATOM   6307 C  CB  . ASP A 1 781  ? 33.522 84.669  -14.567 1.00 12.21 ? 781  ASP A CB  1 
ATOM   6308 C  CG  . ASP A 1 781  ? 33.610 85.716  -13.475 1.00 13.08 ? 781  ASP A CG  1 
ATOM   6309 O  OD1 . ASP A 1 781  ? 33.116 85.498  -12.341 1.00 13.84 ? 781  ASP A OD1 1 
ATOM   6310 O  OD2 . ASP A 1 781  ? 34.192 86.813  -13.680 1.00 19.89 ? 781  ASP A OD2 1 
ATOM   6311 N  N   . ILE A 1 782  ? 30.875 83.046  -12.732 1.00 11.56 ? 782  ILE A N   1 
ATOM   6312 C  CA  . ILE A 1 782  ? 29.473 83.175  -12.338 1.00 13.35 ? 782  ILE A CA  1 
ATOM   6313 C  C   . ILE A 1 782  ? 29.201 84.511  -11.662 1.00 14.82 ? 782  ILE A C   1 
ATOM   6314 O  O   . ILE A 1 782  ? 28.040 84.867  -11.429 1.00 16.10 ? 782  ILE A O   1 
ATOM   6315 C  CB  . ILE A 1 782  ? 29.108 81.973  -11.425 1.00 13.48 ? 782  ILE A CB  1 
ATOM   6316 C  CG1 . ILE A 1 782  ? 27.605 81.828  -11.196 1.00 14.61 ? 782  ILE A CG1 1 
ATOM   6317 C  CG2 . ILE A 1 782  ? 29.820 82.077  -10.082 1.00 14.19 ? 782  ILE A CG2 1 
ATOM   6318 C  CD1 . ILE A 1 782  ? 27.275 80.430  -10.745 1.00 16.23 ? 782  ILE A CD1 1 
ATOM   6319 N  N   . GLY A 1 783  ? 30.260 85.259  -11.355 1.00 15.37 ? 783  GLY A N   1 
ATOM   6320 C  CA  . GLY A 1 783  ? 30.120 86.657  -10.938 1.00 17.15 ? 783  GLY A CA  1 
ATOM   6321 C  C   . GLY A 1 783  ? 29.284 86.741  -9.683  1.00 17.99 ? 783  GLY A C   1 
ATOM   6322 O  O   . GLY A 1 783  ? 29.510 85.989  -8.740  1.00 19.52 ? 783  GLY A O   1 
ATOM   6323 N  N   . SER A 1 784  ? 28.285 87.616  -9.685  1.00 20.09 ? 784  SER A N   1 
ATOM   6324 C  CA  . SER A 1 784  ? 27.464 87.782  -8.489  1.00 20.97 ? 784  SER A CA  1 
ATOM   6325 C  C   . SER A 1 784  ? 26.073 87.164  -8.644  1.00 20.76 ? 784  SER A C   1 
ATOM   6326 O  O   . SER A 1 784  ? 25.126 87.577  -7.954  1.00 21.63 ? 784  SER A O   1 
ATOM   6327 C  CB  . SER A 1 784  ? 27.352 89.258  -8.113  1.00 22.13 ? 784  SER A CB  1 
ATOM   6328 O  OG  . SER A 1 784  ? 26.807 90.002  -9.191  1.00 26.30 ? 784  SER A OG  1 
ATOM   6329 N  N   . LEU A 1 785  ? 25.940 86.175  -9.534  1.00 19.93 ? 785  LEU A N   1 
ATOM   6330 C  CA  . LEU A 1 785  ? 24.646 85.511  -9.717  1.00 19.78 ? 785  LEU A CA  1 
ATOM   6331 C  C   . LEU A 1 785  ? 24.302 84.562  -8.573  1.00 20.40 ? 785  LEU A C   1 
ATOM   6332 O  O   . LEU A 1 785  ? 24.561 83.345  -8.637  1.00 21.36 ? 785  LEU A O   1 
ATOM   6333 C  CB  . LEU A 1 785  ? 24.597 84.736  -11.029 1.00 19.61 ? 785  LEU A CB  1 
ATOM   6334 C  CG  . LEU A 1 785  ? 24.827 85.446  -12.365 1.00 20.14 ? 785  LEU A CG  1 
ATOM   6335 C  CD1 . LEU A 1 785  ? 24.800 84.428  -13.497 1.00 23.34 ? 785  LEU A CD1 1 
ATOM   6336 C  CD2 . LEU A 1 785  ? 23.824 86.567  -12.612 1.00 23.41 ? 785  LEU A CD2 1 
ATOM   6337 N  N   . ASP A 1 786  ? 23.639 85.080  -7.547  1.00 20.24 ? 786  ASP A N   1 
ATOM   6338 C  CA  . ASP A 1 786  ? 23.337 84.246  -6.396  1.00 19.65 ? 786  ASP A CA  1 
ATOM   6339 C  C   . ASP A 1 786  ? 22.271 83.204  -6.735  1.00 16.82 ? 786  ASP A C   1 
ATOM   6340 O  O   . ASP A 1 786  ? 21.424 83.394  -7.611  1.00 17.66 ? 786  ASP A O   1 
ATOM   6341 C  CB  . ASP A 1 786  ? 22.904 85.057  -5.173  1.00 21.02 ? 786  ASP A CB  1 
ATOM   6342 C  CG  . ASP A 1 786  ? 23.843 86.189  -4.872  1.00 25.60 ? 786  ASP A CG  1 
ATOM   6343 O  OD1 . ASP A 1 786  ? 25.086 85.972  -4.773  1.00 25.15 ? 786  ASP A OD1 1 
ATOM   6344 O  OD2 . ASP A 1 786  ? 23.414 87.357  -4.751  1.00 32.10 ? 786  ASP A OD2 1 
ATOM   6345 N  N   . ASN A 1 787  ? 22.383 82.085  -6.040  1.00 15.49 ? 787  ASN A N   1 
ATOM   6346 C  CA  . ASN A 1 787  ? 21.424 80.989  -6.133  1.00 14.09 ? 787  ASN A CA  1 
ATOM   6347 C  C   . ASN A 1 787  ? 21.247 80.529  -7.559  1.00 13.73 ? 787  ASN A C   1 
ATOM   6348 O  O   . ASN A 1 787  ? 20.143 80.356  -8.052  1.00 14.18 ? 787  ASN A O   1 
ATOM   6349 C  CB  . ASN A 1 787  ? 20.112 81.356  -5.422  1.00 14.76 ? 787  ASN A CB  1 
ATOM   6350 C  CG  . ASN A 1 787  ? 20.337 81.580  -3.969  1.00 19.48 ? 787  ASN A CG  1 
ATOM   6351 O  OD1 . ASN A 1 787  ? 21.042 80.793  -3.325  1.00 18.68 ? 787  ASN A OD1 1 
ATOM   6352 N  ND2 . ASN A 1 787  ? 19.785 82.674  -3.431  1.00 25.64 ? 787  ASN A ND2 1 
ATOM   6353 N  N   . THR A 1 788  ? 22.387 80.325  -8.218  1.00 11.88 ? 788  THR A N   1 
ATOM   6354 C  CA  . THR A 1 788  ? 22.431 79.915  -9.610  1.00 12.39 ? 788  THR A CA  1 
ATOM   6355 C  C   . THR A 1 788  ? 23.448 78.784  -9.804  1.00 10.77 ? 788  THR A C   1 
ATOM   6356 O  O   . THR A 1 788  ? 24.533 78.851  -9.240  1.00 11.12 ? 788  THR A O   1 
ATOM   6357 C  CB  . THR A 1 788  ? 22.863 81.108  -10.477 1.00 13.33 ? 788  THR A CB  1 
ATOM   6358 O  OG1 . THR A 1 788  ? 21.873 82.158  -10.363 1.00 15.69 ? 788  THR A OG1 1 
ATOM   6359 C  CG2 . THR A 1 788  ? 22.834 80.741  -11.949 1.00 15.53 ? 788  THR A CG2 1 
ATOM   6360 N  N   . GLU A 1 789  ? 23.064 77.781  -10.579 1.00 9.41  ? 789  GLU A N   1 
ATOM   6361 C  CA  . GLU A 1 789  ? 24.022 76.762  -11.023 1.00 9.83  ? 789  GLU A CA  1 
ATOM   6362 C  C   . GLU A 1 789  ? 24.000 76.783  -12.531 1.00 10.24 ? 789  GLU A C   1 
ATOM   6363 O  O   . GLU A 1 789  ? 22.916 76.664  -13.134 1.00 11.12 ? 789  GLU A O   1 
ATOM   6364 C  CB  . GLU A 1 789  ? 23.682 75.358  -10.463 1.00 10.48 ? 789  GLU A CB  1 
ATOM   6365 C  CG  . GLU A 1 789  ? 23.234 75.391  -9.015  1.00 11.00 ? 789  GLU A CG  1 
ATOM   6366 C  CD  . GLU A 1 789  ? 23.448 74.099  -8.234  1.00 10.16 ? 789  GLU A CD  1 
ATOM   6367 O  OE1 . GLU A 1 789  ? 24.275 73.267  -8.707  1.00 11.04 ? 789  GLU A OE1 1 
ATOM   6368 O  OE2 . GLU A 1 789  ? 22.832 73.963  -7.168  1.00 10.24 ? 789  GLU A OE2 1 
ATOM   6369 N  N   . ILE A 1 790  ? 25.156 76.948  -13.174 1.00 9.13  ? 790  ILE A N   1 
ATOM   6370 C  CA  . ILE A 1 790  ? 25.258 76.992  -14.616 1.00 10.93 ? 790  ILE A CA  1 
ATOM   6371 C  C   . ILE A 1 790  ? 25.622 75.612  -15.140 1.00 9.31  ? 790  ILE A C   1 
ATOM   6372 O  O   . ILE A 1 790  ? 26.620 75.028  -14.686 1.00 9.76  ? 790  ILE A O   1 
ATOM   6373 C  CB  . ILE A 1 790  ? 26.358 78.007  -15.053 1.00 10.61 ? 790  ILE A CB  1 
ATOM   6374 C  CG1 . ILE A 1 790  ? 26.029 79.445  -14.601 1.00 14.53 ? 790  ILE A CG1 1 
ATOM   6375 C  CG2 . ILE A 1 790  ? 26.566 77.946  -16.568 1.00 11.96 ? 790  ILE A CG2 1 
ATOM   6376 C  CD1 . ILE A 1 790  ? 27.234 80.399  -14.707 1.00 17.17 ? 790  ILE A CD1 1 
ATOM   6377 N  N   . VAL A 1 791  ? 24.860 75.114  -16.099 1.00 9.20  ? 791  VAL A N   1 
ATOM   6378 C  CA  . VAL A 1 791  ? 25.044 73.795  -16.673 1.00 9.01  ? 791  VAL A CA  1 
ATOM   6379 C  C   . VAL A 1 791  ? 25.322 73.904  -18.163 1.00 8.96  ? 791  VAL A C   1 
ATOM   6380 O  O   . VAL A 1 791  ? 24.730 74.742  -18.842 1.00 9.22  ? 791  VAL A O   1 
ATOM   6381 C  CB  . VAL A 1 791  ? 23.821 72.870  -16.373 1.00 9.53  ? 791  VAL A CB  1 
ATOM   6382 C  CG1 . VAL A 1 791  ? 22.550 73.344  -17.095 1.00 12.62 ? 791  VAL A CG1 1 
ATOM   6383 C  CG2 . VAL A 1 791  ? 24.147 71.411  -16.711 1.00 11.68 ? 791  VAL A CG2 1 
ATOM   6384 N  N   . MET A 1 792  ? 26.220 73.070  -18.657 1.00 8.52  ? 792  MET A N   1 
ATOM   6385 C  CA  . MET A 1 792  ? 26.467 72.944  -20.080 1.00 8.72  ? 792  MET A CA  1 
ATOM   6386 C  C   . MET A 1 792  ? 25.802 71.658  -20.544 1.00 8.68  ? 792  MET A C   1 
ATOM   6387 O  O   . MET A 1 792  ? 26.139 70.572  -20.043 1.00 9.42  ? 792  MET A O   1 
ATOM   6388 C  CB  . MET A 1 792  ? 27.973 72.898  -20.423 1.00 9.13  ? 792  MET A CB  1 
ATOM   6389 C  CG  . MET A 1 792  ? 28.263 72.739  -21.898 1.00 11.19 ? 792  MET A CG  1 
ATOM   6390 S  SD  . MET A 1 792  ? 30.025 72.836  -22.255 1.00 10.80 ? 792  MET A SD  1 
ATOM   6391 C  CE  . MET A 1 792  ? 30.610 71.327  -21.477 1.00 13.02 ? 792  MET A CE  1 
ATOM   6392 N  N   . ARG A 1 793  ? 24.875 71.751  -21.491 1.00 8.81  ? 793  ARG A N   1 
ATOM   6393 C  CA  . ARG A 1 793  ? 24.160 70.587  -21.994 1.00 9.08  ? 793  ARG A CA  1 
ATOM   6394 C  C   . ARG A 1 793  ? 24.485 70.374  -23.447 1.00 9.49  ? 793  ARG A C   1 
ATOM   6395 O  O   . ARG A 1 793  ? 24.650 71.337  -24.228 1.00 10.14 ? 793  ARG A O   1 
ATOM   6396 C  CB  . ARG A 1 793  ? 22.663 70.806  -21.811 1.00 9.79  ? 793  ARG A CB  1 
ATOM   6397 C  CG  . ARG A 1 793  ? 21.805 69.604  -22.254 1.00 10.13 ? 793  ARG A CG  1 
ATOM   6398 C  CD  . ARG A 1 793  ? 20.305 69.792  -21.957 1.00 10.84 ? 793  ARG A CD  1 
ATOM   6399 N  NE  . ARG A 1 793  ? 20.068 69.873  -20.522 1.00 11.72 ? 793  ARG A NE  1 
ATOM   6400 C  CZ  . ARG A 1 793  ? 18.999 70.436  -19.951 1.00 12.01 ? 793  ARG A CZ  1 
ATOM   6401 N  NH1 . ARG A 1 793  ? 18.030 70.984  -20.723 1.00 12.08 ? 793  ARG A NH1 1 
ATOM   6402 N  NH2 . ARG A 1 793  ? 18.887 70.521  -18.649 1.00 11.70 ? 793  ARG A NH2 1 
ATOM   6403 N  N   . LEU A 1 794  ? 24.577 69.111  -23.829 1.00 9.71  ? 794  LEU A N   1 
ATOM   6404 C  CA  . LEU A 1 794  ? 24.648 68.645  -25.215 1.00 10.41 ? 794  LEU A CA  1 
ATOM   6405 C  C   . LEU A 1 794  ? 23.345 67.947  -25.595 1.00 11.26 ? 794  LEU A C   1 
ATOM   6406 O  O   . LEU A 1 794  ? 22.883 67.071  -24.866 1.00 11.13 ? 794  LEU A O   1 
ATOM   6407 C  CB  . LEU A 1 794  ? 25.787 67.659  -25.397 1.00 11.20 ? 794  LEU A CB  1 
ATOM   6408 C  CG  . LEU A 1 794  ? 27.146 68.309  -25.498 1.00 11.65 ? 794  LEU A CG  1 
ATOM   6409 C  CD1 . LEU A 1 794  ? 28.262 67.322  -25.109 1.00 14.16 ? 794  LEU A CD1 1 
ATOM   6410 C  CD2 . LEU A 1 794  ? 27.342 68.741  -26.941 1.00 16.73 ? 794  LEU A CD2 1 
ATOM   6411 N  N   . GLU A 1 795  ? 22.726 68.361  -26.708 1.00 11.43 ? 795  GLU A N   1 
ATOM   6412 C  CA  . GLU A 1 795  ? 21.473 67.742  -27.195 1.00 13.49 ? 795  GLU A CA  1 
ATOM   6413 C  C   . GLU A 1 795  ? 21.779 67.050  -28.493 1.00 13.44 ? 795  GLU A C   1 
ATOM   6414 O  O   . GLU A 1 795  ? 22.326 67.641  -29.406 1.00 13.99 ? 795  GLU A O   1 
ATOM   6415 C  CB  . GLU A 1 795  ? 20.373 68.803  -27.402 1.00 14.40 ? 795  GLU A CB  1 
ATOM   6416 C  CG  . GLU A 1 795  ? 20.014 69.573  -26.141 1.00 17.34 ? 795  GLU A CG  1 
ATOM   6417 C  CD  . GLU A 1 795  ? 19.112 70.792  -26.375 1.00 18.12 ? 795  GLU A CD  1 
ATOM   6418 O  OE1 . GLU A 1 795  ? 19.135 71.358  -27.490 1.00 24.11 ? 795  GLU A OE1 1 
ATOM   6419 O  OE2 . GLU A 1 795  ? 18.413 71.224  -25.428 1.00 22.57 ? 795  GLU A OE2 1 
ATOM   6420 N  N   . THR A 1 796  ? 21.433 65.764  -28.591 1.00 12.34 ? 796  THR A N   1 
ATOM   6421 C  CA  . THR A 1 796  ? 21.646 64.991  -29.789 1.00 13.05 ? 796  THR A CA  1 
ATOM   6422 C  C   . THR A 1 796  ? 20.395 64.163  -30.131 1.00 12.52 ? 796  THR A C   1 
ATOM   6423 O  O   . THR A 1 796  ? 19.443 64.168  -29.368 1.00 15.14 ? 796  THR A O   1 
ATOM   6424 C  CB  . THR A 1 796  ? 22.837 64.001  -29.667 1.00 12.54 ? 796  THR A CB  1 
ATOM   6425 O  OG1 . THR A 1 796  ? 22.435 62.841  -28.896 1.00 11.72 ? 796  THR A OG1 1 
ATOM   6426 C  CG2 . THR A 1 796  ? 24.039 64.607  -28.913 1.00 13.87 ? 796  THR A CG2 1 
ATOM   6427 N  N   A HIS A 1 797  ? 20.532 63.427  -31.225 0.50 13.19 ? 797  HIS A N   1 
ATOM   6428 N  N   B HIS A 1 797  ? 20.419 63.452  -31.247 0.50 13.53 ? 797  HIS A N   1 
ATOM   6429 C  CA  A HIS A 1 797  ? 19.499 62.502  -31.671 0.50 13.53 ? 797  HIS A CA  1 
ATOM   6430 C  CA  B HIS A 1 797  ? 19.321 62.494  -31.512 0.50 13.66 ? 797  HIS A CA  1 
ATOM   6431 C  C   A HIS A 1 797  ? 19.619 61.117  -31.120 0.50 13.59 ? 797  HIS A C   1 
ATOM   6432 C  C   B HIS A 1 797  ? 19.857 61.023  -31.432 0.50 13.80 ? 797  HIS A C   1 
ATOM   6433 O  O   A HIS A 1 797  ? 18.661 60.338  -31.278 0.50 12.14 ? 797  HIS A O   1 
ATOM   6434 O  O   B HIS A 1 797  ? 19.426 60.083  -32.129 0.50 12.66 ? 797  HIS A O   1 
ATOM   6435 C  CB  A HIS A 1 797  ? 19.420 62.475  -33.196 0.50 13.54 ? 797  HIS A CB  1 
ATOM   6436 C  CB  B HIS A 1 797  ? 18.542 62.822  -32.821 0.50 13.10 ? 797  HIS A CB  1 
ATOM   6437 C  CG  A HIS A 1 797  ? 18.727 63.675  -33.749 0.50 11.55 ? 797  HIS A CG  1 
ATOM   6438 C  CG  B HIS A 1 797  ? 18.059 64.245  -32.956 0.50 14.43 ? 797  HIS A CG  1 
ATOM   6439 N  ND1 A HIS A 1 797  ? 17.990 64.531  -32.951 0.50 13.25 ? 797  HIS A ND1 1 
ATOM   6440 N  ND1 B HIS A 1 797  ? 17.728 65.045  -31.884 0.50 14.36 ? 797  HIS A ND1 1 
ATOM   6441 C  CD2 A HIS A 1 797  ? 18.666 64.177  -35.004 0.50 10.86 ? 797  HIS A CD2 1 
ATOM   6442 C  CD2 B HIS A 1 797  ? 17.818 64.994  -34.067 0.50 11.17 ? 797  HIS A CD2 1 
ATOM   6443 C  CE1 A HIS A 1 797  ? 17.494 65.497  -33.705 0.50 10.14 ? 797  HIS A CE1 1 
ATOM   6444 C  CE1 B HIS A 1 797  ? 17.331 66.230  -32.322 0.50 15.42 ? 797  HIS A CE1 1 
ATOM   6445 N  NE2 A HIS A 1 797  ? 17.903 65.315  -34.944 0.50 13.61 ? 797  HIS A NE2 1 
ATOM   6446 N  NE2 B HIS A 1 797  ? 17.374 66.222  -33.641 0.50 16.38 ? 797  HIS A NE2 1 
ATOM   6447 N  N   . ILE A 1 798  ? 20.789 60.826  -30.502 1.00 13.32 ? 798  ILE A N   1 
ATOM   6448 C  CA  . ILE A 1 798  ? 21.212 59.479  -30.121 1.00 13.04 ? 798  ILE A CA  1 
ATOM   6449 C  C   . ILE A 1 798  ? 20.115 58.888  -29.269 1.00 12.79 ? 798  ILE A C   1 
ATOM   6450 O  O   . ILE A 1 798  ? 19.606 59.506  -28.362 1.00 13.03 ? 798  ILE A O   1 
ATOM   6451 C  CB  . ILE A 1 798  ? 22.546 59.531  -29.368 1.00 12.02 ? 798  ILE A CB  1 
ATOM   6452 C  CG1 . ILE A 1 798  ? 23.639 59.991  -30.307 1.00 13.46 ? 798  ILE A CG1 1 
ATOM   6453 C  CG2 . ILE A 1 798  ? 22.889 58.120  -28.778 1.00 14.16 ? 798  ILE A CG2 1 
ATOM   6454 C  CD1 . ILE A 1 798  ? 24.964 60.330  -29.570 1.00 13.29 ? 798  ILE A CD1 1 
ATOM   6455 N  N   . ASP A 1 799  ? 19.715 57.665  -29.649 1.00 14.27 ? 799  ASP A N   1 
ATOM   6456 C  CA  . ASP A 1 799  ? 18.606 56.995  -28.998 1.00 13.94 ? 799  ASP A CA  1 
ATOM   6457 C  C   . ASP A 1 799  ? 19.036 56.242  -27.730 1.00 13.37 ? 799  ASP A C   1 
ATOM   6458 O  O   . ASP A 1 799  ? 19.001 55.011  -27.670 1.00 12.50 ? 799  ASP A O   1 
ATOM   6459 C  CB  . ASP A 1 799  ? 17.921 56.039  -30.012 1.00 16.02 ? 799  ASP A CB  1 
ATOM   6460 C  CG  . ASP A 1 799  ? 16.607 55.504  -29.512 1.00 18.51 ? 799  ASP A CG  1 
ATOM   6461 O  OD1 . ASP A 1 799  ? 15.990 56.105  -28.635 1.00 23.52 ? 799  ASP A OD1 1 
ATOM   6462 O  OD2 . ASP A 1 799  ? 16.113 54.451  -29.938 1.00 24.54 ? 799  ASP A OD2 1 
ATOM   6463 N  N   . SER A 1 800  ? 19.497 57.002  -26.735 1.00 12.90 ? 800  SER A N   1 
ATOM   6464 C  CA  . SER A 1 800  ? 20.077 56.426  -25.520 1.00 12.13 ? 800  SER A CA  1 
ATOM   6465 C  C   . SER A 1 800  ? 19.016 56.027  -24.516 1.00 11.83 ? 800  SER A C   1 
ATOM   6466 O  O   . SER A 1 800  ? 19.293 55.240  -23.594 1.00 12.01 ? 800  SER A O   1 
ATOM   6467 C  CB  . SER A 1 800  ? 21.078 57.429  -24.895 1.00 11.40 ? 800  SER A CB  1 
ATOM   6468 O  OG  . SER A 1 800  ? 20.438 58.646  -24.561 1.00 11.59 ? 800  SER A OG  1 
ATOM   6469 N  N   . GLY A 1 801  ? 17.792 56.552  -24.629 1.00 12.02 ? 801  GLY A N   1 
ATOM   6470 C  CA  . GLY A 1 801  ? 16.748 56.178  -23.712 1.00 13.03 ? 801  GLY A CA  1 
ATOM   6471 C  C   . GLY A 1 801  ? 17.018 56.705  -22.340 1.00 13.13 ? 801  GLY A C   1 
ATOM   6472 O  O   . GLY A 1 801  ? 17.067 57.924  -22.169 1.00 14.08 ? 801  GLY A O   1 
ATOM   6473 N  N   . ASP A 1 802  ? 17.126 55.804  -21.367 1.00 12.24 ? 802  ASP A N   1 
ATOM   6474 C  CA  . ASP A 1 802  ? 17.413 56.197  -19.996 1.00 12.57 ? 802  ASP A CA  1 
ATOM   6475 C  C   . ASP A 1 802  ? 18.813 55.767  -19.540 1.00 11.65 ? 802  ASP A C   1 
ATOM   6476 O  O   . ASP A 1 802  ? 19.091 55.841  -18.335 1.00 11.92 ? 802  ASP A O   1 
ATOM   6477 C  CB  . ASP A 1 802  ? 16.336 55.662  -19.034 1.00 13.45 ? 802  ASP A CB  1 
ATOM   6478 C  CG  . ASP A 1 802  ? 16.147 54.162  -19.127 1.00 14.74 ? 802  ASP A CG  1 
ATOM   6479 O  OD1 . ASP A 1 802  ? 16.942 53.466  -19.776 1.00 16.61 ? 802  ASP A OD1 1 
ATOM   6480 O  OD2 . ASP A 1 802  ? 15.191 53.613  -18.523 1.00 18.02 ? 802  ASP A OD2 1 
ATOM   6481 N  N   . ILE A 1 803  ? 19.658 55.368  -20.476 1.00 9.89  ? 803  ILE A N   1 
ATOM   6482 C  CA  . ILE A 1 803  ? 20.996 54.875  -20.134 1.00 9.72  ? 803  ILE A CA  1 
ATOM   6483 C  C   . ILE A 1 803  ? 22.054 55.911  -20.452 1.00 9.46  ? 803  ILE A C   1 
ATOM   6484 O  O   . ILE A 1 803  ? 22.025 56.579  -21.494 1.00 8.96  ? 803  ILE A O   1 
ATOM   6485 C  CB  . ILE A 1 803  ? 21.265 53.567  -20.897 1.00 9.92  ? 803  ILE A CB  1 
ATOM   6486 C  CG1 . ILE A 1 803  ? 20.228 52.479  -20.506 1.00 11.80 ? 803  ILE A CG1 1 
ATOM   6487 C  CG2 . ILE A 1 803  ? 22.712 53.059  -20.682 1.00 10.71 ? 803  ILE A CG2 1 
ATOM   6488 C  CD1 . ILE A 1 803  ? 20.198 52.153  -19.031 1.00 15.20 ? 803  ILE A CD1 1 
ATOM   6489 N  N   . PHE A 1 804  ? 23.037 55.997  -19.547 1.00 8.78  ? 804  PHE A N   1 
ATOM   6490 C  CA  . PHE A 1 804  ? 24.247 56.793  -19.793 1.00 8.42  ? 804  PHE A CA  1 
ATOM   6491 C  C   . PHE A 1 804  ? 25.375 56.182  -18.975 1.00 8.06  ? 804  PHE A C   1 
ATOM   6492 O  O   . PHE A 1 804  ? 25.118 55.302  -18.150 1.00 9.51  ? 804  PHE A O   1 
ATOM   6493 C  CB  . PHE A 1 804  ? 24.017 58.290  -19.495 1.00 7.83  ? 804  PHE A CB  1 
ATOM   6494 C  CG  . PHE A 1 804  ? 23.601 58.619  -18.079 1.00 7.39  ? 804  PHE A CG  1 
ATOM   6495 C  CD1 . PHE A 1 804  ? 22.325 58.418  -17.608 1.00 8.21  ? 804  PHE A CD1 1 
ATOM   6496 C  CD2 . PHE A 1 804  ? 24.527 59.249  -17.219 1.00 7.75  ? 804  PHE A CD2 1 
ATOM   6497 C  CE1 . PHE A 1 804  ? 21.957 58.771  -16.356 1.00 8.68  ? 804  PHE A CE1 1 
ATOM   6498 C  CE2 . PHE A 1 804  ? 24.175 59.625  -15.991 1.00 8.30  ? 804  PHE A CE2 1 
ATOM   6499 C  CZ  . PHE A 1 804  ? 22.900 59.397  -15.507 1.00 8.66  ? 804  PHE A CZ  1 
ATOM   6500 N  N   . TYR A 1 805  ? 26.593 56.599  -19.251 1.00 7.72  ? 805  TYR A N   1 
ATOM   6501 C  CA  . TYR A 1 805  ? 27.755 56.033  -18.565 1.00 7.51  ? 805  TYR A CA  1 
ATOM   6502 C  C   . TYR A 1 805  ? 28.578 57.169  -18.000 1.00 8.03  ? 805  TYR A C   1 
ATOM   6503 O  O   . TYR A 1 805  ? 28.754 58.206  -18.657 1.00 8.31  ? 805  TYR A O   1 
ATOM   6504 C  CB  . TYR A 1 805  ? 28.619 55.273  -19.542 1.00 8.33  ? 805  TYR A CB  1 
ATOM   6505 C  CG  . TYR A 1 805  ? 27.924 54.042  -20.086 1.00 8.28  ? 805  TYR A CG  1 
ATOM   6506 C  CD1 . TYR A 1 805  ? 26.959 54.146  -21.107 1.00 10.11 ? 805  TYR A CD1 1 
ATOM   6507 C  CD2 . TYR A 1 805  ? 28.226 52.788  -19.597 1.00 9.90  ? 805  TYR A CD2 1 
ATOM   6508 C  CE1 . TYR A 1 805  ? 26.307 52.998  -21.591 1.00 10.87 ? 805  TYR A CE1 1 
ATOM   6509 C  CE2 . TYR A 1 805  ? 27.572 51.621  -20.095 1.00 10.10 ? 805  TYR A CE2 1 
ATOM   6510 C  CZ  . TYR A 1 805  ? 26.600 51.777  -21.072 1.00 10.82 ? 805  TYR A CZ  1 
ATOM   6511 O  OH  . TYR A 1 805  ? 25.944 50.686  -21.611 1.00 11.96 ? 805  TYR A OH  1 
ATOM   6512 N  N   . THR A 1 806  ? 29.075 56.968  -16.777 1.00 7.73  ? 806  THR A N   1 
ATOM   6513 C  CA  . THR A 1 806  ? 29.966 57.963  -16.143 1.00 6.70  ? 806  THR A CA  1 
ATOM   6514 C  C   . THR A 1 806  ? 31.130 57.200  -15.556 1.00 8.10  ? 806  THR A C   1 
ATOM   6515 O  O   . THR A 1 806  ? 31.052 55.993  -15.301 1.00 8.83  ? 806  THR A O   1 
ATOM   6516 C  CB  . THR A 1 806  ? 29.250 58.754  -15.064 1.00 7.70  ? 806  THR A CB  1 
ATOM   6517 O  OG1 . THR A 1 806  ? 28.839 57.870  -14.020 1.00 8.03  ? 806  THR A OG1 1 
ATOM   6518 C  CG2 . THR A 1 806  ? 27.966 59.447  -15.588 1.00 8.12  ? 806  THR A CG2 1 
ATOM   6519 N  N   . ASP A 1 807  ? 32.242 57.870  -15.348 1.00 6.67  ? 807  ASP A N   1 
ATOM   6520 C  CA  . ASP A 1 807  ? 33.380 57.164  -14.749 1.00 8.06  ? 807  ASP A CA  1 
ATOM   6521 C  C   . ASP A 1 807  ? 33.424 57.244  -13.248 1.00 6.86  ? 807  ASP A C   1 
ATOM   6522 O  O   . ASP A 1 807  ? 32.773 58.055  -12.605 1.00 7.05  ? 807  ASP A O   1 
ATOM   6523 C  CB  . ASP A 1 807  ? 34.681 57.575  -15.383 1.00 9.56  ? 807  ASP A CB  1 
ATOM   6524 C  CG  . ASP A 1 807  ? 35.146 58.873  -14.925 1.00 9.72  ? 807  ASP A CG  1 
ATOM   6525 O  OD1 . ASP A 1 807  ? 34.409 59.897  -15.002 1.00 11.16 ? 807  ASP A OD1 1 
ATOM   6526 O  OD2 . ASP A 1 807  ? 36.316 58.986  -14.422 1.00 11.58 ? 807  ASP A OD2 1 
ATOM   6527 N  N   . LEU A 1 808  ? 34.186 56.310  -12.699 1.00 6.71  ? 808  LEU A N   1 
ATOM   6528 C  CA  . LEU A 1 808  ? 34.489 56.268  -11.276 1.00 6.51  ? 808  LEU A CA  1 
ATOM   6529 C  C   . LEU A 1 808  ? 35.980 56.484  -11.113 1.00 5.70  ? 808  LEU A C   1 
ATOM   6530 O  O   . LEU A 1 808  ? 36.780 55.686  -11.581 1.00 6.21  ? 808  LEU A O   1 
ATOM   6531 C  CB  . LEU A 1 808  ? 34.074 54.954  -10.657 1.00 7.15  ? 808  LEU A CB  1 
ATOM   6532 C  CG  . LEU A 1 808  ? 32.547 54.808  -10.550 1.00 8.20  ? 808  LEU A CG  1 
ATOM   6533 C  CD1 . LEU A 1 808  ? 32.183 53.351  -10.341 1.00 10.22 ? 808  LEU A CD1 1 
ATOM   6534 C  CD2 . LEU A 1 808  ? 31.949 55.653  -9.449  1.00 10.37 ? 808  LEU A CD2 1 
ATOM   6535 N  N   . ASN A 1 809  ? 36.333 57.657  -10.581 1.00 5.76  ? 809  ASN A N   1 
ATOM   6536 C  CA  . ASN A 1 809  ? 37.721 57.977  -10.227 1.00 5.98  ? 809  ASN A CA  1 
ATOM   6537 C  C   . ASN A 1 809  ? 38.691 57.882  -11.381 1.00 6.26  ? 809  ASN A C   1 
ATOM   6538 O  O   . ASN A 1 809  ? 39.892 57.639  -11.192 1.00 6.49  ? 809  ASN A O   1 
ATOM   6539 C  CB  . ASN A 1 809  ? 38.228 57.078  -9.069  1.00 5.51  ? 809  ASN A CB  1 
ATOM   6540 C  CG  . ASN A 1 809  ? 37.209 56.996  -7.962  1.00 6.21  ? 809  ASN A CG  1 
ATOM   6541 O  OD1 . ASN A 1 809  ? 36.331 56.112  -7.988  1.00 6.72  ? 809  ASN A OD1 1 
ATOM   6542 N  ND2 . ASN A 1 809  ? 37.212 57.967  -7.050  1.00 7.21  ? 809  ASN A ND2 1 
ATOM   6543 N  N   . GLY A 1 810  ? 38.211 58.084  -12.618 1.00 5.75  ? 810  GLY A N   1 
ATOM   6544 C  CA  . GLY A 1 810  ? 39.125 57.989  -13.760 1.00 7.78  ? 810  GLY A CA  1 
ATOM   6545 C  C   . GLY A 1 810  ? 39.606 56.580  -14.056 1.00 8.54  ? 810  GLY A C   1 
ATOM   6546 O  O   . GLY A 1 810  ? 40.554 56.421  -14.851 1.00 9.42  ? 810  GLY A O   1 
ATOM   6547 N  N   . LEU A 1 811  ? 38.988 55.584  -13.430 1.00 7.21  ? 811  LEU A N   1 
ATOM   6548 C  CA  . LEU A 1 811  ? 39.444 54.211  -13.501 1.00 8.84  ? 811  LEU A CA  1 
ATOM   6549 C  C   . LEU A 1 811  ? 38.543 53.312  -14.368 1.00 9.41  ? 811  LEU A C   1 
ATOM   6550 O  O   . LEU A 1 811  ? 39.047 52.405  -15.024 1.00 10.95 ? 811  LEU A O   1 
ATOM   6551 C  CB  . LEU A 1 811  ? 39.507 53.643  -12.078 1.00 8.67  ? 811  LEU A CB  1 
ATOM   6552 C  CG  . LEU A 1 811  ? 39.936 52.186  -11.917 1.00 10.02 ? 811  LEU A CG  1 
ATOM   6553 C  CD1 . LEU A 1 811  ? 41.358 51.991  -12.421 1.00 12.24 ? 811  LEU A CD1 1 
ATOM   6554 C  CD2 . LEU A 1 811  ? 39.801 51.673  -10.458 1.00 10.58 ? 811  LEU A CD2 1 
ATOM   6555 N  N   . GLN A 1 812  ? 37.232 53.521  -14.323 1.00 7.54  ? 812  GLN A N   1 
ATOM   6556 C  CA  . GLN A 1 812  ? 36.269 52.600  -14.951 1.00 7.66  ? 812  GLN A CA  1 
ATOM   6557 C  C   . GLN A 1 812  ? 35.024 53.372  -15.268 1.00 8.01  ? 812  GLN A C   1 
ATOM   6558 O  O   . GLN A 1 812  ? 34.752 54.398  -14.650 1.00 8.85  ? 812  GLN A O   1 
ATOM   6559 C  CB  . GLN A 1 812  ? 35.917 51.466  -13.985 1.00 9.69  ? 812  GLN A CB  1 
ATOM   6560 C  CG  . GLN A 1 812  ? 35.362 51.968  -12.649 1.00 10.96 ? 812  GLN A CG  1 
ATOM   6561 C  CD  . GLN A 1 812  ? 35.082 50.847  -11.698 1.00 12.08 ? 812  GLN A CD  1 
ATOM   6562 O  OE1 . GLN A 1 812  ? 34.101 50.120  -11.859 1.00 12.50 ? 812  GLN A OE1 1 
ATOM   6563 N  NE2 . GLN A 1 812  ? 35.902 50.751  -10.656 1.00 13.98 ? 812  GLN A NE2 1 
ATOM   6564 N  N   . PHE A 1 813  ? 34.283 52.918  -16.277 1.00 7.93  ? 813  PHE A N   1 
ATOM   6565 C  CA  . PHE A 1 813  ? 32.982 53.493  -16.619 1.00 8.13  ? 813  PHE A CA  1 
ATOM   6566 C  C   . PHE A 1 813  ? 31.869 52.586  -16.179 1.00 8.07  ? 813  PHE A C   1 
ATOM   6567 O  O   . PHE A 1 813  ? 31.904 51.356  -16.450 1.00 9.86  ? 813  PHE A O   1 
ATOM   6568 C  CB  . PHE A 1 813  ? 32.909 53.793  -18.130 1.00 8.52  ? 813  PHE A CB  1 
ATOM   6569 C  CG  . PHE A 1 813  ? 33.674 55.031  -18.499 1.00 7.82  ? 813  PHE A CG  1 
ATOM   6570 C  CD1 . PHE A 1 813  ? 35.054 55.001  -18.573 1.00 8.38  ? 813  PHE A CD1 1 
ATOM   6571 C  CD2 . PHE A 1 813  ? 33.000 56.243  -18.733 1.00 8.74  ? 813  PHE A CD2 1 
ATOM   6572 C  CE1 . PHE A 1 813  ? 35.766 56.197  -18.847 1.00 10.79 ? 813  PHE A CE1 1 
ATOM   6573 C  CE2 . PHE A 1 813  ? 33.724 57.416  -19.015 1.00 10.56 ? 813  PHE A CE2 1 
ATOM   6574 C  CZ  . PHE A 1 813  ? 35.086 57.369  -19.074 1.00 10.99 ? 813  PHE A CZ  1 
ATOM   6575 N  N   . ILE A 1 814  ? 30.900 53.151  -15.512 1.00 7.42  ? 814  ILE A N   1 
ATOM   6576 C  CA  . ILE A 1 814  ? 29.813 52.387  -14.954 1.00 8.03  ? 814  ILE A CA  1 
ATOM   6577 C  C   . ILE A 1 814  ? 28.520 52.817  -15.639 1.00 7.65  ? 814  ILE A C   1 
ATOM   6578 O  O   . ILE A 1 814  ? 28.286 54.015  -15.897 1.00 7.71  ? 814  ILE A O   1 
ATOM   6579 C  CB  . ILE A 1 814  ? 29.747 52.577  -13.416 1.00 7.66  ? 814  ILE A CB  1 
ATOM   6580 C  CG1 . ILE A 1 814  ? 28.658 51.681  -12.775 1.00 8.35  ? 814  ILE A CG1 1 
ATOM   6581 C  CG2 . ILE A 1 814  ? 29.520 54.026  -13.001 1.00 8.62  ? 814  ILE A CG2 1 
ATOM   6582 C  CD1 . ILE A 1 814  ? 28.827 51.486  -11.260 1.00 9.37  ? 814  ILE A CD1 1 
ATOM   6583 N  N   . LYS A 1 815  ? 27.659 51.842  -15.942 1.00 7.51  ? 815  LYS A N   1 
ATOM   6584 C  CA  A LYS A 1 815  ? 26.354 52.110  -16.521 0.50 8.16  ? 815  LYS A CA  1 
ATOM   6585 C  CA  B LYS A 1 815  ? 26.345 52.116  -16.512 0.50 8.32  ? 815  LYS A CA  1 
ATOM   6586 C  C   . LYS A 1 815  ? 25.436 52.747  -15.489 1.00 7.80  ? 815  LYS A C   1 
ATOM   6587 O  O   . LYS A 1 815  ? 25.314 52.272  -14.354 1.00 8.33  ? 815  LYS A O   1 
ATOM   6588 C  CB  A LYS A 1 815  ? 25.774 50.785  -17.029 0.50 8.53  ? 815  LYS A CB  1 
ATOM   6589 C  CB  B LYS A 1 815  ? 25.707 50.818  -17.023 0.50 8.73  ? 815  LYS A CB  1 
ATOM   6590 C  CG  A LYS A 1 815  ? 24.635 50.900  -18.028 0.50 9.09  ? 815  LYS A CG  1 
ATOM   6591 C  CG  B LYS A 1 815  ? 24.305 51.015  -17.620 0.50 9.24  ? 815  LYS A CG  1 
ATOM   6592 C  CD  A LYS A 1 815  ? 24.158 49.500  -18.429 0.50 9.17  ? 815  LYS A CD  1 
ATOM   6593 C  CD  B LYS A 1 815  ? 23.656 49.709  -18.113 0.50 9.96  ? 815  LYS A CD  1 
ATOM   6594 C  CE  A LYS A 1 815  ? 23.003 49.546  -19.401 0.50 12.44 ? 815  LYS A CE  1 
ATOM   6595 C  CE  B LYS A 1 815  ? 24.553 48.954  -19.060 0.50 12.80 ? 815  LYS A CE  1 
ATOM   6596 N  NZ  A LYS A 1 815  ? 22.585 48.164  -19.802 0.50 14.13 ? 815  LYS A NZ  1 
ATOM   6597 N  NZ  B LYS A 1 815  ? 23.788 47.770  -19.598 0.50 17.24 ? 815  LYS A NZ  1 
ATOM   6598 N  N   . ARG A 1 816  ? 24.790 53.832  -15.888 1.00 7.90  ? 816  ARG A N   1 
ATOM   6599 C  CA  . ARG A 1 816  ? 23.775 54.525  -15.127 1.00 8.12  ? 816  ARG A CA  1 
ATOM   6600 C  C   . ARG A 1 816  ? 22.433 54.401  -15.828 1.00 8.47  ? 816  ARG A C   1 
ATOM   6601 O  O   . ARG A 1 816  ? 22.370 54.368  -17.059 1.00 8.56  ? 816  ARG A O   1 
ATOM   6602 C  CB  . ARG A 1 816  ? 24.077 56.047  -14.999 1.00 8.52  ? 816  ARG A CB  1 
ATOM   6603 C  CG  . ARG A 1 816  ? 25.471 56.418  -14.474 1.00 8.45  ? 816  ARG A CG  1 
ATOM   6604 C  CD  . ARG A 1 816  ? 25.721 55.799  -13.140 1.00 8.65  ? 816  ARG A CD  1 
ATOM   6605 N  NE  . ARG A 1 816  ? 26.922 56.373  -12.497 1.00 7.71  ? 816  ARG A NE  1 
ATOM   6606 C  CZ  . ARG A 1 816  ? 27.293 55.986  -11.278 1.00 8.60  ? 816  ARG A CZ  1 
ATOM   6607 N  NH1 . ARG A 1 816  ? 26.595 55.073  -10.625 1.00 7.71  ? 816  ARG A NH1 1 
ATOM   6608 N  NH2 . ARG A 1 816  ? 28.347 56.556  -10.699 1.00 8.25  ? 816  ARG A NH2 1 
ATOM   6609 N  N   . ARG A 1 817  ? 21.406 54.386  -14.997 1.00 8.31  ? 817  ARG A N   1 
ATOM   6610 C  CA  . ARG A 1 817  ? 20.055 54.434  -15.564 1.00 8.95  ? 817  ARG A CA  1 
ATOM   6611 C  C   . ARG A 1 817  ? 19.323 55.554  -14.899 1.00 9.01  ? 817  ARG A C   1 
ATOM   6612 O  O   . ARG A 1 817  ? 19.186 55.582  -13.678 1.00 9.72  ? 817  ARG A O   1 
ATOM   6613 C  CB  . ARG A 1 817  ? 19.313 53.100  -15.336 1.00 10.19 ? 817  ARG A CB  1 
ATOM   6614 C  CG  . ARG A 1 817  ? 17.859 53.092  -15.810 1.00 11.37 ? 817  ARG A CG  1 
ATOM   6615 C  CD  . ARG A 1 817  ? 17.138 51.723  -15.606 1.00 12.23 ? 817  ARG A CD  1 
ATOM   6616 N  NE  . ARG A 1 817  ? 17.716 50.691  -16.461 1.00 12.77 ? 817  ARG A NE  1 
ATOM   6617 C  CZ  . ARG A 1 817  ? 18.453 49.666  -16.051 1.00 14.18 ? 817  ARG A CZ  1 
ATOM   6618 N  NH1 . ARG A 1 817  ? 18.772 49.536  -14.760 1.00 14.30 ? 817  ARG A NH1 1 
ATOM   6619 N  NH2 . ARG A 1 817  ? 18.894 48.775  -16.943 1.00 17.78 ? 817  ARG A NH2 1 
ATOM   6620 N  N   . ARG A 1 818  ? 18.842 56.497  -15.703 1.00 9.78  ? 818  ARG A N   1 
ATOM   6621 C  CA  A ARG A 1 818  ? 18.019 57.589  -15.196 0.50 10.21 ? 818  ARG A CA  1 
ATOM   6622 C  CA  B ARG A 1 818  ? 18.018 57.588  -15.197 0.50 10.74 ? 818  ARG A CA  1 
ATOM   6623 C  C   . ARG A 1 818  ? 16.800 56.883  -14.609 1.00 10.42 ? 818  ARG A C   1 
ATOM   6624 O  O   . ARG A 1 818  ? 16.304 55.907  -15.171 1.00 12.40 ? 818  ARG A O   1 
ATOM   6625 C  CB  A ARG A 1 818  ? 17.724 58.597  -16.308 0.50 10.64 ? 818  ARG A CB  1 
ATOM   6626 C  CB  B ARG A 1 818  ? 17.590 58.511  -16.339 0.50 10.94 ? 818  ARG A CB  1 
ATOM   6627 C  CG  A ARG A 1 818  ? 16.994 59.845  -15.837 0.50 10.76 ? 818  ARG A CG  1 
ATOM   6628 C  CG  B ARG A 1 818  ? 17.057 59.859  -15.882 0.50 11.76 ? 818  ARG A CG  1 
ATOM   6629 C  CD  A ARG A 1 818  ? 16.281 60.536  -16.988 0.50 8.91  ? 818  ARG A CD  1 
ATOM   6630 C  CD  B ARG A 1 818  ? 16.785 60.775  -17.064 0.50 11.24 ? 818  ARG A CD  1 
ATOM   6631 N  NE  A ARG A 1 818  ? 15.010 59.894  -17.308 0.50 10.93 ? 818  ARG A NE  1 
ATOM   6632 N  NE  B ARG A 1 818  ? 16.105 60.078  -18.152 0.50 17.20 ? 818  ARG A NE  1 
ATOM   6633 C  CZ  A ARG A 1 818  ? 14.715 59.370  -18.494 0.50 10.65 ? 818  ARG A CZ  1 
ATOM   6634 C  CZ  B ARG A 1 818  ? 16.681 59.749  -19.303 0.50 15.63 ? 818  ARG A CZ  1 
ATOM   6635 N  NH1 A ARG A 1 818  ? 15.602 59.410  -19.478 0.50 8.34  ? 818  ARG A NH1 1 
ATOM   6636 N  NH1 B ARG A 1 818  ? 17.952 60.053  -19.522 0.50 10.17 ? 818  ARG A NH1 1 
ATOM   6637 N  NH2 A ARG A 1 818  ? 13.532 58.805  -18.696 0.50 11.64 ? 818  ARG A NH2 1 
ATOM   6638 N  NH2 B ARG A 1 818  ? 15.985 59.115  -20.237 0.50 16.60 ? 818  ARG A NH2 1 
ATOM   6639 N  N   . LEU A 1 819  ? 16.324 57.385  -13.474 1.00 11.22 ? 819  LEU A N   1 
ATOM   6640 C  CA  . LEU A 1 819  ? 15.113 56.842  -12.835 1.00 12.55 ? 819  LEU A CA  1 
ATOM   6641 C  C   . LEU A 1 819  ? 14.145 57.979  -12.568 1.00 12.43 ? 819  LEU A C   1 
ATOM   6642 O  O   . LEU A 1 819  ? 14.382 58.860  -11.760 1.00 12.74 ? 819  LEU A O   1 
ATOM   6643 C  CB  . LEU A 1 819  ? 15.451 56.117  -11.525 1.00 13.29 ? 819  LEU A CB  1 
ATOM   6644 C  CG  . LEU A 1 819  ? 16.367 54.884  -11.649 1.00 13.82 ? 819  LEU A CG  1 
ATOM   6645 C  CD1 . LEU A 1 819  ? 16.783 54.374  -10.272 1.00 16.26 ? 819  LEU A CD1 1 
ATOM   6646 C  CD2 . LEU A 1 819  ? 15.743 53.791  -12.491 1.00 15.81 ? 819  LEU A CD2 1 
ATOM   6647 N  N   . ASP A 1 820  ? 13.016 57.943  -13.273 1.00 13.86 ? 820  ASP A N   1 
ATOM   6648 C  CA  . ASP A 1 820  ? 12.039 58.996  -13.069 1.00 15.57 ? 820  ASP A CA  1 
ATOM   6649 C  C   . ASP A 1 820  ? 11.321 58.876  -11.731 1.00 14.60 ? 820  ASP A C   1 
ATOM   6650 O  O   . ASP A 1 820  ? 10.719 59.836  -11.257 1.00 14.90 ? 820  ASP A O   1 
ATOM   6651 C  CB  . ASP A 1 820  ? 11.078 59.060  -14.252 1.00 16.50 ? 820  ASP A CB  1 
ATOM   6652 C  CG  . ASP A 1 820  ? 11.801 59.401  -15.553 1.00 19.99 ? 820  ASP A CG  1 
ATOM   6653 O  OD1 . ASP A 1 820  ? 12.881 60.065  -15.518 1.00 20.96 ? 820  ASP A OD1 1 
ATOM   6654 O  OD2 . ASP A 1 820  ? 11.379 59.035  -16.665 1.00 24.41 ? 820  ASP A OD2 1 
ATOM   6655 N  N   . LYS A 1 821  ? 11.455 57.726  -11.055 1.00 13.66 ? 821  LYS A N   1 
ATOM   6656 C  CA  . LYS A 1 821  ? 10.899 57.597  -9.698  1.00 14.61 ? 821  LYS A CA  1 
ATOM   6657 C  C   . LYS A 1 821  ? 11.731 58.357  -8.648  1.00 14.65 ? 821  LYS A C   1 
ATOM   6658 O  O   . LYS A 1 821  ? 11.269 58.567  -7.538  1.00 15.67 ? 821  LYS A O   1 
ATOM   6659 C  CB  . LYS A 1 821  ? 10.763 56.123  -9.299  1.00 14.33 ? 821  LYS A CB  1 
ATOM   6660 C  CG  . LYS A 1 821  ? 12.114 55.425  -9.057  1.00 13.88 ? 821  LYS A CG  1 
ATOM   6661 C  CD  . LYS A 1 821  ? 11.932 53.931  -8.944  1.00 14.07 ? 821  LYS A CD  1 
ATOM   6662 C  CE  . LYS A 1 821  ? 13.268 53.239  -8.896  1.00 14.45 ? 821  LYS A CE  1 
ATOM   6663 N  NZ  . LYS A 1 821  ? 13.203 51.756  -9.026  1.00 14.96 ? 821  LYS A NZ  1 
ATOM   6664 N  N   . LEU A 1 822  ? 12.929 58.830  -9.046  1.00 13.64 ? 822  LEU A N   1 
ATOM   6665 C  CA  . LEU A 1 822  ? 13.783 59.647  -8.159  1.00 13.47 ? 822  LEU A CA  1 
ATOM   6666 C  C   . LEU A 1 822  ? 13.803 61.076  -8.679  1.00 12.89 ? 822  LEU A C   1 
ATOM   6667 O  O   . LEU A 1 822  ? 13.649 61.275  -9.874  1.00 12.70 ? 822  LEU A O   1 
ATOM   6668 C  CB  . LEU A 1 822  ? 15.209 59.110  -8.171  1.00 13.66 ? 822  LEU A CB  1 
ATOM   6669 C  CG  . LEU A 1 822  ? 15.375 57.668  -7.695  1.00 15.01 ? 822  LEU A CG  1 
ATOM   6670 C  CD1 . LEU A 1 822  ? 16.856 57.309  -7.638  1.00 16.21 ? 822  LEU A CD1 1 
ATOM   6671 C  CD2 . LEU A 1 822  ? 14.711 57.413  -6.359  1.00 16.43 ? 822  LEU A CD2 1 
ATOM   6672 N  N   . PRO A 1 823  ? 14.029 62.045  -7.790  1.00 12.49 ? 823  PRO A N   1 
ATOM   6673 C  CA  . PRO A 1 823  ? 14.080 63.455  -8.224  1.00 12.16 ? 823  PRO A CA  1 
ATOM   6674 C  C   . PRO A 1 823  ? 15.323 63.745  -9.072  1.00 12.09 ? 823  PRO A C   1 
ATOM   6675 O  O   . PRO A 1 823  ? 16.304 62.969  -9.099  1.00 11.88 ? 823  PRO A O   1 
ATOM   6676 C  CB  . PRO A 1 823  ? 14.085 64.239  -6.926  1.00 13.68 ? 823  PRO A CB  1 
ATOM   6677 C  CG  . PRO A 1 823  ? 14.674 63.303  -5.910  1.00 13.79 ? 823  PRO A CG  1 
ATOM   6678 C  CD  . PRO A 1 823  ? 14.209 61.913  -6.330  1.00 12.66 ? 823  PRO A CD  1 
ATOM   6679 N  N   . LEU A 1 824  ? 15.273 64.864  -9.786  1.00 11.51 ? 824  LEU A N   1 
ATOM   6680 C  CA  . LEU A 1 824  ? 16.324 65.274  -10.684 1.00 11.40 ? 824  LEU A CA  1 
ATOM   6681 C  C   . LEU A 1 824  ? 17.739 65.123  -10.065 1.00 9.93  ? 824  LEU A C   1 
ATOM   6682 O  O   . LEU A 1 824  ? 18.622 64.557  -10.724 1.00 10.07 ? 824  LEU A O   1 
ATOM   6683 C  CB  . LEU A 1 824  ? 16.041 66.727  -11.099 1.00 11.71 ? 824  LEU A CB  1 
ATOM   6684 C  CG  . LEU A 1 824  ? 16.839 67.306  -12.256 1.00 11.33 ? 824  LEU A CG  1 
ATOM   6685 C  CD1 . LEU A 1 824  ? 16.063 68.516  -12.822 1.00 12.93 ? 824  LEU A CD1 1 
ATOM   6686 C  CD2 . LEU A 1 824  ? 18.285 67.724  -11.871 1.00 10.89 ? 824  LEU A CD2 1 
ATOM   6687 N  N   . GLN A 1 825  ? 17.909 65.620  -8.853  1.00 9.85  ? 825  GLN A N   1 
ATOM   6688 C  CA  . GLN A 1 825  ? 19.233 65.666  -8.216  1.00 9.72  ? 825  GLN A CA  1 
ATOM   6689 C  C   . GLN A 1 825  ? 19.772 64.281  -7.895  1.00 10.31 ? 825  GLN A C   1 
ATOM   6690 O  O   . GLN A 1 825  ? 21.012 64.123  -7.724  1.00 9.87  ? 825  GLN A O   1 
ATOM   6691 C  CB  . GLN A 1 825  ? 19.203 66.543  -6.988  1.00 10.50 ? 825  GLN A CB  1 
ATOM   6692 C  CG  . GLN A 1 825  ? 18.281 66.026  -5.874  1.00 10.52 ? 825  GLN A CG  1 
ATOM   6693 C  CD  . GLN A 1 825  ? 16.828 66.518  -5.967  1.00 11.02 ? 825  GLN A CD  1 
ATOM   6694 O  OE1 . GLN A 1 825  ? 16.376 66.967  -7.027  1.00 11.24 ? 825  GLN A OE1 1 
ATOM   6695 N  NE2 . GLN A 1 825  ? 16.121 66.442  -4.853  1.00 11.36 ? 825  GLN A NE2 1 
ATOM   6696 N  N   . ALA A 1 826  ? 18.889 63.263  -7.821  1.00 9.17  ? 826  ALA A N   1 
ATOM   6697 C  CA  . ALA A 1 826  ? 19.326 61.894  -7.604  1.00 9.21  ? 826  ALA A CA  1 
ATOM   6698 C  C   . ALA A 1 826  ? 19.934 61.296  -8.847  1.00 9.89  ? 826  ALA A C   1 
ATOM   6699 O  O   . ALA A 1 826  ? 20.666 60.304  -8.781  1.00 10.26 ? 826  ALA A O   1 
ATOM   6700 C  CB  . ALA A 1 826  ? 18.126 61.033  -7.127  1.00 10.41 ? 826  ALA A CB  1 
ATOM   6701 N  N   . ASN A 1 827  ? 19.573 61.844  -10.008 1.00 9.42  ? 827  ASN A N   1 
ATOM   6702 C  CA  . ASN A 1 827  ? 20.068 61.389  -11.307 1.00 9.32  ? 827  ASN A CA  1 
ATOM   6703 C  C   . ASN A 1 827  ? 21.395 62.018  -11.753 1.00 8.15  ? 827  ASN A C   1 
ATOM   6704 O  O   . ASN A 1 827  ? 21.890 61.710  -12.788 1.00 9.04  ? 827  ASN A O   1 
ATOM   6705 C  CB  . ASN A 1 827  ? 18.952 61.534  -12.356 1.00 9.50  ? 827  ASN A CB  1 
ATOM   6706 C  CG  . ASN A 1 827  ? 17.824 60.515  -12.115 1.00 12.39 ? 827  ASN A CG  1 
ATOM   6707 O  OD1 . ASN A 1 827  ? 18.046 59.326  -12.160 1.00 12.12 ? 827  ASN A OD1 1 
ATOM   6708 N  ND2 . ASN A 1 827  ? 16.636 61.006  -11.786 1.00 14.50 ? 827  ASN A ND2 1 
ATOM   6709 N  N   . TYR A 1 828  ? 21.905 62.901  -10.898 1.00 8.22  ? 828  TYR A N   1 
ATOM   6710 C  CA  . TYR A 1 828  ? 23.238 63.486  -11.056 1.00 8.00  ? 828  TYR A CA  1 
ATOM   6711 C  C   . TYR A 1 828  ? 24.258 62.544  -10.410 1.00 8.16  ? 828  TYR A C   1 
ATOM   6712 O  O   . TYR A 1 828  ? 24.017 62.010  -9.311  1.00 8.51  ? 828  TYR A O   1 
ATOM   6713 C  CB  . TYR A 1 828  ? 23.298 64.859  -10.350 1.00 9.21  ? 828  TYR A CB  1 
ATOM   6714 C  CG  . TYR A 1 828  ? 23.286 65.990  -11.343 1.00 8.12  ? 828  TYR A CG  1 
ATOM   6715 C  CD1 . TYR A 1 828  ? 22.228 66.192  -12.227 1.00 9.28  ? 828  TYR A CD1 1 
ATOM   6716 C  CD2 . TYR A 1 828  ? 24.379 66.840  -11.440 1.00 10.00 ? 828  TYR A CD2 1 
ATOM   6717 C  CE1 . TYR A 1 828  ? 22.277 67.215  -13.186 1.00 10.32 ? 828  TYR A CE1 1 
ATOM   6718 C  CE2 . TYR A 1 828  ? 24.427 67.838  -12.354 1.00 10.62 ? 828  TYR A CE2 1 
ATOM   6719 C  CZ  . TYR A 1 828  ? 23.401 68.008  -13.250 1.00 8.73  ? 828  TYR A CZ  1 
ATOM   6720 O  OH  . TYR A 1 828  ? 23.530 69.041  -14.136 1.00 10.40 ? 828  TYR A OH  1 
ATOM   6721 N  N   . TYR A 1 829  ? 25.393 62.390  -11.100 1.00 7.64  ? 829  TYR A N   1 
ATOM   6722 C  CA  . TYR A 1 829  ? 26.471 61.499  -10.680 1.00 8.32  ? 829  TYR A CA  1 
ATOM   6723 C  C   . TYR A 1 829  ? 27.782 62.252  -10.834 1.00 8.65  ? 829  TYR A C   1 
ATOM   6724 O  O   . TYR A 1 829  ? 27.868 63.225  -11.569 1.00 8.12  ? 829  TYR A O   1 
ATOM   6725 C  CB  . TYR A 1 829  ? 26.509 60.231  -11.543 1.00 7.83  ? 829  TYR A CB  1 
ATOM   6726 C  CG  . TYR A 1 829  ? 25.311 59.335  -11.269 1.00 8.00  ? 829  TYR A CG  1 
ATOM   6727 C  CD1 . TYR A 1 829  ? 25.337 58.460  -10.194 1.00 8.58  ? 829  TYR A CD1 1 
ATOM   6728 C  CD2 . TYR A 1 829  ? 24.131 59.396  -12.054 1.00 9.03  ? 829  TYR A CD2 1 
ATOM   6729 C  CE1 . TYR A 1 829  ? 24.236 57.638  -9.891  1.00 8.60  ? 829  TYR A CE1 1 
ATOM   6730 C  CE2 . TYR A 1 829  ? 23.045 58.586  -11.748 1.00 9.43  ? 829  TYR A CE2 1 
ATOM   6731 C  CZ  . TYR A 1 829  ? 23.118 57.709  -10.692 1.00 8.81  ? 829  TYR A CZ  1 
ATOM   6732 O  OH  . TYR A 1 829  ? 22.072 56.885  -10.335 1.00 10.00 ? 829  TYR A OH  1 
ATOM   6733 N  N   . PRO A 1 830  ? 28.830 61.773  -10.157 1.00 7.88  ? 830  PRO A N   1 
ATOM   6734 C  CA  . PRO A 1 830  ? 30.143 62.381  -10.364 1.00 7.82  ? 830  PRO A CA  1 
ATOM   6735 C  C   . PRO A 1 830  ? 30.596 62.137  -11.801 1.00 7.99  ? 830  PRO A C   1 
ATOM   6736 O  O   . PRO A 1 830  ? 30.365 61.053  -12.350 1.00 8.15  ? 830  PRO A O   1 
ATOM   6737 C  CB  . PRO A 1 830  ? 31.049 61.626  -9.354  1.00 10.96 ? 830  PRO A CB  1 
ATOM   6738 C  CG  . PRO A 1 830  ? 30.170 60.788  -8.512  1.00 9.52  ? 830  PRO A CG  1 
ATOM   6739 C  CD  . PRO A 1 830  ? 28.856 60.610  -9.239  1.00 7.73  ? 830  PRO A CD  1 
ATOM   6740 N  N   . ILE A 1 831  ? 31.226 63.137  -12.423 1.00 6.96  ? 831  ILE A N   1 
ATOM   6741 C  CA  . ILE A 1 831  ? 31.898 62.987  -13.709 1.00 7.56  ? 831  ILE A CA  1 
ATOM   6742 C  C   . ILE A 1 831  ? 33.355 63.292  -13.463 1.00 7.97  ? 831  ILE A C   1 
ATOM   6743 O  O   . ILE A 1 831  ? 33.836 64.386  -13.787 1.00 7.91  ? 831  ILE A O   1 
ATOM   6744 C  CB  . ILE A 1 831  ? 31.307 63.926  -14.808 1.00 6.96  ? 831  ILE A CB  1 
ATOM   6745 C  CG1 . ILE A 1 831  ? 29.786 63.995  -14.747 1.00 8.19  ? 831  ILE A CG1 1 
ATOM   6746 C  CG2 . ILE A 1 831  ? 31.851 63.523  -16.152 1.00 8.44  ? 831  ILE A CG2 1 
ATOM   6747 C  CD1 . ILE A 1 831  ? 29.036 62.680  -15.009 1.00 8.68  ? 831  ILE A CD1 1 
ATOM   6748 N  N   . PRO A 1 832  ? 34.076 62.366  -12.859 1.00 7.04  ? 832  PRO A N   1 
ATOM   6749 C  CA  . PRO A 1 832  ? 35.470 62.671  -12.508 1.00 7.74  ? 832  PRO A CA  1 
ATOM   6750 C  C   . PRO A 1 832  ? 36.357 62.749  -13.716 1.00 8.52  ? 832  PRO A C   1 
ATOM   6751 O  O   . PRO A 1 832  ? 37.325 63.515  -13.593 1.00 11.02 ? 832  PRO A O   1 
ATOM   6752 C  CB  . PRO A 1 832  ? 35.881 61.555  -11.527 1.00 7.73  ? 832  PRO A CB  1 
ATOM   6753 C  CG  . PRO A 1 832  ? 34.849 60.485  -11.719 1.00 8.54  ? 832  PRO A CG  1 
ATOM   6754 C  CD  . PRO A 1 832  ? 33.597 61.112  -12.245 1.00 7.95  ? 832  PRO A CD  1 
ATOM   6755 N  N   . SER A 1 833  ? 36.035 62.124  -14.851 1.00 7.24  ? 833  SER A N   1 
ATOM   6756 C  CA  . SER A 1 833  ? 36.855 62.242  -16.041 1.00 7.54  ? 833  SER A CA  1 
ATOM   6757 C  C   . SER A 1 833  ? 36.107 62.076  -17.386 1.00 6.84  ? 833  SER A C   1 
ATOM   6758 O  O   . SER A 1 833  ? 36.654 62.366  -18.438 1.00 6.80  ? 833  SER A O   1 
ATOM   6759 C  CB  . SER A 1 833  ? 38.071 61.350  -15.995 1.00 10.41 ? 833  SER A CB  1 
ATOM   6760 O  OG  . SER A 1 833  ? 37.768 60.055  -16.295 1.00 11.41 ? 833  SER A OG  1 
ATOM   6761 N  N   . GLY A 1 834  ? 34.892 61.547  -17.333 1.00 7.09  ? 834  GLY A N   1 
ATOM   6762 C  CA  . GLY A 1 834  ? 34.142 61.474  -18.589 1.00 7.31  ? 834  GLY A CA  1 
ATOM   6763 C  C   . GLY A 1 834  ? 32.799 60.818  -18.446 1.00 6.76  ? 834  GLY A C   1 
ATOM   6764 O  O   . GLY A 1 834  ? 32.416 60.224  -17.419 1.00 7.02  ? 834  GLY A O   1 
ATOM   6765 N  N   . MET A 1 835  ? 32.029 60.947  -19.514 1.00 6.90  ? 835  MET A N   1 
ATOM   6766 C  CA  . MET A 1 835  ? 30.683 60.408  -19.562 1.00 7.59  ? 835  MET A CA  1 
ATOM   6767 C  C   . MET A 1 835  ? 30.322 60.189  -21.018 1.00 7.42  ? 835  MET A C   1 
ATOM   6768 O  O   . MET A 1 835  ? 30.872 60.841  -21.888 1.00 7.83  ? 835  MET A O   1 
ATOM   6769 C  CB  . MET A 1 835  ? 29.697 61.383  -18.920 1.00 7.51  ? 835  MET A CB  1 
ATOM   6770 C  CG  . MET A 1 835  ? 29.526 62.682  -19.710 1.00 9.87  ? 835  MET A CG  1 
ATOM   6771 S  SD  . MET A 1 835  ? 28.656 63.998  -18.828 1.00 12.01 ? 835  MET A SD  1 
ATOM   6772 C  CE  . MET A 1 835  ? 27.160 63.154  -18.376 1.00 13.82 ? 835  MET A CE  1 
ATOM   6773 N  N   . PHE A 1 836  ? 29.407 59.260  -21.273 1.00 7.75  ? 836  PHE A N   1 
ATOM   6774 C  CA  . PHE A 1 836  ? 28.973 59.005  -22.653 1.00 8.33  ? 836  PHE A CA  1 
ATOM   6775 C  C   . PHE A 1 836  ? 27.553 58.497  -22.723 1.00 8.66  ? 836  PHE A C   1 
ATOM   6776 O  O   . PHE A 1 836  ? 26.992 57.975  -21.761 1.00 7.84  ? 836  PHE A O   1 
ATOM   6777 C  CB  . PHE A 1 836  ? 29.970 58.179  -23.479 1.00 9.13  ? 836  PHE A CB  1 
ATOM   6778 C  CG  . PHE A 1 836  ? 30.158 56.720  -23.057 1.00 8.04  ? 836  PHE A CG  1 
ATOM   6779 C  CD1 . PHE A 1 836  ? 29.282 55.706  -23.513 1.00 9.22  ? 836  PHE A CD1 1 
ATOM   6780 C  CD2 . PHE A 1 836  ? 31.251 56.351  -22.240 1.00 9.03  ? 836  PHE A CD2 1 
ATOM   6781 C  CE1 . PHE A 1 836  ? 29.492 54.361  -23.127 1.00 11.28 ? 836  PHE A CE1 1 
ATOM   6782 C  CE2 . PHE A 1 836  ? 31.461 55.011  -21.899 1.00 10.59 ? 836  PHE A CE2 1 
ATOM   6783 C  CZ  . PHE A 1 836  ? 30.586 54.018  -22.371 1.00 10.46 ? 836  PHE A CZ  1 
ATOM   6784 N  N   . ILE A 1 837  ? 26.937 58.731  -23.896 1.00 8.28  ? 837  ILE A N   1 
ATOM   6785 C  CA  . ILE A 1 837  ? 25.642 58.119  -24.252 1.00 9.84  ? 837  ILE A CA  1 
ATOM   6786 C  C   . ILE A 1 837  ? 25.844 57.443  -25.585 1.00 9.20  ? 837  ILE A C   1 
ATOM   6787 O  O   . ILE A 1 837  ? 26.693 57.822  -26.379 1.00 9.31  ? 837  ILE A O   1 
ATOM   6788 C  CB  . ILE A 1 837  ? 24.480 59.145  -24.314 1.00 10.13 ? 837  ILE A CB  1 
ATOM   6789 C  CG1 . ILE A 1 837  ? 24.864 60.354  -25.169 1.00 9.57  ? 837  ILE A CG1 1 
ATOM   6790 C  CG2 . ILE A 1 837  ? 23.986 59.498  -22.939 1.00 11.69 ? 837  ILE A CG2 1 
ATOM   6791 C  CD1 . ILE A 1 837  ? 23.695 61.248  -25.599 1.00 11.51 ? 837  ILE A CD1 1 
ATOM   6792 N  N   . GLU A 1 838  ? 25.037 56.398  -25.809 1.00 9.58  ? 838  GLU A N   1 
ATOM   6793 C  CA  . GLU A 1 838  ? 25.144 55.672  -27.072 1.00 10.73 ? 838  GLU A CA  1 
ATOM   6794 C  C   . GLU A 1 838  ? 23.817 54.974  -27.420 1.00 10.16 ? 838  GLU A C   1 
ATOM   6795 O  O   . GLU A 1 838  ? 22.952 54.744  -26.577 1.00 11.62 ? 838  GLU A O   1 
ATOM   6796 C  CB  . GLU A 1 838  ? 26.286 54.656  -27.058 1.00 10.73 ? 838  GLU A CB  1 
ATOM   6797 C  CG  . GLU A 1 838  ? 26.056 53.547  -26.026 1.00 12.70 ? 838  GLU A CG  1 
ATOM   6798 C  CD  . GLU A 1 838  ? 27.149 52.500  -26.015 1.00 13.70 ? 838  GLU A CD  1 
ATOM   6799 O  OE1 . GLU A 1 838  ? 28.156 52.636  -26.702 1.00 14.93 ? 838  GLU A OE1 1 
ATOM   6800 O  OE2 . GLU A 1 838  ? 26.983 51.482  -25.300 1.00 15.60 ? 838  GLU A OE2 1 
ATOM   6801 N  N   . ASP A 1 839  ? 23.685 54.697  -28.720 1.00 11.60 ? 839  ASP A N   1 
ATOM   6802 C  CA  . ASP A 1 839  ? 22.653 53.756  -29.188 1.00 11.86 ? 839  ASP A CA  1 
ATOM   6803 C  C   . ASP A 1 839  ? 23.336 52.668  -29.981 1.00 12.53 ? 839  ASP A C   1 
ATOM   6804 O  O   . ASP A 1 839  ? 24.526 52.464  -29.884 1.00 13.63 ? 839  ASP A O   1 
ATOM   6805 C  CB  . ASP A 1 839  ? 21.509 54.461  -29.934 1.00 12.19 ? 839  ASP A CB  1 
ATOM   6806 C  CG  . ASP A 1 839  ? 21.964 55.230  -31.179 1.00 12.29 ? 839  ASP A CG  1 
ATOM   6807 O  OD1 . ASP A 1 839  ? 22.984 54.881  -31.782 1.00 13.02 ? 839  ASP A OD1 1 
ATOM   6808 O  OD2 . ASP A 1 839  ? 21.289 56.216  -31.588 1.00 16.45 ? 839  ASP A OD2 1 
ATOM   6809 N  N   . ALA A 1 840  ? 22.570 51.957  -30.817 1.00 13.62 ? 840  ALA A N   1 
ATOM   6810 C  CA  . ALA A 1 840  ? 23.165 50.892  -31.598 1.00 14.91 ? 840  ALA A CA  1 
ATOM   6811 C  C   . ALA A 1 840  ? 24.300 51.362  -32.516 1.00 14.91 ? 840  ALA A C   1 
ATOM   6812 O  O   . ALA A 1 840  ? 25.229 50.633  -32.784 1.00 16.28 ? 840  ALA A O   1 
ATOM   6813 C  CB  . ALA A 1 840  ? 22.080 50.152  -32.421 1.00 16.69 ? 840  ALA A CB  1 
ATOM   6814 N  N   . ASN A 1 841  ? 24.191 52.593  -33.030 1.00 13.58 ? 841  ASN A N   1 
ATOM   6815 C  CA  . ASN A 1 841  ? 25.105 53.081  -34.074 1.00 13.17 ? 841  ASN A CA  1 
ATOM   6816 C  C   . ASN A 1 841  ? 26.113 54.182  -33.710 1.00 11.28 ? 841  ASN A C   1 
ATOM   6817 O  O   . ASN A 1 841  ? 27.142 54.269  -34.333 1.00 12.69 ? 841  ASN A O   1 
ATOM   6818 C  CB  . ASN A 1 841  ? 24.278 53.554  -35.296 1.00 13.76 ? 841  ASN A CB  1 
ATOM   6819 C  CG  . ASN A 1 841  ? 23.534 52.394  -35.967 1.00 16.06 ? 841  ASN A CG  1 
ATOM   6820 O  OD1 . ASN A 1 841  ? 24.069 51.304  -36.073 1.00 18.48 ? 841  ASN A OD1 1 
ATOM   6821 N  ND2 . ASN A 1 841  ? 22.307 52.633  -36.365 1.00 20.00 ? 841  ASN A ND2 1 
ATOM   6822 N  N   . THR A 1 842  ? 25.732 54.995  -32.721 1.00 11.39 ? 842  THR A N   1 
ATOM   6823 C  CA  . THR A 1 842  ? 26.409 56.269  -32.460 1.00 10.96 ? 842  THR A CA  1 
ATOM   6824 C  C   . THR A 1 842  ? 26.683 56.403  -30.968 1.00 10.85 ? 842  THR A C   1 
ATOM   6825 O  O   . THR A 1 842  ? 25.836 56.116  -30.160 1.00 11.43 ? 842  THR A O   1 
ATOM   6826 C  CB  . THR A 1 842  ? 25.502 57.437  -32.891 1.00 11.02 ? 842  THR A CB  1 
ATOM   6827 O  OG1 . THR A 1 842  ? 25.096 57.267  -34.264 1.00 13.78 ? 842  THR A OG1 1 
ATOM   6828 C  CG2 . THR A 1 842  ? 26.285 58.780  -32.913 1.00 12.80 ? 842  THR A CG2 1 
ATOM   6829 N  N   . ARG A 1 843  ? 27.854 56.962  -30.677 1.00 10.82 ? 843  ARG A N   1 
ATOM   6830 C  CA  . ARG A 1 843  ? 28.205 57.316  -29.286 1.00 10.13 ? 843  ARG A CA  1 
ATOM   6831 C  C   . ARG A 1 843  ? 28.734 58.759  -29.261 1.00 9.82  ? 843  ARG A C   1 
ATOM   6832 O  O   . ARG A 1 843  ? 29.468 59.165  -30.170 1.00 9.93  ? 843  ARG A O   1 
ATOM   6833 C  CB  . ARG A 1 843  ? 29.290 56.375  -28.755 1.00 10.90 ? 843  ARG A CB  1 
ATOM   6834 C  CG  . ARG A 1 843  ? 29.713 56.650  -27.287 1.00 9.81  ? 843  ARG A CG  1 
ATOM   6835 C  CD  . ARG A 1 843  ? 30.882 55.812  -26.860 1.00 10.04 ? 843  ARG A CD  1 
ATOM   6836 N  NE  . ARG A 1 843  ? 30.487 54.417  -26.580 1.00 10.73 ? 843  ARG A NE  1 
ATOM   6837 C  CZ  . ARG A 1 843  ? 31.303 53.573  -25.980 1.00 11.37 ? 843  ARG A CZ  1 
ATOM   6838 N  NH1 . ARG A 1 843  ? 32.537 53.941  -25.655 1.00 10.15 ? 843  ARG A NH1 1 
ATOM   6839 N  NH2 . ARG A 1 843  ? 30.869 52.348  -25.702 1.00 11.87 ? 843  ARG A NH2 1 
ATOM   6840 N  N   . LEU A 1 844  ? 28.357 59.471  -28.209 1.00 8.97  ? 844  LEU A N   1 
ATOM   6841 C  CA  . LEU A 1 844  ? 28.963 60.789  -27.921 1.00 8.99  ? 844  LEU A CA  1 
ATOM   6842 C  C   . LEU A 1 844  ? 29.620 60.671  -26.536 1.00 8.59  ? 844  LEU A C   1 
ATOM   6843 O  O   . LEU A 1 844  ? 28.935 60.356  -25.567 1.00 8.52  ? 844  LEU A O   1 
ATOM   6844 C  CB  . LEU A 1 844  ? 27.904 61.885  -27.930 1.00 9.87  ? 844  LEU A CB  1 
ATOM   6845 C  CG  . LEU A 1 844  ? 28.528 63.298  -27.818 1.00 10.44 ? 844  LEU A CG  1 
ATOM   6846 C  CD1 . LEU A 1 844  ? 29.424 63.621  -28.987 1.00 13.13 ? 844  LEU A CD1 1 
ATOM   6847 C  CD2 . LEU A 1 844  ? 27.399 64.320  -27.635 1.00 13.25 ? 844  LEU A CD2 1 
ATOM   6848 N  N   . THR A 1 845  ? 30.931 60.941  -26.517 1.00 8.18  ? 845  THR A N   1 
ATOM   6849 C  CA  . THR A 1 845  ? 31.699 60.917  -25.257 1.00 8.65  ? 845  THR A CA  1 
ATOM   6850 C  C   . THR A 1 845  ? 32.221 62.325  -24.962 1.00 8.30  ? 845  THR A C   1 
ATOM   6851 O  O   . THR A 1 845  ? 32.821 62.962  -25.836 1.00 8.53  ? 845  THR A O   1 
ATOM   6852 C  CB  . THR A 1 845  ? 32.896 59.972  -25.378 1.00 8.04  ? 845  THR A CB  1 
ATOM   6853 O  OG1 . THR A 1 845  ? 32.439 58.644  -25.743 1.00 9.45  ? 845  THR A OG1 1 
ATOM   6854 C  CG2 . THR A 1 845  ? 33.609 59.755  -24.022 1.00 8.90  ? 845  THR A CG2 1 
ATOM   6855 N  N   . LEU A 1 846  ? 32.026 62.767  -23.730 1.00 7.87  ? 846  LEU A N   1 
ATOM   6856 C  CA  . LEU A 1 846  ? 32.576 64.049  -23.258 1.00 8.31  ? 846  LEU A CA  1 
ATOM   6857 C  C   . LEU A 1 846  ? 33.625 63.724  -22.188 1.00 6.89  ? 846  LEU A C   1 
ATOM   6858 O  O   . LEU A 1 846  ? 33.266 63.130  -21.163 1.00 7.11  ? 846  LEU A O   1 
ATOM   6859 C  CB  . LEU A 1 846  ? 31.471 64.934  -22.689 1.00 8.95  ? 846  LEU A CB  1 
ATOM   6860 C  CG  . LEU A 1 846  ? 31.909 66.310  -22.172 1.00 10.31 ? 846  LEU A CG  1 
ATOM   6861 C  CD1 . LEU A 1 846  ? 32.377 67.192  -23.335 1.00 10.23 ? 846  LEU A CD1 1 
ATOM   6862 C  CD2 . LEU A 1 846  ? 30.837 67.019  -21.350 1.00 13.16 ? 846  LEU A CD2 1 
ATOM   6863 N  N   . LEU A 1 847  ? 34.883 64.028  -22.465 1.00 7.34  ? 847  LEU A N   1 
ATOM   6864 C  CA  . LEU A 1 847  ? 35.973 63.825  -21.488 1.00 6.12  ? 847  LEU A CA  1 
ATOM   6865 C  C   . LEU A 1 847  ? 36.220 65.134  -20.770 1.00 6.94  ? 847  LEU A C   1 
ATOM   6866 O  O   . LEU A 1 847  ? 36.112 66.204  -21.402 1.00 7.36  ? 847  LEU A O   1 
ATOM   6867 C  CB  . LEU A 1 847  ? 37.248 63.357  -22.170 1.00 7.30  ? 847  LEU A CB  1 
ATOM   6868 C  CG  . LEU A 1 847  ? 37.241 61.997  -22.887 1.00 7.17  ? 847  LEU A CG  1 
ATOM   6869 C  CD1 . LEU A 1 847  ? 36.589 60.888  -22.058 1.00 8.62  ? 847  LEU A CD1 1 
ATOM   6870 C  CD2 . LEU A 1 847  ? 36.593 62.067  -24.270 1.00 9.35  ? 847  LEU A CD2 1 
ATOM   6871 N  N   . THR A 1 848  ? 36.586 65.064  -19.491 1.00 6.57  ? 848  THR A N   1 
ATOM   6872 C  CA  A THR A 1 848  ? 36.814 66.292  -18.692 0.50 6.98  ? 848  THR A CA  1 
ATOM   6873 C  CA  B THR A 1 848  ? 36.775 66.267  -18.675 0.50 7.51  ? 848  THR A CA  1 
ATOM   6874 C  C   . THR A 1 848  ? 38.204 66.376  -18.098 1.00 7.99  ? 848  THR A C   1 
ATOM   6875 O  O   . THR A 1 848  ? 38.879 65.354  -17.808 1.00 8.34  ? 848  THR A O   1 
ATOM   6876 C  CB  A THR A 1 848  ? 35.899 66.416  -17.498 0.50 7.99  ? 848  THR A CB  1 
ATOM   6877 C  CB  B THR A 1 848  ? 35.740 66.259  -17.559 0.50 8.54  ? 848  THR A CB  1 
ATOM   6878 O  OG1 A THR A 1 848  ? 36.277 65.431  -16.517 0.50 6.69  ? 848  THR A OG1 1 
ATOM   6879 O  OG1 B THR A 1 848  ? 34.444 65.957  -18.092 0.50 13.70 ? 848  THR A OG1 1 
ATOM   6880 C  CG2 A THR A 1 848  ? 34.455 66.162  -17.815 0.50 10.34 ? 848  THR A CG2 1 
ATOM   6881 C  CG2 B THR A 1 848  ? 35.565 67.610  -16.966 0.50 7.92  ? 848  THR A CG2 1 
ATOM   6882 N  N   . GLY A 1 849  ? 38.673 67.612  -17.952 1.00 6.39  ? 849  GLY A N   1 
ATOM   6883 C  CA  . GLY A 1 849  ? 39.928 67.870  -17.276 1.00 6.25  ? 849  GLY A CA  1 
ATOM   6884 C  C   . GLY A 1 849  ? 39.771 68.213  -15.814 1.00 6.04  ? 849  GLY A C   1 
ATOM   6885 O  O   . GLY A 1 849  ? 40.727 68.638  -15.170 1.00 6.71  ? 849  GLY A O   1 
ATOM   6886 N  N   . GLN A 1 850  ? 38.583 67.996  -15.276 1.00 5.86  ? 850  GLN A N   1 
ATOM   6887 C  CA  . GLN A 1 850  ? 38.264 68.330  -13.904 1.00 5.79  ? 850  GLN A CA  1 
ATOM   6888 C  C   . GLN A 1 850  ? 37.002 67.576  -13.497 1.00 5.70  ? 850  GLN A C   1 
ATOM   6889 O  O   . GLN A 1 850  ? 36.105 67.383  -14.350 1.00 6.98  ? 850  GLN A O   1 
ATOM   6890 C  CB  . GLN A 1 850  ? 38.059 69.858  -13.747 1.00 6.62  ? 850  GLN A CB  1 
ATOM   6891 C  CG  . GLN A 1 850  ? 36.928 70.446  -14.643 1.00 6.83  ? 850  GLN A CG  1 
ATOM   6892 C  CD  . GLN A 1 850  ? 37.277 70.536  -16.114 1.00 6.91  ? 850  GLN A CD  1 
ATOM   6893 O  OE1 . GLN A 1 850  ? 38.392 70.941  -16.485 1.00 7.57  ? 850  GLN A OE1 1 
ATOM   6894 N  NE2 . GLN A 1 850  ? 36.309 70.214  -16.984 1.00 6.88  ? 850  GLN A NE2 1 
ATOM   6895 N  N   . PRO A 1 851  ? 36.870 67.157  -12.249 1.00 5.72  ? 851  PRO A N   1 
ATOM   6896 C  CA  . PRO A 1 851  ? 35.627 66.486  -11.827 1.00 5.82  ? 851  PRO A CA  1 
ATOM   6897 C  C   . PRO A 1 851  ? 34.519 67.492  -11.618 1.00 6.63  ? 851  PRO A C   1 
ATOM   6898 O  O   . PRO A 1 851  ? 34.713 68.539  -10.987 1.00 6.97  ? 851  PRO A O   1 
ATOM   6899 C  CB  . PRO A 1 851  ? 36.010 65.837  -10.478 1.00 6.56  ? 851  PRO A CB  1 
ATOM   6900 C  CG  . PRO A 1 851  ? 37.170 66.755  -9.964  1.00 6.59  ? 851  PRO A CG  1 
ATOM   6901 C  CD  . PRO A 1 851  ? 37.891 67.245  -11.183 1.00 5.84  ? 851  PRO A CD  1 
ATOM   6902 N  N   . LEU A 1 852  ? 33.349 67.161  -12.170 1.00 6.41  ? 852  LEU A N   1 
ATOM   6903 C  CA  . LEU A 1 852  ? 32.140 67.987  -12.076 1.00 7.46  ? 852  LEU A CA  1 
ATOM   6904 C  C   . LEU A 1 852  ? 30.926 67.083  -12.016 1.00 8.07  ? 852  LEU A C   1 
ATOM   6905 O  O   . LEU A 1 852  ? 31.050 65.888  -12.294 1.00 11.84 ? 852  LEU A O   1 
ATOM   6906 C  CB  . LEU A 1 852  ? 32.014 68.889  -13.296 1.00 7.85  ? 852  LEU A CB  1 
ATOM   6907 C  CG  . LEU A 1 852  ? 33.147 69.912  -13.472 1.00 6.98  ? 852  LEU A CG  1 
ATOM   6908 C  CD1 . LEU A 1 852  ? 33.096 70.486  -14.921 1.00 9.42  ? 852  LEU A CD1 1 
ATOM   6909 C  CD2 . LEU A 1 852  ? 33.085 71.038  -12.492 1.00 8.66  ? 852  LEU A CD2 1 
ATOM   6910 N  N   . GLY A 1 853  ? 29.769 67.590  -11.641 1.00 7.18  ? 853  GLY A N   1 
ATOM   6911 C  CA  . GLY A 1 853  ? 28.557 66.768  -11.608 1.00 7.49  ? 853  GLY A CA  1 
ATOM   6912 C  C   . GLY A 1 853  ? 27.853 66.759  -12.932 1.00 7.23  ? 853  GLY A C   1 
ATOM   6913 O  O   . GLY A 1 853  ? 27.914 67.732  -13.698 1.00 7.29  ? 853  GLY A O   1 
ATOM   6914 N  N   . GLY A 1 854  ? 27.169 65.672  -13.246 1.00 7.12  ? 854  GLY A N   1 
ATOM   6915 C  CA  . GLY A 1 854  ? 26.456 65.642  -14.509 1.00 8.77  ? 854  GLY A CA  1 
ATOM   6916 C  C   . GLY A 1 854  ? 25.461 64.516  -14.609 1.00 7.66  ? 854  GLY A C   1 
ATOM   6917 O  O   . GLY A 1 854  ? 25.278 63.690  -13.694 1.00 7.83  ? 854  GLY A O   1 
ATOM   6918 N  N   . SER A 1 855  ? 24.761 64.494  -15.749 1.00 8.19  ? 855  SER A N   1 
ATOM   6919 C  CA  . SER A 1 855  ? 23.671 63.520  -15.914 1.00 8.83  ? 855  SER A CA  1 
ATOM   6920 C  C   . SER A 1 855  ? 23.315 63.431  -17.368 1.00 8.46  ? 855  SER A C   1 
ATOM   6921 O  O   . SER A 1 855  ? 23.861 64.114  -18.223 1.00 9.03  ? 855  SER A O   1 
ATOM   6922 C  CB  . SER A 1 855  ? 22.434 63.990  -15.159 1.00 9.44  ? 855  SER A CB  1 
ATOM   6923 O  OG  . SER A 1 855  ? 21.439 62.951  -15.106 1.00 10.62 ? 855  SER A OG  1 
ATOM   6924 N  N   . SER A 1 856  ? 22.354 62.548  -17.649 1.00 8.46  ? 856  SER A N   1 
ATOM   6925 C  CA  . SER A 1 856  ? 21.619 62.563  -18.935 1.00 9.36  ? 856  SER A CA  1 
ATOM   6926 C  C   . SER A 1 856  ? 20.140 62.575  -18.542 1.00 10.06 ? 856  SER A C   1 
ATOM   6927 O  O   . SER A 1 856  ? 19.606 61.535  -18.115 1.00 11.04 ? 856  SER A O   1 
ATOM   6928 C  CB  . SER A 1 856  ? 21.966 61.317  -19.734 1.00 8.88  ? 856  SER A CB  1 
ATOM   6929 O  OG  . SER A 1 856  ? 21.102 61.228  -20.884 1.00 9.91  ? 856  SER A OG  1 
ATOM   6930 N  N   . LEU A 1 857  ? 19.459 63.737  -18.582 1.00 10.35 ? 857  LEU A N   1 
ATOM   6931 C  CA  . LEU A 1 857  ? 18.109 63.840  -18.032 1.00 10.87 ? 857  LEU A CA  1 
ATOM   6932 C  C   . LEU A 1 857  ? 17.029 63.535  -19.066 1.00 11.53 ? 857  LEU A C   1 
ATOM   6933 O  O   . LEU A 1 857  ? 15.851 63.485  -18.717 1.00 12.44 ? 857  LEU A O   1 
ATOM   6934 C  CB  . LEU A 1 857  ? 17.876 65.222  -17.422 1.00 11.32 ? 857  LEU A CB  1 
ATOM   6935 C  CG  . LEU A 1 857  ? 18.704 65.510  -16.176 1.00 12.58 ? 857  LEU A CG  1 
ATOM   6936 C  CD1 . LEU A 1 857  ? 18.535 66.954  -15.670 1.00 14.75 ? 857  LEU A CD1 1 
ATOM   6937 C  CD2 . LEU A 1 857  ? 18.366 64.539  -15.046 1.00 13.84 ? 857  LEU A CD2 1 
ATOM   6938 N  N   . ALA A 1 858  ? 17.455 63.281  -20.278 1.00 10.00 ? 858  ALA A N   1 
ATOM   6939 C  CA  . ALA A 1 858  ? 16.533 62.864  -21.363 1.00 11.35 ? 858  ALA A CA  1 
ATOM   6940 C  C   . ALA A 1 858  ? 17.341 62.166  -22.411 1.00 11.85 ? 858  ALA A C   1 
ATOM   6941 O  O   . ALA A 1 858  ? 18.561 62.390  -22.553 1.00 11.10 ? 858  ALA A O   1 
ATOM   6942 C  CB  . ALA A 1 858  ? 15.804 64.101  -21.970 1.00 13.09 ? 858  ALA A CB  1 
ATOM   6943 N  N   . SER A 1 859  ? 16.681 61.291  -23.174 1.00 11.74 ? 859  SER A N   1 
ATOM   6944 C  CA  . SER A 1 859  ? 17.334 60.543  -24.198 1.00 11.25 ? 859  SER A CA  1 
ATOM   6945 C  C   . SER A 1 859  ? 18.098 61.500  -25.130 1.00 10.49 ? 859  SER A C   1 
ATOM   6946 O  O   . SER A 1 859  ? 17.554 62.557  -25.500 1.00 11.84 ? 859  SER A O   1 
ATOM   6947 C  CB  . SER A 1 859  ? 16.267 59.716  -24.986 1.00 12.29 ? 859  SER A CB  1 
ATOM   6948 O  OG  . SER A 1 859  ? 16.837 58.955  -25.963 1.00 13.34 ? 859  SER A OG  1 
ATOM   6949 N  N   . GLY A 1 860  ? 19.308 61.129  -25.524 1.00 11.07 ? 860  GLY A N   1 
ATOM   6950 C  CA  . GLY A 1 860  ? 20.134 61.933  -26.413 1.00 10.99 ? 860  GLY A CA  1 
ATOM   6951 C  C   . GLY A 1 860  ? 20.876 63.103  -25.754 1.00 10.23 ? 860  GLY A C   1 
ATOM   6952 O  O   . GLY A 1 860  ? 21.632 63.786  -26.474 1.00 10.96 ? 860  GLY A O   1 
ATOM   6953 N  N   . GLU A 1 861  ? 20.672 63.334  -24.461 1.00 10.41 ? 861  GLU A N   1 
ATOM   6954 C  CA  . GLU A 1 861  ? 21.336 64.463  -23.774 1.00 10.32 ? 861  GLU A CA  1 
ATOM   6955 C  C   . GLU A 1 861  ? 22.517 64.047  -22.888 1.00 10.91 ? 861  GLU A C   1 
ATOM   6956 O  O   . GLU A 1 861  ? 22.533 62.942  -22.314 1.00 10.96 ? 861  GLU A O   1 
ATOM   6957 C  CB  . GLU A 1 861  ? 20.367 65.190  -22.887 1.00 11.61 ? 861  GLU A CB  1 
ATOM   6958 C  CG  . GLU A 1 861  ? 19.254 65.858  -23.652 1.00 13.31 ? 861  GLU A CG  1 
ATOM   6959 C  CD  . GLU A 1 861  ? 18.364 66.708  -22.775 1.00 16.78 ? 861  GLU A CD  1 
ATOM   6960 O  OE1 . GLU A 1 861  ? 18.530 66.778  -21.523 1.00 15.83 ? 861  GLU A OE1 1 
ATOM   6961 O  OE2 . GLU A 1 861  ? 17.415 67.325  -23.348 1.00 18.37 ? 861  GLU A OE2 1 
ATOM   6962 N  N   . LEU A 1 862  ? 23.483 64.945  -22.774 1.00 9.77  ? 862  LEU A N   1 
ATOM   6963 C  CA  . LEU A 1 862  ? 24.527 64.894  -21.718 1.00 9.81  ? 862  LEU A CA  1 
ATOM   6964 C  C   . LEU A 1 862  ? 24.509 66.267  -21.073 1.00 8.99  ? 862  LEU A C   1 
ATOM   6965 O  O   . LEU A 1 862  ? 24.351 67.271  -21.796 1.00 9.66  ? 862  LEU A O   1 
ATOM   6966 C  CB  . LEU A 1 862  ? 25.906 64.628  -22.354 1.00 9.68  ? 862  LEU A CB  1 
ATOM   6967 C  CG  . LEU A 1 862  ? 26.221 63.259  -22.958 1.00 11.04 ? 862  LEU A CG  1 
ATOM   6968 C  CD1 . LEU A 1 862  ? 27.533 63.254  -23.640 1.00 11.18 ? 862  LEU A CD1 1 
ATOM   6969 C  CD2 . LEU A 1 862  ? 26.147 62.178  -21.891 1.00 11.40 ? 862  LEU A CD2 1 
ATOM   6970 N  N   . GLU A 1 863  ? 24.751 66.366  -19.780 1.00 8.52  ? 863  GLU A N   1 
ATOM   6971 C  CA  . GLU A 1 863  ? 24.953 67.691  -19.219 1.00 8.39  ? 863  GLU A CA  1 
ATOM   6972 C  C   . GLU A 1 863  ? 25.943 67.614  -18.081 1.00 8.27  ? 863  GLU A C   1 
ATOM   6973 O  O   . GLU A 1 863  ? 26.056 66.597  -17.406 1.00 7.36  ? 863  GLU A O   1 
ATOM   6974 C  CB  . GLU A 1 863  ? 23.635 68.321  -18.772 1.00 9.49  ? 863  GLU A CB  1 
ATOM   6975 C  CG  . GLU A 1 863  ? 23.054 67.792  -17.481 1.00 9.96  ? 863  GLU A CG  1 
ATOM   6976 C  CD  . GLU A 1 863  ? 21.758 68.502  -17.115 1.00 9.17  ? 863  GLU A CD  1 
ATOM   6977 O  OE1 . GLU A 1 863  ? 20.876 68.525  -18.016 1.00 11.90 ? 863  GLU A OE1 1 
ATOM   6978 O  OE2 . GLU A 1 863  ? 21.607 69.016  -16.013 1.00 10.38 ? 863  GLU A OE2 1 
ATOM   6979 N  N   . ILE A 1 864  ? 26.652 68.717  -17.877 1.00 7.89  ? 864  ILE A N   1 
ATOM   6980 C  CA  . ILE A 1 864  ? 27.697 68.788  -16.836 1.00 8.18  ? 864  ILE A CA  1 
ATOM   6981 C  C   . ILE A 1 864  ? 27.685 70.178  -16.218 1.00 7.50  ? 864  ILE A C   1 
ATOM   6982 O  O   . ILE A 1 864  ? 27.692 71.207  -16.947 1.00 7.51  ? 864  ILE A O   1 
ATOM   6983 C  CB  . ILE A 1 864  ? 29.059 68.408  -17.444 1.00 8.65  ? 864  ILE A CB  1 
ATOM   6984 C  CG1 . ILE A 1 864  ? 30.154 68.360  -16.378 1.00 11.33 ? 864  ILE A CG1 1 
ATOM   6985 C  CG2 . ILE A 1 864  ? 29.434 69.262  -18.617 1.00 11.88 ? 864  ILE A CG2 1 
ATOM   6986 C  CD1 . ILE A 1 864  ? 31.273 67.373  -16.850 1.00 12.59 ? 864  ILE A CD1 1 
ATOM   6987 N  N   . MET A 1 865  ? 27.635 70.220  -14.902 1.00 6.96  ? 865  MET A N   1 
ATOM   6988 C  CA  . MET A 1 865  ? 27.586 71.488  -14.191 1.00 7.76  ? 865  MET A CA  1 
ATOM   6989 C  C   . MET A 1 865  ? 28.939 72.188  -14.243 1.00 8.44  ? 865  MET A C   1 
ATOM   6990 O  O   . MET A 1 865  ? 29.981 71.565  -14.100 1.00 8.42  ? 865  MET A O   1 
ATOM   6991 C  CB  . MET A 1 865  ? 27.123 71.255  -12.756 1.00 8.13  ? 865  MET A CB  1 
ATOM   6992 C  CG  . MET A 1 865  ? 26.511 72.508  -12.101 1.00 8.35  ? 865  MET A CG  1 
ATOM   6993 S  SD  . MET A 1 865  ? 24.889 72.907  -12.819 1.00 10.99 ? 865  MET A SD  1 
ATOM   6994 C  CE  . MET A 1 865  ? 23.908 71.702  -11.891 1.00 11.58 ? 865  MET A CE  1 
ATOM   6995 N  N   . GLN A 1 866  ? 28.911 73.513  -14.423 1.00 8.37  ? 866  GLN A N   1 
ATOM   6996 C  CA  . GLN A 1 866  ? 30.123 74.342  -14.580 1.00 7.86  ? 866  GLN A CA  1 
ATOM   6997 C  C   . GLN A 1 866  ? 30.520 75.038  -13.280 1.00 8.12  ? 866  GLN A C   1 
ATOM   6998 O  O   . GLN A 1 866  ? 31.704 75.069  -12.897 1.00 8.76  ? 866  GLN A O   1 
ATOM   6999 C  CB  . GLN A 1 866  ? 29.920 75.382  -15.692 1.00 8.86  ? 866  GLN A CB  1 
ATOM   7000 C  CG  . GLN A 1 866  ? 29.607 74.776  -17.041 1.00 9.81  ? 866  GLN A CG  1 
ATOM   7001 C  CD  . GLN A 1 866  ? 30.657 73.785  -17.463 1.00 8.94  ? 866  GLN A CD  1 
ATOM   7002 O  OE1 . GLN A 1 866  ? 31.785 74.156  -17.789 1.00 9.90  ? 866  GLN A OE1 1 
ATOM   7003 N  NE2 . GLN A 1 866  ? 30.297 72.501  -17.476 1.00 9.69  ? 866  GLN A NE2 1 
ATOM   7004 N  N   . ASP A 1 867  ? 29.538 75.650  -12.613 1.00 8.46  ? 867  ASP A N   1 
ATOM   7005 C  CA  . ASP A 1 867  ? 29.779 76.272  -11.288 1.00 8.25  ? 867  ASP A CA  1 
ATOM   7006 C  C   . ASP A 1 867  ? 28.439 76.513  -10.623 1.00 7.83  ? 867  ASP A C   1 
ATOM   7007 O  O   . ASP A 1 867  ? 27.369 76.392  -11.296 1.00 8.47  ? 867  ASP A O   1 
ATOM   7008 C  CB  . ASP A 1 867  ? 30.604 77.567  -11.404 1.00 8.83  ? 867  ASP A CB  1 
ATOM   7009 C  CG  . ASP A 1 867  ? 31.277 77.972  -10.099 1.00 8.43  ? 867  ASP A CG  1 
ATOM   7010 O  OD1 . ASP A 1 867  ? 31.147 77.313  -9.044  1.00 8.31  ? 867  ASP A OD1 1 
ATOM   7011 O  OD2 . ASP A 1 867  ? 31.996 78.992  -10.117 1.00 10.37 ? 867  ASP A OD2 1 
ATOM   7012 N  N   . ARG A 1 868  ? 28.474 76.795  -9.345  1.00 7.95  ? 868  ARG A N   1 
ATOM   7013 C  CA  . ARG A 1 868  ? 27.275 77.005  -8.582  1.00 8.27  ? 868  ARG A CA  1 
ATOM   7014 C  C   . ARG A 1 868  ? 27.604 78.019  -7.492  1.00 8.83  ? 868  ARG A C   1 
ATOM   7015 O  O   . ARG A 1 868  ? 28.637 77.952  -6.838  1.00 9.11  ? 868  ARG A O   1 
ATOM   7016 C  CB  . ARG A 1 868  ? 26.759 75.662  -8.013  1.00 8.73  ? 868  ARG A CB  1 
ATOM   7017 C  CG  . ARG A 1 868  ? 27.753 74.885  -7.141  1.00 9.69  ? 868  ARG A CG  1 
ATOM   7018 C  CD  . ARG A 1 868  ? 27.517 73.379  -7.144  1.00 8.82  ? 868  ARG A CD  1 
ATOM   7019 N  NE  . ARG A 1 868  ? 26.145 73.078  -6.715  1.00 8.42  ? 868  ARG A NE  1 
ATOM   7020 C  CZ  . ARG A 1 868  ? 25.794 72.830  -5.462  1.00 8.40  ? 868  ARG A CZ  1 
ATOM   7021 N  NH1 . ARG A 1 868  ? 26.714 72.706  -4.480  1.00 8.45  ? 868  ARG A NH1 1 
ATOM   7022 N  NH2 . ARG A 1 868  ? 24.485 72.636  -5.205  1.00 8.89  ? 868  ARG A NH2 1 
ATOM   7023 N  N   . ARG A 1 869  ? 26.674 78.950  -7.288  1.00 10.17 ? 869  ARG A N   1 
ATOM   7024 C  CA  . ARG A 1 869  ? 26.825 80.018  -6.303  1.00 10.53 ? 869  ARG A CA  1 
ATOM   7025 C  C   . ARG A 1 869  ? 25.554 80.027  -5.497  1.00 11.18 ? 869  ARG A C   1 
ATOM   7026 O  O   . ARG A 1 869  ? 24.473 80.221  -6.066  1.00 12.16 ? 869  ARG A O   1 
ATOM   7027 C  CB  . ARG A 1 869  ? 27.060 81.358  -7.001  1.00 11.20 ? 869  ARG A CB  1 
ATOM   7028 C  CG  . ARG A 1 869  ? 27.248 82.512  -6.046  1.00 11.98 ? 869  ARG A CG  1 
ATOM   7029 C  CD  . ARG A 1 869  ? 27.621 83.790  -6.791  1.00 13.88 ? 869  ARG A CD  1 
ATOM   7030 N  NE  . ARG A 1 869  ? 27.805 84.950  -5.897  1.00 16.77 ? 869  ARG A NE  1 
ATOM   7031 C  CZ  . ARG A 1 869  ? 28.950 85.293  -5.340  1.00 16.27 ? 869  ARG A CZ  1 
ATOM   7032 N  NH1 . ARG A 1 869  ? 30.041 84.563  -5.523  1.00 16.19 ? 869  ARG A NH1 1 
ATOM   7033 N  NH2 . ARG A 1 869  ? 29.010 86.388  -4.575  1.00 18.98 ? 869  ARG A NH2 1 
ATOM   7034 N  N   . LEU A 1 870  ? 25.695 79.752  -4.210  1.00 12.44 ? 870  LEU A N   1 
ATOM   7035 C  CA  . LEU A 1 870  ? 24.565 79.471  -3.311  1.00 13.11 ? 870  LEU A CA  1 
ATOM   7036 C  C   . LEU A 1 870  ? 24.640 80.306  -2.067  1.00 13.14 ? 870  LEU A C   1 
ATOM   7037 O  O   . LEU A 1 870  ? 25.614 80.283  -1.338  1.00 13.04 ? 870  LEU A O   1 
ATOM   7038 C  CB  . LEU A 1 870  ? 24.567 77.998  -2.915  1.00 13.06 ? 870  LEU A CB  1 
ATOM   7039 C  CG  . LEU A 1 870  ? 24.623 77.166  -4.200  1.00 16.39 ? 870  LEU A CG  1 
ATOM   7040 C  CD1 . LEU A 1 870  ? 25.236 75.826  -3.973  1.00 19.47 ? 870  LEU A CD1 1 
ATOM   7041 C  CD2 . LEU A 1 870  ? 23.302 77.126  -4.973  1.00 13.53 ? 870  LEU A CD2 1 
ATOM   7042 N  N   . ALA A 1 871  ? 23.535 80.998  -1.800  1.00 13.66 ? 871  ALA A N   1 
ATOM   7043 C  CA  . ALA A 1 871  ? 23.509 81.939  -0.712  1.00 15.10 ? 871  ALA A CA  1 
ATOM   7044 C  C   . ALA A 1 871  ? 23.323 81.284  0.664   1.00 16.25 ? 871  ALA A C   1 
ATOM   7045 O  O   . ALA A 1 871  ? 23.726 81.827  1.698   1.00 18.35 ? 871  ALA A O   1 
ATOM   7046 C  CB  . ALA A 1 871  ? 22.396 83.001  -0.934  1.00 15.67 ? 871  ALA A CB  1 
ATOM   7047 N  N   . SER A 1 872  ? 22.720 80.106  0.670   1.00 15.95 ? 872  SER A N   1 
ATOM   7048 C  CA  . SER A 1 872  ? 22.296 79.476  1.908   1.00 16.80 ? 872  SER A CA  1 
ATOM   7049 C  C   . SER A 1 872  ? 23.178 78.316  2.322   1.00 15.15 ? 872  SER A C   1 
ATOM   7050 O  O   . SER A 1 872  ? 23.800 77.654  1.472   1.00 16.27 ? 872  SER A O   1 
ATOM   7051 C  CB  . SER A 1 872  ? 20.854 78.986  1.747   1.00 18.37 ? 872  SER A CB  1 
ATOM   7052 O  OG  . SER A 1 872  ? 19.988 80.098  1.570   1.00 22.74 ? 872  SER A OG  1 
ATOM   7053 N  N   . ASP A 1 873  ? 23.239 78.100  3.629   1.00 15.47 ? 873  ASP A N   1 
ATOM   7054 C  CA  . ASP A 1 873  ? 23.788 76.869  4.207   1.00 14.94 ? 873  ASP A CA  1 
ATOM   7055 C  C   . ASP A 1 873  ? 22.772 75.728  4.028   1.00 14.76 ? 873  ASP A C   1 
ATOM   7056 O  O   . ASP A 1 873  ? 21.564 75.960  4.046   1.00 16.29 ? 873  ASP A O   1 
ATOM   7057 C  CB  . ASP A 1 873  ? 24.095 77.088  5.680   1.00 15.64 ? 873  ASP A CB  1 
ATOM   7058 C  CG  . ASP A 1 873  ? 24.574 75.830  6.356   1.00 15.64 ? 873  ASP A CG  1 
ATOM   7059 O  OD1 . ASP A 1 873  ? 25.663 75.328  5.976   1.00 16.92 ? 873  ASP A OD1 1 
ATOM   7060 O  OD2 . ASP A 1 873  ? 23.904 75.261  7.239   1.00 17.70 ? 873  ASP A OD2 1 
ATOM   7061 N  N   . ASP A 1 874  ? 23.278 74.504  3.829   1.00 13.01 ? 874  ASP A N   1 
ATOM   7062 C  CA  . ASP A 1 874  ? 22.430 73.329  3.610   1.00 12.04 ? 874  ASP A CA  1 
ATOM   7063 C  C   . ASP A 1 874  ? 22.419 72.349  4.786   1.00 12.16 ? 874  ASP A C   1 
ATOM   7064 O  O   . ASP A 1 874  ? 22.191 71.142  4.601   1.00 13.58 ? 874  ASP A O   1 
ATOM   7065 C  CB  . ASP A 1 874  ? 22.774 72.623  2.295   1.00 11.70 ? 874  ASP A CB  1 
ATOM   7066 C  CG  . ASP A 1 874  ? 24.249 72.281  2.161   1.00 10.42 ? 874  ASP A CG  1 
ATOM   7067 O  OD1 . ASP A 1 874  ? 25.070 72.605  3.081   1.00 12.88 ? 874  ASP A OD1 1 
ATOM   7068 O  OD2 . ASP A 1 874  ? 24.594 71.683  1.130   1.00 10.34 ? 874  ASP A OD2 1 
ATOM   7069 N  N   . GLU A 1 875  ? 22.669 72.855  5.991   1.00 12.31 ? 875  GLU A N   1 
ATOM   7070 C  CA  A GLU A 1 875  ? 22.431 72.142  7.264   0.50 12.93 ? 875  GLU A CA  1 
ATOM   7071 C  CA  B GLU A 1 875  ? 22.344 72.076  7.206   0.50 12.53 ? 875  GLU A CA  1 
ATOM   7072 C  C   . GLU A 1 875  ? 23.235 70.860  7.442   1.00 13.11 ? 875  GLU A C   1 
ATOM   7073 O  O   . GLU A 1 875  ? 22.847 69.950  8.161   1.00 13.47 ? 875  GLU A O   1 
ATOM   7074 C  CB  A GLU A 1 875  ? 20.921 71.929  7.525   0.50 13.84 ? 875  GLU A CB  1 
ATOM   7075 C  CB  B GLU A 1 875  ? 20.867 71.586  7.200   0.50 12.62 ? 875  GLU A CB  1 
ATOM   7076 C  CG  A GLU A 1 875  ? 20.093 73.180  7.240   0.50 16.05 ? 875  GLU A CG  1 
ATOM   7077 C  CG  B GLU A 1 875  ? 19.788 72.655  7.063   0.50 13.27 ? 875  GLU A CG  1 
ATOM   7078 C  CD  A GLU A 1 875  ? 18.762 73.217  7.963   0.50 18.96 ? 875  GLU A CD  1 
ATOM   7079 C  CD  B GLU A 1 875  ? 18.392 72.107  7.341   0.50 13.45 ? 875  GLU A CD  1 
ATOM   7080 O  OE1 A GLU A 1 875  ? 18.758 73.161  9.212   0.50 22.22 ? 875  GLU A OE1 1 
ATOM   7081 O  OE1 B GLU A 1 875  ? 17.976 71.127  6.682   0.50 14.65 ? 875  GLU A OE1 1 
ATOM   7082 O  OE2 A GLU A 1 875  ? 17.722 73.323  7.281   0.50 19.47 ? 875  GLU A OE2 1 
ATOM   7083 O  OE2 B GLU A 1 875  ? 17.706 72.657  8.239   0.50 18.51 ? 875  GLU A OE2 1 
ATOM   7084 N  N   . ARG A 1 876  ? 24.413 70.836  6.829   1.00 11.73 ? 876  ARG A N   1 
ATOM   7085 C  CA  . ARG A 1 876  ? 25.322 69.676  6.983   1.00 11.66 ? 876  ARG A CA  1 
ATOM   7086 C  C   . ARG A 1 876  ? 26.590 70.032  7.776   1.00 12.03 ? 876  ARG A C   1 
ATOM   7087 O  O   . ARG A 1 876  ? 27.532 69.227  7.850   1.00 12.45 ? 876  ARG A O   1 
ATOM   7088 C  CB  . ARG A 1 876  ? 25.671 69.044  5.619   1.00 11.65 ? 876  ARG A CB  1 
ATOM   7089 C  CG  . ARG A 1 876  ? 24.434 68.484  4.894   1.00 11.57 ? 876  ARG A CG  1 
ATOM   7090 C  CD  . ARG A 1 876  ? 23.656 67.552  5.785   1.00 12.13 ? 876  ARG A CD  1 
ATOM   7091 N  NE  . ARG A 1 876  ? 22.568 66.812  5.149   1.00 11.59 ? 876  ARG A NE  1 
ATOM   7092 C  CZ  . ARG A 1 876  ? 21.374 67.323  4.897   1.00 12.09 ? 876  ARG A CZ  1 
ATOM   7093 N  NH1 . ARG A 1 876  ? 21.140 68.621  5.113   1.00 11.15 ? 876  ARG A NH1 1 
ATOM   7094 N  NH2 . ARG A 1 876  ? 20.418 66.541  4.419   1.00 11.23 ? 876  ARG A NH2 1 
ATOM   7095 N  N   . GLY A 1 877  ? 26.623 71.212  8.390   1.00 12.32 ? 877  GLY A N   1 
ATOM   7096 C  CA  . GLY A 1 877  ? 27.701 71.565  9.293   1.00 11.95 ? 877  GLY A CA  1 
ATOM   7097 C  C   . GLY A 1 877  ? 28.654 72.640  8.813   1.00 12.00 ? 877  GLY A C   1 
ATOM   7098 O  O   . GLY A 1 877  ? 29.456 73.155  9.608   1.00 12.94 ? 877  GLY A O   1 
ATOM   7099 N  N   . LEU A 1 878  ? 28.571 72.994  7.538   1.00 11.93 ? 878  LEU A N   1 
ATOM   7100 C  CA  . LEU A 1 878  ? 29.508 73.973  6.996   1.00 13.32 ? 878  LEU A CA  1 
ATOM   7101 C  C   . LEU A 1 878  ? 29.258 75.389  7.530   1.00 14.20 ? 878  LEU A C   1 
ATOM   7102 O  O   . LEU A 1 878  ? 30.216 76.141  7.772   1.00 14.75 ? 878  LEU A O   1 
ATOM   7103 C  CB  . LEU A 1 878  ? 29.468 73.922  5.469   1.00 12.94 ? 878  LEU A CB  1 
ATOM   7104 C  CG  . LEU A 1 878  ? 30.288 74.983  4.714   1.00 12.45 ? 878  LEU A CG  1 
ATOM   7105 C  CD1 . LEU A 1 878  ? 31.761 75.015  5.147   1.00 12.89 ? 878  LEU A CD1 1 
ATOM   7106 C  CD2 . LEU A 1 878  ? 30.188 74.787  3.216   1.00 12.62 ? 878  LEU A CD2 1 
ATOM   7107 N  N   . GLY A 1 879  ? 27.981 75.746  7.687   1.00 13.51 ? 879  GLY A N   1 
ATOM   7108 C  CA  . GLY A 1 879  ? 27.605 77.047  8.238   1.00 15.12 ? 879  GLY A CA  1 
ATOM   7109 C  C   . GLY A 1 879  ? 27.907 78.236  7.338   1.00 16.74 ? 879  GLY A C   1 
ATOM   7110 O  O   . GLY A 1 879  ? 28.104 79.357  7.808   1.00 18.31 ? 879  GLY A O   1 
ATOM   7111 N  N   . GLN A 1 880  ? 27.943 77.996  6.034   1.00 15.18 ? 880  GLN A N   1 
ATOM   7112 C  CA  . GLN A 1 880  ? 27.989 79.074  5.052   1.00 15.36 ? 880  GLN A CA  1 
ATOM   7113 C  C   . GLN A 1 880  ? 27.447 78.536  3.728   1.00 15.05 ? 880  GLN A C   1 
ATOM   7114 O  O   . GLN A 1 880  ? 27.399 77.314  3.520   1.00 15.70 ? 880  GLN A O   1 
ATOM   7115 C  CB  . GLN A 1 880  ? 29.432 79.624  4.894   1.00 15.10 ? 880  GLN A CB  1 
ATOM   7116 C  CG  . GLN A 1 880  ? 30.496 78.598  4.441   1.00 16.12 ? 880  GLN A CG  1 
ATOM   7117 C  CD  . GLN A 1 880  ? 31.750 79.241  3.880   1.00 15.29 ? 880  GLN A CD  1 
ATOM   7118 O  OE1 . GLN A 1 880  ? 32.677 79.533  4.601   1.00 15.00 ? 880  GLN A OE1 1 
ATOM   7119 N  NE2 . GLN A 1 880  ? 31.778 79.427  2.579   1.00 17.36 ? 880  GLN A NE2 1 
ATOM   7120 N  N   . GLY A 1 881  ? 27.078 79.441  2.836   1.00 15.93 ? 881  GLY A N   1 
ATOM   7121 C  CA  . GLY A 1 881  ? 26.831 79.073  1.450   1.00 16.00 ? 881  GLY A CA  1 
ATOM   7122 C  C   . GLY A 1 881  ? 28.122 78.960  0.652   1.00 14.84 ? 881  GLY A C   1 
ATOM   7123 O  O   . GLY A 1 881  ? 29.235 78.847  1.218   1.00 15.80 ? 881  GLY A O   1 
ATOM   7124 N  N   . VAL A 1 882  ? 27.973 79.017  -0.671  1.00 13.57 ? 882  VAL A N   1 
ATOM   7125 C  CA  . VAL A 1 882  ? 29.120 79.037  -1.553  1.00 12.69 ? 882  VAL A CA  1 
ATOM   7126 C  C   . VAL A 1 882  ? 29.052 80.365  -2.305  1.00 12.60 ? 882  VAL A C   1 
ATOM   7127 O  O   . VAL A 1 882  ? 28.297 80.512  -3.259  1.00 12.28 ? 882  VAL A O   1 
ATOM   7128 C  CB  . VAL A 1 882  ? 29.091 77.836  -2.495  1.00 12.97 ? 882  VAL A CB  1 
ATOM   7129 C  CG1 . VAL A 1 882  ? 30.248 77.879  -3.467  1.00 13.87 ? 882  VAL A CG1 1 
ATOM   7130 C  CG2 . VAL A 1 882  ? 29.142 76.525  -1.688  1.00 14.48 ? 882  VAL A CG2 1 
ATOM   7131 N  N   . LEU A 1 883  ? 29.835 81.332  -1.815  1.00 12.68 ? 883  LEU A N   1 
ATOM   7132 C  CA  . LEU A 1 883  ? 29.796 82.703  -2.361  1.00 13.23 ? 883  LEU A CA  1 
ATOM   7133 C  C   . LEU A 1 883  ? 31.190 83.211  -2.683  1.00 14.63 ? 883  LEU A C   1 
ATOM   7134 O  O   . LEU A 1 883  ? 31.375 84.421  -2.846  1.00 16.83 ? 883  LEU A O   1 
ATOM   7135 C  CB  . LEU A 1 883  ? 29.085 83.692  -1.409  1.00 14.73 ? 883  LEU A CB  1 
ATOM   7136 C  CG  . LEU A 1 883  ? 27.588 83.419  -1.181  1.00 14.92 ? 883  LEU A CG  1 
ATOM   7137 C  CD1 . LEU A 1 883  ? 26.977 84.302  -0.055  1.00 17.02 ? 883  LEU A CD1 1 
ATOM   7138 C  CD2 . LEU A 1 883  ? 26.774 83.588  -2.462  1.00 16.14 ? 883  LEU A CD2 1 
ATOM   7139 N  N   . ASP A 1 884  ? 32.144 82.303  -2.795  1.00 12.48 ? 884  ASP A N   1 
ATOM   7140 C  CA  . ASP A 1 884  ? 33.561 82.598  -3.013  1.00 11.74 ? 884  ASP A CA  1 
ATOM   7141 C  C   . ASP A 1 884  ? 34.047 82.119  -4.372  1.00 11.78 ? 884  ASP A C   1 
ATOM   7142 O  O   . ASP A 1 884  ? 35.227 81.837  -4.554  1.00 12.05 ? 884  ASP A O   1 
ATOM   7143 C  CB  . ASP A 1 884  ? 34.437 82.000  -1.908  1.00 12.96 ? 884  ASP A CB  1 
ATOM   7144 C  CG  . ASP A 1 884  ? 34.233 80.496  -1.697  1.00 13.62 ? 884  ASP A CG  1 
ATOM   7145 O  OD1 . ASP A 1 884  ? 33.427 79.817  -2.416  1.00 13.17 ? 884  ASP A OD1 1 
ATOM   7146 O  OD2 . ASP A 1 884  ? 34.872 79.942  -0.755  1.00 16.10 ? 884  ASP A OD2 1 
ATOM   7147 N  N   . ASN A 1 885  ? 33.141 82.055  -5.334  1.00 10.85 ? 885  ASN A N   1 
ATOM   7148 C  CA  . ASN A 1 885  ? 33.471 81.667  -6.682  1.00 11.25 ? 885  ASN A CA  1 
ATOM   7149 C  C   . ASN A 1 885  ? 34.563 82.514  -7.277  1.00 12.36 ? 885  ASN A C   1 
ATOM   7150 O  O   . ASN A 1 885  ? 34.684 83.711  -6.958  1.00 12.60 ? 885  ASN A O   1 
ATOM   7151 C  CB  . ASN A 1 885  ? 32.238 81.803  -7.562  1.00 10.91 ? 885  ASN A CB  1 
ATOM   7152 C  CG  . ASN A 1 885  ? 31.044 81.132  -6.969  1.00 10.98 ? 885  ASN A CG  1 
ATOM   7153 O  OD1 . ASN A 1 885  ? 30.391 81.655  -6.081  1.00 12.54 ? 885  ASN A OD1 1 
ATOM   7154 N  ND2 . ASN A 1 885  ? 30.754 79.921  -7.452  1.00 10.98 ? 885  ASN A ND2 1 
ATOM   7155 N  N   . LYS A 1 886  ? 35.338 81.923  -8.169  1.00 11.81 ? 886  LYS A N   1 
ATOM   7156 C  CA  . LYS A 1 886  ? 36.350 82.672  -8.896  1.00 13.86 ? 886  LYS A CA  1 
ATOM   7157 C  C   . LYS A 1 886  ? 36.443 82.085  -10.292 1.00 11.98 ? 886  LYS A C   1 
ATOM   7158 O  O   . LYS A 1 886  ? 36.052 80.927  -10.529 1.00 11.47 ? 886  LYS A O   1 
ATOM   7159 C  CB  . LYS A 1 886  ? 37.692 82.629  -8.166  1.00 15.64 ? 886  LYS A CB  1 
ATOM   7160 C  CG  . LYS A 1 886  ? 38.208 81.217  -7.957  1.00 16.71 ? 886  LYS A CG  1 
ATOM   7161 C  CD  . LYS A 1 886  ? 39.279 81.094  -6.832  1.00 17.83 ? 886  LYS A CD  1 
ATOM   7162 C  CE  . LYS A 1 886  ? 40.665 81.409  -7.378  1.00 19.21 ? 886  LYS A CE  1 
ATOM   7163 N  NZ  . LYS A 1 886  ? 41.778 81.691  -6.400  1.00 20.57 ? 886  LYS A NZ  1 
ATOM   7164 N  N   . PRO A 1 887  ? 36.899 82.857  -11.251 1.00 9.78  ? 887  PRO A N   1 
ATOM   7165 C  CA  . PRO A 1 887  ? 36.992 82.360  -12.624 1.00 9.99  ? 887  PRO A CA  1 
ATOM   7166 C  C   . PRO A 1 887  ? 37.823 81.096  -12.731 1.00 9.93  ? 887  PRO A C   1 
ATOM   7167 O  O   . PRO A 1 887  ? 38.864 80.960  -12.112 1.00 10.14 ? 887  PRO A O   1 
ATOM   7168 C  CB  . PRO A 1 887  ? 37.631 83.533  -13.388 1.00 10.95 ? 887  PRO A CB  1 
ATOM   7169 C  CG  . PRO A 1 887  ? 37.209 84.760  -12.594 1.00 12.05 ? 887  PRO A CG  1 
ATOM   7170 C  CD  . PRO A 1 887  ? 37.207 84.306  -11.164 1.00 10.71 ? 887  PRO A CD  1 
ATOM   7171 N  N   . VAL A 1 888  ? 37.316 80.150  -13.508 1.00 8.87  ? 888  VAL A N   1 
ATOM   7172 C  CA  . VAL A 1 888  ? 37.979 78.874  -13.704 1.00 8.59  ? 888  VAL A CA  1 
ATOM   7173 C  C   . VAL A 1 888  ? 37.898 78.511  -15.166 1.00 7.94  ? 888  VAL A C   1 
ATOM   7174 O  O   . VAL A 1 888  ? 36.851 78.734  -15.839 1.00 9.24  ? 888  VAL A O   1 
ATOM   7175 C  CB  . VAL A 1 888  ? 37.334 77.761  -12.814 1.00 9.20  ? 888  VAL A CB  1 
ATOM   7176 C  CG1 . VAL A 1 888  ? 35.805 77.661  -13.033 1.00 10.48 ? 888  VAL A CG1 1 
ATOM   7177 C  CG2 . VAL A 1 888  ? 37.989 76.422  -13.091 1.00 8.98  ? 888  VAL A CG2 1 
ATOM   7178 N  N   . LEU A 1 889  ? 38.970 77.954  -15.702 1.00 6.92  ? 889  LEU A N   1 
ATOM   7179 C  CA  . LEU A 1 889  ? 38.969 77.457  -17.075 1.00 8.28  ? 889  LEU A CA  1 
ATOM   7180 C  C   . LEU A 1 889  ? 38.788 75.934  -17.096 1.00 8.22  ? 889  LEU A C   1 
ATOM   7181 O  O   . LEU A 1 889  ? 39.696 75.176  -16.772 1.00 8.76  ? 889  LEU A O   1 
ATOM   7182 C  CB  . LEU A 1 889  ? 40.283 77.843  -17.762 1.00 8.94  ? 889  LEU A CB  1 
ATOM   7183 C  CG  . LEU A 1 889  ? 40.384 77.457  -19.242 1.00 10.78 ? 889  LEU A CG  1 
ATOM   7184 C  CD1 . LEU A 1 889  ? 39.430 78.300  -20.084 1.00 11.94 ? 889  LEU A CD1 1 
ATOM   7185 C  CD2 . LEU A 1 889  ? 41.817 77.549  -19.736 1.00 14.17 ? 889  LEU A CD2 1 
ATOM   7186 N  N   . HIS A 1 890  ? 37.578 75.515  -17.417 1.00 7.04  ? 890  HIS A N   1 
ATOM   7187 C  CA  . HIS A 1 890  ? 37.243 74.092  -17.589 1.00 7.07  ? 890  HIS A CA  1 
ATOM   7188 C  C   . HIS A 1 890  ? 37.627 73.615  -18.962 1.00 7.68  ? 890  HIS A C   1 
ATOM   7189 O  O   . HIS A 1 890  ? 37.418 74.351  -19.957 1.00 8.03  ? 890  HIS A O   1 
ATOM   7190 C  CB  . HIS A 1 890  ? 35.754 73.874  -17.380 1.00 7.34  ? 890  HIS A CB  1 
ATOM   7191 C  CG  . HIS A 1 890  ? 35.327 74.026  -15.967 1.00 7.58  ? 890  HIS A CG  1 
ATOM   7192 N  ND1 . HIS A 1 890  ? 36.147 73.675  -14.903 1.00 9.60  ? 890  HIS A ND1 1 
ATOM   7193 C  CD2 . HIS A 1 890  ? 34.158 74.451  -15.433 1.00 9.68  ? 890  HIS A CD2 1 
ATOM   7194 C  CE1 . HIS A 1 890  ? 35.482 73.880  -13.779 1.00 10.51 ? 890  HIS A CE1 1 
ATOM   7195 N  NE2 . HIS A 1 890  ? 34.271 74.347  -14.068 1.00 9.24  ? 890  HIS A NE2 1 
ATOM   7196 N  N   . ILE A 1 891  ? 38.159 72.396  -19.057 1.00 6.43  ? 891  ILE A N   1 
ATOM   7197 C  CA  . ILE A 1 891  ? 38.582 71.851  -20.347 1.00 6.97  ? 891  ILE A CA  1 
ATOM   7198 C  C   . ILE A 1 891  ? 37.922 70.509  -20.614 1.00 6.45  ? 891  ILE A C   1 
ATOM   7199 O  O   . ILE A 1 891  ? 37.649 69.743  -19.664 1.00 6.30  ? 891  ILE A O   1 
ATOM   7200 C  CB  . ILE A 1 891  ? 40.115 71.766  -20.472 1.00 7.08  ? 891  ILE A CB  1 
ATOM   7201 C  CG1 . ILE A 1 891  ? 40.723 70.774  -19.497 1.00 8.97  ? 891  ILE A CG1 1 
ATOM   7202 C  CG2 . ILE A 1 891  ? 40.718 73.172  -20.220 1.00 9.87  ? 891  ILE A CG2 1 
ATOM   7203 C  CD1 . ILE A 1 891  ? 42.244 70.600  -19.708 1.00 9.67  ? 891  ILE A CD1 1 
ATOM   7204 N  N   . TYR A 1 892  ? 37.660 70.233  -21.880 1.00 6.39  ? 892  TYR A N   1 
ATOM   7205 C  CA  . TYR A 1 892  ? 36.963 69.008  -22.299 1.00 6.03  ? 892  TYR A CA  1 
ATOM   7206 C  C   . TYR A 1 892  ? 37.423 68.573  -23.666 1.00 6.19  ? 892  TYR A C   1 
ATOM   7207 O  O   . TYR A 1 892  ? 37.993 69.342  -24.438 1.00 7.02  ? 892  TYR A O   1 
ATOM   7208 C  CB  . TYR A 1 892  ? 35.448 69.249  -22.440 1.00 6.92  ? 892  TYR A CB  1 
ATOM   7209 C  CG  . TYR A 1 892  ? 34.796 69.909  -21.260 1.00 6.28  ? 892  TYR A CG  1 
ATOM   7210 C  CD1 . TYR A 1 892  ? 34.737 71.308  -21.136 1.00 6.72  ? 892  TYR A CD1 1 
ATOM   7211 C  CD2 . TYR A 1 892  ? 34.231 69.148  -20.219 1.00 6.55  ? 892  TYR A CD2 1 
ATOM   7212 C  CE1 . TYR A 1 892  ? 34.144 71.911  -20.063 1.00 7.53  ? 892  TYR A CE1 1 
ATOM   7213 C  CE2 . TYR A 1 892  ? 33.643 69.733  -19.135 1.00 7.73  ? 892  TYR A CE2 1 
ATOM   7214 C  CZ  . TYR A 1 892  ? 33.606 71.108  -19.053 1.00 6.94  ? 892  TYR A CZ  1 
ATOM   7215 O  OH  . TYR A 1 892  ? 33.004 71.656  -17.949 1.00 8.52  ? 892  TYR A OH  1 
ATOM   7216 N  N   . ARG A 1 893  ? 37.145 67.310  -23.982 1.00 6.31  ? 893  ARG A N   1 
ATOM   7217 C  CA  . ARG A 1 893  ? 37.213 66.834  -25.381 1.00 7.50  ? 893  ARG A CA  1 
ATOM   7218 C  C   . ARG A 1 893  ? 35.880 66.201  -25.705 1.00 7.68  ? 893  ARG A C   1 
ATOM   7219 O  O   . ARG A 1 893  ? 35.249 65.593  -24.855 1.00 7.96  ? 893  ARG A O   1 
ATOM   7220 C  CB  . ARG A 1 893  ? 38.323 65.807  -25.588 1.00 7.53  ? 893  ARG A CB  1 
ATOM   7221 C  CG  . ARG A 1 893  ? 39.737 66.336  -25.356 1.00 8.26  ? 893  ARG A CG  1 
ATOM   7222 C  CD  . ARG A 1 893  ? 40.211 67.405  -26.384 1.00 9.54  ? 893  ARG A CD  1 
ATOM   7223 N  NE  . ARG A 1 893  ? 40.333 66.884  -27.736 1.00 9.82  ? 893  ARG A NE  1 
ATOM   7224 C  CZ  . ARG A 1 893  ? 41.408 66.269  -28.175 1.00 9.47  ? 893  ARG A CZ  1 
ATOM   7225 N  NH1 . ARG A 1 893  ? 42.461 66.084  -27.360 1.00 11.79 ? 893  ARG A NH1 1 
ATOM   7226 N  NH2 . ARG A 1 893  ? 41.481 65.833  -29.426 1.00 12.20 ? 893  ARG A NH2 1 
ATOM   7227 N  N   . LEU A 1 894  ? 35.457 66.365  -26.969 1.00 8.48  ? 894  LEU A N   1 
ATOM   7228 C  CA  . LEU A 1 894  ? 34.147 65.876  -27.418 1.00 9.84  ? 894  LEU A CA  1 
ATOM   7229 C  C   . LEU A 1 894  ? 34.367 64.910  -28.558 1.00 9.56  ? 894  LEU A C   1 
ATOM   7230 O  O   . LEU A 1 894  ? 34.900 65.284  -29.597 1.00 10.73 ? 894  LEU A O   1 
ATOM   7231 C  CB  . LEU A 1 894  ? 33.300 67.056  -27.883 1.00 10.31 ? 894  LEU A CB  1 
ATOM   7232 C  CG  . LEU A 1 894  ? 31.859 66.689  -28.234 1.00 11.83 ? 894  LEU A CG  1 
ATOM   7233 C  CD1 . LEU A 1 894  ? 31.116 66.192  -27.015 1.00 15.85 ? 894  LEU A CD1 1 
ATOM   7234 C  CD2 . LEU A 1 894  ? 31.155 67.883  -28.840 1.00 14.95 ? 894  LEU A CD2 1 
ATOM   7235 N  N   . VAL A 1 895  ? 34.010 63.631  -28.333 1.00 9.87  ? 895  VAL A N   1 
ATOM   7236 C  CA  . VAL A 1 895  ? 34.253 62.575  -29.309 1.00 10.92 ? 895  VAL A CA  1 
ATOM   7237 C  C   . VAL A 1 895  ? 32.940 61.947  -29.779 1.00 11.52 ? 895  VAL A C   1 
ATOM   7238 O  O   . VAL A 1 895  ? 32.261 61.261  -29.028 1.00 10.70 ? 895  VAL A O   1 
ATOM   7239 C  CB  . VAL A 1 895  ? 35.160 61.481  -28.687 1.00 10.62 ? 895  VAL A CB  1 
ATOM   7240 C  CG1 . VAL A 1 895  ? 35.548 60.469  -29.749 1.00 13.48 ? 895  VAL A CG1 1 
ATOM   7241 C  CG2 . VAL A 1 895  ? 36.408 62.139  -28.072 1.00 13.17 ? 895  VAL A CG2 1 
ATOM   7242 N  N   . LEU A 1 896  ? 32.576 62.216  -31.034 1.00 11.45 ? 896  LEU A N   1 
ATOM   7243 C  CA  . LEU A 1 896  ? 31.419 61.598  -31.695 1.00 11.88 ? 896  LEU A CA  1 
ATOM   7244 C  C   . LEU A 1 896  ? 31.962 60.458  -32.531 1.00 11.94 ? 896  LEU A C   1 
ATOM   7245 O  O   . LEU A 1 896  ? 32.915 60.617  -33.289 1.00 12.85 ? 896  LEU A O   1 
ATOM   7246 C  CB  . LEU A 1 896  ? 30.739 62.625  -32.613 1.00 11.82 ? 896  LEU A CB  1 
ATOM   7247 C  CG  . LEU A 1 896  ? 29.568 62.004  -33.425 1.00 13.28 ? 896  LEU A CG  1 
ATOM   7248 C  CD1 . LEU A 1 896  ? 28.455 61.712  -32.509 1.00 14.32 ? 896  LEU A CD1 1 
ATOM   7249 C  CD2 . LEU A 1 896  ? 29.111 62.998  -34.476 1.00 14.61 ? 896  LEU A CD2 1 
ATOM   7250 N  N   . GLU A 1 897  ? 31.379 59.259  -32.370 1.00 11.57 ? 897  GLU A N   1 
ATOM   7251 C  CA  . GLU A 1 897  ? 31.921 58.078  -33.053 1.00 12.82 ? 897  GLU A CA  1 
ATOM   7252 C  C   . GLU A 1 897  ? 30.787 57.163  -33.504 1.00 12.76 ? 897  GLU A C   1 
ATOM   7253 O  O   . GLU A 1 897  ? 29.764 57.079  -32.855 1.00 12.42 ? 897  GLU A O   1 
ATOM   7254 C  CB  . GLU A 1 897  ? 32.810 57.279  -32.098 1.00 14.14 ? 897  GLU A CB  1 
ATOM   7255 C  CG  . GLU A 1 897  ? 33.985 58.034  -31.502 1.00 16.72 ? 897  GLU A CG  1 
ATOM   7256 C  CD  . GLU A 1 897  ? 34.697 57.203  -30.439 1.00 15.35 ? 897  GLU A CD  1 
ATOM   7257 O  OE1 . GLU A 1 897  ? 34.095 56.997  -29.347 1.00 20.74 ? 897  GLU A OE1 1 
ATOM   7258 O  OE2 . GLU A 1 897  ? 35.865 56.843  -30.745 1.00 22.49 ? 897  GLU A OE2 1 
ATOM   7259 N  N   . LYS A 1 898  ? 31.042 56.465  -34.607 1.00 13.85 ? 898  LYS A N   1 
ATOM   7260 C  CA  . LYS A 1 898  ? 30.227 55.323  -35.013 1.00 15.94 ? 898  LYS A CA  1 
ATOM   7261 C  C   . LYS A 1 898  ? 30.666 54.061  -34.267 1.00 15.39 ? 898  LYS A C   1 
ATOM   7262 O  O   . LYS A 1 898  ? 31.849 53.696  -34.262 1.00 18.27 ? 898  LYS A O   1 
ATOM   7263 C  CB  . LYS A 1 898  ? 30.375 55.120  -36.515 1.00 16.26 ? 898  LYS A CB  1 
ATOM   7264 C  CG  . LYS A 1 898  ? 29.783 56.242  -37.370 1.00 21.33 ? 898  LYS A CG  1 
ATOM   7265 C  CD  . LYS A 1 898  ? 28.531 56.914  -36.756 1.00 27.14 ? 898  LYS A CD  1 
ATOM   7266 C  CE  . LYS A 1 898  ? 27.176 56.259  -37.101 1.00 28.76 ? 898  LYS A CE  1 
ATOM   7267 N  NZ  . LYS A 1 898  ? 27.132 54.762  -37.136 1.00 32.01 ? 898  LYS A NZ  1 
ATOM   7268 N  N   . VAL A 1 899  ? 29.716 53.416  -33.607 1.00 15.64 ? 899  VAL A N   1 
ATOM   7269 C  CA  . VAL A 1 899  ? 30.054 52.268  -32.761 1.00 15.26 ? 899  VAL A CA  1 
ATOM   7270 C  C   . VAL A 1 899  ? 29.332 50.960  -33.116 1.00 15.35 ? 899  VAL A C   1 
ATOM   7271 O  O   . VAL A 1 899  ? 29.464 49.965  -32.408 1.00 15.36 ? 899  VAL A O   1 
ATOM   7272 C  CB  . VAL A 1 899  ? 29.850 52.573  -31.250 1.00 15.06 ? 899  VAL A CB  1 
ATOM   7273 C  CG1 . VAL A 1 899  ? 30.878 53.610  -30.743 1.00 15.92 ? 899  VAL A CG1 1 
ATOM   7274 C  CG2 . VAL A 1 899  ? 28.470 53.055  -30.974 1.00 14.49 ? 899  VAL A CG2 1 
ATOM   7275 N  N   . ASN A 1 900  ? 28.578 50.953  -34.215 1.00 15.98 ? 900  ASN A N   1 
ATOM   7276 C  CA  . ASN A 1 900  ? 27.876 49.721  -34.601 1.00 17.20 ? 900  ASN A CA  1 
ATOM   7277 C  C   . ASN A 1 900  ? 28.818 48.533  -34.851 1.00 16.49 ? 900  ASN A C   1 
ATOM   7278 O  O   . ASN A 1 900  ? 28.383 47.373  -34.743 1.00 18.76 ? 900  ASN A O   1 
ATOM   7279 C  CB  . ASN A 1 900  ? 26.997 49.937  -35.843 1.00 17.68 ? 900  ASN A CB  1 
ATOM   7280 C  CG  . ASN A 1 900  ? 27.764 50.474  -37.002 1.00 20.38 ? 900  ASN A CG  1 
ATOM   7281 O  OD1 . ASN A 1 900  ? 28.307 51.562  -36.946 1.00 23.49 ? 900  ASN A OD1 1 
ATOM   7282 N  ND2 . ASN A 1 900  ? 27.806 49.708  -38.099 1.00 25.50 ? 900  ASN A ND2 1 
ATOM   7283 N  N   . ASN A 1 901  ? 30.074 48.787  -35.188 1.00 15.85 ? 901  ASN A N   1 
ATOM   7284 C  CA  . ASN A 1 901  ? 31.035 47.701  -35.423 1.00 16.29 ? 901  ASN A CA  1 
ATOM   7285 C  C   . ASN A 1 901  ? 31.821 47.284  -34.176 1.00 15.23 ? 901  ASN A C   1 
ATOM   7286 O  O   . ASN A 1 901  ? 32.594 46.332  -34.220 1.00 15.75 ? 901  ASN A O   1 
ATOM   7287 C  CB  . ASN A 1 901  ? 32.024 48.072  -36.524 1.00 17.71 ? 901  ASN A CB  1 
ATOM   7288 C  CG  . ASN A 1 901  ? 31.428 47.991  -37.903 1.00 21.09 ? 901  ASN A CG  1 
ATOM   7289 O  OD1 . ASN A 1 901  ? 30.719 47.046  -38.244 1.00 25.41 ? 901  ASN A OD1 1 
ATOM   7290 N  ND2 . ASN A 1 901  ? 31.733 48.988  -38.726 1.00 26.04 ? 901  ASN A ND2 1 
ATOM   7291 N  N   . CYS A 1 902  ? 31.610 47.986  -33.072 1.00 14.74 ? 902  CYS A N   1 
ATOM   7292 C  CA  . CYS A 1 902  ? 32.380 47.718  -31.856 1.00 14.83 ? 902  CYS A CA  1 
ATOM   7293 C  C   . CYS A 1 902  ? 31.849 46.495  -31.137 1.00 14.35 ? 902  CYS A C   1 
ATOM   7294 O  O   . CYS A 1 902  ? 30.642 46.284  -31.056 1.00 15.49 ? 902  CYS A O   1 
ATOM   7295 C  CB  . CYS A 1 902  ? 32.284 48.898  -30.894 1.00 15.13 ? 902  CYS A CB  1 
ATOM   7296 S  SG  . CYS A 1 902  ? 33.075 50.398  -31.493 1.00 18.52 ? 902  CYS A SG  1 
ATOM   7297 N  N   . VAL A 1 903  ? 32.750 45.716  -30.570 1.00 13.64 ? 903  VAL A N   1 
ATOM   7298 C  CA  . VAL A 1 903  ? 32.333 44.600  -29.709 1.00 14.45 ? 903  VAL A CA  1 
ATOM   7299 C  C   . VAL A 1 903  ? 32.046 45.156  -28.302 1.00 13.88 ? 903  VAL A C   1 
ATOM   7300 O  O   . VAL A 1 903  ? 32.976 45.481  -27.534 1.00 15.41 ? 903  VAL A O   1 
ATOM   7301 C  CB  . VAL A 1 903  ? 33.400 43.512  -29.675 1.00 13.92 ? 903  VAL A CB  1 
ATOM   7302 C  CG1 . VAL A 1 903  ? 33.011 42.386  -28.690 1.00 15.12 ? 903  VAL A CG1 1 
ATOM   7303 C  CG2 . VAL A 1 903  ? 33.600 42.966  -31.076 1.00 15.02 ? 903  VAL A CG2 1 
ATOM   7304 N  N   . ARG A 1 904  ? 30.785 45.320  -27.979 1.00 13.66 ? 904  ARG A N   1 
ATOM   7305 C  CA  . ARG A 1 904  ? 30.391 45.926  -26.725 1.00 13.47 ? 904  ARG A CA  1 
ATOM   7306 C  C   . ARG A 1 904  ? 29.870 44.871  -25.775 1.00 13.80 ? 904  ARG A C   1 
ATOM   7307 O  O   . ARG A 1 904  ? 29.483 43.771  -26.190 1.00 13.91 ? 904  ARG A O   1 
ATOM   7308 C  CB  . ARG A 1 904  ? 29.318 46.983  -26.980 1.00 13.80 ? 904  ARG A CB  1 
ATOM   7309 C  CG  . ARG A 1 904  ? 29.892 48.235  -27.628 1.00 14.80 ? 904  ARG A CG  1 
ATOM   7310 C  CD  . ARG A 1 904  ? 28.880 49.326  -27.887 1.00 18.43 ? 904  ARG A CD  1 
ATOM   7311 N  NE  . ARG A 1 904  ? 28.107 48.979  -29.068 1.00 18.14 ? 904  ARG A NE  1 
ATOM   7312 C  CZ  . ARG A 1 904  ? 27.137 49.732  -29.551 1.00 20.08 ? 904  ARG A CZ  1 
ATOM   7313 N  NH1 . ARG A 1 904  ? 26.800 50.874  -28.951 1.00 19.13 ? 904  ARG A NH1 1 
ATOM   7314 N  NH2 . ARG A 1 904  ? 26.494 49.316  -30.640 1.00 21.34 ? 904  ARG A NH2 1 
ATOM   7315 N  N   . PRO A 1 905  ? 29.829 45.190  -24.487 1.00 11.75 ? 905  PRO A N   1 
ATOM   7316 C  CA  . PRO A 1 905  ? 29.216 44.261  -23.528 1.00 12.94 ? 905  PRO A CA  1 
ATOM   7317 C  C   . PRO A 1 905  ? 27.760 44.039  -23.856 1.00 13.73 ? 905  PRO A C   1 
ATOM   7318 O  O   . PRO A 1 905  ? 27.137 44.854  -24.526 1.00 13.47 ? 905  PRO A O   1 
ATOM   7319 C  CB  . PRO A 1 905  ? 29.334 45.013  -22.196 1.00 11.84 ? 905  PRO A CB  1 
ATOM   7320 C  CG  . PRO A 1 905  ? 30.507 45.955  -22.393 1.00 11.54 ? 905  PRO A CG  1 
ATOM   7321 C  CD  . PRO A 1 905  ? 30.326 46.435  -23.828 1.00 11.97 ? 905  PRO A CD  1 
ATOM   7322 N  N   . SER A 1 906  ? 27.214 42.935  -23.364 1.00 13.82 ? 906  SER A N   1 
ATOM   7323 C  CA  . SER A 1 906  ? 25.795 42.688  -23.507 1.00 16.64 ? 906  SER A CA  1 
ATOM   7324 C  C   . SER A 1 906  ? 24.955 43.704  -22.736 1.00 17.28 ? 906  SER A C   1 
ATOM   7325 O  O   . SER A 1 906  ? 25.461 44.433  -21.855 1.00 16.53 ? 906  SER A O   1 
ATOM   7326 C  CB  . SER A 1 906  ? 25.485 41.296  -23.004 1.00 18.66 ? 906  SER A CB  1 
ATOM   7327 O  OG  . SER A 1 906  ? 25.215 41.363  -21.635 1.00 23.00 ? 906  SER A OG  1 
ATOM   7328 N  N   . LYS A 1 907  ? 23.669 43.742  -23.051 1.00 17.20 ? 907  LYS A N   1 
ATOM   7329 C  CA  . LYS A 1 907  ? 22.732 44.660  -22.415 1.00 19.72 ? 907  LYS A CA  1 
ATOM   7330 C  C   . LYS A 1 907  ? 22.684 44.514  -20.885 1.00 18.50 ? 907  LYS A C   1 
ATOM   7331 O  O   . LYS A 1 907  ? 22.324 45.467  -20.191 1.00 20.21 ? 907  LYS A O   1 
ATOM   7332 C  CB  . LYS A 1 907  ? 21.333 44.504  -23.044 1.00 19.96 ? 907  LYS A CB  1 
ATOM   7333 C  CG  . LYS A 1 907  ? 21.285 44.927  -24.526 1.00 24.08 ? 907  LYS A CG  1 
ATOM   7334 C  CD  . LYS A 1 907  ? 19.948 44.567  -25.219 1.00 24.40 ? 907  LYS A CD  1 
ATOM   7335 C  CE  . LYS A 1 907  ? 18.759 44.610  -24.251 1.00 31.05 ? 907  LYS A CE  1 
ATOM   7336 N  NZ  . LYS A 1 907  ? 18.539 45.959  -23.631 1.00 33.00 ? 907  LYS A NZ  1 
ATOM   7337 N  N   . LEU A 1 908  ? 23.047 43.351  -20.356 1.00 17.42 ? 908  LEU A N   1 
ATOM   7338 C  CA  . LEU A 1 908  ? 22.968 43.154  -18.906 1.00 17.38 ? 908  LEU A CA  1 
ATOM   7339 C  C   . LEU A 1 908  ? 24.277 43.478  -18.163 1.00 14.98 ? 908  LEU A C   1 
ATOM   7340 O  O   . LEU A 1 908  ? 24.316 43.438  -16.933 1.00 16.61 ? 908  LEU A O   1 
ATOM   7341 C  CB  . LEU A 1 908  ? 22.534 41.720  -18.565 1.00 18.77 ? 908  LEU A CB  1 
ATOM   7342 C  CG  . LEU A 1 908  ? 21.158 41.251  -19.048 1.00 21.95 ? 908  LEU A CG  1 
ATOM   7343 C  CD1 . LEU A 1 908  ? 20.953 39.770  -18.721 1.00 23.87 ? 908  LEU A CD1 1 
ATOM   7344 C  CD2 . LEU A 1 908  ? 20.053 42.111  -18.440 1.00 23.94 ? 908  LEU A CD2 1 
ATOM   7345 N  N   . HIS A 1 909  ? 25.356 43.730  -18.895 1.00 13.02 ? 909  HIS A N   1 
ATOM   7346 C  CA  . HIS A 1 909  ? 26.634 44.040  -18.258 1.00 12.18 ? 909  HIS A CA  1 
ATOM   7347 C  C   . HIS A 1 909  ? 26.589 45.431  -17.617 1.00 11.85 ? 909  HIS A C   1 
ATOM   7348 O  O   . HIS A 1 909  ? 26.107 46.381  -18.222 1.00 12.04 ? 909  HIS A O   1 
ATOM   7349 C  CB  . HIS A 1 909  ? 27.704 44.017  -19.296 1.00 12.53 ? 909  HIS A CB  1 
ATOM   7350 C  CG  . HIS A 1 909  ? 29.064 43.768  -18.750 1.00 11.86 ? 909  HIS A CG  1 
ATOM   7351 N  ND1 . HIS A 1 909  ? 29.769 44.728  -18.036 1.00 12.96 ? 909  HIS A ND1 1 
ATOM   7352 C  CD2 . HIS A 1 909  ? 29.861 42.676  -18.807 1.00 11.84 ? 909  HIS A CD2 1 
ATOM   7353 C  CE1 . HIS A 1 909  ? 30.935 44.217  -17.682 1.00 11.87 ? 909  HIS A CE1 1 
ATOM   7354 N  NE2 . HIS A 1 909  ? 31.029 42.982  -18.163 1.00 12.37 ? 909  HIS A NE2 1 
ATOM   7355 N  N   . PRO A 1 910  ? 27.055 45.561  -16.386 1.00 10.46 ? 910  PRO A N   1 
ATOM   7356 C  CA  . PRO A 1 910  ? 27.009 46.869  -15.708 1.00 10.47 ? 910  PRO A CA  1 
ATOM   7357 C  C   . PRO A 1 910  ? 28.131 47.853  -16.084 1.00 9.15  ? 910  PRO A C   1 
ATOM   7358 O  O   . PRO A 1 910  ? 28.080 48.983  -15.537 1.00 9.23  ? 910  PRO A O   1 
ATOM   7359 C  CB  . PRO A 1 910  ? 27.083 46.518  -14.218 1.00 11.53 ? 910  PRO A CB  1 
ATOM   7360 C  CG  . PRO A 1 910  ? 27.140 45.036  -14.115 1.00 13.06 ? 910  PRO A CG  1 
ATOM   7361 C  CD  . PRO A 1 910  ? 27.487 44.479  -15.475 1.00 12.06 ? 910  PRO A CD  1 
ATOM   7362 N  N   . ALA A 1 911  ? 29.083 47.478  -16.926 1.00 9.25  ? 911  ALA A N   1 
ATOM   7363 C  CA  . ALA A 1 911  ? 30.200 48.383  -17.287 1.00 9.75  ? 911  ALA A CA  1 
ATOM   7364 C  C   . ALA A 1 911  ? 30.076 48.882  -18.701 1.00 9.48  ? 911  ALA A C   1 
ATOM   7365 O  O   . ALA A 1 911  ? 29.371 48.274  -19.535 1.00 10.26 ? 911  ALA A O   1 
ATOM   7366 C  CB  . ALA A 1 911  ? 31.536 47.655  -17.131 1.00 10.93 ? 911  ALA A CB  1 
ATOM   7367 N  N   . GLY A 1 912  ? 30.811 49.945  -19.030 1.00 9.22  ? 912  GLY A N   1 
ATOM   7368 C  CA  . GLY A 1 912  ? 31.083 50.315  -20.408 1.00 9.55  ? 912  GLY A CA  1 
ATOM   7369 C  C   . GLY A 1 912  ? 32.552 50.626  -20.540 1.00 8.53  ? 912  GLY A C   1 
ATOM   7370 O  O   . GLY A 1 912  ? 33.256 50.732  -19.519 1.00 9.28  ? 912  GLY A O   1 
ATOM   7371 N  N   . TYR A 1 913  ? 33.030 50.789  -21.761 1.00 8.98  ? 913  TYR A N   1 
ATOM   7372 C  CA  . TYR A 1 913  ? 34.443 50.964  -22.057 1.00 8.94  ? 913  TYR A CA  1 
ATOM   7373 C  C   . TYR A 1 913  ? 34.609 52.004  -23.138 1.00 9.32  ? 913  TYR A C   1 
ATOM   7374 O  O   . TYR A 1 913  ? 33.787 52.056  -24.082 1.00 10.01 ? 913  TYR A O   1 
ATOM   7375 C  CB  . TYR A 1 913  ? 35.085 49.624  -22.517 1.00 9.74  ? 913  TYR A CB  1 
ATOM   7376 C  CG  . TYR A 1 913  ? 35.023 48.591  -21.410 1.00 9.61  ? 913  TYR A CG  1 
ATOM   7377 C  CD1 . TYR A 1 913  ? 35.917 48.651  -20.354 1.00 9.97  ? 913  TYR A CD1 1 
ATOM   7378 C  CD2 . TYR A 1 913  ? 34.011 47.621  -21.377 1.00 10.64 ? 913  TYR A CD2 1 
ATOM   7379 C  CE1 . TYR A 1 913  ? 35.872 47.770  -19.325 1.00 10.06 ? 913  TYR A CE1 1 
ATOM   7380 C  CE2 . TYR A 1 913  ? 33.940 46.698  -20.322 1.00 10.98 ? 913  TYR A CE2 1 
ATOM   7381 C  CZ  . TYR A 1 913  ? 34.880 46.803  -19.314 1.00 9.98  ? 913  TYR A CZ  1 
ATOM   7382 O  OH  . TYR A 1 913  ? 34.788 45.951  -18.254 1.00 10.75 ? 913  TYR A OH  1 
ATOM   7383 N  N   . LEU A 1 914  ? 35.673 52.788  -23.022 1.00 9.03  ? 914  LEU A N   1 
ATOM   7384 C  CA  . LEU A 1 914  ? 35.987 53.779  -24.033 1.00 9.17  ? 914  LEU A CA  1 
ATOM   7385 C  C   . LEU A 1 914  ? 36.533 53.155  -25.289 1.00 10.12 ? 914  LEU A C   1 
ATOM   7386 O  O   . LEU A 1 914  ? 37.073 52.045  -25.293 1.00 10.63 ? 914  LEU A O   1 
ATOM   7387 C  CB  . LEU A 1 914  ? 37.058 54.738  -23.472 1.00 9.62  ? 914  LEU A CB  1 
ATOM   7388 C  CG  . LEU A 1 914  ? 36.604 55.627  -22.322 1.00 9.64  ? 914  LEU A CG  1 
ATOM   7389 C  CD1 . LEU A 1 914  ? 37.733 56.635  -22.000 1.00 10.27 ? 914  LEU A CD1 1 
ATOM   7390 C  CD2 . LEU A 1 914  ? 35.323 56.400  -22.624 1.00 10.39 ? 914  LEU A CD2 1 
ATOM   7391 N  N   . THR A 1 915  ? 36.400 53.896  -26.391 1.00 10.70 ? 915  THR A N   1 
ATOM   7392 C  CA  . THR A 1 915  ? 37.185 53.625  -27.586 1.00 10.70 ? 915  THR A CA  1 
ATOM   7393 C  C   . THR A 1 915  ? 38.609 54.156  -27.457 1.00 11.21 ? 915  THR A C   1 
ATOM   7394 O  O   . THR A 1 915  ? 38.881 55.020  -26.574 1.00 11.36 ? 915  THR A O   1 
ATOM   7395 C  CB  . THR A 1 915  ? 36.554 54.321  -28.789 1.00 12.02 ? 915  THR A CB  1 
ATOM   7396 O  OG1 . THR A 1 915  ? 36.510 55.736  -28.505 1.00 13.57 ? 915  THR A OG1 1 
ATOM   7397 C  CG2 . THR A 1 915  ? 35.105 53.844  -29.038 1.00 13.33 ? 915  THR A CG2 1 
ATOM   7398 N  N   . SER A 1 916  ? 39.508 53.737  -28.332 1.00 11.32 ? 916  SER A N   1 
ATOM   7399 C  CA  . SER A 1 916  ? 40.832 54.299  -28.403 1.00 12.42 ? 916  SER A CA  1 
ATOM   7400 C  C   . SER A 1 916  ? 40.840 55.826  -28.497 1.00 11.61 ? 916  SER A C   1 
ATOM   7401 O  O   . SER A 1 916  ? 41.577 56.491  -27.764 1.00 11.30 ? 916  SER A O   1 
ATOM   7402 C  CB  . SER A 1 916  ? 41.575 53.734  -29.613 1.00 13.01 ? 916  SER A CB  1 
ATOM   7403 O  OG  . SER A 1 916  ? 42.793 54.410  -29.827 1.00 20.39 ? 916  SER A OG  1 
ATOM   7404 N  N   . ALA A 1 917  ? 40.012 56.398  -29.362 1.00 10.89 ? 917  ALA A N   1 
ATOM   7405 C  CA  . ALA A 1 917  ? 40.049 57.845  -29.545 1.00 10.96 ? 917  ALA A CA  1 
ATOM   7406 C  C   . ALA A 1 917  ? 39.646 58.558  -28.278 1.00 10.40 ? 917  ALA A C   1 
ATOM   7407 O  O   . ALA A 1 917  ? 40.226 59.595  -27.942 1.00 10.09 ? 917  ALA A O   1 
ATOM   7408 C  CB  . ALA A 1 917  ? 39.132 58.278  -30.686 1.00 11.68 ? 917  ALA A CB  1 
ATOM   7409 N  N   . ALA A 1 918  ? 38.632 58.052  -27.589 1.00 9.35  ? 918  ALA A N   1 
ATOM   7410 C  CA  . ALA A 1 918  ? 38.164 58.707  -26.364 1.00 9.29  ? 918  ALA A CA  1 
ATOM   7411 C  C   . ALA A 1 918  ? 39.188 58.591  -25.247 1.00 8.62  ? 918  ALA A C   1 
ATOM   7412 O  O   . ALA A 1 918  ? 39.398 59.552  -24.487 1.00 8.88  ? 918  ALA A O   1 
ATOM   7413 C  CB  . ALA A 1 918  ? 36.802 58.192  -25.946 1.00 9.84  ? 918  ALA A CB  1 
ATOM   7414 N  N   . HIS A 1 919  ? 39.833 57.453  -25.147 1.00 7.77  ? 919  HIS A N   1 
ATOM   7415 C  CA  . HIS A 1 919  ? 40.848 57.266  -24.126 1.00 8.28  ? 919  HIS A CA  1 
ATOM   7416 C  C   . HIS A 1 919  ? 42.025 58.199  -24.391 1.00 8.53  ? 919  HIS A C   1 
ATOM   7417 O  O   . HIS A 1 919  ? 42.520 58.833  -23.485 1.00 8.61  ? 919  HIS A O   1 
ATOM   7418 C  CB  . HIS A 1 919  ? 41.300 55.806  -24.122 1.00 9.33  ? 919  HIS A CB  1 
ATOM   7419 C  CG  . HIS A 1 919  ? 42.486 55.544  -23.254 1.00 10.00 ? 919  HIS A CG  1 
ATOM   7420 N  ND1 . HIS A 1 919  ? 42.452 55.640  -21.883 1.00 14.07 ? 919  HIS A ND1 1 
ATOM   7421 C  CD2 . HIS A 1 919  ? 43.746 55.195  -23.580 1.00 11.97 ? 919  HIS A CD2 1 
ATOM   7422 C  CE1 . HIS A 1 919  ? 43.649 55.349  -21.404 1.00 13.04 ? 919  HIS A CE1 1 
ATOM   7423 N  NE2 . HIS A 1 919  ? 44.446 55.061  -22.411 1.00 12.79 ? 919  HIS A NE2 1 
ATOM   7424 N  N   . LYS A 1 920  ? 42.473 58.278  -25.634 1.00 9.10  ? 920  LYS A N   1 
ATOM   7425 C  CA  . LYS A 1 920  ? 43.546 59.218  -25.966 1.00 10.03 ? 920  LYS A CA  1 
ATOM   7426 C  C   . LYS A 1 920  ? 43.157 60.668  -25.690 1.00 8.58  ? 920  LYS A C   1 
ATOM   7427 O  O   . LYS A 1 920  ? 43.993 61.449  -25.229 1.00 9.00  ? 920  LYS A O   1 
ATOM   7428 C  CB  . LYS A 1 920  ? 44.011 59.046  -27.397 1.00 12.27 ? 920  LYS A CB  1 
ATOM   7429 C  CG  . LYS A 1 920  ? 44.823 57.784  -27.554 1.00 15.96 ? 920  LYS A CG  1 
ATOM   7430 C  CD  . LYS A 1 920  ? 45.615 57.771  -28.864 1.00 20.64 ? 920  LYS A CD  1 
ATOM   7431 C  CE  . LYS A 1 920  ? 46.514 56.546  -28.947 1.00 22.17 ? 920  LYS A CE  1 
ATOM   7432 N  NZ  . LYS A 1 920  ? 47.719 56.639  -28.060 1.00 20.08 ? 920  LYS A NZ  1 
ATOM   7433 N  N   . ALA A 1 921  ? 41.912 61.023  -25.975 1.00 8.23  ? 921  ALA A N   1 
ATOM   7434 C  CA  . ALA A 1 921  ? 41.454 62.365  -25.689 1.00 8.86  ? 921  ALA A CA  1 
ATOM   7435 C  C   . ALA A 1 921  ? 41.489 62.638  -24.170 1.00 8.26  ? 921  ALA A C   1 
ATOM   7436 O  O   . ALA A 1 921  ? 41.858 63.724  -23.743 1.00 8.53  ? 921  ALA A O   1 
ATOM   7437 C  CB  . ALA A 1 921  ? 40.038 62.531  -26.259 1.00 8.28  ? 921  ALA A CB  1 
ATOM   7438 N  N   . SER A 1 922  ? 41.095 61.654  -23.364 1.00 8.01  ? 922  SER A N   1 
ATOM   7439 C  CA  . SER A 1 922  ? 41.199 61.816  -21.909 1.00 7.57  ? 922  SER A CA  1 
ATOM   7440 C  C   . SER A 1 922  ? 42.662 62.001  -21.494 1.00 7.95  ? 922  SER A C   1 
ATOM   7441 O  O   . SER A 1 922  ? 42.967 62.881  -20.681 1.00 8.39  ? 922  SER A O   1 
ATOM   7442 C  CB  . SER A 1 922  ? 40.583 60.588  -21.216 1.00 8.31  ? 922  SER A CB  1 
ATOM   7443 O  OG  . SER A 1 922  ? 40.748 60.737  -19.807 1.00 8.31  ? 922  SER A OG  1 
ATOM   7444 N  N   . GLN A 1 923  ? 43.576 61.239  -22.069 1.00 7.80  ? 923  GLN A N   1 
ATOM   7445 C  CA  . GLN A 1 923  ? 45.007 61.396  -21.743 1.00 8.44  ? 923  GLN A CA  1 
ATOM   7446 C  C   . GLN A 1 923  ? 45.502 62.783  -22.152 1.00 8.66  ? 923  GLN A C   1 
ATOM   7447 O  O   . GLN A 1 923  ? 46.348 63.372  -21.473 1.00 8.63  ? 923  GLN A O   1 
ATOM   7448 C  CB  . GLN A 1 923  ? 45.844 60.329  -22.445 1.00 8.55  ? 923  GLN A CB  1 
ATOM   7449 C  CG  . GLN A 1 923  ? 45.548 58.925  -21.901 1.00 9.40  ? 923  GLN A CG  1 
ATOM   7450 C  CD  . GLN A 1 923  ? 46.501 57.900  -22.474 1.00 11.14 ? 923  GLN A CD  1 
ATOM   7451 O  OE1 . GLN A 1 923  ? 46.671 57.844  -23.707 1.00 11.36 ? 923  GLN A OE1 1 
ATOM   7452 N  NE2 . GLN A 1 923  ? 47.130 57.086  -21.608 1.00 9.94  ? 923  GLN A NE2 1 
ATOM   7453 N  N   A SER A 1 924  ? 44.987 63.309  -23.263 0.50 8.93  ? 924  SER A N   1 
ATOM   7454 N  N   B SER A 1 924  ? 44.992 63.331  -23.253 0.50 8.90  ? 924  SER A N   1 
ATOM   7455 C  CA  A SER A 1 924  ? 45.371 64.643  -23.714 0.50 9.32  ? 924  SER A CA  1 
ATOM   7456 C  CA  B SER A 1 924  ? 45.411 64.667  -23.686 0.50 9.20  ? 924  SER A CA  1 
ATOM   7457 C  C   A SER A 1 924  ? 45.027 65.690  -22.651 0.50 9.19  ? 924  SER A C   1 
ATOM   7458 C  C   B SER A 1 924  ? 44.954 65.767  -22.723 0.50 8.99  ? 924  SER A C   1 
ATOM   7459 O  O   A SER A 1 924  ? 45.781 66.652  -22.445 0.50 9.80  ? 924  SER A O   1 
ATOM   7460 O  O   B SER A 1 924  ? 45.531 66.860  -22.677 0.50 9.29  ? 924  SER A O   1 
ATOM   7461 C  CB  A SER A 1 924  ? 44.678 64.988  -25.039 0.50 9.81  ? 924  SER A CB  1 
ATOM   7462 C  CB  B SER A 1 924  ? 44.867 64.961  -25.074 0.50 9.94  ? 924  SER A CB  1 
ATOM   7463 O  OG  A SER A 1 924  ? 43.359 65.472  -24.859 0.50 10.65 ? 924  SER A OG  1 
ATOM   7464 O  OG  B SER A 1 924  ? 45.498 64.128  -26.022 0.50 10.27 ? 924  SER A OG  1 
ATOM   7465 N  N   . LEU A 1 925  ? 43.903 65.493  -21.968 1.00 8.80  ? 925  LEU A N   1 
ATOM   7466 C  CA  . LEU A 1 925  ? 43.438 66.437  -20.963 1.00 8.57  ? 925  LEU A CA  1 
ATOM   7467 C  C   . LEU A 1 925  ? 44.213 66.265  -19.666 1.00 9.08  ? 925  LEU A C   1 
ATOM   7468 O  O   . LEU A 1 925  ? 44.567 67.252  -19.039 1.00 10.56 ? 925  LEU A O   1 
ATOM   7469 C  CB  . LEU A 1 925  ? 41.942 66.253  -20.676 1.00 8.42  ? 925  LEU A CB  1 
ATOM   7470 C  CG  . LEU A 1 925  ? 41.020 66.546  -21.861 1.00 7.27  ? 925  LEU A CG  1 
ATOM   7471 C  CD1 . LEU A 1 925  ? 39.584 66.278  -21.402 1.00 9.59  ? 925  LEU A CD1 1 
ATOM   7472 C  CD2 . LEU A 1 925  ? 41.182 68.012  -22.321 1.00 10.28 ? 925  LEU A CD2 1 
ATOM   7473 N  N   . LEU A 1 926  ? 44.412 65.023  -19.231 1.00 8.14  ? 926  LEU A N   1 
ATOM   7474 C  CA  . LEU A 1 926  ? 44.965 64.789  -17.889 1.00 8.10  ? 926  LEU A CA  1 
ATOM   7475 C  C   . LEU A 1 926  ? 46.467 64.756  -17.865 1.00 8.38  ? 926  LEU A C   1 
ATOM   7476 O  O   . LEU A 1 926  ? 47.063 65.166  -16.842 1.00 8.79  ? 926  LEU A O   1 
ATOM   7477 C  CB  . LEU A 1 926  ? 44.371 63.514  -17.298 1.00 9.71  ? 926  LEU A CB  1 
ATOM   7478 C  CG  . LEU A 1 926  ? 42.854 63.595  -17.058 1.00 11.45 ? 926  LEU A CG  1 
ATOM   7479 C  CD1 . LEU A 1 926  ? 42.382 62.251  -16.485 1.00 13.42 ? 926  LEU A CD1 1 
ATOM   7480 C  CD2 . LEU A 1 926  ? 42.511 64.761  -16.114 1.00 13.62 ? 926  LEU A CD2 1 
ATOM   7481 N  N   . ASP A 1 927  ? 47.101 64.293  -18.927 1.00 7.28  ? 927  ASP A N   1 
ATOM   7482 C  CA  . ASP A 1 927  ? 48.553 64.230  -18.932 1.00 8.26  ? 927  ASP A CA  1 
ATOM   7483 C  C   . ASP A 1 927  ? 49.097 64.756  -20.249 1.00 7.90  ? 927  ASP A C   1 
ATOM   7484 O  O   . ASP A 1 927  ? 49.662 64.012  -21.049 1.00 8.04  ? 927  ASP A O   1 
ATOM   7485 C  CB  . ASP A 1 927  ? 49.037 62.815  -18.678 1.00 9.05  ? 927  ASP A CB  1 
ATOM   7486 C  CG  . ASP A 1 927  ? 48.696 62.341  -17.270 1.00 9.58  ? 927  ASP A CG  1 
ATOM   7487 O  OD1 . ASP A 1 927  ? 49.421 62.716  -16.297 1.00 10.32 ? 927  ASP A OD1 1 
ATOM   7488 O  OD2 . ASP A 1 927  ? 47.712 61.600  -17.088 1.00 10.66 ? 927  ASP A OD2 1 
ATOM   7489 N  N   . PRO A 1 928  ? 48.945 66.065  -20.461 1.00 8.33  ? 928  PRO A N   1 
ATOM   7490 C  CA  . PRO A 1 928  ? 49.453 66.706  -21.685 1.00 8.51  ? 928  PRO A CA  1 
ATOM   7491 C  C   . PRO A 1 928  ? 50.974 66.695  -21.672 1.00 8.58  ? 928  PRO A C   1 
ATOM   7492 O  O   . PRO A 1 928  ? 51.617 66.451  -20.633 1.00 8.79  ? 928  PRO A O   1 
ATOM   7493 C  CB  . PRO A 1 928  ? 48.945 68.154  -21.551 1.00 10.35 ? 928  PRO A CB  1 
ATOM   7494 C  CG  . PRO A 1 928  ? 48.915 68.372  -20.082 1.00 11.87 ? 928  PRO A CG  1 
ATOM   7495 C  CD  . PRO A 1 928  ? 48.365 67.044  -19.522 1.00 9.60  ? 928  PRO A CD  1 
ATOM   7496 N  N   . LEU A 1 929  ? 51.604 67.042  -22.791 1.00 8.26  ? 929  LEU A N   1 
ATOM   7497 C  CA  . LEU A 1 929  ? 53.025 67.348  -22.787 1.00 8.43  ? 929  LEU A CA  1 
ATOM   7498 C  C   . LEU A 1 929  ? 53.316 68.515  -21.878 1.00 8.56  ? 929  LEU A C   1 
ATOM   7499 O  O   . LEU A 1 929  ? 52.539 69.475  -21.816 1.00 10.37 ? 929  LEU A O   1 
ATOM   7500 C  CB  . LEU A 1 929  ? 53.502 67.695  -24.205 1.00 8.75  ? 929  LEU A CB  1 
ATOM   7501 C  CG  . LEU A 1 929  ? 53.312 66.664  -25.308 1.00 9.10  ? 929  LEU A CG  1 
ATOM   7502 C  CD1 . LEU A 1 929  ? 53.875 67.241  -26.613 1.00 11.08 ? 929  LEU A CD1 1 
ATOM   7503 C  CD2 . LEU A 1 929  ? 54.057 65.367  -24.964 1.00 9.32  ? 929  LEU A CD2 1 
ATOM   7504 N  N   . ASP A 1 930  ? 54.437 68.442  -21.167 1.00 8.19  ? 930  ASP A N   1 
ATOM   7505 C  CA  . ASP A 1 930  ? 54.911 69.564  -20.367 1.00 8.28  ? 930  ASP A CA  1 
ATOM   7506 C  C   . ASP A 1 930  ? 55.927 70.401  -21.137 1.00 8.61  ? 930  ASP A C   1 
ATOM   7507 O  O   . ASP A 1 930  ? 56.806 69.863  -21.811 1.00 10.07 ? 930  ASP A O   1 
ATOM   7508 C  CB  . ASP A 1 930  ? 55.525 69.067  -19.057 1.00 8.58  ? 930  ASP A CB  1 
ATOM   7509 C  CG  . ASP A 1 930  ? 54.701 67.973  -18.406 1.00 10.17 ? 930  ASP A CG  1 
ATOM   7510 O  OD1 . ASP A 1 930  ? 53.601 68.277  -17.899 1.00 12.15 ? 930  ASP A OD1 1 
ATOM   7511 O  OD2 . ASP A 1 930  ? 55.154 66.809  -18.402 1.00 9.94  ? 930  ASP A OD2 1 
ATOM   7512 N  N   . LYS A 1 931  ? 55.800 71.720  -21.033 1.00 8.77  ? 931  LYS A N   1 
ATOM   7513 C  CA  . LYS A 1 931  ? 56.607 72.640  -21.844 1.00 9.05  ? 931  LYS A CA  1 
ATOM   7514 C  C   . LYS A 1 931  ? 57.538 73.435  -20.978 1.00 9.26  ? 931  LYS A C   1 
ATOM   7515 O  O   . LYS A 1 931  ? 57.102 74.044  -19.983 1.00 10.08 ? 931  LYS A O   1 
ATOM   7516 C  CB  . LYS A 1 931  ? 55.685 73.598  -22.619 1.00 10.05 ? 931  LYS A CB  1 
ATOM   7517 C  CG  . LYS A 1 931  ? 54.703 72.934  -23.579 1.00 12.29 ? 931  LYS A CG  1 
ATOM   7518 C  CD  . LYS A 1 931  ? 53.806 73.980  -24.248 1.00 14.14 ? 931  LYS A CD  1 
ATOM   7519 C  CE  . LYS A 1 931  ? 52.769 74.511  -23.283 1.00 17.66 ? 931  LYS A CE  1 
ATOM   7520 N  NZ  . LYS A 1 931  ? 52.098 75.702  -23.806 1.00 18.09 ? 931  LYS A NZ  1 
ATOM   7521 N  N   . PHE A 1 932  ? 58.811 73.482  -21.364 1.00 8.31  ? 932  PHE A N   1 
ATOM   7522 C  CA  . PHE A 1 932  ? 59.858 74.179  -20.610 1.00 8.36  ? 932  PHE A CA  1 
ATOM   7523 C  C   . PHE A 1 932  ? 60.517 75.212  -21.518 1.00 8.13  ? 932  PHE A C   1 
ATOM   7524 O  O   . PHE A 1 932  ? 60.833 74.901  -22.671 1.00 9.64  ? 932  PHE A O   1 
ATOM   7525 C  CB  . PHE A 1 932  ? 60.936 73.199  -20.160 1.00 8.36  ? 932  PHE A CB  1 
ATOM   7526 C  CG  . PHE A 1 932  ? 60.444 72.112  -19.251 1.00 8.60  ? 932  PHE A CG  1 
ATOM   7527 C  CD1 . PHE A 1 932  ? 59.838 70.969  -19.758 1.00 9.80  ? 932  PHE A CD1 1 
ATOM   7528 C  CD2 . PHE A 1 932  ? 60.593 72.247  -17.867 1.00 10.90 ? 932  PHE A CD2 1 
ATOM   7529 C  CE1 . PHE A 1 932  ? 59.405 69.920  -18.889 1.00 9.23  ? 932  PHE A CE1 1 
ATOM   7530 C  CE2 . PHE A 1 932  ? 60.156 71.217  -17.004 1.00 11.10 ? 932  PHE A CE2 1 
ATOM   7531 C  CZ  . PHE A 1 932  ? 59.551 70.075  -17.527 1.00 10.57 ? 932  PHE A CZ  1 
ATOM   7532 N  N   . ILE A 1 933  ? 60.731 76.409  -21.004 1.00 8.33  ? 933  ILE A N   1 
ATOM   7533 C  CA  . ILE A 1 933  ? 61.401 77.481  -21.756 1.00 8.82  ? 933  ILE A CA  1 
ATOM   7534 C  C   . ILE A 1 933  ? 62.738 77.721  -21.091 1.00 9.71  ? 933  ILE A C   1 
ATOM   7535 O  O   . ILE A 1 933  ? 62.791 78.010  -19.894 1.00 8.98  ? 933  ILE A O   1 
ATOM   7536 C  CB  . ILE A 1 933  ? 60.590 78.786  -21.712 1.00 9.05  ? 933  ILE A CB  1 
ATOM   7537 C  CG1 . ILE A 1 933  ? 59.182 78.574  -22.280 1.00 9.53  ? 933  ILE A CG1 1 
ATOM   7538 C  CG2 . ILE A 1 933  ? 61.330 79.889  -22.479 1.00 10.36 ? 933  ILE A CG2 1 
ATOM   7539 C  CD1 . ILE A 1 933  ? 58.256 79.740  -22.033 1.00 11.09 ? 933  ILE A CD1 1 
ATOM   7540 N  N   . PHE A 1 934  ? 63.836 77.608  -21.847 1.00 9.80  ? 934  PHE A N   1 
ATOM   7541 C  CA  . PHE A 1 934  ? 65.148 77.814  -21.236 1.00 10.57 ? 934  PHE A CA  1 
ATOM   7542 C  C   . PHE A 1 934  ? 65.274 79.281  -20.777 1.00 10.93 ? 934  PHE A C   1 
ATOM   7543 O  O   . PHE A 1 934  ? 64.946 80.201  -21.514 1.00 11.79 ? 934  PHE A O   1 
ATOM   7544 C  CB  . PHE A 1 934  ? 66.257 77.445  -22.228 1.00 11.24 ? 934  PHE A CB  1 
ATOM   7545 C  CG  . PHE A 1 934  ? 67.618 77.490  -21.623 1.00 12.40 ? 934  PHE A CG  1 
ATOM   7546 C  CD1 . PHE A 1 934  ? 68.026 76.492  -20.759 1.00 13.13 ? 934  PHE A CD1 1 
ATOM   7547 C  CD2 . PHE A 1 934  ? 68.477 78.568  -21.871 1.00 13.79 ? 934  PHE A CD2 1 
ATOM   7548 C  CE1 . PHE A 1 934  ? 69.304 76.523  -20.165 1.00 15.98 ? 934  PHE A CE1 1 
ATOM   7549 C  CE2 . PHE A 1 934  ? 69.740 78.620  -21.289 1.00 15.26 ? 934  PHE A CE2 1 
ATOM   7550 C  CZ  . PHE A 1 934  ? 70.160 77.613  -20.436 1.00 17.06 ? 934  PHE A CZ  1 
ATOM   7551 N  N   . ALA A 1 935  ? 65.716 79.495  -19.538 1.00 11.87 ? 935  ALA A N   1 
ATOM   7552 C  CA  . ALA A 1 935  ? 65.647 80.822  -18.953 1.00 14.16 ? 935  ALA A CA  1 
ATOM   7553 C  C   . ALA A 1 935  ? 66.768 81.756  -19.421 1.00 16.45 ? 935  ALA A C   1 
ATOM   7554 O  O   . ALA A 1 935  ? 66.517 82.959  -19.669 1.00 19.01 ? 935  ALA A O   1 
ATOM   7555 C  CB  . ALA A 1 935  ? 65.659 80.716  -17.446 1.00 15.99 ? 935  ALA A CB  1 
ATOM   7556 N  N   . GLU A 1 936  ? 67.983 81.237  -19.551 1.00 15.60 ? 936  GLU A N   1 
ATOM   7557 C  CA  A GLU A 1 936  ? 69.201 82.002  -19.873 0.50 16.31 ? 936  GLU A CA  1 
ATOM   7558 C  CA  B GLU A 1 936  ? 69.088 82.132  -19.865 0.50 16.34 ? 936  GLU A CA  1 
ATOM   7559 C  C   . GLU A 1 936  ? 69.297 82.255  -21.370 1.00 16.11 ? 936  GLU A C   1 
ATOM   7560 O  O   . GLU A 1 936  ? 68.542 81.687  -22.168 1.00 16.33 ? 936  GLU A O   1 
ATOM   7561 C  CB  A GLU A 1 936  ? 70.459 81.216  -19.438 0.50 15.90 ? 936  GLU A CB  1 
ATOM   7562 C  CB  B GLU A 1 936  ? 70.337 81.721  -19.090 0.50 16.90 ? 936  GLU A CB  1 
ATOM   7563 C  CG  A GLU A 1 936  ? 70.672 81.026  -17.932 0.50 17.53 ? 936  GLU A CG  1 
ATOM   7564 C  CG  B GLU A 1 936  ? 70.169 81.893  -17.580 0.50 19.39 ? 936  GLU A CG  1 
ATOM   7565 C  CD  A GLU A 1 936  ? 71.715 79.956  -17.596 0.50 18.15 ? 936  GLU A CD  1 
ATOM   7566 C  CD  B GLU A 1 936  ? 69.832 83.320  -17.172 0.50 23.39 ? 936  GLU A CD  1 
ATOM   7567 O  OE1 A GLU A 1 936  ? 71.478 78.755  -17.862 0.50 19.09 ? 936  GLU A OE1 1 
ATOM   7568 O  OE1 B GLU A 1 936  ? 70.511 84.256  -17.647 0.50 24.55 ? 936  GLU A OE1 1 
ATOM   7569 O  OE2 A GLU A 1 936  ? 72.781 80.307  -17.044 0.50 21.23 ? 936  GLU A OE2 1 
ATOM   7570 O  OE2 B GLU A 1 936  ? 68.887 83.513  -16.371 0.50 26.56 ? 936  GLU A OE2 1 
ATOM   7571 N  N   . ASN A 1 937  ? 70.276 83.057  -21.778 1.00 16.17 ? 937  ASN A N   1 
ATOM   7572 C  CA  . ASN A 1 937  ? 70.432 83.318  -23.200 1.00 16.27 ? 937  ASN A CA  1 
ATOM   7573 C  C   . ASN A 1 937  ? 70.961 82.149  -24.016 1.00 15.89 ? 937  ASN A C   1 
ATOM   7574 O  O   . ASN A 1 937  ? 70.535 81.931  -25.158 1.00 15.45 ? 937  ASN A O   1 
ATOM   7575 C  CB  . ASN A 1 937  ? 71.297 84.563  -23.415 1.00 16.45 ? 937  ASN A CB  1 
ATOM   7576 C  CG  . ASN A 1 937  ? 70.549 85.855  -23.089 1.00 18.86 ? 937  ASN A CG  1 
ATOM   7577 O  OD1 . ASN A 1 937  ? 69.313 85.879  -22.970 1.00 20.13 ? 937  ASN A OD1 1 
ATOM   7578 N  ND2 . ASN A 1 937  ? 71.299 86.938  -22.945 1.00 23.15 ? 937  ASN A ND2 1 
ATOM   7579 N  N   . GLU A 1 938  ? 71.888 81.397  -23.430 1.00 16.07 ? 938  GLU A N   1 
ATOM   7580 C  CA  . GLU A 1 938  ? 72.510 80.298  -24.145 1.00 18.18 ? 938  GLU A CA  1 
ATOM   7581 C  C   . GLU A 1 938  ? 72.602 79.054  -23.284 1.00 17.07 ? 938  GLU A C   1 
ATOM   7582 O  O   . GLU A 1 938  ? 73.011 79.121  -22.149 1.00 17.55 ? 938  GLU A O   1 
ATOM   7583 C  CB  . GLU A 1 938  ? 73.912 80.670  -24.621 1.00 19.59 ? 938  GLU A CB  1 
ATOM   7584 C  CG  . GLU A 1 938  ? 74.502 79.587  -25.509 1.00 24.01 ? 938  GLU A CG  1 
ATOM   7585 C  CD  . GLU A 1 938  ? 75.795 79.995  -26.182 1.00 30.71 ? 938  GLU A CD  1 
ATOM   7586 O  OE1 . GLU A 1 938  ? 76.365 81.046  -25.816 1.00 34.00 ? 938  GLU A OE1 1 
ATOM   7587 O  OE2 . GLU A 1 938  ? 76.234 79.245  -27.085 1.00 34.87 ? 938  GLU A OE2 1 
ATOM   7588 N  N   . TRP A 1 939  ? 72.211 77.928  -23.859 1.00 17.46 ? 939  TRP A N   1 
ATOM   7589 C  CA  . TRP A 1 939  ? 72.305 76.641  -23.173 1.00 16.98 ? 939  TRP A CA  1 
ATOM   7590 C  C   . TRP A 1 939  ? 73.500 75.850  -23.715 1.00 17.62 ? 939  TRP A C   1 
ATOM   7591 O  O   . TRP A 1 939  ? 73.412 75.221  -24.761 1.00 19.27 ? 939  TRP A O   1 
ATOM   7592 C  CB  . TRP A 1 939  ? 70.978 75.904  -23.371 1.00 15.80 ? 939  TRP A CB  1 
ATOM   7593 C  CG  . TRP A 1 939  ? 70.867 74.531  -22.765 1.00 13.44 ? 939  TRP A CG  1 
ATOM   7594 C  CD1 . TRP A 1 939  ? 71.746 73.892  -21.921 1.00 14.37 ? 939  TRP A CD1 1 
ATOM   7595 C  CD2 . TRP A 1 939  ? 69.768 73.647  -22.949 1.00 12.78 ? 939  TRP A CD2 1 
ATOM   7596 N  NE1 . TRP A 1 939  ? 71.259 72.647  -21.594 1.00 13.03 ? 939  TRP A NE1 1 
ATOM   7597 C  CE2 . TRP A 1 939  ? 70.058 72.459  -22.236 1.00 11.93 ? 939  TRP A CE2 1 
ATOM   7598 C  CE3 . TRP A 1 939  ? 68.582 73.712  -23.704 1.00 11.26 ? 939  TRP A CE3 1 
ATOM   7599 C  CZ2 . TRP A 1 939  ? 69.172 71.378  -22.199 1.00 13.02 ? 939  TRP A CZ2 1 
ATOM   7600 C  CZ3 . TRP A 1 939  ? 67.712 72.626  -23.692 1.00 13.31 ? 939  TRP A CZ3 1 
ATOM   7601 C  CH2 . TRP A 1 939  ? 68.024 71.465  -22.962 1.00 12.57 ? 939  TRP A CH2 1 
ATOM   7602 N  N   . ILE A 1 940  ? 74.608 75.896  -22.987 1.00 19.89 ? 940  ILE A N   1 
ATOM   7603 C  CA  . ILE A 1 940  ? 75.813 75.185  -23.430 1.00 21.09 ? 940  ILE A CA  1 
ATOM   7604 C  C   . ILE A 1 940  ? 75.665 73.668  -23.181 1.00 19.27 ? 940  ILE A C   1 
ATOM   7605 O  O   . ILE A 1 940  ? 75.242 73.256  -22.107 1.00 19.71 ? 940  ILE A O   1 
ATOM   7606 C  CB  . ILE A 1 940  ? 77.068 75.762  -22.742 1.00 21.57 ? 940  ILE A CB  1 
ATOM   7607 C  CG1 . ILE A 1 940  ? 77.193 77.265  -23.048 1.00 22.60 ? 940  ILE A CG1 1 
ATOM   7608 C  CG2 . ILE A 1 940  ? 78.336 74.969  -23.148 1.00 22.71 ? 940  ILE A CG2 1 
ATOM   7609 C  CD1 . ILE A 1 940  ? 78.563 77.864  -22.742 1.00 24.06 ? 940  ILE A CD1 1 
ATOM   7610 N  N   . GLY A 1 941  ? 75.986 72.857  -24.181 1.00 19.24 ? 941  GLY A N   1 
ATOM   7611 C  CA  . GLY A 1 941  ? 75.923 71.414  -24.038 1.00 18.48 ? 941  GLY A CA  1 
ATOM   7612 C  C   . GLY A 1 941  ? 74.526 70.829  -24.220 1.00 18.01 ? 941  GLY A C   1 
ATOM   7613 O  O   . GLY A 1 941  ? 74.301 69.662  -23.901 1.00 16.74 ? 941  GLY A O   1 
ATOM   7614 N  N   . ALA A 1 942  ? 73.607 71.611  -24.787 1.00 16.97 ? 942  ALA A N   1 
ATOM   7615 C  CA  . ALA A 1 942  ? 72.225 71.165  -25.002 1.00 17.31 ? 942  ALA A CA  1 
ATOM   7616 C  C   . ALA A 1 942  ? 72.146 69.966  -25.919 1.00 17.50 ? 942  ALA A C   1 
ATOM   7617 O  O   . ALA A 1 942  ? 72.851 69.906  -26.935 1.00 18.52 ? 942  ALA A O   1 
ATOM   7618 C  CB  . ALA A 1 942  ? 71.393 72.307  -25.565 1.00 17.31 ? 942  ALA A CB  1 
ATOM   7619 N  N   . GLN A 1 943  ? 71.266 69.022  -25.590 1.00 16.14 ? 943  GLN A N   1 
ATOM   7620 C  CA  . GLN A 1 943  ? 70.995 67.844  -26.393 1.00 17.22 ? 943  GLN A CA  1 
ATOM   7621 C  C   . GLN A 1 943  ? 69.566 67.853  -26.915 1.00 14.91 ? 943  GLN A C   1 
ATOM   7622 O  O   . GLN A 1 943  ? 68.675 68.507  -26.315 1.00 15.89 ? 943  GLN A O   1 
ATOM   7623 C  CB  . GLN A 1 943  ? 71.223 66.548  -25.584 1.00 17.69 ? 943  GLN A CB  1 
ATOM   7624 C  CG  . GLN A 1 943  ? 72.619 66.461  -25.008 1.00 21.57 ? 943  GLN A CG  1 
ATOM   7625 C  CD  . GLN A 1 943  ? 72.800 65.285  -24.063 1.00 22.36 ? 943  GLN A CD  1 
ATOM   7626 O  OE1 . GLN A 1 943  ? 71.843 64.851  -23.397 1.00 27.80 ? 943  GLN A OE1 1 
ATOM   7627 N  NE2 . GLN A 1 943  ? 74.031 64.773  -23.987 1.00 27.46 ? 943  GLN A NE2 1 
ATOM   7628 N  N   . GLY A 1 944  ? 69.310 67.128  -27.992 1.00 14.42 ? 944  GLY A N   1 
ATOM   7629 C  CA  . GLY A 1 944  ? 68.063 67.245  -28.709 1.00 14.79 ? 944  GLY A CA  1 
ATOM   7630 C  C   . GLY A 1 944  ? 66.957 66.340  -28.220 1.00 14.76 ? 944  GLY A C   1 
ATOM   7631 O  O   . GLY A 1 944  ? 65.787 66.571  -28.509 1.00 14.41 ? 944  GLY A O   1 
ATOM   7632 N  N   . GLN A 1 945  ? 67.309 65.287  -27.496 1.00 13.65 ? 945  GLN A N   1 
ATOM   7633 C  CA  . GLN A 1 945  ? 66.297 64.275  -27.151 1.00 14.23 ? 945  GLN A CA  1 
ATOM   7634 C  C   . GLN A 1 945  ? 66.770 63.436  -25.976 1.00 13.26 ? 945  GLN A C   1 
ATOM   7635 O  O   . GLN A 1 945  ? 67.975 63.263  -25.744 1.00 14.00 ? 945  GLN A O   1 
ATOM   7636 C  CB  . GLN A 1 945  ? 66.060 63.374  -28.361 1.00 14.14 ? 945  GLN A CB  1 
ATOM   7637 C  CG  . GLN A 1 945  ? 64.842 62.476  -28.329 1.00 16.27 ? 945  GLN A CG  1 
ATOM   7638 C  CD  . GLN A 1 945  ? 64.766 61.550  -29.548 1.00 16.92 ? 945  GLN A CD  1 
ATOM   7639 O  OE1 . GLN A 1 945  ? 63.908 61.723  -30.417 1.00 20.86 ? 945  GLN A OE1 1 
ATOM   7640 N  NE2 . GLN A 1 945  ? 65.639 60.563  -29.596 1.00 19.33 ? 945  GLN A NE2 1 
ATOM   7641 N  N   . PHE A 1 946  ? 65.786 62.958  -25.211 1.00 11.25 ? 946  PHE A N   1 
ATOM   7642 C  CA  . PHE A 1 946  ? 66.030 61.946  -24.175 1.00 11.31 ? 946  PHE A CA  1 
ATOM   7643 C  C   . PHE A 1 946  ? 64.942 60.901  -24.281 1.00 10.52 ? 946  PHE A C   1 
ATOM   7644 O  O   . PHE A 1 946  ? 63.778 61.253  -24.468 1.00 10.56 ? 946  PHE A O   1 
ATOM   7645 C  CB  . PHE A 1 946  ? 66.057 62.559  -22.762 1.00 11.61 ? 946  PHE A CB  1 
ATOM   7646 C  CG  . PHE A 1 946  ? 65.926 61.529  -21.663 1.00 11.60 ? 946  PHE A CG  1 
ATOM   7647 C  CD1 . PHE A 1 946  ? 66.980 60.666  -21.341 1.00 11.50 ? 946  PHE A CD1 1 
ATOM   7648 C  CD2 . PHE A 1 946  ? 64.711 61.388  -20.986 1.00 12.26 ? 946  PHE A CD2 1 
ATOM   7649 C  CE1 . PHE A 1 946  ? 66.817 59.684  -20.340 1.00 12.81 ? 946  PHE A CE1 1 
ATOM   7650 C  CE2 . PHE A 1 946  ? 64.542 60.420  -20.011 1.00 11.48 ? 946  PHE A CE2 1 
ATOM   7651 C  CZ  . PHE A 1 946  ? 65.578 59.559  -19.695 1.00 12.97 ? 946  PHE A CZ  1 
ATOM   7652 N  N   . GLY A 1 947  ? 65.298 59.613  -24.169 1.00 11.03 ? 947  GLY A N   1 
ATOM   7653 C  CA  . GLY A 1 947  ? 64.317 58.554  -24.186 1.00 12.14 ? 947  GLY A CA  1 
ATOM   7654 C  C   . GLY A 1 947  ? 63.966 57.987  -25.547 1.00 12.66 ? 947  GLY A C   1 
ATOM   7655 O  O   . GLY A 1 947  ? 63.016 57.220  -25.659 1.00 12.82 ? 947  GLY A O   1 
ATOM   7656 N  N   . GLY A 1 948  ? 64.752 58.312  -26.593 1.00 14.57 ? 948  GLY A N   1 
ATOM   7657 C  CA  . GLY A 1 948  ? 64.498 57.767  -27.916 1.00 16.14 ? 948  GLY A CA  1 
ATOM   7658 C  C   . GLY A 1 948  ? 64.546 56.242  -27.945 1.00 16.78 ? 948  GLY A C   1 
ATOM   7659 O  O   . GLY A 1 948  ? 63.933 55.634  -28.828 1.00 19.03 ? 948  GLY A O   1 
ATOM   7660 N  N   . ASP A 1 949  ? 65.247 55.634  -26.982 1.00 17.01 ? 949  ASP A N   1 
ATOM   7661 C  CA  . ASP A 1 949  ? 65.316 54.169  -26.883 1.00 19.17 ? 949  ASP A CA  1 
ATOM   7662 C  C   . ASP A 1 949  ? 64.316 53.542  -25.909 1.00 18.35 ? 949  ASP A C   1 
ATOM   7663 O  O   . ASP A 1 949  ? 64.326 52.308  -25.674 1.00 19.30 ? 949  ASP A O   1 
ATOM   7664 C  CB  . ASP A 1 949  ? 66.754 53.696  -26.559 1.00 20.38 ? 949  ASP A CB  1 
ATOM   7665 C  CG  . ASP A 1 949  ? 67.287 54.229  -25.218 1.00 24.65 ? 949  ASP A CG  1 
ATOM   7666 O  OD1 . ASP A 1 949  ? 66.677 55.133  -24.578 1.00 26.75 ? 949  ASP A OD1 1 
ATOM   7667 O  OD2 . ASP A 1 949  ? 68.349 53.799  -24.707 1.00 30.82 ? 949  ASP A OD2 1 
ATOM   7668 N  N   . HIS A 1 950  ? 63.430 54.366  -25.335 1.00 17.00 ? 950  HIS A N   1 
ATOM   7669 C  CA  . HIS A 1 950  ? 62.414 53.830  -24.423 1.00 14.80 ? 950  HIS A CA  1 
ATOM   7670 C  C   . HIS A 1 950  ? 61.346 53.073  -25.225 1.00 14.91 ? 950  HIS A C   1 
ATOM   7671 O  O   . HIS A 1 950  ? 60.947 53.544  -26.280 1.00 15.39 ? 950  HIS A O   1 
ATOM   7672 C  CB  . HIS A 1 950  ? 61.720 54.966  -23.660 1.00 13.72 ? 950  HIS A CB  1 
ATOM   7673 C  CG  . HIS A 1 950  ? 62.597 55.677  -22.685 1.00 12.84 ? 950  HIS A CG  1 
ATOM   7674 N  ND1 . HIS A 1 950  ? 62.217 56.860  -22.092 1.00 11.11 ? 950  HIS A ND1 1 
ATOM   7675 C  CD2 . HIS A 1 950  ? 63.826 55.385  -22.189 1.00 13.28 ? 950  HIS A CD2 1 
ATOM   7676 C  CE1 . HIS A 1 950  ? 63.162 57.270  -21.269 1.00 12.06 ? 950  HIS A CE1 1 
ATOM   7677 N  NE2 . HIS A 1 950  ? 64.154 56.390  -21.304 1.00 13.63 ? 950  HIS A NE2 1 
ATOM   7678 N  N   . PRO A 1 951  ? 60.889 51.907  -24.767 1.00 15.37 ? 951  PRO A N   1 
ATOM   7679 C  CA  . PRO A 1 951  ? 59.833 51.175  -25.481 1.00 15.44 ? 951  PRO A CA  1 
ATOM   7680 C  C   . PRO A 1 951  ? 58.538 51.972  -25.614 1.00 15.40 ? 951  PRO A C   1 
ATOM   7681 O  O   . PRO A 1 951  ? 58.119 52.653  -24.650 1.00 15.26 ? 951  PRO A O   1 
ATOM   7682 C  CB  . PRO A 1 951  ? 59.600 49.935  -24.594 1.00 16.21 ? 951  PRO A CB  1 
ATOM   7683 C  CG  . PRO A 1 951  ? 60.890 49.766  -23.893 1.00 17.92 ? 951  PRO A CG  1 
ATOM   7684 C  CD  . PRO A 1 951  ? 61.356 51.186  -23.565 1.00 16.96 ? 951  PRO A CD  1 
ATOM   7685 N  N   . SER A 1 952  ? 57.897 51.890  -26.770 1.00 14.67 ? 952  SER A N   1 
ATOM   7686 C  CA  . SER A 1 952  ? 56.634 52.566  -27.005 1.00 14.05 ? 952  SER A CA  1 
ATOM   7687 C  C   . SER A 1 952  ? 55.520 51.544  -26.826 1.00 14.14 ? 952  SER A C   1 
ATOM   7688 O  O   . SER A 1 952  ? 55.225 50.735  -27.732 1.00 15.20 ? 952  SER A O   1 
ATOM   7689 C  CB  . SER A 1 952  ? 56.610 53.221  -28.387 1.00 14.36 ? 952  SER A CB  1 
ATOM   7690 O  OG  . SER A 1 952  ? 55.540 54.135  -28.525 1.00 15.23 ? 952  SER A OG  1 
ATOM   7691 N  N   . ALA A 1 953  ? 54.906 51.548  -25.644 1.00 13.37 ? 953  ALA A N   1 
ATOM   7692 C  CA  . ALA A 1 953  ? 53.987 50.509  -25.216 1.00 13.20 ? 953  ALA A CA  1 
ATOM   7693 C  C   . ALA A 1 953  ? 52.634 50.626  -25.875 1.00 12.65 ? 953  ALA A C   1 
ATOM   7694 O  O   . ALA A 1 953  ? 52.229 51.704  -26.331 1.00 12.75 ? 953  ALA A O   1 
ATOM   7695 C  CB  . ALA A 1 953  ? 53.820 50.545  -23.689 1.00 14.23 ? 953  ALA A CB  1 
ATOM   7696 N  N   A ARG A 1 954  ? 51.902 49.518  -25.903 0.50 12.38 ? 954  ARG A N   1 
ATOM   7697 N  N   B ARG A 1 954  ? 51.911 49.511  -25.882 0.50 12.07 ? 954  ARG A N   1 
ATOM   7698 C  CA  A ARG A 1 954  ? 50.555 49.490  -26.451 0.50 13.23 ? 954  ARG A CA  1 
ATOM   7699 C  CA  B ARG A 1 954  ? 50.531 49.446  -26.342 0.50 12.53 ? 954  ARG A CA  1 
ATOM   7700 C  C   A ARG A 1 954  ? 49.695 50.570  -25.788 0.50 12.21 ? 954  ARG A C   1 
ATOM   7701 C  C   B ARG A 1 954  ? 49.686 50.590  -25.760 0.50 11.85 ? 954  ARG A C   1 
ATOM   7702 O  O   A ARG A 1 954  ? 49.851 50.868  -24.585 0.50 11.65 ? 954  ARG A O   1 
ATOM   7703 O  O   B ARG A 1 954  ? 49.848 50.965  -24.580 0.50 11.02 ? 954  ARG A O   1 
ATOM   7704 C  CB  A ARG A 1 954  ? 49.941 48.112  -26.243 0.50 13.71 ? 954  ARG A CB  1 
ATOM   7705 C  CB  B ARG A 1 954  ? 49.925 48.090  -25.972 0.50 12.88 ? 954  ARG A CB  1 
ATOM   7706 C  CG  A ARG A 1 954  ? 48.714 47.766  -27.101 0.50 15.29 ? 954  ARG A CG  1 
ATOM   7707 C  CG  B ARG A 1 954  ? 50.102 47.713  -24.513 0.50 14.04 ? 954  ARG A CG  1 
ATOM   7708 C  CD  A ARG A 1 954  ? 48.186 46.374  -26.778 0.50 16.42 ? 954  ARG A CD  1 
ATOM   7709 C  CD  B ARG A 1 954  ? 49.613 46.315  -24.161 0.50 14.97 ? 954  ARG A CD  1 
ATOM   7710 N  NE  A ARG A 1 954  ? 48.043 46.297  -25.326 0.50 21.86 ? 954  ARG A NE  1 
ATOM   7711 N  NE  B ARG A 1 954  ? 48.250 46.089  -24.633 0.50 22.28 ? 954  ARG A NE  1 
ATOM   7712 C  CZ  A ARG A 1 954  ? 48.949 45.830  -24.456 0.50 20.65 ? 954  ARG A CZ  1 
ATOM   7713 C  CZ  B ARG A 1 954  ? 47.914 45.344  -25.686 0.50 22.25 ? 954  ARG A CZ  1 
ATOM   7714 N  NH1 A ARG A 1 954  ? 50.115 45.301  -24.841 0.50 20.85 ? 954  ARG A NH1 1 
ATOM   7715 N  NH1 B ARG A 1 954  ? 48.840 44.704  -26.395 0.50 23.61 ? 954  ARG A NH1 1 
ATOM   7716 N  NH2 A ARG A 1 954  ? 48.661 45.886  -23.167 0.50 19.71 ? 954  ARG A NH2 1 
ATOM   7717 N  NH2 B ARG A 1 954  ? 46.637 45.232  -26.020 0.50 24.37 ? 954  ARG A NH2 1 
ATOM   7718 N  N   . GLU A 1 955  ? 48.767 51.112  -26.570 1.00 12.03 ? 955  GLU A N   1 
ATOM   7719 C  CA  . GLU A 1 955  ? 48.040 52.329  -26.198 1.00 12.40 ? 955  GLU A CA  1 
ATOM   7720 C  C   . GLU A 1 955  ? 47.214 52.204  -24.920 1.00 11.56 ? 955  GLU A C   1 
ATOM   7721 O  O   . GLU A 1 955  ? 46.920 53.230  -24.277 1.00 12.17 ? 955  GLU A O   1 
ATOM   7722 C  CB  . GLU A 1 955  ? 47.146 52.790  -27.352 1.00 14.45 ? 955  GLU A CB  1 
ATOM   7723 C  CG  . GLU A 1 955  ? 46.097 51.769  -27.731 1.00 15.10 ? 955  GLU A CG  1 
ATOM   7724 C  CD  . GLU A 1 955  ? 45.149 52.256  -28.798 1.00 21.17 ? 955  GLU A CD  1 
ATOM   7725 O  OE1 . GLU A 1 955  ? 44.959 53.492  -28.931 1.00 26.59 ? 955  GLU A OE1 1 
ATOM   7726 O  OE2 . GLU A 1 955  ? 44.601 51.382  -29.494 1.00 24.11 ? 955  GLU A OE2 1 
ATOM   7727 N  N   . ASP A 1 956  ? 46.807 50.984  -24.583 1.00 10.30 ? 956  ASP A N   1 
ATOM   7728 C  CA  . ASP A 1 956  ? 45.993 50.802  -23.384 1.00 10.83 ? 956  ASP A CA  1 
ATOM   7729 C  C   . ASP A 1 956  ? 46.812 50.711  -22.095 1.00 9.92  ? 956  ASP A C   1 
ATOM   7730 O  O   . ASP A 1 956  ? 46.212 50.620  -21.001 1.00 12.09 ? 956  ASP A O   1 
ATOM   7731 C  CB  . ASP A 1 956  ? 44.987 49.640  -23.518 1.00 11.12 ? 956  ASP A CB  1 
ATOM   7732 C  CG  . ASP A 1 956  ? 45.622 48.335  -23.854 1.00 14.55 ? 956  ASP A CG  1 
ATOM   7733 O  OD1 . ASP A 1 956  ? 46.839 48.282  -24.058 1.00 18.36 ? 956  ASP A OD1 1 
ATOM   7734 O  OD2 . ASP A 1 956  ? 44.920 47.292  -23.916 1.00 16.11 ? 956  ASP A OD2 1 
ATOM   7735 N  N   . LEU A 1 957  ? 48.130 50.707  -22.198 1.00 9.33  ? 957  LEU A N   1 
ATOM   7736 C  CA  . LEU A 1 957  ? 48.981 50.561  -21.004 1.00 10.37 ? 957  LEU A CA  1 
ATOM   7737 C  C   . LEU A 1 957  ? 49.555 51.922  -20.606 1.00 9.54  ? 957  LEU A C   1 
ATOM   7738 O  O   . LEU A 1 957  ? 50.011 52.689  -21.470 1.00 10.68 ? 957  LEU A O   1 
ATOM   7739 C  CB  . LEU A 1 957  ? 50.125 49.584  -21.321 1.00 11.15 ? 957  LEU A CB  1 
ATOM   7740 C  CG  . LEU A 1 957  ? 51.016 49.140  -20.161 1.00 13.67 ? 957  LEU A CG  1 
ATOM   7741 C  CD1 . LEU A 1 957  ? 50.216 48.389  -19.102 1.00 16.31 ? 957  LEU A CD1 1 
ATOM   7742 C  CD2 . LEU A 1 957  ? 52.123 48.236  -20.693 1.00 13.94 ? 957  LEU A CD2 1 
ATOM   7743 N  N   . ASP A 1 958  ? 49.581 52.209  -19.306 1.00 8.82  ? 958  ASP A N   1 
ATOM   7744 C  CA  . ASP A 1 958  ? 50.207 53.416  -18.796 1.00 8.29  ? 958  ASP A CA  1 
ATOM   7745 C  C   . ASP A 1 958  ? 51.147 53.082  -17.657 1.00 7.21  ? 958  ASP A C   1 
ATOM   7746 O  O   . ASP A 1 958  ? 50.903 52.127  -16.887 1.00 8.29  ? 958  ASP A O   1 
ATOM   7747 C  CB  . ASP A 1 958  ? 49.139 54.393  -18.311 1.00 8.82  ? 958  ASP A CB  1 
ATOM   7748 C  CG  . ASP A 1 958  ? 49.669 55.802  -18.134 1.00 9.29  ? 958  ASP A CG  1 
ATOM   7749 O  OD1 . ASP A 1 958  ? 50.784 56.129  -18.598 1.00 9.06  ? 958  ASP A OD1 1 
ATOM   7750 O  OD2 . ASP A 1 958  ? 48.956 56.610  -17.483 1.00 9.68  ? 958  ASP A OD2 1 
ATOM   7751 N  N   . VAL A 1 959  ? 52.214 53.867  -17.551 1.00 7.93  ? 959  VAL A N   1 
ATOM   7752 C  CA  . VAL A 1 959  ? 53.065 53.874  -16.363 1.00 7.96  ? 959  VAL A CA  1 
ATOM   7753 C  C   . VAL A 1 959  ? 52.523 55.002  -15.510 1.00 7.83  ? 959  VAL A C   1 
ATOM   7754 O  O   . VAL A 1 959  ? 52.922 56.172  -15.631 1.00 8.90  ? 959  VAL A O   1 
ATOM   7755 C  CB  . VAL A 1 959  ? 54.527 54.109  -16.730 1.00 8.63  ? 959  VAL A CB  1 
ATOM   7756 C  CG1 . VAL A 1 959  ? 55.428 54.229  -15.453 1.00 8.77  ? 959  VAL A CG1 1 
ATOM   7757 C  CG2 . VAL A 1 959  ? 55.053 52.949  -17.615 1.00 10.08 ? 959  VAL A CG2 1 
ATOM   7758 N  N   . SER A 1 960  ? 51.562 54.659  -14.656 1.00 7.75  ? 960  SER A N   1 
ATOM   7759 C  CA  . SER A 1 960  ? 50.842 55.623  -13.844 1.00 8.20  ? 960  SER A CA  1 
ATOM   7760 C  C   . SER A 1 960  ? 51.759 56.315  -12.855 1.00 8.29  ? 960  SER A C   1 
ATOM   7761 O  O   . SER A 1 960  ? 51.588 57.529  -12.574 1.00 8.99  ? 960  SER A O   1 
ATOM   7762 C  CB  . SER A 1 960  ? 49.733 54.944  -13.065 1.00 8.75  ? 960  SER A CB  1 
ATOM   7763 O  OG  . SER A 1 960  ? 48.899 54.156  -13.913 1.00 11.13 ? 960  SER A OG  1 
ATOM   7764 N  N   . VAL A 1 961  ? 52.729 55.567  -12.303 1.00 8.13  ? 961  VAL A N   1 
ATOM   7765 C  CA  . VAL A 1 961  ? 53.721 56.073  -11.343 1.00 8.11  ? 961  VAL A CA  1 
ATOM   7766 C  C   . VAL A 1 961  ? 55.090 55.525  -11.732 1.00 7.42  ? 961  VAL A C   1 
ATOM   7767 O  O   . VAL A 1 961  ? 55.229 54.327  -11.994 1.00 7.36  ? 961  VAL A O   1 
ATOM   7768 C  CB  . VAL A 1 961  ? 53.387 55.611  -9.930  1.00 8.57  ? 961  VAL A CB  1 
ATOM   7769 C  CG1 . VAL A 1 961  ? 54.496 56.000  -8.925  1.00 10.25 ? 961  VAL A CG1 1 
ATOM   7770 C  CG2 . VAL A 1 961  ? 52.052 56.168  -9.459  1.00 10.25 ? 961  VAL A CG2 1 
ATOM   7771 N  N   . MET A 1 962  ? 56.079 56.416  -11.733 1.00 7.79  ? 962  MET A N   1 
ATOM   7772 C  CA  . MET A 1 962  ? 57.483 56.014  -11.671 1.00 7.90  ? 962  MET A CA  1 
ATOM   7773 C  C   . MET A 1 962  ? 58.074 56.845  -10.548 1.00 7.92  ? 962  MET A C   1 
ATOM   7774 O  O   . MET A 1 962  ? 58.029 58.079  -10.559 1.00 8.58  ? 962  MET A O   1 
ATOM   7775 C  CB  . MET A 1 962  ? 58.194 56.308  -13.007 1.00 7.86  ? 962  MET A CB  1 
ATOM   7776 C  CG  . MET A 1 962  ? 59.693 56.003  -12.943 1.00 8.73  ? 962  MET A CG  1 
ATOM   7777 S  SD  . MET A 1 962  ? 60.443 56.313  -14.541 1.00 10.33 ? 962  MET A SD  1 
ATOM   7778 C  CE  . MET A 1 962  ? 62.192 55.834  -14.217 1.00 9.97  ? 962  MET A CE  1 
ATOM   7779 N  N   . ARG A 1 963  ? 58.626 56.171  -9.548  1.00 8.06  ? 963  ARG A N   1 
ATOM   7780 C  CA  . ARG A 1 963  ? 59.157 56.869  -8.386  1.00 8.01  ? 963  ARG A CA  1 
ATOM   7781 C  C   . ARG A 1 963  ? 60.390 56.155  -7.859  1.00 8.25  ? 963  ARG A C   1 
ATOM   7782 O  O   . ARG A 1 963  ? 60.343 54.959  -7.571  1.00 8.32  ? 963  ARG A O   1 
ATOM   7783 C  CB  . ARG A 1 963  ? 58.096 56.966  -7.288  1.00 8.81  ? 963  ARG A CB  1 
ATOM   7784 C  CG  . ARG A 1 963  ? 58.649 57.336  -5.921  1.00 8.88  ? 963  ARG A CG  1 
ATOM   7785 C  CD  . ARG A 1 963  ? 57.558 57.327  -4.863  1.00 9.81  ? 963  ARG A CD  1 
ATOM   7786 N  NE  . ARG A 1 963  ? 56.328 57.954  -5.339  1.00 9.52  ? 963  ARG A NE  1 
ATOM   7787 C  CZ  . ARG A 1 963  ? 55.119 57.418  -5.212  1.00 9.21  ? 963  ARG A CZ  1 
ATOM   7788 N  NH1 . ARG A 1 963  ? 54.972 56.240  -4.622  1.00 9.18  ? 963  ARG A NH1 1 
ATOM   7789 N  NH2 . ARG A 1 963  ? 54.055 58.060  -5.676  1.00 9.96  ? 963  ARG A NH2 1 
ATOM   7790 N  N   . ARG A 1 964  ? 61.494 56.883  -7.733  1.00 8.65  ? 964  ARG A N   1 
ATOM   7791 C  CA  . ARG A 1 964  ? 62.673 56.307  -7.077  1.00 9.49  ? 964  ARG A CA  1 
ATOM   7792 C  C   . ARG A 1 964  ? 62.387 56.255  -5.571  1.00 9.24  ? 964  ARG A C   1 
ATOM   7793 O  O   . ARG A 1 964  ? 61.938 57.231  -4.965  1.00 9.48  ? 964  ARG A O   1 
ATOM   7794 C  CB  . ARG A 1 964  ? 63.909 57.151  -7.388  1.00 8.75  ? 964  ARG A CB  1 
ATOM   7795 C  CG  . ARG A 1 964  ? 65.196 56.481  -6.825  1.00 9.82  ? 964  ARG A CG  1 
ATOM   7796 C  CD  . ARG A 1 964  ? 66.500 57.143  -7.277  1.00 10.39 ? 964  ARG A CD  1 
ATOM   7797 N  NE  . ARG A 1 964  ? 66.677 56.998  -8.710  1.00 11.84 ? 964  ARG A NE  1 
ATOM   7798 C  CZ  . ARG A 1 964  ? 67.602 56.246  -9.275  1.00 12.17 ? 964  ARG A CZ  1 
ATOM   7799 N  NH1 . ARG A 1 964  ? 68.463 55.536  -8.520  1.00 15.22 ? 964  ARG A NH1 1 
ATOM   7800 N  NH2 . ARG A 1 964  ? 67.708 56.196  -10.596 1.00 12.74 ? 964  ARG A NH2 1 
ATOM   7801 N  N   . LEU A 1 965  ? 62.672 55.086  -5.001  1.00 9.19  ? 965  LEU A N   1 
ATOM   7802 C  CA  . LEU A 1 965  ? 62.288 54.799  -3.623  1.00 9.04  ? 965  LEU A CA  1 
ATOM   7803 C  C   . LEU A 1 965  ? 63.437 54.943  -2.623  1.00 10.88 ? 965  LEU A C   1 
ATOM   7804 O  O   . LEU A 1 965  ? 63.211 54.863  -1.414  1.00 12.43 ? 965  LEU A O   1 
ATOM   7805 C  CB  . LEU A 1 965  ? 61.740 53.389  -3.541  1.00 10.55 ? 965  LEU A CB  1 
ATOM   7806 C  CG  . LEU A 1 965  ? 60.494 53.127  -4.409  1.00 9.51  ? 965  LEU A CG  1 
ATOM   7807 C  CD1 . LEU A 1 965  ? 60.090 51.679  -4.360  1.00 11.72 ? 965  LEU A CD1 1 
ATOM   7808 C  CD2 . LEU A 1 965  ? 59.304 54.003  -3.982  1.00 13.21 ? 965  LEU A CD2 1 
ATOM   7809 N  N   . THR A 1 966  ? 64.659 55.122  -3.138  1.00 11.37 ? 966  THR A N   1 
ATOM   7810 C  CA  . THR A 1 966  ? 65.883 55.189  -2.297  1.00 11.09 ? 966  THR A CA  1 
ATOM   7811 C  C   . THR A 1 966  ? 66.574 56.516  -2.507  1.00 10.95 ? 966  THR A C   1 
ATOM   7812 O  O   . THR A 1 966  ? 66.552 57.061  -3.606  1.00 11.54 ? 966  THR A O   1 
ATOM   7813 C  CB  . THR A 1 966  ? 66.871 54.104  -2.713  1.00 12.34 ? 966  THR A CB  1 
ATOM   7814 O  OG1 . THR A 1 966  ? 66.901 54.006  -4.134  1.00 12.40 ? 966  THR A OG1 1 
ATOM   7815 C  CG2 . THR A 1 966  ? 66.440 52.722  -2.218  1.00 13.20 ? 966  THR A CG2 1 
ATOM   7816 N  N   . LYS A 1 967  ? 67.226 57.002  -1.453  1.00 11.86 ? 967  LYS A N   1 
ATOM   7817 C  CA  . LYS A 1 967  ? 68.067 58.190  -1.507  1.00 12.75 ? 967  LYS A CA  1 
ATOM   7818 C  C   . LYS A 1 967  ? 69.454 57.762  -1.982  1.00 12.54 ? 967  LYS A C   1 
ATOM   7819 O  O   . LYS A 1 967  ? 69.703 56.570  -2.131  1.00 12.49 ? 967  LYS A O   1 
ATOM   7820 C  CB  . LYS A 1 967  ? 68.138 58.858  -0.138  1.00 13.39 ? 967  LYS A CB  1 
ATOM   7821 C  CG  . LYS A 1 967  ? 66.739 59.312  0.386   1.00 17.63 ? 967  LYS A CG  1 
ATOM   7822 C  CD  . LYS A 1 967  ? 66.883 60.114  1.668   1.00 22.78 ? 967  LYS A CD  1 
ATOM   7823 C  CE  . LYS A 1 967  ? 65.536 60.404  2.319   1.00 29.20 ? 967  LYS A CE  1 
ATOM   7824 N  NZ  . LYS A 1 967  ? 64.791 61.427  1.543   1.00 32.57 ? 967  LYS A NZ  1 
ATOM   7825 N  N   . SER A 1 968  ? 70.305 58.754  -2.266  1.00 14.26 ? 968  SER A N   1 
ATOM   7826 C  CA  . SER A 1 968  ? 71.572 58.492  -2.969  1.00 16.31 ? 968  SER A CA  1 
ATOM   7827 C  C   . SER A 1 968  ? 72.551 57.626  -2.183  1.00 17.45 ? 968  SER A C   1 
ATOM   7828 O  O   . SER A 1 968  ? 73.368 56.935  -2.793  1.00 19.51 ? 968  SER A O   1 
ATOM   7829 C  CB  . SER A 1 968  ? 72.247 59.798  -3.377  1.00 16.83 ? 968  SER A CB  1 
ATOM   7830 O  OG  . SER A 1 968  ? 72.498 60.607  -2.254  1.00 21.39 ? 968  SER A OG  1 
ATOM   7831 N  N   . SER A 1 969  ? 72.418 57.615  -0.857  1.00 18.13 ? 969  SER A N   1 
ATOM   7832 C  CA  . SER A 1 969  ? 73.348 56.838  -0.009  1.00 19.61 ? 969  SER A CA  1 
ATOM   7833 C  C   . SER A 1 969  ? 73.096 55.329  -0.017  1.00 19.14 ? 969  SER A C   1 
ATOM   7834 O  O   . SER A 1 969  ? 73.931 54.567  0.474   1.00 19.33 ? 969  SER A O   1 
ATOM   7835 C  CB  . SER A 1 969  ? 73.371 57.380  1.407   1.00 21.45 ? 969  SER A CB  1 
ATOM   7836 O  OG  . SER A 1 969  ? 72.070 57.326  1.950   1.00 25.72 ? 969  SER A OG  1 
ATOM   7837 N  N   . ALA A 1 970  ? 71.966 54.871  -0.555  1.00 17.56 ? 970  ALA A N   1 
ATOM   7838 C  CA  . ALA A 1 970  ? 71.689 53.445  -0.659  1.00 17.57 ? 970  ALA A CA  1 
ATOM   7839 C  C   . ALA A 1 970  ? 72.539 52.759  -1.710  1.00 18.44 ? 970  ALA A C   1 
ATOM   7840 O  O   . ALA A 1 970  ? 72.520 53.140  -2.885  1.00 17.48 ? 970  ALA A O   1 
ATOM   7841 C  CB  . ALA A 1 970  ? 70.184 53.177  -0.950  1.00 17.86 ? 970  ALA A CB  1 
ATOM   7842 N  N   A LYS A 1 971  ? 73.278 51.733  -1.280  0.50 18.77 ? 971  LYS A N   1 
ATOM   7843 N  N   B LYS A 1 971  ? 73.288 51.737  -1.293  0.50 18.64 ? 971  LYS A N   1 
ATOM   7844 C  CA  A LYS A 1 971  ? 74.073 50.885  -2.169  0.50 19.76 ? 971  LYS A CA  1 
ATOM   7845 C  CA  B LYS A 1 971  ? 74.074 50.940  -2.230  0.50 19.54 ? 971  LYS A CA  1 
ATOM   7846 C  C   A LYS A 1 971  ? 73.220 50.260  -3.275  0.50 19.47 ? 971  LYS A C   1 
ATOM   7847 C  C   B LYS A 1 971  ? 73.182 50.333  -3.307  0.50 19.30 ? 971  LYS A C   1 
ATOM   7848 O  O   A LYS A 1 971  ? 73.624 50.218  -4.435  0.50 19.89 ? 971  LYS A O   1 
ATOM   7849 O  O   B LYS A 1 971  ? 73.518 50.389  -4.489  0.50 19.78 ? 971  LYS A O   1 
ATOM   7850 C  CB  A LYS A 1 971  ? 74.765 49.782  -1.348  0.50 19.95 ? 971  LYS A CB  1 
ATOM   7851 C  CB  B LYS A 1 971  ? 74.863 49.838  -1.504  0.50 19.66 ? 971  LYS A CB  1 
ATOM   7852 C  CG  A LYS A 1 971  ? 75.802 48.956  -2.104  0.50 21.23 ? 971  LYS A CG  1 
ATOM   7853 C  CG  B LYS A 1 971  ? 75.826 50.350  -0.447  0.50 20.94 ? 971  LYS A CG  1 
ATOM   7854 C  CD  A LYS A 1 971  ? 76.513 47.947  -1.178  0.50 20.90 ? 971  LYS A CD  1 
ATOM   7855 C  CD  B LYS A 1 971  ? 76.735 49.243  0.078   0.50 20.50 ? 971  LYS A CD  1 
ATOM   7856 C  CE  A LYS A 1 971  ? 77.132 48.594  0.059   0.50 25.00 ? 971  LYS A CE  1 
ATOM   7857 C  CE  B LYS A 1 971  ? 75.975 48.170  0.869   0.50 21.75 ? 971  LYS A CE  1 
ATOM   7858 N  NZ  A LYS A 1 971  ? 78.198 49.595  -0.244  0.50 25.82 ? 971  LYS A NZ  1 
ATOM   7859 N  NZ  B LYS A 1 971  ? 75.221 48.745  2.006   0.50 23.14 ? 971  LYS A NZ  1 
ATOM   7860 N  N   . THR A 1 972  ? 72.046 49.759  -2.897  1.00 18.78 ? 972  THR A N   1 
ATOM   7861 C  CA  . THR A 1 972  ? 71.090 49.211  -3.858  1.00 17.81 ? 972  THR A CA  1 
ATOM   7862 C  C   . THR A 1 972  ? 69.967 50.232  -4.117  1.00 16.46 ? 972  THR A C   1 
ATOM   7863 O  O   . THR A 1 972  ? 69.171 50.530  -3.225  1.00 16.63 ? 972  THR A O   1 
ATOM   7864 C  CB  . THR A 1 972  ? 70.518 47.840  -3.420  1.00 18.53 ? 972  THR A CB  1 
ATOM   7865 O  OG1 . THR A 1 972  ? 71.600 46.911  -3.234  1.00 21.33 ? 972  THR A OG1 1 
ATOM   7866 C  CG2 . THR A 1 972  ? 69.727 47.185  -4.555  1.00 19.66 ? 972  THR A CG2 1 
ATOM   7867 N  N   . GLN A 1 973  ? 69.947 50.789  -5.319  1.00 14.60 ? 973  GLN A N   1 
ATOM   7868 C  CA  . GLN A 1 973  ? 68.888 51.753  -5.661  1.00 13.16 ? 973  GLN A CA  1 
ATOM   7869 C  C   . GLN A 1 973  ? 67.629 50.984  -6.015  1.00 13.09 ? 973  GLN A C   1 
ATOM   7870 O  O   . GLN A 1 973  ? 67.703 49.936  -6.621  1.00 13.81 ? 973  GLN A O   1 
ATOM   7871 C  CB  . GLN A 1 973  ? 69.362 52.624  -6.826  1.00 12.17 ? 973  GLN A CB  1 
ATOM   7872 C  CG  . GLN A 1 973  ? 70.453 53.630  -6.396  1.00 11.95 ? 973  GLN A CG  1 
ATOM   7873 C  CD  . GLN A 1 973  ? 69.959 54.644  -5.392  1.00 13.57 ? 973  GLN A CD  1 
ATOM   7874 O  OE1 . GLN A 1 973  ? 68.940 55.314  -5.631  1.00 13.27 ? 973  GLN A OE1 1 
ATOM   7875 N  NE2 . GLN A 1 973  ? 70.647 54.784  -4.269  1.00 13.57 ? 973  GLN A NE2 1 
ATOM   7876 N  N   . ARG A 1 974  ? 66.458 51.555  -5.681  1.00 12.32 ? 974  ARG A N   1 
ATOM   7877 C  CA  A ARG A 1 974  ? 65.189 50.922  -6.031  0.50 11.67 ? 974  ARG A CA  1 
ATOM   7878 C  CA  B ARG A 1 974  ? 65.158 50.931  -5.926  0.50 12.08 ? 974  ARG A CA  1 
ATOM   7879 C  C   . ARG A 1 974  ? 64.245 51.921  -6.656  1.00 10.95 ? 974  ARG A C   1 
ATOM   7880 O  O   . ARG A 1 974  ? 64.159 53.056  -6.218  1.00 10.76 ? 974  ARG A O   1 
ATOM   7881 C  CB  A ARG A 1 974  ? 64.507 50.285  -4.833  0.50 11.88 ? 974  ARG A CB  1 
ATOM   7882 C  CB  B ARG A 1 974  ? 64.516 50.536  -4.593  0.50 12.00 ? 974  ARG A CB  1 
ATOM   7883 C  CG  A ARG A 1 974  ? 65.342 49.201  -4.141  0.50 10.93 ? 974  ARG A CG  1 
ATOM   7884 C  CG  B ARG A 1 974  ? 65.254 49.381  -3.863  0.50 12.16 ? 974  ARG A CG  1 
ATOM   7885 C  CD  A ARG A 1 974  ? 64.852 48.859  -2.741  0.50 13.78 ? 974  ARG A CD  1 
ATOM   7886 C  CD  B ARG A 1 974  ? 64.900 49.225  -2.374  0.50 14.03 ? 974  ARG A CD  1 
ATOM   7887 N  NE  A ARG A 1 974  ? 63.588 48.144  -2.766  0.50 15.48 ? 974  ARG A NE  1 
ATOM   7888 N  NE  B ARG A 1 974  ? 63.466 49.274  -2.112  0.50 17.02 ? 974  ARG A NE  1 
ATOM   7889 C  CZ  A ARG A 1 974  ? 62.432 48.559  -2.242  0.50 16.25 ? 974  ARG A CZ  1 
ATOM   7890 C  CZ  B ARG A 1 974  ? 62.609 48.273  -2.294  0.50 20.13 ? 974  ARG A CZ  1 
ATOM   7891 N  NH1 A ARG A 1 974  ? 62.308 49.716  -1.598  0.50 15.55 ? 974  ARG A NH1 1 
ATOM   7892 N  NH1 B ARG A 1 974  ? 63.015 47.096  -2.759  0.50 20.80 ? 974  ARG A NH1 1 
ATOM   7893 N  NH2 A ARG A 1 974  ? 61.382 47.773  -2.367  0.50 13.98 ? 974  ARG A NH2 1 
ATOM   7894 N  NH2 B ARG A 1 974  ? 61.325 48.459  -2.022  0.50 19.37 ? 974  ARG A NH2 1 
ATOM   7895 N  N   . VAL A 1 975  ? 63.582 51.481  -7.712  1.00 10.50 ? 975  VAL A N   1 
ATOM   7896 C  CA  . VAL A 1 975  ? 62.630 52.350  -8.426  1.00 10.92 ? 975  VAL A CA  1 
ATOM   7897 C  C   . VAL A 1 975  ? 61.328 51.592  -8.519  1.00 10.46 ? 975  VAL A C   1 
ATOM   7898 O  O   . VAL A 1 975  ? 61.303 50.426  -8.953  1.00 10.75 ? 975  VAL A O   1 
ATOM   7899 C  CB  . VAL A 1 975  ? 63.159 52.716  -9.839  1.00 11.16 ? 975  VAL A CB  1 
ATOM   7900 C  CG1 . VAL A 1 975  ? 62.149 53.610  -10.576 1.00 11.85 ? 975  VAL A CG1 1 
ATOM   7901 C  CG2 . VAL A 1 975  ? 64.487 53.515  -9.734  1.00 14.10 ? 975  VAL A CG2 1 
ATOM   7902 N  N   . GLY A 1 976  ? 60.240 52.273  -8.148  1.00 9.31  ? 976  GLY A N   1 
ATOM   7903 C  CA  . GLY A 1 976  ? 58.920 51.669  -8.197  1.00 10.09 ? 976  GLY A CA  1 
ATOM   7904 C  C   . GLY A 1 976  ? 58.105 52.165  -9.377  1.00 8.60  ? 976  GLY A C   1 
ATOM   7905 O  O   . GLY A 1 976  ? 58.189 53.347  -9.759  1.00 9.24  ? 976  GLY A O   1 
ATOM   7906 N  N   . TYR A 1 977  ? 57.337 51.261  -9.945  1.00 8.42  ? 977  TYR A N   1 
ATOM   7907 C  CA  . TYR A 1 977  ? 56.457 51.553  -11.077 1.00 7.90  ? 977  TYR A CA  1 
ATOM   7908 C  C   . TYR A 1 977  ? 55.062 51.041  -10.771 1.00 8.08  ? 977  TYR A C   1 
ATOM   7909 O  O   . TYR A 1 977  ? 54.912 49.914  -10.278 1.00 8.84  ? 977  TYR A O   1 
ATOM   7910 C  CB  . TYR A 1 977  ? 56.937 50.823  -12.332 1.00 8.83  ? 977  TYR A CB  1 
ATOM   7911 C  CG  . TYR A 1 977  ? 58.334 51.191  -12.742 1.00 8.68  ? 977  TYR A CG  1 
ATOM   7912 C  CD1 . TYR A 1 977  ? 58.555 52.264  -13.615 1.00 9.75  ? 977  TYR A CD1 1 
ATOM   7913 C  CD2 . TYR A 1 977  ? 59.439 50.489  -12.246 1.00 10.57 ? 977  TYR A CD2 1 
ATOM   7914 C  CE1 . TYR A 1 977  ? 59.827 52.619  -14.025 1.00 10.17 ? 977  TYR A CE1 1 
ATOM   7915 C  CE2 . TYR A 1 977  ? 60.753 50.843  -12.670 1.00 10.88 ? 977  TYR A CE2 1 
ATOM   7916 C  CZ  . TYR A 1 977  ? 60.916 51.919  -13.541 1.00 10.07 ? 977  TYR A CZ  1 
ATOM   7917 O  OH  . TYR A 1 977  ? 62.170 52.322  -13.987 1.00 11.67 ? 977  TYR A OH  1 
ATOM   7918 N  N   . VAL A 1 978  ? 54.031 51.847  -11.071 1.00 7.61  ? 978  VAL A N   1 
ATOM   7919 C  CA  . VAL A 1 978  ? 52.657 51.354  -11.076 1.00 8.22  ? 978  VAL A CA  1 
ATOM   7920 C  C   . VAL A 1 978  ? 52.218 51.317  -12.534 1.00 8.33  ? 978  VAL A C   1 
ATOM   7921 O  O   . VAL A 1 978  ? 52.308 52.347  -13.225 1.00 8.72  ? 978  VAL A O   1 
ATOM   7922 C  CB  . VAL A 1 978  ? 51.682 52.240  -10.266 1.00 8.41  ? 978  VAL A CB  1 
ATOM   7923 C  CG1 . VAL A 1 978  ? 50.260 51.711  -10.437 1.00 9.35  ? 978  VAL A CG1 1 
ATOM   7924 C  CG2 . VAL A 1 978  ? 52.108 52.234  -8.775  1.00 9.24  ? 978  VAL A CG2 1 
ATOM   7925 N  N   . LEU A 1 979  ? 51.833 50.146  -13.013 1.00 8.25  ? 979  LEU A N   1 
ATOM   7926 C  CA  . LEU A 1 979  ? 51.367 49.957  -14.371 1.00 9.96  ? 979  LEU A CA  1 
ATOM   7927 C  C   . LEU A 1 979  ? 49.884 49.705  -14.355 1.00 9.31  ? 979  LEU A C   1 
ATOM   7928 O  O   . LEU A 1 979  ? 49.391 48.838  -13.640 1.00 11.22 ? 979  LEU A O   1 
ATOM   7929 C  CB  . LEU A 1 979  ? 51.999 48.713  -15.006 1.00 12.83 ? 979  LEU A CB  1 
ATOM   7930 C  CG  . LEU A 1 979  ? 53.509 48.672  -15.165 1.00 17.41 ? 979  LEU A CG  1 
ATOM   7931 C  CD1 . LEU A 1 979  ? 53.849 47.627  -16.236 1.00 21.54 ? 979  LEU A CD1 1 
ATOM   7932 C  CD2 . LEU A 1 979  ? 54.051 50.023  -15.551 1.00 21.99 ? 979  LEU A CD2 1 
ATOM   7933 N  N   . HIS A 1 980  ? 49.160 50.449  -15.169 1.00 8.55  ? 980  HIS A N   1 
ATOM   7934 C  CA  . HIS A 1 980  ? 47.731 50.271  -15.320 1.00 9.29  ? 980  HIS A CA  1 
ATOM   7935 C  C   . HIS A 1 980  ? 47.345 49.986  -16.762 1.00 9.76  ? 980  HIS A C   1 
ATOM   7936 O  O   . HIS A 1 980  ? 47.779 50.727  -17.652 1.00 10.46 ? 980  HIS A O   1 
ATOM   7937 C  CB  . HIS A 1 980  ? 46.956 51.528  -14.861 1.00 9.58  ? 980  HIS A CB  1 
ATOM   7938 C  CG  . HIS A 1 980  ? 45.486 51.381  -15.032 1.00 9.81  ? 980  HIS A CG  1 
ATOM   7939 N  ND1 . HIS A 1 980  ? 44.764 50.448  -14.325 1.00 9.84  ? 980  HIS A ND1 1 
ATOM   7940 C  CD2 . HIS A 1 980  ? 44.617 51.944  -15.905 1.00 10.10 ? 980  HIS A CD2 1 
ATOM   7941 C  CE1 . HIS A 1 980  ? 43.503 50.464  -14.730 1.00 11.98 ? 980  HIS A CE1 1 
ATOM   7942 N  NE2 . HIS A 1 980  ? 43.389 51.362  -15.693 1.00 11.40 ? 980  HIS A NE2 1 
ATOM   7943 N  N   . ARG A 1 981  ? 46.586 48.917  -17.003 1.00 8.54  ? 981  ARG A N   1 
ATOM   7944 C  CA  . ARG A 1 981  ? 46.089 48.674  -18.351 1.00 9.66  ? 981  ARG A CA  1 
ATOM   7945 C  C   . ARG A 1 981  ? 44.600 48.875  -18.314 1.00 9.32  ? 981  ARG A C   1 
ATOM   7946 O  O   . ARG A 1 981  ? 43.905 48.244  -17.511 1.00 9.70  ? 981  ARG A O   1 
ATOM   7947 C  CB  . ARG A 1 981  ? 46.417 47.263  -18.793 1.00 11.57 ? 981  ARG A CB  1 
ATOM   7948 C  CG  . ARG A 1 981  ? 46.129 47.065  -20.246 1.00 15.74 ? 981  ARG A CG  1 
ATOM   7949 C  CD  . ARG A 1 981  ? 46.805 45.854  -20.783 1.00 20.89 ? 981  ARG A CD  1 
ATOM   7950 N  NE  . ARG A 1 981  ? 46.214 45.483  -22.046 1.00 23.52 ? 981  ARG A NE  1 
ATOM   7951 C  CZ  . ARG A 1 981  ? 46.243 44.251  -22.527 1.00 27.12 ? 981  ARG A CZ  1 
ATOM   7952 N  NH1 . ARG A 1 981  ? 46.844 43.285  -21.830 1.00 26.40 ? 981  ARG A NH1 1 
ATOM   7953 N  NH2 . ARG A 1 981  ? 45.671 43.986  -23.696 1.00 27.77 ? 981  ARG A NH2 1 
ATOM   7954 N  N   . THR A 1 982  ? 44.105 49.779  -19.149 1.00 9.89  ? 982  THR A N   1 
ATOM   7955 C  CA  . THR A 1 982  ? 42.664 49.963  -19.256 1.00 9.91  ? 982  THR A CA  1 
ATOM   7956 C  C   . THR A 1 982  ? 42.113 48.911  -20.228 1.00 10.30 ? 982  THR A C   1 
ATOM   7957 O  O   . THR A 1 982  ? 42.834 47.995  -20.602 1.00 11.88 ? 982  THR A O   1 
ATOM   7958 C  CB  . THR A 1 982  ? 42.362 51.417  -19.682 1.00 9.77  ? 982  THR A CB  1 
ATOM   7959 O  OG1 . THR A 1 982  ? 40.959 51.681  -19.549 1.00 10.51 ? 982  THR A OG1 1 
ATOM   7960 C  CG2 . THR A 1 982  ? 42.780 51.735  -21.138 1.00 11.57 ? 982  THR A CG2 1 
ATOM   7961 N  N   . ASN A 1 983  ? 40.834 49.005  -20.550 1.00 10.31 ? 983  ASN A N   1 
ATOM   7962 C  CA  . ASN A 1 983  ? 40.252 48.130  -21.583 1.00 10.21 ? 983  ASN A CA  1 
ATOM   7963 C  C   . ASN A 1 983  ? 39.522 49.010  -22.586 1.00 10.53 ? 983  ASN A C   1 
ATOM   7964 O  O   . ASN A 1 983  ? 38.657 49.790  -22.204 1.00 10.95 ? 983  ASN A O   1 
ATOM   7965 C  CB  . ASN A 1 983  ? 39.290 47.106  -20.989 1.00 10.64 ? 983  ASN A CB  1 
ATOM   7966 C  CG  . ASN A 1 983  ? 38.776 46.150  -22.031 1.00 10.40 ? 983  ASN A CG  1 
ATOM   7967 O  OD1 . ASN A 1 983  ? 39.503 45.276  -22.431 1.00 12.66 ? 983  ASN A OD1 1 
ATOM   7968 N  ND2 . ASN A 1 983  ? 37.565 46.361  -22.500 1.00 10.90 ? 983  ASN A ND2 1 
ATOM   7969 N  N   . LEU A 1 984  ? 39.976 48.939  -23.832 1.00 9.97  ? 984  LEU A N   1 
ATOM   7970 C  CA  . LEU A 1 984  ? 39.423 49.734  -24.941 1.00 11.75 ? 984  LEU A CA  1 
ATOM   7971 C  C   . LEU A 1 984  ? 38.599 48.828  -25.829 1.00 13.24 ? 984  LEU A C   1 
ATOM   7972 O  O   . LEU A 1 984  ? 38.929 47.658  -26.010 1.00 12.96 ? 984  LEU A O   1 
ATOM   7973 C  CB  . LEU A 1 984  ? 40.555 50.339  -25.773 1.00 12.09 ? 984  LEU A CB  1 
ATOM   7974 C  CG  . LEU A 1 984  ? 41.515 51.195  -24.933 1.00 13.23 ? 984  LEU A CG  1 
ATOM   7975 C  CD1 . LEU A 1 984  ? 42.676 51.654  -25.798 1.00 15.27 ? 984  LEU A CD1 1 
ATOM   7976 C  CD2 . LEU A 1 984  ? 40.803 52.361  -24.265 1.00 12.13 ? 984  LEU A CD2 1 
ATOM   7977 N  N   A MET A 1 985  ? 37.535 49.369  -26.393 0.50 13.61 ? 985  MET A N   1 
ATOM   7978 N  N   B MET A 1 985  ? 37.525 49.371  -26.390 0.50 13.68 ? 985  MET A N   1 
ATOM   7979 C  CA  A MET A 1 985  ? 36.655 48.595  -27.266 0.50 15.93 ? 985  MET A CA  1 
ATOM   7980 C  CA  B MET A 1 985  ? 36.633 48.620  -27.289 0.50 15.91 ? 985  MET A CA  1 
ATOM   7981 C  C   A MET A 1 985  ? 37.343 48.168  -28.541 0.50 16.46 ? 985  MET A C   1 
ATOM   7982 C  C   B MET A 1 985  ? 37.354 48.164  -28.538 0.50 16.55 ? 985  MET A C   1 
ATOM   7983 O  O   A MET A 1 985  ? 38.113 48.919  -29.111 0.50 16.58 ? 985  MET A O   1 
ATOM   7984 O  O   B MET A 1 985  ? 38.135 48.906  -29.105 0.50 16.57 ? 985  MET A O   1 
ATOM   7985 C  CB  A MET A 1 985  ? 35.426 49.413  -27.606 0.50 15.59 ? 985  MET A CB  1 
ATOM   7986 C  CB  B MET A 1 985  ? 35.472 49.494  -27.754 0.50 16.31 ? 985  MET A CB  1 
ATOM   7987 C  CG  A MET A 1 985  ? 34.523 49.620  -26.439 0.50 17.24 ? 985  MET A CG  1 
ATOM   7988 C  CG  B MET A 1 985  ? 34.552 50.005  -26.696 0.50 17.40 ? 985  MET A CG  1 
ATOM   7989 S  SD  A MET A 1 985  ? 32.830 49.414  -26.954 0.50 18.00 ? 985  MET A SD  1 
ATOM   7990 S  SD  B MET A 1 985  ? 32.888 49.377  -26.922 0.50 22.34 ? 985  MET A SD  1 
ATOM   7991 C  CE  A MET A 1 985  ? 32.675 50.955  -27.843 0.50 18.35 ? 985  MET A CE  1 
ATOM   7992 C  CE  B MET A 1 985  ? 33.126 48.096  -25.708 0.50 16.90 ? 985  MET A CE  1 
ATOM   7993 N  N   . GLN A 1 986  ? 37.048 46.947  -28.973 1.00 17.35 ? 986  GLN A N   1 
ATOM   7994 C  CA  . GLN A 1 986  ? 37.518 46.444  -30.263 1.00 18.77 ? 986  GLN A CA  1 
ATOM   7995 C  C   . GLN A 1 986  ? 36.517 46.941  -31.282 1.00 18.70 ? 986  GLN A C   1 
ATOM   7996 O  O   . GLN A 1 986  ? 35.343 46.593  -31.215 1.00 18.26 ? 986  GLN A O   1 
ATOM   7997 C  CB  . GLN A 1 986  ? 37.520 44.901  -30.288 1.00 20.24 ? 986  GLN A CB  1 
ATOM   7998 C  CG  . GLN A 1 986  ? 38.510 44.220  -29.358 1.00 23.64 ? 986  GLN A CG  1 
ATOM   7999 C  CD  . GLN A 1 986  ? 39.944 44.364  -29.827 1.00 28.82 ? 986  GLN A CD  1 
ATOM   8000 O  OE1 . GLN A 1 986  ? 40.214 44.432  -31.036 1.00 30.67 ? 986  GLN A OE1 1 
ATOM   8001 N  NE2 . GLN A 1 986  ? 40.867 44.420  -28.877 1.00 31.42 ? 986  GLN A NE2 1 
ATOM   8002 N  N   . CYS A 1 987  ? 36.975 47.780  -32.209 1.00 20.01 ? 987  CYS A N   1 
ATOM   8003 C  CA  . CYS A 1 987  ? 36.080 48.295  -33.242 1.00 21.96 ? 987  CYS A CA  1 
ATOM   8004 C  C   . CYS A 1 987  ? 36.575 48.042  -34.666 1.00 23.25 ? 987  CYS A C   1 
ATOM   8005 O  O   . CYS A 1 987  ? 36.062 48.653  -35.603 1.00 23.42 ? 987  CYS A O   1 
ATOM   8006 C  CB  . CYS A 1 987  ? 35.753 49.772  -33.017 1.00 22.10 ? 987  CYS A CB  1 
ATOM   8007 S  SG  . CYS A 1 987  ? 35.103 50.119  -31.366 1.00 24.16 ? 987  CYS A SG  1 
ATOM   8008 N  N   . GLY A 1 988  ? 37.538 47.141  -34.830 1.00 24.71 ? 988  GLY A N   1 
ATOM   8009 C  CA  . GLY A 1 988  ? 37.997 46.761  -36.157 1.00 29.32 ? 988  GLY A CA  1 
ATOM   8010 C  C   . GLY A 1 988  ? 39.221 47.482  -36.672 1.00 32.36 ? 988  GLY A C   1 
ATOM   8011 O  O   . GLY A 1 988  ? 39.609 47.295  -37.836 1.00 32.74 ? 988  GLY A O   1 
ATOM   8012 N  N   . THR A 1 989  ? 39.841 48.299  -35.823 1.00 34.80 ? 989  THR A N   1 
ATOM   8013 C  CA  . THR A 1 989  ? 41.086 48.969  -36.189 1.00 37.44 ? 989  THR A CA  1 
ATOM   8014 C  C   . THR A 1 989  ? 42.253 48.076  -35.790 1.00 39.27 ? 989  THR A C   1 
ATOM   8015 O  O   . THR A 1 989  ? 42.442 47.805  -34.603 1.00 39.39 ? 989  THR A O   1 
ATOM   8016 C  CB  . THR A 1 989  ? 41.196 50.331  -35.493 1.00 37.19 ? 989  THR A CB  1 
ATOM   8017 O  OG1 . THR A 1 989  ? 39.985 51.070  -35.700 1.00 37.66 ? 989  THR A OG1 1 
ATOM   8018 C  CG2 . THR A 1 989  ? 42.266 51.188  -36.160 1.00 37.58 ? 989  THR A CG2 1 
ATOM   8019 N  N   . PRO A 1 990  ? 43.028 47.606  -36.770 1.00 41.21 ? 990  PRO A N   1 
ATOM   8020 C  CA  . PRO A 1 990  ? 44.168 46.729  -36.477 1.00 42.54 ? 990  PRO A CA  1 
ATOM   8021 C  C   . PRO A 1 990  ? 45.164 47.358  -35.493 1.00 43.83 ? 990  PRO A C   1 
ATOM   8022 O  O   . PRO A 1 990  ? 45.609 46.632  -34.600 1.00 44.32 ? 990  PRO A O   1 
ATOM   8023 C  CB  . PRO A 1 990  ? 44.812 46.510  -37.852 1.00 42.71 ? 990  PRO A CB  1 
ATOM   8024 C  CG  . PRO A 1 990  ? 43.702 46.745  -38.832 1.00 42.20 ? 990  PRO A CG  1 
ATOM   8025 C  CD  . PRO A 1 990  ? 42.899 47.874  -38.216 1.00 41.41 ? 990  PRO A CD  1 
ATOM   8026 N  N   . GLU A 1 991  ? 45.478 48.652  -35.633 1.00 44.65 ? 991  GLU A N   1 
ATOM   8027 C  CA  . GLU A 1 991  ? 46.472 49.328  -34.782 1.00 45.83 ? 991  GLU A CA  1 
ATOM   8028 C  C   . GLU A 1 991  ? 47.468 48.345  -34.147 1.00 45.85 ? 991  GLU A C   1 
ATOM   8029 O  O   . GLU A 1 991  ? 47.294 47.931  -33.004 1.00 46.58 ? 991  GLU A O   1 
ATOM   8030 C  CB  . GLU A 1 991  ? 45.770 50.152  -33.693 1.00 45.64 ? 991  GLU A CB  1 
ATOM   8031 C  CG  . GLU A 1 991  ? 45.485 51.600  -34.069 1.00 46.46 ? 991  GLU A CG  1 
ATOM   8032 C  CD  . GLU A 1 991  ? 44.434 52.258  -33.179 1.00 46.86 ? 991  GLU A CD  1 
ATOM   8033 O  OE1 . GLU A 1 991  ? 43.983 51.628  -32.194 1.00 47.34 ? 991  GLU A OE1 1 
ATOM   8034 O  OE2 . GLU A 1 991  ? 44.045 53.413  -33.470 1.00 48.43 ? 991  GLU A OE2 1 
ATOM   8035 N  N   . GLU A 1 992  ? 48.499 47.952  -34.885 1.00 45.88 ? 992  GLU A N   1 
ATOM   8036 C  CA  . GLU A 1 992  ? 49.355 46.865  -34.412 1.00 45.83 ? 992  GLU A CA  1 
ATOM   8037 C  C   . GLU A 1 992  ? 50.805 47.252  -34.145 1.00 44.85 ? 992  GLU A C   1 
ATOM   8038 O  O   . GLU A 1 992  ? 51.127 48.439  -34.020 1.00 45.44 ? 992  GLU A O   1 
ATOM   8039 C  CB  . GLU A 1 992  ? 49.271 45.646  -35.350 1.00 46.35 ? 992  GLU A CB  1 
ATOM   8040 C  CG  . GLU A 1 992  ? 48.043 44.761  -35.137 1.00 48.19 ? 992  GLU A CG  1 
ATOM   8041 C  CD  . GLU A 1 992  ? 47.793 44.402  -33.670 1.00 51.20 ? 992  GLU A CD  1 
ATOM   8042 O  OE1 . GLU A 1 992  ? 48.768 44.111  -32.930 1.00 52.08 ? 992  GLU A OE1 1 
ATOM   8043 O  OE2 . GLU A 1 992  ? 46.609 44.401  -33.254 1.00 52.26 ? 992  GLU A OE2 1 
ATOM   8044 N  N   . HIS A 1 993  ? 51.656 46.237  -34.088 1.00 43.41 ? 993  HIS A N   1 
ATOM   8045 C  CA  . HIS A 1 993  ? 53.065 46.372  -33.732 1.00 41.97 ? 993  HIS A CA  1 
ATOM   8046 C  C   . HIS A 1 993  ? 53.373 47.409  -32.671 1.00 40.01 ? 993  HIS A C   1 
ATOM   8047 O  O   . HIS A 1 993  ? 53.534 48.590  -32.968 1.00 40.33 ? 993  HIS A O   1 
ATOM   8048 C  CB  . HIS A 1 993  ? 53.952 46.554  -34.972 1.00 42.82 ? 993  HIS A CB  1 
ATOM   8049 C  CG  . HIS A 1 993  ? 53.895 47.924  -35.577 1.00 44.10 ? 993  HIS A CG  1 
ATOM   8050 N  ND1 . HIS A 1 993  ? 54.503 49.018  -35.006 1.00 46.43 ? 993  HIS A ND1 1 
ATOM   8051 C  CD2 . HIS A 1 993  ? 53.305 48.372  -36.707 1.00 45.73 ? 993  HIS A CD2 1 
ATOM   8052 C  CE1 . HIS A 1 993  ? 54.296 50.079  -35.759 1.00 46.85 ? 993  HIS A CE1 1 
ATOM   8053 N  NE2 . HIS A 1 993  ? 53.565 49.715  -36.795 1.00 46.69 ? 993  HIS A NE2 1 
ATOM   8054 N  N   . THR A 1 994  ? 53.434 46.971  -31.420 1.00 36.81 ? 994  THR A N   1 
ATOM   8055 C  CA  . THR A 1 994  ? 54.062 47.787  -30.379 1.00 33.72 ? 994  THR A CA  1 
ATOM   8056 C  C   . THR A 1 994  ? 55.110 46.990  -29.613 1.00 31.98 ? 994  THR A C   1 
ATOM   8057 O  O   . THR A 1 994  ? 55.121 45.754  -29.641 1.00 32.13 ? 994  THR A O   1 
ATOM   8058 C  CB  . THR A 1 994  ? 53.026 48.432  -29.419 1.00 33.70 ? 994  THR A CB  1 
ATOM   8059 O  OG1 . THR A 1 994  ? 52.092 47.443  -28.969 1.00 32.70 ? 994  THR A OG1 1 
ATOM   8060 C  CG2 . THR A 1 994  ? 52.154 49.446  -30.156 1.00 32.62 ? 994  THR A CG2 1 
ATOM   8061 N  N   . GLN A 1 995  ? 55.984 47.703  -28.912 1.00 29.26 ? 995  GLN A N   1 
ATOM   8062 C  CA  . GLN A 1 995  ? 57.035 47.053  -28.148 1.00 26.55 ? 995  GLN A CA  1 
ATOM   8063 C  C   . GLN A 1 995  ? 56.555 46.695  -26.744 1.00 24.60 ? 995  GLN A C   1 
ATOM   8064 O  O   . GLN A 1 995  ? 55.820 47.456  -26.101 1.00 23.16 ? 995  GLN A O   1 
ATOM   8065 C  CB  . GLN A 1 995  ? 58.276 47.946  -28.069 1.00 26.55 ? 995  GLN A CB  1 
ATOM   8066 C  CG  . GLN A 1 995  ? 58.867 48.305  -29.433 1.00 27.94 ? 995  GLN A CG  1 
ATOM   8067 C  CD  . GLN A 1 995  ? 59.607 49.641  -29.446 1.00 30.17 ? 995  GLN A CD  1 
ATOM   8068 O  OE1 . GLN A 1 995  ? 59.009 50.700  -29.665 1.00 23.81 ? 995  GLN A OE1 1 
ATOM   8069 N  NE2 . GLN A 1 995  ? 60.922 49.588  -29.241 1.00 32.15 ? 995  GLN A NE2 1 
ATOM   8070 N  N   . LYS A 1 996  ? 56.991 45.533  -26.264 1.00 22.28 ? 996  LYS A N   1 
ATOM   8071 C  CA  . LYS A 1 996  ? 56.756 45.149  -24.883 1.00 21.94 ? 996  LYS A CA  1 
ATOM   8072 C  C   . LYS A 1 996  ? 57.470 46.138  -23.981 1.00 20.28 ? 996  LYS A C   1 
ATOM   8073 O  O   . LYS A 1 996  ? 58.640 46.477  -24.201 1.00 20.06 ? 996  LYS A O   1 
ATOM   8074 C  CB  . LYS A 1 996  ? 57.277 43.726  -24.621 1.00 22.90 ? 996  LYS A CB  1 
ATOM   8075 C  CG  . LYS A 1 996  ? 56.368 42.651  -25.189 1.00 26.22 ? 996  LYS A CG  1 
ATOM   8076 C  CD  . LYS A 1 996  ? 54.949 42.763  -24.625 1.00 30.97 ? 996  LYS A CD  1 
ATOM   8077 C  CE  . LYS A 1 996  ? 54.297 41.398  -24.494 1.00 32.52 ? 996  LYS A CE  1 
ATOM   8078 N  NZ  . LYS A 1 996  ? 54.202 40.699  -25.811 1.00 34.81 ? 996  LYS A NZ  1 
ATOM   8079 N  N   . LEU A 1 997  ? 56.760 46.590  -22.955 1.00 19.13 ? 997  LEU A N   1 
ATOM   8080 C  CA  . LEU A 1 997  ? 57.384 47.429  -21.968 1.00 18.35 ? 997  LEU A CA  1 
ATOM   8081 C  C   . LEU A 1 997  ? 57.736 46.571  -20.764 1.00 17.71 ? 997  LEU A C   1 
ATOM   8082 O  O   . LEU A 1 997  ? 56.848 46.005  -20.126 1.00 18.52 ? 997  LEU A O   1 
ATOM   8083 C  CB  . LEU A 1 997  ? 56.413 48.547  -21.568 1.00 18.89 ? 997  LEU A CB  1 
ATOM   8084 C  CG  . LEU A 1 997  ? 56.875 49.404  -20.392 1.00 17.61 ? 997  LEU A CG  1 
ATOM   8085 C  CD1 . LEU A 1 997  ? 58.139 50.186  -20.737 1.00 21.29 ? 997  LEU A CD1 1 
ATOM   8086 C  CD2 . LEU A 1 997  ? 55.757 50.342  -20.038 1.00 20.48 ? 997  LEU A CD2 1 
ATOM   8087 N  N   . ASP A 1 998  ? 59.031 46.508  -20.454 1.00 16.85 ? 998  ASP A N   1 
ATOM   8088 C  CA  . ASP A 1 998  ? 59.515 45.878  -19.227 1.00 17.20 ? 998  ASP A CA  1 
ATOM   8089 C  C   . ASP A 1 998  ? 60.104 46.974  -18.353 1.00 15.99 ? 998  ASP A C   1 
ATOM   8090 O  O   . ASP A 1 998  ? 61.238 47.422  -18.544 1.00 16.00 ? 998  ASP A O   1 
ATOM   8091 C  CB  . ASP A 1 998  ? 60.552 44.783  -19.553 1.00 17.84 ? 998  ASP A CB  1 
ATOM   8092 C  CG  . ASP A 1 998  ? 61.265 44.264  -18.330 1.00 20.48 ? 998  ASP A CG  1 
ATOM   8093 O  OD1 . ASP A 1 998  ? 60.783 44.467  -17.177 1.00 18.65 ? 998  ASP A OD1 1 
ATOM   8094 O  OD2 . ASP A 1 998  ? 62.347 43.632  -18.447 1.00 22.64 ? 998  ASP A OD2 1 
ATOM   8095 N  N   . VAL A 1 999  ? 59.325 47.414  -17.372 1.00 15.40 ? 999  VAL A N   1 
ATOM   8096 C  CA  . VAL A 1 999  ? 59.781 48.545  -16.572 1.00 13.96 ? 999  VAL A CA  1 
ATOM   8097 C  C   . VAL A 1 999  ? 61.046 48.245  -15.786 1.00 14.40 ? 999  VAL A C   1 
ATOM   8098 O  O   . VAL A 1 999  ? 61.813 49.155  -15.443 1.00 14.14 ? 999  VAL A O   1 
ATOM   8099 C  CB  . VAL A 1 999  ? 58.674 49.091  -15.636 1.00 13.93 ? 999  VAL A CB  1 
ATOM   8100 C  CG1 . VAL A 1 999  ? 57.581 49.745  -16.464 1.00 14.91 ? 999  VAL A CG1 1 
ATOM   8101 C  CG2 . VAL A 1 999  ? 58.120 48.004  -14.688 1.00 14.56 ? 999  VAL A CG2 1 
ATOM   8102 N  N   . CYS A 1 1000 ? 61.280 46.964  -15.514 1.00 15.47 ? 1000 CYS A N   1 
ATOM   8103 C  CA  . CYS A 1 1000 ? 62.469 46.604  -14.742 1.00 16.98 ? 1000 CYS A CA  1 
ATOM   8104 C  C   . CYS A 1 1000 ? 63.806 46.812  -15.451 1.00 16.84 ? 1000 CYS A C   1 
ATOM   8105 O  O   . CYS A 1 1000 ? 64.832 46.919  -14.789 1.00 18.56 ? 1000 CYS A O   1 
ATOM   8106 C  CB  . CYS A 1 1000 ? 62.338 45.197  -14.153 1.00 17.83 ? 1000 CYS A CB  1 
ATOM   8107 S  SG  . CYS A 1 1000 ? 61.359 45.224  -12.598 1.00 24.16 ? 1000 CYS A SG  1 
ATOM   8108 N  N   . HIS A 1 1001 ? 63.766 46.951  -16.773 1.00 17.16 ? 1001 HIS A N   1 
ATOM   8109 C  CA  . HIS A 1 1001 ? 64.970 47.231  -17.543 1.00 17.59 ? 1001 HIS A CA  1 
ATOM   8110 C  C   . HIS A 1 1001 ? 65.043 48.676  -18.060 1.00 17.41 ? 1001 HIS A C   1 
ATOM   8111 O  O   . HIS A 1 1001 ? 65.895 49.017  -18.886 1.00 18.10 ? 1001 HIS A O   1 
ATOM   8112 C  CB  . HIS A 1 1001 ? 65.132 46.211  -18.674 1.00 18.05 ? 1001 HIS A CB  1 
ATOM   8113 C  CG  . HIS A 1 1001 ? 65.687 44.902  -18.218 1.00 19.30 ? 1001 HIS A CG  1 
ATOM   8114 N  ND1 . HIS A 1 1001 ? 64.891 43.863  -17.790 1.00 20.23 ? 1001 HIS A ND1 1 
ATOM   8115 C  CD2 . HIS A 1 1001 ? 66.967 44.472  -18.091 1.00 21.62 ? 1001 HIS A CD2 1 
ATOM   8116 C  CE1 . HIS A 1 1001 ? 65.652 42.842  -17.431 1.00 20.23 ? 1001 HIS A CE1 1 
ATOM   8117 N  NE2 . HIS A 1 1001 ? 66.915 43.181  -17.618 1.00 21.30 ? 1001 HIS A NE2 1 
ATOM   8118 N  N   . LEU A 1 1002 ? 64.165 49.549  -17.575 1.00 16.35 ? 1002 LEU A N   1 
ATOM   8119 C  CA  . LEU A 1 1002 ? 64.256 50.962  -17.956 1.00 16.29 ? 1002 LEU A CA  1 
ATOM   8120 C  C   . LEU A 1 1002 ? 65.502 51.653  -17.420 1.00 17.41 ? 1002 LEU A C   1 
ATOM   8121 O  O   . LEU A 1 1002 ? 65.999 52.600  -18.034 1.00 18.99 ? 1002 LEU A O   1 
ATOM   8122 C  CB  . LEU A 1 1002 ? 63.011 51.731  -17.478 1.00 15.97 ? 1002 LEU A CB  1 
ATOM   8123 C  CG  . LEU A 1 1002 ? 61.776 51.605  -18.352 1.00 14.73 ? 1002 LEU A CG  1 
ATOM   8124 C  CD1 . LEU A 1 1002 ? 60.561 52.240  -17.656 1.00 14.49 ? 1002 LEU A CD1 1 
ATOM   8125 C  CD2 . LEU A 1 1002 ? 62.029 52.300  -19.698 1.00 17.87 ? 1002 LEU A CD2 1 
ATOM   8126 N  N   . LEU A 1 1003 ? 65.981 51.222  -16.259 1.00 17.46 ? 1003 LEU A N   1 
ATOM   8127 C  CA  . LEU A 1 1003 ? 67.228 51.743  -15.712 1.00 18.06 ? 1003 LEU A CA  1 
ATOM   8128 C  C   . LEU A 1 1003 ? 68.298 50.651  -15.824 1.00 18.30 ? 1003 LEU A C   1 
ATOM   8129 O  O   . LEU A 1 1003 ? 67.988 49.478  -15.686 1.00 17.99 ? 1003 LEU A O   1 
ATOM   8130 C  CB  . LEU A 1 1003 ? 67.085 52.191  -14.257 1.00 17.87 ? 1003 LEU A CB  1 
ATOM   8131 C  CG  . LEU A 1 1003 ? 66.485 53.594  -14.026 1.00 21.37 ? 1003 LEU A CG  1 
ATOM   8132 C  CD1 . LEU A 1 1003 ? 65.025 53.700  -14.393 1.00 26.18 ? 1003 LEU A CD1 1 
ATOM   8133 C  CD2 . LEU A 1 1003 ? 66.671 53.999  -12.601 1.00 26.13 ? 1003 LEU A CD2 1 
ATOM   8134 N  N   . PRO A 1 1004 ? 69.553 51.031  -16.034 1.00 19.05 ? 1004 PRO A N   1 
ATOM   8135 C  CA  . PRO A 1 1004 ? 70.609 50.031  -16.237 1.00 18.87 ? 1004 PRO A CA  1 
ATOM   8136 C  C   . PRO A 1 1004 ? 70.980 49.304  -14.944 1.00 19.16 ? 1004 PRO A C   1 
ATOM   8137 O  O   . PRO A 1 1004 ? 70.615 49.693  -13.806 1.00 17.73 ? 1004 PRO A O   1 
ATOM   8138 C  CB  . PRO A 1 1004 ? 71.778 50.870  -16.746 1.00 19.31 ? 1004 PRO A CB  1 
ATOM   8139 C  CG  . PRO A 1 1004 ? 71.579 52.197  -16.125 1.00 19.71 ? 1004 PRO A CG  1 
ATOM   8140 C  CD  . PRO A 1 1004 ? 70.074 52.411  -16.067 1.00 18.74 ? 1004 PRO A CD  1 
ATOM   8141 N  N   . ASN A 1 1005 ? 71.719 48.206  -15.132 1.00 19.09 ? 1005 ASN A N   1 
ATOM   8142 C  CA  . ASN A 1 1005 ? 72.291 47.445  -14.007 1.00 19.64 ? 1005 ASN A CA  1 
ATOM   8143 C  C   . ASN A 1 1005 ? 71.250 46.882  -13.046 1.00 18.51 ? 1005 ASN A C   1 
ATOM   8144 O  O   . ASN A 1 1005 ? 71.438 46.919  -11.832 1.00 19.10 ? 1005 ASN A O   1 
ATOM   8145 C  CB  . ASN A 1 1005 ? 73.292 48.291  -13.204 1.00 20.54 ? 1005 ASN A CB  1 
ATOM   8146 C  CG  . ASN A 1 1005 ? 74.264 49.047  -14.082 1.00 24.50 ? 1005 ASN A CG  1 
ATOM   8147 O  OD1 . ASN A 1 1005 ? 74.355 50.277  -14.010 1.00 29.67 ? 1005 ASN A OD1 1 
ATOM   8148 N  ND2 . ASN A 1 1005 ? 74.969 48.328  -14.931 1.00 26.01 ? 1005 ASN A ND2 1 
ATOM   8149 N  N   . VAL A 1 1006 ? 70.157 46.378  -13.611 1.00 19.06 ? 1006 VAL A N   1 
ATOM   8150 C  CA  . VAL A 1 1006 ? 69.116 45.776  -12.799 1.00 18.80 ? 1006 VAL A CA  1 
ATOM   8151 C  C   . VAL A 1 1006 ? 69.690 44.496  -12.164 1.00 19.35 ? 1006 VAL A C   1 
ATOM   8152 O  O   . VAL A 1 1006 ? 70.347 43.689  -12.841 1.00 20.83 ? 1006 VAL A O   1 
ATOM   8153 C  CB  . VAL A 1 1006 ? 67.782 45.543  -13.586 1.00 18.71 ? 1006 VAL A CB  1 
ATOM   8154 C  CG1 . VAL A 1 1006 ? 67.933 44.539  -14.669 1.00 20.11 ? 1006 VAL A CG1 1 
ATOM   8155 C  CG2 . VAL A 1 1006 ? 66.652 45.107  -12.645 1.00 18.76 ? 1006 VAL A CG2 1 
ATOM   8156 N  N   . ALA A 1 1007 ? 69.448 44.360  -10.867 1.00 18.52 ? 1007 ALA A N   1 
ATOM   8157 C  CA  . ALA A 1 1007 ? 69.898 43.210  -10.068 1.00 18.94 ? 1007 ALA A CA  1 
ATOM   8158 C  C   . ALA A 1 1007 ? 68.727 42.361  -9.591  1.00 19.68 ? 1007 ALA A C   1 
ATOM   8159 O  O   . ALA A 1 1007 ? 68.908 41.195  -9.238  1.00 19.70 ? 1007 ALA A O   1 
ATOM   8160 C  CB  . ALA A 1 1007 ? 70.723 43.688  -8.877  1.00 19.31 ? 1007 ALA A CB  1 
ATOM   8161 N  N   . ARG A 1 1008 ? 67.514 42.930  -9.562  1.00 18.66 ? 1008 ARG A N   1 
ATOM   8162 C  CA  . ARG A 1 1008 ? 66.349 42.213  -9.079  1.00 18.55 ? 1008 ARG A CA  1 
ATOM   8163 C  C   . ARG A 1 1008 ? 65.102 42.947  -9.550  1.00 16.63 ? 1008 ARG A C   1 
ATOM   8164 O  O   . ARG A 1 1008 ? 65.130 44.176  -9.714  1.00 16.16 ? 1008 ARG A O   1 
ATOM   8165 C  CB  . ARG A 1 1008 ? 66.375 42.209  -7.547  1.00 18.50 ? 1008 ARG A CB  1 
ATOM   8166 C  CG  . ARG A 1 1008 ? 65.399 41.287  -6.869  1.00 21.83 ? 1008 ARG A CG  1 
ATOM   8167 C  CD  . ARG A 1 1008 ? 65.483 41.360  -5.353  1.00 22.80 ? 1008 ARG A CD  1 
ATOM   8168 N  NE  . ARG A 1 1008 ? 64.716 40.284  -4.735  1.00 31.30 ? 1008 ARG A NE  1 
ATOM   8169 C  CZ  . ARG A 1 1008 ? 65.173 39.050  -4.526  1.00 34.16 ? 1008 ARG A CZ  1 
ATOM   8170 N  NH1 . ARG A 1 1008 ? 66.417 38.721  -4.877  1.00 36.10 ? 1008 ARG A NH1 1 
ATOM   8171 N  NH2 . ARG A 1 1008 ? 64.382 38.137  -3.970  1.00 34.36 ? 1008 ARG A NH2 1 
ATOM   8172 N  N   . CYS A 1 1009 ? 64.028 42.208  -9.764  1.00 16.75 ? 1009 CYS A N   1 
ATOM   8173 C  CA  . CYS A 1 1009 ? 62.728 42.814  -10.115 1.00 16.75 ? 1009 CYS A CA  1 
ATOM   8174 C  C   . CYS A 1 1009 ? 61.676 42.079  -9.305  1.00 16.06 ? 1009 CYS A C   1 
ATOM   8175 O  O   . CYS A 1 1009 ? 61.624 40.847  -9.311  1.00 16.15 ? 1009 CYS A O   1 
ATOM   8176 C  CB  . CYS A 1 1009 ? 62.464 42.651  -11.605 1.00 17.08 ? 1009 CYS A CB  1 
ATOM   8177 S  SG  . CYS A 1 1009 ? 60.902 43.312  -12.235 1.00 22.99 ? 1009 CYS A SG  1 
ATOM   8178 N  N   . GLU A 1 1010 ? 60.842 42.817  -8.578  1.00 14.44 ? 1010 GLU A N   1 
ATOM   8179 C  CA  . GLU A 1 1010 ? 59.823 42.210  -7.754  1.00 14.03 ? 1010 GLU A CA  1 
ATOM   8180 C  C   . GLU A 1 1010 ? 58.464 42.824  -8.077  1.00 12.64 ? 1010 GLU A C   1 
ATOM   8181 O  O   . GLU A 1 1010 ? 58.352 44.042  -8.312  1.00 12.99 ? 1010 GLU A O   1 
ATOM   8182 C  CB  . GLU A 1 1010 ? 60.156 42.445  -6.280  1.00 15.64 ? 1010 GLU A CB  1 
ATOM   8183 C  CG  . GLU A 1 1010 ? 61.384 41.639  -5.846  1.00 20.67 ? 1010 GLU A CG  1 
ATOM   8184 C  CD  . GLU A 1 1010 ? 62.158 42.219  -4.668  1.00 26.13 ? 1010 GLU A CD  1 
ATOM   8185 O  OE1 . GLU A 1 1010 ? 62.554 43.418  -4.671  1.00 26.25 ? 1010 GLU A OE1 1 
ATOM   8186 O  OE2 . GLU A 1 1010 ? 62.420 41.429  -3.726  1.00 29.66 ? 1010 GLU A OE2 1 
ATOM   8187 N  N   . ARG A 1 1011 ? 57.437 42.011  -8.064  1.00 12.36 ? 1011 ARG A N   1 
ATOM   8188 C  CA  . ARG A 1 1011 ? 56.067 42.547  -8.031  1.00 11.75 ? 1011 ARG A CA  1 
ATOM   8189 C  C   . ARG A 1 1011 ? 55.743 42.883  -6.577  1.00 11.95 ? 1011 ARG A C   1 
ATOM   8190 O  O   . ARG A 1 1011 ? 56.060 42.104  -5.659  1.00 12.05 ? 1011 ARG A O   1 
ATOM   8191 C  CB  . ARG A 1 1011 ? 55.073 41.542  -8.567  1.00 12.96 ? 1011 ARG A CB  1 
ATOM   8192 C  CG  . ARG A 1 1011 ? 53.696 42.182  -8.861  1.00 16.01 ? 1011 ARG A CG  1 
ATOM   8193 C  CD  . ARG A 1 1011 ? 52.751 41.265  -9.557  1.00 19.70 ? 1011 ARG A CD  1 
ATOM   8194 N  NE  . ARG A 1 1011 ? 52.495 40.086  -8.737  1.00 26.97 ? 1011 ARG A NE  1 
ATOM   8195 C  CZ  . ARG A 1 1011 ? 51.517 39.982  -7.837  1.00 29.89 ? 1011 ARG A CZ  1 
ATOM   8196 N  NH1 . ARG A 1 1011 ? 50.677 40.994  -7.625  1.00 33.21 ? 1011 ARG A NH1 1 
ATOM   8197 N  NH2 . ARG A 1 1011 ? 51.376 38.853  -7.148  1.00 32.02 ? 1011 ARG A NH2 1 
ATOM   8198 N  N   . THR A 1 1012 ? 55.125 44.044  -6.327  1.00 10.66 ? 1012 THR A N   1 
ATOM   8199 C  CA  . THR A 1 1012 ? 54.810 44.485  -4.978  1.00 9.12  ? 1012 THR A CA  1 
ATOM   8200 C  C   . THR A 1 1012 ? 53.326 44.866  -4.895  1.00 9.60  ? 1012 THR A C   1 
ATOM   8201 O  O   . THR A 1 1012 ? 52.639 45.034  -5.920  1.00 9.80  ? 1012 THR A O   1 
ATOM   8202 C  CB  . THR A 1 1012 ? 55.670 45.686  -4.562  1.00 10.18 ? 1012 THR A CB  1 
ATOM   8203 O  OG1 . THR A 1 1012 ? 55.357 46.810  -5.415  1.00 10.89 ? 1012 THR A OG1 1 
ATOM   8204 C  CG2 . THR A 1 1012 ? 57.139 45.401  -4.766  1.00 10.80 ? 1012 THR A CG2 1 
ATOM   8205 N  N   . THR A 1 1013 ? 52.854 45.064  -3.668  1.00 9.18  ? 1013 THR A N   1 
ATOM   8206 C  CA  . THR A 1 1013 ? 51.608 45.802  -3.488  1.00 9.59  ? 1013 THR A CA  1 
ATOM   8207 C  C   . THR A 1 1013 ? 51.725 47.190  -4.109  1.00 8.26  ? 1013 THR A C   1 
ATOM   8208 O  O   . THR A 1 1013 ? 52.808 47.710  -4.379  1.00 7.97  ? 1013 THR A O   1 
ATOM   8209 C  CB  . THR A 1 1013 ? 51.269 45.938  -2.024  1.00 9.10  ? 1013 THR A CB  1 
ATOM   8210 O  OG1 . THR A 1 1013 ? 52.456 46.350  -1.327  1.00 9.49  ? 1013 THR A OG1 1 
ATOM   8211 C  CG2 . THR A 1 1013 ? 50.849 44.562  -1.415  1.00 11.32 ? 1013 THR A CG2 1 
ATOM   8212 N  N   . LEU A 1 1014 ? 50.563 47.829  -4.327  1.00 8.03  ? 1014 LEU A N   1 
ATOM   8213 C  CA  . LEU A 1 1014 ? 50.579 49.098  -5.085  1.00 7.51  ? 1014 LEU A CA  1 
ATOM   8214 C  C   . LEU A 1 1014 ? 51.246 50.245  -4.353  1.00 6.86  ? 1014 LEU A C   1 
ATOM   8215 O  O   . LEU A 1 1014 ? 51.613 51.252  -4.956  1.00 7.50  ? 1014 LEU A O   1 
ATOM   8216 C  CB  . LEU A 1 1014 ? 49.164 49.543  -5.485  1.00 7.72  ? 1014 LEU A CB  1 
ATOM   8217 C  CG  . LEU A 1 1014 ? 48.368 48.596  -6.379  1.00 7.97  ? 1014 LEU A CG  1 
ATOM   8218 C  CD1 . LEU A 1 1014 ? 47.056 49.258  -6.753  1.00 8.15  ? 1014 LEU A CD1 1 
ATOM   8219 C  CD2 . LEU A 1 1014 ? 49.181 48.248  -7.642  1.00 8.36  ? 1014 LEU A CD2 1 
ATOM   8220 N  N   . THR A 1 1015 ? 51.391 50.110  -3.030  1.00 6.77  ? 1015 THR A N   1 
ATOM   8221 C  CA  . THR A 1 1015 ? 52.086 51.072  -2.167  1.00 7.38  ? 1015 THR A CA  1 
ATOM   8222 C  C   . THR A 1 1015 ? 53.587 50.832  -2.116  1.00 7.32  ? 1015 THR A C   1 
ATOM   8223 O  O   . THR A 1 1015 ? 54.283 51.600  -1.471  1.00 8.67  ? 1015 THR A O   1 
ATOM   8224 C  CB  . THR A 1 1015 ? 51.597 50.951  -0.747  1.00 8.40  ? 1015 THR A CB  1 
ATOM   8225 O  OG1 . THR A 1 1015 ? 51.735 49.563  -0.385  1.00 7.94  ? 1015 THR A OG1 1 
ATOM   8226 C  CG2 . THR A 1 1015 ? 50.086 51.306  -0.640  1.00 8.96  ? 1015 THR A CG2 1 
ATOM   8227 N  N   . PHE A 1 1016 ? 54.052 49.772  -2.776  1.00 7.67  ? 1016 PHE A N   1 
ATOM   8228 C  CA  . PHE A 1 1016 ? 55.460 49.330  -2.834  1.00 9.21  ? 1016 PHE A CA  1 
ATOM   8229 C  C   . PHE A 1 1016 ? 55.923 48.736  -1.509  1.00 10.02 ? 1016 PHE A C   1 
ATOM   8230 O  O   . PHE A 1 1016 ? 57.123 48.453  -1.375  1.00 11.23 ? 1016 PHE A O   1 
ATOM   8231 C  CB  . PHE A 1 1016 ? 56.430 50.431  -3.287  1.00 9.71  ? 1016 PHE A CB  1 
ATOM   8232 C  CG  . PHE A 1 1016 ? 56.071 51.075  -4.601  1.00 8.54  ? 1016 PHE A CG  1 
ATOM   8233 C  CD1 . PHE A 1 1016 ? 55.958 50.308  -5.751  1.00 9.50  ? 1016 PHE A CD1 1 
ATOM   8234 C  CD2 . PHE A 1 1016 ? 55.890 52.465  -4.677  1.00 9.68  ? 1016 PHE A CD2 1 
ATOM   8235 C  CE1 . PHE A 1 1016 ? 55.643 50.942  -6.975  1.00 9.57  ? 1016 PHE A CE1 1 
ATOM   8236 C  CE2 . PHE A 1 1016 ? 55.588 53.068  -5.889  1.00 8.67  ? 1016 PHE A CE2 1 
ATOM   8237 C  CZ  . PHE A 1 1016 ? 55.480 52.280  -7.035  1.00 10.21 ? 1016 PHE A CZ  1 
ATOM   8238 N  N   . LEU A 1 1017 ? 55.032 48.490  -0.546  1.00 9.65  ? 1017 LEU A N   1 
ATOM   8239 C  CA  . LEU A 1 1017 ? 55.485 48.159  0.820   1.00 11.28 ? 1017 LEU A CA  1 
ATOM   8240 C  C   . LEU A 1 1017 ? 55.675 46.675  1.079   1.00 12.48 ? 1017 LEU A C   1 
ATOM   8241 O  O   . LEU A 1 1017 ? 56.271 46.323  2.113   1.00 15.15 ? 1017 LEU A O   1 
ATOM   8242 C  CB  . LEU A 1 1017 ? 54.527 48.779  1.826   1.00 11.03 ? 1017 LEU A CB  1 
ATOM   8243 C  CG  . LEU A 1 1017 ? 54.531 50.300  1.775   1.00 10.47 ? 1017 LEU A CG  1 
ATOM   8244 C  CD1 . LEU A 1 1017 ? 53.465 50.819  2.724   1.00 10.85 ? 1017 LEU A CD1 1 
ATOM   8245 C  CD2 . LEU A 1 1017 ? 55.872 50.909  2.094   1.00 12.70 ? 1017 LEU A CD2 1 
ATOM   8246 N  N   . GLN A 1 1018 ? 55.178 45.801  0.208   1.00 11.06 ? 1018 GLN A N   1 
ATOM   8247 C  CA  . GLN A 1 1018 ? 55.346 44.342  0.392   1.00 13.34 ? 1018 GLN A CA  1 
ATOM   8248 C  C   . GLN A 1 1018 ? 55.697 43.696  -0.925  1.00 13.08 ? 1018 GLN A C   1 
ATOM   8249 O  O   . GLN A 1 1018 ? 55.046 43.972  -1.925  1.00 12.81 ? 1018 GLN A O   1 
ATOM   8250 C  CB  . GLN A 1 1018 ? 54.063 43.704  0.929   1.00 13.69 ? 1018 GLN A CB  1 
ATOM   8251 C  CG  . GLN A 1 1018 ? 54.245 42.195  1.199   1.00 17.23 ? 1018 GLN A CG  1 
ATOM   8252 C  CD  . GLN A 1 1018 ? 52.962 41.429  1.433   1.00 19.23 ? 1018 GLN A CD  1 
ATOM   8253 O  OE1 . GLN A 1 1018 ? 51.869 42.005  1.526   1.00 22.54 ? 1018 GLN A OE1 1 
ATOM   8254 N  NE2 . GLN A 1 1018 ? 53.090 40.097  1.535   1.00 22.30 ? 1018 GLN A NE2 1 
ATOM   8255 N  N   . ASN A 1 1019 ? 56.723 42.838  -0.918  1.00 14.03 ? 1019 ASN A N   1 
ATOM   8256 C  CA  . ASN A 1 1019 ? 57.114 42.088  -2.092  1.00 16.09 ? 1019 ASN A CA  1 
ATOM   8257 C  C   . ASN A 1 1019 ? 56.208 40.889  -2.214  1.00 17.05 ? 1019 ASN A C   1 
ATOM   8258 O  O   . ASN A 1 1019 ? 56.023 40.143  -1.235  1.00 18.47 ? 1019 ASN A O   1 
ATOM   8259 C  CB  . ASN A 1 1019 ? 58.590 41.648  -1.990  1.00 16.40 ? 1019 ASN A CB  1 
ATOM   8260 C  CG  . ASN A 1 1019 ? 59.554 42.835  -1.874  1.00 19.00 ? 1019 ASN A CG  1 
ATOM   8261 O  OD1 . ASN A 1 1019 ? 59.329 43.891  -2.476  1.00 20.91 ? 1019 ASN A OD1 1 
ATOM   8262 N  ND2 . ASN A 1 1019 ? 60.646 42.664  -1.104  1.00 21.75 ? 1019 ASN A ND2 1 
ATOM   8263 N  N   . LEU A 1 1020 ? 55.622 40.698  -3.383  1.00 16.99 ? 1020 LEU A N   1 
ATOM   8264 C  CA  . LEU A 1 1020 ? 54.682 39.624  -3.632  1.00 18.53 ? 1020 LEU A CA  1 
ATOM   8265 C  C   . LEU A 1 1020 ? 55.274 38.514  -4.486  1.00 19.89 ? 1020 LEU A C   1 
ATOM   8266 O  O   . LEU A 1 1020 ? 54.835 37.361  -4.385  1.00 20.73 ? 1020 LEU A O   1 
ATOM   8267 C  CB  . LEU A 1 1020 ? 53.412 40.150  -4.300  1.00 18.83 ? 1020 LEU A CB  1 
ATOM   8268 C  CG  . LEU A 1 1020 ? 52.643 41.225  -3.523  1.00 17.47 ? 1020 LEU A CG  1 
ATOM   8269 C  CD1 . LEU A 1 1020 ? 51.504 41.714  -4.423  1.00 19.89 ? 1020 LEU A CD1 1 
ATOM   8270 C  CD2 . LEU A 1 1020 ? 52.116 40.692  -2.184  1.00 19.01 ? 1020 LEU A CD2 1 
ATOM   8271 N  N   . GLU A 1 1021 ? 56.246 38.845  -5.330  1.00 20.55 ? 1021 GLU A N   1 
ATOM   8272 C  CA  . GLU A 1 1021 ? 56.811 37.871  -6.279  1.00 23.03 ? 1021 GLU A CA  1 
ATOM   8273 C  C   . GLU A 1 1021 ? 58.175 38.317  -6.761  1.00 22.46 ? 1021 GLU A C   1 
ATOM   8274 O  O   . GLU A 1 1021 ? 58.365 39.469  -7.158  1.00 20.42 ? 1021 GLU A O   1 
ATOM   8275 C  CB  . GLU A 1 1021 ? 55.876 37.696  -7.483  1.00 22.60 ? 1021 GLU A CB  1 
ATOM   8276 C  CG  . GLU A 1 1021 ? 56.319 36.651  -8.507  1.00 26.83 ? 1021 GLU A CG  1 
ATOM   8277 C  CD  . GLU A 1 1021 ? 55.432 36.610  -9.740  1.00 27.67 ? 1021 GLU A CD  1 
ATOM   8278 O  OE1 . GLU A 1 1021 ? 54.421 37.366  -9.810  1.00 33.21 ? 1021 GLU A OE1 1 
ATOM   8279 O  OE2 . GLU A 1 1021 ? 55.765 35.817  -10.663 1.00 34.00 ? 1021 GLU A OE2 1 
ATOM   8280 N  N   . HIS A 1 1022 ? 59.122 37.397  -6.747  1.00 22.98 ? 1022 HIS A N   1 
ATOM   8281 C  CA  . HIS A 1 1022 ? 60.441 37.646  -7.258  1.00 23.68 ? 1022 HIS A CA  1 
ATOM   8282 C  C   . HIS A 1 1022 ? 60.445 37.202  -8.703  1.00 23.93 ? 1022 HIS A C   1 
ATOM   8283 O  O   . HIS A 1 1022 ? 60.087 36.079  -9.010  1.00 23.84 ? 1022 HIS A O   1 
ATOM   8284 C  CB  . HIS A 1 1022 ? 61.439 36.832  -6.432  1.00 24.43 ? 1022 HIS A CB  1 
ATOM   8285 C  CG  . HIS A 1 1022 ? 62.864 37.042  -6.819  1.00 28.07 ? 1022 HIS A CG  1 
ATOM   8286 N  ND1 . HIS A 1 1022 ? 63.821 36.065  -6.652  1.00 31.69 ? 1022 HIS A ND1 1 
ATOM   8287 C  CD2 . HIS A 1 1022 ? 63.506 38.113  -7.339  1.00 31.15 ? 1022 HIS A CD2 1 
ATOM   8288 C  CE1 . HIS A 1 1022 ? 64.986 36.515  -7.083  1.00 32.84 ? 1022 HIS A CE1 1 
ATOM   8289 N  NE2 . HIS A 1 1022 ? 64.825 37.757  -7.496  1.00 33.30 ? 1022 HIS A NE2 1 
ATOM   8290 N  N   . LEU A 1 1023 ? 60.802 38.095  -9.607  1.00 23.41 ? 1023 LEU A N   1 
ATOM   8291 C  CA  . LEU A 1 1023 ? 60.494 37.862  -11.006 1.00 24.27 ? 1023 LEU A CA  1 
ATOM   8292 C  C   . LEU A 1 1023 ? 61.651 37.260  -11.792 1.00 25.26 ? 1023 LEU A C   1 
ATOM   8293 O  O   . LEU A 1 1023 ? 62.774 37.768  -11.742 1.00 24.81 ? 1023 LEU A O   1 
ATOM   8294 C  CB  . LEU A 1 1023 ? 59.993 39.147  -11.664 1.00 23.78 ? 1023 LEU A CB  1 
ATOM   8295 C  CG  . LEU A 1 1023 ? 58.621 39.600  -11.158 1.00 23.26 ? 1023 LEU A CG  1 
ATOM   8296 C  CD1 . LEU A 1 1023 ? 58.402 41.071  -11.457 1.00 24.12 ? 1023 LEU A CD1 1 
ATOM   8297 C  CD2 . LEU A 1 1023 ? 57.512 38.748  -11.760 1.00 25.16 ? 1023 LEU A CD2 1 
ATOM   8298 N  N   . ASP A 1 1024 ? 61.336 36.193  -12.529 1.00 27.63 ? 1024 ASP A N   1 
ATOM   8299 C  CA  . ASP A 1 1024 ? 62.309 35.478  -13.360 1.00 29.34 ? 1024 ASP A CA  1 
ATOM   8300 C  C   . ASP A 1 1024 ? 62.858 36.349  -14.463 1.00 29.24 ? 1024 ASP A C   1 
ATOM   8301 O  O   . ASP A 1 1024 ? 62.099 37.040  -15.166 1.00 29.62 ? 1024 ASP A O   1 
ATOM   8302 C  CB  . ASP A 1 1024 ? 61.666 34.244  -13.996 1.00 30.41 ? 1024 ASP A CB  1 
ATOM   8303 C  CG  . ASP A 1 1024 ? 61.199 33.228  -12.966 1.00 34.23 ? 1024 ASP A CG  1 
ATOM   8304 O  OD1 . ASP A 1 1024 ? 61.780 33.193  -11.852 1.00 38.73 ? 1024 ASP A OD1 1 
ATOM   8305 O  OD2 . ASP A 1 1024 ? 60.259 32.419  -13.191 1.00 38.45 ? 1024 ASP A OD2 1 
ATOM   8306 N  N   . GLY A 1 1025 ? 64.178 36.311  -14.609 1.00 28.45 ? 1025 GLY A N   1 
ATOM   8307 C  CA  . GLY A 1 1025 ? 64.873 37.069  -15.630 1.00 28.30 ? 1025 GLY A CA  1 
ATOM   8308 C  C   . GLY A 1 1025 ? 64.883 38.556  -15.365 1.00 27.40 ? 1025 GLY A C   1 
ATOM   8309 O  O   . GLY A 1 1025 ? 65.355 39.317  -16.198 1.00 27.82 ? 1025 GLY A O   1 
ATOM   8310 N  N   . MET A 1 1026 ? 64.368 38.965  -14.202 1.00 26.81 ? 1026 MET A N   1 
ATOM   8311 C  CA  . MET A 1 1026 ? 64.235 40.386  -13.854 1.00 26.84 ? 1026 MET A CA  1 
ATOM   8312 C  C   . MET A 1 1026 ? 63.335 41.096  -14.859 1.00 25.68 ? 1026 MET A C   1 
ATOM   8313 O  O   . MET A 1 1026 ? 63.562 42.268  -15.196 1.00 25.61 ? 1026 MET A O   1 
ATOM   8314 C  CB  . MET A 1 1026 ? 65.604 41.075  -13.762 1.00 26.39 ? 1026 MET A CB  1 
ATOM   8315 C  CG  . MET A 1 1026 ? 66.529 40.463  -12.710 1.00 27.62 ? 1026 MET A CG  1 
ATOM   8316 S  SD  . MET A 1 1026 ? 68.182 41.168  -12.676 1.00 30.27 ? 1026 MET A SD  1 
ATOM   8317 C  CE  . MET A 1 1026 ? 68.852 40.603  -14.278 1.00 32.41 ? 1026 MET A CE  1 
ATOM   8318 N  N   . VAL A 1 1027 ? 62.333 40.377  -15.356 1.00 24.60 ? 1027 VAL A N   1 
ATOM   8319 C  CA  . VAL A 1 1027 ? 61.414 40.932  -16.342 1.00 25.08 ? 1027 VAL A CA  1 
ATOM   8320 C  C   . VAL A 1 1027 ? 60.040 41.154  -15.709 1.00 25.27 ? 1027 VAL A C   1 
ATOM   8321 O  O   . VAL A 1 1027 ? 59.434 40.226  -15.157 1.00 25.13 ? 1027 VAL A O   1 
ATOM   8322 C  CB  . VAL A 1 1027 ? 61.307 40.046  -17.603 1.00 24.76 ? 1027 VAL A CB  1 
ATOM   8323 C  CG1 . VAL A 1 1027 ? 60.136 40.477  -18.481 1.00 25.18 ? 1027 VAL A CG1 1 
ATOM   8324 C  CG2 . VAL A 1 1027 ? 62.626 40.085  -18.405 1.00 25.82 ? 1027 VAL A CG2 1 
ATOM   8325 N  N   . ALA A 1 1028 ? 59.561 42.393  -15.782 1.00 25.06 ? 1028 ALA A N   1 
ATOM   8326 C  CA  . ALA A 1 1028 ? 58.230 42.731  -15.279 1.00 25.73 ? 1028 ALA A CA  1 
ATOM   8327 C  C   . ALA A 1 1028 ? 57.232 42.504  -16.390 1.00 26.13 ? 1028 ALA A C   1 
ATOM   8328 O  O   . ALA A 1 1028 ? 57.274 43.220  -17.397 1.00 26.64 ? 1028 ALA A O   1 
ATOM   8329 C  CB  . ALA A 1 1028 ? 58.181 44.184  -14.826 1.00 25.23 ? 1028 ALA A CB  1 
ATOM   8330 N  N   . PRO A 1 1029 ? 56.331 41.538  -16.211 1.00 25.95 ? 1029 PRO A N   1 
ATOM   8331 C  CA  . PRO A 1 1029 ? 55.312 41.248  -17.228 1.00 26.59 ? 1029 PRO A CA  1 
ATOM   8332 C  C   . PRO A 1 1029 ? 54.288 42.374  -17.304 1.00 26.34 ? 1029 PRO A C   1 
ATOM   8333 O  O   . PRO A 1 1029 ? 54.029 43.030  -16.305 1.00 27.85 ? 1029 PRO A O   1 
ATOM   8334 C  CB  . PRO A 1 1029 ? 54.629 39.977  -16.709 1.00 26.46 ? 1029 PRO A CB  1 
ATOM   8335 C  CG  . PRO A 1 1029 ? 55.411 39.522  -15.509 1.00 26.75 ? 1029 PRO A CG  1 
ATOM   8336 C  CD  . PRO A 1 1029 ? 56.195 40.683  -15.017 1.00 25.98 ? 1029 PRO A CD  1 
ATOM   8337 N  N   . GLU A 1 1030 ? 53.736 42.607  -18.481 1.00 26.11 ? 1030 GLU A N   1 
ATOM   8338 C  CA  . GLU A 1 1030 ? 52.628 43.538  -18.622 1.00 25.66 ? 1030 GLU A CA  1 
ATOM   8339 C  C   . GLU A 1 1030 ? 51.353 42.961  -17.987 1.00 25.01 ? 1030 GLU A C   1 
ATOM   8340 O  O   . GLU A 1 1030 ? 51.203 41.733  -17.820 1.00 26.36 ? 1030 GLU A O   1 
ATOM   8341 C  CB  . GLU A 1 1030 ? 52.390 43.861  -20.098 1.00 25.91 ? 1030 GLU A CB  1 
ATOM   8342 C  CG  . GLU A 1 1030 ? 53.511 44.653  -20.774 1.00 25.10 ? 1030 GLU A CG  1 
ATOM   8343 C  CD  . GLU A 1 1030 ? 53.194 44.992  -22.223 1.00 26.23 ? 1030 GLU A CD  1 
ATOM   8344 O  OE1 . GLU A 1 1030 ? 52.235 44.398  -22.783 1.00 29.14 ? 1030 GLU A OE1 1 
ATOM   8345 O  OE2 . GLU A 1 1030 ? 53.915 45.842  -22.807 1.00 23.28 ? 1030 GLU A OE2 1 
ATOM   8346 N  N   . VAL A 1 1031 ? 50.439 43.858  -17.639 1.00 23.25 ? 1031 VAL A N   1 
ATOM   8347 C  CA  . VAL A 1 1031 ? 49.240 43.492  -16.899 1.00 20.46 ? 1031 VAL A CA  1 
ATOM   8348 C  C   . VAL A 1 1031 ? 48.061 43.223  -17.839 1.00 19.19 ? 1031 VAL A C   1 
ATOM   8349 O  O   . VAL A 1 1031 ? 48.099 43.597  -19.007 1.00 18.72 ? 1031 VAL A O   1 
ATOM   8350 C  CB  . VAL A 1 1031 ? 48.904 44.568  -15.822 1.00 21.24 ? 1031 VAL A CB  1 
ATOM   8351 C  CG1 . VAL A 1 1031 ? 50.095 44.735  -14.868 1.00 23.16 ? 1031 VAL A CG1 1 
ATOM   8352 C  CG2 . VAL A 1 1031 ? 48.517 45.890  -16.436 1.00 21.71 ? 1031 VAL A CG2 1 
ATOM   8353 N  N   . CYS A 1 1032 ? 47.040 42.544  -17.329 1.00 16.28 ? 1032 CYS A N   1 
ATOM   8354 C  CA  . CYS A 1 1032 ? 45.785 42.286  -18.042 1.00 16.01 ? 1032 CYS A CA  1 
ATOM   8355 C  C   . CYS A 1 1032 ? 44.881 43.529  -18.130 1.00 13.87 ? 1032 CYS A C   1 
ATOM   8356 O  O   . CYS A 1 1032 ? 45.006 44.445  -17.317 1.00 12.69 ? 1032 CYS A O   1 
ATOM   8357 C  CB  . CYS A 1 1032 ? 45.028 41.195  -17.312 1.00 15.67 ? 1032 CYS A CB  1 
ATOM   8358 S  SG  . CYS A 1 1032 ? 45.839 39.588  -17.512 1.00 24.16 ? 1032 CYS A SG  1 
ATOM   8359 N  N   . PRO A 1 1033 ? 43.950 43.564  -19.087 1.00 12.95 ? 1033 PRO A N   1 
ATOM   8360 C  CA  . PRO A 1 1033 ? 42.974 44.663  -19.143 1.00 12.20 ? 1033 PRO A CA  1 
ATOM   8361 C  C   . PRO A 1 1033 ? 42.247 44.832  -17.805 1.00 11.17 ? 1033 PRO A C   1 
ATOM   8362 O  O   . PRO A 1 1033 ? 41.780 43.860  -17.188 1.00 11.41 ? 1033 PRO A O   1 
ATOM   8363 C  CB  . PRO A 1 1033 ? 41.992 44.217  -20.238 1.00 12.98 ? 1033 PRO A CB  1 
ATOM   8364 C  CG  . PRO A 1 1033 ? 42.853 43.386  -21.136 1.00 14.06 ? 1033 PRO A CG  1 
ATOM   8365 C  CD  . PRO A 1 1033 ? 43.781 42.614  -20.220 1.00 14.03 ? 1033 PRO A CD  1 
ATOM   8366 N  N   . MET A 1 1034 ? 42.153 46.097  -17.397 1.00 10.55 ? 1034 MET A N   1 
ATOM   8367 C  CA  . MET A 1 1034 ? 41.546 46.545  -16.130 1.00 10.88 ? 1034 MET A CA  1 
ATOM   8368 C  C   . MET A 1 1034 ? 42.353 46.186  -14.880 1.00 12.14 ? 1034 MET A C   1 
ATOM   8369 O  O   . MET A 1 1034 ? 41.878 46.378  -13.755 1.00 15.96 ? 1034 MET A O   1 
ATOM   8370 C  CB  . MET A 1 1034 ? 40.058 46.152  -15.976 1.00 9.90  ? 1034 MET A CB  1 
ATOM   8371 C  CG  . MET A 1 1034 ? 39.182 46.655  -17.101 1.00 11.85 ? 1034 MET A CG  1 
ATOM   8372 S  SD  . MET A 1 1034 ? 39.233 48.450  -17.320 1.00 12.76 ? 1034 MET A SD  1 
ATOM   8373 C  CE  . MET A 1 1034 ? 38.396 48.983  -15.802 1.00 14.33 ? 1034 MET A CE  1 
ATOM   8374 N  N   . GLU A 1 1035 ? 43.578 45.761  -15.064 1.00 10.81 ? 1035 GLU A N   1 
ATOM   8375 C  CA  . GLU A 1 1035 ? 44.418 45.430  -13.915 1.00 11.63 ? 1035 GLU A CA  1 
ATOM   8376 C  C   . GLU A 1 1035 ? 45.463 46.508  -13.713 1.00 10.66 ? 1035 GLU A C   1 
ATOM   8377 O  O   . GLU A 1 1035 ? 45.830 47.230  -14.648 1.00 10.16 ? 1035 GLU A O   1 
ATOM   8378 C  CB  . GLU A 1 1035 ? 45.040 44.049  -14.082 1.00 14.28 ? 1035 GLU A CB  1 
ATOM   8379 C  CG  . GLU A 1 1035 ? 44.014 42.925  -13.888 1.00 21.12 ? 1035 GLU A CG  1 
ATOM   8380 C  CD  . GLU A 1 1035 ? 43.625 42.730  -12.422 1.00 29.26 ? 1035 GLU A CD  1 
ATOM   8381 O  OE1 . GLU A 1 1035 ? 42.774 43.496  -11.897 1.00 31.98 ? 1035 GLU A OE1 1 
ATOM   8382 O  OE2 . GLU A 1 1035 ? 44.190 41.802  -11.790 1.00 35.64 ? 1035 GLU A OE2 1 
ATOM   8383 N  N   . THR A 1 1036 ? 45.928 46.614  -12.469 1.00 10.31 ? 1036 THR A N   1 
ATOM   8384 C  CA  . THR A 1 1036 ? 46.982 47.533  -12.065 1.00 10.69 ? 1036 THR A CA  1 
ATOM   8385 C  C   . THR A 1 1036 ? 47.954 46.700  -11.260 1.00 11.15 ? 1036 THR A C   1 
ATOM   8386 O  O   . THR A 1 1036 ? 47.525 45.935  -10.388 1.00 11.85 ? 1036 THR A O   1 
ATOM   8387 C  CB  . THR A 1 1036 ? 46.383 48.638  -11.184 1.00 10.47 ? 1036 THR A CB  1 
ATOM   8388 O  OG1 . THR A 1 1036 ? 45.302 49.273  -11.873 1.00 11.11 ? 1036 THR A OG1 1 
ATOM   8389 C  CG2 . THR A 1 1036 ? 47.391 49.713  -10.830 1.00 11.61 ? 1036 THR A CG2 1 
ATOM   8390 N  N   . ALA A 1 1037 ? 49.240 46.814  -11.565 1.00 10.08 ? 1037 ALA A N   1 
ATOM   8391 C  CA  . ALA A 1 1037 ? 50.300 46.101  -10.858 1.00 10.37 ? 1037 ALA A CA  1 
ATOM   8392 C  C   . ALA A 1 1037 ? 51.403 47.046  -10.521 1.00 10.37 ? 1037 ALA A C   1 
ATOM   8393 O  O   . ALA A 1 1037 ? 51.547 48.095  -11.158 1.00 11.30 ? 1037 ALA A O   1 
ATOM   8394 C  CB  . ALA A 1 1037 ? 50.847 44.977  -11.725 1.00 12.34 ? 1037 ALA A CB  1 
ATOM   8395 N  N   . ALA A 1 1038 ? 52.170 46.695  -9.506  1.00 8.84  ? 1038 ALA A N   1 
ATOM   8396 C  CA  . ALA A 1 1038 ? 53.329 47.469  -9.123  1.00 9.25  ? 1038 ALA A CA  1 
ATOM   8397 C  C   . ALA A 1 1038 ? 54.574 46.605  -9.169  1.00 9.55  ? 1038 ALA A C   1 
ATOM   8398 O  O   . ALA A 1 1038 ? 54.535 45.415  -8.811  1.00 9.74  ? 1038 ALA A O   1 
ATOM   8399 C  CB  . ALA A 1 1038 ? 53.143 48.077  -7.740  1.00 9.24  ? 1038 ALA A CB  1 
ATOM   8400 N  N   . TYR A 1 1039 ? 55.666 47.222  -9.581  1.00 9.71  ? 1039 TYR A N   1 
ATOM   8401 C  CA  . TYR A 1 1039 ? 56.954 46.517  -9.627  1.00 10.81 ? 1039 TYR A CA  1 
ATOM   8402 C  C   . TYR A 1 1039 ? 58.017 47.392  -9.052  1.00 11.42 ? 1039 TYR A C   1 
ATOM   8403 O  O   . TYR A 1 1039 ? 57.936 48.614  -9.183  1.00 12.48 ? 1039 TYR A O   1 
ATOM   8404 C  CB  . TYR A 1 1039 ? 57.321 46.181  -11.063 1.00 12.13 ? 1039 TYR A CB  1 
ATOM   8405 C  CG  . TYR A 1 1039 ? 56.351 45.276  -11.764 1.00 12.28 ? 1039 TYR A CG  1 
ATOM   8406 C  CD1 . TYR A 1 1039 ? 56.338 43.899  -11.539 1.00 14.49 ? 1039 TYR A CD1 1 
ATOM   8407 C  CD2 . TYR A 1 1039 ? 55.402 45.807  -12.634 1.00 15.69 ? 1039 TYR A CD2 1 
ATOM   8408 C  CE1 . TYR A 1 1039 ? 55.414 43.081  -12.187 1.00 16.60 ? 1039 TYR A CE1 1 
ATOM   8409 C  CE2 . TYR A 1 1039 ? 54.501 44.997  -13.298 1.00 16.87 ? 1039 TYR A CE2 1 
ATOM   8410 C  CZ  . TYR A 1 1039 ? 54.504 43.649  -13.060 1.00 17.89 ? 1039 TYR A CZ  1 
ATOM   8411 O  OH  . TYR A 1 1039 ? 53.605 42.857  -13.747 1.00 20.11 ? 1039 TYR A OH  1 
ATOM   8412 N  N   . VAL A 1 1040 ? 59.031 46.796  -8.412  1.00 11.46 ? 1040 VAL A N   1 
ATOM   8413 C  CA  . VAL A 1 1040 ? 60.198 47.542  -7.954  1.00 12.13 ? 1040 VAL A CA  1 
ATOM   8414 C  C   . VAL A 1 1040 ? 61.424 46.893  -8.566  1.00 12.09 ? 1040 VAL A C   1 
ATOM   8415 O  O   . VAL A 1 1040 ? 61.618 45.656  -8.428  1.00 12.22 ? 1040 VAL A O   1 
ATOM   8416 C  CB  . VAL A 1 1040 ? 60.303 47.539  -6.429  1.00 11.84 ? 1040 VAL A CB  1 
ATOM   8417 C  CG1 . VAL A 1 1040 ? 61.604 48.236  -5.985  1.00 12.80 ? 1040 VAL A CG1 1 
ATOM   8418 C  CG2 . VAL A 1 1040 ? 59.136 48.279  -5.825  1.00 12.19 ? 1040 VAL A CG2 1 
ATOM   8419 N  N   . SER A 1 1041 ? 62.236 47.695  -9.251  1.00 11.49 ? 1041 SER A N   1 
ATOM   8420 C  CA  . SER A 1 1041 ? 63.520 47.229  -9.758  1.00 12.49 ? 1041 SER A CA  1 
ATOM   8421 C  C   . SER A 1 1041 ? 64.619 47.685  -8.828  1.00 12.98 ? 1041 SER A C   1 
ATOM   8422 O  O   . SER A 1 1041 ? 64.605 48.808  -8.338  1.00 12.70 ? 1041 SER A O   1 
ATOM   8423 C  CB  . SER A 1 1041 ? 63.738 47.720  -11.193 1.00 13.07 ? 1041 SER A CB  1 
ATOM   8424 O  OG  . SER A 1 1041 ? 63.783 49.133  -11.305 1.00 13.63 ? 1041 SER A OG  1 
ATOM   8425 N  N   . SER A 1 1042 ? 65.589 46.783  -8.602  1.00 14.00 ? 1042 SER A N   1 
ATOM   8426 C  CA  . SER A 1 1042 ? 66.736 47.072  -7.759  1.00 14.67 ? 1042 SER A CA  1 
ATOM   8427 C  C   . SER A 1 1042 ? 67.987 47.136  -8.640  1.00 15.11 ? 1042 SER A C   1 
ATOM   8428 O  O   . SER A 1 1042 ? 68.117 46.336  -9.576  1.00 16.28 ? 1042 SER A O   1 
ATOM   8429 C  CB  . SER A 1 1042 ? 66.919 45.985  -6.693  1.00 15.14 ? 1042 SER A CB  1 
ATOM   8430 O  OG  . SER A 1 1042 ? 65.799 45.958  -5.830  1.00 16.65 ? 1042 SER A OG  1 
ATOM   8431 N  N   . HIS A 1 1043 ? 68.855 48.103  -8.360  1.00 16.34 ? 1043 HIS A N   1 
ATOM   8432 C  CA  . HIS A 1 1043 ? 70.004 48.387  -9.218  1.00 17.81 ? 1043 HIS A CA  1 
ATOM   8433 C  C   . HIS A 1 1043 ? 71.270 48.519  -8.397  1.00 19.89 ? 1043 HIS A C   1 
ATOM   8434 O  O   . HIS A 1 1043 ? 71.301 49.183  -7.361  1.00 18.49 ? 1043 HIS A O   1 
ATOM   8435 C  CB  . HIS A 1 1043 ? 69.750 49.659  -10.051 1.00 17.46 ? 1043 HIS A CB  1 
ATOM   8436 C  CG  . HIS A 1 1043 ? 68.448 49.614  -10.792 1.00 16.89 ? 1043 HIS A CG  1 
ATOM   8437 N  ND1 . HIS A 1 1043 ? 68.340 49.145  -12.085 1.00 16.33 ? 1043 HIS A ND1 1 
ATOM   8438 C  CD2 . HIS A 1 1043 ? 67.180 49.874  -10.378 1.00 13.94 ? 1043 HIS A CD2 1 
ATOM   8439 C  CE1 . HIS A 1 1043 ? 67.070 49.158  -12.452 1.00 16.27 ? 1043 HIS A CE1 1 
ATOM   8440 N  NE2 . HIS A 1 1043 ? 66.348 49.576  -11.421 1.00 14.03 ? 1043 HIS A NE2 1 
ATOM   8441 N  N   . SER A 1 1044 ? 72.319 47.859  -8.886  1.00 23.66 ? 1044 SER A N   1 
ATOM   8442 C  CA  . SER A 1 1044 ? 73.593 47.805  -8.169  1.00 28.04 ? 1044 SER A CA  1 
ATOM   8443 C  C   . SER A 1 1044 ? 74.574 48.854  -8.678  1.00 30.48 ? 1044 SER A C   1 
ATOM   8444 O  O   . SER A 1 1044 ? 75.604 49.104  -8.040  1.00 31.64 ? 1044 SER A O   1 
ATOM   8445 C  CB  . SER A 1 1044 ? 74.213 46.406  -8.313  1.00 28.17 ? 1044 SER A CB  1 
ATOM   8446 O  OG  . SER A 1 1044 ? 74.155 45.957  -9.662  1.00 29.91 ? 1044 SER A OG  1 
ATOM   8447 N  N   . SER A 1 1045 ? 74.231 49.454  -9.817  1.00 32.84 ? 1045 SER A N   1 
ATOM   8448 C  CA  . SER A 1 1045 ? 75.095 50.319  -10.646 1.00 35.11 ? 1045 SER A CA  1 
ATOM   8449 C  C   . SER A 1 1045 ? 76.631 50.224  -10.489 1.00 36.04 ? 1045 SER A C   1 
ATOM   8450 O  O   . SER A 1 1045 ? 77.371 51.216  -10.421 1.00 37.08 ? 1045 SER A O   1 
ATOM   8451 C  CB  . SER A 1 1045 ? 74.585 51.765  -10.620 1.00 35.06 ? 1045 SER A CB  1 
ATOM   8452 O  OG  . SER A 1 1045 ? 73.297 51.811  -11.202 1.00 35.87 ? 1045 SER A OG  1 
ATOM   8453 O  OXT . SER A 1 1045 ? 77.266 49.159  -10.455 1.00 37.29 ? 1045 SER A OXT 1 
HETATM 8454 C  C1  . NAG B 2 .    ? 58.314 44.901  12.750  1.00 37.33 ? 1046 NAG A C1  1 
HETATM 8455 C  C2  . NAG B 2 .    ? 59.376 44.548  13.785  1.00 34.25 ? 1046 NAG A C2  1 
HETATM 8456 C  C3  . NAG B 2 .    ? 59.985 43.195  13.540  1.00 63.47 ? 1046 NAG A C3  1 
HETATM 8457 C  C4  . NAG B 2 .    ? 58.973 42.161  13.819  1.00 81.24 ? 1046 NAG A C4  1 
HETATM 8458 C  C5  . NAG B 2 .    ? 57.677 42.515  13.130  1.00 71.79 ? 1046 NAG A C5  1 
HETATM 8459 C  C6  . NAG B 2 .    ? 56.505 41.901  13.921  1.00 73.80 ? 1046 NAG A C6  1 
HETATM 8460 C  C7  . NAG B 2 .    ? 60.842 46.073  14.702  1.00 61.56 ? 1046 NAG A C7  1 
HETATM 8461 C  C8  . NAG B 2 .    ? 60.035 45.739  15.984  1.00 91.28 ? 1046 NAG A C8  1 
HETATM 8462 N  N2  . NAG B 2 .    ? 60.475 45.445  13.640  1.00 41.96 ? 1046 NAG A N2  1 
HETATM 8463 O  O3  . NAG B 2 .    ? 61.106 43.021  14.398  1.00 61.96 ? 1046 NAG A O3  1 
HETATM 8464 O  O4  . NAG B 2 .    ? 59.529 40.930  13.329  1.00 89.05 ? 1046 NAG A O4  1 
HETATM 8465 O  O5  . NAG B 2 .    ? 57.324 43.967  13.014  1.00 53.40 ? 1046 NAG A O5  1 
HETATM 8466 O  O6  . NAG B 2 .    ? 56.607 40.462  13.913  1.00 65.13 ? 1046 NAG A O6  1 
HETATM 8467 O  O7  . NAG B 2 .    ? 61.723 46.909  14.691  1.00 89.67 ? 1046 NAG A O7  1 
HETATM 8468 P  P   . PO4 C 3 .    ? 45.239 65.706  -29.688 1.00 24.21 ? 1047 PO4 A P   1 
HETATM 8469 O  O1  . PO4 C 3 .    ? 46.651 65.308  -30.071 1.00 28.88 ? 1047 PO4 A O1  1 
HETATM 8470 O  O2  . PO4 C 3 .    ? 44.921 67.053  -30.314 1.00 29.51 ? 1047 PO4 A O2  1 
HETATM 8471 O  O3  . PO4 C 3 .    ? 44.172 64.711  -30.165 1.00 29.12 ? 1047 PO4 A O3  1 
HETATM 8472 O  O4  . PO4 C 3 .    ? 45.218 65.952  -28.200 1.00 30.25 ? 1047 PO4 A O4  1 
HETATM 8473 ZN ZN  . ZN  D 4 .    ? 34.861 64.375  8.030   1.00 8.16  ? 1048 ZN  A ZN  1 
HETATM 8474 C  C1  . MRD E 5 .    ? 16.820 62.603  10.386  1.00 22.85 ? 1049 MRD A C1  1 
HETATM 8475 C  C2  . MRD E 5 .    ? 16.271 61.213  10.698  1.00 19.60 ? 1049 MRD A C2  1 
HETATM 8476 O  O2  . MRD E 5 .    ? 14.878 61.181  10.302  1.00 21.60 ? 1049 MRD A O2  1 
HETATM 8477 C  CM  . MRD E 5 .    ? 16.999 60.167  9.859   1.00 21.38 ? 1049 MRD A CM  1 
HETATM 8478 C  C3  . MRD E 5 .    ? 16.322 60.897  12.193  1.00 21.29 ? 1049 MRD A C3  1 
HETATM 8479 C  C4  . MRD E 5 .    ? 17.723 60.674  12.750  1.00 25.35 ? 1049 MRD A C4  1 
HETATM 8480 O  O4  . MRD E 5 .    ? 17.680 59.727  13.802  1.00 15.12 ? 1049 MRD A O4  1 
HETATM 8481 C  C5  . MRD E 5 .    ? 18.315 61.995  13.240  1.00 22.01 ? 1049 MRD A C5  1 
HETATM 8482 O  O41 . WZ1 F 6 .    ? 28.588 63.746  11.249  1.00 25.54 ? 1050 WZ1 A O41 1 
HETATM 8483 C  C41 . WZ1 F 6 .    ? 28.201 65.038  11.779  1.00 25.58 ? 1050 WZ1 A C41 1 
HETATM 8484 C  C51 . WZ1 F 6 .    ? 26.709 64.921  12.171  1.00 27.98 ? 1050 WZ1 A C51 1 
HETATM 8485 C  C61 . WZ1 F 6 .    ? 26.410 63.916  13.308  1.00 31.72 ? 1050 WZ1 A C61 1 
HETATM 8486 O  O61 . WZ1 F 6 .    ? 25.287 63.085  12.957  1.00 33.55 ? 1050 WZ1 A O61 1 
HETATM 8487 O  O01 . WZ1 F 6 .    ? 26.226 66.238  12.570  1.00 29.47 ? 1050 WZ1 A O01 1 
HETATM 8488 C  C11 . WZ1 F 6 .    ? 26.251 67.239  11.508  1.00 27.46 ? 1050 WZ1 A C11 1 
HETATM 8489 O  O11 . WZ1 F 6 .    ? 25.599 66.786  10.318  1.00 29.36 ? 1050 WZ1 A O11 1 
HETATM 8490 C  C71 . WZ1 F 6 .    ? 24.369 67.512  10.063  1.00 30.80 ? 1050 WZ1 A C71 1 
HETATM 8491 C  C21 . WZ1 F 6 .    ? 27.690 67.492  11.036  1.00 24.61 ? 1050 WZ1 A C21 1 
HETATM 8492 O  O21 . WZ1 F 6 .    ? 28.414 68.254  12.009  1.00 25.05 ? 1050 WZ1 A O21 1 
HETATM 8493 C  C31 . WZ1 F 6 .    ? 28.438 66.174  10.729  1.00 21.01 ? 1050 WZ1 A C31 1 
HETATM 8494 S  S12 . WZ1 F 6 .    ? 30.213 66.584  10.489  1.00 15.90 ? 1050 WZ1 A S12 1 
HETATM 8495 C  C12 . WZ1 F 6 .    ? 30.744 65.286  9.344   1.00 11.96 ? 1050 WZ1 A C12 1 
HETATM 8496 O  O02 . WZ1 F 6 .    ? 29.947 65.299  8.134   1.00 12.08 ? 1050 WZ1 A O02 1 
HETATM 8497 C  C52 . WZ1 F 6 .    ? 30.093 66.490  7.326   1.00 12.22 ? 1050 WZ1 A C52 1 
HETATM 8498 C  C62 . WZ1 F 6 .    ? 29.001 66.447  6.266   1.00 11.18 ? 1050 WZ1 A C62 1 
HETATM 8499 O  O62 . WZ1 F 6 .    ? 27.724 66.620  6.955   1.00 12.82 ? 1050 WZ1 A O62 1 
HETATM 8500 C  C42 . WZ1 F 6 .    ? 31.503 66.444  6.733   1.00 11.80 ? 1050 WZ1 A C42 1 
HETATM 8501 O  O42 . WZ1 F 6 .    ? 31.700 67.609  5.923   1.00 9.17  ? 1050 WZ1 A O42 1 
HETATM 8502 C  C32 . WZ1 F 6 .    ? 32.519 66.439  7.884   1.00 12.27 ? 1050 WZ1 A C32 1 
HETATM 8503 O  O32 . WZ1 F 6 .    ? 33.795 66.069  7.305   1.00 10.77 ? 1050 WZ1 A O32 1 
HETATM 8504 C  C22 . WZ1 F 6 .    ? 32.240 65.389  8.980   1.00 11.81 ? 1050 WZ1 A C22 1 
HETATM 8505 O  O22 . WZ1 F 6 .    ? 32.719 64.086  8.573   1.00 10.80 ? 1050 WZ1 A O22 1 
HETATM 8506 C  C1  . MPD G 7 .    ? 51.131 75.631  -13.635 1.00 36.64 ? 1051 MPD A C1  1 
HETATM 8507 C  C2  . MPD G 7 .    ? 52.230 76.626  -13.303 1.00 37.60 ? 1051 MPD A C2  1 
HETATM 8508 O  O2  . MPD G 7 .    ? 53.231 76.548  -14.358 1.00 38.11 ? 1051 MPD A O2  1 
HETATM 8509 C  CM  . MPD G 7 .    ? 51.584 78.008  -13.282 1.00 37.00 ? 1051 MPD A CM  1 
HETATM 8510 C  C3  . MPD G 7 .    ? 52.871 76.237  -11.964 1.00 36.73 ? 1051 MPD A C3  1 
HETATM 8511 C  C4  . MPD G 7 .    ? 53.734 77.246  -11.185 1.00 37.49 ? 1051 MPD A C4  1 
HETATM 8512 O  O4  . MPD G 7 .    ? 54.828 76.558  -10.601 1.00 35.57 ? 1051 MPD A O4  1 
HETATM 8513 C  C5  . MPD G 7 .    ? 54.288 78.418  -11.987 1.00 36.68 ? 1051 MPD A C5  1 
HETATM 8514 C  C1  . MPD H 7 .    ? 35.062 71.228  15.515  1.00 48.94 ? 1052 MPD A C1  1 
HETATM 8515 C  C2  . MPD H 7 .    ? 35.412 71.044  16.984  1.00 50.11 ? 1052 MPD A C2  1 
HETATM 8516 O  O2  . MPD H 7 .    ? 36.805 70.635  17.019  1.00 49.42 ? 1052 MPD A O2  1 
HETATM 8517 C  CM  . MPD H 7 .    ? 35.264 72.363  17.745  1.00 49.96 ? 1052 MPD A CM  1 
HETATM 8518 C  C3  . MPD H 7 .    ? 34.550 69.965  17.648  1.00 50.21 ? 1052 MPD A C3  1 
HETATM 8519 C  C4  . MPD H 7 .    ? 33.272 69.612  16.890  1.00 51.06 ? 1052 MPD A C4  1 
HETATM 8520 O  O4  . MPD H 7 .    ? 33.078 68.216  16.945  1.00 50.46 ? 1052 MPD A O4  1 
HETATM 8521 C  C5  . MPD H 7 .    ? 32.062 70.349  17.465  1.00 51.49 ? 1052 MPD A C5  1 
HETATM 8522 O  O   . HOH I 8 .    ? 26.614 46.351  -37.314 1.00 44.67 ? 1053 HOH A O   1 
HETATM 8523 O  O   . HOH I 8 .    ? 22.912 48.930  -36.095 1.00 34.88 ? 1054 HOH A O   1 
HETATM 8524 O  O   . HOH I 8 .    ? 21.769 47.001  -34.580 1.00 49.72 ? 1055 HOH A O   1 
HETATM 8525 O  O   . HOH I 8 .    ? 20.807 51.126  -38.306 1.00 28.95 ? 1056 HOH A O   1 
HETATM 8526 O  O   . HOH I 8 .    ? 21.558 55.395  -36.313 1.00 27.32 ? 1057 HOH A O   1 
HETATM 8527 O  O   . HOH I 8 .    ? 23.876 55.867  -37.733 1.00 63.75 ? 1058 HOH A O   1 
HETATM 8528 O  O   . HOH I 8 .    ? 25.774 58.906  -38.735 1.00 54.22 ? 1059 HOH A O   1 
HETATM 8529 O  O   . HOH I 8 .    ? 24.889 59.425  -36.275 1.00 35.64 ? 1060 HOH A O   1 
HETATM 8530 O  O   . HOH I 8 .    ? 23.453 60.314  -39.227 1.00 52.22 ? 1061 HOH A O   1 
HETATM 8531 O  O   . HOH I 8 .    ? 21.957 61.465  -34.910 1.00 30.29 ? 1062 HOH A O   1 
HETATM 8532 O  O   . HOH I 8 .    ? 22.565 63.308  -33.098 1.00 20.55 ? 1063 HOH A O   1 
HETATM 8533 O  O   . HOH I 8 .    ? 20.803 59.018  -34.460 1.00 18.77 ? 1064 HOH A O   1 
HETATM 8534 O  O   . HOH I 8 .    ? 22.441 56.794  -34.109 1.00 16.63 ? 1065 HOH A O   1 
HETATM 8535 O  O   . HOH I 8 .    ? 19.520 51.891  -30.960 1.00 36.77 ? 1066 HOH A O   1 
HETATM 8536 O  O   . HOH I 8 .    ? 19.764 52.467  -27.108 1.00 27.99 ? 1067 HOH A O   1 
HETATM 8537 O  O   . HOH I 8 .    ? 20.150 52.687  -24.184 1.00 17.00 ? 1068 HOH A O   1 
HETATM 8538 O  O   . HOH I 8 .    ? 22.869 53.052  -24.336 1.00 12.58 ? 1069 HOH A O   1 
HETATM 8539 O  O   . HOH I 8 .    ? 24.722 51.092  -24.009 1.00 12.89 ? 1070 HOH A O   1 
HETATM 8540 O  O   . HOH I 8 .    ? 23.886 48.434  -24.147 1.00 27.39 ? 1071 HOH A O   1 
HETATM 8541 O  O   . HOH I 8 .    ? 22.948 48.681  -26.768 1.00 52.20 ? 1072 HOH A O   1 
HETATM 8542 O  O   . HOH I 8 .    ? 21.516 48.708  -22.418 1.00 38.24 ? 1073 HOH A O   1 
HETATM 8543 O  O   . HOH I 8 .    ? 19.133 50.340  -23.238 1.00 33.10 ? 1074 HOH A O   1 
HETATM 8544 O  O   . HOH I 8 .    ? 16.597 52.935  -22.375 1.00 26.59 ? 1075 HOH A O   1 
HETATM 8545 O  O   . HOH I 8 .    ? 16.076 52.817  -25.295 1.00 41.93 ? 1076 HOH A O   1 
HETATM 8546 O  O   . HOH I 8 .    ? 13.605 55.583  -22.321 1.00 37.90 ? 1077 HOH A O   1 
HETATM 8547 O  O   A HOH I 8 .    ? 13.453 58.088  -21.661 0.50 15.81 ? 1078 HOH A O   1 
HETATM 8548 O  O   B HOH I 8 .    ? 13.149 58.280  -23.082 0.50 21.34 ? 1078 HOH A O   1 
HETATM 8549 O  O   . HOH I 8 .    ? 13.907 60.781  -22.403 1.00 16.92 ? 1079 HOH A O   1 
HETATM 8550 O  O   A HOH I 8 .    ? 12.954 61.974  -25.036 0.50 21.45 ? 1080 HOH A O   1 
HETATM 8551 O  O   B HOH I 8 .    ? 12.148 61.362  -23.983 0.50 16.54 ? 1080 HOH A O   1 
HETATM 8552 O  O   . HOH I 8 .    ? 15.029 63.557  -25.867 1.00 24.19 ? 1081 HOH A O   1 
HETATM 8553 O  O   . HOH I 8 .    ? 18.517 64.922  -26.989 1.00 20.31 ? 1082 HOH A O   1 
HETATM 8554 O  O   . HOH I 8 .    ? 17.150 67.033  -25.980 1.00 28.91 ? 1083 HOH A O   1 
HETATM 8555 O  O   . HOH I 8 .    ? 17.232 70.096  -23.393 1.00 17.34 ? 1084 HOH A O   1 
HETATM 8556 O  O   . HOH I 8 .    ? 15.620 71.048  -27.010 1.00 55.66 ? 1085 HOH A O   1 
HETATM 8557 O  O   . HOH I 8 .    ? 18.625 70.430  -29.845 1.00 35.38 ? 1086 HOH A O   1 
HETATM 8558 O  O   . HOH I 8 .    ? 16.651 74.680  -28.498 1.00 48.18 ? 1087 HOH A O   1 
HETATM 8559 O  O   . HOH I 8 .    ? 16.943 77.738  -25.894 1.00 46.10 ? 1088 HOH A O   1 
HETATM 8560 O  O   . HOH I 8 .    ? 19.340 78.933  -25.473 1.00 31.74 ? 1089 HOH A O   1 
HETATM 8561 O  O   . HOH I 8 .    ? 20.903 78.395  -27.209 1.00 40.88 ? 1090 HOH A O   1 
HETATM 8562 O  O   . HOH I 8 .    ? 22.839 77.261  -27.474 1.00 27.62 ? 1091 HOH A O   1 
HETATM 8563 O  O   . HOH I 8 .    ? 23.243 78.392  -24.806 1.00 16.63 ? 1092 HOH A O   1 
HETATM 8564 O  O   . HOH I 8 .    ? 21.118 79.362  -23.556 1.00 21.26 ? 1093 HOH A O   1 
HETATM 8565 O  O   . HOH I 8 .    ? 19.159 83.453  -25.818 1.00 31.65 ? 1094 HOH A O   1 
HETATM 8566 O  O   . HOH I 8 .    ? 21.502 86.063  -30.807 1.00 32.85 ? 1095 HOH A O   1 
HETATM 8567 O  O   . HOH I 8 .    ? 23.278 86.987  -32.616 1.00 33.08 ? 1096 HOH A O   1 
HETATM 8568 O  O   . HOH I 8 .    ? 25.621 86.088  -31.877 1.00 17.35 ? 1097 HOH A O   1 
HETATM 8569 O  O   . HOH I 8 .    ? 27.195 89.784  -31.841 1.00 37.34 ? 1098 HOH A O   1 
HETATM 8570 O  O   . HOH I 8 .    ? 25.878 91.625  -32.835 1.00 39.46 ? 1099 HOH A O   1 
HETATM 8571 O  O   . HOH I 8 .    ? 28.058 93.556  -29.790 1.00 35.79 ? 1100 HOH A O   1 
HETATM 8572 O  O   . HOH I 8 .    ? 26.815 91.721  -27.655 1.00 30.10 ? 1101 HOH A O   1 
HETATM 8573 O  O   . HOH I 8 .    ? 28.109 90.892  -25.377 1.00 21.27 ? 1102 HOH A O   1 
HETATM 8574 O  O   . HOH I 8 .    ? 29.579 88.716  -26.256 1.00 13.13 ? 1103 HOH A O   1 
HETATM 8575 O  O   . HOH I 8 .    ? 27.031 87.894  -23.649 1.00 25.98 ? 1104 HOH A O   1 
HETATM 8576 O  O   . HOH I 8 .    ? 25.127 88.769  -25.231 1.00 30.78 ? 1105 HOH A O   1 
HETATM 8577 O  O   . HOH I 8 .    ? 23.908 90.893  -26.150 1.00 39.93 ? 1106 HOH A O   1 
HETATM 8578 O  O   . HOH I 8 .    ? 22.535 88.241  -22.731 1.00 48.26 ? 1107 HOH A O   1 
HETATM 8579 O  O   . HOH I 8 .    ? 22.767 88.596  -18.707 1.00 38.48 ? 1108 HOH A O   1 
HETATM 8580 O  O   . HOH I 8 .    ? 23.271 87.195  -16.460 1.00 38.92 ? 1109 HOH A O   1 
HETATM 8581 O  O   . HOH I 8 .    ? 22.822 84.890  -17.041 1.00 32.13 ? 1110 HOH A O   1 
HETATM 8582 O  O   . HOH I 8 .    ? 24.923 83.082  -16.914 1.00 21.34 ? 1111 HOH A O   1 
HETATM 8583 O  O   . HOH I 8 .    ? 25.702 87.586  -16.177 1.00 46.13 ? 1112 HOH A O   1 
HETATM 8584 O  O   . HOH I 8 .    ? 27.671 86.287  -14.505 1.00 29.91 ? 1113 HOH A O   1 
HETATM 8585 O  O   . HOH I 8 .    ? 30.325 87.195  -15.072 1.00 24.24 ? 1114 HOH A O   1 
HETATM 8586 O  O   . HOH I 8 .    ? 29.756 87.334  -17.967 1.00 27.62 ? 1115 HOH A O   1 
HETATM 8587 O  O   . HOH I 8 .    ? 27.563 89.012  -18.238 1.00 45.03 ? 1116 HOH A O   1 
HETATM 8588 O  O   . HOH I 8 .    ? 26.517 88.878  -21.314 1.00 55.00 ? 1117 HOH A O   1 
HETATM 8589 O  O   . HOH I 8 .    ? 21.638 86.127  -19.258 1.00 29.77 ? 1118 HOH A O   1 
HETATM 8590 O  O   . HOH I 8 .    ? 19.744 84.271  -18.419 1.00 30.13 ? 1119 HOH A O   1 
HETATM 8591 O  O   . HOH I 8 .    ? 17.406 81.209  -17.257 1.00 45.29 ? 1120 HOH A O   1 
HETATM 8592 O  O   . HOH I 8 .    ? 15.012 84.081  -18.851 1.00 52.30 ? 1121 HOH A O   1 
HETATM 8593 O  O   . HOH I 8 .    ? 14.094 88.313  -19.939 1.00 30.49 ? 1122 HOH A O   1 
HETATM 8594 O  O   . HOH I 8 .    ? 12.531 77.603  -18.947 1.00 50.23 ? 1123 HOH A O   1 
HETATM 8595 O  O   . HOH I 8 .    ? 12.921 74.808  -18.917 1.00 39.74 ? 1124 HOH A O   1 
HETATM 8596 O  O   . HOH I 8 .    ? 14.961 73.649  -21.905 1.00 36.36 ? 1125 HOH A O   1 
HETATM 8597 O  O   . HOH I 8 .    ? 12.690 74.345  -22.994 1.00 41.72 ? 1126 HOH A O   1 
HETATM 8598 O  O   . HOH I 8 .    ? 16.263 74.801  -23.960 1.00 41.78 ? 1127 HOH A O   1 
HETATM 8599 O  O   . HOH I 8 .    ? 16.070 71.954  -18.981 1.00 20.12 ? 1128 HOH A O   1 
HETATM 8600 O  O   . HOH I 8 .    ? 17.123 70.289  -16.242 1.00 12.39 ? 1129 HOH A O   1 
HETATM 8601 O  O   . HOH I 8 .    ? 16.467 67.826  -19.769 1.00 20.27 ? 1130 HOH A O   1 
HETATM 8602 O  O   . HOH I 8 .    ? 20.574 66.176  -19.568 1.00 12.99 ? 1131 HOH A O   1 
HETATM 8603 O  O   . HOH I 8 .    ? 14.688 66.353  -15.399 1.00 21.74 ? 1132 HOH A O   1 
HETATM 8604 O  O   . HOH I 8 .    ? 14.416 63.935  -16.284 1.00 18.74 ? 1133 HOH A O   1 
HETATM 8605 O  O   . HOH I 8 .    ? 14.613 61.930  -14.410 1.00 23.13 ? 1134 HOH A O   1 
HETATM 8606 O  O   . HOH I 8 .    ? 14.241 62.852  -12.045 1.00 20.42 ? 1135 HOH A O   1 
HETATM 8607 O  O   . HOH I 8 .    ? 12.394 64.378  -12.384 1.00 31.46 ? 1136 HOH A O   1 
HETATM 8608 O  O   . HOH I 8 .    ? 10.663 62.458  -12.211 1.00 36.90 ? 1137 HOH A O   1 
HETATM 8609 O  O   . HOH I 8 .    ? 10.008 62.912  -14.663 1.00 38.28 ? 1138 HOH A O   1 
HETATM 8610 O  O   . HOH I 8 .    ? 8.806  60.446  -16.574 1.00 54.46 ? 1139 HOH A O   1 
HETATM 8611 O  O   . HOH I 8 .    ? 11.407 61.356  -18.167 1.00 21.57 ? 1140 HOH A O   1 
HETATM 8612 O  O   . HOH I 8 .    ? 13.377 62.362  -19.944 1.00 19.23 ? 1141 HOH A O   1 
HETATM 8613 O  O   . HOH I 8 .    ? 11.402 56.673  -18.396 1.00 39.63 ? 1142 HOH A O   1 
HETATM 8614 O  O   . HOH I 8 .    ? 9.837  55.458  -16.221 1.00 47.61 ? 1143 HOH A O   1 
HETATM 8615 O  O   . HOH I 8 .    ? 12.257 55.701  -14.997 1.00 18.82 ? 1144 HOH A O   1 
HETATM 8616 O  O   . HOH I 8 .    ? 14.373 54.263  -16.147 1.00 19.05 ? 1145 HOH A O   1 
HETATM 8617 O  O   . HOH I 8 .    ? 13.375 51.945  -15.140 1.00 27.25 ? 1146 HOH A O   1 
HETATM 8618 O  O   . HOH I 8 .    ? 12.703 51.745  -11.897 1.00 28.56 ? 1147 HOH A O   1 
HETATM 8619 O  O   . HOH I 8 .    ? 11.153 48.841  -11.755 1.00 48.27 ? 1148 HOH A O   1 
HETATM 8620 O  O   . HOH I 8 .    ? 10.473 50.693  -9.100  1.00 30.61 ? 1149 HOH A O   1 
HETATM 8621 O  O   . HOH I 8 .    ? 9.476  48.084  -8.318  1.00 41.47 ? 1150 HOH A O   1 
HETATM 8622 O  O   . HOH I 8 .    ? 8.492  45.536  -7.481  1.00 54.94 ? 1151 HOH A O   1 
HETATM 8623 O  O   . HOH I 8 .    ? 10.325 47.301  -4.747  1.00 45.09 ? 1152 HOH A O   1 
HETATM 8624 O  O   . HOH I 8 .    ? 11.873 48.289  -2.333  1.00 31.27 ? 1153 HOH A O   1 
HETATM 8625 O  O   . HOH I 8 .    ? 13.453 50.937  -1.463  1.00 22.83 ? 1154 HOH A O   1 
HETATM 8626 O  O   . HOH I 8 .    ? 14.401 50.750  1.078   1.00 25.65 ? 1155 HOH A O   1 
HETATM 8627 O  O   . HOH I 8 .    ? 13.478 48.365  1.728   1.00 29.81 ? 1156 HOH A O   1 
HETATM 8628 O  O   . HOH I 8 .    ? 10.411 51.759  2.522   1.00 31.76 ? 1157 HOH A O   1 
HETATM 8629 O  O   . HOH I 8 .    ? 10.885 53.665  4.242   1.00 26.81 ? 1158 HOH A O   1 
HETATM 8630 O  O   . HOH I 8 .    ? 11.406 53.274  6.969   1.00 18.30 ? 1159 HOH A O   1 
HETATM 8631 O  O   . HOH I 8 .    ? 13.791 54.254  4.550   1.00 16.24 ? 1160 HOH A O   1 
HETATM 8632 O  O   . HOH I 8 .    ? 12.496 56.418  5.442   1.00 17.91 ? 1161 HOH A O   1 
HETATM 8633 O  O   . HOH I 8 .    ? 11.618 58.864  8.063   1.00 24.71 ? 1162 HOH A O   1 
HETATM 8634 O  O   . HOH I 8 .    ? 9.789  59.948  6.593   1.00 31.14 ? 1163 HOH A O   1 
HETATM 8635 O  O   . HOH I 8 .    ? 11.326 62.347  5.377   1.00 33.69 ? 1164 HOH A O   1 
HETATM 8636 O  O   . HOH I 8 .    ? 13.233 63.174  6.680   1.00 34.48 ? 1165 HOH A O   1 
HETATM 8637 O  O   . HOH I 8 .    ? 13.769 60.869  7.851   1.00 25.60 ? 1166 HOH A O   1 
HETATM 8638 O  O   . HOH I 8 .    ? 14.475 60.154  5.253   1.00 13.70 ? 1167 HOH A O   1 
HETATM 8639 O  O   . HOH I 8 .    ? 14.472 65.613  5.619   1.00 33.41 ? 1168 HOH A O   1 
HETATM 8640 O  O   . HOH I 8 .    ? 13.510 67.876  4.550   1.00 38.54 ? 1169 HOH A O   1 
HETATM 8641 O  O   . HOH I 8 .    ? 11.617 66.876  2.962   1.00 47.03 ? 1170 HOH A O   1 
HETATM 8642 O  O   . HOH I 8 .    ? 13.256 68.713  0.936   1.00 19.91 ? 1171 HOH A O   1 
HETATM 8643 O  O   . HOH I 8 .    ? 12.590 71.017  -0.283  1.00 24.22 ? 1172 HOH A O   1 
HETATM 8644 O  O   . HOH I 8 .    ? 10.801 68.018  -1.833  1.00 39.22 ? 1173 HOH A O   1 
HETATM 8645 O  O   . HOH I 8 .    ? 13.184 66.765  -4.818  1.00 15.72 ? 1174 HOH A O   1 
HETATM 8646 O  O   . HOH I 8 .    ? 10.930 65.506  -5.426  1.00 37.11 ? 1175 HOH A O   1 
HETATM 8647 O  O   . HOH I 8 .    ? 11.269 62.598  -4.450  1.00 39.19 ? 1176 HOH A O   1 
HETATM 8648 O  O   . HOH I 8 .    ? 12.989 62.019  -2.346  1.00 23.99 ? 1177 HOH A O   1 
HETATM 8649 O  O   . HOH I 8 .    ? 11.548 61.624  -0.169  1.00 41.22 ? 1178 HOH A O   1 
HETATM 8650 O  O   . HOH I 8 .    ? 10.396 62.346  2.020   1.00 29.89 ? 1179 HOH A O   1 
HETATM 8651 O  O   . HOH I 8 .    ? 9.954  64.626  4.623   1.00 38.61 ? 1180 HOH A O   1 
HETATM 8652 O  O   . HOH I 8 .    ? 6.616  59.532  2.733   1.00 44.15 ? 1181 HOH A O   1 
HETATM 8653 O  O   . HOH I 8 .    ? 7.484  58.053  0.471   1.00 34.30 ? 1182 HOH A O   1 
HETATM 8654 O  O   . HOH I 8 .    ? 10.097 57.983  -3.162  1.00 30.92 ? 1183 HOH A O   1 
HETATM 8655 O  O   . HOH I 8 .    ? 11.855 59.495  -4.853  1.00 20.23 ? 1184 HOH A O   1 
HETATM 8656 O  O   . HOH I 8 .    ? 14.149 59.697  -3.378  1.00 14.69 ? 1185 HOH A O   1 
HETATM 8657 O  O   . HOH I 8 .    ? 14.001 57.894  -1.261  1.00 19.94 ? 1186 HOH A O   1 
HETATM 8658 O  O   . HOH I 8 .    ? 13.481 53.619  1.935   1.00 16.86 ? 1187 HOH A O   1 
HETATM 8659 O  O   . HOH I 8 .    ? 17.591 52.851  6.418   1.00 10.95 ? 1188 HOH A O   1 
HETATM 8660 O  O   . HOH I 8 .    ? 19.337 53.645  8.236   1.00 11.86 ? 1189 HOH A O   1 
HETATM 8661 O  O   . HOH I 8 .    ? 20.150 56.132  7.197   1.00 11.59 ? 1190 HOH A O   1 
HETATM 8662 O  O   . HOH I 8 .    ? 21.757 57.254  5.127   1.00 11.56 ? 1191 HOH A O   1 
HETATM 8663 O  O   . HOH I 8 .    ? 23.871 58.307  6.373   1.00 13.51 ? 1192 HOH A O   1 
HETATM 8664 O  O   . HOH I 8 .    ? 27.089 59.462  8.458   1.00 21.53 ? 1193 HOH A O   1 
HETATM 8665 O  O   . HOH I 8 .    ? 27.342 61.201  10.351  1.00 22.93 ? 1194 HOH A O   1 
HETATM 8666 O  O   . HOH I 8 .    ? 24.796 61.452  9.192   1.00 17.84 ? 1195 HOH A O   1 
HETATM 8667 O  O   . HOH I 8 .    ? 24.357 63.260  7.334   1.00 21.83 ? 1196 HOH A O   1 
HETATM 8668 O  O   . HOH I 8 .    ? 26.044 65.078  8.139   1.00 23.11 ? 1197 HOH A O   1 
HETATM 8669 O  O   . HOH I 8 .    ? 20.966 65.341  7.699   1.00 15.15 ? 1198 HOH A O   1 
HETATM 8670 O  O   . HOH I 8 .    ? 20.910 68.000  8.610   1.00 16.01 ? 1199 HOH A O   1 
HETATM 8671 O  O   . HOH I 8 .    ? 21.041 67.760  11.603  1.00 32.76 ? 1200 HOH A O   1 
HETATM 8672 O  O   . HOH I 8 .    ? 21.083 65.301  12.100  1.00 27.85 ? 1201 HOH A O   1 
HETATM 8673 O  O   . HOH I 8 .    ? 21.105 63.456  14.530  1.00 51.62 ? 1202 HOH A O   1 
HETATM 8674 O  O   . HOH I 8 .    ? 22.713 62.707  16.211  1.00 20.88 ? 1203 HOH A O   1 
HETATM 8675 O  O   . HOH I 8 .    ? 23.178 64.479  18.307  1.00 34.35 ? 1204 HOH A O   1 
HETATM 8676 O  O   . HOH I 8 .    ? 25.526 66.154  17.320  1.00 26.20 ? 1205 HOH A O   1 
HETATM 8677 O  O   . HOH I 8 .    ? 26.425 63.769  17.140  1.00 16.43 ? 1206 HOH A O   1 
HETATM 8678 O  O   . HOH I 8 .    ? 28.695 65.306  19.759  1.00 15.71 ? 1207 HOH A O   1 
HETATM 8679 O  O   . HOH I 8 .    ? 29.985 67.079  17.989  1.00 25.57 ? 1208 HOH A O   1 
HETATM 8680 O  O   . HOH I 8 .    ? 32.018 65.681  19.073  1.00 15.02 ? 1209 HOH A O   1 
HETATM 8681 O  O   . HOH I 8 .    ? 33.184 67.095  21.360  1.00 21.32 ? 1210 HOH A O   1 
HETATM 8682 O  O   . HOH I 8 .    ? 32.684 69.705  22.086  1.00 29.99 ? 1211 HOH A O   1 
HETATM 8683 O  O   . HOH I 8 .    ? 32.761 69.450  24.666  1.00 24.90 ? 1212 HOH A O   1 
HETATM 8684 O  O   . HOH I 8 .    ? 35.920 68.424  23.442  1.00 29.06 ? 1213 HOH A O   1 
HETATM 8685 O  O   . HOH I 8 .    ? 35.786 68.057  20.481  1.00 28.59 ? 1214 HOH A O   1 
HETATM 8686 O  O   . HOH I 8 .    ? 36.489 70.232  19.833  1.00 42.67 ? 1215 HOH A O   1 
HETATM 8687 O  O   . HOH I 8 .    ? 38.391 73.783  18.086  1.00 29.67 ? 1216 HOH A O   1 
HETATM 8688 O  O   . HOH I 8 .    ? 39.508 74.724  20.728  1.00 54.42 ? 1217 HOH A O   1 
HETATM 8689 O  O   . HOH I 8 .    ? 41.928 73.511  22.947  1.00 40.09 ? 1218 HOH A O   1 
HETATM 8690 O  O   . HOH I 8 .    ? 43.646 71.700  26.089  1.00 49.60 ? 1219 HOH A O   1 
HETATM 8691 O  O   . HOH I 8 .    ? 42.454 68.835  26.399  1.00 40.30 ? 1220 HOH A O   1 
HETATM 8692 O  O   . HOH I 8 .    ? 44.673 67.896  28.173  1.00 38.38 ? 1221 HOH A O   1 
HETATM 8693 O  O   . HOH I 8 .    ? 46.553 68.639  26.511  1.00 29.01 ? 1222 HOH A O   1 
HETATM 8694 O  O   . HOH I 8 .    ? 48.636 68.289  24.940  1.00 49.21 ? 1223 HOH A O   1 
HETATM 8695 O  O   . HOH I 8 .    ? 50.767 69.682  24.052  1.00 60.05 ? 1224 HOH A O   1 
HETATM 8696 O  O   . HOH I 8 .    ? 52.246 67.895  22.563  1.00 57.51 ? 1225 HOH A O   1 
HETATM 8697 O  O   . HOH I 8 .    ? 53.377 66.349  20.492  1.00 50.36 ? 1226 HOH A O   1 
HETATM 8698 O  O   . HOH I 8 .    ? 53.024 69.749  18.261  1.00 24.77 ? 1227 HOH A O   1 
HETATM 8699 O  O   . HOH I 8 .    ? 52.547 72.610  18.222  1.00 28.18 ? 1228 HOH A O   1 
HETATM 8700 O  O   . HOH I 8 .    ? 54.377 72.961  16.318  1.00 35.01 ? 1229 HOH A O   1 
HETATM 8701 O  O   . HOH I 8 .    ? 54.478 74.219  12.170  1.00 51.02 ? 1230 HOH A O   1 
HETATM 8702 O  O   . HOH I 8 .    ? 54.286 72.060  10.770  1.00 54.86 ? 1231 HOH A O   1 
HETATM 8703 O  O   . HOH I 8 .    ? 52.686 70.797  8.824   1.00 31.71 ? 1232 HOH A O   1 
HETATM 8704 O  O   . HOH I 8 .    ? 50.447 72.298  9.168   1.00 18.82 ? 1233 HOH A O   1 
HETATM 8705 O  O   . HOH I 8 .    ? 51.670 74.676  8.429   1.00 37.45 ? 1234 HOH A O   1 
HETATM 8706 O  O   . HOH I 8 .    ? 48.437 76.662  8.225   1.00 30.56 ? 1235 HOH A O   1 
HETATM 8707 O  O   . HOH I 8 .    ? 46.785 74.522  7.765   1.00 11.83 ? 1236 HOH A O   1 
HETATM 8708 O  O   . HOH I 8 .    ? 46.126 77.820  9.497   1.00 21.12 ? 1237 HOH A O   1 
HETATM 8709 O  O   . HOH I 8 .    ? 47.423 78.405  11.640  1.00 28.72 ? 1238 HOH A O   1 
HETATM 8710 O  O   . HOH I 8 .    ? 47.189 77.441  14.217  1.00 36.83 ? 1239 HOH A O   1 
HETATM 8711 O  O   . HOH I 8 .    ? 45.379 78.125  15.925  1.00 47.94 ? 1240 HOH A O   1 
HETATM 8712 O  O   . HOH I 8 .    ? 45.130 80.567  14.858  1.00 51.36 ? 1241 HOH A O   1 
HETATM 8713 O  O   . HOH I 8 .    ? 40.658 81.380  11.573  1.00 39.81 ? 1242 HOH A O   1 
HETATM 8714 O  O   . HOH I 8 .    ? 38.517 80.194  12.489  1.00 52.21 ? 1243 HOH A O   1 
HETATM 8715 O  O   . HOH I 8 .    ? 38.639 82.415  10.108  1.00 38.46 ? 1244 HOH A O   1 
HETATM 8716 O  O   . HOH I 8 .    ? 41.202 83.154  8.398   1.00 44.02 ? 1245 HOH A O   1 
HETATM 8717 O  O   . HOH I 8 .    ? 43.480 80.800  5.049   1.00 23.23 ? 1246 HOH A O   1 
HETATM 8718 O  O   . HOH I 8 .    ? 46.090 79.592  4.913   1.00 25.47 ? 1247 HOH A O   1 
HETATM 8719 O  O   . HOH I 8 .    ? 49.290 76.528  5.429   1.00 29.71 ? 1248 HOH A O   1 
HETATM 8720 O  O   . HOH I 8 .    ? 50.900 77.244  2.034   1.00 31.53 ? 1249 HOH A O   1 
HETATM 8721 O  O   . HOH I 8 .    ? 52.604 75.269  1.897   1.00 38.33 ? 1250 HOH A O   1 
HETATM 8722 O  O   . HOH I 8 .    ? 55.174 75.762  2.199   1.00 43.82 ? 1251 HOH A O   1 
HETATM 8723 O  O   . HOH I 8 .    ? 56.923 76.100  0.010   1.00 34.22 ? 1252 HOH A O   1 
HETATM 8724 O  O   . HOH I 8 .    ? 57.198 75.411  -2.848  1.00 28.15 ? 1253 HOH A O   1 
HETATM 8725 O  O   . HOH I 8 .    ? 59.248 77.109  -4.241  1.00 29.26 ? 1254 HOH A O   1 
HETATM 8726 O  O   . HOH I 8 .    ? 61.604 77.059  -5.120  1.00 52.60 ? 1255 HOH A O   1 
HETATM 8727 O  O   . HOH I 8 .    ? 60.451 74.918  -4.678  1.00 36.02 ? 1256 HOH A O   1 
HETATM 8728 O  O   . HOH I 8 .    ? 60.823 73.842  -0.265  1.00 52.10 ? 1257 HOH A O   1 
HETATM 8729 O  O   . HOH I 8 .    ? 60.590 72.690  2.030   1.00 42.83 ? 1258 HOH A O   1 
HETATM 8730 O  O   . HOH I 8 .    ? 59.776 71.308  0.152   1.00 34.96 ? 1259 HOH A O   1 
HETATM 8731 O  O   . HOH I 8 .    ? 59.168 70.712  2.988   1.00 47.31 ? 1260 HOH A O   1 
HETATM 8732 O  O   . HOH I 8 .    ? 59.367 68.221  2.471   1.00 22.28 ? 1261 HOH A O   1 
HETATM 8733 O  O   . HOH I 8 .    ? 56.603 66.877  5.222   1.00 30.07 ? 1262 HOH A O   1 
HETATM 8734 O  O   . HOH I 8 .    ? 55.199 68.528  3.581   1.00 33.74 ? 1263 HOH A O   1 
HETATM 8735 O  O   . HOH I 8 .    ? 53.592 69.415  2.240   1.00 38.13 ? 1264 HOH A O   1 
HETATM 8736 O  O   . HOH I 8 .    ? 51.858 69.048  3.856   1.00 31.99 ? 1265 HOH A O   1 
HETATM 8737 O  O   . HOH I 8 .    ? 49.899 67.499  4.238   1.00 17.67 ? 1266 HOH A O   1 
HETATM 8738 O  O   . HOH I 8 .    ? 49.334 68.310  6.733   1.00 26.93 ? 1267 HOH A O   1 
HETATM 8739 O  O   . HOH I 8 .    ? 51.311 66.485  8.486   1.00 24.15 ? 1268 HOH A O   1 
HETATM 8740 O  O   . HOH I 8 .    ? 53.170 68.114  9.137   1.00 30.16 ? 1269 HOH A O   1 
HETATM 8741 O  O   . HOH I 8 .    ? 53.505 66.612  7.082   1.00 41.58 ? 1270 HOH A O   1 
HETATM 8742 O  O   . HOH I 8 .    ? 55.612 67.224  10.233  1.00 43.15 ? 1271 HOH A O   1 
HETATM 8743 O  O   . HOH I 8 .    ? 55.575 67.518  13.367  1.00 31.09 ? 1272 HOH A O   1 
HETATM 8744 O  O   . HOH I 8 .    ? 57.410 69.162  13.651  1.00 32.80 ? 1273 HOH A O   1 
HETATM 8745 O  O   . HOH I 8 .    ? 59.825 68.849  16.661  1.00 53.96 ? 1274 HOH A O   1 
HETATM 8746 O  O   . HOH I 8 .    ? 57.932 69.489  19.978  1.00 40.34 ? 1275 HOH A O   1 
HETATM 8747 O  O   . HOH I 8 .    ? 57.202 67.627  22.704  1.00 44.20 ? 1276 HOH A O   1 
HETATM 8748 O  O   . HOH I 8 .    ? 57.044 64.813  24.090  1.00 30.12 ? 1277 HOH A O   1 
HETATM 8749 O  O   . HOH I 8 .    ? 59.351 62.479  25.718  1.00 35.52 ? 1278 HOH A O   1 
HETATM 8750 O  O   . HOH I 8 .    ? 62.500 62.174  25.482  1.00 33.57 ? 1279 HOH A O   1 
HETATM 8751 O  O   . HOH I 8 .    ? 63.640 57.691  25.482  1.00 44.70 ? 1280 HOH A O   1 
HETATM 8752 O  O   . HOH I 8 .    ? 62.560 55.980  27.277  1.00 48.58 ? 1281 HOH A O   1 
HETATM 8753 O  O   . HOH I 8 .    ? 59.332 55.653  27.062  1.00 32.33 ? 1282 HOH A O   1 
HETATM 8754 O  O   . HOH I 8 .    ? 58.125 52.936  26.295  1.00 45.53 ? 1283 HOH A O   1 
HETATM 8755 O  O   . HOH I 8 .    ? 55.874 52.034  27.246  1.00 33.14 ? 1284 HOH A O   1 
HETATM 8756 O  O   . HOH I 8 .    ? 56.259 49.326  27.127  1.00 43.91 ? 1285 HOH A O   1 
HETATM 8757 O  O   . HOH I 8 .    ? 58.282 48.749  25.621  1.00 48.88 ? 1286 HOH A O   1 
HETATM 8758 O  O   . HOH I 8 .    ? 59.629 50.956  24.802  1.00 35.26 ? 1287 HOH A O   1 
HETATM 8759 O  O   . HOH I 8 .    ? 58.721 51.249  22.213  1.00 25.65 ? 1288 HOH A O   1 
HETATM 8760 O  O   . HOH I 8 .    ? 57.515 49.103  21.365  1.00 25.87 ? 1289 HOH A O   1 
HETATM 8761 O  O   . HOH I 8 .    ? 56.899 47.675  23.257  1.00 44.82 ? 1290 HOH A O   1 
HETATM 8762 O  O   . HOH I 8 .    ? 54.033 46.890  23.441  1.00 33.94 ? 1291 HOH A O   1 
HETATM 8763 O  O   A HOH I 8 .    ? 51.978 50.442  27.371  0.50 18.09 ? 1292 HOH A O   1 
HETATM 8764 O  O   B HOH I 8 .    ? 52.391 49.026  25.505  0.50 21.15 ? 1292 HOH A O   1 
HETATM 8765 O  O   . HOH I 8 .    ? 49.233 49.955  28.302  1.00 17.95 ? 1293 HOH A O   1 
HETATM 8766 O  O   . HOH I 8 .    ? 50.036 47.407  29.035  1.00 26.52 ? 1294 HOH A O   1 
HETATM 8767 O  O   . HOH I 8 .    ? 47.262 45.921  26.690  1.00 30.77 ? 1295 HOH A O   1 
HETATM 8768 O  O   . HOH I 8 .    ? 46.346 43.773  28.360  1.00 38.29 ? 1296 HOH A O   1 
HETATM 8769 O  O   . HOH I 8 .    ? 47.551 43.787  30.664  1.00 45.55 ? 1297 HOH A O   1 
HETATM 8770 O  O   . HOH I 8 .    ? 44.745 45.130  32.546  1.00 38.25 ? 1298 HOH A O   1 
HETATM 8771 O  O   . HOH I 8 .    ? 42.691 46.378  32.885  1.00 42.57 ? 1299 HOH A O   1 
HETATM 8772 O  O   . HOH I 8 .    ? 42.211 48.810  31.308  1.00 22.49 ? 1300 HOH A O   1 
HETATM 8773 O  O   . HOH I 8 .    ? 41.323 50.507  33.120  1.00 22.05 ? 1301 HOH A O   1 
HETATM 8774 O  O   . HOH I 8 .    ? 39.387 49.322  30.179  1.00 20.72 ? 1302 HOH A O   1 
HETATM 8775 O  O   . HOH I 8 .    ? 37.528 47.320  29.725  1.00 18.84 ? 1303 HOH A O   1 
HETATM 8776 O  O   . HOH I 8 .    ? 37.149 45.679  27.478  1.00 13.19 ? 1304 HOH A O   1 
HETATM 8777 O  O   . HOH I 8 .    ? 39.266 43.610  26.866  1.00 29.14 ? 1305 HOH A O   1 
HETATM 8778 O  O   . HOH I 8 .    ? 39.812 45.460  25.581  1.00 28.59 ? 1306 HOH A O   1 
HETATM 8779 O  O   . HOH I 8 .    ? 39.038 43.124  22.692  1.00 27.04 ? 1307 HOH A O   1 
HETATM 8780 O  O   . HOH I 8 .    ? 39.674 39.704  20.127  1.00 27.34 ? 1308 HOH A O   1 
HETATM 8781 O  O   . HOH I 8 .    ? 38.097 38.671  21.958  1.00 34.70 ? 1309 HOH A O   1 
HETATM 8782 O  O   . HOH I 8 .    ? 34.940 38.226  22.238  1.00 44.34 ? 1310 HOH A O   1 
HETATM 8783 O  O   . HOH I 8 .    ? 34.595 35.816  23.720  1.00 49.19 ? 1311 HOH A O   1 
HETATM 8784 O  O   . HOH I 8 .    ? 32.504 34.221  25.411  1.00 47.32 ? 1312 HOH A O   1 
HETATM 8785 O  O   . HOH I 8 .    ? 30.033 30.336  24.462  1.00 44.98 ? 1313 HOH A O   1 
HETATM 8786 O  O   . HOH I 8 .    ? 29.560 31.729  21.931  1.00 29.19 ? 1314 HOH A O   1 
HETATM 8787 O  O   . HOH I 8 .    ? 31.796 33.707  17.018  1.00 31.71 ? 1315 HOH A O   1 
HETATM 8788 O  O   . HOH I 8 .    ? 34.308 34.464  16.269  1.00 20.77 ? 1316 HOH A O   1 
HETATM 8789 O  O   . HOH I 8 .    ? 33.380 35.386  18.485  1.00 65.33 ? 1317 HOH A O   1 
HETATM 8790 O  O   . HOH I 8 .    ? 36.476 33.152  17.269  1.00 41.57 ? 1318 HOH A O   1 
HETATM 8791 O  O   . HOH I 8 .    ? 32.590 31.000  15.920  1.00 49.73 ? 1319 HOH A O   1 
HETATM 8792 O  O   . HOH I 8 .    ? 36.854 29.251  13.155  1.00 32.21 ? 1320 HOH A O   1 
HETATM 8793 O  O   . HOH I 8 .    ? 39.996 35.392  11.373  1.00 23.98 ? 1321 HOH A O   1 
HETATM 8794 O  O   . HOH I 8 .    ? 40.172 39.336  9.184   1.00 28.13 ? 1322 HOH A O   1 
HETATM 8795 O  O   A HOH I 8 .    ? 44.270 41.008  7.820   0.50 19.99 ? 1323 HOH A O   1 
HETATM 8796 O  O   B HOH I 8 .    ? 42.743 39.804  7.834   0.50 25.92 ? 1323 HOH A O   1 
HETATM 8797 O  O   . HOH I 8 .    ? 41.700 43.256  7.938   1.00 15.69 ? 1324 HOH A O   1 
HETATM 8798 O  O   . HOH I 8 .    ? 44.461 46.082  10.065  1.00 12.94 ? 1325 HOH A O   1 
HETATM 8799 O  O   . HOH I 8 .    ? 45.278 44.389  12.009  1.00 40.57 ? 1326 HOH A O   1 
HETATM 8800 O  O   . HOH I 8 .    ? 46.858 46.017  11.463  1.00 31.56 ? 1327 HOH A O   1 
HETATM 8801 O  O   . HOH I 8 .    ? 48.567 44.904  10.093  1.00 37.58 ? 1328 HOH A O   1 
HETATM 8802 O  O   . HOH I 8 .    ? 46.606 43.059  9.841   1.00 33.81 ? 1329 HOH A O   1 
HETATM 8803 O  O   . HOH I 8 .    ? 49.066 41.898  8.371   1.00 25.11 ? 1330 HOH A O   1 
HETATM 8804 O  O   . HOH I 8 .    ? 50.050 44.126  7.072   1.00 16.20 ? 1331 HOH A O   1 
HETATM 8805 O  O   . HOH I 8 .    ? 49.449 44.250  4.444   1.00 15.51 ? 1332 HOH A O   1 
HETATM 8806 O  O   . HOH I 8 .    ? 51.745 44.430  3.027   1.00 22.60 ? 1333 HOH A O   1 
HETATM 8807 O  O   . HOH I 8 .    ? 51.907 46.552  1.303   1.00 12.32 ? 1334 HOH A O   1 
HETATM 8808 O  O   . HOH I 8 .    ? 49.917 48.483  1.425   1.00 10.17 ? 1335 HOH A O   1 
HETATM 8809 O  O   . HOH I 8 .    ? 47.553 46.045  3.693   1.00 11.34 ? 1336 HOH A O   1 
HETATM 8810 O  O   . HOH I 8 .    ? 48.207 41.723  3.703   1.00 18.37 ? 1337 HOH A O   1 
HETATM 8811 O  O   . HOH I 8 .    ? 47.761 39.855  1.805   1.00 48.87 ? 1338 HOH A O   1 
HETATM 8812 O  O   . HOH I 8 .    ? 49.738 41.112  1.386   1.00 35.24 ? 1339 HOH A O   1 
HETATM 8813 O  O   . HOH I 8 .    ? 48.544 40.910  -0.995  1.00 24.43 ? 1340 HOH A O   1 
HETATM 8814 O  O   . HOH I 8 .    ? 47.542 42.989  -2.342  1.00 16.14 ? 1341 HOH A O   1 
HETATM 8815 O  O   . HOH I 8 .    ? 48.040 41.724  -5.275  1.00 25.54 ? 1342 HOH A O   1 
HETATM 8816 O  O   . HOH I 8 .    ? 45.497 41.579  -5.895  1.00 33.05 ? 1343 HOH A O   1 
HETATM 8817 O  O   . HOH I 8 .    ? 43.528 41.874  -7.592  1.00 27.81 ? 1344 HOH A O   1 
HETATM 8818 O  O   . HOH I 8 .    ? 45.654 42.195  -9.037  1.00 33.66 ? 1345 HOH A O   1 
HETATM 8819 O  O   . HOH I 8 .    ? 47.987 43.967  -8.658  1.00 18.19 ? 1346 HOH A O   1 
HETATM 8820 O  O   . HOH I 8 .    ? 48.800 44.249  -6.196  1.00 13.78 ? 1347 HOH A O   1 
HETATM 8821 O  O   . HOH I 8 .    ? 51.069 44.305  -8.004  1.00 10.85 ? 1348 HOH A O   1 
HETATM 8822 O  O   . HOH I 8 .    ? 49.235 41.847  -10.568 1.00 33.38 ? 1349 HOH A O   1 
HETATM 8823 O  O   . HOH I 8 .    ? 47.314 42.027  -12.277 1.00 43.46 ? 1350 HOH A O   1 
HETATM 8824 O  O   . HOH I 8 .    ? 47.222 41.624  -14.647 1.00 30.52 ? 1351 HOH A O   1 
HETATM 8825 O  O   . HOH I 8 .    ? 51.809 41.059  -12.921 1.00 31.19 ? 1352 HOH A O   1 
HETATM 8826 O  O   . HOH I 8 .    ? 53.661 39.213  -12.093 1.00 38.31 ? 1353 HOH A O   1 
HETATM 8827 O  O   . HOH I 8 .    ? 53.424 34.186  -11.112 1.00 46.36 ? 1354 HOH A O   1 
HETATM 8828 O  O   . HOH I 8 .    ? 57.263 36.036  -14.207 1.00 38.08 ? 1355 HOH A O   1 
HETATM 8829 O  O   . HOH I 8 .    ? 58.607 34.971  -12.132 1.00 42.03 ? 1356 HOH A O   1 
HETATM 8830 O  O   . HOH I 8 .    ? 59.313 37.667  -15.354 1.00 28.44 ? 1357 HOH A O   1 
HETATM 8831 O  O   . HOH I 8 .    ? 58.051 37.441  -17.754 1.00 43.23 ? 1358 HOH A O   1 
HETATM 8832 O  O   . HOH I 8 .    ? 57.132 39.087  -19.405 1.00 42.47 ? 1359 HOH A O   1 
HETATM 8833 O  O   . HOH I 8 .    ? 57.193 43.139  -19.920 1.00 27.59 ? 1360 HOH A O   1 
HETATM 8834 O  O   . HOH I 8 .    ? 56.641 46.195  -17.348 1.00 17.40 ? 1361 HOH A O   1 
HETATM 8835 O  O   . HOH I 8 .    ? 60.873 46.943  -22.294 1.00 40.16 ? 1362 HOH A O   1 
HETATM 8836 O  O   . HOH I 8 .    ? 62.445 48.243  -20.797 1.00 40.79 ? 1363 HOH A O   1 
HETATM 8837 O  O   . HOH I 8 .    ? 64.590 49.700  -21.447 1.00 42.76 ? 1364 HOH A O   1 
HETATM 8838 O  O   . HOH I 8 .    ? 65.448 52.253  -21.828 1.00 47.96 ? 1365 HOH A O   1 
HETATM 8839 O  O   . HOH I 8 .    ? 66.654 56.243  -20.233 1.00 18.30 ? 1366 HOH A O   1 
HETATM 8840 O  O   . HOH I 8 .    ? 68.140 56.693  -22.390 1.00 35.67 ? 1367 HOH A O   1 
HETATM 8841 O  O   . HOH I 8 .    ? 70.224 55.318  -23.075 1.00 40.65 ? 1368 HOH A O   1 
HETATM 8842 O  O   . HOH I 8 .    ? 69.887 53.526  -19.601 1.00 42.20 ? 1369 HOH A O   1 
HETATM 8843 O  O   . HOH I 8 .    ? 67.754 54.823  -18.087 1.00 25.17 ? 1370 HOH A O   1 
HETATM 8844 O  O   . HOH I 8 .    ? 70.024 56.704  -17.537 1.00 49.94 ? 1371 HOH A O   1 
HETATM 8845 O  O   . HOH I 8 .    ? 69.441 59.082  -17.005 1.00 34.56 ? 1372 HOH A O   1 
HETATM 8846 O  O   . HOH I 8 .    ? 71.770 62.709  -17.862 1.00 27.26 ? 1373 HOH A O   1 
HETATM 8847 O  O   . HOH I 8 .    ? 70.333 61.886  -20.291 1.00 23.57 ? 1374 HOH A O   1 
HETATM 8848 O  O   . HOH I 8 .    ? 70.203 60.358  -23.223 1.00 36.78 ? 1375 HOH A O   1 
HETATM 8849 O  O   . HOH I 8 .    ? 69.922 62.950  -23.801 1.00 32.25 ? 1376 HOH A O   1 
HETATM 8850 O  O   . HOH I 8 .    ? 69.256 60.729  -27.283 1.00 43.97 ? 1377 HOH A O   1 
HETATM 8851 O  O   . HOH I 8 .    ? 66.926 60.030  -27.075 1.00 22.04 ? 1378 HOH A O   1 
HETATM 8852 O  O   . HOH I 8 .    ? 68.263 57.544  -26.875 1.00 47.52 ? 1379 HOH A O   1 
HETATM 8853 O  O   . HOH I 8 .    ? 67.887 56.567  -29.637 1.00 42.65 ? 1380 HOH A O   1 
HETATM 8854 O  O   . HOH I 8 .    ? 66.366 58.305  -31.112 1.00 43.76 ? 1381 HOH A O   1 
HETATM 8855 O  O   . HOH I 8 .    ? 61.428 54.115  -32.520 1.00 47.01 ? 1382 HOH A O   1 
HETATM 8856 O  O   . HOH I 8 .    ? 59.098 54.334  -33.199 1.00 35.63 ? 1383 HOH A O   1 
HETATM 8857 O  O   . HOH I 8 .    ? 59.999 52.937  -30.523 1.00 37.95 ? 1384 HOH A O   1 
HETATM 8858 O  O   . HOH I 8 .    ? 61.390 54.369  -28.863 1.00 24.35 ? 1385 HOH A O   1 
HETATM 8859 O  O   . HOH I 8 .    ? 62.547 51.886  -32.267 1.00 44.06 ? 1386 HOH A O   1 
HETATM 8860 O  O   . HOH I 8 .    ? 61.316 47.491  -26.721 1.00 54.86 ? 1387 HOH A O   1 
HETATM 8861 O  O   . HOH I 8 .    ? 58.621 44.086  -27.933 1.00 42.19 ? 1388 HOH A O   1 
HETATM 8862 O  O   . HOH I 8 .    ? 52.370 45.188  -27.009 1.00 37.44 ? 1389 HOH A O   1 
HETATM 8863 O  O   . HOH I 8 .    ? 53.337 47.153  -25.061 1.00 19.52 ? 1390 HOH A O   1 
HETATM 8864 O  O   . HOH I 8 .    ? 49.528 44.485  -21.455 1.00 33.34 ? 1391 HOH A O   1 
HETATM 8865 O  O   . HOH I 8 .    ? 46.106 40.688  -22.542 1.00 48.57 ? 1392 HOH A O   1 
HETATM 8866 O  O   . HOH I 8 .    ? 43.414 40.530  -22.893 1.00 36.26 ? 1393 HOH A O   1 
HETATM 8867 O  O   . HOH I 8 .    ? 43.498 42.753  -24.691 1.00 39.25 ? 1394 HOH A O   1 
HETATM 8868 O  O   . HOH I 8 .    ? 45.363 41.478  -26.168 1.00 57.02 ? 1395 HOH A O   1 
HETATM 8869 O  O   . HOH I 8 .    ? 41.506 44.668  -24.261 1.00 22.66 ? 1396 HOH A O   1 
HETATM 8870 O  O   . HOH I 8 .    ? 42.220 47.259  -24.466 1.00 15.75 ? 1397 HOH A O   1 
HETATM 8871 O  O   . HOH I 8 .    ? 43.231 46.168  -22.566 1.00 41.07 ? 1398 HOH A O   1 
HETATM 8872 O  O   . HOH I 8 .    ? 42.656 47.477  -27.165 1.00 31.48 ? 1399 HOH A O   1 
HETATM 8873 O  O   . HOH I 8 .    ? 40.934 48.092  -29.144 1.00 39.80 ? 1400 HOH A O   1 
HETATM 8874 O  O   . HOH I 8 .    ? 39.475 48.645  -32.808 1.00 24.97 ? 1401 HOH A O   1 
HETATM 8875 O  O   . HOH I 8 .    ? 38.740 45.087  -33.526 1.00 24.62 ? 1402 HOH A O   1 
HETATM 8876 O  O   . HOH I 8 .    ? 38.454 46.576  -39.977 1.00 41.65 ? 1403 HOH A O   1 
HETATM 8877 O  O   . HOH I 8 .    ? 31.778 51.072  -35.399 1.00 21.88 ? 1404 HOH A O   1 
HETATM 8878 O  O   . HOH I 8 .    ? 34.691 53.542  -33.135 1.00 37.02 ? 1405 HOH A O   1 
HETATM 8879 O  O   . HOH I 8 .    ? 35.630 55.458  -34.677 1.00 44.59 ? 1406 HOH A O   1 
HETATM 8880 O  O   . HOH I 8 .    ? 33.574 56.979  -35.909 1.00 18.39 ? 1407 HOH A O   1 
HETATM 8881 O  O   . HOH I 8 .    ? 34.769 59.380  -34.928 1.00 21.98 ? 1408 HOH A O   1 
HETATM 8882 O  O   . HOH I 8 .    ? 37.104 58.951  -33.355 1.00 29.07 ? 1409 HOH A O   1 
HETATM 8883 O  O   . HOH I 8 .    ? 37.711 61.350  -32.421 1.00 28.14 ? 1410 HOH A O   1 
HETATM 8884 O  O   . HOH I 8 .    ? 36.115 63.383  -33.870 1.00 37.45 ? 1411 HOH A O   1 
HETATM 8885 O  O   . HOH I 8 .    ? 34.056 64.366  -32.265 1.00 15.93 ? 1412 HOH A O   1 
HETATM 8886 O  O   . HOH I 8 .    ? 36.451 62.623  -38.434 1.00 34.06 ? 1413 HOH A O   1 
HETATM 8887 O  O   . HOH I 8 .    ? 37.188 63.071  -42.056 1.00 39.38 ? 1414 HOH A O   1 
HETATM 8888 O  O   . HOH I 8 .    ? 36.664 63.027  -45.380 1.00 58.76 ? 1415 HOH A O   1 
HETATM 8889 O  O   . HOH I 8 .    ? 34.627 65.986  -42.445 1.00 37.89 ? 1416 HOH A O   1 
HETATM 8890 O  O   . HOH I 8 .    ? 34.263 70.341  -44.808 1.00 45.31 ? 1417 HOH A O   1 
HETATM 8891 O  O   . HOH I 8 .    ? 30.984 69.221  -45.465 1.00 44.24 ? 1418 HOH A O   1 
HETATM 8892 O  O   . HOH I 8 .    ? 30.102 71.409  -44.764 1.00 48.66 ? 1419 HOH A O   1 
HETATM 8893 O  O   . HOH I 8 .    ? 29.048 72.065  -41.973 1.00 36.21 ? 1420 HOH A O   1 
HETATM 8894 O  O   . HOH I 8 .    ? 28.882 69.747  -39.529 1.00 24.24 ? 1421 HOH A O   1 
HETATM 8895 O  O   . HOH I 8 .    ? 24.785 71.550  -39.841 1.00 27.84 ? 1422 HOH A O   1 
HETATM 8896 O  O   . HOH I 8 .    ? 25.956 76.213  -38.977 1.00 32.35 ? 1423 HOH A O   1 
HETATM 8897 O  O   . HOH I 8 .    ? 27.367 76.377  -41.322 1.00 44.93 ? 1424 HOH A O   1 
HETATM 8898 O  O   . HOH I 8 .    ? 28.865 77.808  -43.424 1.00 51.63 ? 1425 HOH A O   1 
HETATM 8899 O  O   . HOH I 8 .    ? 31.320 79.000  -42.842 1.00 29.03 ? 1426 HOH A O   1 
HETATM 8900 O  O   . HOH I 8 .    ? 29.595 81.344  -42.943 1.00 38.55 ? 1427 HOH A O   1 
HETATM 8901 O  O   . HOH I 8 .    ? 26.134 81.585  -42.619 1.00 35.01 ? 1428 HOH A O   1 
HETATM 8902 O  O   . HOH I 8 .    ? 25.243 84.505  -44.095 1.00 41.88 ? 1429 HOH A O   1 
HETATM 8903 O  O   . HOH I 8 .    ? 23.557 84.870  -41.966 1.00 41.81 ? 1430 HOH A O   1 
HETATM 8904 O  O   . HOH I 8 .    ? 24.072 87.305  -40.970 1.00 40.25 ? 1431 HOH A O   1 
HETATM 8905 O  O   . HOH I 8 .    ? 25.947 87.504  -42.867 1.00 38.65 ? 1432 HOH A O   1 
HETATM 8906 O  O   . HOH I 8 .    ? 28.288 87.772  -41.741 1.00 27.78 ? 1433 HOH A O   1 
HETATM 8907 O  O   . HOH I 8 .    ? 28.440 90.446  -42.707 1.00 27.71 ? 1434 HOH A O   1 
HETATM 8908 O  O   . HOH I 8 .    ? 32.620 89.067  -43.198 1.00 27.28 ? 1435 HOH A O   1 
HETATM 8909 O  O   . HOH I 8 .    ? 34.148 86.806  -43.647 1.00 41.61 ? 1436 HOH A O   1 
HETATM 8910 O  O   . HOH I 8 .    ? 39.140 86.458  -41.645 1.00 28.12 ? 1437 HOH A O   1 
HETATM 8911 O  O   . HOH I 8 .    ? 41.042 86.671  -44.012 1.00 47.28 ? 1438 HOH A O   1 
HETATM 8912 O  O   . HOH I 8 .    ? 42.205 87.662  -41.015 1.00 14.69 ? 1439 HOH A O   1 
HETATM 8913 O  O   . HOH I 8 .    ? 43.710 88.335  -38.716 1.00 15.42 ? 1440 HOH A O   1 
HETATM 8914 O  O   . HOH I 8 .    ? 43.458 93.752  -37.738 1.00 22.89 ? 1441 HOH A O   1 
HETATM 8915 O  O   . HOH I 8 .    ? 41.293 94.798  -39.484 1.00 26.59 ? 1442 HOH A O   1 
HETATM 8916 O  O   . HOH I 8 .    ? 40.741 96.322  -37.406 1.00 25.44 ? 1443 HOH A O   1 
HETATM 8917 O  O   . HOH I 8 .    ? 43.203 98.057  -37.218 1.00 34.16 ? 1444 HOH A O   1 
HETATM 8918 O  O   . HOH I 8 .    ? 46.746 95.526  -37.164 1.00 42.18 ? 1445 HOH A O   1 
HETATM 8919 O  O   . HOH I 8 .    ? 48.588 93.957  -37.603 1.00 47.38 ? 1446 HOH A O   1 
HETATM 8920 O  O   . HOH I 8 .    ? 48.305 93.338  -42.812 1.00 57.70 ? 1447 HOH A O   1 
HETATM 8921 O  O   . HOH I 8 .    ? 45.342 91.480  -44.221 1.00 40.56 ? 1448 HOH A O   1 
HETATM 8922 O  O   . HOH I 8 .    ? 46.079 97.001  -43.898 1.00 24.74 ? 1449 HOH A O   1 
HETATM 8923 O  O   . HOH I 8 .    ? 42.274 96.317  -41.907 1.00 38.84 ? 1450 HOH A O   1 
HETATM 8924 O  O   . HOH I 8 .    ? 44.775 101.626 -33.051 1.00 43.35 ? 1451 HOH A O   1 
HETATM 8925 O  O   . HOH I 8 .    ? 47.101 99.779  -31.925 1.00 32.35 ? 1452 HOH A O   1 
HETATM 8926 O  O   . HOH I 8 .    ? 48.747 97.877  -33.555 1.00 27.39 ? 1453 HOH A O   1 
HETATM 8927 O  O   A HOH I 8 .    ? 52.397 98.523  -27.903 0.50 18.41 ? 1454 HOH A O   1 
HETATM 8928 O  O   B HOH I 8 .    ? 51.178 98.560  -29.448 0.50 21.93 ? 1454 HOH A O   1 
HETATM 8929 O  O   . HOH I 8 .    ? 48.642 95.254  -26.890 1.00 24.97 ? 1455 HOH A O   1 
HETATM 8930 O  O   . HOH I 8 .    ? 49.639 94.470  -24.635 1.00 39.46 ? 1456 HOH A O   1 
HETATM 8931 O  O   . HOH I 8 .    ? 49.275 91.837  -24.446 1.00 30.19 ? 1457 HOH A O   1 
HETATM 8932 O  O   . HOH I 8 .    ? 50.946 90.846  -21.690 1.00 45.92 ? 1458 HOH A O   1 
HETATM 8933 O  O   . HOH I 8 .    ? 52.770 92.012  -23.459 1.00 32.32 ? 1459 HOH A O   1 
HETATM 8934 O  O   . HOH I 8 .    ? 55.013 90.213  -23.579 1.00 26.56 ? 1460 HOH A O   1 
HETATM 8935 O  O   . HOH I 8 .    ? 56.351 90.959  -25.785 1.00 23.68 ? 1461 HOH A O   1 
HETATM 8936 O  O   . HOH I 8 .    ? 56.407 92.771  -29.514 1.00 26.54 ? 1462 HOH A O   1 
HETATM 8937 O  O   . HOH I 8 .    ? 55.292 93.380  -31.640 1.00 35.81 ? 1463 HOH A O   1 
HETATM 8938 O  O   . HOH I 8 .    ? 53.800 94.076  -33.306 1.00 33.05 ? 1464 HOH A O   1 
HETATM 8939 O  O   . HOH I 8 .    ? 58.021 94.729  -32.503 1.00 45.74 ? 1465 HOH A O   1 
HETATM 8940 O  O   . HOH I 8 .    ? 58.885 92.405  -32.064 1.00 34.64 ? 1466 HOH A O   1 
HETATM 8941 O  O   . HOH I 8 .    ? 60.423 91.088  -30.920 1.00 32.78 ? 1467 HOH A O   1 
HETATM 8942 O  O   . HOH I 8 .    ? 60.501 91.914  -28.622 1.00 32.92 ? 1468 HOH A O   1 
HETATM 8943 O  O   . HOH I 8 .    ? 61.604 92.417  -33.959 1.00 31.31 ? 1469 HOH A O   1 
HETATM 8944 O  O   . HOH I 8 .    ? 64.107 92.260  -34.146 1.00 25.81 ? 1470 HOH A O   1 
HETATM 8945 O  O   . HOH I 8 .    ? 64.306 90.713  -36.387 1.00 39.90 ? 1471 HOH A O   1 
HETATM 8946 O  O   . HOH I 8 .    ? 61.506 90.828  -37.058 1.00 34.50 ? 1472 HOH A O   1 
HETATM 8947 O  O   . HOH I 8 .    ? 59.663 91.119  -35.386 1.00 24.25 ? 1473 HOH A O   1 
HETATM 8948 O  O   . HOH I 8 .    ? 60.592 94.935  -35.210 1.00 47.18 ? 1474 HOH A O   1 
HETATM 8949 O  O   . HOH I 8 .    ? 65.191 94.167  -35.981 1.00 43.32 ? 1475 HOH A O   1 
HETATM 8950 O  O   . HOH I 8 .    ? 66.185 96.774  -35.651 1.00 41.85 ? 1476 HOH A O   1 
HETATM 8951 O  O   . HOH I 8 .    ? 69.897 98.519  -36.415 1.00 50.06 ? 1477 HOH A O   1 
HETATM 8952 O  O   . HOH I 8 .    ? 70.654 95.478  -35.133 1.00 46.43 ? 1478 HOH A O   1 
HETATM 8953 O  O   . HOH I 8 .    ? 72.422 95.701  -31.266 1.00 32.49 ? 1479 HOH A O   1 
HETATM 8954 O  O   . HOH I 8 .    ? 70.392 88.411  -35.705 1.00 42.66 ? 1480 HOH A O   1 
HETATM 8955 O  O   . HOH I 8 .    ? 68.023 88.183  -35.132 1.00 33.24 ? 1481 HOH A O   1 
HETATM 8956 O  O   . HOH I 8 .    ? 67.413 85.565  -36.016 1.00 35.50 ? 1482 HOH A O   1 
HETATM 8957 O  O   . HOH I 8 .    ? 69.386 83.889  -36.003 1.00 25.98 ? 1483 HOH A O   1 
HETATM 8958 O  O   . HOH I 8 .    ? 69.894 81.981  -33.844 1.00 35.97 ? 1484 HOH A O   1 
HETATM 8959 O  O   . HOH I 8 .    ? 68.426 79.659  -34.724 1.00 28.27 ? 1485 HOH A O   1 
HETATM 8960 O  O   . HOH I 8 .    ? 68.680 79.631  -37.403 1.00 40.32 ? 1486 HOH A O   1 
HETATM 8961 O  O   . HOH I 8 .    ? 67.610 77.256  -38.679 1.00 40.33 ? 1487 HOH A O   1 
HETATM 8962 O  O   . HOH I 8 .    ? 69.980 77.086  -38.022 1.00 38.73 ? 1488 HOH A O   1 
HETATM 8963 O  O   . HOH I 8 .    ? 71.516 76.554  -35.771 1.00 43.45 ? 1489 HOH A O   1 
HETATM 8964 O  O   . HOH I 8 .    ? 69.309 77.046  -34.196 1.00 30.47 ? 1490 HOH A O   1 
HETATM 8965 O  O   . HOH I 8 .    ? 68.075 75.076  -35.090 1.00 30.67 ? 1491 HOH A O   1 
HETATM 8966 O  O   . HOH I 8 .    ? 71.215 72.197  -34.078 1.00 38.25 ? 1492 HOH A O   1 
HETATM 8967 O  O   . HOH I 8 .    ? 71.826 73.875  -29.110 1.00 27.91 ? 1493 HOH A O   1 
HETATM 8968 O  O   . HOH I 8 .    ? 72.681 76.031  -27.122 1.00 37.93 ? 1494 HOH A O   1 
HETATM 8969 O  O   . HOH I 8 .    ? 75.534 76.627  -27.254 1.00 45.90 ? 1495 HOH A O   1 
HETATM 8970 O  O   . HOH I 8 .    ? 76.708 74.153  -26.685 1.00 32.67 ? 1496 HOH A O   1 
HETATM 8971 O  O   . HOH I 8 .    ? 74.819 77.459  -20.680 1.00 36.54 ? 1497 HOH A O   1 
HETATM 8972 O  O   . HOH I 8 .    ? 73.291 76.731  -18.349 1.00 27.71 ? 1498 HOH A O   1 
HETATM 8973 O  O   . HOH I 8 .    ? 74.319 78.191  -16.397 1.00 43.66 ? 1499 HOH A O   1 
HETATM 8974 O  O   . HOH I 8 .    ? 74.913 76.262  -14.241 1.00 25.45 ? 1500 HOH A O   1 
HETATM 8975 O  O   . HOH I 8 .    ? 75.598 73.873  -16.111 1.00 28.81 ? 1501 HOH A O   1 
HETATM 8976 O  O   . HOH I 8 .    ? 77.767 75.372  -17.262 1.00 34.33 ? 1502 HOH A O   1 
HETATM 8977 O  O   . HOH I 8 .    ? 79.977 73.809  -17.659 1.00 29.09 ? 1503 HOH A O   1 
HETATM 8978 O  O   . HOH I 8 .    ? 75.533 74.125  -19.346 1.00 23.93 ? 1504 HOH A O   1 
HETATM 8979 O  O   . HOH I 8 .    ? 77.636 75.866  -11.763 1.00 41.21 ? 1505 HOH A O   1 
HETATM 8980 O  O   . HOH I 8 .    ? 78.231 72.267  -10.129 1.00 31.86 ? 1506 HOH A O   1 
HETATM 8981 O  O   . HOH I 8 .    ? 78.785 68.982  -11.992 1.00 22.99 ? 1507 HOH A O   1 
HETATM 8982 O  O   . HOH I 8 .    ? 77.734 66.453  -11.812 1.00 33.07 ? 1508 HOH A O   1 
HETATM 8983 O  O   . HOH I 8 .    ? 77.651 65.174  -14.686 1.00 24.64 ? 1509 HOH A O   1 
HETATM 8984 O  O   . HOH I 8 .    ? 75.319 64.156  -16.234 1.00 33.71 ? 1510 HOH A O   1 
HETATM 8985 O  O   . HOH I 8 .    ? 74.619 63.517  -13.894 1.00 35.15 ? 1511 HOH A O   1 
HETATM 8986 O  O   . HOH I 8 .    ? 74.701 61.010  -13.159 1.00 42.44 ? 1512 HOH A O   1 
HETATM 8987 O  O   . HOH I 8 .    ? 74.316 60.014  -9.560  1.00 34.80 ? 1513 HOH A O   1 
HETATM 8988 O  O   . HOH I 8 .    ? 72.249 58.818  -11.173 1.00 25.94 ? 1514 HOH A O   1 
HETATM 8989 O  O   . HOH I 8 .    ? 70.272 56.402  -12.414 1.00 35.79 ? 1515 HOH A O   1 
HETATM 8990 O  O   . HOH I 8 .    ? 71.370 54.470  -13.780 1.00 33.51 ? 1516 HOH A O   1 
HETATM 8991 O  O   . HOH I 8 .    ? 74.005 53.864  -13.745 1.00 44.99 ? 1517 HOH A O   1 
HETATM 8992 O  O   . HOH I 8 .    ? 75.374 52.449  -15.687 1.00 40.71 ? 1518 HOH A O   1 
HETATM 8993 O  O   . HOH I 8 .    ? 74.495 53.149  -18.119 1.00 46.00 ? 1519 HOH A O   1 
HETATM 8994 O  O   . HOH I 8 .    ? 76.166 50.038  -16.829 1.00 44.97 ? 1520 HOH A O   1 
HETATM 8995 O  O   . HOH I 8 .    ? 74.488 48.932  -18.508 1.00 43.71 ? 1521 HOH A O   1 
HETATM 8996 O  O   . HOH I 8 .    ? 72.215 47.328  -17.772 1.00 35.29 ? 1522 HOH A O   1 
HETATM 8997 O  O   . HOH I 8 .    ? 70.696 45.497  -16.898 1.00 44.12 ? 1523 HOH A O   1 
HETATM 8998 O  O   . HOH I 8 .    ? 68.720 46.976  -16.558 1.00 31.19 ? 1524 HOH A O   1 
HETATM 8999 O  O   . HOH I 8 .    ? 71.136 43.193  -15.409 1.00 32.49 ? 1525 HOH A O   1 
HETATM 9000 O  O   . HOH I 8 .    ? 69.164 41.802  -17.314 1.00 33.31 ? 1526 HOH A O   1 
HETATM 9001 O  O   . HOH I 8 .    ? 74.678 44.333  -14.187 1.00 47.83 ? 1527 HOH A O   1 
HETATM 9002 O  O   . HOH I 8 .    ? 73.039 43.937  -12.087 1.00 42.22 ? 1528 HOH A O   1 
HETATM 9003 O  O   . HOH I 8 .    ? 76.562 47.023  -11.522 1.00 33.90 ? 1529 HOH A O   1 
HETATM 9004 O  O   . HOH I 8 .    ? 75.602 48.316  -5.420  1.00 52.14 ? 1530 HOH A O   1 
HETATM 9005 O  O   . HOH I 8 .    ? 73.664 46.323  -5.022  1.00 35.14 ? 1531 HOH A O   1 
HETATM 9006 O  O   . HOH I 8 .    ? 71.037 49.541  -0.061  1.00 25.26 ? 1532 HOH A O   1 
HETATM 9007 O  O   . HOH I 8 .    ? 72.247 47.823  1.214   1.00 43.05 ? 1533 HOH A O   1 
HETATM 9008 O  O   . HOH I 8 .    ? 72.822 50.540  1.432   1.00 43.25 ? 1534 HOH A O   1 
HETATM 9009 O  O   . HOH I 8 .    ? 74.363 52.330  1.755   1.00 33.43 ? 1535 HOH A O   1 
HETATM 9010 O  O   . HOH I 8 .    ? 76.721 51.238  2.629   1.00 50.85 ? 1536 HOH A O   1 
HETATM 9011 O  O   . HOH I 8 .    ? 79.825 51.501  -0.300  1.00 25.88 ? 1537 HOH A O   1 
HETATM 9012 O  O   . HOH I 8 .    ? 77.073 52.910  -7.359  1.00 38.05 ? 1538 HOH A O   1 
HETATM 9013 O  O   . HOH I 8 .    ? 76.717 54.087  -10.072 1.00 26.39 ? 1539 HOH A O   1 
HETATM 9014 O  O   . HOH I 8 .    ? 78.590 53.737  -12.017 1.00 35.27 ? 1540 HOH A O   1 
HETATM 9015 O  O   . HOH I 8 .    ? 78.581 53.008  -15.060 1.00 49.77 ? 1541 HOH A O   1 
HETATM 9016 O  O   . HOH I 8 .    ? 10.606 57.900  -20.903 1.00 42.54 ? 1542 HOH A O   1 
HETATM 9017 O  O   . HOH I 8 .    ? 9.688  60.380  -20.342 1.00 28.75 ? 1543 HOH A O   1 
HETATM 9018 O  O   . HOH I 8 .    ? 80.464 64.126  -21.287 1.00 22.63 ? 1544 HOH A O   1 
HETATM 9019 O  O   . HOH I 8 .    ? 80.724 63.577  -16.722 1.00 26.83 ? 1545 HOH A O   1 
HETATM 9020 O  O   . HOH I 8 .    ? 79.638 67.839  -15.099 1.00 37.41 ? 1546 HOH A O   1 
HETATM 9021 O  O   . HOH I 8 .    ? 84.453 68.268  -17.212 1.00 17.44 ? 1547 HOH A O   1 
HETATM 9022 O  O   . HOH I 8 .    ? 83.733 70.075  -20.057 1.00 27.12 ? 1548 HOH A O   1 
HETATM 9023 O  O   . HOH I 8 .    ? 83.582 70.386  -22.863 1.00 26.43 ? 1549 HOH A O   1 
HETATM 9024 O  O   . HOH I 8 .    ? 82.272 69.892  -25.206 1.00 38.94 ? 1550 HOH A O   1 
HETATM 9025 O  O   . HOH I 8 .    ? 84.347 68.472  -27.173 1.00 39.22 ? 1551 HOH A O   1 
HETATM 9026 O  O   . HOH I 8 .    ? 83.921 66.072  -24.985 1.00 43.16 ? 1552 HOH A O   1 
HETATM 9027 O  O   . HOH I 8 .    ? 83.656 67.450  -22.868 1.00 28.40 ? 1553 HOH A O   1 
HETATM 9028 O  O   . HOH I 8 .    ? 74.038 65.998  -17.527 1.00 17.24 ? 1554 HOH A O   1 
HETATM 9029 O  O   . HOH I 8 .    ? 72.904 64.144  -20.972 1.00 28.92 ? 1555 HOH A O   1 
HETATM 9030 O  O   . HOH I 8 .    ? 31.264 46.169  41.840  1.00 32.63 ? 1556 HOH A O   1 
HETATM 9031 O  O   . HOH I 8 .    ? 68.062 58.770  -24.071 1.00 19.17 ? 1557 HOH A O   1 
HETATM 9032 O  O   . HOH I 8 .    ? 60.529 61.008  -18.074 1.00 10.13 ? 1558 HOH A O   1 
HETATM 9033 O  O   . HOH I 8 .    ? 53.743 64.840  -19.803 1.00 8.91  ? 1559 HOH A O   1 
HETATM 9034 O  O   . HOH I 8 .    ? 51.801 69.939  -18.535 1.00 34.37 ? 1560 HOH A O   1 
HETATM 9035 O  O   . HOH I 8 .    ? 51.378 71.513  -20.335 1.00 20.87 ? 1561 HOH A O   1 
HETATM 9036 O  O   . HOH I 8 .    ? 53.645 72.642  -19.224 1.00 14.64 ? 1562 HOH A O   1 
HETATM 9037 O  O   . HOH I 8 .    ? 50.088 73.584  -21.707 1.00 29.24 ? 1563 HOH A O   1 
HETATM 9038 O  O   . HOH I 8 .    ? 48.472 71.764  -22.345 1.00 34.12 ? 1564 HOH A O   1 
HETATM 9039 O  O   . HOH I 8 .    ? 47.511 71.882  -19.967 1.00 33.17 ? 1565 HOH A O   1 
HETATM 9040 O  O   . HOH I 8 .    ? 45.906 70.729  -18.580 1.00 34.30 ? 1566 HOH A O   1 
HETATM 9041 O  O   . HOH I 8 .    ? 46.888 72.510  -17.442 1.00 28.93 ? 1567 HOH A O   1 
HETATM 9042 O  O   . HOH I 8 .    ? 49.630 70.905  -17.659 1.00 34.62 ? 1568 HOH A O   1 
HETATM 9043 O  O   . HOH I 8 .    ? 48.927 69.390  -15.505 1.00 25.70 ? 1569 HOH A O   1 
HETATM 9044 O  O   . HOH I 8 .    ? 46.510 67.644  -15.602 1.00 14.76 ? 1570 HOH A O   1 
HETATM 9045 O  O   . HOH I 8 .    ? 45.054 69.021  -17.156 1.00 21.33 ? 1571 HOH A O   1 
HETATM 9046 O  O   . HOH I 8 .    ? 42.233 75.275  -16.026 1.00 12.72 ? 1572 HOH A O   1 
HETATM 9047 O  O   . HOH I 8 .    ? 41.335 77.598  -14.097 1.00 12.78 ? 1573 HOH A O   1 
HETATM 9048 O  O   . HOH I 8 .    ? 40.382 82.825  -10.677 1.00 15.93 ? 1574 HOH A O   1 
HETATM 9049 O  O   . HOH I 8 .    ? 42.983 82.308  -9.950  1.00 24.68 ? 1575 HOH A O   1 
HETATM 9050 O  O   . HOH I 8 .    ? 43.883 83.190  -7.850  1.00 44.94 ? 1576 HOH A O   1 
HETATM 9051 O  O   . HOH I 8 .    ? 44.921 84.265  -10.672 1.00 45.25 ? 1577 HOH A O   1 
HETATM 9052 O  O   . HOH I 8 .    ? 47.548 81.134  -9.277  1.00 61.00 ? 1578 HOH A O   1 
HETATM 9053 O  O   . HOH I 8 .    ? 45.770 79.228  -7.962  1.00 23.41 ? 1579 HOH A O   1 
HETATM 9054 O  O   . HOH I 8 .    ? 48.397 78.057  -9.721  1.00 27.36 ? 1580 HOH A O   1 
HETATM 9055 O  O   . HOH I 8 .    ? 49.968 79.937  -11.139 1.00 41.79 ? 1581 HOH A O   1 
HETATM 9056 O  O   . HOH I 8 .    ? 50.583 79.125  -15.670 1.00 25.83 ? 1582 HOH A O   1 
HETATM 9057 O  O   . HOH I 8 .    ? 52.524 79.100  -17.609 1.00 20.13 ? 1583 HOH A O   1 
HETATM 9058 O  O   . HOH I 8 .    ? 55.115 80.579  -19.362 1.00 26.10 ? 1584 HOH A O   1 
HETATM 9059 O  O   . HOH I 8 .    ? 57.378 80.208  -18.095 1.00 32.04 ? 1585 HOH A O   1 
HETATM 9060 O  O   . HOH I 8 .    ? 56.266 78.844  -14.622 1.00 27.22 ? 1586 HOH A O   1 
HETATM 9061 O  O   . HOH I 8 .    ? 57.066 80.071  -11.061 1.00 40.60 ? 1587 HOH A O   1 
HETATM 9062 O  O   . HOH I 8 .    ? 57.324 80.446  -8.425  1.00 46.73 ? 1588 HOH A O   1 
HETATM 9063 O  O   . HOH I 8 .    ? 59.393 78.925  -7.764  1.00 38.19 ? 1589 HOH A O   1 
HETATM 9064 O  O   . HOH I 8 .    ? 59.627 76.524  -8.969  1.00 14.89 ? 1590 HOH A O   1 
HETATM 9065 O  O   . HOH I 8 .    ? 61.917 76.341  -10.487 1.00 17.12 ? 1591 HOH A O   1 
HETATM 9066 O  O   . HOH I 8 .    ? 61.437 77.522  -12.880 1.00 19.22 ? 1592 HOH A O   1 
HETATM 9067 O  O   . HOH I 8 .    ? 60.784 79.996  -11.972 1.00 38.07 ? 1593 HOH A O   1 
HETATM 9068 O  O   . HOH I 8 .    ? 60.950 80.555  -9.268  1.00 46.29 ? 1594 HOH A O   1 
HETATM 9069 O  O   . HOH I 8 .    ? 62.785 79.044  -6.542  1.00 48.22 ? 1595 HOH A O   1 
HETATM 9070 O  O   . HOH I 8 .    ? 65.374 78.845  -5.828  1.00 28.04 ? 1596 HOH A O   1 
HETATM 9071 O  O   . HOH I 8 .    ? 65.540 76.677  -3.499  1.00 38.08 ? 1597 HOH A O   1 
HETATM 9072 O  O   . HOH I 8 .    ? 66.879 74.375  -4.371  1.00 26.49 ? 1598 HOH A O   1 
HETATM 9073 O  O   . HOH I 8 .    ? 69.533 73.880  -3.320  1.00 47.18 ? 1599 HOH A O   1 
HETATM 9074 O  O   . HOH I 8 .    ? 73.749 74.058  -5.718  1.00 24.80 ? 1600 HOH A O   1 
HETATM 9075 O  O   . HOH I 8 .    ? 75.351 76.238  -6.022  1.00 50.15 ? 1601 HOH A O   1 
HETATM 9076 O  O   . HOH I 8 .    ? 72.089 80.750  -4.596  1.00 43.55 ? 1602 HOH A O   1 
HETATM 9077 O  O   . HOH I 8 .    ? 70.762 79.050  -2.802  1.00 38.55 ? 1603 HOH A O   1 
HETATM 9078 O  O   . HOH I 8 .    ? 64.538 77.403  0.358   1.00 33.19 ? 1604 HOH A O   1 
HETATM 9079 O  O   . HOH I 8 .    ? 64.169 70.710  -5.271  1.00 16.08 ? 1605 HOH A O   1 
HETATM 9080 O  O   . HOH I 8 .    ? 66.454 71.508  -6.766  1.00 19.39 ? 1606 HOH A O   1 
HETATM 9081 O  O   . HOH I 8 .    ? 68.004 65.542  -3.375  1.00 15.02 ? 1607 HOH A O   1 
HETATM 9082 O  O   . HOH I 8 .    ? 65.920 66.183  -0.375  1.00 25.05 ? 1608 HOH A O   1 
HETATM 9083 O  O   . HOH I 8 .    ? 68.039 67.031  1.098   1.00 38.08 ? 1609 HOH A O   1 
HETATM 9084 O  O   . HOH I 8 .    ? 66.397 68.603  2.009   1.00 34.86 ? 1610 HOH A O   1 
HETATM 9085 O  O   . HOH I 8 .    ? 69.277 63.762  1.827   1.00 45.33 ? 1611 HOH A O   1 
HETATM 9086 O  O   . HOH I 8 .    ? 70.451 62.016  0.090   1.00 37.21 ? 1612 HOH A O   1 
HETATM 9087 O  O   . HOH I 8 .    ? 71.305 59.774  1.103   1.00 36.02 ? 1613 HOH A O   1 
HETATM 9088 O  O   . HOH I 8 .    ? 73.518 62.893  -0.793  1.00 42.61 ? 1614 HOH A O   1 
HETATM 9089 O  O   . HOH I 8 .    ? 69.243 61.424  -2.351  1.00 16.31 ? 1615 HOH A O   1 
HETATM 9090 O  O   . HOH I 8 .    ? 67.566 60.701  -5.632  1.00 12.46 ? 1616 HOH A O   1 
HETATM 9091 O  O   . HOH I 8 .    ? 65.724 60.332  -7.663  1.00 10.24 ? 1617 HOH A O   1 
HETATM 9092 O  O   . HOH I 8 .    ? 63.210 61.325  -7.553  1.00 9.30  ? 1618 HOH A O   1 
HETATM 9093 O  O   . HOH I 8 .    ? 63.159 61.124  -4.812  1.00 14.37 ? 1619 HOH A O   1 
HETATM 9094 O  O   . HOH I 8 .    ? 60.711 60.890  -3.578  1.00 12.67 ? 1620 HOH A O   1 
HETATM 9095 O  O   . HOH I 8 .    ? 60.585 62.262  -1.271  1.00 12.33 ? 1621 HOH A O   1 
HETATM 9096 O  O   . HOH I 8 .    ? 62.207 60.794  0.526   1.00 29.80 ? 1622 HOH A O   1 
HETATM 9097 O  O   . HOH I 8 .    ? 63.239 58.685  -1.367  1.00 15.90 ? 1623 HOH A O   1 
HETATM 9098 O  O   . HOH I 8 .    ? 63.768 57.146  0.844   1.00 28.85 ? 1624 HOH A O   1 
HETATM 9099 O  O   . HOH I 8 .    ? 61.036 56.163  2.067   1.00 33.27 ? 1625 HOH A O   1 
HETATM 9100 O  O   . HOH I 8 .    ? 59.649 57.617  3.363   1.00 33.30 ? 1626 HOH A O   1 
HETATM 9101 O  O   . HOH I 8 .    ? 59.062 58.218  0.981   1.00 25.35 ? 1627 HOH A O   1 
HETATM 9102 O  O   . HOH I 8 .    ? 56.491 58.548  1.365   1.00 27.40 ? 1628 HOH A O   1 
HETATM 9103 O  O   . HOH I 8 .    ? 55.073 57.638  -0.476  1.00 15.52 ? 1629 HOH A O   1 
HETATM 9104 O  O   . HOH I 8 .    ? 56.419 55.805  -2.118  1.00 10.74 ? 1630 HOH A O   1 
HETATM 9105 O  O   . HOH I 8 .    ? 58.927 56.788  -1.380  1.00 12.56 ? 1631 HOH A O   1 
HETATM 9106 O  O   . HOH I 8 .    ? 60.806 58.290  -2.774  1.00 12.21 ? 1632 HOH A O   1 
HETATM 9107 O  O   . HOH I 8 .    ? 60.582 54.835  -0.276  1.00 14.63 ? 1633 HOH A O   1 
HETATM 9108 O  O   . HOH I 8 .    ? 58.806 52.674  -0.084  1.00 13.61 ? 1634 HOH A O   1 
HETATM 9109 O  O   . HOH I 8 .    ? 59.337 50.075  -0.631  1.00 16.76 ? 1635 HOH A O   1 
HETATM 9110 O  O   . HOH I 8 .    ? 59.473 49.030  2.306   1.00 39.85 ? 1636 HOH A O   1 
HETATM 9111 O  O   . HOH I 8 .    ? 59.410 52.068  2.620   1.00 28.96 ? 1637 HOH A O   1 
HETATM 9112 O  O   . HOH I 8 .    ? 58.481 52.843  4.737   1.00 28.60 ? 1638 HOH A O   1 
HETATM 9113 O  O   . HOH I 8 .    ? 60.174 54.964  4.299   1.00 41.09 ? 1639 HOH A O   1 
HETATM 9114 O  O   . HOH I 8 .    ? 60.418 51.599  6.173   1.00 37.53 ? 1640 HOH A O   1 
HETATM 9115 O  O   . HOH I 8 .    ? 62.060 51.641  9.495   1.00 41.34 ? 1641 HOH A O   1 
HETATM 9116 O  O   . HOH I 8 .    ? 60.407 51.323  12.866  1.00 39.39 ? 1642 HOH A O   1 
HETATM 9117 O  O   . HOH I 8 .    ? 58.888 51.237  14.896  1.00 40.68 ? 1643 HOH A O   1 
HETATM 9118 O  O   . HOH I 8 .    ? 57.652 49.290  16.669  1.00 32.95 ? 1644 HOH A O   1 
HETATM 9119 O  O   . HOH I 8 .    ? 55.298 50.424  16.878  1.00 29.14 ? 1645 HOH A O   1 
HETATM 9120 O  O   . HOH I 8 .    ? 54.420 47.778  15.598  1.00 26.81 ? 1646 HOH A O   1 
HETATM 9121 O  O   . HOH I 8 .    ? 56.976 46.790  15.767  1.00 31.12 ? 1647 HOH A O   1 
HETATM 9122 O  O   . HOH I 8 .    ? 58.968 48.865  19.079  1.00 34.99 ? 1648 HOH A O   1 
HETATM 9123 O  O   . HOH I 8 .    ? 60.385 50.837  20.307  1.00 34.34 ? 1649 HOH A O   1 
HETATM 9124 O  O   . HOH I 8 .    ? 60.262 46.322  18.987  1.00 49.76 ? 1650 HOH A O   1 
HETATM 9125 O  O   . HOH I 8 .    ? 58.862 42.144  16.841  1.00 50.69 ? 1651 HOH A O   1 
HETATM 9126 O  O   . HOH I 8 .    ? 52.641 43.808  17.145  1.00 41.89 ? 1652 HOH A O   1 
HETATM 9127 O  O   . HOH I 8 .    ? 49.120 44.052  17.730  1.00 52.69 ? 1653 HOH A O   1 
HETATM 9128 O  O   . HOH I 8 .    ? 46.088 46.235  16.493  1.00 30.75 ? 1654 HOH A O   1 
HETATM 9129 O  O   . HOH I 8 .    ? 48.121 48.424  16.483  1.00 16.08 ? 1655 HOH A O   1 
HETATM 9130 O  O   . HOH I 8 .    ? 48.032 49.603  13.876  1.00 12.68 ? 1656 HOH A O   1 
HETATM 9131 O  O   . HOH I 8 .    ? 47.144 48.689  11.568  1.00 15.71 ? 1657 HOH A O   1 
HETATM 9132 O  O   . HOH I 8 .    ? 43.145 48.127  11.294  1.00 12.64 ? 1658 HOH A O   1 
HETATM 9133 O  O   . HOH I 8 .    ? 44.878 40.421  13.379  1.00 31.76 ? 1659 HOH A O   1 
HETATM 9134 O  O   . HOH I 8 .    ? 41.897 39.190  16.694  1.00 27.75 ? 1660 HOH A O   1 
HETATM 9135 O  O   . HOH I 8 .    ? 39.279 38.977  17.318  1.00 17.01 ? 1661 HOH A O   1 
HETATM 9136 O  O   . HOH I 8 .    ? 43.932 45.089  19.241  1.00 39.58 ? 1662 HOH A O   1 
HETATM 9137 O  O   . HOH I 8 .    ? 45.740 45.128  23.129  1.00 30.87 ? 1663 HOH A O   1 
HETATM 9138 O  O   . HOH I 8 .    ? 44.447 45.487  25.374  1.00 33.09 ? 1664 HOH A O   1 
HETATM 9139 O  O   . HOH I 8 .    ? 49.181 42.359  22.733  1.00 44.59 ? 1665 HOH A O   1 
HETATM 9140 O  O   . HOH I 8 .    ? 43.353 41.237  30.445  1.00 26.53 ? 1666 HOH A O   1 
HETATM 9141 O  O   . HOH I 8 .    ? 37.688 40.522  26.524  1.00 30.47 ? 1667 HOH A O   1 
HETATM 9142 O  O   . HOH I 8 .    ? 37.196 37.492  25.012  1.00 44.94 ? 1668 HOH A O   1 
HETATM 9143 O  O   . HOH I 8 .    ? 30.294 36.669  29.042  1.00 25.75 ? 1669 HOH A O   1 
HETATM 9144 O  O   . HOH I 8 .    ? 27.346 35.112  29.629  1.00 27.01 ? 1670 HOH A O   1 
HETATM 9145 O  O   . HOH I 8 .    ? 26.440 37.487  29.483  1.00 18.72 ? 1671 HOH A O   1 
HETATM 9146 O  O   . HOH I 8 .    ? 28.324 34.884  32.275  1.00 35.57 ? 1672 HOH A O   1 
HETATM 9147 O  O   . HOH I 8 .    ? 27.524 31.038  30.251  1.00 37.29 ? 1673 HOH A O   1 
HETATM 9148 O  O   . HOH I 8 .    ? 26.287 32.884  28.782  1.00 25.87 ? 1674 HOH A O   1 
HETATM 9149 O  O   . HOH I 8 .    ? 22.615 31.427  29.702  1.00 27.25 ? 1675 HOH A O   1 
HETATM 9150 O  O   . HOH I 8 .    ? 20.872 31.782  31.578  1.00 40.96 ? 1676 HOH A O   1 
HETATM 9151 O  O   . HOH I 8 .    ? 18.563 34.203  29.480  1.00 47.49 ? 1677 HOH A O   1 
HETATM 9152 O  O   . HOH I 8 .    ? 19.990 35.728  25.694  1.00 30.41 ? 1678 HOH A O   1 
HETATM 9153 O  O   . HOH I 8 .    ? 18.908 36.821  22.637  1.00 42.08 ? 1679 HOH A O   1 
HETATM 9154 O  O   . HOH I 8 .    ? 18.518 37.687  19.780  1.00 39.14 ? 1680 HOH A O   1 
HETATM 9155 O  O   . HOH I 8 .    ? 19.734 39.316  17.712  1.00 17.52 ? 1681 HOH A O   1 
HETATM 9156 O  O   . HOH I 8 .    ? 21.611 38.059  15.631  1.00 35.65 ? 1682 HOH A O   1 
HETATM 9157 O  O   . HOH I 8 .    ? 22.987 36.949  13.354  1.00 36.01 ? 1683 HOH A O   1 
HETATM 9158 O  O   . HOH I 8 .    ? 22.176 34.604  12.655  1.00 49.50 ? 1684 HOH A O   1 
HETATM 9159 O  O   . HOH I 8 .    ? 25.414 33.283  13.362  1.00 32.52 ? 1685 HOH A O   1 
HETATM 9160 O  O   . HOH I 8 .    ? 24.282 34.500  15.733  1.00 37.21 ? 1686 HOH A O   1 
HETATM 9161 O  O   . HOH I 8 .    ? 21.590 32.064  15.531  1.00 43.10 ? 1687 HOH A O   1 
HETATM 9162 O  O   . HOH I 8 .    ? 20.766 30.435  17.891  1.00 35.24 ? 1688 HOH A O   1 
HETATM 9163 O  O   . HOH I 8 .    ? 16.021 30.894  18.126  1.00 51.78 ? 1689 HOH A O   1 
HETATM 9164 O  O   . HOH I 8 .    ? 16.327 33.534  15.870  1.00 43.47 ? 1690 HOH A O   1 
HETATM 9165 O  O   . HOH I 8 .    ? 16.141 36.400  16.222  1.00 28.80 ? 1691 HOH A O   1 
HETATM 9166 O  O   . HOH I 8 .    ? 17.966 34.938  13.349  1.00 41.34 ? 1692 HOH A O   1 
HETATM 9167 O  O   . HOH I 8 .    ? 18.202 37.709  11.495  1.00 36.36 ? 1693 HOH A O   1 
HETATM 9168 O  O   . HOH I 8 .    ? 20.518 37.889  12.303  1.00 28.74 ? 1694 HOH A O   1 
HETATM 9169 O  O   . HOH I 8 .    ? 25.055 40.114  14.285  1.00 19.92 ? 1695 HOH A O   1 
HETATM 9170 O  O   . HOH I 8 .    ? 27.231 41.450  13.369  1.00 15.68 ? 1696 HOH A O   1 
HETATM 9171 O  O   . HOH I 8 .    ? 28.324 43.943  13.248  1.00 9.88  ? 1697 HOH A O   1 
HETATM 9172 O  O   . HOH I 8 .    ? 27.214 46.418  13.665  1.00 15.65 ? 1698 HOH A O   1 
HETATM 9173 O  O   . HOH I 8 .    ? 27.983 48.634  12.184  1.00 15.28 ? 1699 HOH A O   1 
HETATM 9174 O  O   A HOH I 8 .    ? 25.801 52.181  12.969  0.50 14.15 ? 1700 HOH A O   1 
HETATM 9175 O  O   B HOH I 8 .    ? 27.448 50.977  13.321  0.50 9.91  ? 1700 HOH A O   1 
HETATM 9176 O  O   . HOH I 8 .    ? 25.546 53.757  11.245  1.00 15.33 ? 1701 HOH A O   1 
HETATM 9177 O  O   . HOH I 8 .    ? 19.390 55.314  11.610  1.00 12.56 ? 1702 HOH A O   1 
HETATM 9178 O  O   . HOH I 8 .    ? 18.404 55.005  14.179  1.00 12.43 ? 1703 HOH A O   1 
HETATM 9179 O  O   . HOH I 8 .    ? 20.171 54.813  16.169  1.00 11.16 ? 1704 HOH A O   1 
HETATM 9180 O  O   . HOH I 8 .    ? 16.783 57.136  13.048  1.00 15.09 ? 1705 HOH A O   1 
HETATM 9181 O  O   . HOH I 8 .    ? 17.086 56.357  10.375  1.00 12.42 ? 1706 HOH A O   1 
HETATM 9182 O  O   . HOH I 8 .    ? 15.571 60.445  15.537  1.00 16.29 ? 1707 HOH A O   1 
HETATM 9183 O  O   . HOH I 8 .    ? 13.953 62.488  14.674  1.00 26.33 ? 1708 HOH A O   1 
HETATM 9184 O  O   . HOH I 8 .    ? 13.313 62.979  11.952  1.00 30.26 ? 1709 HOH A O   1 
HETATM 9185 O  O   . HOH I 8 .    ? 14.043 58.319  16.364  1.00 16.64 ? 1710 HOH A O   1 
HETATM 9186 O  O   . HOH I 8 .    ? 14.063 57.737  19.120  1.00 19.61 ? 1711 HOH A O   1 
HETATM 9187 O  O   . HOH I 8 .    ? 11.681 58.458  20.177  1.00 31.51 ? 1712 HOH A O   1 
HETATM 9188 O  O   . HOH I 8 .    ? 12.249 60.982  20.490  1.00 51.28 ? 1713 HOH A O   1 
HETATM 9189 O  O   . HOH I 8 .    ? 11.930 62.245  23.336  1.00 34.59 ? 1714 HOH A O   1 
HETATM 9190 O  O   . HOH I 8 .    ? 11.220 59.595  27.805  1.00 48.76 ? 1715 HOH A O   1 
HETATM 9191 O  O   . HOH I 8 .    ? 12.693 57.413  28.584  1.00 36.80 ? 1716 HOH A O   1 
HETATM 9192 O  O   . HOH I 8 .    ? 14.761 55.928  27.393  1.00 26.54 ? 1717 HOH A O   1 
HETATM 9193 O  O   . HOH I 8 .    ? 14.229 53.902  28.991  1.00 47.01 ? 1718 HOH A O   1 
HETATM 9194 O  O   . HOH I 8 .    ? 16.271 55.576  30.246  1.00 34.15 ? 1719 HOH A O   1 
HETATM 9195 O  O   . HOH I 8 .    ? 16.085 57.785  31.662  1.00 38.47 ? 1720 HOH A O   1 
HETATM 9196 O  O   . HOH I 8 .    ? 18.326 59.658  31.795  1.00 35.67 ? 1721 HOH A O   1 
HETATM 9197 O  O   . HOH I 8 .    ? 20.013 62.487  34.874  1.00 42.87 ? 1722 HOH A O   1 
HETATM 9198 O  O   . HOH I 8 .    ? 22.318 62.790  33.798  1.00 31.54 ? 1723 HOH A O   1 
HETATM 9199 O  O   . HOH I 8 .    ? 22.249 65.735  32.246  1.00 27.92 ? 1724 HOH A O   1 
HETATM 9200 O  O   . HOH I 8 .    ? 22.566 65.989  29.397  1.00 30.25 ? 1725 HOH A O   1 
HETATM 9201 O  O   . HOH I 8 .    ? 20.771 65.457  27.475  1.00 26.67 ? 1726 HOH A O   1 
HETATM 9202 O  O   . HOH I 8 .    ? 23.042 69.452  29.177  1.00 58.30 ? 1727 HOH A O   1 
HETATM 9203 O  O   . HOH I 8 .    ? 24.335 71.532  27.171  1.00 36.67 ? 1728 HOH A O   1 
HETATM 9204 O  O   . HOH I 8 .    ? 23.629 71.482  24.925  1.00 34.12 ? 1729 HOH A O   1 
HETATM 9205 O  O   . HOH I 8 .    ? 25.189 71.326  22.616  1.00 35.06 ? 1730 HOH A O   1 
HETATM 9206 O  O   . HOH I 8 .    ? 24.829 68.379  21.893  1.00 20.77 ? 1731 HOH A O   1 
HETATM 9207 O  O   . HOH I 8 .    ? 22.484 68.319  20.439  1.00 27.50 ? 1732 HOH A O   1 
HETATM 9208 O  O   . HOH I 8 .    ? 20.565 68.399  22.282  1.00 27.56 ? 1733 HOH A O   1 
HETATM 9209 O  O   . HOH I 8 .    ? 21.903 70.950  19.216  1.00 44.27 ? 1734 HOH A O   1 
HETATM 9210 O  O   . HOH I 8 .    ? 26.464 66.990  19.829  1.00 27.27 ? 1735 HOH A O   1 
HETATM 9211 O  O   . HOH I 8 .    ? 28.377 69.655  19.040  1.00 50.65 ? 1736 HOH A O   1 
HETATM 9212 O  O   . HOH I 8 .    ? 30.779 71.225  21.252  1.00 32.04 ? 1737 HOH A O   1 
HETATM 9213 O  O   . HOH I 8 .    ? 28.811 72.621  22.532  1.00 24.18 ? 1738 HOH A O   1 
HETATM 9214 O  O   . HOH I 8 .    ? 27.781 67.815  28.252  1.00 19.40 ? 1739 HOH A O   1 
HETATM 9215 O  O   . HOH I 8 .    ? 28.959 64.567  30.133  1.00 21.89 ? 1740 HOH A O   1 
HETATM 9216 O  O   . HOH I 8 .    ? 29.432 65.802  32.426  1.00 42.06 ? 1741 HOH A O   1 
HETATM 9217 O  O   . HOH I 8 .    ? 27.782 67.527  33.820  1.00 51.48 ? 1742 HOH A O   1 
HETATM 9218 O  O   . HOH I 8 .    ? 30.793 61.900  35.613  1.00 45.69 ? 1743 HOH A O   1 
HETATM 9219 O  O   . HOH I 8 .    ? 30.090 59.400  35.165  1.00 32.11 ? 1744 HOH A O   1 
HETATM 9220 O  O   . HOH I 8 .    ? 31.527 57.551  37.413  1.00 28.13 ? 1745 HOH A O   1 
HETATM 9221 O  O   . HOH I 8 .    ? 30.489 57.485  39.863  1.00 37.80 ? 1746 HOH A O   1 
HETATM 9222 O  O   . HOH I 8 .    ? 28.903 55.295  39.975  1.00 30.84 ? 1747 HOH A O   1 
HETATM 9223 O  O   . HOH I 8 .    ? 28.218 54.784  42.321  1.00 37.25 ? 1748 HOH A O   1 
HETATM 9224 O  O   . HOH I 8 .    ? 27.834 52.218  42.518  1.00 36.88 ? 1749 HOH A O   1 
HETATM 9225 O  O   . HOH I 8 .    ? 30.256 51.556  39.870  1.00 54.75 ? 1750 HOH A O   1 
HETATM 9226 O  O   . HOH I 8 .    ? 28.376 49.356  38.502  1.00 29.17 ? 1751 HOH A O   1 
HETATM 9227 O  O   . HOH I 8 .    ? 29.233 47.032  37.171  1.00 21.25 ? 1752 HOH A O   1 
HETATM 9228 O  O   . HOH I 8 .    ? 31.719 47.560  38.009  1.00 39.47 ? 1753 HOH A O   1 
HETATM 9229 O  O   . HOH I 8 .    ? 33.102 49.465  39.746  1.00 40.32 ? 1754 HOH A O   1 
HETATM 9230 O  O   . HOH I 8 .    ? 33.862 45.949  40.484  1.00 26.95 ? 1755 HOH A O   1 
HETATM 9231 O  O   . HOH I 8 .    ? 30.683 43.949  40.487  1.00 51.04 ? 1756 HOH A O   1 
HETATM 9232 O  O   . HOH I 8 .    ? 28.317 44.484  38.240  1.00 28.47 ? 1757 HOH A O   1 
HETATM 9233 O  O   . HOH I 8 .    ? 28.135 40.550  38.657  1.00 39.63 ? 1758 HOH A O   1 
HETATM 9234 O  O   . HOH I 8 .    ? 31.425 40.720  38.289  1.00 37.99 ? 1759 HOH A O   1 
HETATM 9235 O  O   . HOH I 8 .    ? 67.250 66.449  -32.725 1.00 42.68 ? 1760 HOH A O   1 
HETATM 9236 O  O   . HOH I 8 .    ? 34.850 45.871  33.285  1.00 18.73 ? 1761 HOH A O   1 
HETATM 9237 O  O   . HOH I 8 .    ? 34.237 47.985  36.442  1.00 36.27 ? 1762 HOH A O   1 
HETATM 9238 O  O   . HOH I 8 .    ? 34.597 51.241  36.006  1.00 33.91 ? 1763 HOH A O   1 
HETATM 9239 O  O   . HOH I 8 .    ? 39.525 49.838  36.365  1.00 33.45 ? 1764 HOH A O   1 
HETATM 9240 O  O   . HOH I 8 .    ? 40.163 52.741  36.391  1.00 29.75 ? 1765 HOH A O   1 
HETATM 9241 O  O   . HOH I 8 .    ? 42.672 53.366  35.614  1.00 21.08 ? 1766 HOH A O   1 
HETATM 9242 O  O   . HOH I 8 .    ? 43.831 56.653  33.772  1.00 28.53 ? 1767 HOH A O   1 
HETATM 9243 O  O   . HOH I 8 .    ? 45.581 58.047  32.381  1.00 36.29 ? 1768 HOH A O   1 
HETATM 9244 O  O   . HOH I 8 .    ? 41.895 58.385  34.527  1.00 34.47 ? 1769 HOH A O   1 
HETATM 9245 O  O   . HOH I 8 .    ? 37.928 62.448  35.453  1.00 33.27 ? 1770 HOH A O   1 
HETATM 9246 O  O   . HOH I 8 .    ? 35.588 62.361  34.096  1.00 25.37 ? 1771 HOH A O   1 
HETATM 9247 O  O   . HOH I 8 .    ? 33.744 64.213  33.394  1.00 59.53 ? 1772 HOH A O   1 
HETATM 9248 O  O   . HOH I 8 .    ? 34.185 59.950  35.000  1.00 38.70 ? 1773 HOH A O   1 
HETATM 9249 O  O   . HOH I 8 .    ? 35.810 59.019  36.668  1.00 47.59 ? 1774 HOH A O   1 
HETATM 9250 O  O   . HOH I 8 .    ? 26.799 57.585  40.510  1.00 39.67 ? 1775 HOH A O   1 
HETATM 9251 O  O   . HOH I 8 .    ? 24.346 57.425  38.706  1.00 28.28 ? 1776 HOH A O   1 
HETATM 9252 O  O   . HOH I 8 .    ? 21.178 58.563  37.776  1.00 41.37 ? 1777 HOH A O   1 
HETATM 9253 O  O   . HOH I 8 .    ? 21.560 55.606  40.088  1.00 26.14 ? 1778 HOH A O   1 
HETATM 9254 O  O   . HOH I 8 .    ? 26.416 56.713  43.341  1.00 43.36 ? 1779 HOH A O   1 
HETATM 9255 O  O   . HOH I 8 .    ? 24.249 60.949  36.139  1.00 35.21 ? 1780 HOH A O   1 
HETATM 9256 O  O   . HOH I 8 .    ? 23.215 56.094  30.897  1.00 18.16 ? 1781 HOH A O   1 
HETATM 9257 O  O   . HOH I 8 .    ? 17.577 52.632  33.099  1.00 39.47 ? 1782 HOH A O   1 
HETATM 9258 O  O   . HOH I 8 .    ? 17.898 52.809  35.902  1.00 36.04 ? 1783 HOH A O   1 
HETATM 9259 O  O   . HOH I 8 .    ? 17.885 50.860  38.456  1.00 35.99 ? 1784 HOH A O   1 
HETATM 9260 O  O   . HOH I 8 .    ? 19.081 48.715  37.812  1.00 20.84 ? 1785 HOH A O   1 
HETATM 9261 O  O   . HOH I 8 .    ? 21.131 47.591  39.089  1.00 22.63 ? 1786 HOH A O   1 
HETATM 9262 O  O   . HOH I 8 .    ? 19.933 45.518  40.373  1.00 31.48 ? 1787 HOH A O   1 
HETATM 9263 O  O   . HOH I 8 .    ? 17.672 46.817  39.740  1.00 45.11 ? 1788 HOH A O   1 
HETATM 9264 O  O   . HOH I 8 .    ? 17.756 49.254  41.258  1.00 21.36 ? 1789 HOH A O   1 
HETATM 9265 O  O   . HOH I 8 .    ? 24.263 45.789  40.724  1.00 43.29 ? 1790 HOH A O   1 
HETATM 9266 O  O   . HOH I 8 .    ? 27.591 47.653  45.959  1.00 43.96 ? 1791 HOH A O   1 
HETATM 9267 O  O   . HOH I 8 .    ? 21.206 41.824  35.336  1.00 27.69 ? 1792 HOH A O   1 
HETATM 9268 O  O   . HOH I 8 .    ? 19.848 43.399  34.010  1.00 25.98 ? 1793 HOH A O   1 
HETATM 9269 O  O   . HOH I 8 .    ? 17.326 41.857  32.282  1.00 45.21 ? 1794 HOH A O   1 
HETATM 9270 O  O   . HOH I 8 .    ? 18.336 43.082  27.487  1.00 28.79 ? 1795 HOH A O   1 
HETATM 9271 O  O   . HOH I 8 .    ? 18.150 41.779  25.301  1.00 31.10 ? 1796 HOH A O   1 
HETATM 9272 O  O   . HOH I 8 .    ? 19.081 39.964  26.673  1.00 32.90 ? 1797 HOH A O   1 
HETATM 9273 O  O   . HOH I 8 .    ? 14.132 44.798  27.128  1.00 40.07 ? 1798 HOH A O   1 
HETATM 9274 O  O   . HOH I 8 .    ? 14.884 47.223  27.532  1.00 39.15 ? 1799 HOH A O   1 
HETATM 9275 O  O   . HOH I 8 .    ? 13.834 48.963  29.103  1.00 38.64 ? 1800 HOH A O   1 
HETATM 9276 O  O   . HOH I 8 .    ? 15.792 49.228  31.461  1.00 23.82 ? 1801 HOH A O   1 
HETATM 9277 O  O   . HOH I 8 .    ? 15.053 51.283  32.619  1.00 26.78 ? 1802 HOH A O   1 
HETATM 9278 O  O   . HOH I 8 .    ? 14.582 47.109  32.348  1.00 26.06 ? 1803 HOH A O   1 
HETATM 9279 O  O   . HOH I 8 .    ? 12.384 47.546  31.427  1.00 33.76 ? 1804 HOH A O   1 
HETATM 9280 O  O   . HOH I 8 .    ? 13.476 52.747  26.091  1.00 34.77 ? 1805 HOH A O   1 
HETATM 9281 O  O   . HOH I 8 .    ? 13.032 55.220  25.324  1.00 37.85 ? 1806 HOH A O   1 
HETATM 9282 O  O   . HOH I 8 .    ? 12.473 55.368  22.665  1.00 28.23 ? 1807 HOH A O   1 
HETATM 9283 O  O   . HOH I 8 .    ? 9.810  53.879  22.101  1.00 39.72 ? 1808 HOH A O   1 
HETATM 9284 O  O   . HOH I 8 .    ? 10.921 51.613  21.582  1.00 22.51 ? 1809 HOH A O   1 
HETATM 9285 O  O   . HOH I 8 .    ? 13.541 51.559  21.810  1.00 18.21 ? 1810 HOH A O   1 
HETATM 9286 O  O   . HOH I 8 .    ? 14.408 49.836  19.919  1.00 16.85 ? 1811 HOH A O   1 
HETATM 9287 O  O   . HOH I 8 .    ? 12.652 49.556  17.891  1.00 20.22 ? 1812 HOH A O   1 
HETATM 9288 O  O   . HOH I 8 .    ? 11.656 46.947  17.962  1.00 22.58 ? 1813 HOH A O   1 
HETATM 9289 O  O   . HOH I 8 .    ? 10.971 46.967  21.119  1.00 42.26 ? 1814 HOH A O   1 
HETATM 9290 O  O   . HOH I 8 .    ? 8.690  48.542  19.801  1.00 40.21 ? 1815 HOH A O   1 
HETATM 9291 O  O   . HOH I 8 .    ? 10.347 50.867  18.914  1.00 23.48 ? 1816 HOH A O   1 
HETATM 9292 O  O   . HOH I 8 .    ? 9.465  52.565  16.953  1.00 20.89 ? 1817 HOH A O   1 
HETATM 9293 O  O   . HOH I 8 .    ? 7.651  54.630  17.439  1.00 36.01 ? 1818 HOH A O   1 
HETATM 9294 O  O   . HOH I 8 .    ? 8.781  56.903  16.444  1.00 42.57 ? 1819 HOH A O   1 
HETATM 9295 O  O   . HOH I 8 .    ? 8.371  55.538  20.107  1.00 48.51 ? 1820 HOH A O   1 
HETATM 9296 O  O   . HOH I 8 .    ? 6.846  52.300  16.028  1.00 44.44 ? 1821 HOH A O   1 
HETATM 9297 O  O   . HOH I 8 .    ? 7.704  50.781  12.676  1.00 50.28 ? 1822 HOH A O   1 
HETATM 9298 O  O   . HOH I 8 .    ? 8.139  48.158  12.022  1.00 25.72 ? 1823 HOH A O   1 
HETATM 9299 O  O   . HOH I 8 .    ? 5.983  47.204  13.791  1.00 46.15 ? 1824 HOH A O   1 
HETATM 9300 O  O   . HOH I 8 .    ? 6.291  46.640  16.119  1.00 35.69 ? 1825 HOH A O   1 
HETATM 9301 O  O   . HOH I 8 .    ? 8.662  44.667  13.418  1.00 29.60 ? 1826 HOH A O   1 
HETATM 9302 O  O   . HOH I 8 .    ? 10.366 41.703  12.178  1.00 39.97 ? 1827 HOH A O   1 
HETATM 9303 O  O   . HOH I 8 .    ? 12.912 42.575  12.718  1.00 18.65 ? 1828 HOH A O   1 
HETATM 9304 O  O   . HOH I 8 .    ? 14.525 40.257  12.810  1.00 43.54 ? 1829 HOH A O   1 
HETATM 9305 O  O   . HOH I 8 .    ? 10.913 38.335  11.983  1.00 49.78 ? 1830 HOH A O   1 
HETATM 9306 O  O   . HOH I 8 .    ? 9.563  39.840  19.379  1.00 42.04 ? 1831 HOH A O   1 
HETATM 9307 O  O   . HOH I 8 .    ? 12.062 41.510  19.919  1.00 31.70 ? 1832 HOH A O   1 
HETATM 9308 O  O   . HOH I 8 .    ? 13.140 40.239  22.382  1.00 40.82 ? 1833 HOH A O   1 
HETATM 9309 O  O   . HOH I 8 .    ? 13.148 43.614  22.760  1.00 35.00 ? 1834 HOH A O   1 
HETATM 9310 O  O   . HOH I 8 .    ? 16.646 49.135  24.163  1.00 14.74 ? 1835 HOH A O   1 
HETATM 9311 O  O   . HOH I 8 .    ? 14.286 50.526  24.357  1.00 22.73 ? 1836 HOH A O   1 
HETATM 9312 O  O   . HOH I 8 .    ? 10.454 55.832  26.436  1.00 37.47 ? 1837 HOH A O   1 
HETATM 9313 O  O   . HOH I 8 .    ? 12.871 61.086  30.368  1.00 35.87 ? 1838 HOH A O   1 
HETATM 9314 O  O   . HOH I 8 .    ? 14.363 63.282  30.285  1.00 38.37 ? 1839 HOH A O   1 
HETATM 9315 O  O   . HOH I 8 .    ? 51.362 98.757  -32.194 1.00 43.03 ? 1840 HOH A O   1 
HETATM 9316 O  O   . HOH I 8 .    ? 18.152 60.701  24.509  1.00 18.19 ? 1841 HOH A O   1 
HETATM 9317 O  O   . HOH I 8 .    ? 28.037 61.095  19.502  1.00 11.63 ? 1842 HOH A O   1 
HETATM 9318 O  O   . HOH I 8 .    ? 28.951 62.578  13.829  1.00 54.39 ? 1843 HOH A O   1 
HETATM 9319 O  O   . HOH I 8 .    ? 29.354 65.680  15.612  1.00 26.07 ? 1844 HOH A O   1 
HETATM 9320 O  O   . HOH I 8 .    ? 31.014 68.146  13.789  1.00 24.83 ? 1845 HOH A O   1 
HETATM 9321 O  O   . HOH I 8 .    ? 31.941 71.085  13.413  1.00 27.34 ? 1846 HOH A O   1 
HETATM 9322 O  O   . HOH I 8 .    ? 29.877 72.161  12.260  1.00 21.14 ? 1847 HOH A O   1 
HETATM 9323 O  O   . HOH I 8 .    ? 29.779 75.605  10.833  1.00 25.84 ? 1848 HOH A O   1 
HETATM 9324 O  O   . HOH I 8 .    ? 30.291 77.991  11.637  1.00 43.72 ? 1849 HOH A O   1 
HETATM 9325 O  O   . HOH I 8 .    ? 34.776 77.534  12.398  1.00 27.63 ? 1850 HOH A O   1 
HETATM 9326 O  O   . HOH I 8 .    ? 35.237 76.310  14.887  1.00 45.27 ? 1851 HOH A O   1 
HETATM 9327 O  O   . HOH I 8 .    ? 35.715 73.809  15.097  1.00 34.68 ? 1852 HOH A O   1 
HETATM 9328 O  O   . HOH I 8 .    ? 34.779 70.318  12.975  1.00 17.76 ? 1853 HOH A O   1 
HETATM 9329 O  O   . HOH I 8 .    ? 34.377 67.565  12.237  1.00 14.20 ? 1854 HOH A O   1 
HETATM 9330 O  O   . HOH I 8 .    ? 38.776 62.442  8.414   1.00 9.92  ? 1855 HOH A O   1 
HETATM 9331 O  O   . HOH I 8 .    ? 40.363 62.812  6.108   1.00 8.59  ? 1856 HOH A O   1 
HETATM 9332 O  O   . HOH I 8 .    ? 43.009 56.866  6.132   1.00 10.68 ? 1857 HOH A O   1 
HETATM 9333 O  O   . HOH I 8 .    ? 40.185 56.287  5.776   1.00 11.76 ? 1858 HOH A O   1 
HETATM 9334 O  O   . HOH I 8 .    ? 39.693 55.739  3.051   1.00 13.21 ? 1859 HOH A O   1 
HETATM 9335 O  O   A HOH I 8 .    ? 42.744 56.517  2.766   0.50 8.55  ? 1860 HOH A O   1 
HETATM 9336 O  O   B HOH I 8 .    ? 42.069 55.458  1.543   0.50 16.72 ? 1860 HOH A O   1 
HETATM 9337 O  O   . HOH I 8 .    ? 38.843 53.070  2.212   1.00 25.50 ? 1861 HOH A O   1 
HETATM 9338 O  O   . HOH I 8 .    ? 36.777 51.643  3.750   1.00 12.24 ? 1862 HOH A O   1 
HETATM 9339 O  O   . HOH I 8 .    ? 35.984 53.089  1.337   1.00 11.53 ? 1863 HOH A O   1 
HETATM 9340 O  O   . HOH I 8 .    ? 34.296 52.419  -0.943  1.00 8.58  ? 1864 HOH A O   1 
HETATM 9341 O  O   . HOH I 8 .    ? 37.573 57.054  1.770   1.00 9.35  ? 1865 HOH A O   1 
HETATM 9342 O  O   . HOH I 8 .    ? 32.613 60.152  -1.833  1.00 8.30  ? 1866 HOH A O   1 
HETATM 9343 O  O   . HOH I 8 .    ? 33.145 62.757  0.089   1.00 7.05  ? 1867 HOH A O   1 
HETATM 9344 O  O   . HOH I 8 .    ? 30.983 57.262  4.506   1.00 26.07 ? 1868 HOH A O   1 
HETATM 9345 O  O   . HOH I 8 .    ? 24.421 55.703  -1.725  1.00 12.40 ? 1869 HOH A O   1 
HETATM 9346 O  O   . HOH I 8 .    ? 23.354 53.963  -3.582  1.00 13.23 ? 1870 HOH A O   1 
HETATM 9347 O  O   A HOH I 8 .    ? 24.238 53.224  -6.220  0.50 9.22  ? 1871 HOH A O   1 
HETATM 9348 O  O   B HOH I 8 .    ? 23.979 52.327  -5.271  0.50 14.14 ? 1871 HOH A O   1 
HETATM 9349 O  O   . HOH I 8 .    ? 23.170 54.464  -8.593  1.00 34.87 ? 1872 HOH A O   1 
HETATM 9350 O  O   . HOH I 8 .    ? 22.978 51.799  -8.535  1.00 15.84 ? 1873 HOH A O   1 
HETATM 9351 O  O   . HOH I 8 .    ? 25.574 51.264  -9.384  1.00 12.29 ? 1874 HOH A O   1 
HETATM 9352 O  O   . HOH I 8 .    ? 26.275 48.924  -10.883 1.00 10.12 ? 1875 HOH A O   1 
HETATM 9353 O  O   . HOH I 8 .    ? 26.132 49.609  -13.609 1.00 9.13  ? 1876 HOH A O   1 
HETATM 9354 O  O   . HOH I 8 .    ? 24.749 52.961  -11.686 1.00 9.15  ? 1877 HOH A O   1 
HETATM 9355 O  O   . HOH I 8 .    ? 22.358 54.418  -11.956 1.00 10.03 ? 1878 HOH A O   1 
HETATM 9356 O  O   . HOH I 8 .    ? 19.678 53.529  -11.744 1.00 11.28 ? 1879 HOH A O   1 
HETATM 9357 O  O   . HOH I 8 .    ? 18.621 51.071  -12.382 1.00 12.27 ? 1880 HOH A O   1 
HETATM 9358 O  O   . HOH I 8 .    ? 19.968 46.803  -14.232 1.00 18.02 ? 1881 HOH A O   1 
HETATM 9359 O  O   . HOH I 8 .    ? 17.519 45.618  -13.967 1.00 32.96 ? 1882 HOH A O   1 
HETATM 9360 O  O   . HOH I 8 .    ? 15.976 44.948  -11.665 1.00 38.85 ? 1883 HOH A O   1 
HETATM 9361 O  O   . HOH I 8 .    ? 13.452 45.802  -12.126 1.00 37.71 ? 1884 HOH A O   1 
HETATM 9362 O  O   . HOH I 8 .    ? 19.720 42.412  -14.855 1.00 38.63 ? 1885 HOH A O   1 
HETATM 9363 O  O   . HOH I 8 .    ? 20.090 39.762  -15.107 1.00 41.33 ? 1886 HOH A O   1 
HETATM 9364 O  O   . HOH I 8 .    ? 20.112 39.821  -12.499 1.00 41.30 ? 1887 HOH A O   1 
HETATM 9365 O  O   . HOH I 8 .    ? 22.219 40.756  -11.195 1.00 19.72 ? 1888 HOH A O   1 
HETATM 9366 O  O   . HOH I 8 .    ? 21.889 40.388  -8.655  1.00 27.28 ? 1889 HOH A O   1 
HETATM 9367 O  O   . HOH I 8 .    ? 20.744 42.655  -7.375  1.00 17.87 ? 1890 HOH A O   1 
HETATM 9368 O  O   . HOH I 8 .    ? 19.767 41.594  -4.933  1.00 24.43 ? 1891 HOH A O   1 
HETATM 9369 O  O   . HOH I 8 .    ? 19.138 42.459  -2.447  1.00 25.71 ? 1892 HOH A O   1 
HETATM 9370 O  O   . HOH I 8 .    ? 16.613 43.030  -2.184  1.00 28.46 ? 1893 HOH A O   1 
HETATM 9371 O  O   . HOH I 8 .    ? 15.285 40.447  -2.561  1.00 47.14 ? 1894 HOH A O   1 
HETATM 9372 O  O   . HOH I 8 .    ? 18.424 39.400  -2.452  1.00 36.89 ? 1895 HOH A O   1 
HETATM 9373 O  O   . HOH I 8 .    ? 17.896 38.060  -0.165  1.00 42.78 ? 1896 HOH A O   1 
HETATM 9374 O  O   . HOH I 8 .    ? 19.734 37.142  1.633   1.00 43.82 ? 1897 HOH A O   1 
HETATM 9375 O  O   . HOH I 8 .    ? 21.992 36.940  0.322   1.00 25.32 ? 1898 HOH A O   1 
HETATM 9376 O  O   . HOH I 8 .    ? 22.913 34.994  -1.091  1.00 49.75 ? 1899 HOH A O   1 
HETATM 9377 O  O   . HOH I 8 .    ? 24.624 34.516  0.731   1.00 43.61 ? 1900 HOH A O   1 
HETATM 9378 O  O   . HOH I 8 .    ? 22.397 33.548  1.887   1.00 39.85 ? 1901 HOH A O   1 
HETATM 9379 O  O   . HOH I 8 .    ? 24.770 33.062  6.494   1.00 25.06 ? 1902 HOH A O   1 
HETATM 9380 O  O   . HOH I 8 .    ? 24.459 33.159  9.566   1.00 29.26 ? 1903 HOH A O   1 
HETATM 9381 O  O   . HOH I 8 .    ? 26.291 40.113  8.015   1.00 10.88 ? 1904 HOH A O   1 
HETATM 9382 O  O   . HOH I 8 .    ? 25.891 39.778  5.273   1.00 10.51 ? 1905 HOH A O   1 
HETATM 9383 O  O   . HOH I 8 .    ? 24.052 41.995  6.978   1.00 11.25 ? 1906 HOH A O   1 
HETATM 9384 O  O   . HOH I 8 .    ? 28.193 39.750  11.352  1.00 12.89 ? 1907 HOH A O   1 
HETATM 9385 O  O   . HOH I 8 .    ? 34.739 36.454  3.560   1.00 36.38 ? 1908 HOH A O   1 
HETATM 9386 O  O   . HOH I 8 .    ? 37.167 37.596  2.861   1.00 32.25 ? 1909 HOH A O   1 
HETATM 9387 O  O   . HOH I 8 .    ? 38.326 40.121  1.815   1.00 11.99 ? 1910 HOH A O   1 
HETATM 9388 O  O   . HOH I 8 .    ? 40.021 39.713  -0.305  1.00 23.75 ? 1911 HOH A O   1 
HETATM 9389 O  O   . HOH I 8 .    ? 41.966 40.657  0.591   1.00 41.51 ? 1912 HOH A O   1 
HETATM 9390 O  O   . HOH I 8 .    ? 42.644 39.562  -1.348  1.00 26.41 ? 1913 HOH A O   1 
HETATM 9391 O  O   . HOH I 8 .    ? 44.534 41.861  -0.488  1.00 14.62 ? 1914 HOH A O   1 
HETATM 9392 O  O   . HOH I 8 .    ? 46.101 39.860  0.035   1.00 31.81 ? 1915 HOH A O   1 
HETATM 9393 O  O   . HOH I 8 .    ? 49.049 39.067  -3.122  1.00 45.37 ? 1916 HOH A O   1 
HETATM 9394 O  O   . HOH I 8 .    ? 52.433 36.649  -3.789  1.00 40.31 ? 1917 HOH A O   1 
HETATM 9395 O  O   . HOH I 8 .    ? 55.625 34.517  -4.846  1.00 38.35 ? 1918 HOH A O   1 
HETATM 9396 O  O   . HOH I 8 .    ? 58.161 34.746  -6.068  1.00 37.98 ? 1919 HOH A O   1 
HETATM 9397 O  O   . HOH I 8 .    ? 59.248 39.822  -4.182  1.00 43.93 ? 1920 HOH A O   1 
HETATM 9398 O  O   A HOH I 8 .    ? 63.139 45.727  -3.251  0.50 36.24 ? 1921 HOH A O   1 
HETATM 9399 O  O   B HOH I 8 .    ? 61.261 45.256  -3.770  0.50 22.39 ? 1921 HOH A O   1 
HETATM 9400 O  O   . HOH I 8 .    ? 65.852 45.690  -3.118  1.00 30.24 ? 1922 HOH A O   1 
HETATM 9401 O  O   . HOH I 8 .    ? 67.521 46.671  -1.333  1.00 26.42 ? 1923 HOH A O   1 
HETATM 9402 O  O   . HOH I 8 .    ? 65.485 46.307  0.554   1.00 53.26 ? 1924 HOH A O   1 
HETATM 9403 O  O   . HOH I 8 .    ? 62.882 44.762  -0.556  1.00 45.84 ? 1925 HOH A O   1 
HETATM 9404 O  O   . HOH I 8 .    ? 60.591 46.003  0.698   1.00 38.11 ? 1926 HOH A O   1 
HETATM 9405 O  O   . HOH I 8 .    ? 58.969 46.381  -1.450  1.00 22.39 ? 1927 HOH A O   1 
HETATM 9406 O  O   . HOH I 8 .    ? 57.984 42.248  1.600   1.00 22.39 ? 1928 HOH A O   1 
HETATM 9407 O  O   . HOH I 8 .    ? 59.594 45.096  4.883   1.00 44.32 ? 1929 HOH A O   1 
HETATM 9408 O  O   . HOH I 8 .    ? 54.234 46.026  4.883   1.00 40.44 ? 1930 HOH A O   1 
HETATM 9409 O  O   . HOH I 8 .    ? 54.146 46.305  8.038   1.00 36.85 ? 1931 HOH A O   1 
HETATM 9410 O  O   . HOH I 8 .    ? 52.848 43.989  7.588   1.00 31.97 ? 1932 HOH A O   1 
HETATM 9411 O  O   . HOH I 8 .    ? 51.337 45.372  10.048  1.00 31.53 ? 1933 HOH A O   1 
HETATM 9412 O  O   . HOH I 8 .    ? 53.722 45.028  12.769  1.00 50.14 ? 1934 HOH A O   1 
HETATM 9413 O  O   . HOH I 8 .    ? 52.198 50.649  6.379   1.00 11.19 ? 1935 HOH A O   1 
HETATM 9414 O  O   . HOH I 8 .    ? 56.184 53.427  -0.635  1.00 7.88  ? 1936 HOH A O   1 
HETATM 9415 O  O   . HOH I 8 .    ? 52.235 54.116  -4.847  1.00 8.77  ? 1937 HOH A O   1 
HETATM 9416 O  O   . HOH I 8 .    ? 51.484 56.685  -5.604  1.00 9.42  ? 1938 HOH A O   1 
HETATM 9417 O  O   . HOH I 8 .    ? 49.842 57.645  -7.585  1.00 11.02 ? 1939 HOH A O   1 
HETATM 9418 O  O   . HOH I 8 .    ? 50.905 59.927  -8.949  1.00 12.54 ? 1940 HOH A O   1 
HETATM 9419 O  O   . HOH I 8 .    ? 49.606 62.310  -8.648  1.00 10.96 ? 1941 HOH A O   1 
HETATM 9420 O  O   . HOH I 8 .    ? 50.060 59.538  -11.542 1.00 10.97 ? 1942 HOH A O   1 
HETATM 9421 O  O   . HOH I 8 .    ? 53.714 59.852  -9.376  1.00 12.20 ? 1943 HOH A O   1 
HETATM 9422 O  O   . HOH I 8 .    ? 55.665 59.361  -11.453 1.00 9.14  ? 1944 HOH A O   1 
HETATM 9423 O  O   . HOH I 8 .    ? 61.086 59.683  -8.209  1.00 8.94  ? 1945 HOH A O   1 
HETATM 9424 O  O   . HOH I 8 .    ? 59.580 60.663  -6.169  1.00 14.01 ? 1946 HOH A O   1 
HETATM 9425 O  O   . HOH I 8 .    ? 64.929 59.333  -3.537  1.00 14.10 ? 1947 HOH A O   1 
HETATM 9426 O  O   . HOH I 8 .    ? 68.877 58.290  -5.006  1.00 14.73 ? 1948 HOH A O   1 
HETATM 9427 O  O   . HOH I 8 .    ? 73.879 61.190  -6.215  1.00 44.96 ? 1949 HOH A O   1 
HETATM 9428 O  O   . HOH I 8 .    ? 73.090 65.029  -7.758  1.00 20.26 ? 1950 HOH A O   1 
HETATM 9429 O  O   . HOH I 8 .    ? 73.084 66.638  -10.050 1.00 22.76 ? 1951 HOH A O   1 
HETATM 9430 O  O   . HOH I 8 .    ? 75.658 67.202  -9.549  1.00 35.18 ? 1952 HOH A O   1 
HETATM 9431 O  O   . HOH I 8 .    ? 70.116 69.927  -12.583 1.00 13.85 ? 1953 HOH A O   1 
HETATM 9432 O  O   . HOH I 8 .    ? 66.583 62.633  -12.993 1.00 19.16 ? 1954 HOH A O   1 
HETATM 9433 O  O   . HOH I 8 .    ? 70.029 53.689  -10.074 1.00 37.66 ? 1955 HOH A O   1 
HETATM 9434 O  O   . HOH I 8 .    ? 70.706 52.157  -12.534 1.00 23.06 ? 1956 HOH A O   1 
HETATM 9435 O  O   . HOH I 8 .    ? 63.854 50.176  -13.959 1.00 13.69 ? 1957 HOH A O   1 
HETATM 9436 O  O   . HOH I 8 .    ? 63.555 44.629  -6.671  1.00 16.92 ? 1958 HOH A O   1 
HETATM 9437 O  O   . HOH I 8 .    ? 64.366 43.303  -2.611  1.00 42.92 ? 1959 HOH A O   1 
HETATM 9438 O  O   . HOH I 8 .    ? 68.251 49.382  -0.934  1.00 24.38 ? 1960 HOH A O   1 
HETATM 9439 O  O   . HOH I 8 .    ? 66.044 50.530  0.324   1.00 39.95 ? 1961 HOH A O   1 
HETATM 9440 O  O   . HOH I 8 .    ? 67.408 52.786  1.376   1.00 40.82 ? 1962 HOH A O   1 
HETATM 9441 O  O   . HOH I 8 .    ? 67.133 55.401  0.954   1.00 19.93 ? 1963 HOH A O   1 
HETATM 9442 O  O   . HOH I 8 .    ? 69.951 55.317  1.646   1.00 45.17 ? 1964 HOH A O   1 
HETATM 9443 O  O   . HOH I 8 .    ? 63.569 52.042  -0.268  1.00 28.77 ? 1965 HOH A O   1 
HETATM 9444 O  O   . HOH I 8 .    ? 61.644 59.483  5.294   1.00 48.58 ? 1966 HOH A O   1 
HETATM 9445 O  O   . HOH I 8 .    ? 58.667 60.519  5.923   1.00 32.73 ? 1967 HOH A O   1 
HETATM 9446 O  O   . HOH I 8 .    ? 57.526 58.530  5.444   1.00 21.19 ? 1968 HOH A O   1 
HETATM 9447 O  O   . HOH I 8 .    ? 55.322 59.119  3.870   1.00 15.01 ? 1969 HOH A O   1 
HETATM 9448 O  O   . HOH I 8 .    ? 56.997 61.063  1.617   1.00 15.72 ? 1970 HOH A O   1 
HETATM 9449 O  O   . HOH I 8 .    ? 52.817 58.910  -1.732  1.00 12.47 ? 1971 HOH A O   1 
HETATM 9450 O  O   . HOH I 8 .    ? 57.699 62.454  7.831   1.00 24.05 ? 1972 HOH A O   1 
HETATM 9451 O  O   . HOH I 8 .    ? 56.522 64.496  8.895   1.00 47.17 ? 1973 HOH A O   1 
HETATM 9452 O  O   . HOH I 8 .    ? 52.497 71.049  5.870   1.00 28.49 ? 1974 HOH A O   1 
HETATM 9453 O  O   . HOH I 8 .    ? 52.500 73.208  4.063   1.00 33.33 ? 1975 HOH A O   1 
HETATM 9454 O  O   . HOH I 8 .    ? 56.456 71.271  3.834   1.00 37.17 ? 1976 HOH A O   1 
HETATM 9455 O  O   . HOH I 8 .    ? 54.089 80.365  0.813   1.00 44.53 ? 1977 HOH A O   1 
HETATM 9456 O  O   . HOH I 8 .    ? 51.703 80.146  0.769   1.00 36.58 ? 1978 HOH A O   1 
HETATM 9457 O  O   . HOH I 8 .    ? 51.343 79.296  -1.739  1.00 21.66 ? 1979 HOH A O   1 
HETATM 9458 O  O   . HOH I 8 .    ? 50.345 81.214  -2.966  1.00 38.97 ? 1980 HOH A O   1 
HETATM 9459 O  O   . HOH I 8 .    ? 48.171 80.351  -4.221  1.00 38.20 ? 1981 HOH A O   1 
HETATM 9460 O  O   . HOH I 8 .    ? 41.103 81.829  -3.669  1.00 31.19 ? 1982 HOH A O   1 
HETATM 9461 O  O   . HOH I 8 .    ? 38.822 80.290  -3.225  1.00 33.41 ? 1983 HOH A O   1 
HETATM 9462 O  O   . HOH I 8 .    ? 37.679 80.507  -0.685  1.00 20.38 ? 1984 HOH A O   1 
HETATM 9463 O  O   . HOH I 8 .    ? 38.125 83.279  -1.113  1.00 30.31 ? 1985 HOH A O   1 
HETATM 9464 O  O   . HOH I 8 .    ? 37.267 83.658  -4.141  1.00 28.32 ? 1986 HOH A O   1 
HETATM 9465 O  O   . HOH I 8 .    ? 35.289 84.967  -0.695  1.00 35.87 ? 1987 HOH A O   1 
HETATM 9466 O  O   . HOH I 8 .    ? 32.852 84.316  0.393   1.00 28.76 ? 1988 HOH A O   1 
HETATM 9467 O  O   . HOH I 8 .    ? 31.323 81.686  0.609   1.00 17.65 ? 1989 HOH A O   1 
HETATM 9468 O  O   . HOH I 8 .    ? 29.862 83.080  2.473   1.00 20.67 ? 1990 HOH A O   1 
HETATM 9469 O  O   . HOH I 8 .    ? 27.489 82.356  3.303   1.00 31.24 ? 1991 HOH A O   1 
HETATM 9470 O  O   . HOH I 8 .    ? 24.711 84.027  2.403   1.00 31.90 ? 1992 HOH A O   1 
HETATM 9471 O  O   . HOH I 8 .    ? 58.974 77.989  0.515   1.00 40.48 ? 1993 HOH A O   1 
HETATM 9472 O  O   . HOH I 8 .    ? 55.550 78.543  2.258   1.00 51.30 ? 1994 HOH A O   1 
HETATM 9473 O  O   . HOH I 8 .    ? 18.194 84.429  -4.974  1.00 40.42 ? 1995 HOH A O   1 
HETATM 9474 O  O   . HOH I 8 .    ? 16.681 82.107  -5.101  1.00 31.90 ? 1996 HOH A O   1 
HETATM 9475 O  O   . HOH I 8 .    ? 17.229 80.674  -7.415  1.00 22.44 ? 1997 HOH A O   1 
HETATM 9476 O  O   . HOH I 8 .    ? 18.475 84.376  -8.353  1.00 49.39 ? 1998 HOH A O   1 
HETATM 9477 O  O   . HOH I 8 .    ? 21.008 83.868  -12.473 1.00 35.87 ? 1999 HOH A O   1 
HETATM 9478 O  O   . HOH I 8 .    ? 18.903 80.561  -11.747 1.00 31.83 ? 2000 HOH A O   1 
HETATM 9479 O  O   . HOH I 8 .    ? 15.511 76.998  -13.615 1.00 31.14 ? 2001 HOH A O   1 
HETATM 9480 O  O   . HOH I 8 .    ? 15.875 75.226  -11.719 1.00 19.38 ? 2002 HOH A O   1 
HETATM 9481 O  O   . HOH I 8 .    ? 12.334 75.100  -13.375 1.00 29.49 ? 2003 HOH A O   1 
HETATM 9482 O  O   . HOH I 8 .    ? 13.639 70.010  -9.574  1.00 26.13 ? 2004 HOH A O   1 
HETATM 9483 O  O   . HOH I 8 .    ? 14.117 68.219  -7.789  1.00 18.37 ? 2005 HOH A O   1 
HETATM 9484 O  O   . HOH I 8 .    ? 12.712 66.331  -9.624  1.00 19.56 ? 2006 HOH A O   1 
HETATM 9485 O  O   . HOH I 8 .    ? 12.379 68.407  -11.462 1.00 20.91 ? 2007 HOH A O   1 
HETATM 9486 O  O   . HOH I 8 .    ? 12.771 67.032  -13.635 1.00 20.20 ? 2008 HOH A O   1 
HETATM 9487 O  O   . HOH I 8 .    ? 10.602 64.619  -10.300 1.00 34.83 ? 2009 HOH A O   1 
HETATM 9488 O  O   . HOH I 8 .    ? 11.612 70.823  -7.693  1.00 33.91 ? 2010 HOH A O   1 
HETATM 9489 O  O   . HOH I 8 .    ? 9.742  73.275  -2.584  1.00 45.16 ? 2011 HOH A O   1 
HETATM 9490 O  O   . HOH I 8 .    ? 10.667 77.233  -5.056  1.00 35.80 ? 2012 HOH A O   1 
HETATM 9491 O  O   . HOH I 8 .    ? 8.005  81.385  -4.350  1.00 34.40 ? 2013 HOH A O   1 
HETATM 9492 O  O   . HOH I 8 .    ? 12.035 81.871  0.995   1.00 38.46 ? 2014 HOH A O   1 
HETATM 9493 O  O   . HOH I 8 .    ? 16.119 80.225  -1.072  1.00 50.48 ? 2015 HOH A O   1 
HETATM 9494 O  O   . HOH I 8 .    ? 21.368 78.524  -1.399  1.00 16.41 ? 2016 HOH A O   1 
HETATM 9495 O  O   . HOH I 8 .    ? 24.068 82.965  -3.889  1.00 40.00 ? 2017 HOH A O   1 
HETATM 9496 O  O   . HOH I 8 .    ? 26.777 87.831  -3.889  1.00 41.16 ? 2018 HOH A O   1 
HETATM 9497 O  O   . HOH I 8 .    ? 23.906 89.580  -6.660  1.00 45.35 ? 2019 HOH A O   1 
HETATM 9498 O  O   . HOH I 8 .    ? 22.173 87.838  -7.691  1.00 47.10 ? 2020 HOH A O   1 
HETATM 9499 O  O   . HOH I 8 .    ? 25.034 91.888  -8.218  1.00 55.13 ? 2021 HOH A O   1 
HETATM 9500 O  O   . HOH I 8 .    ? 27.341 88.577  -12.406 1.00 31.78 ? 2022 HOH A O   1 
HETATM 9501 O  O   . HOH I 8 .    ? 29.477 89.997  -12.352 1.00 52.72 ? 2023 HOH A O   1 
HETATM 9502 O  O   . HOH I 8 .    ? 34.177 87.115  -10.471 1.00 31.82 ? 2024 HOH A O   1 
HETATM 9503 O  O   . HOH I 8 .    ? 35.553 86.052  -8.064  1.00 31.33 ? 2025 HOH A O   1 
HETATM 9504 O  O   . HOH I 8 .    ? 35.633 88.451  -6.298  1.00 43.15 ? 2026 HOH A O   1 
HETATM 9505 O  O   . HOH I 8 .    ? 32.826 85.370  -5.616  1.00 17.79 ? 2027 HOH A O   1 
HETATM 9506 O  O   . HOH I 8 .    ? 31.555 87.638  -6.605  1.00 40.39 ? 2028 HOH A O   1 
HETATM 9507 O  O   . HOH I 8 .    ? 32.153 85.233  -8.516  1.00 18.34 ? 2029 HOH A O   1 
HETATM 9508 O  O   . HOH I 8 .    ? 33.559 83.599  -10.376 1.00 15.50 ? 2030 HOH A O   1 
HETATM 9509 O  O   . HOH I 8 .    ? 32.792 81.088  -11.690 1.00 10.39 ? 2031 HOH A O   1 
HETATM 9510 O  O   . HOH I 8 .    ? 34.545 79.166  -9.137  1.00 11.31 ? 2032 HOH A O   1 
HETATM 9511 O  O   . HOH I 8 .    ? 35.861 77.549  -7.330  1.00 12.21 ? 2033 HOH A O   1 
HETATM 9512 O  O   . HOH I 8 .    ? 36.336 79.248  -5.043  1.00 20.42 ? 2034 HOH A O   1 
HETATM 9513 O  O   . HOH I 8 .    ? 33.374 78.633  -5.136  1.00 11.79 ? 2035 HOH A O   1 
HETATM 9514 O  O   . HOH I 8 .    ? 31.393 76.766  -6.341  1.00 10.45 ? 2036 HOH A O   1 
HETATM 9515 O  O   . HOH I 8 .    ? 37.100 71.903  -4.544  1.00 7.98  ? 2037 HOH A O   1 
HETATM 9516 O  O   . HOH I 8 .    ? 37.897 73.322  -2.240  1.00 10.15 ? 2038 HOH A O   1 
HETATM 9517 O  O   . HOH I 8 .    ? 36.645 72.657  0.294   1.00 8.47  ? 2039 HOH A O   1 
HETATM 9518 O  O   . HOH I 8 .    ? 43.575 73.235  5.782   1.00 11.11 ? 2040 HOH A O   1 
HETATM 9519 O  O   . HOH I 8 .    ? 46.125 70.945  0.064   1.00 14.42 ? 2041 HOH A O   1 
HETATM 9520 O  O   . HOH I 8 .    ? 42.053 63.495  -7.153  1.00 6.45  ? 2042 HOH A O   1 
HETATM 9521 O  O   . HOH I 8 .    ? 39.300 64.822  -14.712 1.00 9.98  ? 2043 HOH A O   1 
HETATM 9522 O  O   . HOH I 8 .    ? 39.270 62.871  -19.114 1.00 7.77  ? 2044 HOH A O   1 
HETATM 9523 O  O   . HOH I 8 .    ? 39.698 58.890  -18.019 1.00 21.02 ? 2045 HOH A O   1 
HETATM 9524 O  O   . HOH I 8 .    ? 41.711 58.672  -15.996 1.00 13.60 ? 2046 HOH A O   1 
HETATM 9525 O  O   . HOH I 8 .    ? 44.558 58.772  -15.915 1.00 15.33 ? 2047 HOH A O   1 
HETATM 9526 O  O   . HOH I 8 .    ? 44.563 56.112  -15.345 1.00 16.80 ? 2048 HOH A O   1 
HETATM 9527 O  O   . HOH I 8 .    ? 47.335 55.776  -15.435 1.00 16.56 ? 2049 HOH A O   1 
HETATM 9528 O  O   . HOH I 8 .    ? 45.046 55.062  -18.053 1.00 25.68 ? 2050 HOH A O   1 
HETATM 9529 O  O   . HOH I 8 .    ? 46.011 52.761  -19.075 1.00 16.49 ? 2051 HOH A O   1 
HETATM 9530 O  O   . HOH I 8 .    ? 46.900 53.827  -21.450 1.00 24.99 ? 2052 HOH A O   1 
HETATM 9531 O  O   . HOH I 8 .    ? 48.766 54.910  -22.713 1.00 22.45 ? 2053 HOH A O   1 
HETATM 9532 O  O   . HOH I 8 .    ? 51.320 53.323  -23.893 1.00 12.85 ? 2054 HOH A O   1 
HETATM 9533 O  O   . HOH I 8 .    ? 51.138 52.807  -28.526 1.00 20.45 ? 2055 HOH A O   1 
HETATM 9534 O  O   . HOH I 8 .    ? 49.883 55.163  -29.014 1.00 19.15 ? 2056 HOH A O   1 
HETATM 9535 O  O   . HOH I 8 .    ? 52.161 56.496  -30.205 1.00 25.27 ? 2057 HOH A O   1 
HETATM 9536 O  O   . HOH I 8 .    ? 53.156 55.078  -31.890 1.00 32.21 ? 2058 HOH A O   1 
HETATM 9537 O  O   . HOH I 8 .    ? 53.378 53.411  -30.007 1.00 26.85 ? 2059 HOH A O   1 
HETATM 9538 O  O   . HOH I 8 .    ? 56.451 50.024  -30.053 1.00 33.74 ? 2060 HOH A O   1 
HETATM 9539 O  O   . HOH I 8 .    ? 49.828 47.048  -30.413 1.00 39.32 ? 2061 HOH A O   1 
HETATM 9540 O  O   A HOH I 8 .    ? 48.983 51.016  -29.742 0.50 22.15 ? 2062 HOH A O   1 
HETATM 9541 O  O   B HOH I 8 .    ? 48.699 49.840  -29.205 0.50 16.37 ? 2062 HOH A O   1 
HETATM 9542 O  O   . HOH I 8 .    ? 47.823 49.574  -31.368 1.00 40.71 ? 2063 HOH A O   1 
HETATM 9543 O  O   . HOH I 8 .    ? 47.840 53.580  -31.141 1.00 50.97 ? 2064 HOH A O   1 
HETATM 9544 O  O   . HOH I 8 .    ? 45.649 56.218  -32.538 1.00 45.36 ? 2065 HOH A O   1 
HETATM 9545 O  O   . HOH I 8 .    ? 47.640 57.872  -32.166 1.00 42.77 ? 2066 HOH A O   1 
HETATM 9546 O  O   . HOH I 8 .    ? 50.125 58.414  -30.743 1.00 40.42 ? 2067 HOH A O   1 
HETATM 9547 O  O   . HOH I 8 .    ? 49.115 59.301  -28.558 1.00 31.69 ? 2068 HOH A O   1 
HETATM 9548 O  O   . HOH I 8 .    ? 48.212 61.743  -28.361 1.00 32.88 ? 2069 HOH A O   1 
HETATM 9549 O  O   . HOH I 8 .    ? 46.061 61.379  -29.879 1.00 40.87 ? 2070 HOH A O   1 
HETATM 9550 O  O   . HOH I 8 .    ? 43.697 62.703  -28.368 1.00 21.77 ? 2071 HOH A O   1 
HETATM 9551 O  O   . HOH I 8 .    ? 41.750 61.195  -29.565 1.00 18.58 ? 2072 HOH A O   1 
HETATM 9552 O  O   . HOH I 8 .    ? 42.860 59.350  -31.392 1.00 25.55 ? 2073 HOH A O   1 
HETATM 9553 O  O   . HOH I 8 .    ? 42.929 56.690  -31.461 1.00 25.77 ? 2074 HOH A O   1 
HETATM 9554 O  O   . HOH I 8 .    ? 40.808 55.830  -33.258 1.00 28.44 ? 2075 HOH A O   1 
HETATM 9555 O  O   . HOH I 8 .    ? 38.585 55.103  -31.592 1.00 16.31 ? 2076 HOH A O   1 
HETATM 9556 O  O   . HOH I 8 .    ? 37.209 52.656  -32.288 1.00 30.05 ? 2077 HOH A O   1 
HETATM 9557 O  O   . HOH I 8 .    ? 38.571 51.394  -29.797 1.00 26.03 ? 2078 HOH A O   1 
HETATM 9558 O  O   . HOH I 8 .    ? 43.822 54.845  -26.756 1.00 29.26 ? 2079 HOH A O   1 
HETATM 9559 O  O   . HOH I 8 .    ? 46.909 55.765  -25.471 1.00 18.32 ? 2080 HOH A O   1 
HETATM 9560 O  O   . HOH I 8 .    ? 47.875 59.361  -25.638 1.00 15.29 ? 2081 HOH A O   1 
HETATM 9561 O  O   . HOH I 8 .    ? 47.185 62.093  -25.580 1.00 23.14 ? 2082 HOH A O   1 
HETATM 9562 O  O   . HOH I 8 .    ? 48.697 64.756  -25.948 1.00 65.88 ? 2083 HOH A O   1 
HETATM 9563 O  O   . HOH I 8 .    ? 48.398 64.476  -28.574 1.00 34.05 ? 2084 HOH A O   1 
HETATM 9564 O  O   . HOH I 8 .    ? 47.507 68.222  -30.807 1.00 17.67 ? 2085 HOH A O   1 
HETATM 9565 O  O   . HOH I 8 .    ? 47.375 70.077  -28.596 1.00 27.09 ? 2086 HOH A O   1 
HETATM 9566 O  O   . HOH I 8 .    ? 45.948 68.134  -26.945 1.00 16.58 ? 2087 HOH A O   1 
HETATM 9567 O  O   . HOH I 8 .    ? 47.201 67.839  -24.566 1.00 23.66 ? 2088 HOH A O   1 
HETATM 9568 O  O   . HOH I 8 .    ? 47.176 70.754  -24.740 1.00 35.68 ? 2089 HOH A O   1 
HETATM 9569 O  O   . HOH I 8 .    ? 45.145 71.974  -25.805 1.00 40.19 ? 2090 HOH A O   1 
HETATM 9570 O  O   . HOH I 8 .    ? 43.542 68.306  -25.278 1.00 14.05 ? 2091 HOH A O   1 
HETATM 9571 O  O   . HOH I 8 .    ? 43.531 66.784  -32.283 1.00 26.53 ? 2092 HOH A O   1 
HETATM 9572 O  O   . HOH I 8 .    ? 41.281 68.266  -32.591 1.00 18.46 ? 2093 HOH A O   1 
HETATM 9573 O  O   . HOH I 8 .    ? 39.451 69.072  -35.407 1.00 17.00 ? 2094 HOH A O   1 
HETATM 9574 O  O   . HOH I 8 .    ? 38.702 69.157  -38.163 1.00 18.99 ? 2095 HOH A O   1 
HETATM 9575 O  O   . HOH I 8 .    ? 43.109 65.441  -39.344 1.00 33.61 ? 2096 HOH A O   1 
HETATM 9576 O  O   . HOH I 8 .    ? 45.135 66.498  -34.571 1.00 40.36 ? 2097 HOH A O   1 
HETATM 9577 O  O   . HOH I 8 .    ? 45.209 63.866  -34.511 1.00 46.67 ? 2098 HOH A O   1 
HETATM 9578 O  O   . HOH I 8 .    ? 43.375 63.804  -32.495 1.00 30.75 ? 2099 HOH A O   1 
HETATM 9579 O  O   . HOH I 8 .    ? 41.055 62.892  -31.730 1.00 23.11 ? 2100 HOH A O   1 
HETATM 9580 O  O   . HOH I 8 .    ? 45.158 57.335  -34.884 1.00 50.78 ? 2101 HOH A O   1 
HETATM 9581 O  O   . HOH I 8 .    ? 50.545 61.237  -30.942 1.00 22.72 ? 2102 HOH A O   1 
HETATM 9582 O  O   . HOH I 8 .    ? 53.061 59.298  -32.491 1.00 43.42 ? 2103 HOH A O   1 
HETATM 9583 O  O   . HOH I 8 .    ? 55.210 58.854  -34.175 1.00 35.17 ? 2104 HOH A O   1 
HETATM 9584 O  O   . HOH I 8 .    ? 56.212 65.187  -36.085 1.00 24.81 ? 2105 HOH A O   1 
HETATM 9585 O  O   . HOH I 8 .    ? 56.932 67.629  -35.465 1.00 21.26 ? 2106 HOH A O   1 
HETATM 9586 O  O   . HOH I 8 .    ? 57.754 68.359  -37.860 1.00 39.21 ? 2107 HOH A O   1 
HETATM 9587 O  O   . HOH I 8 .    ? 55.491 69.107  -37.703 1.00 27.04 ? 2108 HOH A O   1 
HETATM 9588 O  O   . HOH I 8 .    ? 56.917 70.006  -39.739 1.00 31.21 ? 2109 HOH A O   1 
HETATM 9589 O  O   . HOH I 8 .    ? 53.995 71.219  -36.862 1.00 13.41 ? 2110 HOH A O   1 
HETATM 9590 O  O   . HOH I 8 .    ? 51.753 70.086  -38.138 1.00 28.87 ? 2111 HOH A O   1 
HETATM 9591 O  O   . HOH I 8 .    ? 49.079 69.106  -36.799 1.00 29.76 ? 2112 HOH A O   1 
HETATM 9592 O  O   . HOH I 8 .    ? 46.652 70.264  -36.675 1.00 17.61 ? 2113 HOH A O   1 
HETATM 9593 O  O   . HOH I 8 .    ? 46.267 70.269  -39.933 1.00 37.29 ? 2114 HOH A O   1 
HETATM 9594 O  O   . HOH I 8 .    ? 46.621 69.716  -43.141 1.00 58.75 ? 2115 HOH A O   1 
HETATM 9595 O  O   . HOH I 8 .    ? 44.735 72.178  -44.389 1.00 36.79 ? 2116 HOH A O   1 
HETATM 9596 O  O   . HOH I 8 .    ? 43.880 72.520  -41.919 1.00 21.26 ? 2117 HOH A O   1 
HETATM 9597 O  O   . HOH I 8 .    ? 42.243 74.664  -41.408 1.00 26.26 ? 2118 HOH A O   1 
HETATM 9598 O  O   . HOH I 8 .    ? 39.805 75.539  -40.292 1.00 18.48 ? 2119 HOH A O   1 
HETATM 9599 O  O   . HOH I 8 .    ? 37.733 75.512  -42.275 1.00 22.68 ? 2120 HOH A O   1 
HETATM 9600 O  O   . HOH I 8 .    ? 35.859 77.315  -42.995 1.00 34.25 ? 2121 HOH A O   1 
HETATM 9601 O  O   . HOH I 8 .    ? 34.064 73.878  -43.755 1.00 44.72 ? 2122 HOH A O   1 
HETATM 9602 O  O   . HOH I 8 .    ? 28.113 68.147  -46.952 1.00 51.33 ? 2123 HOH A O   1 
HETATM 9603 O  O   . HOH I 8 .    ? 23.994 65.258  -43.625 1.00 35.75 ? 2124 HOH A O   1 
HETATM 9604 O  O   . HOH I 8 .    ? 21.919 63.154  -43.085 1.00 45.14 ? 2125 HOH A O   1 
HETATM 9605 O  O   . HOH I 8 .    ? 22.283 60.680  -43.867 1.00 33.84 ? 2126 HOH A O   1 
HETATM 9606 O  O   . HOH I 8 .    ? 24.024 58.497  -43.931 1.00 43.63 ? 2127 HOH A O   1 
HETATM 9607 O  O   . HOH I 8 .    ? 24.628 60.475  -45.930 1.00 47.30 ? 2128 HOH A O   1 
HETATM 9608 O  O   . HOH I 8 .    ? 25.960 57.205  -41.956 1.00 52.61 ? 2129 HOH A O   1 
HETATM 9609 O  O   . HOH I 8 .    ? 28.574 59.825  -39.056 1.00 31.11 ? 2130 HOH A O   1 
HETATM 9610 O  O   . HOH I 8 .    ? 29.149 62.223  -39.763 1.00 25.96 ? 2131 HOH A O   1 
HETATM 9611 O  O   . HOH I 8 .    ? 31.280 58.391  -40.326 1.00 39.19 ? 2132 HOH A O   1 
HETATM 9612 O  O   . HOH I 8 .    ? 33.324 57.019  -38.882 1.00 38.68 ? 2133 HOH A O   1 
HETATM 9613 O  O   . HOH I 8 .    ? 32.186 58.531  -28.453 1.00 13.41 ? 2134 HOH A O   1 
HETATM 9614 O  O   . HOH I 8 .    ? 34.136 56.257  -26.235 1.00 11.08 ? 2135 HOH A O   1 
HETATM 9615 O  O   . HOH I 8 .    ? 31.344 49.904  -23.968 1.00 12.19 ? 2136 HOH A O   1 
HETATM 9616 O  O   . HOH I 8 .    ? 28.728 49.643  -24.339 1.00 16.49 ? 2137 HOH A O   1 
HETATM 9617 O  O   . HOH I 8 .    ? 27.036 47.536  -23.838 1.00 32.51 ? 2138 HOH A O   1 
HETATM 9618 O  O   . HOH I 8 .    ? 27.566 48.426  -21.617 1.00 15.75 ? 2139 HOH A O   1 
HETATM 9619 O  O   . HOH I 8 .    ? 25.322 46.881  -20.913 1.00 23.61 ? 2140 HOH A O   1 
HETATM 9620 O  O   . HOH I 8 .    ? 21.481 46.751  -17.513 1.00 26.81 ? 2141 HOH A O   1 
HETATM 9621 O  O   . HOH I 8 .    ? 23.656 45.964  -15.846 1.00 19.55 ? 2142 HOH A O   1 
HETATM 9622 O  O   . HOH I 8 .    ? 22.571 45.420  -13.365 1.00 16.21 ? 2143 HOH A O   1 
HETATM 9623 O  O   . HOH I 8 .    ? 21.999 42.708  -13.179 1.00 22.42 ? 2144 HOH A O   1 
HETATM 9624 O  O   . HOH I 8 .    ? 24.274 42.026  -14.531 1.00 22.73 ? 2145 HOH A O   1 
HETATM 9625 O  O   . HOH I 8 .    ? 26.695 41.626  -13.157 1.00 12.82 ? 2146 HOH A O   1 
HETATM 9626 O  O   . HOH I 8 .    ? 28.835 42.774  -11.882 1.00 11.00 ? 2147 HOH A O   1 
HETATM 9627 O  O   . HOH I 8 .    ? 24.456 39.060  -11.396 1.00 23.27 ? 2148 HOH A O   1 
HETATM 9628 O  O   . HOH I 8 .    ? 23.798 37.320  -13.358 1.00 36.97 ? 2149 HOH A O   1 
HETATM 9629 O  O   . HOH I 8 .    ? 21.545 37.414  -12.040 1.00 49.71 ? 2150 HOH A O   1 
HETATM 9630 O  O   . HOH I 8 .    ? 22.761 36.890  -9.699  1.00 41.71 ? 2151 HOH A O   1 
HETATM 9631 O  O   . HOH I 8 .    ? 25.413 34.592  -7.149  1.00 42.57 ? 2152 HOH A O   1 
HETATM 9632 O  O   . HOH I 8 .    ? 28.074 35.370  -6.690  1.00 24.32 ? 2153 HOH A O   1 
HETATM 9633 O  O   . HOH I 8 .    ? 30.331 33.481  -6.153  1.00 39.45 ? 2154 HOH A O   1 
HETATM 9634 O  O   . HOH I 8 .    ? 32.084 34.408  -3.209  1.00 20.26 ? 2155 HOH A O   1 
HETATM 9635 O  O   . HOH I 8 .    ? 29.993 34.252  -1.505  1.00 27.70 ? 2156 HOH A O   1 
HETATM 9636 O  O   . HOH I 8 .    ? 27.130 33.956  -3.195  1.00 35.82 ? 2157 HOH A O   1 
HETATM 9637 O  O   . HOH I 8 .    ? 21.452 35.484  -5.228  1.00 33.68 ? 2158 HOH A O   1 
HETATM 9638 O  O   . HOH I 8 .    ? 20.325 37.551  -6.166  1.00 43.56 ? 2159 HOH A O   1 
HETATM 9639 O  O   . HOH I 8 .    ? 23.074 39.227  -15.500 1.00 27.99 ? 2160 HOH A O   1 
HETATM 9640 O  O   . HOH I 8 .    ? 23.593 37.688  -17.591 1.00 38.39 ? 2161 HOH A O   1 
HETATM 9641 O  O   . HOH I 8 .    ? 25.583 36.267  -15.307 1.00 34.63 ? 2162 HOH A O   1 
HETATM 9642 O  O   . HOH I 8 .    ? 29.413 35.041  -16.408 1.00 29.13 ? 2163 HOH A O   1 
HETATM 9643 O  O   . HOH I 8 .    ? 29.512 34.396  -19.200 1.00 45.22 ? 2164 HOH A O   1 
HETATM 9644 O  O   . HOH I 8 .    ? 27.632 36.450  -19.604 1.00 26.34 ? 2165 HOH A O   1 
HETATM 9645 O  O   . HOH I 8 .    ? 27.785 38.682  -22.501 1.00 29.34 ? 2166 HOH A O   1 
HETATM 9646 O  O   . HOH I 8 .    ? 27.271 39.750  -24.788 1.00 43.84 ? 2167 HOH A O   1 
HETATM 9647 O  O   . HOH I 8 .    ? 29.485 41.054  -25.538 1.00 20.46 ? 2168 HOH A O   1 
HETATM 9648 O  O   . HOH I 8 .    ? 30.277 39.059  -27.074 1.00 23.29 ? 2169 HOH A O   1 
HETATM 9649 O  O   . HOH I 8 .    ? 28.462 44.174  -29.589 1.00 32.71 ? 2170 HOH A O   1 
HETATM 9650 O  O   . HOH I 8 .    ? 26.427 44.240  -27.201 1.00 30.26 ? 2171 HOH A O   1 
HETATM 9651 O  O   . HOH I 8 .    ? 28.182 47.033  -31.436 1.00 29.54 ? 2172 HOH A O   1 
HETATM 9652 O  O   . HOH I 8 .    ? 35.607 45.162  -27.355 1.00 17.32 ? 2173 HOH A O   1 
HETATM 9653 O  O   . HOH I 8 .    ? 37.359 45.241  -25.360 1.00 24.37 ? 2174 HOH A O   1 
HETATM 9654 O  O   . HOH I 8 .    ? 39.819 45.287  -26.358 1.00 34.81 ? 2175 HOH A O   1 
HETATM 9655 O  O   . HOH I 8 .    ? 37.002 41.257  -24.494 1.00 28.94 ? 2176 HOH A O   1 
HETATM 9656 O  O   . HOH I 8 .    ? 35.811 41.692  -26.562 1.00 43.12 ? 2177 HOH A O   1 
HETATM 9657 O  O   . HOH I 8 .    ? 38.303 39.555  -26.555 1.00 47.00 ? 2178 HOH A O   1 
HETATM 9658 O  O   . HOH I 8 .    ? 38.695 42.208  -22.045 1.00 28.27 ? 2179 HOH A O   1 
HETATM 9659 O  O   . HOH I 8 .    ? 40.960 40.720  -21.405 1.00 27.43 ? 2180 HOH A O   1 
HETATM 9660 O  O   . HOH I 8 .    ? 41.612 41.149  -17.451 1.00 19.99 ? 2181 HOH A O   1 
HETATM 9661 O  O   . HOH I 8 .    ? 42.619 39.396  -15.723 1.00 28.09 ? 2182 HOH A O   1 
HETATM 9662 O  O   . HOH I 8 .    ? 40.887 42.200  -15.107 1.00 50.59 ? 2183 HOH A O   1 
HETATM 9663 O  O   . HOH I 8 .    ? 39.958 42.750  -12.650 1.00 47.35 ? 2184 HOH A O   1 
HETATM 9664 O  O   . HOH I 8 .    ? 42.212 40.404  -9.724  1.00 42.28 ? 2185 HOH A O   1 
HETATM 9665 O  O   . HOH I 8 .    ? 44.306 38.175  -8.714  1.00 54.23 ? 2186 HOH A O   1 
HETATM 9666 O  O   . HOH I 8 .    ? 43.246 38.507  -6.135  1.00 35.84 ? 2187 HOH A O   1 
HETATM 9667 O  O   . HOH I 8 .    ? 39.879 38.806  -3.364  1.00 22.19 ? 2188 HOH A O   1 
HETATM 9668 O  O   . HOH I 8 .    ? 36.289 36.310  -1.901  1.00 52.72 ? 2189 HOH A O   1 
HETATM 9669 O  O   . HOH I 8 .    ? 35.957 36.034  -4.446  1.00 19.24 ? 2190 HOH A O   1 
HETATM 9670 O  O   . HOH I 8 .    ? 35.779 33.559  -3.516  1.00 58.18 ? 2191 HOH A O   1 
HETATM 9671 O  O   . HOH I 8 .    ? 36.277 33.737  -6.135  1.00 44.37 ? 2192 HOH A O   1 
HETATM 9672 O  O   . HOH I 8 .    ? 33.233 36.645  -4.327  1.00 15.69 ? 2193 HOH A O   1 
HETATM 9673 O  O   . HOH I 8 .    ? 32.349 39.151  -4.843  1.00 11.10 ? 2194 HOH A O   1 
HETATM 9674 O  O   . HOH I 8 .    ? 30.387 34.772  -9.553  1.00 34.20 ? 2195 HOH A O   1 
HETATM 9675 O  O   . HOH I 8 .    ? 30.273 35.163  -12.368 1.00 22.10 ? 2196 HOH A O   1 
HETATM 9676 O  O   . HOH I 8 .    ? 32.738 32.399  -11.605 1.00 46.13 ? 2197 HOH A O   1 
HETATM 9677 O  O   . HOH I 8 .    ? 34.199 32.763  -13.683 1.00 47.61 ? 2198 HOH A O   1 
HETATM 9678 O  O   . HOH I 8 .    ? 36.945 34.945  -15.842 1.00 34.82 ? 2199 HOH A O   1 
HETATM 9679 O  O   . HOH I 8 .    ? 35.984 36.272  -18.133 1.00 49.59 ? 2200 HOH A O   1 
HETATM 9680 O  O   . HOH I 8 .    ? 37.869 35.154  -19.416 1.00 46.52 ? 2201 HOH A O   1 
HETATM 9681 O  O   . HOH I 8 .    ? 35.623 34.182  -21.348 1.00 46.20 ? 2202 HOH A O   1 
HETATM 9682 O  O   . HOH I 8 .    ? 36.341 35.333  -23.618 1.00 34.74 ? 2203 HOH A O   1 
HETATM 9683 O  O   . HOH I 8 .    ? 33.548 38.796  -19.449 1.00 30.12 ? 2204 HOH A O   1 
HETATM 9684 O  O   . HOH I 8 .    ? 32.994 41.041  -17.600 1.00 21.88 ? 2205 HOH A O   1 
HETATM 9685 O  O   . HOH I 8 .    ? 35.746 38.944  -16.035 1.00 31.13 ? 2206 HOH A O   1 
HETATM 9686 O  O   . HOH I 8 .    ? 39.444 38.260  -10.777 1.00 32.95 ? 2207 HOH A O   1 
HETATM 9687 O  O   . HOH I 8 .    ? 41.094 36.564  -12.660 1.00 49.81 ? 2208 HOH A O   1 
HETATM 9688 O  O   . HOH I 8 .    ? 41.436 44.755  -6.820  1.00 13.84 ? 2209 HOH A O   1 
HETATM 9689 O  O   . HOH I 8 .    ? 36.739 44.939  -5.404  1.00 10.03 ? 2210 HOH A O   1 
HETATM 9690 O  O   . HOH I 8 .    ? 31.738 47.036  -8.008  1.00 7.96  ? 2211 HOH A O   1 
HETATM 9691 O  O   . HOH I 8 .    ? 33.488 48.139  -10.079 1.00 8.97  ? 2212 HOH A O   1 
HETATM 9692 O  O   . HOH I 8 .    ? 34.999 48.231  -16.398 1.00 38.47 ? 2213 HOH A O   1 
HETATM 9693 O  O   . HOH I 8 .    ? 35.170 50.523  -17.503 1.00 13.34 ? 2214 HOH A O   1 
HETATM 9694 O  O   . HOH I 8 .    ? 37.594 51.481  -18.472 1.00 17.73 ? 2215 HOH A O   1 
HETATM 9695 O  O   . HOH I 8 .    ? 37.661 52.100  -21.039 1.00 11.91 ? 2216 HOH A O   1 
HETATM 9696 O  O   . HOH I 8 .    ? 39.694 53.914  -20.725 1.00 14.55 ? 2217 HOH A O   1 
HETATM 9697 O  O   . HOH I 8 .    ? 40.375 56.200  -19.199 1.00 25.13 ? 2218 HOH A O   1 
HETATM 9698 O  O   . HOH I 8 .    ? 42.402 54.757  -17.440 1.00 24.12 ? 2219 HOH A O   1 
HETATM 9699 O  O   . HOH I 8 .    ? 41.093 52.336  -16.902 1.00 12.11 ? 2220 HOH A O   1 
HETATM 9700 O  O   . HOH I 8 .    ? 38.517 54.238  -17.454 1.00 34.09 ? 2221 HOH A O   1 
HETATM 9701 O  O   . HOH I 8 .    ? 42.950 59.410  -18.727 1.00 22.65 ? 2222 HOH A O   1 
HETATM 9702 O  O   . HOH I 8 .    ? 45.739 59.954  -18.242 1.00 12.34 ? 2223 HOH A O   1 
HETATM 9703 O  O   . HOH I 8 .    ? 46.661 57.291  -18.754 1.00 13.81 ? 2224 HOH A O   1 
HETATM 9704 O  O   . HOH I 8 .    ? 58.940 53.766  -22.134 1.00 21.32 ? 2225 HOH A O   1 
HETATM 9705 O  O   . HOH I 8 .    ? 63.209 45.750  -22.304 1.00 59.75 ? 2226 HOH A O   1 
HETATM 9706 O  O   . HOH I 8 .    ? 63.080 42.909  -20.898 1.00 29.40 ? 2227 HOH A O   1 
HETATM 9707 O  O   . HOH I 8 .    ? 66.102 35.223  -13.150 1.00 54.30 ? 2228 HOH A O   1 
HETATM 9708 O  O   . HOH I 8 .    ? 63.955 34.810  -9.714  1.00 53.49 ? 2229 HOH A O   1 
HETATM 9709 O  O   . HOH I 8 .    ? 64.461 39.344  -10.169 1.00 22.01 ? 2230 HOH A O   1 
HETATM 9710 O  O   . HOH I 8 .    ? 67.113 38.445  -9.709  1.00 31.49 ? 2231 HOH A O   1 
HETATM 9711 O  O   . HOH I 8 .    ? 70.761 37.214  -11.279 1.00 44.82 ? 2232 HOH A O   1 
HETATM 9712 O  O   . HOH I 8 .    ? 71.123 39.877  -9.328  1.00 37.70 ? 2233 HOH A O   1 
HETATM 9713 O  O   . HOH I 8 .    ? 73.888 52.826  -5.777  1.00 28.21 ? 2234 HOH A O   1 
HETATM 9714 O  O   . HOH I 8 .    ? 60.203 54.369  14.874  1.00 39.10 ? 2235 HOH A O   1 
HETATM 9715 O  O   A HOH I 8 .    ? 61.020 57.400  15.563  0.50 23.51 ? 2236 HOH A O   1 
HETATM 9716 O  O   B HOH I 8 .    ? 61.662 59.341  14.837  0.50 20.78 ? 2236 HOH A O   1 
HETATM 9717 O  O   . HOH I 8 .    ? 63.345 59.507  16.866  1.00 40.35 ? 2237 HOH A O   1 
HETATM 9718 O  O   . HOH I 8 .    ? 62.299 56.958  17.720  1.00 40.10 ? 2238 HOH A O   1 
HETATM 9719 O  O   . HOH I 8 .    ? 53.403 52.819  26.240  1.00 29.90 ? 2239 HOH A O   1 
HETATM 9720 O  O   . HOH I 8 .    ? 56.594 54.125  29.673  1.00 44.82 ? 2240 HOH A O   1 
HETATM 9721 O  O   . HOH I 8 .    ? 53.931 49.379  29.784  1.00 37.50 ? 2241 HOH A O   1 
HETATM 9722 O  O   . HOH I 8 .    ? 55.177 46.350  30.841  1.00 40.01 ? 2242 HOH A O   1 
HETATM 9723 O  O   . HOH I 8 .    ? 49.543 50.794  32.537  1.00 30.60 ? 2243 HOH A O   1 
HETATM 9724 O  O   . HOH I 8 .    ? 47.051 53.215  35.660  1.00 48.80 ? 2244 HOH A O   1 
HETATM 9725 O  O   . HOH I 8 .    ? 47.019 55.838  36.638  1.00 59.14 ? 2245 HOH A O   1 
HETATM 9726 O  O   . HOH I 8 .    ? 51.979 60.273  28.056  1.00 30.53 ? 2246 HOH A O   1 
HETATM 9727 O  O   . HOH I 8 .    ? 50.903 62.104  26.366  1.00 20.73 ? 2247 HOH A O   1 
HETATM 9728 O  O   . HOH I 8 .    ? 51.960 63.909  24.581  1.00 29.65 ? 2248 HOH A O   1 
HETATM 9729 O  O   . HOH I 8 .    ? 47.826 66.285  26.872  1.00 27.05 ? 2249 HOH A O   1 
HETATM 9730 O  O   . HOH I 8 .    ? 48.113 63.609  28.617  1.00 58.45 ? 2250 HOH A O   1 
HETATM 9731 O  O   . HOH I 8 .    ? 42.082 67.466  29.305  1.00 24.58 ? 2251 HOH A O   1 
HETATM 9732 O  O   . HOH I 8 .    ? 39.834 67.125  31.279  1.00 22.62 ? 2252 HOH A O   1 
HETATM 9733 O  O   . HOH I 8 .    ? 48.807 71.748  25.659  1.00 53.58 ? 2253 HOH A O   1 
HETATM 9734 O  O   . HOH I 8 .    ? 47.916 74.016  25.036  1.00 51.47 ? 2254 HOH A O   1 
HETATM 9735 O  O   . HOH I 8 .    ? 49.311 74.506  23.040  1.00 44.24 ? 2255 HOH A O   1 
HETATM 9736 O  O   . HOH I 8 .    ? 45.954 74.256  22.627  1.00 35.11 ? 2256 HOH A O   1 
HETATM 9737 O  O   . HOH I 8 .    ? 52.119 71.798  21.858  1.00 41.44 ? 2257 HOH A O   1 
HETATM 9738 O  O   . HOH I 8 .    ? 51.112 76.479  14.324  1.00 21.61 ? 2258 HOH A O   1 
HETATM 9739 O  O   . HOH I 8 .    ? 51.667 77.773  11.920  1.00 37.78 ? 2259 HOH A O   1 
HETATM 9740 O  O   . HOH I 8 .    ? 38.737 76.959  17.770  1.00 45.57 ? 2260 HOH A O   1 
HETATM 9741 O  O   . HOH I 8 .    ? 36.169 81.100  6.319   1.00 20.30 ? 2261 HOH A O   1 
HETATM 9742 O  O   . HOH I 8 .    ? 33.267 83.085  4.175   1.00 49.61 ? 2262 HOH A O   1 
HETATM 9743 O  O   . HOH I 8 .    ? 30.856 83.415  4.913   1.00 30.71 ? 2263 HOH A O   1 
HETATM 9744 O  O   . HOH I 8 .    ? 30.115 82.515  7.301   1.00 38.96 ? 2264 HOH A O   1 
HETATM 9745 O  O   . HOH I 8 .    ? 31.920 80.507  7.152   1.00 40.82 ? 2265 HOH A O   1 
HETATM 9746 O  O   . HOH I 8 .    ? 30.241 85.783  1.662   1.00 31.22 ? 2266 HOH A O   1 
HETATM 9747 O  O   . HOH I 8 .    ? 30.979 87.018  -2.802  1.00 35.72 ? 2267 HOH A O   1 
HETATM 9748 O  O   . HOH I 8 .    ? 36.664 88.004  -11.887 1.00 47.44 ? 2268 HOH A O   1 
HETATM 9749 O  O   . HOH I 8 .    ? 36.810 86.471  -15.585 1.00 38.12 ? 2269 HOH A O   1 
HETATM 9750 O  O   . HOH I 8 .    ? 38.416 87.062  -17.473 1.00 41.99 ? 2270 HOH A O   1 
HETATM 9751 O  O   . HOH I 8 .    ? 38.305 86.913  -20.147 1.00 39.53 ? 2271 HOH A O   1 
HETATM 9752 O  O   . HOH I 8 .    ? 40.134 86.026  -21.959 1.00 24.44 ? 2272 HOH A O   1 
HETATM 9753 O  O   . HOH I 8 .    ? 42.640 86.447  -21.198 1.00 41.64 ? 2273 HOH A O   1 
HETATM 9754 O  O   . HOH I 8 .    ? 47.017 83.113  -21.027 1.00 39.55 ? 2274 HOH A O   1 
HETATM 9755 O  O   . HOH I 8 .    ? 46.871 80.616  -22.623 1.00 39.72 ? 2275 HOH A O   1 
HETATM 9756 O  O   . HOH I 8 .    ? 45.631 78.857  -24.231 1.00 44.93 ? 2276 HOH A O   1 
HETATM 9757 O  O   . HOH I 8 .    ? 46.337 77.080  -26.060 1.00 32.00 ? 2277 HOH A O   1 
HETATM 9758 O  O   . HOH I 8 .    ? 44.615 76.276  -28.206 1.00 33.78 ? 2278 HOH A O   1 
HETATM 9759 O  O   . HOH I 8 .    ? 42.940 78.288  -29.813 1.00 32.61 ? 2279 HOH A O   1 
HETATM 9760 O  O   . HOH I 8 .    ? 42.769 79.903  -28.103 1.00 39.22 ? 2280 HOH A O   1 
HETATM 9761 O  O   . HOH I 8 .    ? 42.383 82.404  -29.386 1.00 31.96 ? 2281 HOH A O   1 
HETATM 9762 O  O   . HOH I 8 .    ? 40.642 82.940  -31.212 1.00 25.19 ? 2282 HOH A O   1 
HETATM 9763 O  O   . HOH I 8 .    ? 38.224 81.722  -31.384 1.00 13.16 ? 2283 HOH A O   1 
HETATM 9764 O  O   . HOH I 8 .    ? 39.165 83.269  -27.393 1.00 21.75 ? 2284 HOH A O   1 
HETATM 9765 O  O   . HOH I 8 .    ? 41.491 83.474  -26.356 1.00 35.97 ? 2285 HOH A O   1 
HETATM 9766 O  O   . HOH I 8 .    ? 43.552 80.994  -25.296 1.00 34.83 ? 2286 HOH A O   1 
HETATM 9767 O  O   . HOH I 8 .    ? 45.990 82.050  -25.711 1.00 43.52 ? 2287 HOH A O   1 
HETATM 9768 O  O   . HOH I 8 .    ? 44.491 83.677  -28.195 1.00 28.47 ? 2288 HOH A O   1 
HETATM 9769 O  O   . HOH I 8 .    ? 44.777 82.563  -30.562 1.00 23.45 ? 2289 HOH A O   1 
HETATM 9770 O  O   . HOH I 8 .    ? 42.522 79.802  -31.763 1.00 32.58 ? 2290 HOH A O   1 
HETATM 9771 O  O   . HOH I 8 .    ? 44.701 79.212  -33.309 1.00 24.48 ? 2291 HOH A O   1 
HETATM 9772 O  O   . HOH I 8 .    ? 47.975 74.680  -29.454 1.00 35.63 ? 2292 HOH A O   1 
HETATM 9773 O  O   . HOH I 8 .    ? 50.544 73.752  -25.459 1.00 21.08 ? 2293 HOH A O   1 
HETATM 9774 O  O   . HOH I 8 .    ? 51.059 70.922  -23.656 1.00 18.86 ? 2294 HOH A O   1 
HETATM 9775 O  O   . HOH I 8 .    ? 47.499 79.565  -18.465 1.00 27.30 ? 2295 HOH A O   1 
HETATM 9776 O  O   . HOH I 8 .    ? 47.405 81.569  -17.064 1.00 36.00 ? 2296 HOH A O   1 
HETATM 9777 O  O   . HOH I 8 .    ? 44.035 79.228  -21.460 1.00 36.78 ? 2297 HOH A O   1 
HETATM 9778 O  O   . HOH I 8 .    ? 41.905 79.279  -23.388 1.00 25.33 ? 2298 HOH A O   1 
HETATM 9779 O  O   . HOH I 8 .    ? 39.680 81.603  -21.945 1.00 32.45 ? 2299 HOH A O   1 
HETATM 9780 O  O   . HOH I 8 .    ? 35.418 86.254  -17.975 1.00 29.60 ? 2300 HOH A O   1 
HETATM 9781 O  O   . HOH I 8 .    ? 35.154 88.049  -19.820 1.00 39.67 ? 2301 HOH A O   1 
HETATM 9782 O  O   . HOH I 8 .    ? 33.658 88.117  -16.223 1.00 37.24 ? 2302 HOH A O   1 
HETATM 9783 O  O   . HOH I 8 .    ? 33.365 84.345  -18.312 1.00 18.77 ? 2303 HOH A O   1 
HETATM 9784 O  O   . HOH I 8 .    ? 31.647 85.884  -19.788 1.00 24.15 ? 2304 HOH A O   1 
HETATM 9785 O  O   . HOH I 8 .    ? 37.336 92.589  -18.177 1.00 39.44 ? 2305 HOH A O   1 
HETATM 9786 O  O   . HOH I 8 .    ? 41.616 95.301  -23.802 1.00 68.60 ? 2306 HOH A O   1 
HETATM 9787 O  O   . HOH I 8 .    ? 43.610 93.613  -23.915 1.00 37.81 ? 2307 HOH A O   1 
HETATM 9788 O  O   . HOH I 8 .    ? 45.171 92.600  -25.436 1.00 29.64 ? 2308 HOH A O   1 
HETATM 9789 O  O   . HOH I 8 .    ? 45.136 89.937  -25.491 1.00 19.07 ? 2309 HOH A O   1 
HETATM 9790 O  O   . HOH I 8 .    ? 46.974 89.500  -23.694 1.00 30.48 ? 2310 HOH A O   1 
HETATM 9791 O  O   . HOH I 8 .    ? 45.618 95.225  -26.565 1.00 33.12 ? 2311 HOH A O   1 
HETATM 9792 O  O   . HOH I 8 .    ? 44.589 95.551  -30.515 1.00 38.56 ? 2312 HOH A O   1 
HETATM 9793 O  O   . HOH I 8 .    ? 42.585 94.289  -30.529 1.00 37.55 ? 2313 HOH A O   1 
HETATM 9794 O  O   . HOH I 8 .    ? 41.609 96.360  -29.724 1.00 51.48 ? 2314 HOH A O   1 
HETATM 9795 O  O   . HOH I 8 .    ? 40.174 99.881  -32.020 1.00 29.82 ? 2315 HOH A O   1 
HETATM 9796 O  O   . HOH I 8 .    ? 35.156 94.877  -32.268 1.00 24.93 ? 2316 HOH A O   1 
HETATM 9797 O  O   . HOH I 8 .    ? 36.146 93.469  -30.068 1.00 32.04 ? 2317 HOH A O   1 
HETATM 9798 O  O   . HOH I 8 .    ? 31.572 96.777  -27.353 1.00 43.51 ? 2318 HOH A O   1 
HETATM 9799 O  O   . HOH I 8 .    ? 25.334 98.326  -35.131 1.00 47.01 ? 2319 HOH A O   1 
HETATM 9800 O  O   . HOH I 8 .    ? 28.802 93.703  -38.554 1.00 27.00 ? 2320 HOH A O   1 
HETATM 9801 O  O   . HOH I 8 .    ? 31.974 92.399  -36.933 1.00 24.88 ? 2321 HOH A O   1 
HETATM 9802 O  O   . HOH I 8 .    ? 28.072 84.499  -35.469 1.00 16.76 ? 2322 HOH A O   1 
HETATM 9803 O  O   . HOH I 8 .    ? 28.981 81.825  -35.669 1.00 17.47 ? 2323 HOH A O   1 
HETATM 9804 O  O   . HOH I 8 .    ? 22.060 80.145  -35.939 1.00 24.66 ? 2324 HOH A O   1 
HETATM 9805 O  O   . HOH I 8 .    ? 20.700 80.031  -33.562 1.00 37.84 ? 2325 HOH A O   1 
HETATM 9806 O  O   . HOH I 8 .    ? 23.029 78.479  -30.293 1.00 22.64 ? 2326 HOH A O   1 
HETATM 9807 O  O   . HOH I 8 .    ? 30.308 74.836  -29.218 1.00 13.92 ? 2327 HOH A O   1 
HETATM 9808 O  O   . HOH I 8 .    ? 32.423 77.622  -29.665 1.00 13.58 ? 2328 HOH A O   1 
HETATM 9809 O  O   . HOH I 8 .    ? 38.712 83.411  -39.737 1.00 24.41 ? 2329 HOH A O   1 
HETATM 9810 O  O   . HOH I 8 .    ? 36.870 82.329  -41.316 1.00 42.45 ? 2330 HOH A O   1 
HETATM 9811 O  O   . HOH I 8 .    ? 40.065 82.991  -43.973 1.00 48.20 ? 2331 HOH A O   1 
HETATM 9812 O  O   . HOH I 8 .    ? 43.925 79.918  -42.550 1.00 28.10 ? 2332 HOH A O   1 
HETATM 9813 O  O   . HOH I 8 .    ? 46.650 80.220  -42.562 1.00 24.27 ? 2333 HOH A O   1 
HETATM 9814 O  O   . HOH I 8 .    ? 47.626 78.912  -40.414 1.00 19.72 ? 2334 HOH A O   1 
HETATM 9815 O  O   . HOH I 8 .    ? 48.345 80.315  -44.794 1.00 47.87 ? 2335 HOH A O   1 
HETATM 9816 O  O   . HOH I 8 .    ? 49.883 82.286  -43.827 1.00 18.10 ? 2336 HOH A O   1 
HETATM 9817 O  O   . HOH I 8 .    ? 47.639 83.935  -43.884 1.00 46.64 ? 2337 HOH A O   1 
HETATM 9818 O  O   . HOH I 8 .    ? 45.391 83.636  -43.087 1.00 38.42 ? 2338 HOH A O   1 
HETATM 9819 O  O   . HOH I 8 .    ? 43.418 77.257  -43.112 1.00 45.38 ? 2339 HOH A O   1 
HETATM 9820 O  O   . HOH I 8 .    ? 51.414 76.159  -40.885 1.00 29.21 ? 2340 HOH A O   1 
HETATM 9821 O  O   . HOH I 8 .    ? 53.546 76.846  -43.647 1.00 38.60 ? 2341 HOH A O   1 
HETATM 9822 O  O   . HOH I 8 .    ? 53.304 79.226  -44.771 1.00 36.86 ? 2342 HOH A O   1 
HETATM 9823 O  O   . HOH I 8 .    ? 51.116 80.342  -45.514 1.00 48.97 ? 2343 HOH A O   1 
HETATM 9824 O  O   . HOH I 8 .    ? 54.379 82.862  -44.452 1.00 45.20 ? 2344 HOH A O   1 
HETATM 9825 O  O   . HOH I 8 .    ? 55.515 87.408  -47.895 1.00 55.09 ? 2345 HOH A O   1 
HETATM 9826 O  O   . HOH I 8 .    ? 57.144 88.925  -46.171 1.00 40.29 ? 2346 HOH A O   1 
HETATM 9827 O  O   . HOH I 8 .    ? 56.775 89.831  -43.713 1.00 36.66 ? 2347 HOH A O   1 
HETATM 9828 O  O   . HOH I 8 .    ? 54.171 90.601  -43.166 1.00 33.22 ? 2348 HOH A O   1 
HETATM 9829 O  O   . HOH I 8 .    ? 53.635 92.937  -40.340 1.00 41.75 ? 2349 HOH A O   1 
HETATM 9830 O  O   . HOH I 8 .    ? 56.385 94.234  -38.592 1.00 64.85 ? 2350 HOH A O   1 
HETATM 9831 O  O   . HOH I 8 .    ? 59.153 86.982  -46.026 1.00 43.80 ? 2351 HOH A O   1 
HETATM 9832 O  O   . HOH I 8 .    ? 62.143 81.467  -44.327 1.00 39.54 ? 2352 HOH A O   1 
HETATM 9833 O  O   . HOH I 8 .    ? 60.806 78.784  -41.581 1.00 26.05 ? 2353 HOH A O   1 
HETATM 9834 O  O   . HOH I 8 .    ? 61.534 76.663  -39.753 1.00 21.95 ? 2354 HOH A O   1 
HETATM 9835 O  O   . HOH I 8 .    ? 64.088 77.002  -40.350 1.00 35.17 ? 2355 HOH A O   1 
HETATM 9836 O  O   . HOH I 8 .    ? 64.025 78.510  -37.793 1.00 27.30 ? 2356 HOH A O   1 
HETATM 9837 O  O   . HOH I 8 .    ? 64.384 77.917  -35.261 1.00 14.83 ? 2357 HOH A O   1 
HETATM 9838 O  O   . HOH I 8 .    ? 61.992 83.089  -38.318 1.00 24.40 ? 2358 HOH A O   1 
HETATM 9839 O  O   . HOH I 8 .    ? 65.588 87.519  -41.348 1.00 40.28 ? 2359 HOH A O   1 
HETATM 9840 O  O   . HOH I 8 .    ? 71.485 85.986  -36.041 1.00 50.45 ? 2360 HOH A O   1 
HETATM 9841 O  O   . HOH I 8 .    ? 73.092 85.615  -33.924 1.00 52.75 ? 2361 HOH A O   1 
HETATM 9842 O  O   . HOH I 8 .    ? 72.069 82.805  -31.796 1.00 47.26 ? 2362 HOH A O   1 
HETATM 9843 O  O   . HOH I 8 .    ? 70.084 83.049  -29.815 1.00 23.35 ? 2363 HOH A O   1 
HETATM 9844 O  O   . HOH I 8 .    ? 71.452 82.421  -27.548 1.00 46.76 ? 2364 HOH A O   1 
HETATM 9845 O  O   . HOH I 8 .    ? 67.834 81.703  -25.624 1.00 14.74 ? 2365 HOH A O   1 
HETATM 9846 O  O   . HOH I 8 .    ? 67.818 78.967  -25.265 1.00 13.02 ? 2366 HOH A O   1 
HETATM 9847 O  O   . HOH I 8 .    ? 70.563 78.048  -26.062 1.00 24.23 ? 2367 HOH A O   1 
HETATM 9848 O  O   . HOH I 8 .    ? 68.447 79.358  -28.559 1.00 24.09 ? 2368 HOH A O   1 
HETATM 9849 O  O   . HOH I 8 .    ? 70.316 77.367  -31.684 1.00 49.84 ? 2369 HOH A O   1 
HETATM 9850 O  O   A HOH I 8 .    ? 63.505 67.902  -31.709 0.50 17.03 ? 2370 HOH A O   1 
HETATM 9851 O  O   B HOH I 8 .    ? 65.167 67.913  -31.169 0.50 18.40 ? 2370 HOH A O   1 
HETATM 9852 O  O   . HOH I 8 .    ? 64.103 65.491  -30.558 1.00 43.65 ? 2371 HOH A O   1 
HETATM 9853 O  O   . HOH I 8 .    ? 61.848 63.868  -30.604 1.00 25.66 ? 2372 HOH A O   1 
HETATM 9854 O  O   . HOH I 8 .    ? 59.570 67.143  -34.688 1.00 26.04 ? 2373 HOH A O   1 
HETATM 9855 O  O   . HOH I 8 .    ? 61.272 67.528  -36.601 1.00 32.23 ? 2374 HOH A O   1 
HETATM 9856 O  O   . HOH I 8 .    ? 61.635 68.971  -41.685 1.00 30.50 ? 2375 HOH A O   1 
HETATM 9857 O  O   . HOH I 8 .    ? 66.114 74.649  -41.216 1.00 39.38 ? 2376 HOH A O   1 
HETATM 9858 O  O   . HOH I 8 .    ? 63.850 77.069  -44.499 1.00 45.25 ? 2377 HOH A O   1 
HETATM 9859 O  O   . HOH I 8 .    ? 63.264 74.699  -46.030 1.00 36.76 ? 2378 HOH A O   1 
HETATM 9860 O  O   . HOH I 8 .    ? 55.489 74.321  -43.149 1.00 51.80 ? 2379 HOH A O   1 
HETATM 9861 O  O   . HOH I 8 .    ? 58.435 77.268  -38.518 1.00 14.77 ? 2380 HOH A O   1 
HETATM 9862 O  O   . HOH I 8 .    ? 54.011 64.228  -38.362 1.00 26.41 ? 2381 HOH A O   1 
HETATM 9863 O  O   . HOH I 8 .    ? 47.427 67.772  -33.850 1.00 39.42 ? 2382 HOH A O   1 
HETATM 9864 O  O   . HOH I 8 .    ? 55.000 81.066  -23.619 1.00 14.80 ? 2383 HOH A O   1 
HETATM 9865 O  O   . HOH I 8 .    ? 53.137 86.778  -21.444 1.00 27.63 ? 2384 HOH A O   1 
HETATM 9866 O  O   . HOH I 8 .    ? 56.851 87.658  -20.041 1.00 28.38 ? 2385 HOH A O   1 
HETATM 9867 O  O   . HOH I 8 .    ? 59.290 87.205  -20.545 1.00 35.61 ? 2386 HOH A O   1 
HETATM 9868 O  O   . HOH I 8 .    ? 56.431 90.037  -21.256 1.00 34.20 ? 2387 HOH A O   1 
HETATM 9869 O  O   . HOH I 8 .    ? 26.958 72.249  20.865  1.00 39.79 ? 2388 HOH A O   1 
HETATM 9870 O  O   . HOH I 8 .    ? 64.138 89.639  -22.244 1.00 25.87 ? 2389 HOH A O   1 
HETATM 9871 O  O   . HOH I 8 .    ? 66.593 89.124  -21.198 1.00 40.26 ? 2390 HOH A O   1 
HETATM 9872 O  O   . HOH I 8 .    ? 67.726 88.137  -23.334 1.00 25.11 ? 2391 HOH A O   1 
HETATM 9873 O  O   . HOH I 8 .    ? 65.140 87.959  -24.198 1.00 27.55 ? 2392 HOH A O   1 
HETATM 9874 O  O   . HOH I 8 .    ? 62.319 85.617  -22.968 1.00 31.87 ? 2393 HOH A O   1 
HETATM 9875 O  O   . HOH I 8 .    ? 64.160 84.072  -19.404 1.00 46.93 ? 2394 HOH A O   1 
HETATM 9876 O  O   . HOH I 8 .    ? 62.709 82.653  -17.067 1.00 41.26 ? 2395 HOH A O   1 
HETATM 9877 O  O   . HOH I 8 .    ? 62.161 80.700  -18.859 1.00 22.48 ? 2396 HOH A O   1 
HETATM 9878 O  O   . HOH I 8 .    ? 60.187 83.843  -16.716 1.00 37.42 ? 2397 HOH A O   1 
HETATM 9879 O  O   . HOH I 8 .    ? 63.595 82.150  -14.400 1.00 40.90 ? 2398 HOH A O   1 
HETATM 9880 O  O   . HOH I 8 .    ? 66.546 81.789  -14.297 1.00 28.65 ? 2399 HOH A O   1 
HETATM 9881 O  O   . HOH I 8 .    ? 66.934 81.417  -11.246 1.00 33.04 ? 2400 HOH A O   1 
HETATM 9882 O  O   . HOH I 8 .    ? 65.144 79.778  -8.808  1.00 40.87 ? 2401 HOH A O   1 
HETATM 9883 O  O   . HOH I 8 .    ? 74.185 80.048  -10.454 1.00 45.83 ? 2402 HOH A O   1 
HETATM 9884 O  O   . HOH I 8 .    ? 73.620 78.922  -13.246 1.00 50.70 ? 2403 HOH A O   1 
HETATM 9885 O  O   . HOH I 8 .    ? 71.478 84.012  -14.647 1.00 45.04 ? 2404 HOH A O   1 
HETATM 9886 O  O   . HOH I 8 .    ? 71.863 84.514  -20.007 1.00 33.29 ? 2405 HOH A O   1 
HETATM 9887 O  O   . HOH I 8 .    ? 73.422 82.347  -21.150 1.00 26.74 ? 2406 HOH A O   1 
HETATM 9888 O  O   . HOH I 8 .    ? 75.309 83.672  -22.829 1.00 37.58 ? 2407 HOH A O   1 
HETATM 9889 O  O   . HOH I 8 .    ? 74.176 86.448  -23.287 1.00 46.66 ? 2408 HOH A O   1 
HETATM 9890 O  O   . HOH I 8 .    ? 71.887 87.607  -27.710 1.00 45.19 ? 2409 HOH A O   1 
HETATM 9891 O  O   . HOH I 8 .    ? 66.949 84.410  -22.169 1.00 26.62 ? 2410 HOH A O   1 
HETATM 9892 O  O   . HOH I 8 .    ? 68.650 78.841  -18.058 1.00 21.98 ? 2411 HOH A O   1 
HETATM 9893 O  O   . HOH I 8 .    ? 46.928 87.931  -13.580 1.00 40.02 ? 2412 HOH A O   1 
HETATM 9894 O  O   . HOH I 8 .    ? 40.807 85.213  -12.194 1.00 26.42 ? 2413 HOH A O   1 
HETATM 9895 O  O   . HOH I 8 .    ? 5.401  81.249  -3.323  1.00 37.89 ? 2414 HOH A O   1 
HETATM 9896 O  O   A HOH I 8 .    ? 26.616 74.806  2.266   0.50 10.53 ? 2415 HOH A O   1 
HETATM 9897 O  O   B HOH I 8 .    ? 26.301 75.858  1.547   0.50 14.53 ? 2415 HOH A O   1 
HETATM 9898 O  O   . HOH I 8 .    ? 26.179 72.743  5.554   1.00 12.08 ? 2416 HOH A O   1 
HETATM 9899 O  O   . HOH I 8 .    ? 25.323 73.731  8.722   1.00 21.62 ? 2417 HOH A O   1 
HETATM 9900 O  O   . HOH I 8 .    ? 26.384 74.982  10.999  1.00 29.57 ? 2418 HOH A O   1 
HETATM 9901 O  O   . HOH I 8 .    ? 22.824 72.520  10.875  1.00 46.88 ? 2419 HOH A O   1 
HETATM 9902 O  O   . HOH I 8 .    ? 24.449 70.636  11.139  1.00 45.47 ? 2420 HOH A O   1 
HETATM 9903 O  O   . HOH I 8 .    ? 20.199 72.584  11.242  1.00 51.05 ? 2421 HOH A O   1 
HETATM 9904 O  O   . HOH I 8 .    ? 18.621 70.450  10.385  1.00 48.40 ? 2422 HOH A O   1 
HETATM 9905 O  O   . HOH I 8 .    ? 16.878 68.407  10.674  1.00 46.69 ? 2423 HOH A O   1 
HETATM 9906 O  O   . HOH I 8 .    ? 15.689 70.154  6.496   1.00 26.34 ? 2424 HOH A O   1 
HETATM 9907 O  O   . HOH I 8 .    ? 15.618 73.584  5.509   1.00 24.86 ? 2425 HOH A O   1 
HETATM 9908 O  O   . HOH I 8 .    ? 17.727 74.447  3.873   1.00 20.28 ? 2426 HOH A O   1 
HETATM 9909 O  O   . HOH I 8 .    ? 19.280 72.472  3.045   1.00 15.97 ? 2427 HOH A O   1 
HETATM 9910 O  O   . HOH I 8 .    ? 18.611 70.016  4.204   1.00 14.38 ? 2428 HOH A O   1 
HETATM 9911 O  O   . HOH I 8 .    ? 19.127 76.597  4.695   1.00 24.36 ? 2429 HOH A O   1 
HETATM 9912 O  O   . HOH I 8 .    ? 19.726 77.072  7.272   1.00 61.22 ? 2430 HOH A O   1 
HETATM 9913 O  O   . HOH I 8 .    ? 21.975 76.406  8.570   1.00 29.87 ? 2431 HOH A O   1 
HETATM 9914 O  O   . HOH I 8 .    ? 21.341 78.811  7.584   1.00 49.76 ? 2432 HOH A O   1 
HETATM 9915 O  O   . HOH I 8 .    ? 21.756 79.917  5.331   1.00 26.16 ? 2433 HOH A O   1 
HETATM 9916 O  O   . HOH I 8 .    ? 16.911 74.566  -3.000  1.00 13.21 ? 2434 HOH A O   1 
HETATM 9917 O  O   . HOH I 8 .    ? 20.157 74.332  -6.766  1.00 12.50 ? 2435 HOH A O   1 
HETATM 9918 O  O   . HOH I 8 .    ? 24.681 70.580  -8.728  1.00 11.86 ? 2436 HOH A O   1 
HETATM 9919 O  O   . HOH I 8 .    ? 26.839 68.935  -9.221  1.00 8.76  ? 2437 HOH A O   1 
HETATM 9920 O  O   . HOH I 8 .    ? 32.658 64.710  -9.977  1.00 17.54 ? 2438 HOH A O   1 
HETATM 9921 O  O   . HOH I 8 .    ? 34.296 58.587  -8.757  1.00 7.64  ? 2439 HOH A O   1 
HETATM 9922 O  O   . HOH I 8 .    ? 30.262 58.434  -11.776 1.00 7.43  ? 2440 HOH A O   1 
HETATM 9923 O  O   . HOH I 8 .    ? 26.826 60.954  -3.286  1.00 8.34  ? 2441 HOH A O   1 
HETATM 9924 O  O   . HOH I 8 .    ? 20.684 57.445  -5.181  1.00 10.41 ? 2442 HOH A O   1 
HETATM 9925 O  O   . HOH I 8 .    ? 21.564 57.988  -7.698  1.00 8.94  ? 2443 HOH A O   1 
HETATM 9926 O  O   . HOH I 8 .    ? 19.872 57.385  -11.726 1.00 14.41 ? 2444 HOH A O   1 
HETATM 9927 O  O   . HOH I 8 .    ? 11.837 54.983  -12.312 1.00 19.27 ? 2445 HOH A O   1 
HETATM 9928 O  O   . HOH I 8 .    ? 8.002  57.781  -11.573 1.00 38.23 ? 2446 HOH A O   1 
HETATM 9929 O  O   . HOH I 8 .    ? 7.199  56.721  -8.931  1.00 47.08 ? 2447 HOH A O   1 
HETATM 9930 O  O   . HOH I 8 .    ? 8.676  57.652  -6.833  1.00 25.98 ? 2448 HOH A O   1 
HETATM 9931 O  O   . HOH I 8 .    ? 8.719  54.984  -6.013  1.00 29.13 ? 2449 HOH A O   1 
HETATM 9932 O  O   . HOH I 8 .    ? 4.387  56.680  -6.167  1.00 38.88 ? 2450 HOH A O   1 
HETATM 9933 O  O   . HOH I 8 .    ? 5.556  57.954  7.068   1.00 31.31 ? 2451 HOH A O   1 
HETATM 9934 O  O   . HOH I 8 .    ? 4.629  59.086  11.258  1.00 49.59 ? 2452 HOH A O   1 
HETATM 9935 O  O   . HOH I 8 .    ? 9.050  50.517  8.172   1.00 29.68 ? 2453 HOH A O   1 
HETATM 9936 O  O   . HOH I 8 .    ? 8.636  49.368  5.609   1.00 43.68 ? 2454 HOH A O   1 
HETATM 9937 O  O   . HOH I 8 .    ? 11.875 51.616  14.381  1.00 17.09 ? 2455 HOH A O   1 
HETATM 9938 O  O   . HOH I 8 .    ? 14.096 49.122  15.507  1.00 16.81 ? 2456 HOH A O   1 
HETATM 9939 O  O   . HOH I 8 .    ? 17.401 41.700  9.262   1.00 27.43 ? 2457 HOH A O   1 
HETATM 9940 O  O   . HOH I 8 .    ? 16.581 38.459  5.973   1.00 48.19 ? 2458 HOH A O   1 
HETATM 9941 O  O   . HOH I 8 .    ? 18.369 36.782  5.762   1.00 34.95 ? 2459 HOH A O   1 
HETATM 9942 O  O   . HOH I 8 .    ? 31.141 33.602  2.863   1.00 24.39 ? 2460 HOH A O   1 
HETATM 9943 O  O   . HOH I 8 .    ? 30.746 29.766  5.921   1.00 38.88 ? 2461 HOH A O   1 
HETATM 9944 O  O   . HOH I 8 .    ? 37.009 34.096  5.582   1.00 45.14 ? 2462 HOH A O   1 
HETATM 9945 O  O   . HOH I 8 .    ? 38.925 33.328  6.830   1.00 43.58 ? 2463 HOH A O   1 
HETATM 9946 O  O   . HOH I 8 .    ? 47.726 40.169  5.959   1.00 34.93 ? 2464 HOH A O   1 
HETATM 9947 O  O   . HOH I 8 .    ? 51.055 40.376  5.025   1.00 49.44 ? 2465 HOH A O   1 
HETATM 9948 O  O   . HOH I 8 .    ? 41.301 59.061  13.503  1.00 10.49 ? 2466 HOH A O   1 
HETATM 9949 O  O   . HOH I 8 .    ? 39.416 57.460  14.855  1.00 9.16  ? 2467 HOH A O   1 
HETATM 9950 O  O   . HOH I 8 .    ? 36.956 57.736  13.397  1.00 9.59  ? 2468 HOH A O   1 
HETATM 9951 O  O   . HOH I 8 .    ? 37.679 59.095  11.059  1.00 10.67 ? 2469 HOH A O   1 
HETATM 9952 O  O   . HOH I 8 .    ? 30.281 55.877  17.147  1.00 9.73  ? 2470 HOH A O   1 
HETATM 9953 O  O   . HOH I 8 .    ? 27.809 53.459  20.052  1.00 15.01 ? 2471 HOH A O   1 
HETATM 9954 O  O   . HOH I 8 .    ? 27.152 52.316  22.489  1.00 26.13 ? 2472 HOH A O   1 
HETATM 9955 O  O   . HOH I 8 .    ? 27.523 50.260  23.213  1.00 29.25 ? 2473 HOH A O   1 
HETATM 9956 O  O   . HOH I 8 .    ? 33.749 60.408  23.278  1.00 12.73 ? 2474 HOH A O   1 
HETATM 9957 O  O   . HOH I 8 .    ? 23.098 65.074  14.122  1.00 41.71 ? 2475 HOH A O   1 
HETATM 9958 O  O   . HOH I 8 .    ? 12.154 71.376  4.812   1.00 36.94 ? 2476 HOH A O   1 
HETATM 9959 O  O   . HOH I 8 .    ? 10.371 77.275  4.035   1.00 45.33 ? 2477 HOH A O   1 
HETATM 9960 O  O   . HOH I 8 .    ? 19.569 67.315  -2.669  1.00 26.65 ? 2478 HOH A O   1 
HETATM 9961 O  O   . HOH I 8 .    ? 20.322 58.768  -21.899 1.00 10.57 ? 2479 HOH A O   1 
HETATM 9962 O  O   . HOH I 8 .    ? 23.826 55.489  -23.349 1.00 10.25 ? 2480 HOH A O   1 
HETATM 9963 O  O   . HOH I 8 .    ? 16.985 50.861  -19.218 1.00 24.01 ? 2481 HOH A O   1 
HETATM 9964 O  O   . HOH I 8 .    ? 18.380 48.850  -19.808 1.00 38.23 ? 2482 HOH A O   1 
HETATM 9965 O  O   . HOH I 8 .    ? 14.432 51.029  -18.377 1.00 54.28 ? 2483 HOH A O   1 
HETATM 9966 O  O   . HOH I 8 .    ? 48.691 96.141  -44.349 1.00 46.42 ? 2484 HOH A O   1 
HETATM 9967 O  O   . HOH I 8 .    ? 23.879 39.291  -21.033 1.00 36.90 ? 2485 HOH A O   1 
HETATM 9968 O  O   . HOH I 8 .    ? 28.595 41.276  -21.613 1.00 14.21 ? 2486 HOH A O   1 
HETATM 9969 O  O   . HOH I 8 .    ? 15.154 53.894  -32.074 1.00 36.57 ? 2487 HOH A O   1 
HETATM 9970 O  O   . HOH I 8 .    ? 28.608 58.203  -48.625 1.00 54.95 ? 2488 HOH A O   1 
HETATM 9971 O  O   . HOH I 8 .    ? 23.128 78.495  -42.062 1.00 40.89 ? 2489 HOH A O   1 
HETATM 9972 O  O   . HOH I 8 .    ? 23.360 82.528  -40.560 1.00 25.20 ? 2490 HOH A O   1 
HETATM 9973 O  O   . HOH I 8 .    ? 21.258 82.083  -37.816 1.00 38.82 ? 2491 HOH A O   1 
HETATM 9974 O  O   . HOH I 8 .    ? 23.246 88.584  -38.276 1.00 34.53 ? 2492 HOH A O   1 
HETATM 9975 O  O   . HOH I 8 .    ? 27.923 102.142 -19.157 1.00 32.27 ? 2493 HOH A O   1 
HETATM 9976 O  O   . HOH I 8 .    ? 26.562 100.852 -15.260 1.00 41.36 ? 2494 HOH A O   1 
HETATM 9977 O  O   . HOH I 8 .    ? 48.383 89.166  -30.767 1.00 14.95 ? 2495 HOH A O   1 
HETATM 9978 O  O   . HOH I 8 .    ? 68.247 66.047  -40.588 1.00 13.18 ? 2496 HOH A O   1 
HETATM 9979 O  O   . HOH I 8 .    ? 67.464 64.593  -38.412 1.00 17.90 ? 2497 HOH A O   1 
HETATM 9980 O  O   . HOH I 8 .    ? 18.351 29.060  23.489  1.00 40.37 ? 2498 HOH A O   1 
HETATM 9981 O  O   . HOH I 8 .    ? 19.705 81.589  -42.493 1.00 42.88 ? 2499 HOH A O   1 
HETATM 9982 O  O   . HOH I 8 .    ? 21.311 82.514  -44.292 1.00 49.12 ? 2500 HOH A O   1 
HETATM 9983 O  O   . HOH I 8 .    ? 22.181 80.724  -42.248 1.00 27.21 ? 2501 HOH A O   1 
HETATM 9984 O  O   . HOH I 8 .    ? 11.397 33.756  22.924  1.00 37.46 ? 2502 HOH A O   1 
HETATM 9985 O  O   . HOH I 8 .    ? 22.108 29.066  28.217  1.00 42.02 ? 2503 HOH A O   1 
HETATM 9986 O  O   . HOH I 8 .    ? 22.272 35.090  35.024  1.00 34.54 ? 2504 HOH A O   1 
HETATM 9987 O  O   . HOH I 8 .    ? 24.790 34.584  35.907  1.00 35.73 ? 2505 HOH A O   1 
# 
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    ARG 1    1    ?    ?   ?   A . n 
A 1 2    SER 2    2    ?    ?   ?   A . n 
A 1 3    SER 3    3    ?    ?   ?   A . n 
A 1 4    HIS 4    4    ?    ?   ?   A . n 
A 1 5    HIS 5    5    ?    ?   ?   A . n 
A 1 6    HIS 6    6    ?    ?   ?   A . n 
A 1 7    HIS 7    7    ?    ?   ?   A . n 
A 1 8    HIS 8    8    ?    ?   ?   A . n 
A 1 9    HIS 9    9    ?    ?   ?   A . n 
A 1 10   GLY 10   10   ?    ?   ?   A . n 
A 1 11   GLU 11   11   ?    ?   ?   A . n 
A 1 12   PHE 12   12   ?    ?   ?   A . n 
A 1 13   ASP 13   13   ?    ?   ?   A . n 
A 1 14   ASP 14   14   ?    ?   ?   A . n 
A 1 15   PRO 15   15   ?    ?   ?   A . n 
A 1 16   ILE 16   16   ?    ?   ?   A . n 
A 1 17   ARG 17   17   ?    ?   ?   A . n 
A 1 18   PRO 18   18   ?    ?   ?   A . n 
A 1 19   PRO 19   19   ?    ?   ?   A . n 
A 1 20   LEU 20   20   ?    ?   ?   A . n 
A 1 21   LYS 21   21   ?    ?   ?   A . n 
A 1 22   VAL 22   22   ?    ?   ?   A . n 
A 1 23   ALA 23   23   ?    ?   ?   A . n 
A 1 24   ARG 24   24   ?    ?   ?   A . n 
A 1 25   SER 25   25   ?    ?   ?   A . n 
A 1 26   PRO 26   26   ?    ?   ?   A . n 
A 1 27   ARG 27   27   ?    ?   ?   A . n 
A 1 28   PRO 28   28   ?    ?   ?   A . n 
A 1 29   GLY 29   29   ?    ?   ?   A . n 
A 1 30   GLN 30   30   30   GLN GLN A . n 
A 1 31   CYS 31   31   31   CYS CYS A . n 
A 1 32   GLN 32   32   32   GLN GLN A . n 
A 1 33   ASP 33   33   33   ASP ASP A . n 
A 1 34   VAL 34   34   34   VAL VAL A . n 
A 1 35   VAL 35   35   35   VAL VAL A . n 
A 1 36   GLN 36   36   36   GLN GLN A . n 
A 1 37   ASP 37   37   37   ASP ASP A . n 
A 1 38   VAL 38   38   38   VAL VAL A . n 
A 1 39   PRO 39   39   39   PRO PRO A . n 
A 1 40   ASN 40   40   40   ASN ASN A . n 
A 1 41   VAL 41   41   41   VAL VAL A . n 
A 1 42   ASP 42   42   42   ASP ASP A . n 
A 1 43   VAL 43   43   43   VAL VAL A . n 
A 1 44   GLN 44   44   44   GLN GLN A . n 
A 1 45   MET 45   45   45   MET MET A . n 
A 1 46   LEU 46   46   46   LEU LEU A . n 
A 1 47   GLU 47   47   47   GLU GLU A . n 
A 1 48   LEU 48   48   48   LEU LEU A . n 
A 1 49   TYR 49   49   49   TYR TYR A . n 
A 1 50   ASP 50   50   50   ASP ASP A . n 
A 1 51   ARG 51   51   51   ARG ARG A . n 
A 1 52   MET 52   52   52   MET MET A . n 
A 1 53   SER 53   53   53   SER SER A . n 
A 1 54   PHE 54   54   54   PHE PHE A . n 
A 1 55   LYS 55   55   55   LYS LYS A . n 
A 1 56   ASP 56   56   56   ASP ASP A . n 
A 1 57   ILE 57   57   57   ILE ILE A . n 
A 1 58   ASP 58   58   58   ASP ASP A . n 
A 1 59   GLY 59   59   59   GLY GLY A . n 
A 1 60   GLY 60   60   60   GLY GLY A . n 
A 1 61   VAL 61   61   61   VAL VAL A . n 
A 1 62   TRP 62   62   62   TRP TRP A . n 
A 1 63   LYS 63   63   63   LYS LYS A . n 
A 1 64   GLN 64   64   64   GLN GLN A . n 
A 1 65   GLY 65   65   65   GLY GLY A . n 
A 1 66   TRP 66   66   66   TRP TRP A . n 
A 1 67   ASN 67   67   67   ASN ASN A . n 
A 1 68   ILE 68   68   68   ILE ILE A . n 
A 1 69   LYS 69   69   69   LYS LYS A . n 
A 1 70   TYR 70   70   70   TYR TYR A . n 
A 1 71   ASP 71   71   71   ASP ASP A . n 
A 1 72   PRO 72   72   72   PRO PRO A . n 
A 1 73   LEU 73   73   73   LEU LEU A . n 
A 1 74   LYS 74   74   74   LYS LYS A . n 
A 1 75   TYR 75   75   75   TYR TYR A . n 
A 1 76   ASN 76   76   76   ASN ASN A . n 
A 1 77   ALA 77   77   77   ALA ALA A . n 
A 1 78   HIS 78   78   78   HIS HIS A . n 
A 1 79   HIS 79   79   79   HIS HIS A . n 
A 1 80   LYS 80   80   80   LYS LYS A . n 
A 1 81   LEU 81   81   81   LEU LEU A . n 
A 1 82   LYS 82   82   82   LYS LYS A . n 
A 1 83   VAL 83   83   83   VAL VAL A . n 
A 1 84   PHE 84   84   84   PHE PHE A . n 
A 1 85   VAL 85   85   85   VAL VAL A . n 
A 1 86   VAL 86   86   86   VAL VAL A . n 
A 1 87   PRO 87   87   87   PRO PRO A . n 
A 1 88   HIS 88   88   88   HIS HIS A . n 
A 1 89   SER 89   89   89   SER SER A . n 
A 1 90   HIS 90   90   90   HIS HIS A . n 
A 1 91   ASN 91   91   91   ASN ASN A . n 
A 1 92   ASP 92   92   92   ASP ASP 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   TRP 95   95   95   TRP TRP A . n 
A 1 96   ILE 96   96   96   ILE ILE A . n 
A 1 97   GLN 97   97   97   GLN GLN A . n 
A 1 98   THR 98   98   98   THR THR A . n 
A 1 99   PHE 99   99   99   PHE PHE A . n 
A 1 100  GLU 100  100  100  GLU GLU A . n 
A 1 101  GLU 101  101  101  GLU GLU A . n 
A 1 102  TYR 102  102  102  TYR TYR A . n 
A 1 103  TYR 103  103  103  TYR TYR A . n 
A 1 104  GLN 104  104  104  GLN GLN A . n 
A 1 105  HIS 105  105  105  HIS HIS A . n 
A 1 106  ASP 106  106  106  ASP ASP A . n 
A 1 107  THR 107  107  107  THR THR A . n 
A 1 108  LYS 108  108  108  LYS LYS A . n 
A 1 109  HIS 109  109  109  HIS HIS A . n 
A 1 110  ILE 110  110  110  ILE ILE A . n 
A 1 111  LEU 111  111  111  LEU LEU A . n 
A 1 112  SER 112  112  112  SER SER A . n 
A 1 113  ASN 113  113  113  ASN ASN A . n 
A 1 114  ALA 114  114  114  ALA ALA A . n 
A 1 115  LEU 115  115  115  LEU LEU A . n 
A 1 116  ARG 116  116  116  ARG ARG A . n 
A 1 117  HIS 117  117  117  HIS HIS A . n 
A 1 118  LEU 118  118  118  LEU LEU A . n 
A 1 119  HIS 119  119  119  HIS HIS A . n 
A 1 120  ASP 120  120  120  ASP ASP A . n 
A 1 121  ASN 121  121  121  ASN ASN A . n 
A 1 122  PRO 122  122  122  PRO PRO A . n 
A 1 123  GLU 123  123  123  GLU GLU A . n 
A 1 124  MET 124  124  124  MET MET A . n 
A 1 125  LYS 125  125  125  LYS LYS A . n 
A 1 126  PHE 126  126  126  PHE PHE A . n 
A 1 127  ILE 127  127  127  ILE ILE A . n 
A 1 128  TRP 128  128  128  TRP TRP A . n 
A 1 129  ALA 129  129  129  ALA ALA A . n 
A 1 130  GLU 130  130  130  GLU GLU A . n 
A 1 131  ILE 131  131  131  ILE ILE A . n 
A 1 132  SER 132  132  132  SER SER A . n 
A 1 133  TYR 133  133  133  TYR TYR A . n 
A 1 134  PHE 134  134  134  PHE PHE A . n 
A 1 135  ALA 135  135  135  ALA ALA A . n 
A 1 136  ARG 136  136  136  ARG ARG A . n 
A 1 137  PHE 137  137  137  PHE PHE A . n 
A 1 138  TYR 138  138  138  TYR TYR A . n 
A 1 139  HIS 139  139  139  HIS HIS A . n 
A 1 140  ASP 140  140  140  ASP ASP A . n 
A 1 141  LEU 141  141  141  LEU LEU A . n 
A 1 142  GLY 142  142  142  GLY GLY A . n 
A 1 143  GLU 143  143  143  GLU GLU A . n 
A 1 144  ASN 144  144  144  ASN ASN A . n 
A 1 145  LYS 145  145  145  LYS LYS A . n 
A 1 146  LYS 146  146  146  LYS LYS A . n 
A 1 147  LEU 147  147  147  LEU LEU A . n 
A 1 148  GLN 148  148  148  GLN GLN A . n 
A 1 149  MET 149  149  149  MET MET A . n 
A 1 150  LYS 150  150  150  LYS LYS A . n 
A 1 151  SER 151  151  151  SER SER A . n 
A 1 152  ILE 152  152  152  ILE ILE A . n 
A 1 153  VAL 153  153  153  VAL VAL A . n 
A 1 154  LYS 154  154  154  LYS LYS A . n 
A 1 155  ASN 155  155  155  ASN ASN A . n 
A 1 156  GLY 156  156  156  GLY GLY A . n 
A 1 157  GLN 157  157  157  GLN GLN A . n 
A 1 158  LEU 158  158  158  LEU LEU A . n 
A 1 159  GLU 159  159  159  GLU GLU A . n 
A 1 160  PHE 160  160  160  PHE PHE A . n 
A 1 161  VAL 161  161  161  VAL VAL A . n 
A 1 162  THR 162  162  162  THR THR A . n 
A 1 163  GLY 163  163  163  GLY GLY A . n 
A 1 164  GLY 164  164  164  GLY GLY A . n 
A 1 165  TRP 165  165  165  TRP TRP A . n 
A 1 166  VAL 166  166  166  VAL VAL A . n 
A 1 167  MET 167  167  167  MET MET A . n 
A 1 168  PRO 168  168  168  PRO PRO A . n 
A 1 169  ASP 169  169  169  ASP ASP A . n 
A 1 170  GLU 170  170  170  GLU GLU A . n 
A 1 171  ALA 171  171  171  ALA ALA A . n 
A 1 172  ASN 172  172  172  ASN ASN A . n 
A 1 173  SER 173  173  173  SER SER A . n 
A 1 174  HIS 174  174  174  HIS HIS A . n 
A 1 175  TRP 175  175  175  TRP TRP A . n 
A 1 176  ARG 176  176  176  ARG ARG A . n 
A 1 177  ASN 177  177  177  ASN ASN A . n 
A 1 178  VAL 178  178  178  VAL VAL A . n 
A 1 179  LEU 179  179  179  LEU LEU A . n 
A 1 180  LEU 180  180  180  LEU LEU A . n 
A 1 181  GLN 181  181  181  GLN GLN A . n 
A 1 182  LEU 182  182  182  LEU LEU A . n 
A 1 183  THR 183  183  183  THR THR A . n 
A 1 184  GLU 184  184  184  GLU GLU A . n 
A 1 185  GLY 185  185  185  GLY GLY A . n 
A 1 186  GLN 186  186  186  GLN GLN A . n 
A 1 187  THR 187  187  187  THR THR A . n 
A 1 188  TRP 188  188  188  TRP TRP A . n 
A 1 189  LEU 189  189  189  LEU LEU A . n 
A 1 190  LYS 190  190  190  LYS LYS A . n 
A 1 191  GLN 191  191  191  GLN GLN A . n 
A 1 192  PHE 192  192  192  PHE PHE A . n 
A 1 193  MET 193  193  193  MET MET A . n 
A 1 194  ASN 194  194  194  ASN ASN A . n 
A 1 195  VAL 195  195  195  VAL VAL A . n 
A 1 196  THR 196  196  196  THR THR A . n 
A 1 197  PRO 197  197  197  PRO PRO A . n 
A 1 198  THR 198  198  198  THR THR A . n 
A 1 199  ALA 199  199  199  ALA ALA A . n 
A 1 200  SER 200  200  200  SER SER A . n 
A 1 201  TRP 201  201  201  TRP TRP A . n 
A 1 202  ALA 202  202  202  ALA ALA A . n 
A 1 203  ILE 203  203  203  ILE ILE A . n 
A 1 204  ALA 204  204  204  ALA ALA A . n 
A 1 205  PRO 205  205  205  PRO PRO A . n 
A 1 206  PHE 206  206  206  PHE PHE A . n 
A 1 207  GLY 207  207  207  GLY GLY A . n 
A 1 208  HIS 208  208  208  HIS HIS A . n 
A 1 209  SER 209  209  209  SER SER A . n 
A 1 210  PRO 210  210  210  PRO PRO A . n 
A 1 211  THR 211  211  211  THR THR A . n 
A 1 212  MET 212  212  212  MET MET A . n 
A 1 213  PRO 213  213  213  PRO PRO A . n 
A 1 214  TYR 214  214  214  TYR TYR A . n 
A 1 215  ILE 215  215  215  ILE ILE A . n 
A 1 216  LEU 216  216  216  LEU LEU A . n 
A 1 217  GLN 217  217  217  GLN GLN A . n 
A 1 218  LYS 218  218  218  LYS LYS A . n 
A 1 219  SER 219  219  219  SER SER A . n 
A 1 220  GLY 220  220  220  GLY GLY A . n 
A 1 221  PHE 221  221  221  PHE PHE A . n 
A 1 222  LYS 222  222  222  LYS LYS A . n 
A 1 223  ASN 223  223  223  ASN ASN A . n 
A 1 224  MET 224  224  224  MET MET A . n 
A 1 225  LEU 225  225  225  LEU LEU A . n 
A 1 226  ILE 226  226  226  ILE ILE A . n 
A 1 227  GLN 227  227  227  GLN GLN A . n 
A 1 228  ARG 228  228  228  ARG ARG A . n 
A 1 229  THR 229  229  229  THR THR A . n 
A 1 230  HIS 230  230  230  HIS HIS A . n 
A 1 231  TYR 231  231  231  TYR TYR A . n 
A 1 232  SER 232  232  232  SER SER A . n 
A 1 233  VAL 233  233  233  VAL VAL A . n 
A 1 234  LYS 234  234  234  LYS LYS A . n 
A 1 235  LYS 235  235  235  LYS LYS A . n 
A 1 236  GLU 236  236  236  GLU GLU A . n 
A 1 237  LEU 237  237  237  LEU LEU A . n 
A 1 238  ALA 238  238  238  ALA ALA A . n 
A 1 239  GLN 239  239  239  GLN GLN A . n 
A 1 240  GLN 240  240  240  GLN GLN A . n 
A 1 241  ARG 241  241  241  ARG ARG A . n 
A 1 242  GLN 242  242  242  GLN GLN A . n 
A 1 243  LEU 243  243  243  LEU LEU A . n 
A 1 244  GLU 244  244  244  GLU GLU A . n 
A 1 245  PHE 245  245  245  PHE PHE A . n 
A 1 246  LEU 246  246  246  LEU LEU A . n 
A 1 247  TRP 247  247  247  TRP TRP A . n 
A 1 248  ARG 248  248  248  ARG ARG A . n 
A 1 249  GLN 249  249  249  GLN GLN A . n 
A 1 250  ILE 250  250  250  ILE ILE A . n 
A 1 251  TRP 251  251  251  TRP TRP A . n 
A 1 252  ASP 252  252  252  ASP ASP A . n 
A 1 253  ASN 253  253  253  ASN ASN A . n 
A 1 254  LYS 254  254  254  LYS LYS A . n 
A 1 255  GLY 255  255  255  GLY GLY A . n 
A 1 256  ASP 256  256  256  ASP ASP A . n 
A 1 257  THR 257  257  257  THR THR A . n 
A 1 258  ALA 258  258  258  ALA ALA A . n 
A 1 259  LEU 259  259  259  LEU LEU A . n 
A 1 260  PHE 260  260  260  PHE PHE A . n 
A 1 261  THR 261  261  261  THR THR A . n 
A 1 262  HIS 262  262  262  HIS HIS A . n 
A 1 263  MET 263  263  263  MET MET A . n 
A 1 264  MET 264  264  264  MET MET A . n 
A 1 265  PRO 265  265  265  PRO PRO A . n 
A 1 266  PHE 266  266  266  PHE PHE A . n 
A 1 267  TYR 267  267  267  TYR TYR A . n 
A 1 268  SER 268  268  268  SER SER A . n 
A 1 269  TYR 269  269  269  TYR TYR A . n 
A 1 270  ASP 270  270  270  ASP ASP A . n 
A 1 271  ILE 271  271  271  ILE ILE A . n 
A 1 272  PRO 272  272  272  PRO PRO A . n 
A 1 273  HIS 273  273  273  HIS HIS A . n 
A 1 274  THR 274  274  274  THR THR A . n 
A 1 275  CYS 275  275  275  CYS CYS A . n 
A 1 276  GLY 276  276  276  GLY GLY A . n 
A 1 277  PRO 277  277  277  PRO PRO A . n 
A 1 278  ASP 278  278  278  ASP ASP A . n 
A 1 279  PRO 279  279  279  PRO PRO A . n 
A 1 280  LYS 280  280  280  LYS LYS A . n 
A 1 281  VAL 281  281  281  VAL VAL A . n 
A 1 282  CYS 282  282  282  CYS CYS A . n 
A 1 283  CYS 283  283  283  CYS CYS A . n 
A 1 284  GLN 284  284  284  GLN GLN A . n 
A 1 285  PHE 285  285  285  PHE PHE A . n 
A 1 286  ASP 286  286  286  ASP ASP A . n 
A 1 287  PHE 287  287  287  PHE PHE A . n 
A 1 288  LYS 288  288  288  LYS LYS A . n 
A 1 289  ARG 289  289  289  ARG ARG A . n 
A 1 290  MET 290  290  290  MET MET A . n 
A 1 291  GLY 291  291  291  GLY GLY A . n 
A 1 292  SER 292  292  292  SER SER A . n 
A 1 293  PHE 293  293  293  PHE PHE A . n 
A 1 294  GLY 294  294  294  GLY GLY A . n 
A 1 295  LEU 295  295  295  LEU LEU A . n 
A 1 296  SER 296  296  296  SER SER A . n 
A 1 297  CYS 297  297  297  CYS CYS A . n 
A 1 298  PRO 298  298  298  PRO PRO A . n 
A 1 299  TRP 299  299  299  TRP TRP A . n 
A 1 300  LYS 300  300  300  LYS LYS A . n 
A 1 301  VAL 301  301  301  VAL VAL A . n 
A 1 302  PRO 302  302  302  PRO PRO A . n 
A 1 303  PRO 303  303  303  PRO PRO A . n 
A 1 304  ARG 304  304  304  ARG ARG A . n 
A 1 305  THR 305  305  305  THR THR A . n 
A 1 306  ILE 306  306  306  ILE ILE A . n 
A 1 307  SER 307  307  307  SER SER A . n 
A 1 308  ASP 308  308  308  ASP ASP A . n 
A 1 309  GLN 309  309  309  GLN GLN A . n 
A 1 310  ASN 310  310  310  ASN ASN A . n 
A 1 311  VAL 311  311  311  VAL VAL A . n 
A 1 312  ALA 312  312  312  ALA ALA A . n 
A 1 313  ALA 313  313  313  ALA ALA A . n 
A 1 314  ARG 314  314  314  ARG ARG A . n 
A 1 315  SER 315  315  315  SER SER A . n 
A 1 316  ASP 316  316  316  ASP ASP A . n 
A 1 317  LEU 317  317  317  LEU LEU A . n 
A 1 318  LEU 318  318  318  LEU LEU A . n 
A 1 319  VAL 319  319  319  VAL VAL A . n 
A 1 320  ASP 320  320  320  ASP ASP A . n 
A 1 321  GLN 321  321  321  GLN GLN A . n 
A 1 322  TRP 322  322  322  TRP TRP A . n 
A 1 323  LYS 323  323  323  LYS LYS A . n 
A 1 324  LYS 324  324  324  LYS LYS A . n 
A 1 325  LYS 325  325  325  LYS LYS A . n 
A 1 326  ALA 326  326  326  ALA ALA A . n 
A 1 327  GLU 327  327  327  GLU GLU A . n 
A 1 328  LEU 328  328  328  LEU LEU A . n 
A 1 329  TYR 329  329  329  TYR TYR A . n 
A 1 330  ARG 330  330  330  ARG ARG A . n 
A 1 331  THR 331  331  331  THR THR A . n 
A 1 332  ASN 332  332  332  ASN ASN A . n 
A 1 333  VAL 333  333  333  VAL VAL A . n 
A 1 334  LEU 334  334  334  LEU LEU A . n 
A 1 335  LEU 335  335  335  LEU LEU A . n 
A 1 336  ILE 336  336  336  ILE ILE A . n 
A 1 337  PRO 337  337  337  PRO PRO A . n 
A 1 338  LEU 338  338  338  LEU LEU A . n 
A 1 339  GLY 339  339  339  GLY GLY A . n 
A 1 340  ASP 340  340  340  ASP ASP A . n 
A 1 341  ASP 341  341  341  ASP ASP A . n 
A 1 342  PHE 342  342  342  PHE PHE A . n 
A 1 343  ARG 343  343  343  ARG ARG A . n 
A 1 344  PHE 344  344  344  PHE PHE A . n 
A 1 345  LYS 345  345  345  LYS LYS A . n 
A 1 346  GLN 346  346  346  GLN GLN A . n 
A 1 347  ASN 347  347  347  ASN ASN A . n 
A 1 348  THR 348  348  348  THR THR A . n 
A 1 349  GLU 349  349  349  GLU GLU A . n 
A 1 350  TRP 350  350  350  TRP TRP A . n 
A 1 351  ASP 351  351  351  ASP ASP A . n 
A 1 352  VAL 352  352  352  VAL VAL A . n 
A 1 353  GLN 353  353  353  GLN GLN A . n 
A 1 354  ARG 354  354  354  ARG ARG A . n 
A 1 355  VAL 355  355  355  VAL VAL A . n 
A 1 356  ASN 356  356  356  ASN ASN A . n 
A 1 357  TYR 357  357  357  TYR TYR A . n 
A 1 358  GLU 358  358  358  GLU GLU A . n 
A 1 359  ARG 359  359  359  ARG ARG A . n 
A 1 360  LEU 360  360  360  LEU LEU A . n 
A 1 361  PHE 361  361  361  PHE PHE A . n 
A 1 362  GLU 362  362  362  GLU GLU A . n 
A 1 363  HIS 363  363  363  HIS HIS A . n 
A 1 364  ILE 364  364  364  ILE ILE A . n 
A 1 365  ASN 365  365  365  ASN ASN A . n 
A 1 366  SER 366  366  366  SER SER A . n 
A 1 367  GLN 367  367  367  GLN GLN A . n 
A 1 368  ALA 368  368  368  ALA ALA A . n 
A 1 369  HIS 369  369  369  HIS HIS A . n 
A 1 370  PHE 370  370  370  PHE PHE A . n 
A 1 371  ASN 371  371  371  ASN ASN A . n 
A 1 372  VAL 372  372  372  VAL VAL A . n 
A 1 373  GLN 373  373  373  GLN GLN A . n 
A 1 374  ALA 374  374  374  ALA ALA A . n 
A 1 375  GLN 375  375  375  GLN GLN A . n 
A 1 376  PHE 376  376  376  PHE PHE A . n 
A 1 377  GLY 377  377  377  GLY GLY A . n 
A 1 378  THR 378  378  378  THR THR A . n 
A 1 379  LEU 379  379  379  LEU LEU A . n 
A 1 380  GLN 380  380  380  GLN GLN A . n 
A 1 381  GLU 381  381  381  GLU GLU A . n 
A 1 382  TYR 382  382  382  TYR TYR A . n 
A 1 383  PHE 383  383  383  PHE PHE A . n 
A 1 384  ASP 384  384  384  ASP ASP A . n 
A 1 385  ALA 385  385  385  ALA ALA A . n 
A 1 386  VAL 386  386  386  VAL VAL A . n 
A 1 387  HIS 387  387  387  HIS HIS A . n 
A 1 388  GLN 388  388  388  GLN GLN A . n 
A 1 389  ALA 389  389  389  ALA ALA A . n 
A 1 390  GLU 390  390  390  GLU GLU A . n 
A 1 391  ARG 391  391  391  ARG ARG A . n 
A 1 392  ALA 392  392  392  ALA ALA A . n 
A 1 393  GLY 393  393  393  GLY GLY A . n 
A 1 394  GLN 394  394  394  GLN GLN A . n 
A 1 395  ALA 395  395  395  ALA ALA A . n 
A 1 396  GLU 396  396  396  GLU GLU A . n 
A 1 397  PHE 397  397  397  PHE PHE A . n 
A 1 398  PRO 398  398  398  PRO PRO A . n 
A 1 399  THR 399  399  399  THR THR A . n 
A 1 400  LEU 400  400  400  LEU LEU A . n 
A 1 401  SER 401  401  401  SER SER A . n 
A 1 402  GLY 402  402  402  GLY GLY A . n 
A 1 403  ASP 403  403  403  ASP ASP A . n 
A 1 404  PHE 404  404  404  PHE PHE A . n 
A 1 405  PHE 405  405  405  PHE PHE A . n 
A 1 406  THR 406  406  406  THR THR A . n 
A 1 407  TYR 407  407  407  TYR TYR A . n 
A 1 408  ALA 408  408  408  ALA ALA A . n 
A 1 409  ASP 409  409  409  ASP ASP A . n 
A 1 410  ARG 410  410  410  ARG ARG A . n 
A 1 411  SER 411  411  411  SER SER A . n 
A 1 412  ASP 412  412  412  ASP ASP A . n 
A 1 413  ASN 413  413  413  ASN ASN A . n 
A 1 414  TYR 414  414  414  TYR TYR A . n 
A 1 415  TRP 415  415  415  TRP TRP A . n 
A 1 416  SER 416  416  416  SER SER A . n 
A 1 417  GLY 417  417  417  GLY GLY A . n 
A 1 418  TYR 418  418  418  TYR TYR A . n 
A 1 419  TYR 419  419  419  TYR TYR A . n 
A 1 420  THR 420  420  420  THR THR A . n 
A 1 421  SER 421  421  421  SER SER A . n 
A 1 422  ARG 422  422  422  ARG ARG A . n 
A 1 423  PRO 423  423  423  PRO PRO A . n 
A 1 424  TYR 424  424  424  TYR TYR A . n 
A 1 425  HIS 425  425  425  HIS HIS A . n 
A 1 426  LYS 426  426  426  LYS LYS A . n 
A 1 427  ARG 427  427  427  ARG ARG A . n 
A 1 428  MET 428  428  428  MET MET A . n 
A 1 429  ASP 429  429  429  ASP ASP A . n 
A 1 430  ARG 430  430  430  ARG ARG A . n 
A 1 431  VAL 431  431  431  VAL VAL A . n 
A 1 432  LEU 432  432  432  LEU LEU A . n 
A 1 433  MET 433  433  433  MET MET A . n 
A 1 434  HIS 434  434  434  HIS HIS A . n 
A 1 435  TYR 435  435  435  TYR TYR A . n 
A 1 436  VAL 436  436  436  VAL VAL A . n 
A 1 437  ARG 437  437  437  ARG ARG A . n 
A 1 438  ALA 438  438  438  ALA ALA A . n 
A 1 439  ALA 439  439  439  ALA ALA A . n 
A 1 440  GLU 440  440  440  GLU GLU A . n 
A 1 441  MET 441  441  441  MET MET A . n 
A 1 442  LEU 442  442  442  LEU LEU A . n 
A 1 443  SER 443  443  443  SER SER A . n 
A 1 444  ALA 444  444  444  ALA ALA A . n 
A 1 445  TRP 445  445  445  TRP TRP A . n 
A 1 446  HIS 446  446  446  HIS HIS A . n 
A 1 447  SER 447  447  447  SER SER A . n 
A 1 448  TRP 448  448  448  TRP TRP A . n 
A 1 449  ASP 449  449  449  ASP ASP A . n 
A 1 450  GLY 450  450  450  GLY GLY A . n 
A 1 451  MET 451  451  451  MET MET A . n 
A 1 452  ALA 452  452  452  ALA ALA A . n 
A 1 453  ARG 453  453  453  ARG ARG A . n 
A 1 454  ILE 454  454  454  ILE ILE A . n 
A 1 455  GLU 455  455  455  GLU GLU A . n 
A 1 456  GLU 456  456  456  GLU GLU A . n 
A 1 457  ARG 457  457  457  ARG ARG A . n 
A 1 458  LEU 458  458  458  LEU LEU A . n 
A 1 459  GLU 459  459  459  GLU GLU A . n 
A 1 460  GLN 460  460  460  GLN GLN A . n 
A 1 461  ALA 461  461  461  ALA ALA A . n 
A 1 462  ARG 462  462  462  ARG ARG A . n 
A 1 463  ARG 463  463  463  ARG ARG A . n 
A 1 464  GLU 464  464  464  GLU GLU A . n 
A 1 465  LEU 465  465  465  LEU LEU A . n 
A 1 466  SER 466  466  466  SER SER A . n 
A 1 467  LEU 467  467  467  LEU LEU A . n 
A 1 468  PHE 468  468  468  PHE PHE A . n 
A 1 469  GLN 469  469  469  GLN GLN A . n 
A 1 470  HIS 470  470  470  HIS HIS A . n 
A 1 471  HIS 471  471  471  HIS HIS A . n 
A 1 472  ASP 472  472  472  ASP ASP A . n 
A 1 473  GLY 473  473  473  GLY GLY A . n 
A 1 474  ILE 474  474  474  ILE ILE A . n 
A 1 475  THR 475  475  475  THR THR A . n 
A 1 476  GLY 476  476  476  GLY GLY A . n 
A 1 477  THR 477  477  477  THR THR A . n 
A 1 478  ALA 478  478  478  ALA ALA A . n 
A 1 479  LYS 479  479  479  LYS LYS A . n 
A 1 480  THR 480  480  480  THR THR A . n 
A 1 481  HIS 481  481  481  HIS HIS A . n 
A 1 482  VAL 482  482  482  VAL VAL A . n 
A 1 483  VAL 483  483  483  VAL VAL A . n 
A 1 484  VAL 484  484  484  VAL VAL A . n 
A 1 485  ASP 485  485  485  ASP ASP A . n 
A 1 486  TYR 486  486  486  TYR TYR A . n 
A 1 487  GLU 487  487  487  GLU GLU A . n 
A 1 488  GLN 488  488  488  GLN GLN A . n 
A 1 489  ARG 489  489  489  ARG ARG A . n 
A 1 490  MET 490  490  490  MET MET A . n 
A 1 491  GLN 491  491  491  GLN GLN A . n 
A 1 492  GLU 492  492  492  GLU GLU A . n 
A 1 493  ALA 493  493  493  ALA ALA A . n 
A 1 494  LEU 494  494  494  LEU LEU A . n 
A 1 495  LYS 495  495  495  LYS LYS A . n 
A 1 496  ALA 496  496  496  ALA ALA A . n 
A 1 497  CYS 497  497  497  CYS CYS A . n 
A 1 498  GLN 498  498  498  GLN GLN A . n 
A 1 499  MET 499  499  499  MET MET A . n 
A 1 500  VAL 500  500  500  VAL VAL A . n 
A 1 501  MET 501  501  501  MET MET A . n 
A 1 502  GLN 502  502  502  GLN GLN A . n 
A 1 503  GLN 503  503  503  GLN GLN A . n 
A 1 504  SER 504  504  504  SER SER A . n 
A 1 505  VAL 505  505  505  VAL VAL A . n 
A 1 506  TYR 506  506  506  TYR TYR A . n 
A 1 507  ARG 507  507  507  ARG ARG A . n 
A 1 508  LEU 508  508  508  LEU LEU A . n 
A 1 509  LEU 509  509  509  LEU LEU A . n 
A 1 510  THR 510  510  510  THR THR A . n 
A 1 511  LYS 511  511  511  LYS LYS A . n 
A 1 512  PRO 512  512  512  PRO PRO A . n 
A 1 513  SER 513  513  513  SER SER A . n 
A 1 514  ILE 514  514  514  ILE ILE A . n 
A 1 515  TYR 515  515  515  TYR TYR A . n 
A 1 516  SER 516  516  516  SER SER A . n 
A 1 517  PRO 517  517  517  PRO PRO A . n 
A 1 518  ASP 518  518  518  ASP ASP A . n 
A 1 519  PHE 519  519  519  PHE PHE A . n 
A 1 520  SER 520  520  520  SER SER A . n 
A 1 521  PHE 521  521  521  PHE PHE 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  PHE 524  524  524  PHE PHE A . n 
A 1 525  THR 525  525  525  THR THR A . n 
A 1 526  LEU 526  526  526  LEU LEU A . n 
A 1 527  ASP 527  527  527  ASP ASP A . n 
A 1 528  ASP 528  528  528  ASP ASP A . n 
A 1 529  SER 529  529  529  SER SER A . n 
A 1 530  ARG 530  530  530  ARG ARG A . n 
A 1 531  TRP 531  531  531  TRP TRP A . n 
A 1 532  PRO 532  532  532  PRO PRO A . n 
A 1 533  GLY 533  533  533  GLY GLY A . n 
A 1 534  SER 534  534  534  SER SER A . n 
A 1 535  GLY 535  535  535  GLY GLY A . n 
A 1 536  VAL 536  536  536  VAL VAL A . n 
A 1 537  GLU 537  537  537  GLU GLU A . n 
A 1 538  ASP 538  538  538  ASP ASP A . n 
A 1 539  SER 539  539  539  SER SER A . n 
A 1 540  ARG 540  540  540  ARG ARG A . n 
A 1 541  THR 541  541  541  THR THR A . n 
A 1 542  THR 542  542  542  THR THR A . n 
A 1 543  ILE 543  543  543  ILE ILE A . n 
A 1 544  ILE 544  544  544  ILE ILE A . n 
A 1 545  LEU 545  545  545  LEU LEU A . n 
A 1 546  GLY 546  546  546  GLY GLY A . n 
A 1 547  GLU 547  547  547  GLU GLU A . n 
A 1 548  ASP 548  548  548  ASP ASP A . n 
A 1 549  ILE 549  549  549  ILE ILE A . n 
A 1 550  LEU 550  550  550  LEU LEU A . n 
A 1 551  PRO 551  551  551  PRO PRO A . n 
A 1 552  SER 552  552  552  SER SER A . n 
A 1 553  LYS 553  553  553  LYS LYS A . n 
A 1 554  HIS 554  554  554  HIS HIS A . n 
A 1 555  VAL 555  555  555  VAL VAL A . n 
A 1 556  VAL 556  556  556  VAL VAL A . n 
A 1 557  MET 557  557  557  MET MET A . n 
A 1 558  HIS 558  558  558  HIS HIS A . n 
A 1 559  ASN 559  559  559  ASN ASN A . n 
A 1 560  THR 560  560  560  THR THR A . n 
A 1 561  LEU 561  561  561  LEU LEU A . n 
A 1 562  PRO 562  562  562  PRO PRO A . n 
A 1 563  HIS 563  563  563  HIS HIS A . n 
A 1 564  TRP 564  564  564  TRP TRP A . n 
A 1 565  ARG 565  565  565  ARG ARG A . n 
A 1 566  GLU 566  566  566  GLU GLU A . n 
A 1 567  GLN 567  567  567  GLN GLN A . n 
A 1 568  LEU 568  568  568  LEU LEU A . n 
A 1 569  VAL 569  569  569  VAL VAL A . n 
A 1 570  ASP 570  570  570  ASP ASP A . n 
A 1 571  PHE 571  571  571  PHE PHE A . n 
A 1 572  TYR 572  572  572  TYR TYR A . n 
A 1 573  VAL 573  573  573  VAL VAL A . n 
A 1 574  SER 574  574  574  SER SER A . n 
A 1 575  SER 575  575  575  SER SER A . n 
A 1 576  PRO 576  576  576  PRO PRO A . n 
A 1 577  PHE 577  577  577  PHE PHE A . n 
A 1 578  VAL 578  578  578  VAL VAL A . n 
A 1 579  SER 579  579  579  SER SER A . n 
A 1 580  VAL 580  580  580  VAL VAL A . n 
A 1 581  THR 581  581  581  THR THR A . n 
A 1 582  ASP 582  582  582  ASP ASP A . n 
A 1 583  LEU 583  583  583  LEU LEU A . n 
A 1 584  ALA 584  584  584  ALA ALA A . n 
A 1 585  ASN 585  585  585  ASN ASN A . n 
A 1 586  ASN 586  586  586  ASN ASN A . n 
A 1 587  PRO 587  587  587  PRO PRO A . n 
A 1 588  VAL 588  588  588  VAL VAL A . n 
A 1 589  GLU 589  589  589  GLU GLU A . n 
A 1 590  ALA 590  590  590  ALA ALA A . n 
A 1 591  GLN 591  591  591  GLN GLN A . n 
A 1 592  VAL 592  592  592  VAL VAL A . n 
A 1 593  SER 593  593  593  SER SER A . n 
A 1 594  PRO 594  594  594  PRO PRO A . n 
A 1 595  VAL 595  595  595  VAL VAL A . n 
A 1 596  TRP 596  596  596  TRP TRP A . n 
A 1 597  SER 597  597  597  SER SER A . n 
A 1 598  TRP 598  598  598  TRP TRP A . n 
A 1 599  HIS 599  599  599  HIS HIS A . n 
A 1 600  HIS 600  600  600  HIS HIS A . n 
A 1 601  ASP 601  601  601  ASP ASP A . n 
A 1 602  THR 602  602  602  THR THR A . n 
A 1 603  LEU 603  603  603  LEU LEU A . n 
A 1 604  THR 604  604  604  THR THR A . n 
A 1 605  LYS 605  605  605  LYS LYS A . n 
A 1 606  THR 606  606  606  THR THR A . n 
A 1 607  ILE 607  607  607  ILE ILE A . n 
A 1 608  HIS 608  608  608  HIS HIS A . n 
A 1 609  PRO 609  609  609  PRO PRO A . n 
A 1 610  GLN 610  610  610  GLN GLN A . n 
A 1 611  GLY 611  611  611  GLY GLY A . n 
A 1 612  SER 612  612  612  SER SER A . n 
A 1 613  THR 613  613  613  THR THR A . n 
A 1 614  THR 614  614  614  THR THR A . n 
A 1 615  LYS 615  615  615  LYS LYS A . n 
A 1 616  TYR 616  616  616  TYR TYR A . n 
A 1 617  ARG 617  617  617  ARG ARG A . n 
A 1 618  ILE 618  618  618  ILE ILE A . n 
A 1 619  ILE 619  619  619  ILE ILE A . n 
A 1 620  PHE 620  620  620  PHE PHE A . n 
A 1 621  LYS 621  621  621  LYS LYS A . n 
A 1 622  ALA 622  622  622  ALA ALA A . n 
A 1 623  ARG 623  623  623  ARG ARG A . n 
A 1 624  VAL 624  624  624  VAL VAL A . n 
A 1 625  PRO 625  625  625  PRO PRO A . n 
A 1 626  PRO 626  626  626  PRO PRO A . n 
A 1 627  MET 627  627  627  MET MET A . n 
A 1 628  GLY 628  628  628  GLY GLY A . n 
A 1 629  LEU 629  629  629  LEU LEU A . n 
A 1 630  ALA 630  630  630  ALA ALA A . n 
A 1 631  THR 631  631  631  THR THR A . n 
A 1 632  TYR 632  632  632  TYR TYR A . n 
A 1 633  VAL 633  633  633  VAL VAL A . n 
A 1 634  LEU 634  634  634  LEU LEU A . n 
A 1 635  THR 635  635  635  THR THR A . n 
A 1 636  ILE 636  636  636  ILE ILE A . n 
A 1 637  SER 637  637  637  SER SER A . n 
A 1 638  ASP 638  638  638  ASP ASP A . n 
A 1 639  SER 639  639  639  SER SER A . n 
A 1 640  LYS 640  640  640  LYS LYS A . n 
A 1 641  PRO 641  641  641  PRO PRO A . n 
A 1 642  GLU 642  642  642  GLU GLU A . n 
A 1 643  HIS 643  643  643  HIS HIS A . n 
A 1 644  THR 644  644  644  THR THR A . n 
A 1 645  SER 645  645  645  SER SER A . n 
A 1 646  TYR 646  646  646  TYR TYR A . n 
A 1 647  ALA 647  647  647  ALA ALA A . n 
A 1 648  SER 648  648  648  SER SER A . n 
A 1 649  ASN 649  649  649  ASN ASN A . n 
A 1 650  LEU 650  650  650  LEU LEU A . n 
A 1 651  LEU 651  651  651  LEU LEU A . n 
A 1 652  LEU 652  652  652  LEU LEU A . n 
A 1 653  ARG 653  653  653  ARG ARG A . n 
A 1 654  LYS 654  654  654  LYS LYS A . n 
A 1 655  ASN 655  655  655  ASN ASN A . n 
A 1 656  PRO 656  656  656  PRO PRO A . n 
A 1 657  THR 657  657  657  THR THR A . n 
A 1 658  SER 658  658  658  SER SER A . n 
A 1 659  LEU 659  659  659  LEU LEU A . n 
A 1 660  PRO 660  660  660  PRO PRO A . n 
A 1 661  LEU 661  661  661  LEU LEU A . n 
A 1 662  GLY 662  662  662  GLY GLY A . n 
A 1 663  GLN 663  663  663  GLN GLN A . n 
A 1 664  TYR 664  664  664  TYR TYR A . n 
A 1 665  PRO 665  665  665  PRO PRO A . n 
A 1 666  GLU 666  666  666  GLU GLU A . n 
A 1 667  ASP 667  667  667  ASP ASP A . n 
A 1 668  VAL 668  668  668  VAL VAL A . n 
A 1 669  LYS 669  669  669  LYS LYS A . n 
A 1 670  PHE 670  670  670  PHE PHE A . n 
A 1 671  GLY 671  671  671  GLY GLY A . n 
A 1 672  ASP 672  672  672  ASP ASP A . n 
A 1 673  PRO 673  673  673  PRO PRO A . n 
A 1 674  ARG 674  674  674  ARG ARG A . n 
A 1 675  GLU 675  675  675  GLU GLU A . n 
A 1 676  ILE 676  676  676  ILE ILE A . n 
A 1 677  SER 677  677  677  SER SER A . n 
A 1 678  LEU 678  678  678  LEU LEU A . n 
A 1 679  ARG 679  679  679  ARG ARG A . n 
A 1 680  VAL 680  680  680  VAL VAL A . n 
A 1 681  GLY 681  681  681  GLY GLY A . n 
A 1 682  ASN 682  682  682  ASN ASN A . n 
A 1 683  GLY 683  683  683  GLY GLY A . n 
A 1 684  PRO 684  684  684  PRO PRO A . n 
A 1 685  THR 685  685  685  THR THR A . n 
A 1 686  LEU 686  686  686  LEU LEU A . n 
A 1 687  ALA 687  687  687  ALA ALA A . n 
A 1 688  PHE 688  688  688  PHE PHE A . n 
A 1 689  SER 689  689  689  SER SER A . n 
A 1 690  GLU 690  690  690  GLU GLU A . n 
A 1 691  GLN 691  691  691  GLN GLN A . n 
A 1 692  GLY 692  692  692  GLY GLY A . n 
A 1 693  LEU 693  693  693  LEU LEU A . n 
A 1 694  LEU 694  694  694  LEU LEU A . n 
A 1 695  LYS 695  695  695  LYS LYS A . n 
A 1 696  SER 696  696  696  SER SER A . n 
A 1 697  ILE 697  697  697  ILE ILE A . n 
A 1 698  GLN 698  698  698  GLN GLN A . n 
A 1 699  LEU 699  699  699  LEU LEU A . n 
A 1 700  THR 700  700  700  THR THR A . n 
A 1 701  GLN 701  701  701  GLN GLN A . n 
A 1 702  ASP 702  702  702  ASP ASP A . n 
A 1 703  SER 703  703  703  SER SER A . n 
A 1 704  PRO 704  704  704  PRO PRO A . n 
A 1 705  HIS 705  705  705  HIS HIS A . n 
A 1 706  VAL 706  706  706  VAL VAL A . n 
A 1 707  PRO 707  707  707  PRO PRO A . n 
A 1 708  VAL 708  708  708  VAL VAL A . n 
A 1 709  HIS 709  709  709  HIS HIS A . n 
A 1 710  PHE 710  710  710  PHE PHE A . n 
A 1 711  LYS 711  711  711  LYS LYS A . n 
A 1 712  PHE 712  712  712  PHE PHE A . n 
A 1 713  LEU 713  713  713  LEU LEU A . n 
A 1 714  LYS 714  714  714  LYS LYS A . n 
A 1 715  TYR 715  715  715  TYR TYR A . n 
A 1 716  GLY 716  716  716  GLY GLY A . n 
A 1 717  VAL 717  717  717  VAL VAL A . n 
A 1 718  ARG 718  718  718  ARG ARG A . n 
A 1 719  SER 719  719  719  SER SER A . n 
A 1 720  HIS 720  720  720  HIS HIS A . n 
A 1 721  GLY 721  721  721  GLY GLY A . n 
A 1 722  ASP 722  722  722  ASP ASP A . n 
A 1 723  ARG 723  723  723  ARG ARG A . n 
A 1 724  SER 724  724  724  SER SER A . n 
A 1 725  GLY 725  725  725  GLY GLY A . n 
A 1 726  ALA 726  726  726  ALA ALA A . n 
A 1 727  TYR 727  727  727  TYR TYR A . n 
A 1 728  LEU 728  728  728  LEU LEU A . n 
A 1 729  PHE 729  729  729  PHE PHE A . n 
A 1 730  LEU 730  730  730  LEU LEU A . n 
A 1 731  PRO 731  731  731  PRO PRO A . n 
A 1 732  ASN 732  732  732  ASN ASN A . n 
A 1 733  GLY 733  733  733  GLY GLY A . n 
A 1 734  PRO 734  734  734  PRO PRO 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  PRO 737  737  737  PRO PRO A . n 
A 1 738  VAL 738  738  738  VAL VAL A . n 
A 1 739  GLU 739  739  739  GLU GLU A . n 
A 1 740  LEU 740  740  740  LEU LEU A . n 
A 1 741  GLY 741  741  741  GLY GLY A . n 
A 1 742  GLN 742  742  742  GLN GLN A . n 
A 1 743  PRO 743  743  743  PRO PRO A . n 
A 1 744  VAL 744  744  744  VAL VAL A . n 
A 1 745  VAL 745  745  745  VAL VAL A . n 
A 1 746  LEU 746  746  746  LEU LEU A . n 
A 1 747  VAL 747  747  747  VAL VAL A . n 
A 1 748  THR 748  748  748  THR THR A . n 
A 1 749  LYS 749  749  749  LYS LYS A . n 
A 1 750  GLY 750  750  750  GLY GLY A . n 
A 1 751  LYS 751  751  751  LYS LYS A . n 
A 1 752  LEU 752  752  752  LEU LEU A . n 
A 1 753  GLU 753  753  753  GLU GLU A . n 
A 1 754  SER 754  754  754  SER SER A . n 
A 1 755  SER 755  755  755  SER SER A . n 
A 1 756  VAL 756  756  756  VAL VAL A . n 
A 1 757  SER 757  757  757  SER SER A . n 
A 1 758  VAL 758  758  758  VAL VAL A . n 
A 1 759  GLY 759  759  759  GLY GLY A . n 
A 1 760  LEU 760  760  760  LEU LEU A . n 
A 1 761  PRO 761  761  761  PRO PRO A . n 
A 1 762  SER 762  762  762  SER SER A . n 
A 1 763  VAL 763  763  763  VAL VAL A . n 
A 1 764  VAL 764  764  764  VAL VAL A . n 
A 1 765  HIS 765  765  765  HIS HIS A . n 
A 1 766  GLN 766  766  766  GLN GLN A . n 
A 1 767  THR 767  767  767  THR THR A . n 
A 1 768  ILE 768  768  768  ILE ILE A . n 
A 1 769  MET 769  769  769  MET MET A . n 
A 1 770  ARG 770  770  770  ARG ARG A . n 
A 1 771  GLY 771  771  771  GLY GLY A . n 
A 1 772  GLY 772  772  772  GLY GLY A . n 
A 1 773  ALA 773  773  773  ALA ALA A . n 
A 1 774  PRO 774  774  774  PRO PRO A . n 
A 1 775  GLU 775  775  775  GLU GLU A . n 
A 1 776  ILE 776  776  776  ILE ILE A . n 
A 1 777  ARG 777  777  777  ARG ARG A . n 
A 1 778  ASN 778  778  778  ASN ASN 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  ASP 781  781  781  ASP ASP A . n 
A 1 782  ILE 782  782  782  ILE ILE A . n 
A 1 783  GLY 783  783  783  GLY GLY A . n 
A 1 784  SER 784  784  784  SER SER A . n 
A 1 785  LEU 785  785  785  LEU LEU A . n 
A 1 786  ASP 786  786  786  ASP ASP A . n 
A 1 787  ASN 787  787  787  ASN ASN A . n 
A 1 788  THR 788  788  788  THR THR A . n 
A 1 789  GLU 789  789  789  GLU GLU A . n 
A 1 790  ILE 790  790  790  ILE ILE A . n 
A 1 791  VAL 791  791  791  VAL VAL A . n 
A 1 792  MET 792  792  792  MET MET A . n 
A 1 793  ARG 793  793  793  ARG ARG A . n 
A 1 794  LEU 794  794  794  LEU LEU A . n 
A 1 795  GLU 795  795  795  GLU GLU A . n 
A 1 796  THR 796  796  796  THR THR A . n 
A 1 797  HIS 797  797  797  HIS HIS A . n 
A 1 798  ILE 798  798  798  ILE ILE A . n 
A 1 799  ASP 799  799  799  ASP ASP A . n 
A 1 800  SER 800  800  800  SER SER A . n 
A 1 801  GLY 801  801  801  GLY GLY A . n 
A 1 802  ASP 802  802  802  ASP ASP A . n 
A 1 803  ILE 803  803  803  ILE ILE A . n 
A 1 804  PHE 804  804  804  PHE PHE A . n 
A 1 805  TYR 805  805  805  TYR TYR A . n 
A 1 806  THR 806  806  806  THR THR A . n 
A 1 807  ASP 807  807  807  ASP ASP A . n 
A 1 808  LEU 808  808  808  LEU LEU A . n 
A 1 809  ASN 809  809  809  ASN ASN A . n 
A 1 810  GLY 810  810  810  GLY GLY A . n 
A 1 811  LEU 811  811  811  LEU LEU A . n 
A 1 812  GLN 812  812  812  GLN GLN A . n 
A 1 813  PHE 813  813  813  PHE PHE A . n 
A 1 814  ILE 814  814  814  ILE ILE A . n 
A 1 815  LYS 815  815  815  LYS LYS A . n 
A 1 816  ARG 816  816  816  ARG ARG A . n 
A 1 817  ARG 817  817  817  ARG ARG A . n 
A 1 818  ARG 818  818  818  ARG ARG A . n 
A 1 819  LEU 819  819  819  LEU LEU A . n 
A 1 820  ASP 820  820  820  ASP ASP A . n 
A 1 821  LYS 821  821  821  LYS LYS A . n 
A 1 822  LEU 822  822  822  LEU LEU A . n 
A 1 823  PRO 823  823  823  PRO PRO A . n 
A 1 824  LEU 824  824  824  LEU LEU A . n 
A 1 825  GLN 825  825  825  GLN GLN A . n 
A 1 826  ALA 826  826  826  ALA ALA A . n 
A 1 827  ASN 827  827  827  ASN ASN A . n 
A 1 828  TYR 828  828  828  TYR TYR A . n 
A 1 829  TYR 829  829  829  TYR TYR A . n 
A 1 830  PRO 830  830  830  PRO PRO A . n 
A 1 831  ILE 831  831  831  ILE ILE A . n 
A 1 832  PRO 832  832  832  PRO PRO A . n 
A 1 833  SER 833  833  833  SER SER A . n 
A 1 834  GLY 834  834  834  GLY GLY A . n 
A 1 835  MET 835  835  835  MET MET A . n 
A 1 836  PHE 836  836  836  PHE PHE A . n 
A 1 837  ILE 837  837  837  ILE ILE A . n 
A 1 838  GLU 838  838  838  GLU GLU A . n 
A 1 839  ASP 839  839  839  ASP ASP A . n 
A 1 840  ALA 840  840  840  ALA ALA A . n 
A 1 841  ASN 841  841  841  ASN ASN A . n 
A 1 842  THR 842  842  842  THR THR A . n 
A 1 843  ARG 843  843  843  ARG ARG A . n 
A 1 844  LEU 844  844  844  LEU LEU A . n 
A 1 845  THR 845  845  845  THR THR A . n 
A 1 846  LEU 846  846  846  LEU LEU A . n 
A 1 847  LEU 847  847  847  LEU LEU A . n 
A 1 848  THR 848  848  848  THR THR A . n 
A 1 849  GLY 849  849  849  GLY GLY A . n 
A 1 850  GLN 850  850  850  GLN GLN A . n 
A 1 851  PRO 851  851  851  PRO PRO A . n 
A 1 852  LEU 852  852  852  LEU LEU A . n 
A 1 853  GLY 853  853  853  GLY GLY A . n 
A 1 854  GLY 854  854  854  GLY GLY A . n 
A 1 855  SER 855  855  855  SER SER A . n 
A 1 856  SER 856  856  856  SER SER A . n 
A 1 857  LEU 857  857  857  LEU LEU A . n 
A 1 858  ALA 858  858  858  ALA ALA A . n 
A 1 859  SER 859  859  859  SER SER A . n 
A 1 860  GLY 860  860  860  GLY GLY A . n 
A 1 861  GLU 861  861  861  GLU GLU A . n 
A 1 862  LEU 862  862  862  LEU LEU A . n 
A 1 863  GLU 863  863  863  GLU GLU A . n 
A 1 864  ILE 864  864  864  ILE ILE A . n 
A 1 865  MET 865  865  865  MET MET A . n 
A 1 866  GLN 866  866  866  GLN GLN A . n 
A 1 867  ASP 867  867  867  ASP ASP A . n 
A 1 868  ARG 868  868  868  ARG ARG A . n 
A 1 869  ARG 869  869  869  ARG ARG A . n 
A 1 870  LEU 870  870  870  LEU LEU A . n 
A 1 871  ALA 871  871  871  ALA ALA A . n 
A 1 872  SER 872  872  872  SER SER A . n 
A 1 873  ASP 873  873  873  ASP ASP A . n 
A 1 874  ASP 874  874  874  ASP ASP A . n 
A 1 875  GLU 875  875  875  GLU GLU A . n 
A 1 876  ARG 876  876  876  ARG ARG A . n 
A 1 877  GLY 877  877  877  GLY GLY A . n 
A 1 878  LEU 878  878  878  LEU LEU A . n 
A 1 879  GLY 879  879  879  GLY GLY A . n 
A 1 880  GLN 880  880  880  GLN GLN A . n 
A 1 881  GLY 881  881  881  GLY GLY A . n 
A 1 882  VAL 882  882  882  VAL VAL A . n 
A 1 883  LEU 883  883  883  LEU LEU A . n 
A 1 884  ASP 884  884  884  ASP ASP A . n 
A 1 885  ASN 885  885  885  ASN ASN A . n 
A 1 886  LYS 886  886  886  LYS LYS A . n 
A 1 887  PRO 887  887  887  PRO PRO A . n 
A 1 888  VAL 888  888  888  VAL VAL A . n 
A 1 889  LEU 889  889  889  LEU LEU A . n 
A 1 890  HIS 890  890  890  HIS HIS A . n 
A 1 891  ILE 891  891  891  ILE ILE A . n 
A 1 892  TYR 892  892  892  TYR TYR A . n 
A 1 893  ARG 893  893  893  ARG ARG A . n 
A 1 894  LEU 894  894  894  LEU LEU A . n 
A 1 895  VAL 895  895  895  VAL VAL A . n 
A 1 896  LEU 896  896  896  LEU LEU A . n 
A 1 897  GLU 897  897  897  GLU GLU A . n 
A 1 898  LYS 898  898  898  LYS LYS A . n 
A 1 899  VAL 899  899  899  VAL VAL A . n 
A 1 900  ASN 900  900  900  ASN ASN A . n 
A 1 901  ASN 901  901  901  ASN ASN A . n 
A 1 902  CYS 902  902  902  CYS CYS A . n 
A 1 903  VAL 903  903  903  VAL VAL A . n 
A 1 904  ARG 904  904  904  ARG ARG A . n 
A 1 905  PRO 905  905  905  PRO PRO A . n 
A 1 906  SER 906  906  906  SER SER A . n 
A 1 907  LYS 907  907  907  LYS LYS A . n 
A 1 908  LEU 908  908  908  LEU LEU A . n 
A 1 909  HIS 909  909  909  HIS HIS A . n 
A 1 910  PRO 910  910  910  PRO PRO A . n 
A 1 911  ALA 911  911  911  ALA ALA A . n 
A 1 912  GLY 912  912  912  GLY GLY A . n 
A 1 913  TYR 913  913  913  TYR TYR A . n 
A 1 914  LEU 914  914  914  LEU LEU A . n 
A 1 915  THR 915  915  915  THR THR A . n 
A 1 916  SER 916  916  916  SER SER A . n 
A 1 917  ALA 917  917  917  ALA ALA A . n 
A 1 918  ALA 918  918  918  ALA ALA A . n 
A 1 919  HIS 919  919  919  HIS HIS A . n 
A 1 920  LYS 920  920  920  LYS LYS A . n 
A 1 921  ALA 921  921  921  ALA ALA A . n 
A 1 922  SER 922  922  922  SER SER A . n 
A 1 923  GLN 923  923  923  GLN GLN A . n 
A 1 924  SER 924  924  924  SER SER A . n 
A 1 925  LEU 925  925  925  LEU LEU A . n 
A 1 926  LEU 926  926  926  LEU LEU A . n 
A 1 927  ASP 927  927  927  ASP ASP A . n 
A 1 928  PRO 928  928  928  PRO PRO A . n 
A 1 929  LEU 929  929  929  LEU LEU A . n 
A 1 930  ASP 930  930  930  ASP ASP A . n 
A 1 931  LYS 931  931  931  LYS LYS A . n 
A 1 932  PHE 932  932  932  PHE PHE A . n 
A 1 933  ILE 933  933  933  ILE ILE A . n 
A 1 934  PHE 934  934  934  PHE PHE A . n 
A 1 935  ALA 935  935  935  ALA ALA A . n 
A 1 936  GLU 936  936  936  GLU GLU A . n 
A 1 937  ASN 937  937  937  ASN ASN A . n 
A 1 938  GLU 938  938  938  GLU GLU A . n 
A 1 939  TRP 939  939  939  TRP TRP A . n 
A 1 940  ILE 940  940  940  ILE ILE A . n 
A 1 941  GLY 941  941  941  GLY GLY A . n 
A 1 942  ALA 942  942  942  ALA ALA A . n 
A 1 943  GLN 943  943  943  GLN GLN A . n 
A 1 944  GLY 944  944  944  GLY GLY A . n 
A 1 945  GLN 945  945  945  GLN GLN A . n 
A 1 946  PHE 946  946  946  PHE PHE A . n 
A 1 947  GLY 947  947  947  GLY GLY A . n 
A 1 948  GLY 948  948  948  GLY GLY A . n 
A 1 949  ASP 949  949  949  ASP ASP A . n 
A 1 950  HIS 950  950  950  HIS HIS A . n 
A 1 951  PRO 951  951  951  PRO PRO A . n 
A 1 952  SER 952  952  952  SER SER A . n 
A 1 953  ALA 953  953  953  ALA ALA A . n 
A 1 954  ARG 954  954  954  ARG ARG A . n 
A 1 955  GLU 955  955  955  GLU GLU A . n 
A 1 956  ASP 956  956  956  ASP ASP A . n 
A 1 957  LEU 957  957  957  LEU LEU A . n 
A 1 958  ASP 958  958  958  ASP ASP A . n 
A 1 959  VAL 959  959  959  VAL VAL A . n 
A 1 960  SER 960  960  960  SER SER A . n 
A 1 961  VAL 961  961  961  VAL VAL A . n 
A 1 962  MET 962  962  962  MET MET A . n 
A 1 963  ARG 963  963  963  ARG ARG A . n 
A 1 964  ARG 964  964  964  ARG ARG A . n 
A 1 965  LEU 965  965  965  LEU LEU A . n 
A 1 966  THR 966  966  966  THR THR A . n 
A 1 967  LYS 967  967  967  LYS LYS A . n 
A 1 968  SER 968  968  968  SER SER A . n 
A 1 969  SER 969  969  969  SER SER A . n 
A 1 970  ALA 970  970  970  ALA ALA A . n 
A 1 971  LYS 971  971  971  LYS LYS A . n 
A 1 972  THR 972  972  972  THR THR A . n 
A 1 973  GLN 973  973  973  GLN GLN A . n 
A 1 974  ARG 974  974  974  ARG ARG A . n 
A 1 975  VAL 975  975  975  VAL VAL A . n 
A 1 976  GLY 976  976  976  GLY GLY A . n 
A 1 977  TYR 977  977  977  TYR TYR A . n 
A 1 978  VAL 978  978  978  VAL VAL A . n 
A 1 979  LEU 979  979  979  LEU LEU A . n 
A 1 980  HIS 980  980  980  HIS HIS A . n 
A 1 981  ARG 981  981  981  ARG ARG A . n 
A 1 982  THR 982  982  982  THR THR A . n 
A 1 983  ASN 983  983  983  ASN ASN A . n 
A 1 984  LEU 984  984  984  LEU LEU A . n 
A 1 985  MET 985  985  985  MET MET A . n 
A 1 986  GLN 986  986  986  GLN GLN A . n 
A 1 987  CYS 987  987  987  CYS CYS A . n 
A 1 988  GLY 988  988  988  GLY GLY A . n 
A 1 989  THR 989  989  989  THR THR A . n 
A 1 990  PRO 990  990  990  PRO PRO A . n 
A 1 991  GLU 991  991  991  GLU GLU A . n 
A 1 992  GLU 992  992  992  GLU GLU A . n 
A 1 993  HIS 993  993  993  HIS HIS A . n 
A 1 994  THR 994  994  994  THR THR A . n 
A 1 995  GLN 995  995  995  GLN GLN A . n 
A 1 996  LYS 996  996  996  LYS LYS A . n 
A 1 997  LEU 997  997  997  LEU LEU A . n 
A 1 998  ASP 998  998  998  ASP ASP A . n 
A 1 999  VAL 999  999  999  VAL VAL A . n 
A 1 1000 CYS 1000 1000 1000 CYS CYS A . n 
A 1 1001 HIS 1001 1001 1001 HIS HIS A . n 
A 1 1002 LEU 1002 1002 1002 LEU LEU 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 ASN 1005 1005 1005 ASN ASN A . n 
A 1 1006 VAL 1006 1006 1006 VAL VAL A . n 
A 1 1007 ALA 1007 1007 1007 ALA ALA A . n 
A 1 1008 ARG 1008 1008 1008 ARG ARG A . n 
A 1 1009 CYS 1009 1009 1009 CYS CYS A . n 
A 1 1010 GLU 1010 1010 1010 GLU GLU A . n 
A 1 1011 ARG 1011 1011 1011 ARG ARG A . n 
A 1 1012 THR 1012 1012 1012 THR THR A . n 
A 1 1013 THR 1013 1013 1013 THR THR A . n 
A 1 1014 LEU 1014 1014 1014 LEU LEU A . n 
A 1 1015 THR 1015 1015 1015 THR THR A . n 
A 1 1016 PHE 1016 1016 1016 PHE PHE A . n 
A 1 1017 LEU 1017 1017 1017 LEU LEU A . n 
A 1 1018 GLN 1018 1018 1018 GLN GLN A . n 
A 1 1019 ASN 1019 1019 1019 ASN ASN A . n 
A 1 1020 LEU 1020 1020 1020 LEU LEU A . n 
A 1 1021 GLU 1021 1021 1021 GLU GLU A . n 
A 1 1022 HIS 1022 1022 1022 HIS HIS A . n 
A 1 1023 LEU 1023 1023 1023 LEU LEU A . n 
A 1 1024 ASP 1024 1024 1024 ASP ASP A . n 
A 1 1025 GLY 1025 1025 1025 GLY GLY A . n 
A 1 1026 MET 1026 1026 1026 MET MET A . n 
A 1 1027 VAL 1027 1027 1027 VAL VAL A . n 
A 1 1028 ALA 1028 1028 1028 ALA ALA A . n 
A 1 1029 PRO 1029 1029 1029 PRO PRO A . n 
A 1 1030 GLU 1030 1030 1030 GLU GLU A . n 
A 1 1031 VAL 1031 1031 1031 VAL VAL A . n 
A 1 1032 CYS 1032 1032 1032 CYS CYS A . n 
A 1 1033 PRO 1033 1033 1033 PRO PRO A . n 
A 1 1034 MET 1034 1034 1034 MET MET A . n 
A 1 1035 GLU 1035 1035 1035 GLU GLU A . n 
A 1 1036 THR 1036 1036 1036 THR THR A . n 
A 1 1037 ALA 1037 1037 1037 ALA ALA A . n 
A 1 1038 ALA 1038 1038 1038 ALA ALA A . n 
A 1 1039 TYR 1039 1039 1039 TYR TYR A . n 
A 1 1040 VAL 1040 1040 1040 VAL VAL A . n 
A 1 1041 SER 1041 1041 1041 SER SER A . n 
A 1 1042 SER 1042 1042 1042 SER SER A . n 
A 1 1043 HIS 1043 1043 1043 HIS HIS A . n 
A 1 1044 SER 1044 1044 1044 SER SER A . n 
A 1 1045 SER 1045 1045 1045 SER SER A . 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 
B 2 NAG 1    1046 1    NAG NAG A . 
C 3 PO4 1    1047 1    PO4 PO4 A . 
D 4 ZN  1    1048 1    ZN  ZN  A . 
E 5 MRD 1    1049 1    MRD MRD A . 
F 6 WZ1 1    1050 1    WZ1 WZ1 A . 
G 7 MPD 1    1051 1    MPD MPD A . 
H 7 MPD 1    1052 2    MPD MPD A . 
I 8 HOH 1    1053 1    HOH HOH A . 
I 8 HOH 2    1054 2    HOH HOH A . 
I 8 HOH 3    1055 3    HOH HOH A . 
I 8 HOH 4    1056 4    HOH HOH A . 
I 8 HOH 5    1057 5    HOH HOH A . 
I 8 HOH 6    1058 6    HOH HOH A . 
I 8 HOH 7    1059 7    HOH HOH A . 
I 8 HOH 8    1060 8    HOH HOH A . 
I 8 HOH 9    1061 9    HOH HOH A . 
I 8 HOH 10   1062 10   HOH HOH A . 
I 8 HOH 11   1063 11   HOH HOH A . 
I 8 HOH 12   1064 12   HOH HOH A . 
I 8 HOH 13   1065 13   HOH HOH A . 
I 8 HOH 14   1066 14   HOH HOH A . 
I 8 HOH 15   1067 15   HOH HOH A . 
I 8 HOH 16   1068 16   HOH HOH A . 
I 8 HOH 17   1069 17   HOH HOH A . 
I 8 HOH 18   1070 18   HOH HOH A . 
I 8 HOH 19   1071 19   HOH HOH A . 
I 8 HOH 20   1072 20   HOH HOH A . 
I 8 HOH 21   1073 21   HOH HOH A . 
I 8 HOH 22   1074 22   HOH HOH A . 
I 8 HOH 23   1075 23   HOH HOH A . 
I 8 HOH 24   1076 24   HOH HOH A . 
I 8 HOH 25   1077 25   HOH HOH A . 
I 8 HOH 26   1078 26   HOH HOH A . 
I 8 HOH 27   1079 27   HOH HOH A . 
I 8 HOH 28   1080 28   HOH HOH A . 
I 8 HOH 29   1081 29   HOH HOH A . 
I 8 HOH 30   1082 30   HOH HOH A . 
I 8 HOH 31   1083 31   HOH HOH A . 
I 8 HOH 32   1084 32   HOH HOH A . 
I 8 HOH 33   1085 33   HOH HOH A . 
I 8 HOH 34   1086 34   HOH HOH A . 
I 8 HOH 35   1087 35   HOH HOH A . 
I 8 HOH 36   1088 36   HOH HOH A . 
I 8 HOH 37   1089 37   HOH HOH A . 
I 8 HOH 38   1090 38   HOH HOH A . 
I 8 HOH 39   1091 39   HOH HOH A . 
I 8 HOH 40   1092 40   HOH HOH A . 
I 8 HOH 41   1093 41   HOH HOH A . 
I 8 HOH 42   1094 42   HOH HOH A . 
I 8 HOH 43   1095 43   HOH HOH A . 
I 8 HOH 44   1096 44   HOH HOH A . 
I 8 HOH 45   1097 45   HOH HOH A . 
I 8 HOH 46   1098 46   HOH HOH A . 
I 8 HOH 47   1099 47   HOH HOH A . 
I 8 HOH 48   1100 48   HOH HOH A . 
I 8 HOH 49   1101 49   HOH HOH A . 
I 8 HOH 50   1102 50   HOH HOH A . 
I 8 HOH 51   1103 51   HOH HOH A . 
I 8 HOH 52   1104 52   HOH HOH A . 
I 8 HOH 53   1105 53   HOH HOH A . 
I 8 HOH 54   1106 54   HOH HOH A . 
I 8 HOH 55   1107 55   HOH HOH A . 
I 8 HOH 56   1108 56   HOH HOH A . 
I 8 HOH 57   1109 57   HOH HOH A . 
I 8 HOH 58   1110 58   HOH HOH A . 
I 8 HOH 59   1111 59   HOH HOH A . 
I 8 HOH 60   1112 60   HOH HOH A . 
I 8 HOH 61   1113 61   HOH HOH A . 
I 8 HOH 62   1114 62   HOH HOH A . 
I 8 HOH 63   1115 63   HOH HOH A . 
I 8 HOH 64   1116 64   HOH HOH A . 
I 8 HOH 65   1117 65   HOH HOH A . 
I 8 HOH 66   1118 66   HOH HOH A . 
I 8 HOH 67   1119 67   HOH HOH A . 
I 8 HOH 68   1120 68   HOH HOH A . 
I 8 HOH 69   1121 69   HOH HOH A . 
I 8 HOH 70   1122 70   HOH HOH A . 
I 8 HOH 71   1123 71   HOH HOH A . 
I 8 HOH 72   1124 72   HOH HOH A . 
I 8 HOH 73   1125 73   HOH HOH A . 
I 8 HOH 74   1126 74   HOH HOH A . 
I 8 HOH 75   1127 75   HOH HOH A . 
I 8 HOH 76   1128 76   HOH HOH A . 
I 8 HOH 77   1129 77   HOH HOH A . 
I 8 HOH 78   1130 78   HOH HOH A . 
I 8 HOH 79   1131 79   HOH HOH A . 
I 8 HOH 80   1132 80   HOH HOH A . 
I 8 HOH 81   1133 81   HOH HOH A . 
I 8 HOH 82   1134 82   HOH HOH A . 
I 8 HOH 83   1135 83   HOH HOH A . 
I 8 HOH 84   1136 84   HOH HOH A . 
I 8 HOH 85   1137 85   HOH HOH A . 
I 8 HOH 86   1138 86   HOH HOH A . 
I 8 HOH 87   1139 87   HOH HOH A . 
I 8 HOH 88   1140 88   HOH HOH A . 
I 8 HOH 89   1141 89   HOH HOH A . 
I 8 HOH 90   1142 90   HOH HOH A . 
I 8 HOH 91   1143 91   HOH HOH A . 
I 8 HOH 92   1144 92   HOH HOH A . 
I 8 HOH 93   1145 93   HOH HOH A . 
I 8 HOH 94   1146 94   HOH HOH A . 
I 8 HOH 95   1147 95   HOH HOH A . 
I 8 HOH 96   1148 96   HOH HOH A . 
I 8 HOH 97   1149 97   HOH HOH A . 
I 8 HOH 98   1150 98   HOH HOH A . 
I 8 HOH 99   1151 99   HOH HOH A . 
I 8 HOH 100  1152 100  HOH HOH A . 
I 8 HOH 101  1153 101  HOH HOH A . 
I 8 HOH 102  1154 102  HOH HOH A . 
I 8 HOH 103  1155 103  HOH HOH A . 
I 8 HOH 104  1156 104  HOH HOH A . 
I 8 HOH 105  1157 105  HOH HOH A . 
I 8 HOH 106  1158 106  HOH HOH A . 
I 8 HOH 107  1159 107  HOH HOH A . 
I 8 HOH 108  1160 108  HOH HOH A . 
I 8 HOH 109  1161 109  HOH HOH A . 
I 8 HOH 110  1162 110  HOH HOH A . 
I 8 HOH 111  1163 111  HOH HOH A . 
I 8 HOH 112  1164 112  HOH HOH A . 
I 8 HOH 113  1165 113  HOH HOH A . 
I 8 HOH 114  1166 114  HOH HOH A . 
I 8 HOH 115  1167 115  HOH HOH A . 
I 8 HOH 116  1168 116  HOH HOH A . 
I 8 HOH 117  1169 117  HOH HOH A . 
I 8 HOH 118  1170 118  HOH HOH A . 
I 8 HOH 119  1171 119  HOH HOH A . 
I 8 HOH 120  1172 120  HOH HOH A . 
I 8 HOH 121  1173 121  HOH HOH A . 
I 8 HOH 122  1174 122  HOH HOH A . 
I 8 HOH 123  1175 123  HOH HOH A . 
I 8 HOH 124  1176 124  HOH HOH A . 
I 8 HOH 125  1177 125  HOH HOH A . 
I 8 HOH 126  1178 126  HOH HOH A . 
I 8 HOH 127  1179 127  HOH HOH A . 
I 8 HOH 128  1180 128  HOH HOH A . 
I 8 HOH 129  1181 129  HOH HOH A . 
I 8 HOH 130  1182 130  HOH HOH A . 
I 8 HOH 131  1183 131  HOH HOH A . 
I 8 HOH 132  1184 132  HOH HOH A . 
I 8 HOH 133  1185 133  HOH HOH A . 
I 8 HOH 134  1186 134  HOH HOH A . 
I 8 HOH 135  1187 135  HOH HOH A . 
I 8 HOH 136  1188 136  HOH HOH A . 
I 8 HOH 137  1189 137  HOH HOH A . 
I 8 HOH 138  1190 138  HOH HOH A . 
I 8 HOH 139  1191 139  HOH HOH A . 
I 8 HOH 140  1192 140  HOH HOH A . 
I 8 HOH 141  1193 141  HOH HOH A . 
I 8 HOH 142  1194 142  HOH HOH A . 
I 8 HOH 143  1195 143  HOH HOH A . 
I 8 HOH 144  1196 144  HOH HOH A . 
I 8 HOH 145  1197 145  HOH HOH A . 
I 8 HOH 146  1198 146  HOH HOH A . 
I 8 HOH 147  1199 147  HOH HOH A . 
I 8 HOH 148  1200 148  HOH HOH A . 
I 8 HOH 149  1201 149  HOH HOH A . 
I 8 HOH 150  1202 150  HOH HOH A . 
I 8 HOH 151  1203 151  HOH HOH A . 
I 8 HOH 152  1204 152  HOH HOH A . 
I 8 HOH 153  1205 153  HOH HOH A . 
I 8 HOH 154  1206 154  HOH HOH A . 
I 8 HOH 155  1207 155  HOH HOH A . 
I 8 HOH 156  1208 156  HOH HOH A . 
I 8 HOH 157  1209 157  HOH HOH A . 
I 8 HOH 158  1210 158  HOH HOH A . 
I 8 HOH 159  1211 159  HOH HOH A . 
I 8 HOH 160  1212 160  HOH HOH A . 
I 8 HOH 161  1213 161  HOH HOH A . 
I 8 HOH 162  1214 162  HOH HOH A . 
I 8 HOH 163  1215 163  HOH HOH A . 
I 8 HOH 164  1216 164  HOH HOH A . 
I 8 HOH 165  1217 165  HOH HOH A . 
I 8 HOH 166  1218 166  HOH HOH A . 
I 8 HOH 167  1219 167  HOH HOH A . 
I 8 HOH 168  1220 168  HOH HOH A . 
I 8 HOH 169  1221 169  HOH HOH A . 
I 8 HOH 170  1222 170  HOH HOH A . 
I 8 HOH 171  1223 171  HOH HOH A . 
I 8 HOH 172  1224 172  HOH HOH A . 
I 8 HOH 173  1225 173  HOH HOH A . 
I 8 HOH 174  1226 174  HOH HOH A . 
I 8 HOH 175  1227 175  HOH HOH A . 
I 8 HOH 176  1228 176  HOH HOH A . 
I 8 HOH 177  1229 177  HOH HOH A . 
I 8 HOH 178  1230 178  HOH HOH A . 
I 8 HOH 179  1231 179  HOH HOH A . 
I 8 HOH 180  1232 180  HOH HOH A . 
I 8 HOH 181  1233 181  HOH HOH A . 
I 8 HOH 182  1234 182  HOH HOH A . 
I 8 HOH 183  1235 183  HOH HOH A . 
I 8 HOH 184  1236 184  HOH HOH A . 
I 8 HOH 185  1237 185  HOH HOH A . 
I 8 HOH 186  1238 186  HOH HOH A . 
I 8 HOH 187  1239 187  HOH HOH A . 
I 8 HOH 188  1240 188  HOH HOH A . 
I 8 HOH 189  1241 189  HOH HOH A . 
I 8 HOH 190  1242 190  HOH HOH A . 
I 8 HOH 191  1243 191  HOH HOH A . 
I 8 HOH 192  1244 192  HOH HOH A . 
I 8 HOH 193  1245 193  HOH HOH A . 
I 8 HOH 194  1246 194  HOH HOH A . 
I 8 HOH 195  1247 195  HOH HOH A . 
I 8 HOH 196  1248 196  HOH HOH A . 
I 8 HOH 197  1249 197  HOH HOH A . 
I 8 HOH 198  1250 198  HOH HOH A . 
I 8 HOH 199  1251 199  HOH HOH A . 
I 8 HOH 200  1252 200  HOH HOH A . 
I 8 HOH 201  1253 201  HOH HOH A . 
I 8 HOH 202  1254 202  HOH HOH A . 
I 8 HOH 203  1255 203  HOH HOH A . 
I 8 HOH 204  1256 204  HOH HOH A . 
I 8 HOH 205  1257 205  HOH HOH A . 
I 8 HOH 206  1258 206  HOH HOH A . 
I 8 HOH 207  1259 207  HOH HOH A . 
I 8 HOH 208  1260 208  HOH HOH A . 
I 8 HOH 209  1261 209  HOH HOH A . 
I 8 HOH 210  1262 210  HOH HOH A . 
I 8 HOH 211  1263 211  HOH HOH A . 
I 8 HOH 212  1264 212  HOH HOH A . 
I 8 HOH 213  1265 213  HOH HOH A . 
I 8 HOH 214  1266 214  HOH HOH A . 
I 8 HOH 215  1267 215  HOH HOH A . 
I 8 HOH 216  1268 216  HOH HOH A . 
I 8 HOH 217  1269 217  HOH HOH A . 
I 8 HOH 218  1270 218  HOH HOH A . 
I 8 HOH 219  1271 219  HOH HOH A . 
I 8 HOH 220  1272 220  HOH HOH A . 
I 8 HOH 221  1273 221  HOH HOH A . 
I 8 HOH 222  1274 222  HOH HOH A . 
I 8 HOH 223  1275 223  HOH HOH A . 
I 8 HOH 224  1276 224  HOH HOH A . 
I 8 HOH 225  1277 225  HOH HOH A . 
I 8 HOH 226  1278 226  HOH HOH A . 
I 8 HOH 227  1279 227  HOH HOH A . 
I 8 HOH 228  1280 228  HOH HOH A . 
I 8 HOH 229  1281 229  HOH HOH A . 
I 8 HOH 230  1282 230  HOH HOH A . 
I 8 HOH 231  1283 231  HOH HOH A . 
I 8 HOH 232  1284 232  HOH HOH A . 
I 8 HOH 233  1285 233  HOH HOH A . 
I 8 HOH 234  1286 234  HOH HOH A . 
I 8 HOH 235  1287 235  HOH HOH A . 
I 8 HOH 236  1288 236  HOH HOH A . 
I 8 HOH 237  1289 237  HOH HOH A . 
I 8 HOH 238  1290 238  HOH HOH A . 
I 8 HOH 239  1291 239  HOH HOH A . 
I 8 HOH 240  1292 240  HOH HOH A . 
I 8 HOH 241  1293 241  HOH HOH A . 
I 8 HOH 242  1294 242  HOH HOH A . 
I 8 HOH 243  1295 243  HOH HOH A . 
I 8 HOH 244  1296 244  HOH HOH A . 
I 8 HOH 245  1297 245  HOH HOH A . 
I 8 HOH 246  1298 246  HOH HOH A . 
I 8 HOH 247  1299 247  HOH HOH A . 
I 8 HOH 248  1300 248  HOH HOH A . 
I 8 HOH 249  1301 249  HOH HOH A . 
I 8 HOH 250  1302 250  HOH HOH A . 
I 8 HOH 251  1303 251  HOH HOH A . 
I 8 HOH 252  1304 252  HOH HOH A . 
I 8 HOH 253  1305 253  HOH HOH A . 
I 8 HOH 254  1306 254  HOH HOH A . 
I 8 HOH 255  1307 255  HOH HOH A . 
I 8 HOH 256  1308 256  HOH HOH A . 
I 8 HOH 257  1309 257  HOH HOH A . 
I 8 HOH 258  1310 258  HOH HOH A . 
I 8 HOH 259  1311 259  HOH HOH A . 
I 8 HOH 260  1312 260  HOH HOH A . 
I 8 HOH 261  1313 261  HOH HOH A . 
I 8 HOH 262  1314 262  HOH HOH A . 
I 8 HOH 263  1315 263  HOH HOH A . 
I 8 HOH 264  1316 264  HOH HOH A . 
I 8 HOH 265  1317 265  HOH HOH A . 
I 8 HOH 266  1318 266  HOH HOH A . 
I 8 HOH 267  1319 267  HOH HOH A . 
I 8 HOH 268  1320 268  HOH HOH A . 
I 8 HOH 269  1321 269  HOH HOH A . 
I 8 HOH 270  1322 270  HOH HOH A . 
I 8 HOH 271  1323 271  HOH HOH A . 
I 8 HOH 272  1324 272  HOH HOH A . 
I 8 HOH 273  1325 273  HOH HOH A . 
I 8 HOH 274  1326 274  HOH HOH A . 
I 8 HOH 275  1327 275  HOH HOH A . 
I 8 HOH 276  1328 276  HOH HOH A . 
I 8 HOH 277  1329 277  HOH HOH A . 
I 8 HOH 278  1330 278  HOH HOH A . 
I 8 HOH 279  1331 279  HOH HOH A . 
I 8 HOH 280  1332 280  HOH HOH A . 
I 8 HOH 281  1333 281  HOH HOH A . 
I 8 HOH 282  1334 282  HOH HOH A . 
I 8 HOH 283  1335 283  HOH HOH A . 
I 8 HOH 284  1336 284  HOH HOH A . 
I 8 HOH 285  1337 285  HOH HOH A . 
I 8 HOH 286  1338 286  HOH HOH A . 
I 8 HOH 287  1339 287  HOH HOH A . 
I 8 HOH 288  1340 288  HOH HOH A . 
I 8 HOH 289  1341 289  HOH HOH A . 
I 8 HOH 290  1342 290  HOH HOH A . 
I 8 HOH 291  1343 291  HOH HOH A . 
I 8 HOH 292  1344 292  HOH HOH A . 
I 8 HOH 293  1345 293  HOH HOH A . 
I 8 HOH 294  1346 294  HOH HOH A . 
I 8 HOH 295  1347 295  HOH HOH A . 
I 8 HOH 296  1348 296  HOH HOH A . 
I 8 HOH 297  1349 297  HOH HOH A . 
I 8 HOH 298  1350 298  HOH HOH A . 
I 8 HOH 299  1351 299  HOH HOH A . 
I 8 HOH 300  1352 300  HOH HOH A . 
I 8 HOH 301  1353 301  HOH HOH A . 
I 8 HOH 302  1354 302  HOH HOH A . 
I 8 HOH 303  1355 303  HOH HOH A . 
I 8 HOH 304  1356 304  HOH HOH A . 
I 8 HOH 305  1357 305  HOH HOH A . 
I 8 HOH 306  1358 306  HOH HOH A . 
I 8 HOH 307  1359 307  HOH HOH A . 
I 8 HOH 308  1360 308  HOH HOH A . 
I 8 HOH 309  1361 309  HOH HOH A . 
I 8 HOH 310  1362 310  HOH HOH A . 
I 8 HOH 311  1363 311  HOH HOH A . 
I 8 HOH 312  1364 312  HOH HOH A . 
I 8 HOH 313  1365 313  HOH HOH A . 
I 8 HOH 314  1366 314  HOH HOH A . 
I 8 HOH 315  1367 315  HOH HOH A . 
I 8 HOH 316  1368 316  HOH HOH A . 
I 8 HOH 317  1369 317  HOH HOH A . 
I 8 HOH 318  1370 318  HOH HOH A . 
I 8 HOH 319  1371 319  HOH HOH A . 
I 8 HOH 320  1372 320  HOH HOH A . 
I 8 HOH 321  1373 321  HOH HOH A . 
I 8 HOH 322  1374 322  HOH HOH A . 
I 8 HOH 323  1375 323  HOH HOH A . 
I 8 HOH 324  1376 324  HOH HOH A . 
I 8 HOH 325  1377 325  HOH HOH A . 
I 8 HOH 326  1378 326  HOH HOH A . 
I 8 HOH 327  1379 327  HOH HOH A . 
I 8 HOH 328  1380 328  HOH HOH A . 
I 8 HOH 329  1381 329  HOH HOH A . 
I 8 HOH 330  1382 330  HOH HOH A . 
I 8 HOH 331  1383 331  HOH HOH A . 
I 8 HOH 332  1384 332  HOH HOH A . 
I 8 HOH 333  1385 333  HOH HOH A . 
I 8 HOH 334  1386 334  HOH HOH A . 
I 8 HOH 335  1387 335  HOH HOH A . 
I 8 HOH 336  1388 336  HOH HOH A . 
I 8 HOH 337  1389 337  HOH HOH A . 
I 8 HOH 338  1390 338  HOH HOH A . 
I 8 HOH 339  1391 339  HOH HOH A . 
I 8 HOH 340  1392 340  HOH HOH A . 
I 8 HOH 341  1393 341  HOH HOH A . 
I 8 HOH 342  1394 342  HOH HOH A . 
I 8 HOH 343  1395 343  HOH HOH A . 
I 8 HOH 344  1396 344  HOH HOH A . 
I 8 HOH 345  1397 345  HOH HOH A . 
I 8 HOH 346  1398 346  HOH HOH A . 
I 8 HOH 347  1399 347  HOH HOH A . 
I 8 HOH 348  1400 348  HOH HOH A . 
I 8 HOH 349  1401 349  HOH HOH A . 
I 8 HOH 350  1402 350  HOH HOH A . 
I 8 HOH 351  1403 351  HOH HOH A . 
I 8 HOH 352  1404 352  HOH HOH A . 
I 8 HOH 353  1405 353  HOH HOH A . 
I 8 HOH 354  1406 354  HOH HOH A . 
I 8 HOH 355  1407 355  HOH HOH A . 
I 8 HOH 356  1408 356  HOH HOH A . 
I 8 HOH 357  1409 357  HOH HOH A . 
I 8 HOH 358  1410 358  HOH HOH A . 
I 8 HOH 359  1411 359  HOH HOH A . 
I 8 HOH 360  1412 360  HOH HOH A . 
I 8 HOH 361  1413 361  HOH HOH A . 
I 8 HOH 362  1414 362  HOH HOH A . 
I 8 HOH 363  1415 363  HOH HOH A . 
I 8 HOH 364  1416 364  HOH HOH A . 
I 8 HOH 365  1417 365  HOH HOH A . 
I 8 HOH 366  1418 366  HOH HOH A . 
I 8 HOH 367  1419 367  HOH HOH A . 
I 8 HOH 368  1420 368  HOH HOH A . 
I 8 HOH 369  1421 369  HOH HOH A . 
I 8 HOH 370  1422 370  HOH HOH A . 
I 8 HOH 371  1423 371  HOH HOH A . 
I 8 HOH 372  1424 372  HOH HOH A . 
I 8 HOH 373  1425 373  HOH HOH A . 
I 8 HOH 374  1426 374  HOH HOH A . 
I 8 HOH 375  1427 375  HOH HOH A . 
I 8 HOH 376  1428 376  HOH HOH A . 
I 8 HOH 377  1429 377  HOH HOH A . 
I 8 HOH 378  1430 378  HOH HOH A . 
I 8 HOH 379  1431 379  HOH HOH A . 
I 8 HOH 380  1432 380  HOH HOH A . 
I 8 HOH 381  1433 381  HOH HOH A . 
I 8 HOH 382  1434 382  HOH HOH A . 
I 8 HOH 383  1435 383  HOH HOH A . 
I 8 HOH 384  1436 384  HOH HOH A . 
I 8 HOH 385  1437 385  HOH HOH A . 
I 8 HOH 386  1438 386  HOH HOH A . 
I 8 HOH 387  1439 387  HOH HOH A . 
I 8 HOH 388  1440 388  HOH HOH A . 
I 8 HOH 389  1441 389  HOH HOH A . 
I 8 HOH 390  1442 390  HOH HOH A . 
I 8 HOH 391  1443 391  HOH HOH A . 
I 8 HOH 392  1444 392  HOH HOH A . 
I 8 HOH 393  1445 393  HOH HOH A . 
I 8 HOH 394  1446 394  HOH HOH A . 
I 8 HOH 395  1447 395  HOH HOH A . 
I 8 HOH 396  1448 396  HOH HOH A . 
I 8 HOH 397  1449 397  HOH HOH A . 
I 8 HOH 398  1450 398  HOH HOH A . 
I 8 HOH 399  1451 399  HOH HOH A . 
I 8 HOH 400  1452 400  HOH HOH A . 
I 8 HOH 401  1453 401  HOH HOH A . 
I 8 HOH 402  1454 402  HOH HOH A . 
I 8 HOH 403  1455 403  HOH HOH A . 
I 8 HOH 404  1456 404  HOH HOH A . 
I 8 HOH 405  1457 405  HOH HOH A . 
I 8 HOH 406  1458 406  HOH HOH A . 
I 8 HOH 407  1459 407  HOH HOH A . 
I 8 HOH 408  1460 408  HOH HOH A . 
I 8 HOH 409  1461 409  HOH HOH A . 
I 8 HOH 410  1462 410  HOH HOH A . 
I 8 HOH 411  1463 411  HOH HOH A . 
I 8 HOH 412  1464 412  HOH HOH A . 
I 8 HOH 413  1465 413  HOH HOH A . 
I 8 HOH 414  1466 414  HOH HOH A . 
I 8 HOH 415  1467 415  HOH HOH A . 
I 8 HOH 416  1468 416  HOH HOH A . 
I 8 HOH 417  1469 417  HOH HOH A . 
I 8 HOH 418  1470 418  HOH HOH A . 
I 8 HOH 419  1471 419  HOH HOH A . 
I 8 HOH 420  1472 420  HOH HOH A . 
I 8 HOH 421  1473 421  HOH HOH A . 
I 8 HOH 422  1474 422  HOH HOH A . 
I 8 HOH 423  1475 423  HOH HOH A . 
I 8 HOH 424  1476 424  HOH HOH A . 
I 8 HOH 425  1477 425  HOH HOH A . 
I 8 HOH 426  1478 426  HOH HOH A . 
I 8 HOH 427  1479 427  HOH HOH A . 
I 8 HOH 428  1480 428  HOH HOH A . 
I 8 HOH 429  1481 429  HOH HOH A . 
I 8 HOH 430  1482 430  HOH HOH A . 
I 8 HOH 431  1483 431  HOH HOH A . 
I 8 HOH 432  1484 432  HOH HOH A . 
I 8 HOH 433  1485 433  HOH HOH A . 
I 8 HOH 434  1486 434  HOH HOH A . 
I 8 HOH 435  1487 435  HOH HOH A . 
I 8 HOH 436  1488 436  HOH HOH A . 
I 8 HOH 437  1489 437  HOH HOH A . 
I 8 HOH 438  1490 438  HOH HOH A . 
I 8 HOH 439  1491 439  HOH HOH A . 
I 8 HOH 440  1492 440  HOH HOH A . 
I 8 HOH 441  1493 441  HOH HOH A . 
I 8 HOH 442  1494 442  HOH HOH A . 
I 8 HOH 443  1495 443  HOH HOH A . 
I 8 HOH 444  1496 444  HOH HOH A . 
I 8 HOH 445  1497 445  HOH HOH A . 
I 8 HOH 446  1498 446  HOH HOH A . 
I 8 HOH 447  1499 447  HOH HOH A . 
I 8 HOH 448  1500 448  HOH HOH A . 
I 8 HOH 449  1501 449  HOH HOH A . 
I 8 HOH 450  1502 450  HOH HOH A . 
I 8 HOH 451  1503 451  HOH HOH A . 
I 8 HOH 452  1504 452  HOH HOH A . 
I 8 HOH 453  1505 453  HOH HOH A . 
I 8 HOH 454  1506 454  HOH HOH A . 
I 8 HOH 455  1507 455  HOH HOH A . 
I 8 HOH 456  1508 456  HOH HOH A . 
I 8 HOH 457  1509 457  HOH HOH A . 
I 8 HOH 458  1510 458  HOH HOH A . 
I 8 HOH 459  1511 459  HOH HOH A . 
I 8 HOH 460  1512 460  HOH HOH A . 
I 8 HOH 461  1513 461  HOH HOH A . 
I 8 HOH 462  1514 462  HOH HOH A . 
I 8 HOH 463  1515 463  HOH HOH A . 
I 8 HOH 464  1516 464  HOH HOH A . 
I 8 HOH 465  1517 465  HOH HOH A . 
I 8 HOH 466  1518 466  HOH HOH A . 
I 8 HOH 467  1519 467  HOH HOH A . 
I 8 HOH 468  1520 468  HOH HOH A . 
I 8 HOH 469  1521 469  HOH HOH A . 
I 8 HOH 470  1522 470  HOH HOH A . 
I 8 HOH 471  1523 471  HOH HOH A . 
I 8 HOH 472  1524 472  HOH HOH A . 
I 8 HOH 473  1525 473  HOH HOH A . 
I 8 HOH 474  1526 474  HOH HOH A . 
I 8 HOH 475  1527 475  HOH HOH A . 
I 8 HOH 476  1528 476  HOH HOH A . 
I 8 HOH 477  1529 477  HOH HOH A . 
I 8 HOH 478  1530 478  HOH HOH A . 
I 8 HOH 479  1531 479  HOH HOH A . 
I 8 HOH 480  1532 480  HOH HOH A . 
I 8 HOH 481  1533 481  HOH HOH A . 
I 8 HOH 482  1534 482  HOH HOH A . 
I 8 HOH 483  1535 483  HOH HOH A . 
I 8 HOH 484  1536 484  HOH HOH A . 
I 8 HOH 485  1537 485  HOH HOH A . 
I 8 HOH 486  1538 486  HOH HOH A . 
I 8 HOH 487  1539 487  HOH HOH A . 
I 8 HOH 488  1540 488  HOH HOH A . 
I 8 HOH 489  1541 489  HOH HOH A . 
I 8 HOH 490  1542 490  HOH HOH A . 
I 8 HOH 491  1543 491  HOH HOH A . 
I 8 HOH 492  1544 492  HOH HOH A . 
I 8 HOH 493  1545 493  HOH HOH A . 
I 8 HOH 494  1546 494  HOH HOH A . 
I 8 HOH 495  1547 495  HOH HOH A . 
I 8 HOH 496  1548 496  HOH HOH A . 
I 8 HOH 497  1549 497  HOH HOH A . 
I 8 HOH 498  1550 498  HOH HOH A . 
I 8 HOH 499  1551 499  HOH HOH A . 
I 8 HOH 500  1552 500  HOH HOH A . 
I 8 HOH 501  1553 501  HOH HOH A . 
I 8 HOH 502  1554 502  HOH HOH A . 
I 8 HOH 503  1555 503  HOH HOH A . 
I 8 HOH 504  1556 504  HOH HOH A . 
I 8 HOH 505  1557 505  HOH HOH A . 
I 8 HOH 506  1558 506  HOH HOH A . 
I 8 HOH 507  1559 507  HOH HOH A . 
I 8 HOH 508  1560 508  HOH HOH A . 
I 8 HOH 509  1561 509  HOH HOH A . 
I 8 HOH 510  1562 510  HOH HOH A . 
I 8 HOH 511  1563 511  HOH HOH A . 
I 8 HOH 512  1564 512  HOH HOH A . 
I 8 HOH 513  1565 513  HOH HOH A . 
I 8 HOH 514  1566 514  HOH HOH A . 
I 8 HOH 515  1567 515  HOH HOH A . 
I 8 HOH 516  1568 516  HOH HOH A . 
I 8 HOH 517  1569 517  HOH HOH A . 
I 8 HOH 518  1570 518  HOH HOH A . 
I 8 HOH 519  1571 519  HOH HOH A . 
I 8 HOH 520  1572 520  HOH HOH A . 
I 8 HOH 521  1573 521  HOH HOH A . 
I 8 HOH 522  1574 522  HOH HOH A . 
I 8 HOH 523  1575 523  HOH HOH A . 
I 8 HOH 524  1576 524  HOH HOH A . 
I 8 HOH 525  1577 525  HOH HOH A . 
I 8 HOH 526  1578 526  HOH HOH A . 
I 8 HOH 527  1579 527  HOH HOH A . 
I 8 HOH 528  1580 528  HOH HOH A . 
I 8 HOH 529  1581 529  HOH HOH A . 
I 8 HOH 530  1582 530  HOH HOH A . 
I 8 HOH 531  1583 531  HOH HOH A . 
I 8 HOH 532  1584 532  HOH HOH A . 
I 8 HOH 533  1585 533  HOH HOH A . 
I 8 HOH 534  1586 534  HOH HOH A . 
I 8 HOH 535  1587 535  HOH HOH A . 
I 8 HOH 536  1588 536  HOH HOH A . 
I 8 HOH 537  1589 537  HOH HOH A . 
I 8 HOH 538  1590 538  HOH HOH A . 
I 8 HOH 539  1591 539  HOH HOH A . 
I 8 HOH 540  1592 540  HOH HOH A . 
I 8 HOH 541  1593 541  HOH HOH A . 
I 8 HOH 542  1594 542  HOH HOH A . 
I 8 HOH 543  1595 543  HOH HOH A . 
I 8 HOH 544  1596 544  HOH HOH A . 
I 8 HOH 545  1597 545  HOH HOH A . 
I 8 HOH 546  1598 546  HOH HOH A . 
I 8 HOH 547  1599 547  HOH HOH A . 
I 8 HOH 548  1600 548  HOH HOH A . 
I 8 HOH 549  1601 549  HOH HOH A . 
I 8 HOH 550  1602 550  HOH HOH A . 
I 8 HOH 551  1603 551  HOH HOH A . 
I 8 HOH 552  1604 552  HOH HOH A . 
I 8 HOH 553  1605 553  HOH HOH A . 
I 8 HOH 554  1606 554  HOH HOH A . 
I 8 HOH 555  1607 555  HOH HOH A . 
I 8 HOH 556  1608 556  HOH HOH A . 
I 8 HOH 557  1609 557  HOH HOH A . 
I 8 HOH 558  1610 558  HOH HOH A . 
I 8 HOH 559  1611 559  HOH HOH A . 
I 8 HOH 560  1612 560  HOH HOH A . 
I 8 HOH 561  1613 561  HOH HOH A . 
I 8 HOH 562  1614 562  HOH HOH A . 
I 8 HOH 563  1615 563  HOH HOH A . 
I 8 HOH 564  1616 564  HOH HOH A . 
I 8 HOH 565  1617 565  HOH HOH A . 
I 8 HOH 566  1618 566  HOH HOH A . 
I 8 HOH 567  1619 567  HOH HOH A . 
I 8 HOH 568  1620 568  HOH HOH A . 
I 8 HOH 569  1621 569  HOH HOH A . 
I 8 HOH 570  1622 570  HOH HOH A . 
I 8 HOH 571  1623 571  HOH HOH A . 
I 8 HOH 572  1624 572  HOH HOH A . 
I 8 HOH 573  1625 573  HOH HOH A . 
I 8 HOH 574  1626 574  HOH HOH A . 
I 8 HOH 575  1627 575  HOH HOH A . 
I 8 HOH 576  1628 576  HOH HOH A . 
I 8 HOH 577  1629 577  HOH HOH A . 
I 8 HOH 578  1630 578  HOH HOH A . 
I 8 HOH 579  1631 579  HOH HOH A . 
I 8 HOH 580  1632 580  HOH HOH A . 
I 8 HOH 581  1633 581  HOH HOH A . 
I 8 HOH 582  1634 582  HOH HOH A . 
I 8 HOH 583  1635 583  HOH HOH A . 
I 8 HOH 584  1636 584  HOH HOH A . 
I 8 HOH 585  1637 585  HOH HOH A . 
I 8 HOH 586  1638 586  HOH HOH A . 
I 8 HOH 587  1639 587  HOH HOH A . 
I 8 HOH 588  1640 588  HOH HOH A . 
I 8 HOH 589  1641 589  HOH HOH A . 
I 8 HOH 590  1642 590  HOH HOH A . 
I 8 HOH 591  1643 591  HOH HOH A . 
I 8 HOH 592  1644 592  HOH HOH A . 
I 8 HOH 593  1645 593  HOH HOH A . 
I 8 HOH 594  1646 594  HOH HOH A . 
I 8 HOH 595  1647 595  HOH HOH A . 
I 8 HOH 596  1648 596  HOH HOH A . 
I 8 HOH 597  1649 597  HOH HOH A . 
I 8 HOH 598  1650 598  HOH HOH A . 
I 8 HOH 599  1651 599  HOH HOH A . 
I 8 HOH 600  1652 600  HOH HOH A . 
I 8 HOH 601  1653 601  HOH HOH A . 
I 8 HOH 602  1654 602  HOH HOH A . 
I 8 HOH 603  1655 603  HOH HOH A . 
I 8 HOH 604  1656 604  HOH HOH A . 
I 8 HOH 605  1657 605  HOH HOH A . 
I 8 HOH 606  1658 606  HOH HOH A . 
I 8 HOH 607  1659 607  HOH HOH A . 
I 8 HOH 608  1660 608  HOH HOH A . 
I 8 HOH 609  1661 609  HOH HOH A . 
I 8 HOH 610  1662 610  HOH HOH A . 
I 8 HOH 611  1663 611  HOH HOH A . 
I 8 HOH 612  1664 612  HOH HOH A . 
I 8 HOH 613  1665 613  HOH HOH A . 
I 8 HOH 614  1666 614  HOH HOH A . 
I 8 HOH 615  1667 615  HOH HOH A . 
I 8 HOH 616  1668 616  HOH HOH A . 
I 8 HOH 617  1669 617  HOH HOH A . 
I 8 HOH 618  1670 618  HOH HOH A . 
I 8 HOH 619  1671 619  HOH HOH A . 
I 8 HOH 620  1672 620  HOH HOH A . 
I 8 HOH 621  1673 621  HOH HOH A . 
I 8 HOH 622  1674 622  HOH HOH A . 
I 8 HOH 623  1675 623  HOH HOH A . 
I 8 HOH 624  1676 624  HOH HOH A . 
I 8 HOH 625  1677 625  HOH HOH A . 
I 8 HOH 626  1678 626  HOH HOH A . 
I 8 HOH 627  1679 627  HOH HOH A . 
I 8 HOH 628  1680 628  HOH HOH A . 
I 8 HOH 629  1681 629  HOH HOH A . 
I 8 HOH 630  1682 630  HOH HOH A . 
I 8 HOH 631  1683 631  HOH HOH A . 
I 8 HOH 632  1684 632  HOH HOH A . 
I 8 HOH 633  1685 633  HOH HOH A . 
I 8 HOH 634  1686 634  HOH HOH A . 
I 8 HOH 635  1687 635  HOH HOH A . 
I 8 HOH 636  1688 636  HOH HOH A . 
I 8 HOH 637  1689 637  HOH HOH A . 
I 8 HOH 638  1690 638  HOH HOH A . 
I 8 HOH 639  1691 639  HOH HOH A . 
I 8 HOH 640  1692 640  HOH HOH A . 
I 8 HOH 641  1693 641  HOH HOH A . 
I 8 HOH 642  1694 642  HOH HOH A . 
I 8 HOH 643  1695 643  HOH HOH A . 
I 8 HOH 644  1696 644  HOH HOH A . 
I 8 HOH 645  1697 645  HOH HOH A . 
I 8 HOH 646  1698 646  HOH HOH A . 
I 8 HOH 647  1699 647  HOH HOH A . 
I 8 HOH 648  1700 648  HOH HOH A . 
I 8 HOH 649  1701 649  HOH HOH A . 
I 8 HOH 650  1702 650  HOH HOH A . 
I 8 HOH 651  1703 651  HOH HOH A . 
I 8 HOH 652  1704 652  HOH HOH A . 
I 8 HOH 653  1705 653  HOH HOH A . 
I 8 HOH 654  1706 654  HOH HOH A . 
I 8 HOH 655  1707 655  HOH HOH A . 
I 8 HOH 656  1708 656  HOH HOH A . 
I 8 HOH 657  1709 657  HOH HOH A . 
I 8 HOH 658  1710 658  HOH HOH A . 
I 8 HOH 659  1711 659  HOH HOH A . 
I 8 HOH 660  1712 660  HOH HOH A . 
I 8 HOH 661  1713 661  HOH HOH A . 
I 8 HOH 662  1714 662  HOH HOH A . 
I 8 HOH 663  1715 663  HOH HOH A . 
I 8 HOH 664  1716 664  HOH HOH A . 
I 8 HOH 665  1717 665  HOH HOH A . 
I 8 HOH 666  1718 666  HOH HOH A . 
I 8 HOH 667  1719 667  HOH HOH A . 
I 8 HOH 668  1720 668  HOH HOH A . 
I 8 HOH 669  1721 669  HOH HOH A . 
I 8 HOH 670  1722 670  HOH HOH A . 
I 8 HOH 671  1723 671  HOH HOH A . 
I 8 HOH 672  1724 672  HOH HOH A . 
I 8 HOH 673  1725 673  HOH HOH A . 
I 8 HOH 674  1726 674  HOH HOH A . 
I 8 HOH 675  1727 675  HOH HOH A . 
I 8 HOH 676  1728 676  HOH HOH A . 
I 8 HOH 677  1729 677  HOH HOH A . 
I 8 HOH 678  1730 678  HOH HOH A . 
I 8 HOH 679  1731 679  HOH HOH A . 
I 8 HOH 680  1732 680  HOH HOH A . 
I 8 HOH 681  1733 681  HOH HOH A . 
I 8 HOH 682  1734 682  HOH HOH A . 
I 8 HOH 683  1735 683  HOH HOH A . 
I 8 HOH 684  1736 684  HOH HOH A . 
I 8 HOH 685  1737 685  HOH HOH A . 
I 8 HOH 686  1738 686  HOH HOH A . 
I 8 HOH 687  1739 687  HOH HOH A . 
I 8 HOH 688  1740 688  HOH HOH A . 
I 8 HOH 689  1741 689  HOH HOH A . 
I 8 HOH 690  1742 690  HOH HOH A . 
I 8 HOH 691  1743 691  HOH HOH A . 
I 8 HOH 692  1744 692  HOH HOH A . 
I 8 HOH 693  1745 693  HOH HOH A . 
I 8 HOH 694  1746 694  HOH HOH A . 
I 8 HOH 695  1747 695  HOH HOH A . 
I 8 HOH 696  1748 696  HOH HOH A . 
I 8 HOH 697  1749 697  HOH HOH A . 
I 8 HOH 698  1750 698  HOH HOH A . 
I 8 HOH 699  1751 699  HOH HOH A . 
I 8 HOH 700  1752 700  HOH HOH A . 
I 8 HOH 701  1753 701  HOH HOH A . 
I 8 HOH 702  1754 702  HOH HOH A . 
I 8 HOH 703  1755 703  HOH HOH A . 
I 8 HOH 704  1756 704  HOH HOH A . 
I 8 HOH 705  1757 705  HOH HOH A . 
I 8 HOH 706  1758 706  HOH HOH A . 
I 8 HOH 707  1759 707  HOH HOH A . 
I 8 HOH 708  1760 708  HOH HOH A . 
I 8 HOH 709  1761 709  HOH HOH A . 
I 8 HOH 710  1762 710  HOH HOH A . 
I 8 HOH 711  1763 711  HOH HOH A . 
I 8 HOH 712  1764 712  HOH HOH A . 
I 8 HOH 713  1765 713  HOH HOH A . 
I 8 HOH 714  1766 714  HOH HOH A . 
I 8 HOH 715  1767 715  HOH HOH A . 
I 8 HOH 716  1768 716  HOH HOH A . 
I 8 HOH 717  1769 717  HOH HOH A . 
I 8 HOH 718  1770 718  HOH HOH A . 
I 8 HOH 719  1771 719  HOH HOH A . 
I 8 HOH 720  1772 720  HOH HOH A . 
I 8 HOH 721  1773 721  HOH HOH A . 
I 8 HOH 722  1774 722  HOH HOH A . 
I 8 HOH 723  1775 723  HOH HOH A . 
I 8 HOH 724  1776 724  HOH HOH A . 
I 8 HOH 725  1777 725  HOH HOH A . 
I 8 HOH 726  1778 726  HOH HOH A . 
I 8 HOH 727  1779 727  HOH HOH A . 
I 8 HOH 728  1780 728  HOH HOH A . 
I 8 HOH 729  1781 729  HOH HOH A . 
I 8 HOH 730  1782 730  HOH HOH A . 
I 8 HOH 731  1783 731  HOH HOH A . 
I 8 HOH 732  1784 732  HOH HOH A . 
I 8 HOH 733  1785 733  HOH HOH A . 
I 8 HOH 734  1786 734  HOH HOH A . 
I 8 HOH 735  1787 735  HOH HOH A . 
I 8 HOH 736  1788 736  HOH HOH A . 
I 8 HOH 737  1789 737  HOH HOH A . 
I 8 HOH 738  1790 738  HOH HOH A . 
I 8 HOH 739  1791 739  HOH HOH A . 
I 8 HOH 740  1792 740  HOH HOH A . 
I 8 HOH 741  1793 741  HOH HOH A . 
I 8 HOH 742  1794 742  HOH HOH A . 
I 8 HOH 743  1795 743  HOH HOH A . 
I 8 HOH 744  1796 744  HOH HOH A . 
I 8 HOH 745  1797 745  HOH HOH A . 
I 8 HOH 746  1798 746  HOH HOH A . 
I 8 HOH 747  1799 747  HOH HOH A . 
I 8 HOH 748  1800 748  HOH HOH A . 
I 8 HOH 749  1801 749  HOH HOH A . 
I 8 HOH 750  1802 750  HOH HOH A . 
I 8 HOH 751  1803 751  HOH HOH A . 
I 8 HOH 752  1804 752  HOH HOH A . 
I 8 HOH 753  1805 753  HOH HOH A . 
I 8 HOH 754  1806 754  HOH HOH A . 
I 8 HOH 755  1807 755  HOH HOH A . 
I 8 HOH 756  1808 756  HOH HOH A . 
I 8 HOH 757  1809 757  HOH HOH A . 
I 8 HOH 758  1810 758  HOH HOH A . 
I 8 HOH 759  1811 759  HOH HOH A . 
I 8 HOH 760  1812 760  HOH HOH A . 
I 8 HOH 761  1813 761  HOH HOH A . 
I 8 HOH 762  1814 762  HOH HOH A . 
I 8 HOH 763  1815 763  HOH HOH A . 
I 8 HOH 764  1816 764  HOH HOH A . 
I 8 HOH 765  1817 765  HOH HOH A . 
I 8 HOH 766  1818 766  HOH HOH A . 
I 8 HOH 767  1819 767  HOH HOH A . 
I 8 HOH 768  1820 768  HOH HOH A . 
I 8 HOH 769  1821 769  HOH HOH A . 
I 8 HOH 770  1822 770  HOH HOH A . 
I 8 HOH 771  1823 771  HOH HOH A . 
I 8 HOH 772  1824 772  HOH HOH A . 
I 8 HOH 773  1825 773  HOH HOH A . 
I 8 HOH 774  1826 774  HOH HOH A . 
I 8 HOH 775  1827 775  HOH HOH A . 
I 8 HOH 776  1828 776  HOH HOH A . 
I 8 HOH 777  1829 777  HOH HOH A . 
I 8 HOH 778  1830 778  HOH HOH A . 
I 8 HOH 779  1831 779  HOH HOH A . 
I 8 HOH 780  1832 780  HOH HOH A . 
I 8 HOH 781  1833 781  HOH HOH A . 
I 8 HOH 782  1834 782  HOH HOH A . 
I 8 HOH 783  1835 783  HOH HOH A . 
I 8 HOH 784  1836 784  HOH HOH A . 
I 8 HOH 785  1837 785  HOH HOH A . 
I 8 HOH 786  1838 786  HOH HOH A . 
I 8 HOH 787  1839 787  HOH HOH A . 
I 8 HOH 788  1840 788  HOH HOH A . 
I 8 HOH 789  1841 789  HOH HOH A . 
I 8 HOH 790  1842 790  HOH HOH A . 
I 8 HOH 791  1843 791  HOH HOH A . 
I 8 HOH 792  1844 792  HOH HOH A . 
I 8 HOH 793  1845 793  HOH HOH A . 
I 8 HOH 794  1846 794  HOH HOH A . 
I 8 HOH 795  1847 795  HOH HOH A . 
I 8 HOH 796  1848 796  HOH HOH A . 
I 8 HOH 797  1849 797  HOH HOH A . 
I 8 HOH 798  1850 798  HOH HOH A . 
I 8 HOH 799  1851 799  HOH HOH A . 
I 8 HOH 800  1852 800  HOH HOH A . 
I 8 HOH 801  1853 801  HOH HOH A . 
I 8 HOH 802  1854 802  HOH HOH A . 
I 8 HOH 803  1855 803  HOH HOH A . 
I 8 HOH 804  1856 804  HOH HOH A . 
I 8 HOH 805  1857 805  HOH HOH A . 
I 8 HOH 806  1858 806  HOH HOH A . 
I 8 HOH 807  1859 807  HOH HOH A . 
I 8 HOH 808  1860 808  HOH HOH A . 
I 8 HOH 809  1861 809  HOH HOH A . 
I 8 HOH 810  1862 810  HOH HOH A . 
I 8 HOH 811  1863 811  HOH HOH A . 
I 8 HOH 812  1864 812  HOH HOH A . 
I 8 HOH 813  1865 813  HOH HOH A . 
I 8 HOH 814  1866 814  HOH HOH A . 
I 8 HOH 815  1867 815  HOH HOH A . 
I 8 HOH 816  1868 816  HOH HOH A . 
I 8 HOH 817  1869 817  HOH HOH A . 
I 8 HOH 818  1870 818  HOH HOH A . 
I 8 HOH 819  1871 819  HOH HOH A . 
I 8 HOH 820  1872 820  HOH HOH A . 
I 8 HOH 821  1873 821  HOH HOH A . 
I 8 HOH 822  1874 822  HOH HOH A . 
I 8 HOH 823  1875 823  HOH HOH A . 
I 8 HOH 824  1876 824  HOH HOH A . 
I 8 HOH 825  1877 825  HOH HOH A . 
I 8 HOH 826  1878 826  HOH HOH A . 
I 8 HOH 827  1879 827  HOH HOH A . 
I 8 HOH 828  1880 828  HOH HOH A . 
I 8 HOH 829  1881 829  HOH HOH A . 
I 8 HOH 830  1882 830  HOH HOH A . 
I 8 HOH 831  1883 831  HOH HOH A . 
I 8 HOH 832  1884 833  HOH HOH A . 
I 8 HOH 833  1885 834  HOH HOH A . 
I 8 HOH 834  1886 835  HOH HOH A . 
I 8 HOH 835  1887 836  HOH HOH A . 
I 8 HOH 836  1888 837  HOH HOH A . 
I 8 HOH 837  1889 838  HOH HOH A . 
I 8 HOH 838  1890 839  HOH HOH A . 
I 8 HOH 839  1891 840  HOH HOH A . 
I 8 HOH 840  1892 841  HOH HOH A . 
I 8 HOH 841  1893 842  HOH HOH A . 
I 8 HOH 842  1894 843  HOH HOH A . 
I 8 HOH 843  1895 844  HOH HOH A . 
I 8 HOH 844  1896 845  HOH HOH A . 
I 8 HOH 845  1897 846  HOH HOH A . 
I 8 HOH 846  1898 847  HOH HOH A . 
I 8 HOH 847  1899 848  HOH HOH A . 
I 8 HOH 848  1900 849  HOH HOH A . 
I 8 HOH 849  1901 850  HOH HOH A . 
I 8 HOH 850  1902 851  HOH HOH A . 
I 8 HOH 851  1903 852  HOH HOH A . 
I 8 HOH 852  1904 853  HOH HOH A . 
I 8 HOH 853  1905 854  HOH HOH A . 
I 8 HOH 854  1906 855  HOH HOH A . 
I 8 HOH 855  1907 856  HOH HOH A . 
I 8 HOH 856  1908 857  HOH HOH A . 
I 8 HOH 857  1909 858  HOH HOH A . 
I 8 HOH 858  1910 859  HOH HOH A . 
I 8 HOH 859  1911 860  HOH HOH A . 
I 8 HOH 860  1912 861  HOH HOH A . 
I 8 HOH 861  1913 862  HOH HOH A . 
I 8 HOH 862  1914 863  HOH HOH A . 
I 8 HOH 863  1915 864  HOH HOH A . 
I 8 HOH 864  1916 865  HOH HOH A . 
I 8 HOH 865  1917 866  HOH HOH A . 
I 8 HOH 866  1918 867  HOH HOH A . 
I 8 HOH 867  1919 868  HOH HOH A . 
I 8 HOH 868  1920 869  HOH HOH A . 
I 8 HOH 869  1921 870  HOH HOH A . 
I 8 HOH 870  1922 871  HOH HOH A . 
I 8 HOH 871  1923 872  HOH HOH A . 
I 8 HOH 872  1924 873  HOH HOH A . 
I 8 HOH 873  1925 874  HOH HOH A . 
I 8 HOH 874  1926 875  HOH HOH A . 
I 8 HOH 875  1927 876  HOH HOH A . 
I 8 HOH 876  1928 877  HOH HOH A . 
I 8 HOH 877  1929 878  HOH HOH A . 
I 8 HOH 878  1930 879  HOH HOH A . 
I 8 HOH 879  1931 880  HOH HOH A . 
I 8 HOH 880  1932 881  HOH HOH A . 
I 8 HOH 881  1933 882  HOH HOH A . 
I 8 HOH 882  1934 883  HOH HOH A . 
I 8 HOH 883  1935 884  HOH HOH A . 
I 8 HOH 884  1936 885  HOH HOH A . 
I 8 HOH 885  1937 886  HOH HOH A . 
I 8 HOH 886  1938 887  HOH HOH A . 
I 8 HOH 887  1939 888  HOH HOH A . 
I 8 HOH 888  1940 889  HOH HOH A . 
I 8 HOH 889  1941 890  HOH HOH A . 
I 8 HOH 890  1942 891  HOH HOH A . 
I 8 HOH 891  1943 892  HOH HOH A . 
I 8 HOH 892  1944 893  HOH HOH A . 
I 8 HOH 893  1945 894  HOH HOH A . 
I 8 HOH 894  1946 895  HOH HOH A . 
I 8 HOH 895  1947 896  HOH HOH A . 
I 8 HOH 896  1948 897  HOH HOH A . 
I 8 HOH 897  1949 898  HOH HOH A . 
I 8 HOH 898  1950 899  HOH HOH A . 
I 8 HOH 899  1951 900  HOH HOH A . 
I 8 HOH 900  1952 901  HOH HOH A . 
I 8 HOH 901  1953 902  HOH HOH A . 
I 8 HOH 902  1954 903  HOH HOH A . 
I 8 HOH 903  1955 904  HOH HOH A . 
I 8 HOH 904  1956 905  HOH HOH A . 
I 8 HOH 905  1957 906  HOH HOH A . 
I 8 HOH 906  1958 907  HOH HOH A . 
I 8 HOH 907  1959 908  HOH HOH A . 
I 8 HOH 908  1960 909  HOH HOH A . 
I 8 HOH 909  1961 910  HOH HOH A . 
I 8 HOH 910  1962 911  HOH HOH A . 
I 8 HOH 911  1963 912  HOH HOH A . 
I 8 HOH 912  1964 913  HOH HOH A . 
I 8 HOH 913  1965 914  HOH HOH A . 
I 8 HOH 914  1966 915  HOH HOH A . 
I 8 HOH 915  1967 916  HOH HOH A . 
I 8 HOH 916  1968 917  HOH HOH A . 
I 8 HOH 917  1969 918  HOH HOH A . 
I 8 HOH 918  1970 919  HOH HOH A . 
I 8 HOH 919  1971 920  HOH HOH A . 
I 8 HOH 920  1972 921  HOH HOH A . 
I 8 HOH 921  1973 922  HOH HOH A . 
I 8 HOH 922  1974 923  HOH HOH A . 
I 8 HOH 923  1975 924  HOH HOH A . 
I 8 HOH 924  1976 925  HOH HOH A . 
I 8 HOH 925  1977 926  HOH HOH A . 
I 8 HOH 926  1978 927  HOH HOH A . 
I 8 HOH 927  1979 928  HOH HOH A . 
I 8 HOH 928  1980 929  HOH HOH A . 
I 8 HOH 929  1981 930  HOH HOH A . 
I 8 HOH 930  1982 931  HOH HOH A . 
I 8 HOH 931  1983 932  HOH HOH A . 
I 8 HOH 932  1984 933  HOH HOH A . 
I 8 HOH 933  1985 934  HOH HOH A . 
I 8 HOH 934  1986 935  HOH HOH A . 
I 8 HOH 935  1987 936  HOH HOH A . 
I 8 HOH 936  1988 937  HOH HOH A . 
I 8 HOH 937  1989 938  HOH HOH A . 
I 8 HOH 938  1990 939  HOH HOH A . 
I 8 HOH 939  1991 940  HOH HOH A . 
I 8 HOH 940  1992 941  HOH HOH A . 
I 8 HOH 941  1993 942  HOH HOH A . 
I 8 HOH 942  1994 943  HOH HOH A . 
I 8 HOH 943  1995 944  HOH HOH A . 
I 8 HOH 944  1996 945  HOH HOH A . 
I 8 HOH 945  1997 946  HOH HOH A . 
I 8 HOH 946  1998 947  HOH HOH A . 
I 8 HOH 947  1999 948  HOH HOH A . 
I 8 HOH 948  2000 949  HOH HOH A . 
I 8 HOH 949  2001 950  HOH HOH A . 
I 8 HOH 950  2002 951  HOH HOH A . 
I 8 HOH 951  2003 952  HOH HOH A . 
I 8 HOH 952  2004 953  HOH HOH A . 
I 8 HOH 953  2005 954  HOH HOH A . 
I 8 HOH 954  2006 955  HOH HOH A . 
I 8 HOH 955  2007 956  HOH HOH A . 
I 8 HOH 956  2008 957  HOH HOH A . 
I 8 HOH 957  2009 958  HOH HOH A . 
I 8 HOH 958  2010 959  HOH HOH A . 
I 8 HOH 959  2011 960  HOH HOH A . 
I 8 HOH 960  2012 961  HOH HOH A . 
I 8 HOH 961  2013 962  HOH HOH A . 
I 8 HOH 962  2014 963  HOH HOH A . 
I 8 HOH 963  2015 964  HOH HOH A . 
I 8 HOH 964  2016 965  HOH HOH A . 
I 8 HOH 965  2017 966  HOH HOH A . 
I 8 HOH 966  2018 967  HOH HOH A . 
I 8 HOH 967  2019 968  HOH HOH A . 
I 8 HOH 968  2020 969  HOH HOH A . 
I 8 HOH 969  2021 970  HOH HOH A . 
I 8 HOH 970  2022 971  HOH HOH A . 
I 8 HOH 971  2023 972  HOH HOH A . 
I 8 HOH 972  2024 973  HOH HOH A . 
I 8 HOH 973  2025 974  HOH HOH A . 
I 8 HOH 974  2026 975  HOH HOH A . 
I 8 HOH 975  2027 976  HOH HOH A . 
I 8 HOH 976  2028 977  HOH HOH A . 
I 8 HOH 977  2029 978  HOH HOH A . 
I 8 HOH 978  2030 979  HOH HOH A . 
I 8 HOH 979  2031 980  HOH HOH A . 
I 8 HOH 980  2032 981  HOH HOH A . 
I 8 HOH 981  2033 982  HOH HOH A . 
I 8 HOH 982  2034 983  HOH HOH A . 
I 8 HOH 983  2035 984  HOH HOH A . 
I 8 HOH 984  2036 985  HOH HOH A . 
I 8 HOH 985  2037 986  HOH HOH A . 
I 8 HOH 986  2038 987  HOH HOH A . 
I 8 HOH 987  2039 988  HOH HOH A . 
I 8 HOH 988  2040 989  HOH HOH A . 
I 8 HOH 989  2041 990  HOH HOH A . 
I 8 HOH 990  2042 991  HOH HOH A . 
I 8 HOH 991  2043 992  HOH HOH A . 
I 8 HOH 992  2044 993  HOH HOH A . 
I 8 HOH 993  2045 994  HOH HOH A . 
I 8 HOH 994  2046 995  HOH HOH A . 
I 8 HOH 995  2047 996  HOH HOH A . 
I 8 HOH 996  2048 997  HOH HOH A . 
I 8 HOH 997  2049 998  HOH HOH A . 
I 8 HOH 998  2050 999  HOH HOH A . 
I 8 HOH 999  2051 1000 HOH HOH A . 
I 8 HOH 1000 2052 1001 HOH HOH A . 
I 8 HOH 1001 2053 1002 HOH HOH A . 
I 8 HOH 1002 2054 1003 HOH HOH A . 
I 8 HOH 1003 2055 1004 HOH HOH A . 
I 8 HOH 1004 2056 1005 HOH HOH A . 
I 8 HOH 1005 2057 1006 HOH HOH A . 
I 8 HOH 1006 2058 1007 HOH HOH A . 
I 8 HOH 1007 2059 1008 HOH HOH A . 
I 8 HOH 1008 2060 1009 HOH HOH A . 
I 8 HOH 1009 2061 1010 HOH HOH A . 
I 8 HOH 1010 2062 1011 HOH HOH A . 
I 8 HOH 1011 2063 1012 HOH HOH A . 
I 8 HOH 1012 2064 1013 HOH HOH A . 
I 8 HOH 1013 2065 1014 HOH HOH A . 
I 8 HOH 1014 2066 1015 HOH HOH A . 
I 8 HOH 1015 2067 1016 HOH HOH A . 
I 8 HOH 1016 2068 1017 HOH HOH A . 
I 8 HOH 1017 2069 1018 HOH HOH A . 
I 8 HOH 1018 2070 1019 HOH HOH A . 
I 8 HOH 1019 2071 1020 HOH HOH A . 
I 8 HOH 1020 2072 1021 HOH HOH A . 
I 8 HOH 1021 2073 1022 HOH HOH A . 
I 8 HOH 1022 2074 1023 HOH HOH A . 
I 8 HOH 1023 2075 1024 HOH HOH A . 
I 8 HOH 1024 2076 1025 HOH HOH A . 
I 8 HOH 1025 2077 1026 HOH HOH A . 
I 8 HOH 1026 2078 1027 HOH HOH A . 
I 8 HOH 1027 2079 1028 HOH HOH A . 
I 8 HOH 1028 2080 1029 HOH HOH A . 
I 8 HOH 1029 2081 1030 HOH HOH A . 
I 8 HOH 1030 2082 1031 HOH HOH A . 
I 8 HOH 1031 2083 1032 HOH HOH A . 
I 8 HOH 1032 2084 1033 HOH HOH A . 
I 8 HOH 1033 2085 1034 HOH HOH A . 
I 8 HOH 1034 2086 1035 HOH HOH A . 
I 8 HOH 1035 2087 1036 HOH HOH A . 
I 8 HOH 1036 2088 1037 HOH HOH A . 
I 8 HOH 1037 2089 1038 HOH HOH A . 
I 8 HOH 1038 2090 1039 HOH HOH A . 
I 8 HOH 1039 2091 1040 HOH HOH A . 
I 8 HOH 1040 2092 1041 HOH HOH A . 
I 8 HOH 1041 2093 1042 HOH HOH A . 
I 8 HOH 1042 2094 1043 HOH HOH A . 
I 8 HOH 1043 2095 1044 HOH HOH A . 
I 8 HOH 1044 2096 1045 HOH HOH A . 
I 8 HOH 1045 2097 1046 HOH HOH A . 
I 8 HOH 1046 2098 1047 HOH HOH A . 
I 8 HOH 1047 2099 1048 HOH HOH A . 
I 8 HOH 1048 2100 1049 HOH HOH A . 
I 8 HOH 1049 2101 1050 HOH HOH A . 
I 8 HOH 1050 2102 1051 HOH HOH A . 
I 8 HOH 1051 2103 1052 HOH HOH A . 
I 8 HOH 1052 2104 1053 HOH HOH A . 
I 8 HOH 1053 2105 1054 HOH HOH A . 
I 8 HOH 1054 2106 1055 HOH HOH A . 
I 8 HOH 1055 2107 1056 HOH HOH A . 
I 8 HOH 1056 2108 1057 HOH HOH A . 
I 8 HOH 1057 2109 1058 HOH HOH A . 
I 8 HOH 1058 2110 1059 HOH HOH A . 
I 8 HOH 1059 2111 1060 HOH HOH A . 
I 8 HOH 1060 2112 1061 HOH HOH A . 
I 8 HOH 1061 2113 1062 HOH HOH A . 
I 8 HOH 1062 2114 1063 HOH HOH A . 
I 8 HOH 1063 2115 1064 HOH HOH A . 
I 8 HOH 1064 2116 1065 HOH HOH A . 
I 8 HOH 1065 2117 1066 HOH HOH A . 
I 8 HOH 1066 2118 1067 HOH HOH A . 
I 8 HOH 1067 2119 1068 HOH HOH A . 
I 8 HOH 1068 2120 1069 HOH HOH A . 
I 8 HOH 1069 2121 1070 HOH HOH A . 
I 8 HOH 1070 2122 1071 HOH HOH A . 
I 8 HOH 1071 2123 1072 HOH HOH A . 
I 8 HOH 1072 2124 1073 HOH HOH A . 
I 8 HOH 1073 2125 1074 HOH HOH A . 
I 8 HOH 1074 2126 1075 HOH HOH A . 
I 8 HOH 1075 2127 1076 HOH HOH A . 
I 8 HOH 1076 2128 1077 HOH HOH A . 
I 8 HOH 1077 2129 1078 HOH HOH A . 
I 8 HOH 1078 2130 1079 HOH HOH A . 
I 8 HOH 1079 2131 1080 HOH HOH A . 
I 8 HOH 1080 2132 1081 HOH HOH A . 
I 8 HOH 1081 2133 1082 HOH HOH A . 
I 8 HOH 1082 2134 1083 HOH HOH A . 
I 8 HOH 1083 2135 1084 HOH HOH A . 
I 8 HOH 1084 2136 1085 HOH HOH A . 
I 8 HOH 1085 2137 1086 HOH HOH A . 
I 8 HOH 1086 2138 1087 HOH HOH A . 
I 8 HOH 1087 2139 1088 HOH HOH A . 
I 8 HOH 1088 2140 1089 HOH HOH A . 
I 8 HOH 1089 2141 1090 HOH HOH A . 
I 8 HOH 1090 2142 1091 HOH HOH A . 
I 8 HOH 1091 2143 1092 HOH HOH A . 
I 8 HOH 1092 2144 1093 HOH HOH A . 
I 8 HOH 1093 2145 1094 HOH HOH A . 
I 8 HOH 1094 2146 1095 HOH HOH A . 
I 8 HOH 1095 2147 1096 HOH HOH A . 
I 8 HOH 1096 2148 1097 HOH HOH A . 
I 8 HOH 1097 2149 1098 HOH HOH A . 
I 8 HOH 1098 2150 1099 HOH HOH A . 
I 8 HOH 1099 2151 1100 HOH HOH A . 
I 8 HOH 1100 2152 1101 HOH HOH A . 
I 8 HOH 1101 2153 1102 HOH HOH A . 
I 8 HOH 1102 2154 1103 HOH HOH A . 
I 8 HOH 1103 2155 1104 HOH HOH A . 
I 8 HOH 1104 2156 1105 HOH HOH A . 
I 8 HOH 1105 2157 1106 HOH HOH A . 
I 8 HOH 1106 2158 1107 HOH HOH A . 
I 8 HOH 1107 2159 1108 HOH HOH A . 
I 8 HOH 1108 2160 1109 HOH HOH A . 
I 8 HOH 1109 2161 1110 HOH HOH A . 
I 8 HOH 1110 2162 1111 HOH HOH A . 
I 8 HOH 1111 2163 1112 HOH HOH A . 
I 8 HOH 1112 2164 1113 HOH HOH A . 
I 8 HOH 1113 2165 1114 HOH HOH A . 
I 8 HOH 1114 2166 1115 HOH HOH A . 
I 8 HOH 1115 2167 1116 HOH HOH A . 
I 8 HOH 1116 2168 1117 HOH HOH A . 
I 8 HOH 1117 2169 1118 HOH HOH A . 
I 8 HOH 1118 2170 1119 HOH HOH A . 
I 8 HOH 1119 2171 1120 HOH HOH A . 
I 8 HOH 1120 2172 1121 HOH HOH A . 
I 8 HOH 1121 2173 1122 HOH HOH A . 
I 8 HOH 1122 2174 1123 HOH HOH A . 
I 8 HOH 1123 2175 1124 HOH HOH A . 
I 8 HOH 1124 2176 1125 HOH HOH A . 
I 8 HOH 1125 2177 1126 HOH HOH A . 
I 8 HOH 1126 2178 1127 HOH HOH A . 
I 8 HOH 1127 2179 1128 HOH HOH A . 
I 8 HOH 1128 2180 1129 HOH HOH A . 
I 8 HOH 1129 2181 1130 HOH HOH A . 
I 8 HOH 1130 2182 1131 HOH HOH A . 
I 8 HOH 1131 2183 1132 HOH HOH A . 
I 8 HOH 1132 2184 1133 HOH HOH A . 
I 8 HOH 1133 2185 1134 HOH HOH A . 
I 8 HOH 1134 2186 1135 HOH HOH A . 
I 8 HOH 1135 2187 1136 HOH HOH A . 
I 8 HOH 1136 2188 1137 HOH HOH A . 
I 8 HOH 1137 2189 1138 HOH HOH A . 
I 8 HOH 1138 2190 1139 HOH HOH A . 
I 8 HOH 1139 2191 1140 HOH HOH A . 
I 8 HOH 1140 2192 1141 HOH HOH A . 
I 8 HOH 1141 2193 1142 HOH HOH A . 
I 8 HOH 1142 2194 1143 HOH HOH A . 
I 8 HOH 1143 2195 1144 HOH HOH A . 
I 8 HOH 1144 2196 1145 HOH HOH A . 
I 8 HOH 1145 2197 1146 HOH HOH A . 
I 8 HOH 1146 2198 1147 HOH HOH A . 
I 8 HOH 1147 2199 1148 HOH HOH A . 
I 8 HOH 1148 2200 1149 HOH HOH A . 
I 8 HOH 1149 2201 1150 HOH HOH A . 
I 8 HOH 1150 2202 1151 HOH HOH A . 
I 8 HOH 1151 2203 1152 HOH HOH A . 
I 8 HOH 1152 2204 1153 HOH HOH A . 
I 8 HOH 1153 2205 1154 HOH HOH A . 
I 8 HOH 1154 2206 1155 HOH HOH A . 
I 8 HOH 1155 2207 1156 HOH HOH A . 
I 8 HOH 1156 2208 1157 HOH HOH A . 
I 8 HOH 1157 2209 1158 HOH HOH A . 
I 8 HOH 1158 2210 1159 HOH HOH A . 
I 8 HOH 1159 2211 1160 HOH HOH A . 
I 8 HOH 1160 2212 1161 HOH HOH A . 
I 8 HOH 1161 2213 1162 HOH HOH A . 
I 8 HOH 1162 2214 1163 HOH HOH A . 
I 8 HOH 1163 2215 1164 HOH HOH A . 
I 8 HOH 1164 2216 1165 HOH HOH A . 
I 8 HOH 1165 2217 1166 HOH HOH A . 
I 8 HOH 1166 2218 1167 HOH HOH A . 
I 8 HOH 1167 2219 1168 HOH HOH A . 
I 8 HOH 1168 2220 1169 HOH HOH A . 
I 8 HOH 1169 2221 1170 HOH HOH A . 
I 8 HOH 1170 2222 1171 HOH HOH A . 
I 8 HOH 1171 2223 1172 HOH HOH A . 
I 8 HOH 1172 2224 1173 HOH HOH A . 
I 8 HOH 1173 2225 1174 HOH HOH A . 
I 8 HOH 1174 2226 1175 HOH HOH A . 
I 8 HOH 1175 2227 1176 HOH HOH A . 
I 8 HOH 1176 2228 1177 HOH HOH A . 
I 8 HOH 1177 2229 1178 HOH HOH A . 
I 8 HOH 1178 2230 1179 HOH HOH A . 
I 8 HOH 1179 2231 1180 HOH HOH A . 
I 8 HOH 1180 2232 1181 HOH HOH A . 
I 8 HOH 1181 2233 1182 HOH HOH A . 
I 8 HOH 1182 2234 1183 HOH HOH A . 
I 8 HOH 1183 2235 1184 HOH HOH A . 
I 8 HOH 1184 2236 1185 HOH HOH A . 
I 8 HOH 1185 2237 1186 HOH HOH A . 
I 8 HOH 1186 2238 1187 HOH HOH A . 
I 8 HOH 1187 2239 1188 HOH HOH A . 
I 8 HOH 1188 2240 1189 HOH HOH A . 
I 8 HOH 1189 2241 1190 HOH HOH A . 
I 8 HOH 1190 2242 1191 HOH HOH A . 
I 8 HOH 1191 2243 1192 HOH HOH A . 
I 8 HOH 1192 2244 1193 HOH HOH A . 
I 8 HOH 1193 2245 1194 HOH HOH A . 
I 8 HOH 1194 2246 1195 HOH HOH A . 
I 8 HOH 1195 2247 1196 HOH HOH A . 
I 8 HOH 1196 2248 1197 HOH HOH A . 
I 8 HOH 1197 2249 1198 HOH HOH A . 
I 8 HOH 1198 2250 1199 HOH HOH A . 
I 8 HOH 1199 2251 1200 HOH HOH A . 
I 8 HOH 1200 2252 1201 HOH HOH A . 
I 8 HOH 1201 2253 1202 HOH HOH A . 
I 8 HOH 1202 2254 1203 HOH HOH A . 
I 8 HOH 1203 2255 1204 HOH HOH A . 
I 8 HOH 1204 2256 1205 HOH HOH A . 
I 8 HOH 1205 2257 1206 HOH HOH A . 
I 8 HOH 1206 2258 1207 HOH HOH A . 
I 8 HOH 1207 2259 1208 HOH HOH A . 
I 8 HOH 1208 2260 1209 HOH HOH A . 
I 8 HOH 1209 2261 1210 HOH HOH A . 
I 8 HOH 1210 2262 1211 HOH HOH A . 
I 8 HOH 1211 2263 1212 HOH HOH A . 
I 8 HOH 1212 2264 1213 HOH HOH A . 
I 8 HOH 1213 2265 1214 HOH HOH A . 
I 8 HOH 1214 2266 1215 HOH HOH A . 
I 8 HOH 1215 2267 1216 HOH HOH A . 
I 8 HOH 1216 2268 1217 HOH HOH A . 
I 8 HOH 1217 2269 1218 HOH HOH A . 
I 8 HOH 1218 2270 1219 HOH HOH A . 
I 8 HOH 1219 2271 1220 HOH HOH A . 
I 8 HOH 1220 2272 1221 HOH HOH A . 
I 8 HOH 1221 2273 1222 HOH HOH A . 
I 8 HOH 1222 2274 1223 HOH HOH A . 
I 8 HOH 1223 2275 1224 HOH HOH A . 
I 8 HOH 1224 2276 1225 HOH HOH A . 
I 8 HOH 1225 2277 1226 HOH HOH A . 
I 8 HOH 1226 2278 1227 HOH HOH A . 
I 8 HOH 1227 2279 1228 HOH HOH A . 
I 8 HOH 1228 2280 1229 HOH HOH A . 
I 8 HOH 1229 2281 1230 HOH HOH A . 
I 8 HOH 1230 2282 1231 HOH HOH A . 
I 8 HOH 1231 2283 1232 HOH HOH A . 
I 8 HOH 1232 2284 1233 HOH HOH A . 
I 8 HOH 1233 2285 1234 HOH HOH A . 
I 8 HOH 1234 2286 1235 HOH HOH A . 
I 8 HOH 1235 2287 1236 HOH HOH A . 
I 8 HOH 1236 2288 1237 HOH HOH A . 
I 8 HOH 1237 2289 1238 HOH HOH A . 
I 8 HOH 1238 2290 1239 HOH HOH A . 
I 8 HOH 1239 2291 1240 HOH HOH A . 
I 8 HOH 1240 2292 1241 HOH HOH A . 
I 8 HOH 1241 2293 1242 HOH HOH A . 
I 8 HOH 1242 2294 1243 HOH HOH A . 
I 8 HOH 1243 2295 1244 HOH HOH A . 
I 8 HOH 1244 2296 1245 HOH HOH A . 
I 8 HOH 1245 2297 1246 HOH HOH A . 
I 8 HOH 1246 2298 1247 HOH HOH A . 
I 8 HOH 1247 2299 1248 HOH HOH A . 
I 8 HOH 1248 2300 1249 HOH HOH A . 
I 8 HOH 1249 2301 1250 HOH HOH A . 
I 8 HOH 1250 2302 1251 HOH HOH A . 
I 8 HOH 1251 2303 1252 HOH HOH A . 
I 8 HOH 1252 2304 1253 HOH HOH A . 
I 8 HOH 1253 2305 1254 HOH HOH A . 
I 8 HOH 1254 2306 1255 HOH HOH A . 
I 8 HOH 1255 2307 1256 HOH HOH A . 
I 8 HOH 1256 2308 1257 HOH HOH A . 
I 8 HOH 1257 2309 1258 HOH HOH A . 
I 8 HOH 1258 2310 1259 HOH HOH A . 
I 8 HOH 1259 2311 1260 HOH HOH A . 
I 8 HOH 1260 2312 1261 HOH HOH A . 
I 8 HOH 1261 2313 1262 HOH HOH A . 
I 8 HOH 1262 2314 1263 HOH HOH A . 
I 8 HOH 1263 2315 1264 HOH HOH A . 
I 8 HOH 1264 2316 1265 HOH HOH A . 
I 8 HOH 1265 2317 1266 HOH HOH A . 
I 8 HOH 1266 2318 1267 HOH HOH A . 
I 8 HOH 1267 2319 1268 HOH HOH A . 
I 8 HOH 1268 2320 1269 HOH HOH A . 
I 8 HOH 1269 2321 1270 HOH HOH A . 
I 8 HOH 1270 2322 1271 HOH HOH A . 
I 8 HOH 1271 2323 1272 HOH HOH A . 
I 8 HOH 1272 2324 1273 HOH HOH A . 
I 8 HOH 1273 2325 1274 HOH HOH A . 
I 8 HOH 1274 2326 1275 HOH HOH A . 
I 8 HOH 1275 2327 1276 HOH HOH A . 
I 8 HOH 1276 2328 1277 HOH HOH A . 
I 8 HOH 1277 2329 1278 HOH HOH A . 
I 8 HOH 1278 2330 1279 HOH HOH A . 
I 8 HOH 1279 2331 1280 HOH HOH A . 
I 8 HOH 1280 2332 1281 HOH HOH A . 
I 8 HOH 1281 2333 1282 HOH HOH A . 
I 8 HOH 1282 2334 1283 HOH HOH A . 
I 8 HOH 1283 2335 1284 HOH HOH A . 
I 8 HOH 1284 2336 1285 HOH HOH A . 
I 8 HOH 1285 2337 1286 HOH HOH A . 
I 8 HOH 1286 2338 1287 HOH HOH A . 
I 8 HOH 1287 2339 1288 HOH HOH A . 
I 8 HOH 1288 2340 1289 HOH HOH A . 
I 8 HOH 1289 2341 1290 HOH HOH A . 
I 8 HOH 1290 2342 1291 HOH HOH A . 
I 8 HOH 1291 2343 1292 HOH HOH A . 
I 8 HOH 1292 2344 1293 HOH HOH A . 
I 8 HOH 1293 2345 1294 HOH HOH A . 
I 8 HOH 1294 2346 1295 HOH HOH A . 
I 8 HOH 1295 2347 1296 HOH HOH A . 
I 8 HOH 1296 2348 1297 HOH HOH A . 
I 8 HOH 1297 2349 1298 HOH HOH A . 
I 8 HOH 1298 2350 1299 HOH HOH A . 
I 8 HOH 1299 2351 1300 HOH HOH A . 
I 8 HOH 1300 2352 1301 HOH HOH A . 
I 8 HOH 1301 2353 1302 HOH HOH A . 
I 8 HOH 1302 2354 1303 HOH HOH A . 
I 8 HOH 1303 2355 1304 HOH HOH A . 
I 8 HOH 1304 2356 1305 HOH HOH A . 
I 8 HOH 1305 2357 1306 HOH HOH A . 
I 8 HOH 1306 2358 1307 HOH HOH A . 
I 8 HOH 1307 2359 1308 HOH HOH A . 
I 8 HOH 1308 2360 1309 HOH HOH A . 
I 8 HOH 1309 2361 1310 HOH HOH A . 
I 8 HOH 1310 2362 1311 HOH HOH A . 
I 8 HOH 1311 2363 1312 HOH HOH A . 
I 8 HOH 1312 2364 1313 HOH HOH A . 
I 8 HOH 1313 2365 1314 HOH HOH A . 
I 8 HOH 1314 2366 1315 HOH HOH A . 
I 8 HOH 1315 2367 1316 HOH HOH A . 
I 8 HOH 1316 2368 1317 HOH HOH A . 
I 8 HOH 1317 2369 1318 HOH HOH A . 
I 8 HOH 1318 2370 1319 HOH HOH A . 
I 8 HOH 1319 2371 1320 HOH HOH A . 
I 8 HOH 1320 2372 1321 HOH HOH A . 
I 8 HOH 1321 2373 1322 HOH HOH A . 
I 8 HOH 1322 2374 1323 HOH HOH A . 
I 8 HOH 1323 2375 1324 HOH HOH A . 
I 8 HOH 1324 2376 1325 HOH HOH A . 
I 8 HOH 1325 2377 1326 HOH HOH A . 
I 8 HOH 1326 2378 1327 HOH HOH A . 
I 8 HOH 1327 2379 1328 HOH HOH A . 
I 8 HOH 1328 2380 1329 HOH HOH A . 
I 8 HOH 1329 2381 1330 HOH HOH A . 
I 8 HOH 1330 2382 1331 HOH HOH A . 
I 8 HOH 1331 2383 1332 HOH HOH A . 
I 8 HOH 1332 2384 1333 HOH HOH A . 
I 8 HOH 1333 2385 1334 HOH HOH A . 
I 8 HOH 1334 2386 1335 HOH HOH A . 
I 8 HOH 1335 2387 1336 HOH HOH A . 
I 8 HOH 1336 2388 1337 HOH HOH A . 
I 8 HOH 1337 2389 1338 HOH HOH A . 
I 8 HOH 1338 2390 1339 HOH HOH A . 
I 8 HOH 1339 2391 1340 HOH HOH A . 
I 8 HOH 1340 2392 1341 HOH HOH A . 
I 8 HOH 1341 2393 1342 HOH HOH A . 
I 8 HOH 1342 2394 1343 HOH HOH A . 
I 8 HOH 1343 2395 1344 HOH HOH A . 
I 8 HOH 1344 2396 1345 HOH HOH A . 
I 8 HOH 1345 2397 1346 HOH HOH A . 
I 8 HOH 1346 2398 1347 HOH HOH A . 
I 8 HOH 1347 2399 1348 HOH HOH A . 
I 8 HOH 1348 2400 1349 HOH HOH A . 
I 8 HOH 1349 2401 1350 HOH HOH A . 
I 8 HOH 1350 2402 1351 HOH HOH A . 
I 8 HOH 1351 2403 1352 HOH HOH A . 
I 8 HOH 1352 2404 1353 HOH HOH A . 
I 8 HOH 1353 2405 1354 HOH HOH A . 
I 8 HOH 1354 2406 1355 HOH HOH A . 
I 8 HOH 1355 2407 1356 HOH HOH A . 
I 8 HOH 1356 2408 1357 HOH HOH A . 
I 8 HOH 1357 2409 1358 HOH HOH A . 
I 8 HOH 1358 2410 1359 HOH HOH A . 
I 8 HOH 1359 2411 1360 HOH HOH A . 
I 8 HOH 1360 2412 1361 HOH HOH A . 
I 8 HOH 1361 2413 1362 HOH HOH A . 
I 8 HOH 1362 2414 1363 HOH HOH A . 
I 8 HOH 1363 2415 1364 HOH HOH A . 
I 8 HOH 1364 2416 1365 HOH HOH A . 
I 8 HOH 1365 2417 1366 HOH HOH A . 
I 8 HOH 1366 2418 1367 HOH HOH A . 
I 8 HOH 1367 2419 1368 HOH HOH A . 
I 8 HOH 1368 2420 1369 HOH HOH A . 
I 8 HOH 1369 2421 1370 HOH HOH A . 
I 8 HOH 1370 2422 1371 HOH HOH A . 
I 8 HOH 1371 2423 1372 HOH HOH A . 
I 8 HOH 1372 2424 1373 HOH HOH A . 
I 8 HOH 1373 2425 1374 HOH HOH A . 
I 8 HOH 1374 2426 1375 HOH HOH A . 
I 8 HOH 1375 2427 1376 HOH HOH A . 
I 8 HOH 1376 2428 1377 HOH HOH A . 
I 8 HOH 1377 2429 1378 HOH HOH A . 
I 8 HOH 1378 2430 1379 HOH HOH A . 
I 8 HOH 1379 2431 1380 HOH HOH A . 
I 8 HOH 1380 2432 1381 HOH HOH A . 
I 8 HOH 1381 2433 1382 HOH HOH A . 
I 8 HOH 1382 2434 1383 HOH HOH A . 
I 8 HOH 1383 2435 1384 HOH HOH A . 
I 8 HOH 1384 2436 1385 HOH HOH A . 
I 8 HOH 1385 2437 1386 HOH HOH A . 
I 8 HOH 1386 2438 1387 HOH HOH A . 
I 8 HOH 1387 2439 1388 HOH HOH A . 
I 8 HOH 1388 2440 1389 HOH HOH A . 
I 8 HOH 1389 2441 1390 HOH HOH A . 
I 8 HOH 1390 2442 1391 HOH HOH A . 
I 8 HOH 1391 2443 1392 HOH HOH A . 
I 8 HOH 1392 2444 1393 HOH HOH A . 
I 8 HOH 1393 2445 1394 HOH HOH A . 
I 8 HOH 1394 2446 1395 HOH HOH A . 
I 8 HOH 1395 2447 1396 HOH HOH A . 
I 8 HOH 1396 2448 1397 HOH HOH A . 
I 8 HOH 1397 2449 1398 HOH HOH A . 
I 8 HOH 1398 2450 1399 HOH HOH A . 
I 8 HOH 1399 2451 1400 HOH HOH A . 
I 8 HOH 1400 2452 1401 HOH HOH A . 
I 8 HOH 1401 2453 1402 HOH HOH A . 
I 8 HOH 1402 2454 1403 HOH HOH A . 
I 8 HOH 1403 2455 1404 HOH HOH A . 
I 8 HOH 1404 2456 1405 HOH HOH A . 
I 8 HOH 1405 2457 1406 HOH HOH A . 
I 8 HOH 1406 2458 1407 HOH HOH A . 
I 8 HOH 1407 2459 1408 HOH HOH A . 
I 8 HOH 1408 2460 1409 HOH HOH A . 
I 8 HOH 1409 2461 1410 HOH HOH A . 
I 8 HOH 1410 2462 1411 HOH HOH A . 
I 8 HOH 1411 2463 1412 HOH HOH A . 
I 8 HOH 1412 2464 1413 HOH HOH A . 
I 8 HOH 1413 2465 1414 HOH HOH A . 
I 8 HOH 1414 2466 1415 HOH HOH A . 
I 8 HOH 1415 2467 1416 HOH HOH A . 
I 8 HOH 1416 2468 1417 HOH HOH A . 
I 8 HOH 1417 2469 1418 HOH HOH A . 
I 8 HOH 1418 2470 1419 HOH HOH A . 
I 8 HOH 1419 2471 1420 HOH HOH A . 
I 8 HOH 1420 2472 1421 HOH HOH A . 
I 8 HOH 1421 2473 1422 HOH HOH A . 
I 8 HOH 1422 2474 1423 HOH HOH A . 
I 8 HOH 1423 2475 1424 HOH HOH A . 
I 8 HOH 1424 2476 1425 HOH HOH A . 
I 8 HOH 1425 2477 1426 HOH HOH A . 
I 8 HOH 1426 2478 1427 HOH HOH A . 
I 8 HOH 1427 2479 1428 HOH HOH A . 
I 8 HOH 1428 2480 1429 HOH HOH A . 
I 8 HOH 1429 2481 1430 HOH HOH A . 
I 8 HOH 1430 2482 1431 HOH HOH A . 
I 8 HOH 1431 2483 1432 HOH HOH A . 
I 8 HOH 1432 2484 1433 HOH HOH A . 
I 8 HOH 1433 2485 1434 HOH HOH A . 
I 8 HOH 1434 2486 1435 HOH HOH A . 
I 8 HOH 1435 2487 1436 HOH HOH A . 
I 8 HOH 1436 2488 1437 HOH HOH A . 
I 8 HOH 1437 2489 1438 HOH HOH A . 
I 8 HOH 1438 2490 1439 HOH HOH A . 
I 8 HOH 1439 2491 1440 HOH HOH A . 
I 8 HOH 1440 2492 1441 HOH HOH A . 
I 8 HOH 1441 2493 1442 HOH HOH A . 
I 8 HOH 1442 2494 1443 HOH HOH A . 
I 8 HOH 1443 2495 1444 HOH HOH A . 
I 8 HOH 1444 2496 1445 HOH HOH A . 
I 8 HOH 1445 2497 1446 HOH HOH A . 
I 8 HOH 1446 2498 1447 HOH HOH A . 
I 8 HOH 1447 2499 1448 HOH HOH A . 
I 8 HOH 1448 2500 1449 HOH HOH A . 
I 8 HOH 1449 2501 1450 HOH HOH A . 
I 8 HOH 1450 2502 1451 HOH HOH A . 
I 8 HOH 1451 2503 1452 HOH HOH A . 
I 8 HOH 1452 2504 1453 HOH HOH A . 
I 8 HOH 1453 2505 1454 HOH HOH A . 
# 
_pdbx_struct_mod_residue.id               1 
_pdbx_struct_mod_residue.label_asym_id    A 
_pdbx_struct_mod_residue.label_comp_id    ASN 
_pdbx_struct_mod_residue.label_seq_id     194 
_pdbx_struct_mod_residue.auth_asym_id     A 
_pdbx_struct_mod_residue.auth_comp_id     ASN 
_pdbx_struct_mod_residue.auth_seq_id      194 
_pdbx_struct_mod_residue.PDB_ins_code     ? 
_pdbx_struct_mod_residue.parent_comp_id   ASN 
_pdbx_struct_mod_residue.details          'GLYCOSYLATION SITE' 
# 
_pdbx_struct_assembly.id                   1 
_pdbx_struct_assembly.details              author_and_software_defined_assembly 
_pdbx_struct_assembly.method_details       PISA 
_pdbx_struct_assembly.oligomeric_details   monomeric 
_pdbx_struct_assembly.oligomeric_count     1 
# 
_pdbx_struct_assembly_gen.assembly_id       1 
_pdbx_struct_assembly_gen.oper_expression   1 
_pdbx_struct_assembly_gen.asym_id_list      A,B,C,D,E,F,G,H,I 
# 
_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  NE2 ? A HIS 90  ? A HIS 90   ? 1_555 ZN ? D ZN . ? A ZN 1048 ? 1_555 OD1 ? A ASP 92  ? A ASP 92   ? 1_555 96.2  ? 
2  NE2 ? A HIS 90  ? A HIS 90   ? 1_555 ZN ? D ZN . ? A ZN 1048 ? 1_555 NE2 ? A HIS 471 ? A HIS 471  ? 1_555 106.5 ? 
3  OD1 ? A ASP 92  ? A ASP 92   ? 1_555 ZN ? D ZN . ? A ZN 1048 ? 1_555 NE2 ? A HIS 471 ? A HIS 471  ? 1_555 98.5  ? 
4  NE2 ? A HIS 90  ? A HIS 90   ? 1_555 ZN ? D ZN . ? A ZN 1048 ? 1_555 O32 ? F WZ1 .   ? A WZ1 1050 ? 1_555 152.6 ? 
5  OD1 ? A ASP 92  ? A ASP 92   ? 1_555 ZN ? D ZN . ? A ZN 1048 ? 1_555 O32 ? F WZ1 .   ? A WZ1 1050 ? 1_555 92.8  ? 
6  NE2 ? A HIS 471 ? A HIS 471  ? 1_555 ZN ? D ZN . ? A ZN 1048 ? 1_555 O32 ? F WZ1 .   ? A WZ1 1050 ? 1_555 97.5  ? 
7  NE2 ? A HIS 90  ? A HIS 90   ? 1_555 ZN ? D ZN . ? A ZN 1048 ? 1_555 O22 ? F WZ1 .   ? A WZ1 1050 ? 1_555 85.2  ? 
8  OD1 ? A ASP 92  ? A ASP 92   ? 1_555 ZN ? D ZN . ? A ZN 1048 ? 1_555 O22 ? F WZ1 .   ? A WZ1 1050 ? 1_555 144.8 ? 
9  NE2 ? A HIS 471 ? A HIS 471  ? 1_555 ZN ? D ZN . ? A ZN 1048 ? 1_555 O22 ? F WZ1 .   ? A WZ1 1050 ? 1_555 114.9 ? 
10 O32 ? F WZ1 .   ? A WZ1 1050 ? 1_555 ZN ? D ZN . ? A ZN 1048 ? 1_555 O22 ? F WZ1 .   ? A WZ1 1050 ? 1_555 72.8  ? 
# 
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 2008-07-01 
2 'Structure model' 1 1 2011-07-13 
3 'Structure model' 1 2 2017-10-25 
# 
_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' 'Non-polymer description'   
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 
# 
_phasing.method   MR 
# 
loop_
_software.name 
_software.version 
_software.date 
_software.type 
_software.contact_author 
_software.contact_author_email 
_software.classification 
_software.location 
_software.language 
_software.citation_id 
_software.pdbx_ordinal 
DENZO       .       ?                    package 'Zbyszek Otwinowski' zbyszek@mix.swmed.edu    'data reduction'  
http://www.lnls.br/infra/linhasluz/denzo-hkl.htm ?          ? 1 
SCALEPACK   .       ?                    package 'Zbyszek Otwinowski' zbyszek@mix.swmed.edu    'data scaling'    
http://www.lnls.br/infra/linhasluz/denzo-hkl.htm ?          ? 2 
CNS         .       ?                    package 'Axel T. Brunger'    axel.brunger@yale.edu    refinement        
http://cns.csb.yale.edu/v1.1/                    Fortran_77 ? 3 
REFMAC      .       ?                    program 'Murshudov, G.N.'    ccp4@dl.ac.uk            refinement        
http://www.ccp4.ac.uk/main.html                  Fortran_77 ? 4 
PDB_EXTRACT 3.004   'September 10, 2007' package PDB                  sw-help@rcsb.rutgers.edu 'data extraction' 
http://pdb.rutgers.edu/software/                 C++        ? 5 
ADSC        Quantum ?                    ?       ?                    ?                        'data collection' ? ?          ? 6 
CNS         .       ?                    ?       ?                    ?                        phasing           ? ?          ? 7 
# 
_pdbx_database_remark.id     999 
_pdbx_database_remark.text   
;SEQUENCE  
E970K conflict in UNP entry Q24451
;
# 
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 ASP A 56  ? ? -105.11 78.32   
2  1 HIS A 79  ? ? -151.78 84.74   
3  1 TRP A 95  ? ? -170.91 -83.65  
4  1 ASP A 106 ? ? -132.50 -61.01  
5  1 THR A 162 ? ? 69.11   -67.59  
6  1 GLN A 227 ? ? -139.31 -44.21  
7  1 ASP A 340 ? ? -172.88 -171.73 
8  1 LYS A 345 ? ? -87.14  -70.24  
9  1 SER A 411 ? ? 41.96   -126.36 
10 1 SER A 411 ? ? 48.95   -130.46 
11 1 ILE A 549 ? ? -140.73 -48.67  
12 1 LEU A 550 ? ? -171.16 117.58  
13 1 PRO A 562 ? ? -84.69  40.41   
14 1 ARG A 653 ? ? -173.30 147.78  
15 1 ASN A 732 ? ? -92.20  57.35   
16 1 GLN A 742 ? A -119.60 76.69   
17 1 SER A 762 ? ? 72.44   -4.05   
18 1 ILE A 831 ? ? -118.03 75.83   
19 1 SER A 833 ? ? -152.15 -15.09  
20 1 ASP A 839 ? ? -124.04 -160.35 
21 1 GLU A 991 ? ? 22.70   82.27   
22 1 GLU A 992 ? ? -116.91 -161.77 
23 1 HIS A 993 ? ? 36.17   93.75   
# 
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 ARG 1  ? A ARG 1  
2  1 Y 1 A SER 2  ? A SER 2  
3  1 Y 1 A SER 3  ? A SER 3  
4  1 Y 1 A HIS 4  ? A HIS 4  
5  1 Y 1 A HIS 5  ? A HIS 5  
6  1 Y 1 A HIS 6  ? A HIS 6  
7  1 Y 1 A HIS 7  ? A HIS 7  
8  1 Y 1 A HIS 8  ? A HIS 8  
9  1 Y 1 A HIS 9  ? A HIS 9  
10 1 Y 1 A GLY 10 ? A GLY 10 
11 1 Y 1 A GLU 11 ? A GLU 11 
12 1 Y 1 A PHE 12 ? A PHE 12 
13 1 Y 1 A ASP 13 ? A ASP 13 
14 1 Y 1 A ASP 14 ? A ASP 14 
15 1 Y 1 A PRO 15 ? A PRO 15 
16 1 Y 1 A ILE 16 ? A ILE 16 
17 1 Y 1 A ARG 17 ? A ARG 17 
18 1 Y 1 A PRO 18 ? A PRO 18 
19 1 Y 1 A PRO 19 ? A PRO 19 
20 1 Y 1 A LEU 20 ? A LEU 20 
21 1 Y 1 A LYS 21 ? A LYS 21 
22 1 Y 1 A VAL 22 ? A VAL 22 
23 1 Y 1 A ALA 23 ? A ALA 23 
24 1 Y 1 A ARG 24 ? A ARG 24 
25 1 Y 1 A SER 25 ? A SER 25 
26 1 Y 1 A PRO 26 ? A PRO 26 
27 1 Y 1 A ARG 27 ? A ARG 27 
28 1 Y 1 A PRO 28 ? A PRO 28 
29 1 Y 1 A GLY 29 ? A GLY 29 
# 
loop_
_pdbx_entity_nonpoly.entity_id 
_pdbx_entity_nonpoly.name 
_pdbx_entity_nonpoly.comp_id 
2 N-ACETYL-D-GLUCOSAMINE                                             NAG 
3 'PHOSPHATE ION'                                                    PO4 
4 'ZINC ION'                                                         ZN  
5 '(4R)-2-METHYLPENTANE-2,4-DIOL'                                    MRD 
6 'methyl 3-S-alpha-D-mannopyranosyl-3-thio-alpha-D-mannopyranoside' WZ1 
7 '(4S)-2-METHYL-2,4-PENTANEDIOL'                                    MPD 
8 water                                                              HOH 
# 
